HEADER    SIGNALING PROTEIN, HYDROLASE            12-AUG-10   3OE9              
TITLE     CRYSTAL STRUCTURE OF THE CHEMOKINE CXCR4 RECEPTOR IN COMPLEX WITH A   
TITLE    2 SMALL MOLECULE ANTAGONIST IT1T IN P1 SPACEGROUP                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: C-X-C CHEMOKINE RECEPTOR TYPE 4, LYSOZYME CHIMERA;         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CXCR4 RESIDUES 2-228, LYSOZYME RESIDUES 1002-1161, CXCR4   
COMPND   5 RESIDUES 231-319;                                                    
COMPND   6 SYNONYM: CXC-R4, CXCR-4, STROMAL CELL-DERIVED FACTOR 1 RECEPTOR, SDF-
COMPND   7 1 RECEPTOR, FUSIN, LEUKOCYTE-DERIVED SEVEN TRANSMEMBRANE DOMAIN      
COMPND   8 RECEPTOR, LESTR, LCR1, FB22, NPYRL, HM89, LYSIS PROTEIN, MURAMIDASE, 
COMPND   9 ENDOLYSIN;                                                           
COMPND  10 EC: 3.2.1.17;                                                        
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4;          
SOURCE   3 ORGANISM_TAXID: 9606, 10665;                                         
SOURCE   4 GENE: CXCR4, CXCR4_HUMAN,E;                                          
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACMID;                               
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PFASTBAC                                  
KEYWDS    STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE, ACCELERATED 
KEYWDS   2 TECHNOLOGIES CENTER FOR GENE TO 3D STRUCTURE, ATCG3D, 7TM, G         
KEYWDS   3 PROTEIN-COUPLED RECEPTOR, GPCR, SIGNAL TRANSDUCTION, CHEMOTAXIS,     
KEYWDS   4 HYDROLASE, CANCER, HIV-1 CO-RECEPTOR, CHEMOKINE, CXCL12, SDF1,       
KEYWDS   5 ISOTHIOUREA, IT1T, CHIMERA, T4L FUSION, MEMBRANE PROTEIN,            
KEYWDS   6 TRANSMEMBRANE, SINGNALING PROTEIN, PSI-BIOLOGY, GPCR NETWORK,        
KEYWDS   7 SIGNALING PROTEIN                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.WU,C.D.MOL,G.W.HAN,V.KATRITCH,E.Y.T.CHIEN,W.LIU,V.CHEREZOV,         
AUTHOR   2 R.C.STEVENS,ACCELERATED TECHNOLOGIES CENTER FOR GENE TO 3D STRUCTURE 
AUTHOR   3 (ATCG3D),GPCR NETWORK (GPCR)                                         
REVDAT   6   06-OCT-21 3OE9    1       REMARK SEQADV LINK                       
REVDAT   5   26-JUL-17 3OE9    1       SOURCE REMARK                            
REVDAT   4   02-MAY-12 3OE9    1       REMARK VERSN                             
REVDAT   3   16-FEB-11 3OE9    1       HEADER                                   
REVDAT   2   05-JAN-11 3OE9    1       JRNL                                     
REVDAT   1   27-OCT-10 3OE9    0                                                
JRNL        AUTH   B.WU,E.Y.CHIEN,C.D.MOL,G.FENALTI,W.LIU,V.KATRITCH,R.ABAGYAN, 
JRNL        AUTH 2 A.BROOUN,P.WELLS,F.C.BI,D.J.HAMEL,P.KUHN,T.M.HANDEL,         
JRNL        AUTH 3 V.CHEREZOV,R.C.STEVENS                                       
JRNL        TITL   STRUCTURES OF THE CXCR4 CHEMOKINE GPCR WITH SMALL-MOLECULE   
JRNL        TITL 2 AND CYCLIC PEPTIDE ANTAGONISTS.                              
JRNL        REF    SCIENCE                       V. 330  1066 2010              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   20929726                                                     
JRNL        DOI    10.1126/SCIENCE.1194396                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.8.0                                         
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.92                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 24209                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.254                          
REMARK   3   R VALUE            (WORKING SET)  : 0.252                          
REMARK   3   FREE R VALUE                      : 0.284                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.110                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1238                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 12                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.10                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.24                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2854                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2742                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2695                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2729                   
REMARK   3   BIN FREE R VALUE                        : 0.2969                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.57                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 159                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6726                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 54                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 64.28                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 105.2                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -7.31230                                             
REMARK   3    B22 (A**2) : 10.84260                                             
REMARK   3    B33 (A**2) : -3.53030                                             
REMARK   3    B12 (A**2) : -0.72090                                             
REMARK   3    B13 (A**2) : 2.52740                                              
REMARK   3    B23 (A**2) : 3.47380                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.821               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.894                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.883                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 6951   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 9449   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2323   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 135    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1011   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 6951   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 928    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 7932   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.009                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.40                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.41                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 23.70                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|28 - A|228 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):   16.4734    6.8035   12.9796           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3510 T22:    0.1647                                    
REMARK   3     T33:   -0.2206 T12:    0.0846                                    
REMARK   3     T13:   -0.0302 T23:   -0.0687                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.3063 L22:    1.5910                                    
REMARK   3     L33:    3.9389 L12:   -0.1305                                    
REMARK   3     L13:   -0.1757 L23:    1.8772                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.2796 S12:   -0.1275 S13:    0.4144                     
REMARK   3     S21:   -0.2893 S22:   -0.4561 S23:   -0.0326                     
REMARK   3     S31:   -0.1982 S32:   -0.2736 S33:    0.1765                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { A|1002 - A|1161 }                                    
REMARK   3    ORIGIN FOR THE GROUP (A):   14.4287  -21.2173  -21.6157           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1727 T22:    0.3080                                    
REMARK   3     T33:   -0.3235 T12:    0.0424                                    
REMARK   3     T13:   -0.0699 T23:   -0.0603                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.9397 L22:    4.0947                                    
REMARK   3     L33:    1.2030 L12:    1.3475                                    
REMARK   3     L13:    1.2099 L23:    1.4315                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0232 S12:   -0.3173 S13:    0.0325                     
REMARK   3     S21:    0.0768 S22:   -0.1125 S23:   -0.0353                     
REMARK   3     S31:    0.0199 S32:   -0.2459 S33:    0.1358                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { A|236 - A|303 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):   17.7056   -6.2519   18.1897           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2310 T22:    0.1231                                    
REMARK   3     T33:   -0.0374 T12:   -0.0638                                    
REMARK   3     T13:   -0.0266 T23:    0.0010                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.4927 L22:    1.1248                                    
REMARK   3     L33:    3.1549 L12:   -0.9749                                    
REMARK   3     L13:    0.3319 L23:    0.0596                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0140 S12:   -0.1143 S13:   -0.2250                     
REMARK   3     S21:    0.0661 S22:    0.0546 S23:   -0.1501                     
REMARK   3     S31:    0.1270 S32:   -0.0103 S33:   -0.0405                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { B|35 - B|228 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):  -16.6707   -7.3315   12.0396           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0962 T22:   -0.2256                                    
REMARK   3     T33:   -0.1974 T12:    0.0192                                    
REMARK   3     T13:    0.0158 T23:    0.0237                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.2595 L22:    2.1451                                    
REMARK   3     L33:    6.1044 L12:   -0.1748                                    
REMARK   3     L13:   -1.7488 L23:   -1.9412                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.3254 S12:    0.1598 S13:   -0.2068                     
REMARK   3     S21:   -0.2293 S22:   -0.5696 S23:   -0.1584                     
REMARK   3     S31:    0.5544 S32:    0.3182 S33:    0.2442                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: { B|1002 - B|1161 }                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -12.7978   20.4696  -21.8853           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2114 T22:   -0.0252                                    
REMARK   3     T33:   -0.2151 T12:    0.0340                                    
REMARK   3     T13:    0.0710 T23:    0.1198                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.1694 L22:    4.4694                                    
REMARK   3     L33:    3.2848 L12:   -0.7910                                    
REMARK   3     L13:   -0.9940 L23:   -0.9892                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.2185 S12:   -0.2826 S13:    0.0888                     
REMARK   3     S21:    0.1749 S22:    0.4085 S23:   -0.0891                     
REMARK   3     S31:   -0.0059 S32:   -0.3252 S33:   -0.1900                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: { B|236 - B|303 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -18.5824    6.1483   16.8941           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0247 T22:   -0.1118                                    
REMARK   3     T33:   -0.0226 T12:   -0.0516                                    
REMARK   3     T13:    0.1077 T23:    0.0248                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.4242 L22:    1.5655                                    
REMARK   3     L33:    3.0671 L12:   -0.6137                                    
REMARK   3     L13:   -1.3253 L23:   -2.6801                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0484 S12:   -0.0597 S13:    0.1125                     
REMARK   3     S21:    0.1702 S22:    0.0339 S23:    0.1186                     
REMARK   3     S31:   -0.2133 S32:    0.0370 S33:   -0.0822                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3OE9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-OCT-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000061005.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-APR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 9                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0330                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24209                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.12000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.27                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.26                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: LIPIDIC CUBIC PHASE MADE OF MONOOLEIN    
REMARK 280  AND CHOLESTEROL, 27-35% PEG400, 0.27-0.33M SODIUM MALONATE, 5MM     
REMARK 280  HEXAMINE COBALT CHLORIDE, 0.1M MES PH 6.0, LIPIDIC CUBIC PHASE,     
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1910 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 43680 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP A    -9                                                      
REMARK 465     TYR A    -8                                                      
REMARK 465     LYS A    -7                                                      
REMARK 465     ASP A    -6                                                      
REMARK 465     ASP A    -5                                                      
REMARK 465     ASP A    -4                                                      
REMARK 465     ASP A    -3                                                      
REMARK 465     ALA A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     PRO A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     ILE A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     ILE A     6                                                      
REMARK 465     TYR A     7                                                      
REMARK 465     THR A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     ASP A    10                                                      
REMARK 465     ASN A    11                                                      
REMARK 465     TYR A    12                                                      
REMARK 465     THR A    13                                                      
REMARK 465     GLU A    14                                                      
REMARK 465     GLU A    15                                                      
REMARK 465     MET A    16                                                      
REMARK 465     GLY A    17                                                      
REMARK 465     SER A    18                                                      
REMARK 465     GLY A    19                                                      
REMARK 465     ASP A    20                                                      
REMARK 465     TYR A    21                                                      
REMARK 465     ASP A    22                                                      
REMARK 465     SER A    23                                                      
REMARK 465     MET A    24                                                      
REMARK 465     LYS A    25                                                      
REMARK 465     GLU A    26                                                      
REMARK 465     PRO A    27                                                      
REMARK 465     GLU A    31                                                      
REMARK 465     GLU A    32                                                      
REMARK 465     ASN A    33                                                      
REMARK 465     ALA A    34                                                      
REMARK 465     ASP A  1020                                                      
REMARK 465     THR A  1021                                                      
REMARK 465     GLU A  1022                                                      
REMARK 465     SER A  1200                                                      
REMARK 465     GLY A  1201                                                      
REMARK 465     SER A  1202                                                      
REMARK 465     GLY A   231                                                      
REMARK 465     HIS A   232                                                      
REMARK 465     GLN A   233                                                      
REMARK 465     LYS A   234                                                      
REMARK 465     ARG A   235                                                      
REMARK 465     GLN A   272                                                      
REMARK 465     GLY A   273                                                      
REMARK 465     PHE A   304                                                      
REMARK 465     LEU A   305                                                      
REMARK 465     GLY A   306                                                      
REMARK 465     ALA A   307                                                      
REMARK 465     LYS A   308                                                      
REMARK 465     PHE A   309                                                      
REMARK 465     LYS A   310                                                      
REMARK 465     THR A   311                                                      
REMARK 465     SER A   312                                                      
REMARK 465     ALA A   313                                                      
REMARK 465     GLN A   314                                                      
REMARK 465     HIS A   315                                                      
REMARK 465     ALA A   316                                                      
REMARK 465     LEU A   317                                                      
REMARK 465     THR A   318                                                      
REMARK 465     SER A   319                                                      
REMARK 465     GLY A   320                                                      
REMARK 465     ARG A   321                                                      
REMARK 465     PRO A   322                                                      
REMARK 465     LEU A   323                                                      
REMARK 465     GLU A   324                                                      
REMARK 465     VAL A   325                                                      
REMARK 465     LEU A   326                                                      
REMARK 465     PHE A   327                                                      
REMARK 465     GLN A   328                                                      
REMARK 465     ASP B    -9                                                      
REMARK 465     TYR B    -8                                                      
REMARK 465     LYS B    -7                                                      
REMARK 465     ASP B    -6                                                      
REMARK 465     ASP B    -5                                                      
REMARK 465     ASP B    -4                                                      
REMARK 465     ASP B    -3                                                      
REMARK 465     ALA B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 465     PRO B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     ILE B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     ILE B     6                                                      
REMARK 465     TYR B     7                                                      
REMARK 465     THR B     8                                                      
REMARK 465     SER B     9                                                      
REMARK 465     ASP B    10                                                      
REMARK 465     ASN B    11                                                      
REMARK 465     TYR B    12                                                      
REMARK 465     THR B    13                                                      
REMARK 465     GLU B    14                                                      
REMARK 465     GLU B    15                                                      
REMARK 465     MET B    16                                                      
REMARK 465     GLY B    17                                                      
REMARK 465     SER B    18                                                      
REMARK 465     GLY B    19                                                      
REMARK 465     ASP B    20                                                      
REMARK 465     TYR B    21                                                      
REMARK 465     ASP B    22                                                      
REMARK 465     SER B    23                                                      
REMARK 465     MET B    24                                                      
REMARK 465     LYS B    25                                                      
REMARK 465     GLU B    26                                                      
REMARK 465     PRO B    27                                                      
REMARK 465     CYS B    28                                                      
REMARK 465     PHE B    29                                                      
REMARK 465     ARG B    30                                                      
REMARK 465     GLU B    31                                                      
REMARK 465     GLU B    32                                                      
REMARK 465     ASN B    33                                                      
REMARK 465     ALA B    34                                                      
REMARK 465     GLN B    66                                                      
REMARK 465     LYS B    67                                                      
REMARK 465     LYS B    68                                                      
REMARK 465     LEU B    69                                                      
REMARK 465     THR B  1021                                                      
REMARK 465     GLU B  1022                                                      
REMARK 465     GLY B  1023                                                      
REMARK 465     SER B  1200                                                      
REMARK 465     GLY B  1201                                                      
REMARK 465     SER B  1202                                                      
REMARK 465     GLY B   231                                                      
REMARK 465     HIS B   232                                                      
REMARK 465     GLN B   233                                                      
REMARK 465     LYS B   234                                                      
REMARK 465     ARG B   235                                                      
REMARK 465     PHE B   304                                                      
REMARK 465     LEU B   305                                                      
REMARK 465     GLY B   306                                                      
REMARK 465     ALA B   307                                                      
REMARK 465     LYS B   308                                                      
REMARK 465     PHE B   309                                                      
REMARK 465     LYS B   310                                                      
REMARK 465     THR B   311                                                      
REMARK 465     SER B   312                                                      
REMARK 465     ALA B   313                                                      
REMARK 465     GLN B   314                                                      
REMARK 465     HIS B   315                                                      
REMARK 465     ALA B   316                                                      
REMARK 465     LEU B   317                                                      
REMARK 465     THR B   318                                                      
REMARK 465     SER B   319                                                      
REMARK 465     GLY B   320                                                      
REMARK 465     ARG B   321                                                      
REMARK 465     PRO B   322                                                      
REMARK 465     LEU B   323                                                      
REMARK 465     GLU B   324                                                      
REMARK 465     VAL B   325                                                      
REMARK 465     LEU B   326                                                      
REMARK 465     PHE B   327                                                      
REMARK 465     GLN B   328                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER A 144    OG                                                  
REMARK 470     LYS A 236    CG   CD   CE   NZ                                   
REMARK 470     LEU A 238    CD1  CD2                                            
REMARK 470     ILE A 300    CG1  CG2  CD1                                       
REMARK 470     LYS B 236    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH1  ARG B  1014     CG2  THR B  1026              2.04            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PRO A 147   CD    PRO A 147   N       0.086                       
REMARK 500    HIS B 228   C     ASN B1002   N       0.214                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLN A  66   CB  -  CA  -  C   ANGL. DEV. = -16.9 DEGREES          
REMARK 500    LYS A  67   N   -  CA  -  CB  ANGL. DEV. = -12.2 DEGREES          
REMARK 500    LYS A  68   CB  -  CA  -  C   ANGL. DEV. = -16.8 DEGREES          
REMARK 500    LYS A  68   N   -  CA  -  C   ANGL. DEV. =  35.1 DEGREES          
REMARK 500    LEU A  69   N   -  CA  -  CB  ANGL. DEV. =  13.6 DEGREES          
REMARK 500    ASP A  74   CB  -  CG  -  OD2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    ALA A 100   N   -  CA  -  C   ANGL. DEV. =  17.9 DEGREES          
REMARK 500    ARG A 146   CB  -  CA  -  C   ANGL. DEV. =  17.3 DEGREES          
REMARK 500    ARG A 146   N   -  CA  -  CB  ANGL. DEV. = -12.8 DEGREES          
REMARK 500    PRO A 147   C   -  N   -  CD  ANGL. DEV. = -19.7 DEGREES          
REMARK 500    PRO A 147   N   -  CA  -  C   ANGL. DEV. = -18.4 DEGREES          
REMARK 500    PRO A 191   CB  -  CA  -  C   ANGL. DEV. = -19.2 DEGREES          
REMARK 500    PRO A 191   N   -  CA  -  C   ANGL. DEV. =  23.0 DEGREES          
REMARK 500    ASN A 192   N   -  CA  -  C   ANGL. DEV. = -27.3 DEGREES          
REMARK 500    ASP A 193   N   -  CA  -  CB  ANGL. DEV. = -16.0 DEGREES          
REMARK 500    ALA B 100   CB  -  CA  -  C   ANGL. DEV. = -20.0 DEGREES          
REMARK 500    ALA B 100   N   -  CA  -  C   ANGL. DEV. =  29.9 DEGREES          
REMARK 500    TRP B 102   N   -  CA  -  C   ANGL. DEV. = -21.5 DEGREES          
REMARK 500    GLU B 153   CB  -  CA  -  C   ANGL. DEV. =  17.2 DEGREES          
REMARK 500    LYS B 154   N   -  CA  -  CB  ANGL. DEV. = -12.6 DEGREES          
REMARK 500    VAL B 158   CB  -  CA  -  C   ANGL. DEV. =  14.6 DEGREES          
REMARK 500    ASN B1002   C   -  N   -  CA  ANGL. DEV. =  23.6 DEGREES          
REMARK 500    LYS B1019   CB  -  CA  -  C   ANGL. DEV. =  18.6 DEGREES          
REMARK 500    ALA B 237   CB  -  CA  -  C   ANGL. DEV. =  -9.0 DEGREES          
REMARK 500    GLU B 268   N   -  CA  -  C   ANGL. DEV. =  20.0 DEGREES          
REMARK 500    GLN B 272   CB  -  CA  -  C   ANGL. DEV. =  15.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    CYS A 296       52.21    -91.12                                   
REMARK 500    LEU A 297      -36.95   -130.84                                   
REMARK 500    MET B  72      -13.25     78.15                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    HIS B 228        -18.71                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ITD A 1500                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ITD B 1500                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: ATCG3D_11   RELATED DB: TARGETDB                         
REMARK 900 RELATED ID: 3ODU   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN AT 2.5 A IN P21 SPACEGROUP                              
REMARK 900 RELATED ID: 3OE0   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN IN COMPLEX WITH A CYCLIC PEPTIDE CVX15                  
REMARK 900 RELATED ID: 3OE6   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN IN I222 SPACEGROUP                                      
REMARK 900 RELATED ID: 3OE8   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN IN P1 SPACEGROUP WITH 3 MOLECULES PER ASYMMETRIC UNIT   
REMARK 900 RELATED ID: GPCR-34   RELATED DB: TARGETTRACK                        
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE PROTEIN IS A FUSION PROTEIN WITH RESIDUES ASN1002-TYR1161 OF T4  
REMARK 999 LYSOZYME INSERTED BETWEEN HIS228 AND GLY231 OF CXCR4, AS INDICATED   
REMARK 999 AS CXCR4-3 IN THE PUBLICATION.                                       
DBREF  3OE9 A    2   228  UNP    P61073   CXCR4_HUMAN      2    228             
DBREF  3OE9 A 1002  1161  UNP    P00720   LYS_BPT4      1002   1161             
DBREF  3OE9 A  231   319  UNP    P61073   CXCR4_HUMAN    231    319             
DBREF  3OE9 B    2   228  UNP    P61073   CXCR4_HUMAN      2    228             
DBREF  3OE9 B 1002  1161  UNP    P00720   LYS_BPT4      1002   1161             
DBREF  3OE9 B  231   319  UNP    P61073   CXCR4_HUMAN    231    319             
SEQADV 3OE9 ASP A   -9  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 TYR A   -8  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 LYS A   -7  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 ASP A   -6  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 ASP A   -5  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 ASP A   -4  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 ASP A   -3  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 ALA A   -2  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 GLY A   -1  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 ALA A    0  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 PRO A    1  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 TRP A  125  UNP  P61073    LEU   125 ENGINEERED MUTATION            
SEQADV 3OE9 THR A 1054  UNP  P00720    CYS  1054 ENGINEERED MUTATION            
SEQADV 3OE9 ALA A 1097  UNP  P00720    CYS  1097 ENGINEERED MUTATION            
SEQADV 3OE9 SER A 1200  UNP  P61073              LINKER                         
SEQADV 3OE9 GLY A 1201  UNP  P61073              LINKER                         
SEQADV 3OE9 SER A 1202  UNP  P61073              LINKER                         
SEQADV 3OE9 PRO A  240  UNP  P61073    THR   240 ENGINEERED MUTATION            
SEQADV 3OE9 GLY A  320  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 ARG A  321  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 PRO A  322  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 LEU A  323  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 GLU A  324  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 VAL A  325  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 LEU A  326  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 PHE A  327  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 GLN A  328  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 ASP B   -9  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 TYR B   -8  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 LYS B   -7  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 ASP B   -6  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 ASP B   -5  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 ASP B   -4  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 ASP B   -3  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 ALA B   -2  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 GLY B   -1  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 ALA B    0  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 PRO B    1  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 TRP B  125  UNP  P61073    LEU   125 ENGINEERED MUTATION            
SEQADV 3OE9 THR B 1054  UNP  P00720    CYS  1054 ENGINEERED MUTATION            
SEQADV 3OE9 ALA B 1097  UNP  P00720    CYS  1097 ENGINEERED MUTATION            
SEQADV 3OE9 SER B 1200  UNP  P61073              LINKER                         
SEQADV 3OE9 GLY B 1201  UNP  P61073              LINKER                         
SEQADV 3OE9 SER B 1202  UNP  P61073              LINKER                         
SEQADV 3OE9 PRO B  240  UNP  P61073    THR   240 ENGINEERED MUTATION            
SEQADV 3OE9 GLY B  320  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 ARG B  321  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 PRO B  322  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 LEU B  323  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 GLU B  324  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 VAL B  325  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 LEU B  326  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 PHE B  327  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE9 GLN B  328  UNP  P61073              EXPRESSION TAG                 
SEQRES   1 A  499  ASP TYR LYS ASP ASP ASP ASP ALA GLY ALA PRO GLU GLY          
SEQRES   2 A  499  ILE SER ILE TYR THR SER ASP ASN TYR THR GLU GLU MET          
SEQRES   3 A  499  GLY SER GLY ASP TYR ASP SER MET LYS GLU PRO CYS PHE          
SEQRES   4 A  499  ARG GLU GLU ASN ALA ASN PHE ASN LYS ILE PHE LEU PRO          
SEQRES   5 A  499  THR ILE TYR SER ILE ILE PHE LEU THR GLY ILE VAL GLY          
SEQRES   6 A  499  ASN GLY LEU VAL ILE LEU VAL MET GLY TYR GLN LYS LYS          
SEQRES   7 A  499  LEU ARG SER MET THR ASP LYS TYR ARG LEU HIS LEU SER          
SEQRES   8 A  499  VAL ALA ASP LEU LEU PHE VAL ILE THR LEU PRO PHE TRP          
SEQRES   9 A  499  ALA VAL ASP ALA VAL ALA ASN TRP TYR PHE GLY ASN PHE          
SEQRES  10 A  499  LEU CYS LYS ALA VAL HIS VAL ILE TYR THR VAL ASN LEU          
SEQRES  11 A  499  TYR SER SER VAL TRP ILE LEU ALA PHE ILE SER LEU ASP          
SEQRES  12 A  499  ARG TYR LEU ALA ILE VAL HIS ALA THR ASN SER GLN ARG          
SEQRES  13 A  499  PRO ARG LYS LEU LEU ALA GLU LYS VAL VAL TYR VAL GLY          
SEQRES  14 A  499  VAL TRP ILE PRO ALA LEU LEU LEU THR ILE PRO ASP PHE          
SEQRES  15 A  499  ILE PHE ALA ASN VAL SER GLU ALA ASP ASP ARG TYR ILE          
SEQRES  16 A  499  CYS ASP ARG PHE TYR PRO ASN ASP LEU TRP VAL VAL VAL          
SEQRES  17 A  499  PHE GLN PHE GLN HIS ILE MET VAL GLY LEU ILE LEU PRO          
SEQRES  18 A  499  GLY ILE VAL ILE LEU SER CYS TYR CYS ILE ILE ILE SER          
SEQRES  19 A  499  LYS LEU SER HIS ASN ILE PHE GLU MET LEU ARG ILE ASP          
SEQRES  20 A  499  GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP THR GLU GLY          
SEQRES  21 A  499  TYR TYR THR ILE GLY ILE GLY HIS LEU LEU THR LYS SER          
SEQRES  22 A  499  PRO SER LEU ASN ALA ALA LYS SER GLU LEU ASP LYS ALA          
SEQRES  23 A  499  ILE GLY ARG ASN THR ASN GLY VAL ILE THR LYS ASP GLU          
SEQRES  24 A  499  ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP ALA ALA VAL          
SEQRES  25 A  499  ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS PRO VAL TYR          
SEQRES  26 A  499  ASP SER LEU ASP ALA VAL ARG ARG ALA ALA LEU ILE ASN          
SEQRES  27 A  499  MET VAL PHE GLN MET GLY GLU THR GLY VAL ALA GLY PHE          
SEQRES  28 A  499  THR ASN SER LEU ARG MET LEU GLN GLN LYS ARG TRP ASP          
SEQRES  29 A  499  GLU ALA ALA VAL ASN LEU ALA LYS SER ARG TRP TYR ASN          
SEQRES  30 A  499  GLN THR PRO ASN ARG ALA LYS ARG VAL ILE THR THR PHE          
SEQRES  31 A  499  ARG THR GLY THR TRP ASP ALA TYR SER GLY SER GLY HIS          
SEQRES  32 A  499  GLN LYS ARG LYS ALA LEU LYS PRO THR VAL ILE LEU ILE          
SEQRES  33 A  499  LEU ALA PHE PHE ALA CYS TRP LEU PRO TYR TYR ILE GLY          
SEQRES  34 A  499  ILE SER ILE ASP SER PHE ILE LEU LEU GLU ILE ILE LYS          
SEQRES  35 A  499  GLN GLY CYS GLU PHE GLU ASN THR VAL HIS LYS TRP ILE          
SEQRES  36 A  499  SER ILE THR GLU ALA LEU ALA PHE PHE HIS CYS CYS LEU          
SEQRES  37 A  499  ASN PRO ILE LEU TYR ALA PHE LEU GLY ALA LYS PHE LYS          
SEQRES  38 A  499  THR SER ALA GLN HIS ALA LEU THR SER GLY ARG PRO LEU          
SEQRES  39 A  499  GLU VAL LEU PHE GLN                                          
SEQRES   1 B  499  ASP TYR LYS ASP ASP ASP ASP ALA GLY ALA PRO GLU GLY          
SEQRES   2 B  499  ILE SER ILE TYR THR SER ASP ASN TYR THR GLU GLU MET          
SEQRES   3 B  499  GLY SER GLY ASP TYR ASP SER MET LYS GLU PRO CYS PHE          
SEQRES   4 B  499  ARG GLU GLU ASN ALA ASN PHE ASN LYS ILE PHE LEU PRO          
SEQRES   5 B  499  THR ILE TYR SER ILE ILE PHE LEU THR GLY ILE VAL GLY          
SEQRES   6 B  499  ASN GLY LEU VAL ILE LEU VAL MET GLY TYR GLN LYS LYS          
SEQRES   7 B  499  LEU ARG SER MET THR ASP LYS TYR ARG LEU HIS LEU SER          
SEQRES   8 B  499  VAL ALA ASP LEU LEU PHE VAL ILE THR LEU PRO PHE TRP          
SEQRES   9 B  499  ALA VAL ASP ALA VAL ALA ASN TRP TYR PHE GLY ASN PHE          
SEQRES  10 B  499  LEU CYS LYS ALA VAL HIS VAL ILE TYR THR VAL ASN LEU          
SEQRES  11 B  499  TYR SER SER VAL TRP ILE LEU ALA PHE ILE SER LEU ASP          
SEQRES  12 B  499  ARG TYR LEU ALA ILE VAL HIS ALA THR ASN SER GLN ARG          
SEQRES  13 B  499  PRO ARG LYS LEU LEU ALA GLU LYS VAL VAL TYR VAL GLY          
SEQRES  14 B  499  VAL TRP ILE PRO ALA LEU LEU LEU THR ILE PRO ASP PHE          
SEQRES  15 B  499  ILE PHE ALA ASN VAL SER GLU ALA ASP ASP ARG TYR ILE          
SEQRES  16 B  499  CYS ASP ARG PHE TYR PRO ASN ASP LEU TRP VAL VAL VAL          
SEQRES  17 B  499  PHE GLN PHE GLN HIS ILE MET VAL GLY LEU ILE LEU PRO          
SEQRES  18 B  499  GLY ILE VAL ILE LEU SER CYS TYR CYS ILE ILE ILE SER          
SEQRES  19 B  499  LYS LEU SER HIS ASN ILE PHE GLU MET LEU ARG ILE ASP          
SEQRES  20 B  499  GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP THR GLU GLY          
SEQRES  21 B  499  TYR TYR THR ILE GLY ILE GLY HIS LEU LEU THR LYS SER          
SEQRES  22 B  499  PRO SER LEU ASN ALA ALA LYS SER GLU LEU ASP LYS ALA          
SEQRES  23 B  499  ILE GLY ARG ASN THR ASN GLY VAL ILE THR LYS ASP GLU          
SEQRES  24 B  499  ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP ALA ALA VAL          
SEQRES  25 B  499  ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS PRO VAL TYR          
SEQRES  26 B  499  ASP SER LEU ASP ALA VAL ARG ARG ALA ALA LEU ILE ASN          
SEQRES  27 B  499  MET VAL PHE GLN MET GLY GLU THR GLY VAL ALA GLY PHE          
SEQRES  28 B  499  THR ASN SER LEU ARG MET LEU GLN GLN LYS ARG TRP ASP          
SEQRES  29 B  499  GLU ALA ALA VAL ASN LEU ALA LYS SER ARG TRP TYR ASN          
SEQRES  30 B  499  GLN THR PRO ASN ARG ALA LYS ARG VAL ILE THR THR PHE          
SEQRES  31 B  499  ARG THR GLY THR TRP ASP ALA TYR SER GLY SER GLY HIS          
SEQRES  32 B  499  GLN LYS ARG LYS ALA LEU LYS PRO THR VAL ILE LEU ILE          
SEQRES  33 B  499  LEU ALA PHE PHE ALA CYS TRP LEU PRO TYR TYR ILE GLY          
SEQRES  34 B  499  ILE SER ILE ASP SER PHE ILE LEU LEU GLU ILE ILE LYS          
SEQRES  35 B  499  GLN GLY CYS GLU PHE GLU ASN THR VAL HIS LYS TRP ILE          
SEQRES  36 B  499  SER ILE THR GLU ALA LEU ALA PHE PHE HIS CYS CYS LEU          
SEQRES  37 B  499  ASN PRO ILE LEU TYR ALA PHE LEU GLY ALA LYS PHE LYS          
SEQRES  38 B  499  THR SER ALA GLN HIS ALA LEU THR SER GLY ARG PRO LEU          
SEQRES  39 B  499  GLU VAL LEU PHE GLN                                          
HET    ITD  A1500      27                                                       
HET    ITD  B1500      27                                                       
HETNAM     ITD (6,6-DIMETHYL-5,6-DIHYDROIMIDAZO[2,1-B][1,3]THIAZOL-3-           
HETNAM   2 ITD  YL)METHYL N,N'-DICYCLOHEXYLIMIDOTHIOCARBAMATE                   
FORMUL   3  ITD    2(C21 H34 N4 S2)                                             
HELIX    1   1 PHE A   40  TYR A   65  1                                  26    
HELIX    2   2 SER A   71  ILE A   89  1                                  19    
HELIX    3   3 THR A   90  ALA A  100  1                                  11    
HELIX    4   4 GLY A  105  VAL A  139  1                                  35    
HELIX    5   5 PRO A  147  LYS A  154  1                                   8    
HELIX    6   6 LYS A  154  VAL A  160  1                                   7    
HELIX    7   7 VAL A  160  LEU A  167  1                                   8    
HELIX    8   8 ILE A  169  PHE A  174  1                                   6    
HELIX    9   9 ASP A  193  VAL A  198  1                                   6    
HELIX   10  10 VAL A  198  LEU A  208  1                                  11    
HELIX   11  11 LEU A  208  SER A  227  1                                  20    
HELIX   12  12 HIS A  228  GLU A 1011  1                                  11    
HELIX   13  13 SER A 1038  GLY A 1051  1                                  14    
HELIX   14  14 THR A 1059  LEU A 1079  1                                  21    
HELIX   15  15 LYS A 1083  LEU A 1091  1                                   9    
HELIX   16  16 ASP A 1092  PHE A 1104  1                                  13    
HELIX   17  17 GLY A 1107  GLY A 1113  1                                   7    
HELIX   18  18 PHE A 1114  GLN A 1123  1                                  10    
HELIX   19  19 ARG A 1125  LYS A 1135  1                                  11    
HELIX   20  20 THR A 1142  GLY A 1156  1                                  15    
HELIX   21  21 LEU A  238  LEU A  267  1                                  30    
HELIX   22  22 CYS A  274  PHE A  292  1                                  19    
HELIX   23  23 PHE A  293  TYR A  302  5                                  10    
HELIX   24  24 PHE B   36  MET B   63  1                                  28    
HELIX   25  25 ASP B   74  ALA B  100  1                                  27    
HELIX   26  26 PHE B  104  VAL B  139  1                                  36    
HELIX   27  27 PRO B  147  ALA B  152  1                                   6    
HELIX   28  28 LYS B  154  VAL B  160  1                                   7    
HELIX   29  29 VAL B  160  LEU B  166  1                                   7    
HELIX   30  30 THR B  168  PHE B  174  1                                   7    
HELIX   31  31 ASN B  192  LEU B  208  1                                  17    
HELIX   32  32 LEU B  208  GLU B 1011  1                                  31    
HELIX   33  33 SER B 1038  ILE B 1050  1                                  13    
HELIX   34  34 THR B 1059  LEU B 1079  1                                  21    
HELIX   35  35 LEU B 1084  LEU B 1091  1                                   8    
HELIX   36  36 ASP B 1092  MET B 1106  1                                  15    
HELIX   37  37 GLY B 1107  ALA B 1112  1                                   6    
HELIX   38  38 PHE B 1114  GLN B 1122  1                                   9    
HELIX   39  39 ARG B 1125  ALA B 1134  1                                  10    
HELIX   40  40 SER B 1136  THR B 1142  1                                   7    
HELIX   41  41 THR B 1142  GLY B 1156  1                                  15    
HELIX   42  42 LEU B  238  LEU B  267  1                                  30    
HELIX   43  43 GLY B  273  ALA B  291  1                                  19    
HELIX   44  44 PHE B  292  CYS B  296  5                                   5    
SHEET    1   A 2 ALA A 175  SER A 178  0                                        
SHEET    2   A 2 ILE A 185  ARG A 188 -1  O  ILE A 185   N  SER A 178           
SHEET    1   B 3 LEU A1013  TYR A1018  0                                        
SHEET    2   B 3 TYR A1025  ILE A1029 -1  O  THR A1026   N  TYR A1018           
SHEET    3   B 3 HIS A1031  THR A1034 -1  O  HIS A1031   N  ILE A1027           
SHEET    1   C 2 ALA B 175  SER B 178  0                                        
SHEET    2   C 2 ILE B 185  ARG B 188 -1  O  ILE B 185   N  SER B 178           
SHEET    1   D 3 LEU B1013  ARG B1014  0                                        
SHEET    2   D 3 TYR B1025  ILE B1029 -1  O  GLY B1028   N  ARG B1014           
SHEET    3   D 3 HIS B1031  THR B1034 -1  O  LEU B1033   N  TYR B1025           
SSBOND   1 CYS A   28    CYS A  274                          1555   1555  2.04  
SSBOND   2 CYS A  109    CYS A  186                          1555   1555  2.04  
SSBOND   3 CYS B  109    CYS B  186                          1555   1555  2.03  
LINK         C   HIS A 228                 N   ASN A1002     1555   1555  1.33  
LINK         C   HIS B 228                 N   ASN B1002     1555   1555  1.55  
SITE     1 AC1 10 LYS A  38  TRP A  94  ASP A  97  VAL A 112                    
SITE     2 AC1 10 HIS A 113  ARG A 183  CYS A 186  ASP A 187                    
SITE     3 AC1 10 ARG A 188  GLU A 288                                          
SITE     1 AC2 10 TRP B  94  ASP B  97  VAL B 112  TYR B 116                    
SITE     2 AC2 10 ARG B 183  ILE B 185  CYS B 186  ASP B 187                    
SITE     3 AC2 10 ARG B 188  GLU B 288                                          
CRYST1   72.497   72.739   84.273  64.66  73.93  61.31 P 1           2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013794 -0.007549 -0.001421        0.00000                         
SCALE2      0.000000  0.015672 -0.005857        0.00000                         
SCALE3      0.000000  0.000000  0.013183        0.00000                         
ATOM      1  N   CYS A  28      11.149  -6.211  42.367  1.00161.33           N  
ANISOU    1  N   CYS A  28    18165  29916  13216  -4543    426   1769       N  
ATOM      2  CA  CYS A  28      12.481  -6.322  41.770  1.00158.89           C  
ANISOU    2  CA  CYS A  28    18017  29188  13165  -4094    196   1965       C  
ATOM      3  C   CYS A  28      13.252  -4.991  41.797  1.00160.62           C  
ANISOU    3  C   CYS A  28    17869  29680  13480  -3781     36   1551       C  
ATOM      4  O   CYS A  28      12.675  -3.949  42.123  1.00159.58           O  
ANISOU    4  O   CYS A  28    17365  29978  13289  -3896    104   1075       O  
ATOM      5  CB  CYS A  28      12.399  -6.895  40.356  1.00156.08           C  
ANISOU    5  CB  CYS A  28    17896  28111  13298  -3991    200   2026       C  
ATOM      6  SG  CYS A  28      11.923  -8.643  40.283  1.00163.77           S  
ANISOU    6  SG  CYS A  28    19388  28617  14219  -4272    335   2605       S  
ATOM      7  N   PHE A  29      14.557  -5.036  41.457  1.00156.10           N  
ANISOU    7  N   PHE A  29    17394  28852  13064  -3391   -170   1716       N  
ATOM      8  CA  PHE A  29      15.443  -3.872  41.423  1.00153.54           C  
ANISOU    8  CA  PHE A  29    16755  28721  12862  -3096   -321   1362       C  
ATOM      9  C   PHE A  29      16.318  -3.829  40.171  1.00153.59           C  
ANISOU    9  C   PHE A  29    16854  28166  13338  -2743   -450   1359       C  
ATOM     10  O   PHE A  29      16.639  -4.876  39.608  1.00153.28           O  
ANISOU   10  O   PHE A  29    17156  27656  13427  -2640   -491   1744       O  
ATOM     11  CB  PHE A  29      16.310  -3.827  42.690  1.00158.83           C  
ANISOU   11  CB  PHE A  29    17351  29910  13088  -2999   -451   1526       C  
ATOM     12  CG  PHE A  29      15.817  -2.848  43.724  1.00162.10           C  
ANISOU   12  CG  PHE A  29    17377  31028  13187  -3197   -381   1126       C  
ATOM     13  CD1 PHE A  29      16.350  -1.568  43.802  1.00163.47           C  
ANISOU   13  CD1 PHE A  29    17170  31465  13477  -3025   -469    642       C  
ATOM     14  CD2 PHE A  29      14.804  -3.198  44.611  1.00167.92           C  
ANISOU   14  CD2 PHE A  29    18121  32166  13516  -3571   -215   1209       C  
ATOM     15  CE1 PHE A  29      15.884  -0.656  44.753  1.00166.08           C  
ANISOU   15  CE1 PHE A  29    17129  32438  13536  -3201   -406    228       C  
ATOM     16  CE2 PHE A  29      14.335  -2.284  45.557  1.00172.34           C  
ANISOU   16  CE2 PHE A  29    18296  33407  13780  -3748   -148    797       C  
ATOM     17  CZ  PHE A  29      14.879  -1.019  45.623  1.00168.51           C  
ANISOU   17  CZ  PHE A  29    17432  33166  13430  -3551   -251    299       C  
ATOM     18  N   ARG A  30      16.706  -2.610  39.746  1.00147.20           N  
ANISOU   18  N   ARG A  30    15740  27409  12783  -2567   -507    915       N  
ATOM     19  CA  ARG A  30      17.555  -2.378  38.574  1.00143.65           C  
ANISOU   19  CA  ARG A  30    15323  26499  12760  -2252   -610    855       C  
ATOM     20  C   ARG A  30      19.037  -2.267  38.960  1.00147.39           C  
ANISOU   20  C   ARG A  30    15739  27110  13150  -1957   -801    958       C  
ATOM     21  O   ARG A  30      19.393  -1.537  39.885  1.00147.87           O  
ANISOU   21  O   ARG A  30    15531  27674  12981  -1959   -851    751       O  
ATOM     22  CB  ARG A  30      17.097  -1.125  37.803  1.00141.52           C  
ANISOU   22  CB  ARG A  30    14783  26154  12833  -2243   -545    338       C  
ATOM     23  CG  ARG A  30      16.027  -1.403  36.756  1.00151.56           C  
ANISOU   23  CG  ARG A  30    16182  27036  14370  -2359   -421    287       C  
ATOM     24  CD  ARG A  30      15.260  -0.145  36.390  1.00161.08           C  
ANISOU   24  CD  ARG A  30    17094  28335  15775  -2408   -345   -228       C  
ATOM     25  NE  ARG A  30      13.991  -0.053  37.113  1.00171.27           N  
ANISOU   25  NE  ARG A  30    18250  30001  16826  -2721   -209   -404       N  
ATOM     26  CZ  ARG A  30      13.807   0.639  38.235  1.00185.46           C  
ANISOU   26  CZ  ARG A  30    19775  32340  18352  -2844   -188   -652       C  
ATOM     27  NH1 ARG A  30      14.810   1.318  38.778  1.00172.41           N  
ANISOU   27  NH1 ARG A  30    17954  30916  16640  -2685   -298   -762       N  
ATOM     28  NH2 ARG A  30      12.617   0.661  38.818  1.00172.20           N  
ANISOU   28  NH2 ARG A  30    17969  31004  16457  -3135    -52   -822       N  
ATOM     29  N   ASN A  35      24.373  -4.353  36.780  1.00144.21           N  
ANISOU   29  N   ASN A  35    15836  25578  13380   -516  -1482   1810       N  
ATOM     30  CA  ASN A  35      25.370  -3.480  36.170  1.00141.55           C  
ANISOU   30  CA  ASN A  35    15234  25249  13300   -311  -1541   1489       C  
ATOM     31  C   ASN A  35      26.730  -4.174  35.993  1.00145.77           C  
ANISOU   31  C   ASN A  35    15841  25687  13856     59  -1735   1704       C  
ATOM     32  O   ASN A  35      27.766  -3.668  36.445  1.00146.56           O  
ANISOU   32  O   ASN A  35    15683  26142  13862    227  -1857   1547       O  
ATOM     33  CB  ASN A  35      25.478  -2.143  36.933  1.00143.58           C  
ANISOU   33  CB  ASN A  35    15092  26032  13429   -425  -1522   1078       C  
ATOM     34  CG  ASN A  35      24.411  -1.116  36.602  1.00167.16           C  
ANISOU   34  CG  ASN A  35    17928  28993  16592   -691  -1338    710       C  
ATOM     35  OD1 ASN A  35      23.471  -1.355  35.828  1.00158.19           O  
ANISOU   35  OD1 ASN A  35    16967  27491  15647   -813  -1217    747       O  
ATOM     36  ND2 ASN A  35      24.556   0.075  37.165  1.00160.45           N  
ANISOU   36  ND2 ASN A  35    16736  28532  15694   -770  -1322    318       N  
ATOM     37  N   PHE A  36      26.715  -5.339  35.319  1.00141.72           N  
ANISOU   37  N   PHE A  36    15668  24697  13481    188  -1763   2032       N  
ATOM     38  CA  PHE A  36      27.905  -6.136  35.006  1.00142.75           C  
ANISOU   38  CA  PHE A  36    15906  24654  13680    565  -1946   2240       C  
ATOM     39  C   PHE A  36      28.447  -5.673  33.645  1.00142.33           C  
ANISOU   39  C   PHE A  36    15725  24310  14042    698  -1907   1962       C  
ATOM     40  O   PHE A  36      29.661  -5.519  33.479  1.00142.13           O  
ANISOU   40  O   PHE A  36    15526  24399  14077    967  -2032   1859       O  
ATOM     41  CB  PHE A  36      27.564  -7.644  35.014  1.00147.06           C  
ANISOU   41  CB  PHE A  36    16897  24808  14170    627  -1989   2726       C  
ATOM     42  CG  PHE A  36      28.634  -8.592  34.516  1.00150.10           C  
ANISOU   42  CG  PHE A  36    17445  24894  14693   1031  -2168   2940       C  
ATOM     43  CD1 PHE A  36      29.801  -8.797  35.243  1.00156.29           C  
ANISOU   43  CD1 PHE A  36    18135  25994  15255   1356  -2395   3055       C  
ATOM     44  CD2 PHE A  36      28.445  -9.327  33.351  1.00150.79           C  
ANISOU   44  CD2 PHE A  36    17775  24402  15117   1099  -2120   3018       C  
ATOM     45  CE1 PHE A  36      30.782  -9.684  34.788  1.00159.02           C  
ANISOU   45  CE1 PHE A  36    18616  26071  15732   1760  -2573   3230       C  
ATOM     46  CE2 PHE A  36      29.425 -10.220  32.900  1.00155.40           C  
ANISOU   46  CE2 PHE A  36    18499  24710  15837   1488  -2289   3186       C  
ATOM     47  CZ  PHE A  36      30.585 -10.392  33.622  1.00156.72           C  
ANISOU   47  CZ  PHE A  36    18566  25186  15795   1823  -2516   3292       C  
ATOM     48  N   ASN A  37      27.552  -5.366  32.704  1.00134.98           N  
ANISOU   48  N   ASN A  37    14850  23063  13375    500  -1729   1812       N  
ATOM     49  CA  ASN A  37      27.949  -4.928  31.355  1.00131.22           C  
ANISOU   49  CA  ASN A  37    14281  22309  13269    600  -1670   1575       C  
ATOM     50  C   ASN A  37      27.997  -3.405  31.099  1.00131.57           C  
ANISOU   50  C   ASN A  37    13991  22556  13445    469  -1562   1149       C  
ATOM     51  O   ASN A  37      27.964  -2.959  29.952  1.00128.61           O  
ANISOU   51  O   ASN A  37    13582  21924  13360    468  -1463    972       O  
ATOM     52  CB  ASN A  37      27.066  -5.601  30.300  1.00129.49           C  
ANISOU   52  CB  ASN A  37    14339  21583  13276    523  -1561   1680       C  
ATOM     53  CG  ASN A  37      27.244  -7.106  30.265  1.00152.39           C  
ANISOU   53  CG  ASN A  37    17574  24171  16157    700  -1666   2058       C  
ATOM     54  OD1 ASN A  37      26.499  -7.846  30.907  1.00148.08           O  
ANISOU   54  OD1 ASN A  37    17264  23563  15435    556  -1653   2327       O  
ATOM     55  ND2 ASN A  37      28.236  -7.567  29.512  1.00144.55           N  
ANISOU   55  ND2 ASN A  37    16602  22969  15350   1006  -1764   2074       N  
ATOM     56  N   LYS A  38      28.079  -2.629  32.174  1.00128.33           N  
ANISOU   56  N   LYS A  38    13344  22602  12815    360  -1581    991       N  
ATOM     57  CA  LYS A  38      28.217  -1.168  32.146  1.00125.95           C  
ANISOU   57  CA  LYS A  38    12715  22515  12624    236  -1493    577       C  
ATOM     58  C   LYS A  38      29.544  -0.428  31.960  1.00128.32           C  
ANISOU   58  C   LYS A  38    12723  22991  13042    381  -1540    320       C  
ATOM     59  O   LYS A  38      29.543   0.797  31.827  1.00126.57           O  
ANISOU   59  O   LYS A  38    12269  22860  12961    240  -1435    -21       O  
ATOM     60  CB  LYS A  38      27.514  -0.748  33.450  1.00130.11           C  
ANISOU   60  CB  LYS A  38    13133  23455  12849     17  -1477    505       C  
ATOM     61  CG  LYS A  38      25.988  -0.860  33.390  1.00144.05           C  
ANISOU   61  CG  LYS A  38    15068  25063  14602   -235  -1340    554       C  
ATOM     62  CD  LYS A  38      25.322   0.224  32.523  1.00150.56           C  
ANISOU   62  CD  LYS A  38    15787  25692  15728   -375  -1181    224       C  
ATOM     63  CE  LYS A  38      23.866  -0.064  32.233  1.00160.34           C  
ANISOU   63  CE  LYS A  38    17206  26729  16988   -568  -1064    282       C  
ATOM     64  NZ  LYS A  38      23.686  -1.231  31.322  1.00167.58           N  
ANISOU   64  NZ  LYS A  38    18433  27214  18027   -478  -1066    575       N  
ATOM     65  N   ILE A  39      30.670  -1.175  31.940  1.00125.36           N  
ANISOU   65  N   ILE A  39    12357  22655  12620    662  -1694    472       N  
ATOM     66  CA  ILE A  39      32.030  -0.668  31.697  1.00125.09           C  
ANISOU   66  CA  ILE A  39    12040  22796  12693    822  -1747    240       C  
ATOM     67  C   ILE A  39      32.584  -1.362  30.415  1.00125.80           C  
ANISOU   67  C   ILE A  39    12274  22495  13031   1042  -1756    354       C  
ATOM     68  O   ILE A  39      33.626  -0.972  29.882  1.00125.47           O  
ANISOU   68  O   ILE A  39    12021  22512  13140   1153  -1755    155       O  
ATOM     69  CB  ILE A  39      32.949  -0.757  32.962  1.00132.11           C  
ANISOU   69  CB  ILE A  39    12709  24222  13265    966  -1937    220       C  
ATOM     70  CG1 ILE A  39      32.278  -0.115  34.197  1.00133.57           C  
ANISOU   70  CG1 ILE A  39    12763  24803  13184    732  -1915    100       C  
ATOM     71  CG2 ILE A  39      34.327  -0.115  32.735  1.00133.92           C  
ANISOU   71  CG2 ILE A  39    12587  24685  13612   1089  -1973    -95       C  
ATOM     72  CD1 ILE A  39      31.698  -1.084  35.177  1.00142.69           C  
ANISOU   72  CD1 ILE A  39    14146  26093  13976    756  -2023    465       C  
ATOM     73  N   PHE A  40      31.809  -2.336  29.888  1.00119.77           N  
ANISOU   73  N   PHE A  40    11854  21333  12319   1069  -1740    641       N  
ATOM     74  CA  PHE A  40      32.050  -3.084  28.652  1.00117.70           C  
ANISOU   74  CA  PHE A  40    11771  20663  12288   1247  -1732    750       C  
ATOM     75  C   PHE A  40      31.139  -2.504  27.548  1.00114.53           C  
ANISOU   75  C   PHE A  40    11444  19939  12135   1040  -1527    622       C  
ATOM     76  O   PHE A  40      31.536  -2.451  26.386  1.00113.11           O  
ANISOU   76  O   PHE A  40    11255  19543  12180   1127  -1464    537       O  
ATOM     77  CB  PHE A  40      31.770  -4.590  28.876  1.00121.92           C  
ANISOU   77  CB  PHE A  40    12644  20970  12711   1411  -1858   1140       C  
ATOM     78  CG  PHE A  40      31.241  -5.359  27.685  1.00122.47           C  
ANISOU   78  CG  PHE A  40    12988  20533  13013   1445  -1788   1259       C  
ATOM     79  CD1 PHE A  40      29.874  -5.550  27.510  1.00124.28           C  
ANISOU   79  CD1 PHE A  40    13442  20514  13267   1207  -1667   1355       C  
ATOM     80  CD2 PHE A  40      32.110  -5.905  26.747  1.00125.50           C  
ANISOU   80  CD2 PHE A  40    13381  20720  13582   1715  -1843   1244       C  
ATOM     81  CE1 PHE A  40      29.384  -6.258  26.407  1.00124.26           C  
ANISOU   81  CE1 PHE A  40    13668  20073  13473   1232  -1605   1427       C  
ATOM     82  CE2 PHE A  40      31.619  -6.614  25.643  1.00127.38           C  
ANISOU   82  CE2 PHE A  40    13855  20517  14028   1745  -1778   1317       C  
ATOM     83  CZ  PHE A  40      30.259  -6.788  25.483  1.00124.00           C  
ANISOU   83  CZ  PHE A  40    13647  19845  13622   1502  -1662   1407       C  
ATOM     84  N   LEU A  41      29.903  -2.119  27.928  1.00106.78           N  
ANISOU   84  N   LEU A  41    10535  18949  11088    782  -1432    616       N  
ATOM     85  CA  LEU A  41      28.868  -1.517  27.087  1.00102.13           C  
ANISOU   85  CA  LEU A  41    10008  18113  10683    588  -1259    493       C  
ATOM     86  C   LEU A  41      29.299  -0.146  26.497  1.00100.34           C  
ANISOU   86  C   LEU A  41     9539  17936  10650    519  -1143    176       C  
ATOM     87  O   LEU A  41      29.055   0.050  25.304  1.00 97.48           O  
ANISOU   87  O   LEU A  41     9252  17290  10497    517  -1038    131       O  
ATOM     88  CB  LEU A  41      27.559  -1.407  27.899  1.00102.29           C  
ANISOU   88  CB  LEU A  41    10104  18224  10539    347  -1212    527       C  
ATOM     89  CG  LEU A  41      26.265  -0.979  27.202  1.00104.47           C  
ANISOU   89  CG  LEU A  41    10465  18274  10955    160  -1062    427       C  
ATOM     90  CD1 LEU A  41      25.796  -2.025  26.234  1.00103.96           C  
ANISOU   90  CD1 LEU A  41    10668  17828  11003    227  -1046    613       C  
ATOM     91  CD2 LEU A  41      25.163  -0.773  28.215  1.00106.74           C  
ANISOU   91  CD2 LEU A  41    10743  18769  11045    -71  -1027    404       C  
ATOM     92  N   PRO A  42      29.975   0.782  27.248  1.00 95.47           N  
ANISOU   92  N   PRO A  42     8641  17660   9974    464  -1154    -43       N  
ATOM     93  CA  PRO A  42      30.410   2.057  26.643  1.00 93.12           C  
ANISOU   93  CA  PRO A  42     8140  17349   9892    375  -1024   -331       C  
ATOM     94  C   PRO A  42      31.448   1.906  25.535  1.00 93.14           C  
ANISOU   94  C   PRO A  42     8110  17207  10071    533   -998   -344       C  
ATOM     95  O   PRO A  42      31.584   2.814  24.716  1.00 91.58           O  
ANISOU   95  O   PRO A  42     7842  16881  10075    443   -854   -509       O  
ATOM     96  CB  PRO A  42      31.003   2.820  27.827  1.00 96.95           C  
ANISOU   96  CB  PRO A  42     8331  18257  10249    294  -1069   -554       C  
ATOM     97  CG  PRO A  42      31.438   1.765  28.767  1.00104.02           C  
ANISOU   97  CG  PRO A  42     9246  19407  10870    458  -1257   -355       C  
ATOM     98  CD  PRO A  42      30.357   0.743  28.673  1.00 99.17           C  
ANISOU   98  CD  PRO A  42     8958  18547  10174    466  -1279    -51       C  
ATOM     99  N   THR A  43      32.186   0.779  25.517  1.00 88.26           N  
ANISOU   99  N   THR A  43     7545  16616   9375    770  -1135   -174       N  
ATOM    100  CA  THR A  43      33.170   0.509  24.467  1.00 86.99           C  
ANISOU  100  CA  THR A  43     7339  16348   9363    942  -1118   -200       C  
ATOM    101  C   THR A  43      32.428   0.258  23.146  1.00 87.22           C  
ANISOU  101  C   THR A  43     7604  15976   9558    934  -1006   -107       C  
ATOM    102  O   THR A  43      32.897   0.697  22.097  1.00 85.66           O  
ANISOU  102  O   THR A  43     7343  15680   9523    938   -891   -215       O  
ATOM    103  CB  THR A  43      34.201  -0.583  24.857  1.00 92.00           C  
ANISOU  103  CB  THR A  43     7936  17144   9876   1234  -1312    -84       C  
ATOM    104  OG1 THR A  43      33.879  -1.831  24.242  1.00 89.17           O  
ANISOU  104  OG1 THR A  43     7856  16474   9549   1413  -1373    158       O  
ATOM    105  CG2 THR A  43      34.386  -0.742  26.371  1.00 91.04           C  
ANISOU  105  CG2 THR A  43     7715  17383   9492   1266  -1474    -42       C  
ATOM    106  N   ILE A  44      31.237  -0.392  23.218  1.00 82.53           N  
ANISOU  106  N   ILE A  44     7267  15182   8909    898  -1027     79       N  
ATOM    107  CA  ILE A  44      30.370  -0.669  22.064  1.00 80.28           C  
ANISOU  107  CA  ILE A  44     7198  14555   8752    879   -935    148       C  
ATOM    108  C   ILE A  44      29.852   0.632  21.422  1.00 80.94           C  
ANISOU  108  C   ILE A  44     7223  14563   8969    698   -764    -24       C  
ATOM    109  O   ILE A  44      29.908   0.740  20.199  1.00 79.55           O  
ANISOU  109  O   ILE A  44     7099  14202   8925    741   -672    -44       O  
ATOM    110  CB  ILE A  44      29.279  -1.758  22.342  1.00 83.61           C  
ANISOU  110  CB  ILE A  44     7887  14800   9083    871   -999    365       C  
ATOM    111  CG1 ILE A  44      29.930  -3.160  22.491  1.00 86.46           C  
ANISOU  111  CG1 ILE A  44     8366  15094   9392   1111  -1152    561       C  
ATOM    112  CG2 ILE A  44      28.207  -1.787  21.244  1.00 81.90           C  
ANISOU  112  CG2 ILE A  44     7837  14294   8987    798   -889    361       C  
ATOM    113  CD1 ILE A  44      29.010  -4.309  23.018  1.00 96.22           C  
ANISOU  113  CD1 ILE A  44     9876  16161  10522   1084  -1222    807       C  
ATOM    114  N   TYR A  45      29.424   1.637  22.228  1.00 76.63           N  
ANISOU  114  N   TYR A  45     6563  14167   8386    511   -723   -155       N  
ATOM    115  CA  TYR A  45      28.988   2.928  21.670  1.00 75.15           C  
ANISOU  115  CA  TYR A  45     6329  13878   8347    364   -572   -319       C  
ATOM    116  C   TYR A  45      30.172   3.623  20.984  1.00 79.11           C  
ANISOU  116  C   TYR A  45     6675  14395   8988    382   -478   -442       C  
ATOM    117  O   TYR A  45      29.987   4.237  19.937  1.00 78.60           O  
ANISOU  117  O   TYR A  45     6669  14134   9062    346   -348   -470       O  
ATOM    118  CB  TYR A  45      28.412   3.888  22.734  1.00 76.85           C  
ANISOU  118  CB  TYR A  45     6426  14258   8516    178   -554   -479       C  
ATOM    119  CG  TYR A  45      27.391   3.321  23.697  1.00 79.29           C  
ANISOU  119  CG  TYR A  45     6818  14666   8643    117   -637   -398       C  
ATOM    120  CD1 TYR A  45      26.215   2.733  23.231  1.00 79.72           C  
ANISOU  120  CD1 TYR A  45     7083  14522   8686    110   -627   -276       C  
ATOM    121  CD2 TYR A  45      27.539   3.476  25.070  1.00 82.12           C  
ANISOU  121  CD2 TYR A  45     7026  15344   8833     39   -709   -472       C  
ATOM    122  CE1 TYR A  45      25.261   2.230  24.114  1.00 80.70           C  
ANISOU  122  CE1 TYR A  45     7273  14750   8638     13   -676   -212       C  
ATOM    123  CE2 TYR A  45      26.589   2.988  25.963  1.00 83.73           C  
ANISOU  123  CE2 TYR A  45     7303  15668   8843    -45   -763   -391       C  
ATOM    124  CZ  TYR A  45      25.447   2.369  25.480  1.00 90.54           C  
ANISOU  124  CZ  TYR A  45     8381  16315   9704    -70   -738   -259       C  
ATOM    125  OH  TYR A  45      24.506   1.898  26.362  1.00 93.73           O  
ANISOU  125  OH  TYR A  45     8847  16854   9913   -190   -768   -189       O  
ATOM    126  N   SER A  46      31.382   3.507  21.571  1.00 75.87           N  
ANISOU  126  N   SER A  46     6065  14237   8526    437   -542   -513       N  
ATOM    127  CA  SER A  46      32.615   4.100  21.062  1.00 76.06           C  
ANISOU  127  CA  SER A  46     5894  14341   8663    428   -450   -661       C  
ATOM    128  C   SER A  46      33.064   3.478  19.741  1.00 77.75           C  
ANISOU  128  C   SER A  46     6199  14396   8947    579   -407   -564       C  
ATOM    129  O   SER A  46      33.505   4.217  18.859  1.00 77.49           O  
ANISOU  129  O   SER A  46     6109  14293   9042    502   -249   -650       O  
ATOM    130  CB  SER A  46      33.723   4.021  22.105  1.00 81.98           C  
ANISOU  130  CB  SER A  46     6382  15455   9312    468   -556   -786       C  
ATOM    131  OG  SER A  46      33.349   4.711  23.287  1.00 90.98           O  
ANISOU  131  OG  SER A  46     7407  16779  10381    311   -580   -919       O  
ATOM    132  N   ILE A  47      32.946   2.133  19.597  1.00 72.49           N  
ANISOU  132  N   ILE A  47     5677  13667   8197    784   -536   -391       N  
ATOM    133  CA  ILE A  47      33.300   1.417  18.361  1.00 71.29           C  
ANISOU  133  CA  ILE A  47     5611  13371   8104    948   -510   -325       C  
ATOM    134  C   ILE A  47      32.417   1.957  17.235  1.00 73.06           C  
ANISOU  134  C   ILE A  47     5998  13341   8420    850   -358   -295       C  
ATOM    135  O   ILE A  47      32.925   2.360  16.192  1.00 71.54           O  
ANISOU  135  O   ILE A  47     5763  13113   8306    844   -227   -346       O  
ATOM    136  CB  ILE A  47      33.199  -0.135  18.507  1.00 74.47           C  
ANISOU  136  CB  ILE A  47     6167  13703   8426   1181   -684   -157       C  
ATOM    137  CG1 ILE A  47      34.251  -0.685  19.488  1.00 77.18           C  
ANISOU  137  CG1 ILE A  47     6347  14307   8671   1340   -848   -171       C  
ATOM    138  CG2 ILE A  47      33.331  -0.838  17.145  1.00 74.37           C  
ANISOU  138  CG2 ILE A  47     6260  13505   8491   1335   -645   -124       C  
ATOM    139  CD1 ILE A  47      33.854  -1.976  20.204  1.00 85.75           C  
ANISOU  139  CD1 ILE A  47     7622  15318   9641   1502  -1038     41       C  
ATOM    140  N   ILE A  48      31.104   2.027  17.499  1.00 70.09           N  
ANISOU  140  N   ILE A  48     5790  12825   8017    768   -374   -222       N  
ATOM    141  CA  ILE A  48      30.082   2.526  16.582  1.00 69.28           C  
ANISOU  141  CA  ILE A  48     5842  12506   7975    701   -267   -195       C  
ATOM    142  C   ILE A  48      30.229   4.025  16.298  1.00 75.17           C  
ANISOU  142  C   ILE A  48     6503  13234   8826    541   -108   -305       C  
ATOM    143  O   ILE A  48      29.995   4.433  15.162  1.00 74.84           O  
ANISOU  143  O   ILE A  48     6555  13041   8839    543      5   -272       O  
ATOM    144  CB  ILE A  48      28.654   2.063  16.991  1.00 71.26           C  
ANISOU  144  CB  ILE A  48     6266  12650   8159    672   -342   -114       C  
ATOM    145  CG1 ILE A  48      28.598   0.519  16.994  1.00 72.12           C  
ANISOU  145  CG1 ILE A  48     6499  12704   8201    824   -466     13       C  
ATOM    146  CG2 ILE A  48      27.572   2.631  16.044  1.00 70.74           C  
ANISOU  146  CG2 ILE A  48     6332  12401   8145    631   -249   -116       C  
ATOM    147  CD1 ILE A  48      27.662  -0.076  17.925  1.00 80.00           C  
ANISOU  147  CD1 ILE A  48     7601  13692   9103    764   -558     93       C  
ATOM    148  N   PHE A  49      30.671   4.828  17.292  1.00 73.27           N  
ANISOU  148  N   PHE A  49     6086  13144   8609    406    -97   -438       N  
ATOM    149  CA  PHE A  49      30.906   6.262  17.100  1.00 73.84           C  
ANISOU  149  CA  PHE A  49     6076  13166   8815    234     62   -561       C  
ATOM    150  C   PHE A  49      32.100   6.451  16.160  1.00 78.62           C  
ANISOU  150  C   PHE A  49     6591  13796   9485    236    191   -582       C  
ATOM    151  O   PHE A  49      31.971   7.143  15.157  1.00 78.26           O  
ANISOU  151  O   PHE A  49     6640  13575   9520    178    341   -540       O  
ATOM    152  CB  PHE A  49      31.118   6.983  18.446  1.00 76.81           C  
ANISOU  152  CB  PHE A  49     6261  13719   9204     84     37   -742       C  
ATOM    153  CG  PHE A  49      31.766   8.348  18.363  1.00 79.93           C  
ANISOU  153  CG  PHE A  49     6517  14090   9764   -106    202   -914       C  
ATOM    154  CD1 PHE A  49      33.088   8.534  18.754  1.00 84.74           C  
ANISOU  154  CD1 PHE A  49     6871  14931  10394   -176    233  -1072       C  
ATOM    155  CD2 PHE A  49      31.057   9.446  17.893  1.00 81.88           C  
ANISOU  155  CD2 PHE A  49     6885  14074  10151   -213    326   -927       C  
ATOM    156  CE1 PHE A  49      33.685   9.797  18.680  1.00 87.28           C  
ANISOU  156  CE1 PHE A  49     7062  15213  10887   -391    406  -1250       C  
ATOM    157  CE2 PHE A  49      31.655  10.708  17.819  1.00 86.48           C  
ANISOU  157  CE2 PHE A  49     7367  14579  10911   -406    491  -1075       C  
ATOM    158  CZ  PHE A  49      32.965  10.874  18.210  1.00 86.36           C  
ANISOU  158  CZ  PHE A  49     7099  14787  10927   -514    541  -1240       C  
ATOM    159  N   LEU A  50      33.228   5.783  16.453  1.00 76.24           N  
ANISOU  159  N   LEU A  50     6113  13723   9130    317    128   -638       N  
ATOM    160  CA  LEU A  50      34.448   5.843  15.648  1.00 77.64           C  
ANISOU  160  CA  LEU A  50     6154  13996   9349    322    244   -698       C  
ATOM    161  C   LEU A  50      34.240   5.316  14.226  1.00 81.75           C  
ANISOU  161  C   LEU A  50     6846  14366   9848    446    305   -558       C  
ATOM    162  O   LEU A  50      34.688   5.956  13.275  1.00 82.23           O  
ANISOU  162  O   LEU A  50     6893  14388   9963    354    487   -566       O  
ATOM    163  CB  LEU A  50      35.603   5.108  16.355  1.00 79.05           C  
ANISOU  163  CB  LEU A  50     6092  14485   9457    436    120   -807       C  
ATOM    164  CG  LEU A  50      36.819   5.955  16.739  1.00 85.59           C  
ANISOU  164  CG  LEU A  50     6613  15553  10353    271    221  -1040       C  
ATOM    165  CD1 LEU A  50      36.532   6.847  17.932  1.00 85.93           C  
ANISOU  165  CD1 LEU A  50     6560  15658  10430     86    207  -1175       C  
ATOM    166  CD2 LEU A  50      37.984   5.079  17.085  1.00 90.10           C  
ANISOU  166  CD2 LEU A  50     6954  16442  10840    453     94  -1139       C  
ATOM    167  N   THR A  51      33.534   4.185  14.076  1.00 77.82           N  
ANISOU  167  N   THR A  51     6513  13788   9268    636    165   -435       N  
ATOM    168  CA  THR A  51      33.255   3.601  12.762  1.00 77.64           C  
ANISOU  168  CA  THR A  51     6641  13645   9213    765    205   -337       C  
ATOM    169  C   THR A  51      32.167   4.399  12.028  1.00 81.64           C  
ANISOU  169  C   THR A  51     7345  13934   9741    678    312   -244       C  
ATOM    170  O   THR A  51      32.308   4.663  10.834  1.00 82.33           O  
ANISOU  170  O   THR A  51     7488  13976   9817    684    443   -198       O  
ATOM    171  CB  THR A  51      32.919   2.105  12.880  1.00 87.44           C  
ANISOU  171  CB  THR A  51     7979  14859  10384    984     22   -270       C  
ATOM    172  OG1 THR A  51      33.778   1.506  13.849  1.00 89.92           O  
ANISOU  172  OG1 THR A  51     8134  15357  10676   1072   -108   -330       O  
ATOM    173  CG2 THR A  51      33.064   1.367  11.561  1.00 87.74           C  
ANISOU  173  CG2 THR A  51     8085  14854  10397   1139     57   -249       C  
ATOM    174  N   GLY A  52      31.113   4.775  12.753  1.00 76.69           N  
ANISOU  174  N   GLY A  52     6810  13200   9129    609    251   -224       N  
ATOM    175  CA  GLY A  52      29.977   5.528  12.232  1.00 75.22           C  
ANISOU  175  CA  GLY A  52     6798  12818   8964    563    312   -156       C  
ATOM    176  C   GLY A  52      30.288   6.938  11.784  1.00 79.52           C  
ANISOU  176  C   GLY A  52     7337  13273   9605    413    496   -162       C  
ATOM    177  O   GLY A  52      29.773   7.366  10.754  1.00 79.28           O  
ANISOU  177  O   GLY A  52     7463  13100   9561    443    580    -58       O  
ATOM    178  N   ILE A  53      31.122   7.676  12.540  1.00 77.13           N  
ANISOU  178  N   ILE A  53     6859  13049   9397    248    561   -284       N  
ATOM    179  CA  ILE A  53      31.487   9.046  12.173  1.00 78.47           C  
ANISOU  179  CA  ILE A  53     7029  13095   9692     66    756   -300       C  
ATOM    180  C   ILE A  53      32.424   9.068  10.957  1.00 83.27           C  
ANISOU  180  C   ILE A  53     7624  13745  10271     49    923   -231       C  
ATOM    181  O   ILE A  53      32.174   9.826  10.023  1.00 83.21           O  
ANISOU  181  O   ILE A  53     7773  13560  10283      1   1067   -106       O  
ATOM    182  CB  ILE A  53      31.946   9.918  13.390  1.00 82.79           C  
ANISOU  182  CB  ILE A  53     7392  13694  10371   -135    783   -492       C  
ATOM    183  CG1 ILE A  53      31.461  11.391  13.310  1.00 84.34           C  
ANISOU  183  CG1 ILE A  53     7695  13618  10733   -293    916   -502       C  
ATOM    184  CG2 ILE A  53      33.428   9.753  13.795  1.00 85.26           C  
ANISOU  184  CG2 ILE A  53     7427  14272  10696   -226    825   -647       C  
ATOM    185  CD1 ILE A  53      32.146  12.358  12.266  1.00 95.20           C  
ANISOU  185  CD1 ILE A  53     9134  14830  12209   -445   1164   -424       C  
ATOM    186  N   VAL A  54      33.459   8.199  10.952  1.00 80.61           N  
ANISOU  186  N   VAL A  54     7105  13652   9870    108    897   -308       N  
ATOM    187  CA  VAL A  54      34.429   8.066   9.862  1.00 82.02           C  
ANISOU  187  CA  VAL A  54     7219  13945   9998    100   1049   -289       C  
ATOM    188  C   VAL A  54      33.757   7.499   8.604  1.00 86.13           C  
ANISOU  188  C   VAL A  54     7947  14389  10388    276   1045   -122       C  
ATOM    189  O   VAL A  54      33.974   8.026   7.514  1.00 87.57           O  
ANISOU  189  O   VAL A  54     8206  14537  10531    213   1224    -24       O  
ATOM    190  CB  VAL A  54      35.686   7.273  10.318  1.00 86.42           C  
ANISOU  190  CB  VAL A  54     7494  14812  10530    149    992   -463       C  
ATOM    191  CG1 VAL A  54      36.397   6.587   9.155  1.00 87.24           C  
ANISOU  191  CG1 VAL A  54     7545  15069  10532    260   1066   -454       C  
ATOM    192  CG2 VAL A  54      36.649   8.177  11.081  1.00 88.08           C  
ANISOU  192  CG2 VAL A  54     7464  15144  10859    -91   1099   -646       C  
ATOM    193  N   GLY A  55      32.922   6.477   8.788  1.00 81.09           N  
ANISOU  193  N   GLY A  55     7400  13731   9680    477    850    -95       N  
ATOM    194  CA  GLY A  55      32.186   5.807   7.724  1.00 80.48           C  
ANISOU  194  CA  GLY A  55     7494  13605   9482    654    813     11       C  
ATOM    195  C   GLY A  55      31.218   6.715   6.999  1.00 85.32           C  
ANISOU  195  C   GLY A  55     8323  14024  10069    626    895    161       C  
ATOM    196  O   GLY A  55      31.375   6.941   5.796  1.00 86.34           O  
ANISOU  196  O   GLY A  55     8529  14173  10104    644   1025    259       O  
ATOM    197  N   ASN A  56      30.217   7.248   7.726  1.00 81.40           N  
ANISOU  197  N   ASN A  56     7923  13360   9646    593    816    176       N  
ATOM    198  CA  ASN A  56      29.196   8.153   7.186  1.00 81.67           C  
ANISOU  198  CA  ASN A  56     8161  13196   9674    605    857    304       C  
ATOM    199  C   ASN A  56      29.775   9.503   6.761  1.00 89.54           C  
ANISOU  199  C   ASN A  56     9201  14071  10747    434   1071    393       C  
ATOM    200  O   ASN A  56      29.260  10.116   5.827  1.00 90.05           O  
ANISOU  200  O   ASN A  56     9456  14007  10753    483   1145    558       O  
ATOM    201  CB  ASN A  56      28.043   8.341   8.169  1.00 79.36           C  
ANISOU  201  CB  ASN A  56     7916  12787   9451    619    713    248       C  
ATOM    202  CG  ASN A  56      27.243   7.086   8.412  1.00 98.19           C  
ANISOU  202  CG  ASN A  56    10311  15251  11746    765    530    198       C  
ATOM    203  OD1 ASN A  56      26.407   6.679   7.594  1.00 94.23           O  
ANISOU  203  OD1 ASN A  56     9930  14737  11138    909    480    251       O  
ATOM    204  ND2 ASN A  56      27.459   6.461   9.561  1.00 86.43           N  
ANISOU  204  ND2 ASN A  56     8697  13848  10294    724    426     92       N  
ATOM    205  N   GLY A  57      30.840   9.934   7.439  1.00 88.82           N  
ANISOU  205  N   GLY A  57     8938  14029  10782    237   1167    285       N  
ATOM    206  CA  GLY A  57      31.547  11.178   7.155  1.00 92.16           C  
ANISOU  206  CA  GLY A  57     9373  14333  11310     16   1394    336       C  
ATOM    207  C   GLY A  57      32.150  11.210   5.764  1.00100.10           C  
ANISOU  207  C   GLY A  57    10443  15410  12181      3   1576    487       C  
ATOM    208  O   GLY A  57      32.021  12.215   5.061  1.00101.58           O  
ANISOU  208  O   GLY A  57    10813  15404  12380    -82   1736    666       O  
ATOM    209  N   LEU A  58      32.793  10.104   5.341  1.00 98.09           N  
ANISOU  209  N   LEU A  58    10048  15432  11790     98   1553    422       N  
ATOM    210  CA  LEU A  58      33.355  10.033   3.994  1.00100.69           C  
ANISOU  210  CA  LEU A  58    10410  15892  11956     97   1724    537       C  
ATOM    211  C   LEU A  58      32.309   9.744   2.909  1.00106.27           C  
ANISOU  211  C   LEU A  58    11348  16559  12469    318   1664    717       C  
ATOM    212  O   LEU A  58      32.573  10.011   1.738  1.00108.41           O  
ANISOU  212  O   LEU A  58    11709  16896  12587    301   1825    867       O  
ATOM    213  CB  LEU A  58      34.638   9.182   3.868  1.00101.54           C  
ANISOU  213  CB  LEU A  58    10245  16330  12005     82   1771    365       C  
ATOM    214  CG  LEU A  58      34.614   7.736   4.349  1.00104.30           C  
ANISOU  214  CG  LEU A  58    10455  16854  12320    308   1539    196       C  
ATOM    215  CD1 LEU A  58      34.226   6.782   3.230  1.00104.32           C  
ANISOU  215  CD1 LEU A  58    10539  16969  12128    536   1486    243       C  
ATOM    216  CD2 LEU A  58      35.972   7.342   4.882  1.00107.69           C  
ANISOU  216  CD2 LEU A  58    10574  17535  12807    237   1566    -20       C  
ATOM    217  N   VAL A  59      31.118   9.232   3.296  1.00101.58           N  
ANISOU  217  N   VAL A  59    10844  15882  11870    512   1440    696       N  
ATOM    218  CA  VAL A  59      30.006   8.982   2.370  1.00101.68           C  
ANISOU  218  CA  VAL A  59    11051  15875  11708    727   1357    823       C  
ATOM    219  C   VAL A  59      29.397  10.336   2.005  1.00109.22           C  
ANISOU  219  C   VAL A  59    12240  16577  12682    687   1447   1040       C  
ATOM    220  O   VAL A  59      29.269  10.639   0.818  1.00110.49           O  
ANISOU  220  O   VAL A  59    12553  16764  12663    754   1544   1231       O  
ATOM    221  CB  VAL A  59      28.974   7.958   2.922  1.00102.60           C  
ANISOU  221  CB  VAL A  59    11156  16004  11821    915   1105    696       C  
ATOM    222  CG1 VAL A  59      27.652   8.008   2.157  1.00102.05           C  
ANISOU  222  CG1 VAL A  59    11280  15884  11610   1107   1015    800       C  
ATOM    223  CG2 VAL A  59      29.550   6.548   2.891  1.00101.61           C  
ANISOU  223  CG2 VAL A  59    10864  16102  11641   1002   1031    535       C  
ATOM    224  N   ILE A  60      29.095  11.174   3.028  1.00107.15           N  
ANISOU  224  N   ILE A  60    12003  16073  12635    579   1423   1009       N  
ATOM    225  CA  ILE A  60      28.586  12.537   2.846  1.00109.61           C  
ANISOU  225  CA  ILE A  60    12536  16084  13028    539   1503   1190       C  
ATOM    226  C   ILE A  60      29.656  13.404   2.133  1.00119.16           C  
ANISOU  226  C   ILE A  60    13806  17233  14234    322   1787   1362       C  
ATOM    227  O   ILE A  60      29.300  14.325   1.395  1.00121.03           O  
ANISOU  227  O   ILE A  60    14290  17266  14428    342   1884   1609       O  
ATOM    228  CB  ILE A  60      28.016  13.147   4.165  1.00111.47           C  
ANISOU  228  CB  ILE A  60    12751  16094  13508    483   1401   1057       C  
ATOM    229  CG1 ILE A  60      27.044  14.341   3.916  1.00113.47           C  
ANISOU  229  CG1 ILE A  60    13262  16024  13829    570   1397   1220       C  
ATOM    230  CG2 ILE A  60      29.087  13.422   5.229  1.00112.21           C  
ANISOU  230  CG2 ILE A  60    12635  16191  13809    212   1493    876       C  
ATOM    231  CD1 ILE A  60      27.653  15.813   3.809  1.00124.17           C  
ANISOU  231  CD1 ILE A  60    14757  17056  15367    351   1626   1366       C  
ATOM    232  N   LEU A  61      30.956  13.058   2.307  1.00117.92           N  
ANISOU  232  N   LEU A  61    13425  17274  14105    125   1917   1234       N  
ATOM    233  CA  LEU A  61      32.074  13.726   1.636  1.00121.92           C  
ANISOU  233  CA  LEU A  61    13936  17795  14591   -120   2207   1353       C  
ATOM    234  C   LEU A  61      32.027  13.388   0.138  1.00129.09           C  
ANISOU  234  C   LEU A  61    14973  18886  15190     12   2286   1563       C  
ATOM    235  O   LEU A  61      32.140  14.295  -0.676  1.00131.87           O  
ANISOU  235  O   LEU A  61    15531  19102  15472    -87   2480   1824       O  
ATOM    236  CB  LEU A  61      33.425  13.292   2.247  1.00121.99           C  
ANISOU  236  CB  LEU A  61    13615  18047  14690   -329   2293   1100       C  
ATOM    237  CG  LEU A  61      34.619  14.235   2.071  1.00130.25           C  
ANISOU  237  CG  LEU A  61    14601  19057  15832   -685   2603   1127       C  
ATOM    238  CD1 LEU A  61      35.483  14.242   3.316  1.00130.07           C  
ANISOU  238  CD1 LEU A  61    14272  19118  16029   -886   2604    819       C  
ATOM    239  CD2 LEU A  61      35.465  13.850   0.859  1.00134.81           C  
ANISOU  239  CD2 LEU A  61    15118  19934  16167   -735   2794   1207       C  
ATOM    240  N   VAL A  62      31.834  12.099  -0.216  1.00125.02           N  
ANISOU  240  N   VAL A  62    14345  18668  14488    234   2134   1450       N  
ATOM    241  CA  VAL A  62      31.774  11.636  -1.607  1.00126.83           C  
ANISOU  241  CA  VAL A  62    14652  19135  14404    380   2186   1585       C  
ATOM    242  C   VAL A  62      30.453  12.034  -2.288  1.00133.25           C  
ANISOU  242  C   VAL A  62    15760  19801  15069    611   2084   1820       C  
ATOM    243  O   VAL A  62      30.484  12.759  -3.281  1.00135.82           O  
ANISOU  243  O   VAL A  62    16287  20093  15226    587   2244   2097       O  
ATOM    244  CB  VAL A  62      32.112  10.118  -1.751  1.00128.79           C  
ANISOU  244  CB  VAL A  62    14659  19742  14533    529   2069   1337       C  
ATOM    245  CG1 VAL A  62      31.801   9.594  -3.154  1.00129.77           C  
ANISOU  245  CG1 VAL A  62    14863  20114  14328    722   2079   1433       C  
ATOM    246  CG2 VAL A  62      33.570   9.838  -1.394  1.00129.36           C  
ANISOU  246  CG2 VAL A  62    14447  20013  14691    324   2208   1143       C  
ATOM    247  N   MET A  63      29.310  11.561  -1.757  1.00129.03           N  
ANISOU  247  N   MET A  63    15243  19199  14583    832   1822   1710       N  
ATOM    248  CA  MET A  63      27.978  11.804  -2.311  1.00130.03           C  
ANISOU  248  CA  MET A  63    15595  19242  14571   1089   1681   1863       C  
ATOM    249  C   MET A  63      27.527  13.270  -2.329  1.00138.21           C  
ANISOU  249  C   MET A  63    16900  19916  15699   1060   1750   2126       C  
ATOM    250  O   MET A  63      27.122  13.764  -3.386  1.00140.39           O  
ANISOU  250  O   MET A  63    17399  20182  15759   1194   1794   2393       O  
ATOM    251  CB  MET A  63      26.929  10.899  -1.640  1.00129.22           C  
ANISOU  251  CB  MET A  63    15401  19179  14519   1287   1402   1632       C  
ATOM    252  CG  MET A  63      26.820   9.527  -2.268  1.00131.90           C  
ANISOU  252  CG  MET A  63    15615  19852  14651   1451   1303   1478       C  
ATOM    253  SD  MET A  63      28.207   8.422  -1.906  1.00135.24           S  
ANISOU  253  SD  MET A  63    15748  20498  15141   1304   1371   1237       S  
ATOM    254  CE  MET A  63      27.825   7.080  -2.997  1.00131.79           C  
ANISOU  254  CE  MET A  63    15251  20392  14431   1548   1266   1107       C  
ATOM    255  N   GLY A  64      27.606  13.931  -1.173  1.00135.50           N  
ANISOU  255  N   GLY A  64    16532  19286  15668    900   1754   2042       N  
ATOM    256  CA  GLY A  64      27.193  15.318  -0.963  1.00138.06           C  
ANISOU  256  CA  GLY A  64    17090  19205  16161    864   1804   2226       C  
ATOM    257  C   GLY A  64      27.774  16.354  -1.905  1.00147.59           C  
ANISOU  257  C   GLY A  64    18534  20250  17292    731   2063   2568       C  
ATOM    258  O   GLY A  64      27.050  17.257  -2.332  1.00149.62           O  
ANISOU  258  O   GLY A  64    19078  20240  17531    872   2047   2821       O  
ATOM    259  N   TYR A  65      29.076  16.240  -2.236  1.00146.54           N  
ANISOU  259  N   TYR A  65    18287  20279  17110    461   2305   2583       N  
ATOM    260  CA  TYR A  65      29.745  17.196  -3.125  1.00151.50           C  
ANISOU  260  CA  TYR A  65    19130  20777  17656    267   2596   2911       C  
ATOM    261  C   TYR A  65      29.939  16.735  -4.591  1.00158.80           C  
ANISOU  261  C   TYR A  65    20126  22050  18162    370   2690   3124       C  
ATOM    262  O   TYR A  65      30.554  17.446  -5.394  1.00162.47           O  
ANISOU  262  O   TYR A  65    20761  22463  18508    189   2954   3414       O  
ATOM    263  CB  TYR A  65      30.989  17.833  -2.440  1.00154.21           C  
ANISOU  263  CB  TYR A  65    19349  20964  18281   -164   2850   2815       C  
ATOM    264  CG  TYR A  65      32.375  17.354  -2.841  1.00157.09           C  
ANISOU  264  CG  TYR A  65    19482  21679  18527   -431   3086   2732       C  
ATOM    265  CD1 TYR A  65      33.427  18.258  -2.983  1.00163.02           C  
ANISOU  265  CD1 TYR A  65    20266  22290  19383   -821   3416   2843       C  
ATOM    266  CD2 TYR A  65      32.658  16.001  -2.991  1.00155.10           C  
ANISOU  266  CD2 TYR A  65    18954  21886  18090   -307   2979   2502       C  
ATOM    267  CE1 TYR A  65      34.713  17.825  -3.304  1.00165.12           C  
ANISOU  267  CE1 TYR A  65    20276  22917  19546  -1076   3636   2722       C  
ATOM    268  CE2 TYR A  65      33.938  15.557  -3.318  1.00157.10           C  
ANISOU  268  CE2 TYR A  65    18964  22477  18248   -527   3182   2384       C  
ATOM    269  CZ  TYR A  65      34.964  16.474  -3.472  1.00168.57           C  
ANISOU  269  CZ  TYR A  65    20431  23833  19786   -911   3510   2486       C  
ATOM    270  OH  TYR A  65      36.227  16.042  -3.794  1.00170.77           O  
ANISOU  270  OH  TYR A  65    20436  24485  19964  -1131   3714   2337       O  
ATOM    271  N   GLN A  66      29.351  15.567  -4.941  1.00153.84           N  
ANISOU  271  N   GLN A  66    19376  21771  17305    659   2475   2979       N  
ATOM    272  CA  GLN A  66      29.418  14.960  -6.276  1.00155.64           C  
ANISOU  272  CA  GLN A  66    19622  22393  17122    800   2518   3098       C  
ATOM    273  C   GLN A  66      28.173  15.065  -7.189  1.00161.80           C  
ANISOU  273  C   GLN A  66    20650  23213  17613   1168   2351   3325       C  
ATOM    274  O   GLN A  66      27.042  15.112  -6.692  1.00159.79           O  
ANISOU  274  O   GLN A  66    20457  22789  17466   1403   2105   3259       O  
ATOM    275  CB  GLN A  66      29.332  13.428  -6.174  1.00153.36           C  
ANISOU  275  CB  GLN A  66    19035  22496  16740    961   2330   2742       C  
ATOM    276  CG  GLN A  66      30.298  12.697  -7.103  1.00168.43           C  
ANISOU  276  CG  GLN A  66    20775  24844  18375    887   2494   2687       C  
ATOM    277  CD  GLN A  66      29.854  11.282  -7.367  1.00183.56           C  
ANISOU  277  CD  GLN A  66    22503  27110  20132   1148   2279   2410       C  
ATOM    278  OE1 GLN A  66      30.448  10.319  -6.873  1.00176.70           O  
ANISOU  278  OE1 GLN A  66    21357  26407  19372   1099   2240   2096       O  
ATOM    279  NE2 GLN A  66      28.794  11.121  -8.150  1.00175.66           N  
ANISOU  279  NE2 GLN A  66    21646  26222  18874   1439   2130   2509       N  
ATOM    280  N   LYS A  67      28.396  15.134  -8.525  1.00162.29           N  
ANISOU  280  N   LYS A  67    20841  23528  17293   1215   2491   3585       N  
ATOM    281  CA  LYS A  67      27.367  15.273  -9.557  1.00164.41           C  
ANISOU  281  CA  LYS A  67    21341  23911  17216   1561   2361   3831       C  
ATOM    282  C   LYS A  67      27.047  14.088 -10.497  1.00168.71           C  
ANISOU  282  C   LYS A  67    21732  25001  17371   1810   2237   3678       C  
ATOM    283  O   LYS A  67      25.923  13.996 -10.992  1.00168.67           O  
ANISOU  283  O   LYS A  67    21835  25094  17157   2151   2024   3735       O  
ATOM    284  CB  LYS A  67      28.013  16.417 -10.368  1.00171.99           C  
ANISOU  284  CB  LYS A  67    22594  24729  18026   1370   2666   4292       C  
ATOM    285  CG  LYS A  67      27.029  17.263 -11.160  1.00186.77           C  
ANISOU  285  CG  LYS A  67    24851  26448  19666   1666   2582   4709       C  
ATOM    286  CD  LYS A  67      27.757  18.234 -12.074  1.00200.23           C  
ANISOU  286  CD  LYS A  67    26849  28066  21163   1458   2908   5188       C  
ATOM    287  CE  LYS A  67      26.802  19.140 -12.804  1.00212.31           C  
ANISOU  287  CE  LYS A  67    28798  29394  22476   1772   2816   5644       C  
ATOM    288  NZ  LYS A  67      27.516  20.043 -13.743  1.00225.89           N  
ANISOU  288  NZ  LYS A  67    30833  31035  23960   1560   3147   6153       N  
ATOM    289  N   LYS A  68      28.049  13.207 -10.745  1.00165.23           N  
ANISOU  289  N   LYS A  68    21024  24921  16836   1644   2370   3461       N  
ATOM    290  CA  LYS A  68      28.046  12.060 -11.672  1.00165.09           C  
ANISOU  290  CA  LYS A  68    20822  25438  16467   1813   2314   3272       C  
ATOM    291  C   LYS A  68      27.341  10.737 -12.086  1.00166.95           C  
ANISOU  291  C   LYS A  68    20860  26069  16504   2109   2072   2942       C  
ATOM    292  O   LYS A  68      27.113  10.515 -13.278  1.00168.99           O  
ANISOU  292  O   LYS A  68    21156  26702  16349   2283   2078   3025       O  
ATOM    293  CB  LYS A  68      29.462  11.467 -11.823  1.00167.86           C  
ANISOU  293  CB  LYS A  68    20909  26078  16794   1543   2544   3085       C  
ATOM    294  CG  LYS A  68      30.419  12.352 -12.611  1.00183.76           C  
ANISOU  294  CG  LYS A  68    23063  28156  18601   1283   2893   3431       C  
ATOM    295  CD  LYS A  68      31.585  11.557 -13.194  1.00192.82           C  
ANISOU  295  CD  LYS A  68    23920  29786  19558   1127   3085   3214       C  
ATOM    296  CE  LYS A  68      32.620  12.444 -13.846  1.00205.95           C  
ANISOU  296  CE  LYS A  68    25689  31515  21047    800   3465   3528       C  
ATOM    297  NZ  LYS A  68      32.100  13.114 -15.071  1.00218.93           N  
ANISOU  297  NZ  LYS A  68    27659  33272  22253    927   3540   3974       N  
ATOM    298  N   LEU A  69      27.086   9.828 -11.106  1.00159.40           N  
ANISOU  298  N   LEU A  69    19681  25044  15839   2140   1882   2555       N  
ATOM    299  CA  LEU A  69      26.489   8.504 -11.320  1.00157.31           C  
ANISOU  299  CA  LEU A  69    19213  25081  15475   2363   1668   2195       C  
ATOM    300  C   LEU A  69      25.589   8.446 -10.098  1.00157.23           C  
ANISOU  300  C   LEU A  69    19203  24729  15807   2423   1441   2050       C  
ATOM    301  O   LEU A  69      26.060   8.204  -8.982  1.00154.03           O  
ANISOU  301  O   LEU A  69    18671  24111  15741   2245   1443   1883       O  
ATOM    302  CB  LEU A  69      27.299   7.192 -11.389  1.00156.26           C  
ANISOU  302  CB  LEU A  69    18771  25247  15352   2302   1697   1819       C  
ATOM    303  CG  LEU A  69      26.609   5.990 -12.055  1.00160.75           C  
ANISOU  303  CG  LEU A  69    19195  26168  15713   2558   1513   1511       C  
ATOM    304  CD1 LEU A  69      27.601   5.175 -12.870  1.00162.57           C  
ANISOU  304  CD1 LEU A  69    19213  26813  15742   2519   1653   1311       C  
ATOM    305  CD2 LEU A  69      25.903   5.101 -11.026  1.00159.43           C  
ANISOU  305  CD2 LEU A  69    18905  25810  15860   2627   1271   1182       C  
ATOM    306  N   ARG A  70      24.291   8.702 -10.313  1.00153.82           N  
ANISOU  306  N   ARG A  70    18905  24272  15266   2678   1247   2114       N  
ATOM    307  CA  ARG A  70      23.311   8.711  -9.236  1.00150.53           C  
ANISOU  307  CA  ARG A  70    18485  23577  15132   2748   1034   1974       C  
ATOM    308  C   ARG A  70      21.981   8.023  -9.518  1.00152.36           C  
ANISOU  308  C   ARG A  70    18652  24011  15226   3030    777   1753       C  
ATOM    309  O   ARG A  70      21.057   8.618 -10.086  1.00153.97           O  
ANISOU  309  O   ARG A  70    19008  24267  15227   3266    672   1913       O  
ATOM    310  CB  ARG A  70      23.139  10.147  -8.692  1.00152.33           C  
ANISOU  310  CB  ARG A  70    18953  23389  15537   2691   1081   2284       C  
ATOM    311  CG  ARG A  70      22.997  11.236  -9.761  1.00167.03           C  
ANISOU  311  CG  ARG A  70    21099  25259  17108   2817   1172   2702       C  
ATOM    312  CD  ARG A  70      21.846  12.185  -9.474  1.00178.44           C  
ANISOU  312  CD  ARG A  70    22755  26417  18629   3030   1008   2863       C  
ATOM    313  NE  ARG A  70      21.949  12.806  -8.151  1.00185.32           N  
ANISOU  313  NE  ARG A  70    23647  26837  19930   2847   1021   2833       N  
ATOM    314  CZ  ARG A  70      22.602  13.935  -7.896  1.00201.67           C  
ANISOU  314  CZ  ARG A  70    25906  28552  22169   2653   1211   3106       C  
ATOM    315  NH1 ARG A  70      23.218  14.590  -8.874  1.00193.32           N  
ANISOU  315  NH1 ARG A  70    25053  27513  20885   2599   1418   3467       N  
ATOM    316  NH2 ARG A  70      22.643  14.419  -6.664  1.00186.73           N  
ANISOU  316  NH2 ARG A  70    23995  26290  20666   2496   1205   3013       N  
ATOM    317  N   SER A  71      21.898   6.743  -9.120  1.00145.12           N  
ANISOU  317  N   SER A  71    17504  23212  14424   3006    675   1374       N  
ATOM    318  CA  SER A  71      20.669   5.959  -9.205  1.00143.36           C  
ANISOU  318  CA  SER A  71    17178  23153  14138   3206    445   1092       C  
ATOM    319  C   SER A  71      19.950   6.522  -7.981  1.00143.15           C  
ANISOU  319  C   SER A  71    17209  22771  14411   3171    333   1102       C  
ATOM    320  O   SER A  71      20.615   6.849  -6.996  1.00141.04           O  
ANISOU  320  O   SER A  71    16951  22210  14428   2954    424   1161       O  
ATOM    321  CB  SER A  71      20.971   4.461  -9.204  1.00145.41           C  
ANISOU  321  CB  SER A  71    17204  23600  14447   3152    415    714       C  
ATOM    322  OG  SER A  71      21.629   4.043  -8.020  1.00151.22           O  
ANISOU  322  OG  SER A  71    17849  24072  15535   2929    453    601       O  
ATOM    323  N   MET A  72      18.621   6.709  -8.077  1.00138.48           N  
ANISOU  323  N   MET A  72    16644  22236  13735   3391    142   1041       N  
ATOM    324  CA  MET A  72      17.740   7.302  -7.058  1.00136.14           C  
ANISOU  324  CA  MET A  72    16387  21669  13668   3412     16   1022       C  
ATOM    325  C   MET A  72      17.980   6.849  -5.610  1.00134.19           C  
ANISOU  325  C   MET A  72    16020  21172  13795   3161     17    832       C  
ATOM    326  O   MET A  72      17.859   7.676  -4.709  1.00132.95           O  
ANISOU  326  O   MET A  72    15936  20726  13854   3090     17    926       O  
ATOM    327  CB  MET A  72      16.263   7.196  -7.460  1.00139.63           C  
ANISOU  327  CB  MET A  72    16786  22330  13938   3693   -207    862       C  
ATOM    328  CG  MET A  72      15.889   8.064  -8.655  1.00147.25           C  
ANISOU  328  CG  MET A  72    17927  23464  14558   3987   -239   1136       C  
ATOM    329  SD  MET A  72      15.915   9.843  -8.320  1.00153.43           S  
ANISOU  329  SD  MET A  72    19010  23828  15457   4050   -191   1568       S  
ATOM    330  CE  MET A  72      15.702  10.471  -9.964  1.00155.09           C  
ANISOU  330  CE  MET A  72    19425  24320  15182   4384   -205   1900       C  
ATOM    331  N   THR A  73      18.352   5.564  -5.396  1.00127.23           N  
ANISOU  331  N   THR A  73    14965  20395  12982   3035     21    573       N  
ATOM    332  CA  THR A  73      18.670   4.983  -4.081  1.00123.24           C  
ANISOU  332  CA  THR A  73    14352  19684  12789   2807     22    412       C  
ATOM    333  C   THR A  73      19.874   5.614  -3.373  1.00124.30           C  
ANISOU  333  C   THR A  73    14538  19570  13121   2598    181    600       C  
ATOM    334  O   THR A  73      19.939   5.553  -2.149  1.00121.83           O  
ANISOU  334  O   THR A  73    14171  19061  13056   2443    159    524       O  
ATOM    335  CB  THR A  73      18.952   3.476  -4.176  1.00129.70           C  
ANISOU  335  CB  THR A  73    15011  20648  13622   2747      3    139       C  
ATOM    336  OG1 THR A  73      19.870   3.225  -5.241  1.00130.62           O  
ANISOU  336  OG1 THR A  73    15120  20959  13549   2787    120    195       O  
ATOM    337  CG2 THR A  73      17.684   2.652  -4.354  1.00128.15           C  
ANISOU  337  CG2 THR A  73    14715  20618  13359   2854   -163   -149       C  
ATOM    338  N   ASP A  74      20.808   6.231  -4.138  1.00121.27           N  
ANISOU  338  N   ASP A  74    14248  19218  12611   2584    346    837       N  
ATOM    339  CA  ASP A  74      21.998   6.916  -3.617  1.00120.36           C  
ANISOU  339  CA  ASP A  74    14169  18901  12661   2371    522   1007       C  
ATOM    340  C   ASP A  74      21.563   8.206  -2.916  1.00122.60           C  
ANISOU  340  C   ASP A  74    14589  18886  13106   2343    514   1166       C  
ATOM    341  O   ASP A  74      22.166   8.584  -1.912  1.00121.16           O  
ANISOU  341  O   ASP A  74    14377  18492  13167   2143    584   1170       O  
ATOM    342  CB  ASP A  74      22.987   7.234  -4.739  1.00124.90           C  
ANISOU  342  CB  ASP A  74    14805  19625  13026   2352    714   1206       C  
ATOM    343  CG  ASP A  74      23.710   6.031  -5.290  1.00135.72           C  
ANISOU  343  CG  ASP A  74    16009  21272  14286   2342    757   1021       C  
ATOM    344  OD1 ASP A  74      24.471   5.350  -4.591  1.00134.51           O  
ANISOU  344  OD1 ASP A  74    15707  21082  14317   2202    781    860       O  
ATOM    345  OD2 ASP A  74      23.410   5.810  -6.450  1.00143.92           O  
ANISOU  345  OD2 ASP A  74    17073  22574  15039   2506    748   1035       O  
ATOM    346  N   LYS A  75      20.509   8.865  -3.440  1.00119.52           N  
ANISOU  346  N   LYS A  75    14338  18494  12582   2560    417   1273       N  
ATOM    347  CA  LYS A  75      19.936  10.086  -2.872  1.00119.42           C  
ANISOU  347  CA  LYS A  75    14461  18193  12718   2597    380   1398       C  
ATOM    348  C   LYS A  75      19.293   9.758  -1.514  1.00119.36           C  
ANISOU  348  C   LYS A  75    14314  18083  12956   2524    244   1135       C  
ATOM    349  O   LYS A  75      19.504  10.499  -0.553  1.00118.45           O  
ANISOU  349  O   LYS A  75    14219  17707  13079   2387    285   1158       O  
ATOM    350  CB  LYS A  75      18.924  10.721  -3.848  1.00124.39           C  
ANISOU  350  CB  LYS A  75    15257  18892  13113   2907    277   1555       C  
ATOM    351  CG  LYS A  75      18.666  12.208  -3.600  1.00138.61           C  
ANISOU  351  CG  LYS A  75    17271  20350  15042   2965    296   1790       C  
ATOM    352  CD  LYS A  75      17.724  12.812  -4.632  1.00150.01           C  
ANISOU  352  CD  LYS A  75    18895  21872  16229   3316    181   1975       C  
ATOM    353  CE  LYS A  75      18.446  13.475  -5.785  1.00161.12           C  
ANISOU  353  CE  LYS A  75    20537  23268  17414   3344    353   2367       C  
ATOM    354  NZ  LYS A  75      17.491  14.019  -6.791  1.00174.42           N  
ANISOU  354  NZ  LYS A  75    22405  25056  18812   3723    216   2564       N  
ATOM    355  N   TYR A  76      18.556   8.621  -1.432  1.00113.42           N  
ANISOU  355  N   TYR A  76    13410  17544  12141   2592     97    873       N  
ATOM    356  CA  TYR A  76      17.927   8.127  -0.200  1.00110.40           C  
ANISOU  356  CA  TYR A  76    12884  17115  11946   2498    -18    620       C  
ATOM    357  C   TYR A  76      19.007   7.705   0.804  1.00110.45           C  
ANISOU  357  C   TYR A  76    12796  17012  12158   2226     79    571       C  
ATOM    358  O   TYR A  76      18.838   7.912   2.007  1.00108.74           O  
ANISOU  358  O   TYR A  76    12521  16661  12136   2101     46    479       O  
ATOM    359  CB  TYR A  76      17.040   6.905  -0.476  1.00111.21           C  
ANISOU  359  CB  TYR A  76    12857  17473  11925   2588   -157    365       C  
ATOM    360  CG  TYR A  76      15.785   7.148  -1.284  1.00115.50           C  
ANISOU  360  CG  TYR A  76    13427  18192  12268   2861   -296    319       C  
ATOM    361  CD1 TYR A  76      14.667   7.747  -0.708  1.00117.85           C  
ANISOU  361  CD1 TYR A  76    13705  18435  12637   2955   -422    224       C  
ATOM    362  CD2 TYR A  76      15.662   6.653  -2.579  1.00118.01           C  
ANISOU  362  CD2 TYR A  76    13745  18777  12315   3031   -318    312       C  
ATOM    363  CE1 TYR A  76      13.488   7.924  -1.431  1.00120.66           C  
ANISOU  363  CE1 TYR A  76    14052  18991  12802   3231   -571    146       C  
ATOM    364  CE2 TYR A  76      14.486   6.817  -3.309  1.00120.85           C  
ANISOU  364  CE2 TYR A  76    14099  19349  12468   3299   -466    239       C  
ATOM    365  CZ  TYR A  76      13.401   7.452  -2.730  1.00129.18           C  
ANISOU  365  CZ  TYR A  76    15138  20342  13601   3405   -597    157       C  
ATOM    366  OH  TYR A  76      12.241   7.617  -3.446  1.00133.27           O  
ANISOU  366  OH  TYR A  76    15626  21101  13909   3694   -758     62       O  
ATOM    367  N   ARG A  77      20.108   7.097   0.303  1.00105.35           N  
ANISOU  367  N   ARG A  77    12120  16460  11451   2152    190    615       N  
ATOM    368  CA  ARG A  77      21.245   6.646   1.108  1.00102.86           C  
ANISOU  368  CA  ARG A  77    11701  16085  11297   1939    273    570       C  
ATOM    369  C   ARG A  77      21.955   7.825   1.768  1.00106.55           C  
ANISOU  369  C   ARG A  77    12213  16335  11935   1783    392    706       C  
ATOM    370  O   ARG A  77      22.472   7.664   2.873  1.00105.27           O  
ANISOU  370  O   ARG A  77    11946  16103  11947   1615    401    617       O  
ATOM    371  CB  ARG A  77      22.221   5.790   0.284  1.00102.06           C  
ANISOU  371  CB  ARG A  77    11543  16160  11076   1939    358    563       C  
ATOM    372  CG  ARG A  77      21.717   4.373   0.018  1.00107.39           C  
ANISOU  372  CG  ARG A  77    12127  17002  11674   2028    240    347       C  
ATOM    373  CD  ARG A  77      22.734   3.532  -0.725  1.00114.78           C  
ANISOU  373  CD  ARG A  77    12991  18099  12523   2039    320    301       C  
ATOM    374  NE  ARG A  77      23.498   2.682   0.188  1.00120.24           N  
ANISOU  374  NE  ARG A  77    13567  18725  13393   1920    310    183       N  
ATOM    375  CZ  ARG A  77      24.423   1.804  -0.191  1.00132.76           C  
ANISOU  375  CZ  ARG A  77    15059  20421  14962   1936    352     92       C  
ATOM    376  NH1 ARG A  77      24.722   1.655  -1.475  1.00121.79           N  
ANISOU  376  NH1 ARG A  77    13663  19235  13376   2043    424     89       N  
ATOM    377  NH2 ARG A  77      25.062   1.076   0.714  1.00115.93           N  
ANISOU  377  NH2 ARG A  77    12838  18213  12998   1861    318      1       N  
ATOM    378  N   LEU A  78      21.951   9.012   1.110  1.00104.36           N  
ANISOU  378  N   LEU A  78    12096  15947  11608   1840    479    919       N  
ATOM    379  CA  LEU A  78      22.523  10.254   1.639  1.00104.73           C  
ANISOU  379  CA  LEU A  78    12212  15742  11837   1688    604   1044       C  
ATOM    380  C   LEU A  78      21.683  10.710   2.832  1.00106.90           C  
ANISOU  380  C   LEU A  78    12458  15855  12304   1672    486    910       C  
ATOM    381  O   LEU A  78      22.240  11.150   3.837  1.00105.83           O  
ANISOU  381  O   LEU A  78    12255  15583  12372   1481    544    853       O  
ATOM    382  CB  LEU A  78      22.577  11.350   0.557  1.00107.79           C  
ANISOU  382  CB  LEU A  78    12820  16021  12114   1773    719   1327       C  
ATOM    383  CG  LEU A  78      23.174  12.700   0.980  1.00114.16           C  
ANISOU  383  CG  LEU A  78    13733  16514  13128   1599    873   1472       C  
ATOM    384  CD1 LEU A  78      24.682  12.733   0.779  1.00115.30           C  
ANISOU  384  CD1 LEU A  78    13823  16694  13292   1354   1100   1547       C  
ATOM    385  CD2 LEU A  78      22.518  13.840   0.240  1.00119.46           C  
ANISOU  385  CD2 LEU A  78    14666  16984  13738   1771    881   1720       C  
ATOM    386  N   HIS A  79      20.345  10.560   2.731  1.00103.23           N  
ANISOU  386  N   HIS A  79    12015  15448  11762   1869    318    825       N  
ATOM    387  CA  HIS A  79      19.401  10.896   3.800  1.00102.50           C  
ANISOU  387  CA  HIS A  79    11865  15264  11816   1876    195    657       C  
ATOM    388  C   HIS A  79      19.623   9.967   4.996  1.00103.08           C  
ANISOU  388  C   HIS A  79    11746  15432  11988   1689    154    447       C  
ATOM    389  O   HIS A  79      19.551  10.415   6.140  1.00101.88           O  
ANISOU  389  O   HIS A  79    11524  15182  12006   1569    140    339       O  
ATOM    390  CB  HIS A  79      17.951  10.807   3.293  1.00104.12           C  
ANISOU  390  CB  HIS A  79    12100  15581  11880   2136     27    586       C  
ATOM    391  CG  HIS A  79      17.509  11.985   2.478  1.00110.60           C  
ANISOU  391  CG  HIS A  79    13117  16258  12647   2353     23    780       C  
ATOM    392  ND1 HIS A  79      18.174  12.359   1.320  1.00114.60           N  
ANISOU  392  ND1 HIS A  79    13793  16734  13015   2412    143   1056       N  
ATOM    393  CD2 HIS A  79      16.450  12.810   2.658  1.00113.83           C  
ANISOU  393  CD2 HIS A  79    13579  16561  13109   2538    -94    736       C  
ATOM    394  CE1 HIS A  79      17.517  13.408   0.854  1.00116.68           C  
ANISOU  394  CE1 HIS A  79    14233  16846  13255   2629     95   1204       C  
ATOM    395  NE2 HIS A  79      16.472  13.715   1.622  1.00116.65           N  
ANISOU  395  NE2 HIS A  79    14164  16786  13373   2729    -56   1010       N  
ATOM    396  N   LEU A  80      19.946   8.689   4.715  1.00 97.96           N  
ANISOU  396  N   LEU A  80    11020  14971  11230   1671    139    395       N  
ATOM    397  CA  LEU A  80      20.237   7.669   5.716  1.00 95.59           C  
ANISOU  397  CA  LEU A  80    10573  14750  10997   1519     99    245       C  
ATOM    398  C   LEU A  80      21.576   7.957   6.400  1.00 98.23           C  
ANISOU  398  C   LEU A  80    10846  15010  11467   1329    214    287       C  
ATOM    399  O   LEU A  80      21.647   7.909   7.627  1.00 96.96           O  
ANISOU  399  O   LEU A  80    10584  14838  11419   1195    180    179       O  
ATOM    400  CB  LEU A  80      20.226   6.269   5.065  1.00 95.13           C  
ANISOU  400  CB  LEU A  80    10480  14865  10799   1584     54    188       C  
ATOM    401  CG  LEU A  80      20.617   5.052   5.920  1.00 98.44           C  
ANISOU  401  CG  LEU A  80    10790  15337  11277   1459     13     75       C  
ATOM    402  CD1 LEU A  80      19.618   4.804   7.042  1.00 97.79           C  
ANISOU  402  CD1 LEU A  80    10648  15258  11250   1381    -93    -68       C  
ATOM    403  CD2 LEU A  80      20.707   3.812   5.063  1.00100.62           C  
ANISOU  403  CD2 LEU A  80    11061  15730  11442   1546    -11     26       C  
ATOM    404  N   SER A  81      22.616   8.284   5.609  1.00 95.34           N  
ANISOU  404  N   SER A  81    10527  14625  11072   1311    354    432       N  
ATOM    405  CA  SER A  81      23.960   8.599   6.098  1.00 95.34           C  
ANISOU  405  CA  SER A  81    10445  14591  11190   1127    481    452       C  
ATOM    406  C   SER A  81      23.998   9.862   6.969  1.00100.49           C  
ANISOU  406  C   SER A  81    11097  15056  12028    994    531    433       C  
ATOM    407  O   SER A  81      24.709   9.870   7.973  1.00 99.68           O  
ANISOU  407  O   SER A  81    10857  14975  12042    830    553    332       O  
ATOM    408  CB  SER A  81      24.940   8.720   4.937  1.00 99.57           C  
ANISOU  408  CB  SER A  81    11026  15173  11633   1128    637    597       C  
ATOM    409  OG  SER A  81      26.273   8.777   5.412  1.00107.17           O  
ANISOU  409  OG  SER A  81    11856  16169  12693    948    750    564       O  
ATOM    410  N   VAL A  82      23.236  10.916   6.597  1.00 98.73           N  
ANISOU  410  N   VAL A  82    11022  14657  11834   1078    538    515       N  
ATOM    411  CA  VAL A  82      23.154  12.172   7.359  1.00 99.57           C  
ANISOU  411  CA  VAL A  82    11146  14542  12143    977    579    474       C  
ATOM    412  C   VAL A  82      22.438  11.927   8.699  1.00101.58           C  
ANISOU  412  C   VAL A  82    11263  14858  12475    941    437    245       C  
ATOM    413  O   VAL A  82      22.870  12.456   9.724  1.00101.51           O  
ANISOU  413  O   VAL A  82    11150  14794  12626    774    474    125       O  
ATOM    414  CB  VAL A  82      22.541  13.339   6.526  1.00105.83           C  
ANISOU  414  CB  VAL A  82    12162  15098  12950   1117    615    641       C  
ATOM    415  CG1 VAL A  82      22.195  14.546   7.399  1.00106.82           C  
ANISOU  415  CG1 VAL A  82    12305  14971  13311   1056    616    544       C  
ATOM    416  CG2 VAL A  82      23.484  13.760   5.403  1.00107.79           C  
ANISOU  416  CG2 VAL A  82    12544  15272  13138   1071    804    885       C  
ATOM    417  N   ALA A  83      21.377  11.091   8.684  1.00 96.52           N  
ANISOU  417  N   ALA A  83    10606  14360  11709   1078    287    171       N  
ATOM    418  CA  ALA A  83      20.597  10.715   9.868  1.00 94.96           C  
ANISOU  418  CA  ALA A  83    10279  14266  11537   1034    162    -35       C  
ATOM    419  C   ALA A  83      21.465   9.946  10.865  1.00 98.63           C  
ANISOU  419  C   ALA A  83    10586  14871  12017    852    168   -113       C  
ATOM    420  O   ALA A  83      21.367  10.182  12.070  1.00 97.92           O  
ANISOU  420  O   ALA A  83    10380  14821  12006    733    135   -260       O  
ATOM    421  CB  ALA A  83      19.402   9.868   9.459  1.00 94.76           C  
ANISOU  421  CB  ALA A  83    10268  14380  11357   1188     32    -86       C  
ATOM    422  N   ASP A  84      22.331   9.044  10.353  1.00 95.50           N  
ANISOU  422  N   ASP A  84    10182  14567  11538    849    204    -20       N  
ATOM    423  CA  ASP A  84      23.252   8.244  11.159  1.00 94.73           C  
ANISOU  423  CA  ASP A  84     9948  14604  11441    730    195    -68       C  
ATOM    424  C   ASP A  84      24.359   9.125  11.730  1.00 99.59           C  
ANISOU  424  C   ASP A  84    10468  15180  12192    571    302   -101       C  
ATOM    425  O   ASP A  84      24.634   9.036  12.924  1.00 98.79           O  
ANISOU  425  O   ASP A  84    10227  15180  12128    457    260   -221       O  
ATOM    426  CB  ASP A  84      23.838   7.071  10.342  1.00 96.38           C  
ANISOU  426  CB  ASP A  84    10175  14905  11539    812    196     16       C  
ATOM    427  CG  ASP A  84      22.847   5.981   9.950  1.00107.74           C  
ANISOU  427  CG  ASP A  84    11675  16402  12861    931     86     -1       C  
ATOM    428  OD1 ASP A  84      21.836   5.799  10.674  1.00108.08           O  
ANISOU  428  OD1 ASP A  84    11701  16470  12895    904     -7    -93       O  
ATOM    429  OD2 ASP A  84      23.114   5.265   8.954  1.00113.63           O  
ANISOU  429  OD2 ASP A  84    12465  17186  13523   1033     99     54       O  
ATOM    430  N   LEU A  85      24.952  10.010  10.887  1.00 97.74           N  
ANISOU  430  N   LEU A  85    10307  14808  12022    553    446     -2       N  
ATOM    431  CA  LEU A  85      26.022  10.949  11.251  1.00 99.01           C  
ANISOU  431  CA  LEU A  85    10384  14904  12331    372    583    -42       C  
ATOM    432  C   LEU A  85      25.609  11.851  12.414  1.00102.94           C  
ANISOU  432  C   LEU A  85    10811  15324  12978    263    557   -212       C  
ATOM    433  O   LEU A  85      26.395  12.043  13.342  1.00103.13           O  
ANISOU  433  O   LEU A  85    10662  15440  13081    103    585   -352       O  
ATOM    434  CB  LEU A  85      26.446  11.790  10.032  1.00101.05           C  
ANISOU  434  CB  LEU A  85    10787  14985  12622    365    754    125       C  
ATOM    435  CG  LEU A  85      27.665  12.697  10.197  1.00108.06           C  
ANISOU  435  CG  LEU A  85    11595  15800  13663    141    939     95       C  
ATOM    436  CD1 LEU A  85      28.969  11.929   9.969  1.00108.49           C  
ANISOU  436  CD1 LEU A  85    11496  16083  13642     74   1007     86       C  
ATOM    437  CD2 LEU A  85      27.591  13.867   9.238  1.00113.12           C  
ANISOU  437  CD2 LEU A  85    12444  16160  14377    119   1096    268       C  
ATOM    438  N   LEU A  86      24.370  12.379  12.365  1.00 98.99           N  
ANISOU  438  N   LEU A  86    10422  14683  12505    364    494   -228       N  
ATOM    439  CA  LEU A  86      23.793  13.240  13.395  1.00 99.19           C  
ANISOU  439  CA  LEU A  86    10381  14635  12670    298    457   -420       C  
ATOM    440  C   LEU A  86      23.671  12.445  14.702  1.00101.51           C  
ANISOU  440  C   LEU A  86    10483  15201  12884    225    339   -593       C  
ATOM    441  O   LEU A  86      24.060  12.946  15.760  1.00101.78           O  
ANISOU  441  O   LEU A  86    10364  15295  13014     76    354   -774       O  
ATOM    442  CB  LEU A  86      22.413  13.748  12.928  1.00 99.54           C  
ANISOU  442  CB  LEU A  86    10578  14520  12722    483    387   -401       C  
ATOM    443  CG  LEU A  86      21.735  14.813  13.789  1.00105.13           C  
ANISOU  443  CG  LEU A  86    11239  15104  13600    459    356   -611       C  
ATOM    444  CD1 LEU A  86      21.998  16.203  13.242  1.00107.92           C  
ANISOU  444  CD1 LEU A  86    11744  15098  14163    454    481   -541       C  
ATOM    445  CD2 LEU A  86      20.248  14.574  13.852  1.00106.32           C  
ANISOU  445  CD2 LEU A  86    11407  15327  13663    639    205   -694       C  
ATOM    446  N   PHE A  87      23.186  11.188  14.606  1.00 96.09           N  
ANISOU  446  N   PHE A  87     9809  14683  12016    321    230   -533       N  
ATOM    447  CA  PHE A  87      23.006  10.294  15.747  1.00 94.50           C  
ANISOU  447  CA  PHE A  87     9473  14727  11706    259    121   -634       C  
ATOM    448  C   PHE A  87      24.314   9.783  16.344  1.00 97.85           C  
ANISOU  448  C   PHE A  87     9759  15318  12103    155    135   -637       C  
ATOM    449  O   PHE A  87      24.405   9.708  17.562  1.00 97.58           O  
ANISOU  449  O   PHE A  87     9578  15462  12037     55     80   -769       O  
ATOM    450  CB  PHE A  87      22.028   9.147  15.423  1.00 94.90           C  
ANISOU  450  CB  PHE A  87     9603  14857  11596    373     16   -567       C  
ATOM    451  CG  PHE A  87      21.990   8.020  16.432  1.00 95.77           C  
ANISOU  451  CG  PHE A  87     9624  15187  11576    301    -76   -595       C  
ATOM    452  CD1 PHE A  87      22.474   6.759  16.107  1.00 98.51           C  
ANISOU  452  CD1 PHE A  87    10015  15588  11825    350   -110   -461       C  
ATOM    453  CD2 PHE A  87      21.501   8.228  17.718  1.00 98.23           C  
ANISOU  453  CD2 PHE A  87     9814  15649  11860    188   -125   -753       C  
ATOM    454  CE1 PHE A  87      22.458   5.721  17.046  1.00 99.26           C  
ANISOU  454  CE1 PHE A  87    10065  15845  11805    291   -195   -450       C  
ATOM    455  CE2 PHE A  87      21.505   7.195  18.662  1.00100.76           C  
ANISOU  455  CE2 PHE A  87    10075  16176  12033    113   -201   -738       C  
ATOM    456  CZ  PHE A  87      21.967   5.945  18.314  1.00 98.45           C  
ANISOU  456  CZ  PHE A  87     9859  15895  11653    168   -237   -569       C  
ATOM    457  N   VAL A  88      25.313   9.424  15.514  1.00 94.09           N  
ANISOU  457  N   VAL A  88     9311  14819  11619    190    202   -508       N  
ATOM    458  CA  VAL A  88      26.597   8.918  16.019  1.00 94.13           C  
ANISOU  458  CA  VAL A  88     9163  15008  11596    126    203   -530       C  
ATOM    459  C   VAL A  88      27.355   9.944  16.873  1.00 99.31           C  
ANISOU  459  C   VAL A  88     9639  15719  12375    -48    273   -710       C  
ATOM    460  O   VAL A  88      28.024   9.561  17.831  1.00 99.45           O  
ANISOU  460  O   VAL A  88     9482  15968  12335   -104    213   -802       O  
ATOM    461  CB  VAL A  88      27.482   8.155  14.997  1.00 98.03           C  
ANISOU  461  CB  VAL A  88     9691  15517  12038    220    244   -393       C  
ATOM    462  CG1 VAL A  88      26.770   6.914  14.467  1.00 96.43           C  
ANISOU  462  CG1 VAL A  88     9621  15312  11707    379    144   -276       C  
ATOM    463  CG2 VAL A  88      27.945   9.057  13.859  1.00 98.95           C  
ANISOU  463  CG2 VAL A  88     9876  15468  12253    191    414   -331       C  
ATOM    464  N   ILE A  89      27.168  11.249  16.574  1.00 96.48           N  
ANISOU  464  N   ILE A  89     9328  15145  12186   -127    388   -770       N  
ATOM    465  CA  ILE A  89      27.711  12.390  17.321  1.00 97.73           C  
ANISOU  465  CA  ILE A  89     9335  15290  12509   -313    471   -978       C  
ATOM    466  C   ILE A  89      27.177  12.344  18.781  1.00100.34           C  
ANISOU  466  C   ILE A  89     9513  15828  12784   -364    347  -1182       C  
ATOM    467  O   ILE A  89      27.863  12.781  19.703  1.00101.36           O  
ANISOU  467  O   ILE A  89     9436  16113  12963   -508    364  -1385       O  
ATOM    468  CB  ILE A  89      27.356  13.712  16.557  1.00102.28           C  
ANISOU  468  CB  ILE A  89    10068  15507  13286   -347    609   -955       C  
ATOM    469  CG1 ILE A  89      28.316  13.925  15.357  1.00103.83           C  
ANISOU  469  CG1 ILE A  89    10347  15570  13533   -386    777   -791       C  
ATOM    470  CG2 ILE A  89      27.305  14.958  17.475  1.00104.87           C  
ANISOU  470  CG2 ILE A  89    10284  15745  13816   -509    657  -1216       C  
ATOM    471  CD1 ILE A  89      27.844  14.937  14.277  1.00112.79           C  
ANISOU  471  CD1 ILE A  89    11729  16334  14794   -355    900   -640       C  
ATOM    472  N   THR A  90      25.973  11.772  18.971  1.00 94.55           N  
ANISOU  472  N   THR A  90     8866  15129  11927   -257    229  -1137       N  
ATOM    473  CA  THR A  90      25.305  11.603  20.260  1.00 93.65           C  
ANISOU  473  CA  THR A  90     8631  15238  11713   -303    118  -1298       C  
ATOM    474  C   THR A  90      25.892  10.438  21.114  1.00 95.59           C  
ANISOU  474  C   THR A  90     8754  15817  11750   -312     13  -1260       C  
ATOM    475  O   THR A  90      25.701  10.425  22.329  1.00 95.69           O  
ANISOU  475  O   THR A  90     8621  16074  11665   -391    -57  -1409       O  
ATOM    476  CB  THR A  90      23.769  11.639  20.049  1.00101.40           C  
ANISOU  476  CB  THR A  90     9743  16115  12669   -210     64  -1293       C  
ATOM    477  OG1 THR A  90      23.230  12.832  20.613  1.00103.42           O  
ANISOU  477  OG1 THR A  90     9923  16304  13068   -275     89  -1535       O  
ATOM    478  CG2 THR A  90      23.030  10.402  20.575  1.00 98.77           C  
ANISOU  478  CG2 THR A  90     9416  16006  12108   -174    -59  -1230       C  
ATOM    479  N   LEU A  91      26.615   9.483  20.484  1.00 90.78           N  
ANISOU  479  N   LEU A  91     8203  15223  11067   -219     -2  -1067       N  
ATOM    480  CA  LEU A  91      27.220   8.325  21.165  1.00 90.47           C  
ANISOU  480  CA  LEU A  91     8084  15449  10844   -177   -115   -994       C  
ATOM    481  C   LEU A  91      28.209   8.587  22.329  1.00 95.55           C  
ANISOU  481  C   LEU A  91     8472  16391  11443   -273   -147  -1169       C  
ATOM    482  O   LEU A  91      28.071   7.893  23.340  1.00 95.45           O  
ANISOU  482  O   LEU A  91     8402  16628  11238   -261   -269  -1152       O  
ATOM    483  CB  LEU A  91      27.731   7.251  20.201  1.00 89.88           C  
ANISOU  483  CB  LEU A  91     8126  15301  10724    -25   -133   -779       C  
ATOM    484  CG  LEU A  91      26.678   6.468  19.408  1.00 93.13           C  
ANISOU  484  CG  LEU A  91     8762  15538  11083     86   -166   -609       C  
ATOM    485  CD1 LEU A  91      27.337   5.635  18.339  1.00 93.05           C  
ANISOU  485  CD1 LEU A  91     8838  15446  11071    227   -156   -458       C  
ATOM    486  CD2 LEU A  91      25.820   5.576  20.321  1.00 95.04           C  
ANISOU  486  CD2 LEU A  91     9045  15909  11156     78   -287   -561       C  
ATOM    487  N   PRO A  92      29.171   9.563  22.278  1.00 93.20           N  
ANISOU  487  N   PRO A  92     8013  16098  11301   -380    -42  -1344       N  
ATOM    488  CA  PRO A  92      30.026   9.810  23.457  1.00 94.64           C  
ANISOU  488  CA  PRO A  92     7920  16615  11424   -474    -86  -1557       C  
ATOM    489  C   PRO A  92      29.202  10.159  24.698  1.00 98.33           C  
ANISOU  489  C   PRO A  92     8297  17265  11798   -564   -153  -1729       C  
ATOM    490  O   PRO A  92      29.597   9.773  25.797  1.00 99.27           O  
ANISOU  490  O   PRO A  92     8244  17742  11730   -572   -261  -1803       O  
ATOM    491  CB  PRO A  92      30.922  10.978  23.022  1.00 97.89           C  
ANISOU  491  CB  PRO A  92     8205  16919  12072   -620     80  -1745       C  
ATOM    492  CG  PRO A  92      30.216  11.608  21.881  1.00101.48           C  
ANISOU  492  CG  PRO A  92     8889  16961  12709   -627    208  -1646       C  
ATOM    493  CD  PRO A  92      29.538  10.475  21.176  1.00 95.06           C  
ANISOU  493  CD  PRO A  92     8304  16053  11760   -435    128  -1358       C  
ATOM    494  N   PHE A  93      28.037  10.840  24.517  1.00 93.66           N  
ANISOU  494  N   PHE A  93     7817  16455  11313   -612   -100  -1788       N  
ATOM    495  CA  PHE A  93      27.107  11.176  25.600  1.00 94.03           C  
ANISOU  495  CA  PHE A  93     7779  16674  11274   -690   -154  -1972       C  
ATOM    496  C   PHE A  93      26.603   9.886  26.268  1.00 95.66           C  
ANISOU  496  C   PHE A  93     8035  17135  11174   -620   -295  -1793       C  
ATOM    497  O   PHE A  93      26.672   9.786  27.492  1.00 96.57           O  
ANISOU  497  O   PHE A  93     7981  17606  11104   -686   -371  -1915       O  
ATOM    498  CB  PHE A  93      25.918  12.018  25.095  1.00 95.73           C  
ANISOU  498  CB  PHE A  93     8123  16583  11665   -699    -83  -2048       C  
ATOM    499  CG  PHE A  93      26.250  13.368  24.501  1.00 98.82           C  
ANISOU  499  CG  PHE A  93     8510  16668  12368   -771     59  -2205       C  
ATOM    500  CD1 PHE A  93      26.427  14.479  25.315  1.00104.00           C  
ANISOU  500  CD1 PHE A  93     8966  17391  13160   -920    105  -2550       C  
ATOM    501  CD2 PHE A  93      26.324  13.541  23.124  1.00100.70           C  
ANISOU  501  CD2 PHE A  93     8956  16542  12762   -696    152  -2010       C  
ATOM    502  CE1 PHE A  93      26.716  15.730  24.764  1.00106.46           C  
ANISOU  502  CE1 PHE A  93     9302  17362  13787  -1003    248  -2684       C  
ATOM    503  CE2 PHE A  93      26.603  14.797  22.572  1.00105.04           C  
ANISOU  503  CE2 PHE A  93     9539  16778  13595   -774    295  -2115       C  
ATOM    504  CZ  PHE A  93      26.796  15.882  23.397  1.00105.24           C  
ANISOU  504  CZ  PHE A  93     9382  16825  13779   -932    345  -2446       C  
ATOM    505  N   TRP A  94      26.153   8.888  25.458  1.00 89.17           N  
ANISOU  505  N   TRP A  94     7447  16138  10296   -495   -324  -1503       N  
ATOM    506  CA  TRP A  94      25.698   7.565  25.911  1.00 88.17           C  
ANISOU  506  CA  TRP A  94     7422  16164   9915   -438   -437  -1288       C  
ATOM    507  C   TRP A  94      26.811   6.870  26.703  1.00 94.17           C  
ANISOU  507  C   TRP A  94     8063  17227  10491   -393   -541  -1220       C  
ATOM    508  O   TRP A  94      26.534   6.267  27.738  1.00 94.61           O  
ANISOU  508  O   TRP A  94     8093  17555  10302   -418   -634  -1163       O  
ATOM    509  CB  TRP A  94      25.344   6.666  24.711  1.00 84.99           C  
ANISOU  509  CB  TRP A  94     7273  15474   9547   -308   -434  -1023       C  
ATOM    510  CG  TRP A  94      24.009   6.891  24.063  1.00 84.34           C  
ANISOU  510  CG  TRP A  94     7332  15174   9539   -315   -384  -1030       C  
ATOM    511  CD1 TRP A  94      23.663   7.918  23.234  1.00 86.87           C  
ANISOU  511  CD1 TRP A  94     7685  15254  10069   -305   -292  -1139       C  
ATOM    512  CD2 TRP A  94      22.911   5.969  24.038  1.00 83.45           C  
ANISOU  512  CD2 TRP A  94     7366  15046   9296   -311   -426   -899       C  
ATOM    513  NE1 TRP A  94      22.386   7.729  22.754  1.00 85.28           N  
ANISOU  513  NE1 TRP A  94     7614  14930   9858   -271   -294  -1107       N  
ATOM    514  CE2 TRP A  94      21.905   6.535  23.224  1.00 86.47           C  
ANISOU  514  CE2 TRP A  94     7826  15223   9808   -291   -367   -977       C  
ATOM    515  CE3 TRP A  94      22.668   4.726  24.647  1.00 84.99           C  
ANISOU  515  CE3 TRP A  94     7637  15379   9277   -330   -505   -724       C  
ATOM    516  CZ2 TRP A  94      20.673   5.903  23.007  1.00 85.20           C  
ANISOU  516  CZ2 TRP A  94     7776  15029   9565   -299   -384   -926       C  
ATOM    517  CZ3 TRP A  94      21.450   4.102  24.432  1.00 85.98           C  
ANISOU  517  CZ3 TRP A  94     7897  15434   9338   -369   -501   -657       C  
ATOM    518  CH2 TRP A  94      20.462   4.696  23.635  1.00 85.67           C  
ANISOU  518  CH2 TRP A  94     7893  15231   9428   -359   -441   -780       C  
ATOM    519  N   ALA A  95      28.066   6.959  26.201  1.00 92.00           N  
ANISOU  519  N   ALA A  95     7712  16921  10324   -322   -522  -1224       N  
ATOM    520  CA  ALA A  95      29.258   6.365  26.806  1.00 93.71           C  
ANISOU  520  CA  ALA A  95     7787  17425  10392   -235   -629  -1188       C  
ATOM    521  C   ALA A  95      29.632   7.027  28.133  1.00100.79           C  
ANISOU  521  C   ALA A  95     8403  18721  11171   -350   -670  -1451       C  
ATOM    522  O   ALA A  95      30.020   6.319  29.062  1.00102.18           O  
ANISOU  522  O   ALA A  95     8505  19225  11093   -279   -808  -1374       O  
ATOM    523  CB  ALA A  95      30.427   6.426  25.837  1.00 94.39           C  
ANISOU  523  CB  ALA A  95     7830  17389  10645   -148   -575  -1186       C  
ATOM    524  N   VAL A  96      29.515   8.371  28.224  1.00 98.34           N  
ANISOU  524  N   VAL A  96     7942  18382  11042   -516   -556  -1761       N  
ATOM    525  CA  VAL A  96      29.811   9.145  29.438  1.00100.89           C  
ANISOU  525  CA  VAL A  96     7973  19074  11288   -649   -577  -2084       C  
ATOM    526  C   VAL A  96      28.773   8.838  30.534  1.00106.17           C  
ANISOU  526  C   VAL A  96     8649  19998  11691   -698   -659  -2077       C  
ATOM    527  O   VAL A  96      29.141   8.663  31.702  1.00107.81           O  
ANISOU  527  O   VAL A  96     8669  20646  11647   -713   -762  -2165       O  
ATOM    528  CB  VAL A  96      29.983  10.662  29.134  1.00105.52           C  
ANISOU  528  CB  VAL A  96     8419  19485  12190   -818   -418  -2426       C  
ATOM    529  CG1 VAL A  96      29.866  11.520  30.395  1.00107.55           C  
ANISOU  529  CG1 VAL A  96     8404  20073  12389   -976   -429  -2803       C  
ATOM    530  CG2 VAL A  96      31.315  10.925  28.433  1.00106.08           C  
ANISOU  530  CG2 VAL A  96     8389  19480  12439   -816   -344  -2477       C  
ATOM    531  N   ASP A  97      27.490   8.722  30.131  1.00101.33           N  
ANISOU  531  N   ASP A  97     8248  19139  11114   -719   -614  -1966       N  
ATOM    532  CA  ASP A  97      26.357   8.384  30.994  1.00101.67           C  
ANISOU  532  CA  ASP A  97     8322  19390  10919   -789   -660  -1945       C  
ATOM    533  C   ASP A  97      26.514   6.961  31.551  1.00105.73           C  
ANISOU  533  C   ASP A  97     8944  20128  11101   -695   -793  -1615       C  
ATOM    534  O   ASP A  97      26.194   6.728  32.718  1.00107.14           O  
ANISOU  534  O   ASP A  97     9035  20685  10989   -766   -858  -1637       O  
ATOM    535  CB  ASP A  97      25.042   8.547  30.206  1.00102.06           C  
ANISOU  535  CB  ASP A  97     8568  19093  11117   -812   -576  -1907       C  
ATOM    536  CG  ASP A  97      23.821   7.876  30.802  1.00115.66           C  
ANISOU  536  CG  ASP A  97    10379  20973  12595   -875   -609  -1805       C  
ATOM    537  OD1 ASP A  97      23.401   6.828  30.263  1.00115.49           O  
ANISOU  537  OD1 ASP A  97    10591  20779  12511   -810   -629  -1501       O  
ATOM    538  OD2 ASP A  97      23.269   8.413  31.789  1.00123.61           O  
ANISOU  538  OD2 ASP A  97    11210  22276  13480  -1003   -604  -2051       O  
ATOM    539  N   ALA A  98      27.041   6.034  30.728  1.00101.15           N  
ANISOU  539  N   ALA A  98     8552  19318  10563   -532   -833  -1317       N  
ATOM    540  CA  ALA A  98      27.282   4.638  31.098  1.00102.18           C  
ANISOU  540  CA  ALA A  98     8828  19560  10434   -405   -963   -975       C  
ATOM    541  C   ALA A  98      28.481   4.460  32.047  1.00109.47           C  
ANISOU  541  C   ALA A  98     9548  20900  11146   -314  -1096  -1003       C  
ATOM    542  O   ALA A  98      28.438   3.584  32.915  1.00110.38           O  
ANISOU  542  O   ALA A  98     9725  21264  10949   -263  -1214   -787       O  
ATOM    543  CB  ALA A  98      27.476   3.791  29.850  1.00101.25           C  
ANISOU  543  CB  ALA A  98     8956  19041  10472   -245   -960   -707       C  
ATOM    544  N   VAL A  99      29.547   5.275  31.877  1.00107.53           N  
ANISOU  544  N   VAL A  99     9062  20736  11061   -296  -1075  -1263       N  
ATOM    545  CA  VAL A  99      30.753   5.182  32.709  1.00110.53           C  
ANISOU  545  CA  VAL A  99     9197  21544  11254   -198  -1206  -1348       C  
ATOM    546  C   VAL A  99      30.450   5.756  34.085  1.00117.83           C  
ANISOU  546  C   VAL A  99     9896  22939  11936   -346  -1239  -1584       C  
ATOM    547  O   VAL A  99      30.414   4.999  35.055  1.00119.72           O  
ANISOU  547  O   VAL A  99    10154  23514  11818   -280  -1373  -1402       O  
ATOM    548  CB  VAL A  99      32.090   5.567  32.011  1.00114.62           C  
ANISOU  548  CB  VAL A  99     9542  22015  11996   -109  -1184  -1506       C  
ATOM    549  CG1 VAL A  99      32.410   4.624  30.861  1.00113.09           C  
ANISOU  549  CG1 VAL A  99     9583  21465  11922     89  -1200  -1208       C  
ATOM    550  CG2 VAL A  99      32.110   7.024  31.549  1.00113.57           C  
ANISOU  550  CG2 VAL A  99     9240  21733  12177   -315  -1003  -1878       C  
ATOM    551  N   ALA A 100      30.254   7.087  34.181  1.00115.02           N  
ANISOU  551  N   ALA A 100     9327  22611  11764   -540  -1117  -1989       N  
ATOM    552  CA  ALA A 100      30.005   7.737  35.466  1.00117.34           C  
ANISOU  552  CA  ALA A 100     9363  23370  11850   -686  -1140  -2291       C  
ATOM    553  C   ALA A 100      28.875   8.696  35.857  1.00121.67           C  
ANISOU  553  C   ALA A 100     9834  23935  12459   -904  -1028  -2588       C  
ATOM    554  O   ALA A 100      28.411   8.620  36.994  1.00123.26           O  
ANISOU  554  O   ALA A 100     9929  24560  12346   -979  -1084  -2659       O  
ATOM    555  CB  ALA A 100      31.248   8.577  35.736  1.00120.01           C  
ANISOU  555  CB  ALA A 100     9347  23967  12285   -710  -1147  -2667       C  
ATOM    556  N   ASN A 101      28.450   9.613  34.947  1.00116.73           N  
ANISOU  556  N   ASN A 101     9254  22875  12223   -995   -874  -2769       N  
ATOM    557  CA  ASN A 101      27.434  10.627  35.263  1.00116.97           C  
ANISOU  557  CA  ASN A 101     9193  22890  12360  -1166   -776  -3098       C  
ATOM    558  C   ASN A 101      26.835  11.305  34.015  1.00119.72           C  
ANISOU  558  C   ASN A 101     9715  22653  13119  -1186   -633  -3133       C  
ATOM    559  O   ASN A 101      27.127  10.901  32.887  1.00117.55           O  
ANISOU  559  O   ASN A 101     9650  22001  13011  -1080   -605  -2869       O  
ATOM    560  CB  ASN A 101      27.740  11.571  36.447  1.00119.87           C  
ANISOU  560  CB  ASN A 101     9185  23719  12640  -1303   -787  -3574       C  
ATOM    561  CG  ASN A 101      26.566  11.882  37.345  1.00139.66           C  
ANISOU  561  CG  ASN A 101    11604  26493  14968  -1428   -773  -3779       C  
ATOM    562  OD1 ASN A 101      25.495  11.277  37.249  1.00133.03           O  
ANISOU  562  OD1 ASN A 101    10970  25572  14001  -1425   -766  -3544       O  
ATOM    563  ND2 ASN A 101      26.750  12.834  38.252  1.00132.18           N  
ANISOU  563  ND2 ASN A 101    10325  25895  14002  -1553   -763  -4254       N  
ATOM    564  N   TRP A 102      25.988  12.339  34.239  1.00117.46           N  
ANISOU  564  N   TRP A 102     9335  22313  12982  -1307   -552  -3468       N  
ATOM    565  CA  TRP A 102      25.338  13.150  33.209  1.00116.11           C  
ANISOU  565  CA  TRP A 102     9305  21624  13187  -1311   -432  -3548       C  
ATOM    566  C   TRP A 102      25.605  14.619  33.584  1.00122.77           C  
ANISOU  566  C   TRP A 102     9897  22461  14289  -1440   -352  -4046       C  
ATOM    567  O   TRP A 102      24.841  15.223  34.348  1.00123.89           O  
ANISOU  567  O   TRP A 102     9887  22786  14398  -1523   -346  -4366       O  
ATOM    568  CB  TRP A 102      23.832  12.888  33.031  1.00113.58           C  
ANISOU  568  CB  TRP A 102     9154  21189  12812  -1291   -422  -3453       C  
ATOM    569  CG  TRP A 102      23.241  13.688  31.910  1.00113.32           C  
ANISOU  569  CG  TRP A 102     9272  20633  13150  -1244   -325  -3510       C  
ATOM    570  CD1 TRP A 102      22.686  14.931  31.990  1.00117.41           C  
ANISOU  570  CD1 TRP A 102     9689  21009  13913  -1291   -259  -3879       C  
ATOM    571  CD2 TRP A 102      23.243  13.337  30.522  1.00111.05           C  
ANISOU  571  CD2 TRP A 102     9264  19896  13034  -1119   -287  -3191       C  
ATOM    572  NE1 TRP A 102      22.302  15.360  30.742  1.00115.49           N  
ANISOU  572  NE1 TRP A 102     9665  20246  13970  -1190   -192  -3775       N  
ATOM    573  CE2 TRP A 102      22.629  14.399  29.821  1.00114.87           C  
ANISOU  573  CE2 TRP A 102     9816  19993  13838  -1090   -205  -3356       C  
ATOM    574  CE3 TRP A 102      23.682  12.213  29.802  1.00110.69           C  
ANISOU  574  CE3 TRP A 102     9417  19743  12895  -1015   -321  -2789       C  
ATOM    575  CZ2 TRP A 102      22.453  14.375  28.434  1.00112.56           C  
ANISOU  575  CZ2 TRP A 102     9782  19247  13740   -966   -156  -3114       C  
ATOM    576  CZ3 TRP A 102      23.503  12.188  28.428  1.00110.44           C  
ANISOU  576  CZ3 TRP A 102     9622  19270  13069   -906   -265  -2586       C  
ATOM    577  CH2 TRP A 102      22.891  13.257  27.758  1.00111.10           C  
ANISOU  577  CH2 TRP A 102     9768  19009  13436   -884   -184  -2738       C  
ATOM    578  N   TYR A 103      26.684  15.185  33.025  1.00119.91           N  
ANISOU  578  N   TYR A 103     9489  21879  14192  -1467   -281  -4124       N  
ATOM    579  CA  TYR A 103      27.128  16.562  33.275  1.00122.07           C  
ANISOU  579  CA  TYR A 103     9541  22081  14760  -1616   -185  -4585       C  
ATOM    580  C   TYR A 103      26.560  17.554  32.249  1.00125.98           C  
ANISOU  580  C   TYR A 103    10225  21961  15680  -1616    -51  -4641       C  
ATOM    581  O   TYR A 103      26.670  18.768  32.440  1.00127.84           O  
ANISOU  581  O   TYR A 103    10324  22049  16201  -1737     38  -5028       O  
ATOM    582  CB  TYR A 103      28.672  16.636  33.271  1.00124.37           C  
ANISOU  582  CB  TYR A 103     9656  22498  15101  -1679   -165  -4658       C  
ATOM    583  CG  TYR A 103      29.368  15.443  33.894  1.00125.84           C  
ANISOU  583  CG  TYR A 103     9744  23187  14883  -1590   -316  -4457       C  
ATOM    584  CD1 TYR A 103      29.834  14.393  33.107  1.00125.78           C  
ANISOU  584  CD1 TYR A 103     9939  23060  14794  -1438   -358  -4023       C  
ATOM    585  CD2 TYR A 103      29.565  15.366  35.270  1.00128.84           C  
ANISOU  585  CD2 TYR A 103     9829  24168  14956  -1641   -423  -4704       C  
ATOM    586  CE1 TYR A 103      30.463  13.286  33.676  1.00126.67           C  
ANISOU  586  CE1 TYR A 103     9982  23597  14550  -1320   -512  -3827       C  
ATOM    587  CE2 TYR A 103      30.200  14.268  35.849  1.00130.17           C  
ANISOU  587  CE2 TYR A 103     9929  24793  14737  -1526   -578  -4488       C  
ATOM    588  CZ  TYR A 103      30.648  13.230  35.048  1.00134.45           C  
ANISOU  588  CZ  TYR A 103    10694  25164  15227  -1357   -625  -4044       C  
ATOM    589  OH  TYR A 103      31.275  12.146  35.614  1.00135.10           O  
ANISOU  589  OH  TYR A 103    10727  25659  14945  -1211   -791  -3824       O  
ATOM    590  N   PHE A 104      25.949  17.030  31.172  1.00120.23           N  
ANISOU  590  N   PHE A 104     9814  20878  14988  -1474    -42  -4259       N  
ATOM    591  CA  PHE A 104      25.407  17.779  30.035  1.00119.55           C  
ANISOU  591  CA  PHE A 104     9962  20211  15249  -1418     62  -4204       C  
ATOM    592  C   PHE A 104      24.255  18.744  30.289  1.00124.71           C  
ANISOU  592  C   PHE A 104    10599  20707  16079  -1411     80  -4507       C  
ATOM    593  O   PHE A 104      24.218  19.807  29.666  1.00125.40           O  
ANISOU  593  O   PHE A 104    10779  20339  16530  -1418    182  -4623       O  
ATOM    594  CB  PHE A 104      25.177  16.866  28.823  1.00118.56           C  
ANISOU  594  CB  PHE A 104    10151  19827  15071  -1256     52  -3722       C  
ATOM    595  CG  PHE A 104      26.349  15.942  28.583  1.00119.46           C  
ANISOU  595  CG  PHE A 104    10264  20093  15034  -1244     30  -3467       C  
ATOM    596  CD1 PHE A 104      26.272  14.596  28.919  1.00121.38           C  
ANISOU  596  CD1 PHE A 104    10536  20650  14932  -1156    -94  -3213       C  
ATOM    597  CD2 PHE A 104      27.564  16.437  28.119  1.00122.85           C  
ANISOU  597  CD2 PHE A 104    10636  20376  15664  -1330    135  -3513       C  
ATOM    598  CE1 PHE A 104      27.372  13.750  28.743  1.00122.13           C  
ANISOU  598  CE1 PHE A 104    10619  20886  14901  -1109   -133  -3003       C  
ATOM    599  CE2 PHE A 104      28.663  15.591  27.944  1.00125.41           C  
ANISOU  599  CE2 PHE A 104    10917  20887  15844  -1301    104  -3324       C  
ATOM    600  CZ  PHE A 104      28.558  14.253  28.253  1.00122.17           C  
ANISOU  600  CZ  PHE A 104    10545  20770  15103  -1170    -40  -3073       C  
ATOM    601  N   GLY A 105      23.350  18.391  31.198  1.00121.47           N  
ANISOU  601  N   GLY A 105    10069  20669  15414  -1398    -13  -4636       N  
ATOM    602  CA  GLY A 105      22.239  19.257  31.573  1.00122.76           C  
ANISOU  602  CA  GLY A 105    10160  20770  15711  -1381    -10  -4981       C  
ATOM    603  C   GLY A 105      20.896  18.977  30.933  1.00125.13           C  
ANISOU  603  C   GLY A 105    10669  20880  15996  -1211    -46  -4808       C  
ATOM    604  O   GLY A 105      20.712  17.946  30.284  1.00122.03           O  
ANISOU  604  O   GLY A 105    10474  20459  15432  -1122    -81  -4406       O  
ATOM    605  N   ASN A 106      19.958  19.927  31.121  1.00123.88           N  
ANISOU  605  N   ASN A 106    10446  20594  16028  -1161    -40  -5149       N  
ATOM    606  CA  ASN A 106      18.560  19.915  30.671  1.00123.12           C  
ANISOU  606  CA  ASN A 106    10470  20366  15945   -988    -84  -5126       C  
ATOM    607  C   ASN A 106      18.354  19.849  29.150  1.00124.88           C  
ANISOU  607  C   ASN A 106    11032  20068  16347   -802    -64  -4752       C  
ATOM    608  O   ASN A 106      17.681  18.930  28.673  1.00122.17           O  
ANISOU  608  O   ASN A 106    10820  19793  15804   -703   -117  -4479       O  
ATOM    609  CB  ASN A 106      17.803  21.108  31.294  1.00127.74           C  
ANISOU  609  CB  ASN A 106    10865  20933  16737   -964    -85  -5650       C  
ATOM    610  CG  ASN A 106      16.332  21.193  30.958  1.00152.45           C  
ANISOU  610  CG  ASN A 106    14053  23990  19880   -770   -143  -5715       C  
ATOM    611  OD1 ASN A 106      15.905  22.001  30.125  1.00147.92           O  
ANISOU  611  OD1 ASN A 106    13644  22932  19628   -585   -136  -5740       O  
ATOM    612  ND2 ASN A 106      15.521  20.386  31.625  1.00144.00           N  
ANISOU  612  ND2 ASN A 106    12843  23415  18457   -810   -201  -5757       N  
ATOM    613  N   PHE A 107      18.897  20.837  28.404  1.00122.46           N  
ANISOU  613  N   PHE A 107    10865  19255  16412   -764     18  -4754       N  
ATOM    614  CA  PHE A 107      18.752  20.946  26.948  1.00121.11           C  
ANISOU  614  CA  PHE A 107    11020  18583  16416   -584     47  -4412       C  
ATOM    615  C   PHE A 107      19.342  19.773  26.184  1.00120.88           C  
ANISOU  615  C   PHE A 107    11160  18589  16180   -581     53  -3943       C  
ATOM    616  O   PHE A 107      18.701  19.269  25.260  1.00118.83           O  
ANISOU  616  O   PHE A 107    11103  18194  15853   -411     14  -3669       O  
ATOM    617  CB  PHE A 107      19.315  22.282  26.426  1.00125.55           C  
ANISOU  617  CB  PHE A 107    11695  18605  17404   -588    156  -4506       C  
ATOM    618  CG  PHE A 107      18.936  22.604  24.997  1.00127.06           C  
ANISOU  618  CG  PHE A 107    12225  18278  17775   -369    176  -4194       C  
ATOM    619  CD1 PHE A 107      19.786  22.282  23.945  1.00129.01           C  
ANISOU  619  CD1 PHE A 107    12695  18292  18033   -388    260  -3790       C  
ATOM    620  CD2 PHE A 107      17.734  23.239  24.705  1.00130.55           C  
ANISOU  620  CD2 PHE A 107    12752  18493  18359   -131    106  -4316       C  
ATOM    621  CE1 PHE A 107      19.436  22.580  22.625  1.00130.07           C  
ANISOU  621  CE1 PHE A 107    13141  17987  18292   -183    279  -3492       C  
ATOM    622  CE2 PHE A 107      17.386  23.539  23.383  1.00133.57           C  
ANISOU  622  CE2 PHE A 107    13452  18423  18876     99    109  -4012       C  
ATOM    623  CZ  PHE A 107      18.240  23.208  22.354  1.00130.50           C  
ANISOU  623  CZ  PHE A 107    13291  17820  18472     65    198  -3593       C  
ATOM    624  N   LEU A 108      20.557  19.350  26.563  1.00116.13           N  
ANISOU  624  N   LEU A 108    10461  18182  15482   -755     94  -3879       N  
ATOM    625  CA  LEU A 108      21.251  18.241  25.922  1.00113.27           C  
ANISOU  625  CA  LEU A 108    10228  17870  14938   -749     96  -3477       C  
ATOM    626  C   LEU A 108      20.629  16.877  26.219  1.00114.45           C  
ANISOU  626  C   LEU A 108    10372  18385  14727   -706    -12  -3303       C  
ATOM    627  O   LEU A 108      20.767  15.979  25.392  1.00112.08           O  
ANISOU  627  O   LEU A 108    10250  18013  14320   -625    -24  -2957       O  
ATOM    628  CB  LEU A 108      22.756  18.285  26.216  1.00114.09           C  
ANISOU  628  CB  LEU A 108    10209  18066  15073   -924    167  -3498       C  
ATOM    629  CG  LEU A 108      23.663  18.796  25.081  1.00119.20           C  
ANISOU  629  CG  LEU A 108    11030  18290  15973   -940    299  -3316       C  
ATOM    630  CD1 LEU A 108      23.297  20.216  24.634  1.00121.64           C  
ANISOU  630  CD1 LEU A 108    11450  18119  16650   -919    390  -3473       C  
ATOM    631  CD2 LEU A 108      25.097  18.795  25.513  1.00122.64           C  
ANISOU  631  CD2 LEU A 108    11278  18906  16412  -1129    363  -3404       C  
ATOM    632  N   CYS A 109      19.895  16.737  27.354  1.00111.11           N  
ANISOU  632  N   CYS A 109     9754  18339  14124   -764    -80  -3548       N  
ATOM    633  CA  CYS A 109      19.180  15.504  27.718  1.00109.21           C  
ANISOU  633  CA  CYS A 109     9512  18438  13544   -761   -161  -3401       C  
ATOM    634  C   CYS A 109      18.012  15.322  26.763  1.00110.64           C  
ANISOU  634  C   CYS A 109     9879  18400  13761   -593   -185  -3273       C  
ATOM    635  O   CYS A 109      17.734  14.201  26.336  1.00108.60           O  
ANISOU  635  O   CYS A 109     9747  18201  13314   -557   -219  -2996       O  
ATOM    636  CB  CYS A 109      18.711  15.540  29.170  1.00111.24           C  
ANISOU  636  CB  CYS A 109     9502  19165  13598   -892   -203  -3715       C  
ATOM    637  SG  CYS A 109      17.869  14.030  29.723  1.00114.18           S  
ANISOU  637  SG  CYS A 109     9880  19965  13537   -948   -272  -3518       S  
ATOM    638  N   LYS A 110      17.343  16.443  26.425  1.00107.28           N  
ANISOU  638  N   LYS A 110     9465  17713  13585   -481   -171  -3492       N  
ATOM    639  CA  LYS A 110      16.223  16.518  25.491  1.00105.96           C  
ANISOU  639  CA  LYS A 110     9449  17328  13482   -279   -207  -3428       C  
ATOM    640  C   LYS A 110      16.739  16.246  24.074  1.00106.84           C  
ANISOU  640  C   LYS A 110     9836  17079  13680   -157   -175  -3048       C  
ATOM    641  O   LYS A 110      16.208  15.367  23.392  1.00104.40           O  
ANISOU  641  O   LYS A 110     9652  16791  13226    -66   -216  -2828       O  
ATOM    642  CB  LYS A 110      15.558  17.905  25.564  1.00110.81           C  
ANISOU  642  CB  LYS A 110    10001  17735  14367   -164   -211  -3773       C  
ATOM    643  CG  LYS A 110      14.836  18.182  26.875  1.00126.90           C  
ANISOU  643  CG  LYS A 110    11749  20156  16312   -252   -248  -4197       C  
ATOM    644  CD  LYS A 110      14.500  19.661  27.016  1.00139.02           C  
ANISOU  644  CD  LYS A 110    13211  21436  18173   -146   -244  -4572       C  
ATOM    645  CE  LYS A 110      13.831  19.991  28.328  1.00150.49           C  
ANISOU  645  CE  LYS A 110    14346  23293  19539   -232   -275  -5043       C  
ATOM    646  NZ  LYS A 110      12.436  19.475  28.395  1.00158.19           N  
ANISOU  646  NZ  LYS A 110    15240  24551  20312   -141   -348  -5134       N  
ATOM    647  N   ALA A 111      17.811  16.965  23.663  1.00103.53           N  
ANISOU  647  N   ALA A 111     9495  16359  13484   -181    -91  -2986       N  
ATOM    648  CA  ALA A 111      18.455  16.856  22.351  1.00102.28           C  
ANISOU  648  CA  ALA A 111     9578  15872  13410    -94    -33  -2646       C  
ATOM    649  C   ALA A 111      18.908  15.434  22.015  1.00103.53           C  
ANISOU  649  C   ALA A 111     9803  16213  13323   -122    -52  -2341       C  
ATOM    650  O   ALA A 111      18.604  14.959  20.922  1.00101.90           O  
ANISOU  650  O   ALA A 111     9781  15863  13072     21    -65  -2100       O  
ATOM    651  CB  ALA A 111      19.621  17.828  22.244  1.00104.66           C  
ANISOU  651  CB  ALA A 111     9894  15906  13965   -196     85  -2682       C  
ATOM    652  N   VAL A 112      19.600  14.750  22.955  1.00 99.58           N  
ANISOU  652  N   VAL A 112     9148  16030  12656   -286    -64  -2362       N  
ATOM    653  CA  VAL A 112      20.067  13.365  22.781  1.00 97.58           C  
ANISOU  653  CA  VAL A 112     8951  15943  12180   -301    -96  -2090       C  
ATOM    654  C   VAL A 112      18.865  12.430  22.555  1.00100.22           C  
ANISOU  654  C   VAL A 112     9364  16384  12332   -220   -173  -1997       C  
ATOM    655  O   VAL A 112      18.895  11.600  21.643  1.00 98.57           O  
ANISOU  655  O   VAL A 112     9314  16082  12058   -133   -182  -1747       O  
ATOM    656  CB  VAL A 112      20.996  12.916  23.948  1.00101.93           C  
ANISOU  656  CB  VAL A 112     9316  16827  12587   -463   -115  -2148       C  
ATOM    657  CG1 VAL A 112      21.122  11.396  24.038  1.00100.45           C  
ANISOU  657  CG1 VAL A 112     9184  16842  12138   -456   -183  -1898       C  
ATOM    658  CG2 VAL A 112      22.376  13.558  23.828  1.00102.75           C  
ANISOU  658  CG2 VAL A 112     9363  16818  12858   -533    -31  -2178       C  
ATOM    659  N   HIS A 113      17.793  12.619  23.342  1.00 97.27           N  
ANISOU  659  N   HIS A 113     8863  16207  11889   -256   -218  -2231       N  
ATOM    660  CA  HIS A 113      16.566  11.838  23.232  1.00 96.18           C  
ANISOU  660  CA  HIS A 113     8755  16203  11585   -219   -274  -2209       C  
ATOM    661  C   HIS A 113      15.814  12.101  21.924  1.00100.63           C  
ANISOU  661  C   HIS A 113     9476  16497  12261    -12   -286  -2145       C  
ATOM    662  O   HIS A 113      15.286  11.154  21.338  1.00 99.17           O  
ANISOU  662  O   HIS A 113     9385  16344  11949     35   -317  -1998       O  
ATOM    663  CB  HIS A 113      15.676  12.053  24.460  1.00 97.88           C  
ANISOU  663  CB  HIS A 113     8757  16744  11688   -332   -301  -2511       C  
ATOM    664  CG  HIS A 113      16.061  11.184  25.616  1.00101.26           C  
ANISOU  664  CG  HIS A 113     9079  17531  11865   -527   -312  -2468       C  
ATOM    665  ND1 HIS A 113      17.143  11.488  26.421  1.00103.74           N  
ANISOU  665  ND1 HIS A 113     9277  17968  12173   -627   -299  -2524       N  
ATOM    666  CD2 HIS A 113      15.507  10.027  26.049  1.00102.61           C  
ANISOU  666  CD2 HIS A 113     9256  17951  11780   -634   -335  -2362       C  
ATOM    667  CE1 HIS A 113      17.203  10.518  27.319  1.00103.28           C  
ANISOU  667  CE1 HIS A 113     9164  18242  11837   -762   -328  -2434       C  
ATOM    668  NE2 HIS A 113      16.239   9.619  27.137  1.00103.01           N  
ANISOU  668  NE2 HIS A 113     9214  18274  11650   -782   -343  -2321       N  
ATOM    669  N   VAL A 114      15.802  13.367  21.445  1.00 98.85           N  
ANISOU  669  N   VAL A 114     9289  15998  12270    115   -262  -2247       N  
ATOM    670  CA  VAL A 114      15.120  13.712  20.190  1.00 98.75           C  
ANISOU  670  CA  VAL A 114     9438  15734  12349    348   -287  -2167       C  
ATOM    671  C   VAL A 114      15.873  13.249  18.950  1.00100.81           C  
ANISOU  671  C   VAL A 114     9910  15784  12609    428   -248  -1832       C  
ATOM    672  O   VAL A 114      15.242  12.877  17.960  1.00100.31           O  
ANISOU  672  O   VAL A 114     9965  15664  12485    588   -288  -1718       O  
ATOM    673  CB  VAL A 114      14.574  15.164  20.080  1.00104.98           C  
ANISOU  673  CB  VAL A 114    10220  16299  13368    501   -299  -2382       C  
ATOM    674  CG1 VAL A 114      13.643  15.502  21.241  1.00106.05           C  
ANISOU  674  CG1 VAL A 114    10120  16697  13477    449   -350  -2757       C  
ATOM    675  CG2 VAL A 114      15.687  16.196  19.943  1.00106.07           C  
ANISOU  675  CG2 VAL A 114    10433  16121  13749    470   -206  -2342       C  
ATOM    676  N   ILE A 115      17.218  13.264  19.010  1.00 96.42           N  
ANISOU  676  N   ILE A 115     9377  15150  12108    316   -169  -1704       N  
ATOM    677  CA  ILE A 115      18.089  12.831  17.917  1.00 95.27           C  
ANISOU  677  CA  ILE A 115     9397  14847  11956    367   -115  -1414       C  
ATOM    678  C   ILE A 115      18.022  11.301  17.759  1.00 97.31           C  
ANISOU  678  C   ILE A 115     9678  15300  11996    350   -163  -1265       C  
ATOM    679  O   ILE A 115      18.037  10.799  16.635  1.00 96.24           O  
ANISOU  679  O   ILE A 115     9684  15069  11813    469   -161  -1079       O  
ATOM    680  CB  ILE A 115      19.518  13.436  18.072  1.00 99.18           C  
ANISOU  680  CB  ILE A 115     9871  15220  12595    243     -7  -1380       C  
ATOM    681  CG1 ILE A 115      19.518  14.919  17.616  1.00101.53           C  
ANISOU  681  CG1 ILE A 115    10256  15180  13140    306     65  -1433       C  
ATOM    682  CG2 ILE A 115      20.596  12.625  17.336  1.00 99.20           C  
ANISOU  682  CG2 ILE A 115     9956  15214  12523    231     45  -1127       C  
ATOM    683  CD1 ILE A 115      20.724  15.769  18.052  1.00110.07           C  
ANISOU  683  CD1 ILE A 115    11266  16144  14411    128    184  -1513       C  
ATOM    684  N   TYR A 116      17.877  10.575  18.881  1.00 93.36           N  
ANISOU  684  N   TYR A 116     9043  15069  11359    206   -208  -1353       N  
ATOM    685  CA  TYR A 116      17.742   9.119  18.886  1.00 91.80           C  
ANISOU  685  CA  TYR A 116     8882  15025  10975    169   -252  -1219       C  
ATOM    686  C   TYR A 116      16.405   8.694  18.269  1.00 95.68           C  
ANISOU  686  C   TYR A 116     9429  15534  11392    265   -302  -1251       C  
ATOM    687  O   TYR A 116      16.378   7.725  17.514  1.00 94.17           O  
ANISOU  687  O   TYR A 116     9344  15314  11124    316   -315  -1101       O  
ATOM    688  CB  TYR A 116      17.910   8.559  20.313  1.00 92.83           C  
ANISOU  688  CB  TYR A 116     8873  15430  10968    -17   -279  -1284       C  
ATOM    689  CG  TYR A 116      17.723   7.061  20.444  1.00 93.35           C  
ANISOU  689  CG  TYR A 116     9000  15616  10851    -72   -320  -1133       C  
ATOM    690  CD1 TYR A 116      18.443   6.174  19.649  1.00 94.38           C  
ANISOU  690  CD1 TYR A 116     9265  15624  10972      2   -320   -910       C  
ATOM    691  CD2 TYR A 116      16.873   6.527  21.407  1.00 94.54           C  
ANISOU  691  CD2 TYR A 116     9075  16004  10843   -213   -350  -1218       C  
ATOM    692  CE1 TYR A 116      18.295   4.796  19.783  1.00 94.41           C  
ANISOU  692  CE1 TYR A 116     9343  15687  10841    -46   -358   -776       C  
ATOM    693  CE2 TYR A 116      16.716   5.149  21.550  1.00 95.22           C  
ANISOU  693  CE2 TYR A 116     9246  16157  10778   -288   -373  -1059       C  
ATOM    694  CZ  TYR A 116      17.438   4.286  20.742  1.00100.54           C  
ANISOU  694  CZ  TYR A 116    10071  16657  11473   -198   -381   -837       C  
ATOM    695  OH  TYR A 116      17.289   2.927  20.878  1.00100.80           O  
ANISOU  695  OH  TYR A 116    10207  16703  11390   -265   -404   -685       O  
ATOM    696  N   THR A 117      15.310   9.424  18.574  1.00 93.95           N  
ANISOU  696  N   THR A 117     9120  15374  11201    297   -333  -1475       N  
ATOM    697  CA  THR A 117      13.979   9.126  18.032  1.00 94.39           C  
ANISOU  697  CA  THR A 117     9183  15494  11186    396   -388  -1561       C  
ATOM    698  C   THR A 117      13.857   9.387  16.538  1.00 99.09           C  
ANISOU  698  C   THR A 117     9931  15879  11839    631   -401  -1444       C  
ATOM    699  O   THR A 117      13.259   8.566  15.838  1.00 98.42           O  
ANISOU  699  O   THR A 117     9893  15853  11649    691   -437  -1407       O  
ATOM    700  CB  THR A 117      12.841   9.727  18.862  1.00104.38           C  
ANISOU  700  CB  THR A 117    10271  16944  12442    366   -425  -1866       C  
ATOM    701  OG1 THR A 117      13.295  10.893  19.552  1.00105.29           O  
ANISOU  701  OG1 THR A 117    10304  17001  12699    347   -401  -2000       O  
ATOM    702  CG2 THR A 117      12.256   8.722  19.841  1.00103.56           C  
ANISOU  702  CG2 THR A 117    10048  17151  12148    146   -428  -1951       C  
ATOM    703  N   VAL A 118      14.440  10.505  16.042  1.00 96.52           N  
ANISOU  703  N   VAL A 118     9688  15315  11671    753   -365  -1382       N  
ATOM    704  CA  VAL A 118      14.422  10.829  14.613  1.00 96.78           C  
ANISOU  704  CA  VAL A 118     9889  15151  11733    977   -367  -1226       C  
ATOM    705  C   VAL A 118      15.171   9.753  13.798  1.00 99.71           C  
ANISOU  705  C   VAL A 118    10369  15513  12003    966   -332   -995       C  
ATOM    706  O   VAL A 118      14.618   9.254  12.820  1.00 99.28           O  
ANISOU  706  O   VAL A 118    10383  15490  11850   1105   -374   -947       O  
ATOM    707  CB  VAL A 118      14.793  12.308  14.266  1.00102.21           C  
ANISOU  707  CB  VAL A 118    10669  15555  12612   1098   -324  -1192       C  
ATOM    708  CG1 VAL A 118      16.268  12.618  14.512  1.00101.82           C  
ANISOU  708  CG1 VAL A 118    10650  15364  12673    943   -207  -1067       C  
ATOM    709  CG2 VAL A 118      14.394  12.665  12.836  1.00103.08           C  
ANISOU  709  CG2 VAL A 118    10952  15512  12701   1365   -353  -1044       C  
ATOM    710  N   ASN A 119      16.364   9.325  14.274  1.00 95.54           N  
ANISOU  710  N   ASN A 119     9828  14984  11488    806   -268   -892       N  
ATOM    711  CA  ASN A 119      17.180   8.281  13.645  1.00 94.43           C  
ANISOU  711  CA  ASN A 119     9765  14844  11271    797   -239   -707       C  
ATOM    712  C   ASN A 119      16.497   6.910  13.720  1.00 98.02           C  
ANISOU  712  C   ASN A 119    10200  15460  11585    756   -303   -742       C  
ATOM    713  O   ASN A 119      16.710   6.081  12.837  1.00 97.89           O  
ANISOU  713  O   ASN A 119    10265  15424  11504    824   -302   -636       O  
ATOM    714  CB  ASN A 119      18.577   8.225  14.273  1.00 93.35           C  
ANISOU  714  CB  ASN A 119     9584  14697  11189    655   -173   -632       C  
ATOM    715  CG  ASN A 119      19.477   7.145  13.712  1.00109.17           C  
ANISOU  715  CG  ASN A 119    11643  16712  13125    665   -153   -473       C  
ATOM    716  OD1 ASN A 119      19.593   6.051  14.272  1.00 99.47           O  
ANISOU  716  OD1 ASN A 119    10380  15596  11820    589   -197   -463       O  
ATOM    717  ND2 ASN A 119      20.107   7.415  12.578  1.00101.45           N  
ANISOU  717  ND2 ASN A 119    10758  15618  12172    767    -85   -344       N  
ATOM    718  N   LEU A 120      15.681   6.679  14.762  1.00 94.01           N  
ANISOU  718  N   LEU A 120     9580  15110  11031    631   -347   -901       N  
ATOM    719  CA  LEU A 120      14.965   5.419  14.953  1.00 93.32           C  
ANISOU  719  CA  LEU A 120     9475  15161  10822    540   -385   -943       C  
ATOM    720  C   LEU A 120      13.870   5.227  13.902  1.00 97.52           C  
ANISOU  720  C   LEU A 120    10033  15722  11300    681   -430  -1027       C  
ATOM    721  O   LEU A 120      13.762   4.141  13.329  1.00 96.81           O  
ANISOU  721  O   LEU A 120     9998  15642  11144    677   -438   -986       O  
ATOM    722  CB  LEU A 120      14.384   5.350  16.376  1.00 93.72           C  
ANISOU  722  CB  LEU A 120     9391  15400  10818    343   -398  -1090       C  
ATOM    723  CG  LEU A 120      14.482   4.004  17.100  1.00 98.33           C  
ANISOU  723  CG  LEU A 120     9987  16081  11292    152   -396  -1014       C  
ATOM    724  CD1 LEU A 120      15.926   3.567  17.278  1.00 97.98           C  
ANISOU  724  CD1 LEU A 120    10016  15944  11269    139   -379   -806       C  
ATOM    725  CD2 LEU A 120      13.834   4.082  18.463  1.00101.57           C  
ANISOU  725  CD2 LEU A 120    10262  16715  11616    -45   -394  -1157       C  
ATOM    726  N   TYR A 121      13.097   6.296  13.619  1.00 95.00           N  
ANISOU  726  N   TYR A 121     9672  15410  11015    824   -464  -1156       N  
ATOM    727  CA  TYR A 121      11.998   6.282  12.652  1.00 95.50           C  
ANISOU  727  CA  TYR A 121     9730  15544  11011    999   -529  -1265       C  
ATOM    728  C   TYR A 121      12.411   6.570  11.211  1.00 97.71           C  
ANISOU  728  C   TYR A 121    10151  15690  11283   1234   -530  -1106       C  
ATOM    729  O   TYR A 121      11.950   5.869  10.314  1.00 97.20           O  
ANISOU  729  O   TYR A 121    10107  15708  11118   1320   -566  -1130       O  
ATOM    730  CB  TYR A 121      10.854   7.216  13.087  1.00 98.65           C  
ANISOU  730  CB  TYR A 121     9997  16054  11431   1071   -589  -1504       C  
ATOM    731  CG  TYR A 121      10.192   6.837  14.397  1.00101.80           C  
ANISOU  731  CG  TYR A 121    10226  16667  11786    836   -584  -1707       C  
ATOM    732  CD1 TYR A 121       9.593   5.592  14.567  1.00103.99           C  
ANISOU  732  CD1 TYR A 121    10449  17115  11947    662   -578  -1781       C  
ATOM    733  CD2 TYR A 121      10.111   7.748  15.448  1.00103.43           C  
ANISOU  733  CD2 TYR A 121    10321  16914  12062    778   -579  -1842       C  
ATOM    734  CE1 TYR A 121       8.974   5.243  15.766  1.00105.82           C  
ANISOU  734  CE1 TYR A 121    10535  17559  12114    419   -553  -1945       C  
ATOM    735  CE2 TYR A 121       9.485   7.414  16.648  1.00104.90           C  
ANISOU  735  CE2 TYR A 121    10338  17345  12173    555   -565  -2034       C  
ATOM    736  CZ  TYR A 121       8.919   6.160  16.803  1.00112.95           C  
ANISOU  736  CZ  TYR A 121    11319  18540  13056    370   -547  -2069       C  
ATOM    737  OH  TYR A 121       8.299   5.827  17.981  1.00115.15           O  
ANISOU  737  OH  TYR A 121    11441  19072  13238    123   -514  -2236       O  
ATOM    738  N   SER A 122      13.256   7.599  10.982  1.00 93.56           N  
ANISOU  738  N   SER A 122     9719  14976  10856   1322   -483   -955       N  
ATOM    739  CA  SER A 122      13.706   7.982   9.640  1.00 93.54           C  
ANISOU  739  CA  SER A 122     9865  14851  10826   1526   -462   -772       C  
ATOM    740  C   SER A 122      14.433   6.857   8.901  1.00 95.72           C  
ANISOU  740  C   SER A 122    10203  15152  11013   1499   -421   -643       C  
ATOM    741  O   SER A 122      14.102   6.601   7.744  1.00 96.18           O  
ANISOU  741  O   SER A 122    10316  15271  10957   1667   -453   -617       O  
ATOM    742  CB  SER A 122      14.571   9.238   9.682  1.00 97.57           C  
ANISOU  742  CB  SER A 122    10465  15132  11474   1552   -386   -628       C  
ATOM    743  OG  SER A 122      15.770   9.008  10.403  1.00104.10           O  
ANISOU  743  OG  SER A 122    11269  15905  12380   1342   -296   -556       O  
ATOM    744  N   SER A 123      15.395   6.173   9.577  1.00 89.78           N  
ANISOU  744  N   SER A 123     9431  14373  10307   1307   -363   -583       N  
ATOM    745  CA  SER A 123      16.199   5.078   9.016  1.00 88.29           C  
ANISOU  745  CA  SER A 123     9289  14190  10066   1286   -328   -483       C  
ATOM    746  C   SER A 123      15.348   3.985   8.373  1.00 90.91           C  
ANISOU  746  C   SER A 123     9609  14648  10286   1335   -391   -597       C  
ATOM    747  O   SER A 123      15.466   3.752   7.172  1.00 91.16           O  
ANISOU  747  O   SER A 123     9699  14707  10232   1482   -387   -553       O  
ATOM    748  CB  SER A 123      17.132   4.484  10.069  1.00 90.41           C  
ANISOU  748  CB  SER A 123     9517  14434  10402   1094   -293   -442       C  
ATOM    749  OG  SER A 123      16.404   3.909  11.143  1.00 97.66           O  
ANISOU  749  OG  SER A 123    10356  15441  11310    943   -344   -568       O  
ATOM    750  N   VAL A 124      14.466   3.356   9.162  1.00 86.11           N  
ANISOU  750  N   VAL A 124     8915  14132   9669   1201   -440   -759       N  
ATOM    751  CA  VAL A 124      13.568   2.296   8.708  1.00 85.89           C  
ANISOU  751  CA  VAL A 124     8854  14220   9559   1191   -487   -912       C  
ATOM    752  C   VAL A 124      12.598   2.796   7.616  1.00 89.81           C  
ANISOU  752  C   VAL A 124     9327  14845   9953   1410   -551  -1023       C  
ATOM    753  O   VAL A 124      12.298   2.049   6.683  1.00 90.11           O  
ANISOU  753  O   VAL A 124     9365  14970   9902   1484   -576  -1101       O  
ATOM    754  CB  VAL A 124      12.882   1.573   9.905  1.00 89.77           C  
ANISOU  754  CB  VAL A 124     9264  14779  10068    949   -497  -1044       C  
ATOM    755  CG1 VAL A 124      12.006   2.520  10.729  1.00 89.77           C  
ANISOU  755  CG1 VAL A 124     9151  14886  10072    910   -525  -1177       C  
ATOM    756  CG2 VAL A 124      12.114   0.327   9.461  1.00 90.37           C  
ANISOU  756  CG2 VAL A 124     9317  14931  10090    882   -518  -1199       C  
ATOM    757  N   TRP A 125      12.170   4.074   7.704  1.00 85.92           N  
ANISOU  757  N   TRP A 125     8817  14358   9470   1535   -583  -1030       N  
ATOM    758  CA  TRP A 125      11.275   4.683   6.722  1.00 86.63           C  
ANISOU  758  CA  TRP A 125     8896  14566   9455   1791   -664  -1109       C  
ATOM    759  C   TRP A 125      11.984   5.071   5.431  1.00 90.45           C  
ANISOU  759  C   TRP A 125     9519  14990   9860   2005   -640   -903       C  
ATOM    760  O   TRP A 125      11.340   5.158   4.384  1.00 91.53           O  
ANISOU  760  O   TRP A 125     9657  15271   9851   2222   -711   -954       O  
ATOM    761  CB  TRP A 125      10.478   5.839   7.327  1.00 86.01           C  
ANISOU  761  CB  TRP A 125     8748  14505   9428   1868   -722  -1213       C  
ATOM    762  CG  TRP A 125       9.186   5.388   7.935  1.00 87.34           C  
ANISOU  762  CG  TRP A 125     8731  14892   9562   1772   -787  -1513       C  
ATOM    763  CD1 TRP A 125       8.919   5.217   9.260  1.00 89.56           C  
ANISOU  763  CD1 TRP A 125     8900  15214   9913   1529   -759  -1638       C  
ATOM    764  CD2 TRP A 125       8.021   4.943   7.229  1.00 88.45           C  
ANISOU  764  CD2 TRP A 125     8759  15279   9570   1885   -877  -1740       C  
ATOM    765  NE1 TRP A 125       7.642   4.737   9.427  1.00 89.98           N  
ANISOU  765  NE1 TRP A 125     8782  15515   9891   1471   -813  -1924       N  
ATOM    766  CE2 TRP A 125       7.065   4.565   8.196  1.00 92.62           C  
ANISOU  766  CE2 TRP A 125     9102  15978  10110   1687   -889  -2006       C  
ATOM    767  CE3 TRP A 125       7.682   4.848   5.867  1.00 91.00           C  
ANISOU  767  CE3 TRP A 125     9103  15726   9748   2135   -948  -1759       C  
ATOM    768  CZ2 TRP A 125       5.793   4.096   7.847  1.00 93.44           C  
ANISOU  768  CZ2 TRP A 125     9032  16365  10107   1715   -962  -2307       C  
ATOM    769  CZ3 TRP A 125       6.428   4.368   5.521  1.00 93.95           C  
ANISOU  769  CZ3 TRP A 125     9301  16389  10007   2183  -1037  -2061       C  
ATOM    770  CH2 TRP A 125       5.499   4.001   6.504  1.00 94.84           C  
ANISOU  770  CH2 TRP A 125     9221  16659  10156   1968  -1041  -2340       C  
ATOM    771  N   ILE A 126      13.315   5.262   5.495  1.00 85.70           N  
ANISOU  771  N   ILE A 126     9021  14209   9332   1936   -536   -681       N  
ATOM    772  CA  ILE A 126      14.146   5.537   4.326  1.00 86.16           C  
ANISOU  772  CA  ILE A 126     9206  14226   9307   2081   -477   -475       C  
ATOM    773  C   ILE A 126      14.266   4.218   3.544  1.00 89.48           C  
ANISOU  773  C   ILE A 126     9598  14788   9612   2084   -480   -550       C  
ATOM    774  O   ILE A 126      14.192   4.229   2.313  1.00 90.68           O  
ANISOU  774  O   ILE A 126     9795  15060   9601   2271   -494   -513       O  
ATOM    775  CB  ILE A 126      15.503   6.201   4.724  1.00 88.83           C  
ANISOU  775  CB  ILE A 126     9626  14352   9772   1975   -352   -258       C  
ATOM    776  CG1 ILE A 126      15.347   7.740   4.777  1.00 90.46           C  
ANISOU  776  CG1 ILE A 126     9919  14408  10045   2080   -342   -149       C  
ATOM    777  CG2 ILE A 126      16.664   5.794   3.791  1.00 89.63           C  
ANISOU  777  CG2 ILE A 126     9798  14461   9798   1993   -254   -100       C  
ATOM    778  CD1 ILE A 126      16.296   8.465   5.723  1.00 98.17           C  
ANISOU  778  CD1 ILE A 126    10909  15178  11213   1902   -241    -61       C  
ATOM    779  N   LEU A 127      14.361   3.085   4.273  1.00 83.98           N  
ANISOU  779  N   LEU A 127     8829  14083   8995   1884   -475   -670       N  
ATOM    780  CA  LEU A 127      14.412   1.742   3.695  1.00 83.77           C  
ANISOU  780  CA  LEU A 127     8774  14142   8912   1862   -482   -785       C  
ATOM    781  C   LEU A 127      13.061   1.388   3.062  1.00 89.42           C  
ANISOU  781  C   LEU A 127     9404  15071   9501   1962   -579  -1021       C  
ATOM    782  O   LEU A 127      13.032   0.675   2.058  1.00 90.31           O  
ANISOU  782  O   LEU A 127     9502  15307   9505   2049   -592  -1113       O  
ATOM    783  CB  LEU A 127      14.817   0.684   4.739  1.00 82.51           C  
ANISOU  783  CB  LEU A 127     8591  13867   8893   1626   -457   -826       C  
ATOM    784  CG  LEU A 127      16.142   0.879   5.493  1.00 85.77           C  
ANISOU  784  CG  LEU A 127     9050  14113   9424   1526   -382   -635       C  
ATOM    785  CD1 LEU A 127      16.310  -0.179   6.551  1.00 85.10           C  
ANISOU  785  CD1 LEU A 127     8949  13941   9444   1329   -389   -675       C  
ATOM    786  CD2 LEU A 127      17.334   0.858   4.562  1.00 88.21           C  
ANISOU  786  CD2 LEU A 127     9412  14409   9695   1635   -312   -506       C  
ATOM    787  N   ALA A 128      11.952   1.911   3.632  1.00 86.38           N  
ANISOU  787  N   ALA A 128     8940  14757   9123   1956   -649  -1147       N  
ATOM    788  CA  ALA A 128      10.597   1.734   3.102  1.00 87.82           C  
ANISOU  788  CA  ALA A 128     9003  15183   9180   2063   -750  -1402       C  
ATOM    789  C   ALA A 128      10.472   2.516   1.790  1.00 94.00           C  
ANISOU  789  C   ALA A 128     9836  16102   9776   2386   -806  -1321       C  
ATOM    790  O   ALA A 128       9.917   2.000   0.818  1.00 94.83           O  
ANISOU  790  O   ALA A 128     9874  16436   9723   2511   -867  -1485       O  
ATOM    791  CB  ALA A 128       9.565   2.217   4.109  1.00 88.52           C  
ANISOU  791  CB  ALA A 128     8980  15326   9328   1985   -803  -1554       C  
ATOM    792  N   PHE A 129      11.047   3.736   1.751  1.00 91.32           N  
ANISOU  792  N   PHE A 129     9625  15622   9452   2510   -776  -1059       N  
ATOM    793  CA  PHE A 129      11.071   4.600   0.572  1.00 93.38           C  
ANISOU  793  CA  PHE A 129     9988  15957   9534   2809   -809   -896       C  
ATOM    794  C   PHE A 129      12.022   4.048  -0.490  1.00 96.67           C  
ANISOU  794  C   PHE A 129    10479  16428   9824   2847   -731   -774       C  
ATOM    795  O   PHE A 129      11.805   4.282  -1.680  1.00 98.07           O  
ANISOU  795  O   PHE A 129    10692  16795   9775   3086   -775   -729       O  
ATOM    796  CB  PHE A 129      11.413   6.046   0.967  1.00 95.94           C  
ANISOU  796  CB  PHE A 129    10445  16053   9954   2882   -778   -652       C  
ATOM    797  CG  PHE A 129      10.209   6.948   1.134  1.00 99.49           C  
ANISOU  797  CG  PHE A 129    10850  16563  10387   3083   -912   -756       C  
ATOM    798  CD1 PHE A 129       9.165   6.596   1.984  1.00102.43           C  
ANISOU  798  CD1 PHE A 129    11034  17056  10829   2990   -994  -1062       C  
ATOM    799  CD2 PHE A 129      10.132   8.163   0.462  1.00104.10           C  
ANISOU  799  CD2 PHE A 129    11584  17078  10890   3367   -952   -546       C  
ATOM    800  CE1 PHE A 129       8.052   7.430   2.135  1.00105.15           C  
ANISOU  800  CE1 PHE A 129    11307  17486  11160   3196  -1124  -1197       C  
ATOM    801  CE2 PHE A 129       9.024   9.002   0.624  1.00108.73           C  
ANISOU  801  CE2 PHE A 129    12129  17706  11478   3594  -1094   -654       C  
ATOM    802  CZ  PHE A 129       7.993   8.631   1.461  1.00106.41           C  
ANISOU  802  CZ  PHE A 129    11615  17564  11254   3515  -1183   -997       C  
ATOM    803  N   ILE A 130      13.057   3.292  -0.054  1.00 90.81           N  
ANISOU  803  N   ILE A 130     9747  15545   9211   2624   -622   -735       N  
ATOM    804  CA  ILE A 130      14.023   2.606  -0.915  1.00 90.48           C  
ANISOU  804  CA  ILE A 130     9738  15558   9082   2632   -542   -678       C  
ATOM    805  C   ILE A 130      13.305   1.412  -1.561  1.00 94.31           C  
ANISOU  805  C   ILE A 130    10096  16280   9456   2666   -617   -979       C  
ATOM    806  O   ILE A 130      13.451   1.193  -2.761  1.00 95.01           O  
ANISOU  806  O   ILE A 130    10185  16571   9344   2824   -618   -996       O  
ATOM    807  CB  ILE A 130      15.314   2.230  -0.119  1.00 91.83           C  
ANISOU  807  CB  ILE A 130     9938  15502   9449   2410   -424   -568       C  
ATOM    808  CG1 ILE A 130      16.339   3.383  -0.180  1.00 92.28           C  
ANISOU  808  CG1 ILE A 130    10119  15420   9523   2427   -313   -266       C  
ATOM    809  CG2 ILE A 130      15.952   0.915  -0.597  1.00 92.93           C  
ANISOU  809  CG2 ILE A 130    10030  15702   9576   2361   -387   -687       C  
ATOM    810  CD1 ILE A 130      17.408   3.397   0.929  1.00 96.08           C  
ANISOU  810  CD1 ILE A 130    10602  15682  10223   2209   -221   -174       C  
ATOM    811  N   SER A 131      12.497   0.680  -0.766  1.00 90.28           N  
ANISOU  811  N   SER A 131     9475  15760   9069   2507   -673  -1225       N  
ATOM    812  CA  SER A 131      11.700  -0.453  -1.236  1.00 91.34           C  
ANISOU  812  CA  SER A 131     9476  16089   9140   2488   -736  -1554       C  
ATOM    813  C   SER A 131      10.616   0.012  -2.205  1.00 96.94           C  
ANISOU  813  C   SER A 131    10105  17122   9608   2742   -853  -1690       C  
ATOM    814  O   SER A 131      10.371  -0.677  -3.196  1.00 98.33           O  
ANISOU  814  O   SER A 131    10199  17532   9631   2834   -888  -1889       O  
ATOM    815  CB  SER A 131      11.086  -1.214  -0.064  1.00 94.73           C  
ANISOU  815  CB  SER A 131     9823  16407   9762   2220   -744  -1749       C  
ATOM    816  OG  SER A 131      11.977  -2.212   0.411  1.00103.36           O  
ANISOU  816  OG  SER A 131    10969  17280  11023   2024   -663  -1720       O  
ATOM    817  N   LEU A 132       9.993   1.190  -1.938  1.00 93.21           N  
ANISOU  817  N   LEU A 132     9649  16670   9096   2878   -922  -1595       N  
ATOM    818  CA  LEU A 132       8.973   1.818  -2.794  1.00 94.91           C  
ANISOU  818  CA  LEU A 132     9801  17185   9075   3178  -1058  -1684       C  
ATOM    819  C   LEU A 132       9.588   2.116  -4.163  1.00 99.79           C  
ANISOU  819  C   LEU A 132    10525  17951   9441   3424  -1044  -1493       C  
ATOM    820  O   LEU A 132       9.017   1.741  -5.185  1.00101.23           O  
ANISOU  820  O   LEU A 132    10606  18468   9390   3599  -1129  -1682       O  
ATOM    821  CB  LEU A 132       8.463   3.125  -2.160  1.00 94.94           C  
ANISOU  821  CB  LEU A 132     9849  17093   9131   3293  -1120  -1556       C  
ATOM    822  CG  LEU A 132       7.186   3.045  -1.337  1.00 99.33           C  
ANISOU  822  CG  LEU A 132    10216  17756   9769   3221  -1215  -1864       C  
ATOM    823  CD1 LEU A 132       7.259   3.979  -0.148  1.00 98.02           C  
ANISOU  823  CD1 LEU A 132    10110  17334   9800   3144  -1191  -1726       C  
ATOM    824  CD2 LEU A 132       5.973   3.377  -2.187  1.00104.80           C  
ANISOU  824  CD2 LEU A 132    10776  18816  10226   3536  -1388  -2068       C  
ATOM    825  N   ASP A 133      10.789   2.734  -4.161  1.00 95.62           N  
ANISOU  825  N   ASP A 133    10185  17194   8953   3409   -923  -1136       N  
ATOM    826  CA  ASP A 133      11.606   3.079  -5.328  1.00 97.11           C  
ANISOU  826  CA  ASP A 133    10499  17481   8918   3577   -858   -893       C  
ATOM    827  C   ASP A 133      11.827   1.854  -6.232  1.00101.44           C  
ANISOU  827  C   ASP A 133    10936  18285   9322   3568   -842  -1119       C  
ATOM    828  O   ASP A 133      11.749   1.980  -7.454  1.00103.27           O  
ANISOU  828  O   ASP A 133    11173  18815   9252   3795   -875  -1095       O  
ATOM    829  CB  ASP A 133      12.949   3.680  -4.858  1.00 97.77           C  
ANISOU  829  CB  ASP A 133    10754  17237   9156   3434   -693   -550       C  
ATOM    830  CG  ASP A 133      14.030   3.805  -5.913  1.00109.78           C  
ANISOU  830  CG  ASP A 133    12381  18843  10486   3502   -571   -323       C  
ATOM    831  OD1 ASP A 133      14.794   2.834  -6.095  1.00110.03           O  
ANISOU  831  OD1 ASP A 133    12346  18917  10544   3372   -488   -430       O  
ATOM    832  OD2 ASP A 133      14.156   4.893  -6.504  1.00117.26           O  
ANISOU  832  OD2 ASP A 133    13485  19796  11271   3674   -549    -31       O  
ATOM    833  N   ARG A 134      12.094   0.678  -5.619  1.00 96.07           N  
ANISOU  833  N   ARG A 134    10160  17484   8857   3314   -794  -1340       N  
ATOM    834  CA  ARG A 134      12.309  -0.599  -6.309  1.00 96.19           C  
ANISOU  834  CA  ARG A 134    10064  17671   8814   3275   -776  -1608       C  
ATOM    835  C   ARG A 134      11.024  -1.091  -6.965  1.00101.11           C  
ANISOU  835  C   ARG A 134    10509  18647   9262   3398   -915  -1972       C  
ATOM    836  O   ARG A 134      11.076  -1.599  -8.082  1.00102.58           O  
ANISOU  836  O   ARG A 134    10619  19125   9231   3524   -930  -2130       O  
ATOM    837  CB  ARG A 134      12.867  -1.675  -5.350  1.00 93.85           C  
ANISOU  837  CB  ARG A 134     9742  17084   8831   2982   -701  -1727       C  
ATOM    838  CG  ARG A 134      14.208  -1.349  -4.673  1.00100.20           C  
ANISOU  838  CG  ARG A 134    10680  17580   9810   2856   -572  -1422       C  
ATOM    839  CD  ARG A 134      15.401  -1.334  -5.617  1.00106.28           C  
ANISOU  839  CD  ARG A 134    11497  18446  10438   2949   -468  -1284       C  
ATOM    840  NE  ARG A 134      15.604  -0.018  -6.227  1.00110.25           N  
ANISOU  840  NE  ARG A 134    12114  19050  10725   3118   -433   -975       N  
ATOM    841  CZ  ARG A 134      16.486   0.233  -7.188  1.00123.76           C  
ANISOU  841  CZ  ARG A 134    13874  20911  12238   3212   -333   -819       C  
ATOM    842  NH1 ARG A 134      16.601   1.458  -7.684  1.00109.57           N  
ANISOU  842  NH1 ARG A 134    12212  19169  10252   3344   -294   -507       N  
ATOM    843  NH2 ARG A 134      17.257  -0.736  -7.663  1.00112.93           N  
ANISOU  843  NH2 ARG A 134    12419  19632  10856   3175   -267   -975       N  
ATOM    844  N   TYR A 135       9.875  -0.931  -6.275  1.00 96.99           N  
ANISOU  844  N   TYR A 135     9898  18129   8824   3360  -1016  -2131       N  
ATOM    845  CA  TYR A 135       8.556  -1.318  -6.778  1.00 98.91           C  
ANISOU  845  CA  TYR A 135     9937  18730   8915   3462  -1154  -2512       C  
ATOM    846  C   TYR A 135       8.231  -0.532  -8.055  1.00104.85           C  
ANISOU  846  C   TYR A 135    10692  19863   9282   3842  -1257  -2427       C  
ATOM    847  O   TYR A 135       7.764  -1.116  -9.035  1.00106.57           O  
ANISOU  847  O   TYR A 135    10756  20456   9278   3965  -1329  -2714       O  
ATOM    848  CB  TYR A 135       7.480  -1.136  -5.685  1.00 99.47           C  
ANISOU  848  CB  TYR A 135     9910  18730   9153   3338  -1223  -2665       C  
ATOM    849  CG  TYR A 135       6.058  -1.022  -6.196  1.00104.16           C  
ANISOU  849  CG  TYR A 135    10294  19735   9545   3526  -1388  -2988       C  
ATOM    850  CD1 TYR A 135       5.352  -2.147  -6.612  1.00107.77           C  
ANISOU  850  CD1 TYR A 135    10529  20453   9966   3430  -1426  -3446       C  
ATOM    851  CD2 TYR A 135       5.407   0.209  -6.233  1.00106.29           C  
ANISOU  851  CD2 TYR A 135    10577  20129   9678   3801  -1510  -2859       C  
ATOM    852  CE1 TYR A 135       4.042  -2.047  -7.082  1.00111.61           C  
ANISOU  852  CE1 TYR A 135    10785  21364  10258   3601  -1583  -3783       C  
ATOM    853  CE2 TYR A 135       4.096   0.320  -6.698  1.00110.08           C  
ANISOU  853  CE2 TYR A 135    10840  21022   9963   4007  -1681  -3176       C  
ATOM    854  CZ  TYR A 135       3.413  -0.812  -7.114  1.00119.59           C  
ANISOU  854  CZ  TYR A 135    11798  22527  11113   3901  -1717  -3647       C  
ATOM    855  OH  TYR A 135       2.116  -0.707  -7.561  1.00123.19           O  
ANISOU  855  OH  TYR A 135    12005  23431  11372   4100  -1889  -3997       O  
ATOM    856  N   LEU A 136       8.530   0.781  -8.047  1.00100.54           N  
ANISOU  856  N   LEU A 136    10331  19210   8657   4023  -1258  -2023       N  
ATOM    857  CA  LEU A 136       8.319   1.670  -9.186  1.00102.61           C  
ANISOU  857  CA  LEU A 136    10663  19770   8554   4396  -1347  -1837       C  
ATOM    858  C   LEU A 136       9.321   1.366 -10.292  1.00107.61           C  
ANISOU  858  C   LEU A 136    11365  20560   8962   4455  -1247  -1712       C  
ATOM    859  O   LEU A 136       8.981   1.515 -11.459  1.00110.38           O  
ANISOU  859  O   LEU A 136    11678  21313   8948   4731  -1333  -1740       O  
ATOM    860  CB  LEU A 136       8.413   3.154  -8.773  1.00102.33           C  
ANISOU  860  CB  LEU A 136    10842  19486   8551   4540  -1357  -1421       C  
ATOM    861  CG  LEU A 136       7.533   3.638  -7.606  1.00105.38           C  
ANISOU  861  CG  LEU A 136    11174  19695   9172   4495  -1444  -1515       C  
ATOM    862  CD1 LEU A 136       7.880   5.058  -7.229  1.00105.39           C  
ANISOU  862  CD1 LEU A 136    11413  19388   9244   4612  -1420  -1098       C  
ATOM    863  CD2 LEU A 136       6.049   3.538  -7.926  1.00109.55           C  
ANISOU  863  CD2 LEU A 136    11475  20617   9532   4711  -1651  -1875       C  
ATOM    864  N   ALA A 137      10.542   0.928  -9.932  1.00102.05           N  
ANISOU  864  N   ALA A 137    10744  19575   8455   4209  -1071  -1594       N  
ATOM    865  CA  ALA A 137      11.599   0.609 -10.896  1.00102.95           C  
ANISOU  865  CA  ALA A 137    10901  19834   8382   4236   -953  -1499       C  
ATOM    866  C   ALA A 137      11.363  -0.704 -11.649  1.00108.41           C  
ANISOU  866  C   ALA A 137    11373  20858   8960   4229   -989  -1948       C  
ATOM    867  O   ALA A 137      11.685  -0.777 -12.835  1.00110.44           O  
ANISOU  867  O   ALA A 137    11609  21460   8892   4397   -972  -1947       O  
ATOM    868  CB  ALA A 137      12.957   0.585 -10.210  1.00101.21           C  
ANISOU  868  CB  ALA A 137    10807  19225   8423   3990   -766  -1266       C  
ATOM    869  N   ILE A 138      10.811  -1.733 -10.969  1.00103.87           N  
ANISOU  869  N   ILE A 138    10638  20179   8648   4024  -1028  -2335       N  
ATOM    870  CA  ILE A 138      10.567  -3.055 -11.565  1.00105.08           C  
ANISOU  870  CA  ILE A 138    10583  20573   8769   3972  -1052  -2807       C  
ATOM    871  C   ILE A 138       9.165  -3.186 -12.169  1.00113.19           C  
ANISOU  871  C   ILE A 138    11404  22036   9568   4144  -1227  -3166       C  
ATOM    872  O   ILE A 138       9.042  -3.578 -13.331  1.00115.19           O  
ANISOU  872  O   ILE A 138    11528  22714   9526   4308  -1271  -3392       O  
ATOM    873  CB  ILE A 138      10.936  -4.232 -10.595  1.00105.39           C  
ANISOU  873  CB  ILE A 138    10587  20225   9230   3633   -967  -3021       C  
ATOM    874  CG1 ILE A 138      12.340  -4.076  -9.924  1.00102.96           C  
ANISOU  874  CG1 ILE A 138    10463  19510   9145   3488   -813  -2673       C  
ATOM    875  CG2 ILE A 138      10.761  -5.613 -11.241  1.00107.50           C  
ANISOU  875  CG2 ILE A 138    10662  20682   9502   3574   -978  -3514       C  
ATOM    876  CD1 ILE A 138      13.588  -3.867 -10.848  1.00109.90           C  
ANISOU  876  CD1 ILE A 138    11412  20527   9820   3610   -701  -2472       C  
ATOM    877  N   VAL A 139       8.122  -2.866 -11.382  1.00111.15           N  
ANISOU  877  N   VAL A 139    11091  21706   9435   4106  -1327  -3245       N  
ATOM    878  CA  VAL A 139       6.723  -2.980 -11.813  1.00114.37           C  
ANISOU  878  CA  VAL A 139    11266  22533   9656   4253  -1500  -3626       C  
ATOM    879  C   VAL A 139       6.290  -1.871 -12.785  1.00123.45           C  
ANISOU  879  C   VAL A 139    12443  24093  10371   4678  -1640  -3431       C  
ATOM    880  O   VAL A 139       5.790  -2.191 -13.865  1.00126.36           O  
ANISOU  880  O   VAL A 139    12635  24957  10417   4878  -1743  -3711       O  
ATOM    881  CB  VAL A 139       5.711  -3.195 -10.646  1.00116.82           C  
ANISOU  881  CB  VAL A 139    11457  22677  10253   4034  -1548  -3864       C  
ATOM    882  CG1 VAL A 139       4.366  -3.701 -11.169  1.00119.46           C  
ANISOU  882  CG1 VAL A 139    11482  23481  10427   4107  -1696  -4394       C  
ATOM    883  CG2 VAL A 139       6.265  -4.160  -9.594  1.00113.91           C  
ANISOU  883  CG2 VAL A 139    11135  21841  10305   3620  -1397  -3932       C  
ATOM    884  N   HIS A 140       6.474  -0.584 -12.414  1.00121.13           N  
ANISOU  884  N   HIS A 140    12369  23593  10062   4822  -1649  -2963       N  
ATOM    885  CA  HIS A 140       6.067   0.548 -13.259  1.00125.13           C  
ANISOU  885  CA  HIS A 140    12953  24413  10178   5243  -1786  -2715       C  
ATOM    886  C   HIS A 140       7.149   1.289 -14.066  1.00132.43           C  
ANISOU  886  C   HIS A 140    14137  25335  10844   5415  -1689  -2219       C  
ATOM    887  O   HIS A 140       7.058   2.504 -14.275  1.00133.42           O  
ANISOU  887  O   HIS A 140    14454  25443  10797   5681  -1748  -1828       O  
ATOM    888  CB  HIS A 140       5.112   1.495 -12.497  1.00125.94           C  
ANISOU  888  CB  HIS A 140    13068  24407  10376   5375  -1923  -2640       C  
ATOM    889  CG  HIS A 140       4.060   0.788 -11.695  1.00128.68           C  
ANISOU  889  CG  HIS A 140    13145  24790  10956   5175  -1993  -3129       C  
ATOM    890  ND1 HIS A 140       3.185  -0.114 -12.278  1.00132.79           N  
ANISOU  890  ND1 HIS A 140    13359  25768  11328   5196  -2098  -3658       N  
ATOM    891  CD2 HIS A 140       3.772   0.884 -10.376  1.00128.01           C  
ANISOU  891  CD2 HIS A 140    13053  24361  11226   4939  -1961  -3163       C  
ATOM    892  CE1 HIS A 140       2.413  -0.546 -11.298  1.00131.02           C  
ANISOU  892  CE1 HIS A 140    12959  25440  11382   4950  -2111  -3982       C  
ATOM    893  NE2 HIS A 140       2.720   0.032 -10.140  1.00128.48           N  
ANISOU  893  NE2 HIS A 140    12808  24655  11352   4797  -2033  -3695       N  
ATOM    894  N   ALA A 141       8.179   0.535 -14.506  1.00130.59           N  
ANISOU  894  N   ALA A 141    13909  25111  10599   5252  -1532  -2248       N  
ATOM    895  CA  ALA A 141       9.331   1.034 -15.264  1.00132.63           C  
ANISOU  895  CA  ALA A 141    14374  25393  10624   5334  -1394  -1836       C  
ATOM    896  C   ALA A 141       9.017   2.052 -16.367  1.00143.67           C  
ANISOU  896  C   ALA A 141    15890  27166  11531   5740  -1498  -1535       C  
ATOM    897  O   ALA A 141       9.563   3.159 -16.358  1.00143.54           O  
ANISOU  897  O   ALA A 141    16153  26927  11459   5821  -1423  -1017       O  
ATOM    898  CB  ALA A 141      10.132  -0.135 -15.821  1.00133.39           C  
ANISOU  898  CB  ALA A 141    14344  25643  10693   5172  -1270  -2097       C  
ATOM    899  N   THR A 142       8.112   1.683 -17.291  1.00146.22           N  
ANISOU  899  N   THR A 142    16002  28055  11502   5993  -1673  -1864       N  
ATOM    900  CA  THR A 142       7.649   2.515 -18.404  1.00151.91           C  
ANISOU  900  CA  THR A 142    16796  29223  11701   6426  -1815  -1637       C  
ATOM    901  C   THR A 142       6.124   2.657 -18.304  1.00160.54           C  
ANISOU  901  C   THR A 142    17695  30580  12722   6680  -2087  -1941       C  
ATOM    902  O   THR A 142       5.582   3.690 -18.704  1.00163.29           O  
ANISOU  902  O   THR A 142    18170  31081  12792   7056  -2240  -1657       O  
ATOM    903  CB  THR A 142       8.101   1.902 -19.747  1.00164.10           C  
ANISOU  903  CB  THR A 142    18233  31307  12810   6519  -1771  -1771       C  
ATOM    904  OG1 THR A 142       9.520   1.722 -19.734  1.00163.17           O  
ANISOU  904  OG1 THR A 142    18258  30938  12802   6259  -1511  -1542       O  
ATOM    905  CG2 THR A 142       7.711   2.752 -20.955  1.00167.61           C  
ANISOU  905  CG2 THR A 142    18775  32251  12657   6973  -1908  -1490       C  
ATOM    906  N   ASN A 143       5.456   1.635 -17.779  1.00157.46           N  
ANISOU  906  N   ASN A 143    17005  30239  12584   6476  -2142  -2509       N  
ATOM    907  CA  ASN A 143       4.006   1.662 -17.632  1.00159.62           C  
ANISOU  907  CA  ASN A 143    17039  30796  12815   6665  -2381  -2875       C  
ATOM    908  C   ASN A 143       3.516   2.967 -17.013  1.00164.37           C  
ANISOU  908  C   ASN A 143    17827  31134  13492   6885  -2491  -2514       C  
ATOM    909  O   ASN A 143       2.558   3.572 -17.494  1.00167.20           O  
ANISOU  909  O   ASN A 143    18119  31855  13556   7289  -2721  -2539       O  
ATOM    910  CB  ASN A 143       3.530   0.473 -16.796  1.00159.48           C  
ANISOU  910  CB  ASN A 143    16737  30667  13191   6288  -2352  -3450       C  
ATOM    911  CG  ASN A 143       4.130  -0.841 -17.256  1.00187.17           C  
ANISOU  911  CG  ASN A 143    20098  34295  16723   6033  -2220  -3795       C  
ATOM    912  OD1 ASN A 143       3.564  -1.533 -18.102  1.00187.84           O  
ANISOU  912  OD1 ASN A 143    19965  34784  16623   6061  -2304  -4200       O  
ATOM    913  ND2 ASN A 143       5.284  -1.191 -16.700  1.00174.11           N  
ANISOU  913  ND2 ASN A 143    18611  32162  15381   5712  -2000  -3607       N  
ATOM    914  N   SER A 144       4.180   3.396 -15.945  1.00158.29           N  
ANISOU  914  N   SER A 144    17281  29742  13119   6634  -2336  -2198       N  
ATOM    915  CA  SER A 144       3.815   4.629 -15.259  1.00158.45           C  
ANISOU  915  CA  SER A 144    17488  29442  13273   6805  -2416  -1873       C  
ATOM    916  C   SER A 144       5.042   5.496 -14.995  1.00161.10           C  
ANISOU  916  C   SER A 144    18213  29263  13736   6713  -2221  -1259       C  
ATOM    917  O   SER A 144       5.990   5.063 -14.340  1.00157.31           O  
ANISOU  917  O   SER A 144    17797  28407  13568   6324  -2008  -1206       O  
ATOM    918  CB  SER A 144       3.097   4.320 -13.944  1.00159.64           C  
ANISOU  918  CB  SER A 144    17450  29359  13848   6561  -2447  -2223       C  
ATOM    919  N   GLN A 145       5.016   6.722 -15.508  1.00160.65           N  
ANISOU  919  N   GLN A 145    18415  29190  13436   7074  -2297   -801       N  
ATOM    920  CA  GLN A 145       6.126   7.650 -15.330  1.00159.87           C  
ANISOU  920  CA  GLN A 145    18695  28607  13441   6992  -2108   -211       C  
ATOM    921  C   GLN A 145       6.531   7.776 -13.865  1.00159.39           C  
ANISOU  921  C   GLN A 145    18690  27946  13925   6627  -1971   -189       C  
ATOM    922  O   GLN A 145       5.708   7.595 -12.967  1.00157.69           O  
ANISOU  922  O   GLN A 145    18288  27659  13967   6567  -2077   -517       O  
ATOM    923  CB  GLN A 145       5.757   9.035 -15.865  1.00165.40           C  
ANISOU  923  CB  GLN A 145    19669  29293  13882   7448  -2245    244       C  
ATOM    924  CG  GLN A 145       6.681   9.545 -16.959  1.00181.85           C  
ANISOU  924  CG  GLN A 145    22051  31447  15597   7560  -2114    762       C  
ATOM    925  CD  GLN A 145       6.123  10.760 -17.673  1.00200.21           C  
ANISOU  925  CD  GLN A 145    24695  33520  17857   7714  -2291   1178       C  
ATOM    926  OE1 GLN A 145       5.724  11.738 -17.040  1.00197.10           O  
ANISOU  926  OE1 GLN A 145    24407  33049  17431   8198  -2380   1370       O  
ATOM    927  NE2 GLN A 145       6.092  10.705 -19.000  1.00195.08           N  
ANISOU  927  NE2 GLN A 145    24077  33392  16654   8005  -2356   1304       N  
ATOM    928  N   ARG A 146       7.802   8.086 -13.632  1.00153.59           N  
ANISOU  928  N   ARG A 146    18195  26816  13345   6378  -1733    183       N  
ATOM    929  CA  ARG A 146       8.316   8.237 -12.281  1.00149.03           C  
ANISOU  929  CA  ARG A 146    17675  25695  13253   6033  -1594    226       C  
ATOM    930  C   ARG A 146       7.584   9.140 -11.277  1.00151.73           C  
ANISOU  930  C   ARG A 146    18067  25715  13870   6127  -1709    251       C  
ATOM    931  O   ARG A 146       7.334  10.316 -11.575  1.00154.01           O  
ANISOU  931  O   ARG A 146    18578  25888  14049   6438  -1791    583       O  
ATOM    932  CB  ARG A 146       9.827   8.235 -12.628  1.00148.52           C  
ANISOU  932  CB  ARG A 146    17803  25462  13165   5801  -1329    565       C  
ATOM    933  CG  ARG A 146      10.278   9.356 -13.567  1.00164.11           C  
ANISOU  933  CG  ARG A 146    20099  27421  14835   6038  -1275   1104       C  
ATOM    934  CD  ARG A 146      11.486   8.951 -14.385  1.00176.85           C  
ANISOU  934  CD  ARG A 146    21773  29187  16235   5874  -1056   1274       C  
ATOM    935  NE  ARG A 146      11.101   8.484 -15.717  1.00190.47           N  
ANISOU  935  NE  ARG A 146    23396  31512  17462   6141  -1158   1169       N  
ATOM    936  CZ  ARG A 146      10.944   7.209 -16.057  1.00204.10           C  
ANISOU  936  CZ  ARG A 146    24825  33633  19090   6072  -1195    710       C  
ATOM    937  NH1 ARG A 146      11.146   6.246 -15.164  1.00187.55           N  
ANISOU  937  NH1 ARG A 146    22528  31366  17368   5747  -1136    343       N  
ATOM    938  NH2 ARG A 146      10.591   6.886 -17.291  1.00194.02           N  
ANISOU  938  NH2 ARG A 146    23456  32921  17341   6331  -1290    615       N  
ATOM    939  N   PRO A 147       7.334   8.648 -10.025  1.00144.46           N  
ANISOU  939  N   PRO A 147    16964  24598  13326   5843  -1696    -69       N  
ATOM    940  CA  PRO A 147       6.829   9.540  -8.965  1.00143.54           C  
ANISOU  940  CA  PRO A 147    16898  24143  13500   5879  -1763    -40       C  
ATOM    941  C   PRO A 147       8.090   9.385  -8.096  1.00143.70           C  
ANISOU  941  C   PRO A 147    17018  23735  13849   5442  -1513    107       C  
ATOM    942  O   PRO A 147       8.233  10.035  -7.067  1.00141.68           O  
ANISOU  942  O   PRO A 147    16839  23093  13900   5319  -1467    191       O  
ATOM    943  CB  PRO A 147       5.622   8.847  -8.313  1.00144.16           C  
ANISOU  943  CB  PRO A 147    16637  24454  13685   5845  -1919   -573       C  
ATOM    944  CG  PRO A 147       5.121   7.851  -9.315  1.00150.09           C  
ANISOU  944  CG  PRO A 147    17170  25744  14113   5952  -2014   -876       C  
ATOM    945  CD  PRO A 147       6.295   7.490 -10.142  1.00145.72           C  
ANISOU  945  CD  PRO A 147    16763  25211  13393   5851  -1846   -628       C  
ATOM    946  N   ARG A 148       9.023   8.513  -8.561  1.00139.23           N  
ANISOU  946  N   ARG A 148    16434  23270  13199   5227  -1359    119       N  
ATOM    947  CA  ARG A 148      10.357   8.160  -8.067  1.00136.25           C  
ANISOU  947  CA  ARG A 148    16123  22610  13038   4853  -1125    243       C  
ATOM    948  C   ARG A 148      11.223   9.422  -7.899  1.00140.65           C  
ANISOU  948  C   ARG A 148    16976  22762  13702   4829   -985    708       C  
ATOM    949  O   ARG A 148      12.053   9.487  -6.986  1.00137.77           O  
ANISOU  949  O   ARG A 148    16647  22062  13636   4526   -833    771       O  
ATOM    950  CB  ARG A 148      11.020   7.212  -9.087  1.00137.04           C  
ANISOU  950  CB  ARG A 148    16166  23013  12890   4802  -1036    199       C  
ATOM    951  CG  ARG A 148      11.649   5.975  -8.473  1.00144.89           C  
ANISOU  951  CG  ARG A 148    16999  23945  14109   4446   -924    -59       C  
ATOM    952  CD  ARG A 148      12.094   4.965  -9.518  1.00155.55           C  
ANISOU  952  CD  ARG A 148    18251  25634  15218   4445   -874   -198       C  
ATOM    953  NE  ARG A 148      13.265   5.413 -10.279  1.00165.96           N  
ANISOU  953  NE  ARG A 148    19747  26947  16364   4449   -704    157       N  
ATOM    954  CZ  ARG A 148      14.506   4.965 -10.099  1.00179.79           C  
ANISOU  954  CZ  ARG A 148    21503  28563  18245   4196   -517    207       C  
ATOM    955  NH1 ARG A 148      14.760   4.042  -9.178  1.00163.54           N  
ANISOU  955  NH1 ARG A 148    19307  26340  16493   3942   -489    -49       N  
ATOM    956  NH2 ARG A 148      15.498   5.427 -10.846  1.00169.96           N  
ANISOU  956  NH2 ARG A 148    20400  27363  16815   4199   -357    513       N  
ATOM    957  N   LYS A 149      11.014  10.421  -8.787  1.00140.65           N  
ANISOU  957  N   LYS A 149    17190  22798  13454   5150  -1039   1030       N  
ATOM    958  CA  LYS A 149      11.699  11.714  -8.756  1.00141.85           C  
ANISOU  958  CA  LYS A 149    17657  22550  13691   5157   -912   1489       C  
ATOM    959  C   LYS A 149      11.164  12.523  -7.571  1.00143.64           C  
ANISOU  959  C   LYS A 149    17910  22400  14268   5161   -988   1439       C  
ATOM    960  O   LYS A 149      11.949  13.056  -6.789  1.00141.98           O  
ANISOU  960  O   LYS A 149    17811  21782  14352   4913   -830   1588       O  
ATOM    961  CB  LYS A 149      11.465  12.483 -10.071  1.00149.30           C  
ANISOU  961  CB  LYS A 149    18831  23655  14242   5534   -974   1844       C  
ATOM    962  CG  LYS A 149      12.183  11.904 -11.286  1.00164.69           C  
ANISOU  962  CG  LYS A 149    20798  25956  15819   5513   -855   1969       C  
ATOM    963  CD  LYS A 149      13.320  12.810 -11.739  1.00175.49           C  
ANISOU  963  CD  LYS A 149    22489  27061  17129   5412   -620   2489       C  
ATOM    964  CE  LYS A 149      14.042  12.280 -12.953  1.00186.22           C  
ANISOU  964  CE  LYS A 149    23853  28808  18093   5386   -488   2609       C  
ATOM    965  NZ  LYS A 149      15.212  13.131 -13.301  1.00196.73           N  
ANISOU  965  NZ  LYS A 149    25479  29881  19390   5216   -221   3097       N  
ATOM    966  N   LEU A 150       9.823  12.567  -7.425  1.00139.84           N  
ANISOU  966  N   LEU A 150    17291  22092  13752   5436  -1230   1182       N  
ATOM    967  CA  LEU A 150       9.101  13.290  -6.379  1.00138.85           C  
ANISOU  967  CA  LEU A 150    17140  21700  13916   5503  -1340   1060       C  
ATOM    968  C   LEU A 150       9.398  12.776  -4.973  1.00137.19           C  
ANISOU  968  C   LEU A 150    16749  21305  14072   5101  -1245    789       C  
ATOM    969  O   LEU A 150       9.560  13.589  -4.061  1.00136.28           O  
ANISOU  969  O   LEU A 150    16717  20812  14250   5012  -1200    853       O  
ATOM    970  CB  LEU A 150       7.591  13.258  -6.657  1.00141.01           C  
ANISOU  970  CB  LEU A 150    17244  22319  14016   5890  -1623    781       C  
ATOM    971  CG  LEU A 150       6.793  14.487  -6.238  1.00148.40           C  
ANISOU  971  CG  LEU A 150    18278  23013  15094   6198  -1779    830       C  
ATOM    972  CD1 LEU A 150       6.793  15.544  -7.337  1.00153.57           C  
ANISOU  972  CD1 LEU A 150    19261  23584  15505   6607  -1843   1279       C  
ATOM    973  CD2 LEU A 150       5.365  14.108  -5.912  1.00151.12           C  
ANISOU  973  CD2 LEU A 150    18302  23705  15409   6395  -2021    355       C  
ATOM    974  N   LEU A 151       9.487  11.439  -4.798  1.00130.07           N  
ANISOU  974  N   LEU A 151    15610  20660  13150   4861  -1213    494       N  
ATOM    975  CA  LEU A 151       9.785  10.824  -3.497  1.00125.60           C  
ANISOU  975  CA  LEU A 151    14881  19950  12889   4482  -1126    260       C  
ATOM    976  C   LEU A 151      11.228  11.088  -3.062  1.00127.58           C  
ANISOU  976  C   LEU A 151    15285  19855  13335   4182   -897    521       C  
ATOM    977  O   LEU A 151      11.465  11.329  -1.882  1.00125.11           O  
ANISOU  977  O   LEU A 151    14936  19289  13311   3966   -841    455       O  
ATOM    978  CB  LEU A 151       9.489   9.308  -3.462  1.00123.40           C  
ANISOU  978  CB  LEU A 151    14343  19999  12544   4315  -1153   -100       C  
ATOM    979  CG  LEU A 151       8.134   8.782  -3.960  1.00129.35           C  
ANISOU  979  CG  LEU A 151    14888  21169  13091   4543  -1354   -432       C  
ATOM    980  CD1 LEU A 151       8.126   7.274  -3.967  1.00127.63           C  
ANISOU  980  CD1 LEU A 151    14461  21186  12846   4308  -1323   -742       C  
ATOM    981  CD2 LEU A 151       6.980   9.270  -3.105  1.00132.10           C  
ANISOU  981  CD2 LEU A 151    15102  21513  13577   4636  -1500   -670       C  
ATOM    982  N   ALA A 152      12.178  11.065  -4.018  1.00125.24           N  
ANISOU  982  N   ALA A 152    15139  19581  12866   4172   -765    798       N  
ATOM    983  CA  ALA A 152      13.604  11.299  -3.775  1.00124.17           C  
ANISOU  983  CA  ALA A 152    15126  19177  12875   3894   -536   1036       C  
ATOM    984  C   ALA A 152      13.950  12.784  -3.623  1.00130.56           C  
ANISOU  984  C   ALA A 152    16188  19594  13826   3935   -458   1359       C  
ATOM    985  O   ALA A 152      14.802  13.119  -2.798  1.00128.70           O  
ANISOU  985  O   ALA A 152    15980  19067  13853   3662   -310   1415       O  
ATOM    986  CB  ALA A 152      14.435  10.679  -4.888  1.00125.57           C  
ANISOU  986  CB  ALA A 152    15336  19578  12797   3864   -419   1168       C  
ATOM    987  N   GLU A 153      13.303  13.664  -4.423  1.00130.97           N  
ANISOU  987  N   GLU A 153    16425  19633  13705   4279   -558   1567       N  
ATOM    988  CA  GLU A 153      13.537  15.114  -4.412  1.00133.68           C  
ANISOU  988  CA  GLU A 153    17054  19564  14176   4361   -494   1901       C  
ATOM    989  C   GLU A 153      12.733  15.870  -3.346  1.00137.63           C  
ANISOU  989  C   GLU A 153    17525  19796  14971   4447   -621   1734       C  
ATOM    990  O   GLU A 153      13.289  16.767  -2.711  1.00137.69           O  
ANISOU  990  O   GLU A 153    17668  19389  15257   4295   -502   1864       O  
ATOM    991  CB  GLU A 153      13.256  15.740  -5.793  1.00139.53           C  
ANISOU  991  CB  GLU A 153    18046  20388  14583   4716   -544   2249       C  
ATOM    992  CG  GLU A 153      14.281  15.438  -6.874  1.00151.59           C  
ANISOU  992  CG  GLU A 153    19687  22077  15834   4609   -355   2529       C  
ATOM    993  CD  GLU A 153      13.833  15.788  -8.284  1.00177.87           C  
ANISOU  993  CD  GLU A 153    23208  25632  18742   4985   -441   2816       C  
ATOM    994  OE1 GLU A 153      13.343  16.921  -8.498  1.00175.25           O  
ANISOU  994  OE1 GLU A 153    23129  25052  18408   5260   -521   3080       O  
ATOM    995  OE2 GLU A 153      13.984  14.929  -9.182  1.00171.23           O  
ANISOU  995  OE2 GLU A 153    22269  25221  17568   5016   -431   2776       O  
ATOM    996  N   LYS A 154      11.426  15.559  -3.185  1.00134.11           N  
ANISOU  996  N   LYS A 154    16898  19595  14462   4691   -858   1432       N  
ATOM    997  CA  LYS A 154      10.573  16.295  -2.247  1.00134.50           C  
ANISOU  997  CA  LYS A 154    16897  19444  14762   4814   -992   1242       C  
ATOM    998  C   LYS A 154       9.768  15.603  -1.140  1.00135.89           C  
ANISOU  998  C   LYS A 154    16741  19815  15077   4707  -1107    764       C  
ATOM    999  O   LYS A 154       9.719  16.135  -0.033  1.00134.76           O  
ANISOU  999  O   LYS A 154    16551  19423  15228   4588  -1092    631       O  
ATOM   1000  CB  LYS A 154       9.563  17.186  -2.997  1.00141.37           C  
ANISOU 1000  CB  LYS A 154    17924  20311  15481   5315  -1195   1372       C  
ATOM   1001  CG  LYS A 154      10.191  18.380  -3.714  1.00159.44           C  
ANISOU 1001  CG  LYS A 154    20612  22212  17755   5447  -1091   1875       C  
ATOM   1002  CD  LYS A 154       9.168  19.167  -4.533  1.00173.95           C  
ANISOU 1002  CD  LYS A 154    22619  24075  19400   5992  -1317   2030       C  
ATOM   1003  CE  LYS A 154       9.802  20.291  -5.322  1.00188.73           C  
ANISOU 1003  CE  LYS A 154    24927  25555  21226   6115  -1202   2583       C  
ATOM   1004  NZ  LYS A 154      10.199  21.437  -4.457  1.00198.28           N  
ANISOU 1004  NZ  LYS A 154    26323  26147  22866   5986  -1095   2683       N  
ATOM   1005  N   VAL A 155       9.108  14.459  -1.447  1.00131.54           N  
ANISOU 1005  N   VAL A 155    15958  19710  14312   4746  -1216    499       N  
ATOM   1006  CA  VAL A 155       8.225  13.693  -0.546  1.00129.41           C  
ANISOU 1006  CA  VAL A 155    15369  19683  14118   4640  -1320     46       C  
ATOM   1007  C   VAL A 155       8.950  13.222   0.721  1.00131.52           C  
ANISOU 1007  C   VAL A 155    15526  19800  14645   4196  -1166    -77       C  
ATOM   1008  O   VAL A 155       8.399  13.395   1.805  1.00130.36           O  
ANISOU 1008  O   VAL A 155    15227  19621  14683   4119  -1216   -331       O  
ATOM   1009  CB  VAL A 155       7.432  12.557  -1.253  1.00132.96           C  
ANISOU 1009  CB  VAL A 155    15612  20624  14284   4746  -1444   -201       C  
ATOM   1010  CG1 VAL A 155       6.572  11.760  -0.269  1.00130.73           C  
ANISOU 1010  CG1 VAL A 155    15009  20564  14099   4571  -1514   -658       C  
ATOM   1011  CG2 VAL A 155       6.571  13.107  -2.387  1.00136.64           C  
ANISOU 1011  CG2 VAL A 155    16148  21287  14481   5228  -1635   -127       C  
ATOM   1012  N   VAL A 156      10.183  12.674   0.589  1.00127.81           N  
ANISOU 1012  N   VAL A 156    15127  19259  14176   3924   -985    100       N  
ATOM   1013  CA  VAL A 156      11.021  12.181   1.699  1.00125.37           C  
ANISOU 1013  CA  VAL A 156    14728  18827  14079   3527   -842     24       C  
ATOM   1014  C   VAL A 156      11.141  13.175   2.886  1.00130.91           C  
ANISOU 1014  C   VAL A 156    15444  19220  15076   3422   -807    -10       C  
ATOM   1015  O   VAL A 156      11.157  12.748   4.042  1.00128.78           O  
ANISOU 1015  O   VAL A 156    15004  18976  14950   3173   -783   -227       O  
ATOM   1016  CB  VAL A 156      12.392  11.618   1.211  1.00128.38           C  
ANISOU 1016  CB  VAL A 156    15200  19173  14405   3325   -664    245       C  
ATOM   1017  CG1 VAL A 156      13.290  12.706   0.614  1.00130.22           C  
ANISOU 1017  CG1 VAL A 156    15696  19125  14658   3377   -536    618       C  
ATOM   1018  CG2 VAL A 156      13.115  10.837   2.308  1.00125.26           C  
ANISOU 1018  CG2 VAL A 156    14670  18744  14180   2961   -563    117       C  
ATOM   1019  N   TYR A 157      11.169  14.488   2.585  1.00130.92           N  
ANISOU 1019  N   TYR A 157    15649  18937  15156   3622   -809    195       N  
ATOM   1020  CA  TYR A 157      11.251  15.574   3.560  1.00131.73           C  
ANISOU 1020  CA  TYR A 157    15788  18713  15550   3566   -780    155       C  
ATOM   1021  C   TYR A 157       9.986  15.667   4.421  1.00135.92           C  
ANISOU 1021  C   TYR A 157    16103  19381  16161   3670   -947   -219       C  
ATOM   1022  O   TYR A 157      10.090  15.685   5.643  1.00133.99           O  
ANISOU 1022  O   TYR A 157    15713  19090  16108   3438   -905   -426       O  
ATOM   1023  CB  TYR A 157      11.507  16.912   2.837  1.00136.74           C  
ANISOU 1023  CB  TYR A 157    16729  18988  16239   3790   -749    484       C  
ATOM   1024  CG  TYR A 157      12.963  17.206   2.536  1.00139.07           C  
ANISOU 1024  CG  TYR A 157    17221  19022  16596   3555   -518    809       C  
ATOM   1025  CD1 TYR A 157      13.606  18.299   3.107  1.00142.56           C  
ANISOU 1025  CD1 TYR A 157    17793  19044  17327   3419   -393    902       C  
ATOM   1026  CD2 TYR A 157      13.692  16.403   1.660  1.00138.99           C  
ANISOU 1026  CD2 TYR A 157    17250  19200  16360   3464   -418    994       C  
ATOM   1027  CE1 TYR A 157      14.944  18.577   2.832  1.00143.95           C  
ANISOU 1027  CE1 TYR A 157    18126  19006  17564   3174   -166   1173       C  
ATOM   1028  CE2 TYR A 157      15.033  16.667   1.384  1.00140.31           C  
ANISOU 1028  CE2 TYR A 157    17566  19171  16575   3237   -196   1262       C  
ATOM   1029  CZ  TYR A 157      15.655  17.755   1.973  1.00149.05           C  
ANISOU 1029  CZ  TYR A 157    18794  19872  17968   3083    -66   1353       C  
ATOM   1030  OH  TYR A 157      16.974  18.025   1.698  1.00149.94           O  
ANISOU 1030  OH  TYR A 157    19030  19812  18129   2832    167   1593       O  
ATOM   1031  N   VAL A 158       8.799  15.699   3.790  1.00134.75           N  
ANISOU 1031  N   VAL A 158    15910  19444  15846   4017  -1134   -324       N  
ATOM   1032  CA  VAL A 158       7.515  15.841   4.489  1.00135.46           C  
ANISOU 1032  CA  VAL A 158    15773  19708  15989   4154  -1300   -703       C  
ATOM   1033  C   VAL A 158       6.779  14.505   4.779  1.00137.36           C  
ANISOU 1033  C   VAL A 158    15713  20405  16074   4014  -1361  -1037       C  
ATOM   1034  O   VAL A 158       5.805  14.487   5.536  1.00137.15           O  
ANISOU 1034  O   VAL A 158    15454  20562  16095   4029  -1459  -1386       O  
ATOM   1035  CB  VAL A 158       6.590  16.909   3.832  1.00143.67           C  
ANISOU 1035  CB  VAL A 158    16920  20670  16997   4644  -1485   -670       C  
ATOM   1036  CG1 VAL A 158       5.811  17.683   4.894  1.00144.79           C  
ANISOU 1036  CG1 VAL A 158    16914  20731  17370   4731  -1581   -990       C  
ATOM   1037  CG2 VAL A 158       7.383  17.875   2.949  1.00146.03           C  
ANISOU 1037  CG2 VAL A 158    17593  20574  17317   4806  -1412   -210       C  
ATOM   1038  N   GLY A 159       7.271  13.409   4.210  1.00132.40           N  
ANISOU 1038  N   GLY A 159    15087  19943  15275   3859  -1290   -940       N  
ATOM   1039  CA  GLY A 159       6.680  12.086   4.390  1.00130.70           C  
ANISOU 1039  CA  GLY A 159    14627  20102  14930   3696  -1323  -1224       C  
ATOM   1040  C   GLY A 159       7.401  11.197   5.380  1.00131.65           C  
ANISOU 1040  C   GLY A 159    14663  20202  15155   3259  -1176  -1276       C  
ATOM   1041  O   GLY A 159       6.788  10.295   5.958  1.00130.27           O  
ANISOU 1041  O   GLY A 159    14276  20274  14946   3077  -1195  -1550       O  
ATOM   1042  N   VAL A 160       8.714  11.435   5.568  1.00126.88           N  
ANISOU 1042  N   VAL A 160    14225  19313  14670   3088  -1027  -1009       N  
ATOM   1043  CA  VAL A 160       9.571  10.663   6.473  1.00124.06           C  
ANISOU 1043  CA  VAL A 160    13813  18919  14406   2712   -896  -1011       C  
ATOM   1044  C   VAL A 160      10.362  11.487   7.489  1.00127.48           C  
ANISOU 1044  C   VAL A 160    14289  19083  15065   2548   -799   -944       C  
ATOM   1045  O   VAL A 160      10.459  11.082   8.652  1.00125.91           O  
ANISOU 1045  O   VAL A 160    13951  18942  14945   2290   -760  -1094       O  
ATOM   1046  CB  VAL A 160      10.609   9.793   5.694  1.00126.85           C  
ANISOU 1046  CB  VAL A 160    14274  19266  14658   2615   -796   -793       C  
ATOM   1047  CG1 VAL A 160      11.702   9.237   6.609  1.00124.43           C  
ANISOU 1047  CG1 VAL A 160    13948  18858  14472   2283   -667   -740       C  
ATOM   1048  CG2 VAL A 160       9.924   8.665   4.933  1.00126.70           C  
ANISOU 1048  CG2 VAL A 160    14163  19540  14438   2677   -870   -933       C  
ATOM   1049  N   TRP A 161      10.924  12.635   7.047  1.00125.07           N  
ANISOU 1049  N   TRP A 161    14177  18490  14854   2688   -756   -719       N  
ATOM   1050  CA  TRP A 161      11.751  13.532   7.850  1.00124.65           C  
ANISOU 1050  CA  TRP A 161    14180  18150  15032   2539   -651   -655       C  
ATOM   1051  C   TRP A 161      10.884  14.331   8.817  1.00128.58           C  
ANISOU 1051  C   TRP A 161    14552  18622  15680   2595   -735   -925       C  
ATOM   1052  O   TRP A 161      11.040  14.161  10.026  1.00127.23           O  
ANISOU 1052  O   TRP A 161    14227  18509  15607   2352   -695  -1106       O  
ATOM   1053  CB  TRP A 161      12.617  14.450   6.978  1.00125.25           C  
ANISOU 1053  CB  TRP A 161    14515  17913  15161   2641   -556   -326       C  
ATOM   1054  CG  TRP A 161      13.952  13.878   6.619  1.00124.92           C  
ANISOU 1054  CG  TRP A 161    14546  17842  15075   2434   -400   -106       C  
ATOM   1055  CD1 TRP A 161      14.201  12.819   5.795  1.00126.80           C  
ANISOU 1055  CD1 TRP A 161    14790  18281  15107   2436   -388    -14       C  
ATOM   1056  CD2 TRP A 161      15.228  14.365   7.045  1.00124.78           C  
ANISOU 1056  CD2 TRP A 161    14587  17595  15228   2206   -236     18       C  
ATOM   1057  NE1 TRP A 161      15.554  12.601   5.703  1.00125.50           N  
ANISOU 1057  NE1 TRP A 161    14678  18033  14973   2235   -230    157       N  
ATOM   1058  CE2 TRP A 161      16.210  13.542   6.451  1.00127.58           C  
ANISOU 1058  CE2 TRP A 161    14970  18043  15460   2087   -133    183       C  
ATOM   1059  CE3 TRP A 161      15.639  15.417   7.881  1.00127.09           C  
ANISOU 1059  CE3 TRP A 161    14891  17625  15773   2086   -164    -28       C  
ATOM   1060  CZ2 TRP A 161      17.579  13.734   6.671  1.00126.89           C  
ANISOU 1060  CZ2 TRP A 161    14907  17821  15483   1857     36    302       C  
ATOM   1061  CZ3 TRP A 161      16.995  15.611   8.094  1.00128.56           C  
ANISOU 1061  CZ3 TRP A 161    15106  17668  16071   1839      8     89       C  
ATOM   1062  CH2 TRP A 161      17.949  14.775   7.496  1.00128.08           C  
ANISOU 1062  CH2 TRP A 161    15060  17731  15874   1728    105    253       C  
ATOM   1063  N   ILE A 162       9.970  15.179   8.296  1.00126.42           N  
ANISOU 1063  N   ILE A 162    14337  18285  15411   2930   -859   -963       N  
ATOM   1064  CA  ILE A 162       9.053  16.010   9.087  1.00127.24           C  
ANISOU 1064  CA  ILE A 162    14315  18368  15661   3053   -959  -1250       C  
ATOM   1065  C   ILE A 162       8.153  15.207  10.059  1.00128.13           C  
ANISOU 1065  C   ILE A 162    14118  18862  15703   2905  -1024  -1628       C  
ATOM   1066  O   ILE A 162       8.143  15.566  11.239  1.00127.53           O  
ANISOU 1066  O   ILE A 162    13904  18775  15775   2745   -995  -1840       O  
ATOM   1067  CB  ILE A 162       8.332  17.115   8.247  1.00133.90           C  
ANISOU 1067  CB  ILE A 162    15312  19033  16531   3491  -1091  -1183       C  
ATOM   1068  CG1 ILE A 162       9.355  18.184   7.784  1.00136.01           C  
ANISOU 1068  CG1 ILE A 162    15889  18823  16965   3529   -976   -836       C  
ATOM   1069  CG2 ILE A 162       7.181  17.782   9.022  1.00136.68           C  
ANISOU 1069  CG2 ILE A 162    15478  19449  17005   3664  -1230  -1555       C  
ATOM   1070  CD1 ILE A 162       9.084  18.844   6.423  1.00144.80           C  
ANISOU 1070  CD1 ILE A 162    17270  19766  17981   3923  -1055   -545       C  
ATOM   1071  N   PRO A 163       7.467  14.097   9.657  1.00122.55           N  
ANISOU 1071  N   PRO A 163    13289  18499  14775   2910  -1089  -1727       N  
ATOM   1072  CA  PRO A 163       6.659  13.350  10.638  1.00121.12           C  
ANISOU 1072  CA  PRO A 163    12824  18661  14536   2712  -1116  -2072       C  
ATOM   1073  C   PRO A 163       7.477  12.886  11.844  1.00122.81           C  
ANISOU 1073  C   PRO A 163    12970  18870  14821   2313   -980  -2081       C  
ATOM   1074  O   PRO A 163       7.055  13.126  12.973  1.00122.77           O  
ANISOU 1074  O   PRO A 163    12781  18984  14882   2190   -983  -2342       O  
ATOM   1075  CB  PRO A 163       6.101  12.177   9.825  1.00122.24           C  
ANISOU 1075  CB  PRO A 163    12907  19091  14447   2736  -1166  -2100       C  
ATOM   1076  CG  PRO A 163       6.109  12.660   8.427  1.00128.33           C  
ANISOU 1076  CG  PRO A 163    13871  19744  15144   3090  -1240  -1884       C  
ATOM   1077  CD  PRO A 163       7.353  13.483   8.319  1.00123.97           C  
ANISOU 1077  CD  PRO A 163    13568  18788  14746   3079  -1133  -1558       C  
ATOM   1078  N   ALA A 164       8.679  12.315  11.601  1.00117.59           N  
ANISOU 1078  N   ALA A 164    12455  18079  14145   2138   -867  -1800       N  
ATOM   1079  CA  ALA A 164       9.599  11.856  12.648  1.00115.64           C  
ANISOU 1079  CA  ALA A 164    12164  17825  13948   1799   -751  -1765       C  
ATOM   1080  C   ALA A 164      10.139  13.030  13.478  1.00120.09           C  
ANISOU 1080  C   ALA A 164    12728  18182  14721   1753   -703  -1809       C  
ATOM   1081  O   ALA A 164      10.352  12.872  14.680  1.00119.22           O  
ANISOU 1081  O   ALA A 164    12477  18185  14638   1511   -658  -1947       O  
ATOM   1082  CB  ALA A 164      10.746  11.071  12.033  1.00114.81           C  
ANISOU 1082  CB  ALA A 164    12212  17625  13786   1697   -663  -1470       C  
ATOM   1083  N   LEU A 165      10.308  14.213  12.844  1.00117.87           N  
ANISOU 1083  N   LEU A 165    12603  17603  14580   1984   -714  -1703       N  
ATOM   1084  CA  LEU A 165      10.765  15.444  13.496  1.00118.67           C  
ANISOU 1084  CA  LEU A 165    12723  17448  14918   1963   -667  -1765       C  
ATOM   1085  C   LEU A 165       9.651  16.031  14.379  1.00123.12           C  
ANISOU 1085  C   LEU A 165    13081  18145  15554   2038   -761  -2145       C  
ATOM   1086  O   LEU A 165       9.933  16.841  15.264  1.00123.60           O  
ANISOU 1086  O   LEU A 165    13076  18089  15799   1951   -722  -2303       O  
ATOM   1087  CB  LEU A 165      11.217  16.470  12.446  1.00120.65           C  
ANISOU 1087  CB  LEU A 165    13238  17308  15296   2187   -642  -1509       C  
ATOM   1088  CG  LEU A 165      12.334  17.413  12.870  1.00126.22           C  
ANISOU 1088  CG  LEU A 165    14036  17680  16243   2041   -512  -1432       C  
ATOM   1089  CD1 LEU A 165      13.696  16.878  12.439  1.00124.91           C  
ANISOU 1089  CD1 LEU A 165    13985  17448  16028   1840   -368  -1137       C  
ATOM   1090  CD2 LEU A 165      12.117  18.800  12.287  1.00131.99           C  
ANISOU 1090  CD2 LEU A 165    14964  18019  17168   2308   -535  -1358       C  
ATOM   1091  N   LEU A 166       8.387  15.632  14.125  1.00119.33           N  
ANISOU 1091  N   LEU A 166    12479  17930  14930   2199   -883  -2324       N  
ATOM   1092  CA  LEU A 166       7.226  16.053  14.912  1.00120.43           C  
ANISOU 1092  CA  LEU A 166    12380  18278  15101   2276   -977  -2725       C  
ATOM   1093  C   LEU A 166       6.838  14.965  15.924  1.00122.31           C  
ANISOU 1093  C   LEU A 166    12366  18938  15169   1963   -944  -2939       C  
ATOM   1094  O   LEU A 166       6.226  15.269  16.947  1.00123.02           O  
ANISOU 1094  O   LEU A 166    12229  19227  15284   1892   -963  -3273       O  
ATOM   1095  CB  LEU A 166       6.028  16.461  14.027  1.00122.70           C  
ANISOU 1095  CB  LEU A 166    12666  18608  15349   2677  -1139  -2830       C  
ATOM   1096  CG  LEU A 166       6.223  17.644  13.055  1.00129.65           C  
ANISOU 1096  CG  LEU A 166    13810  19066  16385   3037  -1194  -2618       C  
ATOM   1097  CD1 LEU A 166       4.974  17.885  12.240  1.00132.11           C  
ANISOU 1097  CD1 LEU A 166    14089  19503  16605   3451  -1379  -2734       C  
ATOM   1098  CD2 LEU A 166       6.620  18.927  13.780  1.00133.78           C  
ANISOU 1098  CD2 LEU A 166    14369  19255  17205   3047  -1156  -2719       C  
ATOM   1099  N   LEU A 167       7.236  13.701  15.656  1.00116.17           N  
ANISOU 1099  N   LEU A 167    11636  18284  14218   1768   -885  -2741       N  
ATOM   1100  CA  LEU A 167       7.016  12.550  16.542  1.00114.43           C  
ANISOU 1100  CA  LEU A 167    11243  18404  13833   1444   -834  -2855       C  
ATOM   1101  C   LEU A 167       8.003  12.622  17.714  1.00117.48           C  
ANISOU 1101  C   LEU A 167    11598  18763  14276   1166   -732  -2824       C  
ATOM   1102  O   LEU A 167       7.902  11.853  18.673  1.00116.40           O  
ANISOU 1102  O   LEU A 167    11322  18897  14007    891   -685  -2913       O  
ATOM   1103  CB  LEU A 167       7.246  11.236  15.770  1.00112.63           C  
ANISOU 1103  CB  LEU A 167    11123  18225  13445   1359   -807  -2624       C  
ATOM   1104  CG  LEU A 167       6.038  10.617  15.084  1.00117.55           C  
ANISOU 1104  CG  LEU A 167    11653  19087  13922   1469   -888  -2775       C  
ATOM   1105  CD1 LEU A 167       6.456   9.872  13.835  1.00116.40           C  
ANISOU 1105  CD1 LEU A 167    11692  18836  13699   1548   -887  -2512       C  
ATOM   1106  CD2 LEU A 167       5.303   9.672  16.023  1.00119.61           C  
ANISOU 1106  CD2 LEU A 167    11699  19706  14043   1168   -849  -3002       C  
ATOM   1107  N   THR A 168       8.968  13.545  17.607  1.00114.47           N  
ANISOU 1107  N   THR A 168    11352  18060  14083   1234   -695  -2691       N  
ATOM   1108  CA  THR A 168      10.030  13.802  18.565  1.00114.09           C  
ANISOU 1108  CA  THR A 168    11278  17956  14117   1013   -606  -2670       C  
ATOM   1109  C   THR A 168       9.582  14.761  19.695  1.00120.50           C  
ANISOU 1109  C   THR A 168    11882  18868  15036    985   -621  -3036       C  
ATOM   1110  O   THR A 168      10.275  14.876  20.708  1.00119.61           O  
ANISOU 1110  O   THR A 168    11676  18826  14943    771   -557  -3103       O  
ATOM   1111  CB  THR A 168      11.292  14.195  17.782  1.00122.08           C  
ANISOU 1111  CB  THR A 168    12522  18598  15265   1069   -541  -2360       C  
ATOM   1112  OG1 THR A 168      12.402  13.431  18.246  1.00120.98           O  
ANISOU 1112  OG1 THR A 168    12391  18522  15054    821   -459  -2195       O  
ATOM   1113  CG2 THR A 168      11.584  15.694  17.798  1.00122.58           C  
ANISOU 1113  CG2 THR A 168    12639  18344  15592   1195   -525  -2440       C  
ATOM   1114  N   ILE A 169       8.415  15.438  19.507  1.00120.10           N  
ANISOU 1114  N   ILE A 169    11741  18845  15045   1220   -716  -3294       N  
ATOM   1115  CA  ILE A 169       7.781  16.371  20.460  1.00122.39           C  
ANISOU 1115  CA  ILE A 169    11812  19246  15445   1253   -751  -3702       C  
ATOM   1116  C   ILE A 169       7.499  15.715  21.846  1.00127.23           C  
ANISOU 1116  C   ILE A 169    12155  20325  15863    937   -705  -3941       C  
ATOM   1117  O   ILE A 169       7.936  16.295  22.844  1.00127.67           O  
ANISOU 1117  O   ILE A 169    12090  20420  15998    808   -662  -4123       O  
ATOM   1118  CB  ILE A 169       6.580  17.169  19.839  1.00127.62           C  
ANISOU 1118  CB  ILE A 169    12442  19840  16207   1626   -882  -3917       C  
ATOM   1119  CG1 ILE A 169       7.059  18.057  18.655  1.00128.85           C  
ANISOU 1119  CG1 ILE A 169    12897  19484  16578   1925   -911  -3655       C  
ATOM   1120  CG2 ILE A 169       5.850  18.020  20.901  1.00130.63           C  
ANISOU 1120  CG2 ILE A 169    12553  20391  16688   1658   -923  -4397       C  
ATOM   1121  CD1 ILE A 169       5.965  18.522  17.643  1.00137.12           C  
ANISOU 1121  CD1 ILE A 169    13997  20456  17648   2347  -1063  -3709       C  
ATOM   1122  N   PRO A 170       6.884  14.496  21.957  1.00123.74           N  
ANISOU 1122  N   PRO A 170    11626  20230  15161    781   -699  -3925       N  
ATOM   1123  CA  PRO A 170       6.707  13.885  23.294  1.00124.13           C  
ANISOU 1123  CA  PRO A 170    11454  20705  15006    455   -635  -4096       C  
ATOM   1124  C   PRO A 170       8.018  13.633  24.051  1.00128.48           C  
ANISOU 1124  C   PRO A 170    12057  21237  15522    209   -550  -3906       C  
ATOM   1125  O   PRO A 170       7.994  13.479  25.265  1.00128.66           O  
ANISOU 1125  O   PRO A 170    11892  21588  15404    -20   -507  -4076       O  
ATOM   1126  CB  PRO A 170       5.976  12.570  22.996  1.00124.91           C  
ANISOU 1126  CB  PRO A 170    11537  21056  14866    333   -627  -4013       C  
ATOM   1127  CG  PRO A 170       6.238  12.293  21.561  1.00127.77           C  
ANISOU 1127  CG  PRO A 170    12148  21101  15296    537   -667  -3712       C  
ATOM   1128  CD  PRO A 170       6.293  13.636  20.911  1.00124.38           C  
ANISOU 1128  CD  PRO A 170    11798  20345  15117    875   -741  -3771       C  
ATOM   1129  N   ASP A 171       9.155  13.610  23.340  1.00124.93           N  
ANISOU 1129  N   ASP A 171    11845  20437  15184    263   -528  -3571       N  
ATOM   1130  CA  ASP A 171      10.475  13.422  23.939  1.00124.48           C  
ANISOU 1130  CA  ASP A 171    11830  20356  15112     72   -461  -3400       C  
ATOM   1131  C   ASP A 171      11.159  14.772  24.191  1.00130.20           C  
ANISOU 1131  C   ASP A 171    12529  20849  16093    141   -445  -3550       C  
ATOM   1132  O   ASP A 171      12.213  14.812  24.827  1.00129.59           O  
ANISOU 1132  O   ASP A 171    12423  20797  16017    -19   -394  -3503       O  
ATOM   1133  CB  ASP A 171      11.346  12.493  23.073  1.00124.55           C  
ANISOU 1133  CB  ASP A 171    12077  20170  15075     63   -437  -2978       C  
ATOM   1134  CG  ASP A 171      10.696  11.158  22.759  1.00136.99           C  
ANISOU 1134  CG  ASP A 171    13696  21917  16437     -8   -447  -2843       C  
ATOM   1135  OD1 ASP A 171      10.428  10.389  23.707  1.00138.13           O  
ANISOU 1135  OD1 ASP A 171    13728  22381  16373   -236   -421  -2887       O  
ATOM   1136  OD2 ASP A 171      10.430  10.895  21.569  1.00143.76           O  
ANISOU 1136  OD2 ASP A 171    14699  22594  17331    158   -477  -2703       O  
ATOM   1137  N   PHE A 172      10.555  15.876  23.707  1.00129.12           N  
ANISOU 1137  N   PHE A 172    12398  20483  16178    382   -492  -3742       N  
ATOM   1138  CA  PHE A 172      11.087  17.224  23.911  1.00131.14           C  
ANISOU 1138  CA  PHE A 172    12646  20460  16720    450   -471  -3911       C  
ATOM   1139  C   PHE A 172      10.770  17.747  25.317  1.00137.07           C  
ANISOU 1139  C   PHE A 172    13100  21521  17459    317   -468  -4349       C  
ATOM   1140  O   PHE A 172      11.538  18.553  25.845  1.00137.99           O  
ANISOU 1140  O   PHE A 172    13164  21517  17751    244   -423  -4490       O  
ATOM   1141  CB  PHE A 172      10.564  18.206  22.845  1.00134.62           C  
ANISOU 1141  CB  PHE A 172    13241  20497  17411    782   -529  -3923       C  
ATOM   1142  CG  PHE A 172      11.614  18.736  21.896  1.00136.42           C  
ANISOU 1142  CG  PHE A 172    13742  20238  17851    862   -471  -3617       C  
ATOM   1143  CD1 PHE A 172      11.593  18.393  20.549  1.00138.82           C  
ANISOU 1143  CD1 PHE A 172    14292  20327  18126   1040   -490  -3274       C  
ATOM   1144  CD2 PHE A 172      12.615  19.591  22.345  1.00140.00           C  
ANISOU 1144  CD2 PHE A 172    14195  20472  18527    744   -387  -3691       C  
ATOM   1145  CE1 PHE A 172      12.570  18.879  19.670  1.00140.08           C  
ANISOU 1145  CE1 PHE A 172    14701  20068  18454   1090   -416  -2982       C  
ATOM   1146  CE2 PHE A 172      13.590  20.076  21.467  1.00143.22           C  
ANISOU 1146  CE2 PHE A 172    14849  20442  19126    778   -307  -3410       C  
ATOM   1147  CZ  PHE A 172      13.560  19.718  20.136  1.00140.40           C  
ANISOU 1147  CZ  PHE A 172    14743  19885  18718    948   -319  -3047       C  
ATOM   1148  N   ILE A 173       9.648  17.289  25.919  1.00133.98           N  
ANISOU 1148  N   ILE A 173    12501  21548  16857    269   -507  -4583       N  
ATOM   1149  CA  ILE A 173       9.218  17.722  27.250  1.00135.85           C  
ANISOU 1149  CA  ILE A 173    12427  22155  17035    142   -502  -5025       C  
ATOM   1150  C   ILE A 173       9.193  16.611  28.323  1.00138.67           C  
ANISOU 1150  C   ILE A 173    12618  23055  17017   -173   -455  -5014       C  
ATOM   1151  O   ILE A 173       9.516  16.894  29.478  1.00139.82           O  
ANISOU 1151  O   ILE A 173    12560  23476  17090   -345   -422  -5251       O  
ATOM   1152  CB  ILE A 173       7.931  18.603  27.173  1.00141.59           C  
ANISOU 1152  CB  ILE A 173    13007  22886  17906    389   -582  -5432       C  
ATOM   1153  CG1 ILE A 173       7.992  19.902  28.042  1.00145.15           C  
ANISOU 1153  CG1 ILE A 173    13257  23311  18584    418   -582  -5894       C  
ATOM   1154  CG2 ILE A 173       6.597  17.826  27.228  1.00142.20           C  
ANISOU 1154  CG2 ILE A 173    12928  23377  17725    383   -621  -5558       C  
ATOM   1155  CD1 ILE A 173       7.939  19.787  29.612  1.00153.55           C  
ANISOU 1155  CD1 ILE A 173    13980  24931  19429    138   -535  -6255       C  
ATOM   1156  N   PHE A 174       8.843  15.360  27.948  1.00132.87           N  
ANISOU 1156  N   PHE A 174    11977  22465  16043   -252   -450  -4736       N  
ATOM   1157  CA  PHE A 174       8.798  14.242  28.901  1.00132.15           C  
ANISOU 1157  CA  PHE A 174    11781  22836  15595   -554   -397  -4663       C  
ATOM   1158  C   PHE A 174      10.182  13.707  29.314  1.00133.89           C  
ANISOU 1158  C   PHE A 174    12106  23052  15716   -725   -358  -4359       C  
ATOM   1159  O   PHE A 174      10.283  13.007  30.325  1.00134.24           O  
ANISOU 1159  O   PHE A 174    12045  23491  15470   -962   -323  -4331       O  
ATOM   1160  CB  PHE A 174       7.868  13.120  28.419  1.00133.24           C  
ANISOU 1160  CB  PHE A 174    11973  23116  15536   -602   -395  -4516       C  
ATOM   1161  CG  PHE A 174       6.393  13.444  28.475  1.00136.79           C  
ANISOU 1161  CG  PHE A 174    12206  23807  15963   -527   -422  -4902       C  
ATOM   1162  CD1 PHE A 174       5.760  14.070  27.408  1.00140.25           C  
ANISOU 1162  CD1 PHE A 174    12694  23970  16625   -212   -503  -5004       C  
ATOM   1163  CD2 PHE A 174       5.632  13.105  29.587  1.00140.85           C  
ANISOU 1163  CD2 PHE A 174    12457  24849  16210   -767   -368  -5163       C  
ATOM   1164  CE1 PHE A 174       4.392  14.357  27.454  1.00143.15           C  
ANISOU 1164  CE1 PHE A 174    12833  24591  16966   -114   -545  -5387       C  
ATOM   1165  CE2 PHE A 174       4.264  13.392  29.632  1.00145.61           C  
ANISOU 1165  CE2 PHE A 174    12825  25713  16787   -701   -389  -5554       C  
ATOM   1166  CZ  PHE A 174       3.653  14.016  28.565  1.00143.89           C  
ANISOU 1166  CZ  PHE A 174    12642  25221  16808   -364   -485  -5676       C  
ATOM   1167  N   ALA A 175      11.243  14.058  28.555  1.00128.11           N  
ANISOU 1167  N   ALA A 175    11568  21897  15211   -601   -363  -4139       N  
ATOM   1168  CA  ALA A 175      12.623  13.672  28.854  1.00126.56           C  
ANISOU 1168  CA  ALA A 175    11446  21683  14957   -721   -336  -3890       C  
ATOM   1169  C   ALA A 175      13.288  14.786  29.654  1.00130.74           C  
ANISOU 1169  C   ALA A 175    11797  22254  15626   -763   -320  -4192       C  
ATOM   1170  O   ALA A 175      13.415  15.911  29.160  1.00131.20           O  
ANISOU 1170  O   ALA A 175    11879  21967  16002   -614   -318  -4350       O  
ATOM   1171  CB  ALA A 175      13.395  13.410  27.569  1.00125.31           C  
ANISOU 1171  CB  ALA A 175    11567  21088  14957   -585   -335  -3519       C  
ATOM   1172  N   ASN A 176      13.674  14.487  30.904  1.00127.13           N  
ANISOU 1172  N   ASN A 176    11157  22223  14924   -966   -310  -4284       N  
ATOM   1173  CA  ASN A 176      14.301  15.459  31.800  1.00128.37           C  
ANISOU 1173  CA  ASN A 176    11097  22508  15168  -1036   -297  -4619       C  
ATOM   1174  C   ASN A 176      15.420  14.846  32.644  1.00130.75           C  
ANISOU 1174  C   ASN A 176    11334  23119  15225  -1206   -298  -4473       C  
ATOM   1175  O   ASN A 176      15.537  13.621  32.740  1.00128.67           O  
ANISOU 1175  O   ASN A 176    11178  23031  14681  -1279   -314  -4133       O  
ATOM   1176  CB  ASN A 176      13.245  16.128  32.702  1.00132.01           C  
ANISOU 1176  CB  ASN A 176    11276  23301  15581  -1076   -299  -5109       C  
ATOM   1177  CG  ASN A 176      12.261  17.022  31.980  1.00157.94           C  
ANISOU 1177  CG  ASN A 176    14576  26274  19161   -861   -318  -5348       C  
ATOM   1178  OD1 ASN A 176      12.632  17.947  31.246  1.00154.20           O  
ANISOU 1178  OD1 ASN A 176    14215  25326  19048   -698   -318  -5385       O  
ATOM   1179  ND2 ASN A 176      10.976  16.784  32.197  1.00150.40           N  
ANISOU 1179  ND2 ASN A 176    13501  25591  18054   -856   -334  -5524       N  
ATOM   1180  N   VAL A 177      16.238  15.716  33.262  1.00128.50           N  
ANISOU 1180  N   VAL A 177    10871  22898  15055  -1260   -287  -4747       N  
ATOM   1181  CA  VAL A 177      17.356  15.347  34.135  1.00128.87           C  
ANISOU 1181  CA  VAL A 177    10800  23282  14884  -1395   -304  -4697       C  
ATOM   1182  C   VAL A 177      16.908  15.122  35.588  1.00133.93           C  
ANISOU 1182  C   VAL A 177    11174  24564  15148  -1559   -323  -4934       C  
ATOM   1183  O   VAL A 177      16.286  16.005  36.190  1.00135.23           O  
ANISOU 1183  O   VAL A 177    11108  24902  15373  -1593   -306  -5391       O  
ATOM   1184  CB  VAL A 177      18.566  16.321  34.038  1.00133.79           C  
ANISOU 1184  CB  VAL A 177    11348  23684  15802  -1394   -275  -4874       C  
ATOM   1185  CG1 VAL A 177      19.416  16.012  32.817  1.00131.50           C  
ANISOU 1185  CG1 VAL A 177    11323  22941  15699  -1296   -255  -4486       C  
ATOM   1186  CG2 VAL A 177      18.130  17.789  34.047  1.00135.47           C  
ANISOU 1186  CG2 VAL A 177    11429  23674  16368  -1358   -233  -5348       C  
ATOM   1187  N   SER A 178      17.214  13.929  36.138  1.00129.74           N  
ANISOU 1187  N   SER A 178    10684  24386  14225  -1653   -359  -4617       N  
ATOM   1188  CA  SER A 178      16.891  13.565  37.519  1.00131.55           C  
ANISOU 1188  CA  SER A 178    10696  25259  14027  -1821   -373  -4750       C  
ATOM   1189  C   SER A 178      18.129  13.712  38.388  1.00136.80           C  
ANISOU 1189  C   SER A 178    11181  26252  14546  -1878   -421  -4837       C  
ATOM   1190  O   SER A 178      19.218  13.295  37.992  1.00135.29           O  
ANISOU 1190  O   SER A 178    11119  25894  14392  -1810   -461  -4548       O  
ATOM   1191  CB  SER A 178      16.353  12.137  37.602  1.00134.03           C  
ANISOU 1191  CB  SER A 178    11195  25749  13981  -1895   -378  -4322       C  
ATOM   1192  OG  SER A 178      16.285  11.679  38.945  1.00143.82           O  
ANISOU 1192  OG  SER A 178    12266  27616  14764  -2065   -390  -4353       O  
ATOM   1193  N   GLU A 179      17.957  14.307  39.570  1.00136.02           N  
ANISOU 1193  N   GLU A 179    10762  26650  14272  -1995   -420  -5265       N  
ATOM   1194  CA  GLU A 179      19.042  14.518  40.524  1.00137.97           C  
ANISOU 1194  CA  GLU A 179    10775  27307  14339  -2056   -472  -5432       C  
ATOM   1195  C   GLU A 179      18.789  13.651  41.771  1.00144.26           C  
ANISOU 1195  C   GLU A 179    11465  28800  14548  -2189   -511  -5318       C  
ATOM   1196  O   GLU A 179      18.930  14.117  42.906  1.00146.64           O  
ANISOU 1196  O   GLU A 179    11451  29642  14623  -2289   -528  -5688       O  
ATOM   1197  CB  GLU A 179      19.192  16.021  40.848  1.00141.29           C  
ANISOU 1197  CB  GLU A 179    10896  27723  15066  -2082   -437  -6064       C  
ATOM   1198  CG  GLU A 179      19.439  16.881  39.613  1.00149.45           C  
ANISOU 1198  CG  GLU A 179    12074  28035  16674  -1964   -386  -6129       C  
ATOM   1199  CD  GLU A 179      19.919  18.311  39.801  1.00171.52           C  
ANISOU 1199  CD  GLU A 179    14634  30701  19835  -1994   -346  -6678       C  
ATOM   1200  OE1 GLU A 179      19.951  18.800  40.954  1.00170.67           O  
ANISOU 1200  OE1 GLU A 179    14191  31090  19564  -2106   -359  -7126       O  
ATOM   1201  OE2 GLU A 179      20.258  18.949  38.778  1.00160.29           O  
ANISOU 1201  OE2 GLU A 179    13367  28671  18865  -1914   -295  -6661       O  
ATOM   1202  N   ALA A 180      18.413  12.368  41.525  1.00139.97           N  
ANISOU 1202  N   ALA A 180    11199  28228  13756  -2195   -519  -4795       N  
ATOM   1203  CA  ALA A 180      18.073  11.334  42.514  1.00141.90           C  
ANISOU 1203  CA  ALA A 180    11452  29020  13443  -2327   -537  -4540       C  
ATOM   1204  C   ALA A 180      19.080  11.062  43.648  1.00148.17           C  
ANISOU 1204  C   ALA A 180    12083  30381  13832  -2351   -634  -4502       C  
ATOM   1205  O   ALA A 180      18.724  11.216  44.818  1.00150.87           O  
ANISOU 1205  O   ALA A 180    12178  31342  13804  -2491   -626  -4746       O  
ATOM   1206  CB  ALA A 180      17.819  10.000  41.815  1.00140.66           C  
ANISOU 1206  CB  ALA A 180    11683  28558  13204  -2299   -535  -3933       C  
ATOM   1207  N   ASP A 181      20.332  10.686  43.299  1.00143.33           N  
ANISOU 1207  N   ASP A 181    11586  29590  13281  -2203   -729  -4225       N  
ATOM   1208  CA  ASP A 181      21.436  10.459  44.238  1.00145.43           C  
ANISOU 1208  CA  ASP A 181    11691  30360  13204  -2168   -849  -4193       C  
ATOM   1209  C   ASP A 181      22.433  11.459  43.649  1.00147.34           C  
ANISOU 1209  C   ASP A 181    11789  30292  13902  -2066   -864  -4515       C  
ATOM   1210  O   ASP A 181      22.104  12.173  42.699  1.00144.42           O  
ANISOU 1210  O   ASP A 181    11476  29392  14005  -2048   -776  -4692       O  
ATOM   1211  CB  ASP A 181      22.136   9.100  43.992  1.00146.70           C  
ANISOU 1211  CB  ASP A 181    12164  30413  13162  -2030   -953  -3551       C  
ATOM   1212  CG  ASP A 181      21.364   7.869  44.408  1.00157.78           C  
ANISOU 1212  CG  ASP A 181    13813  31993  14144  -2117   -942  -3084       C  
ATOM   1213  OD1 ASP A 181      21.057   7.039  43.526  1.00156.30           O  
ANISOU 1213  OD1 ASP A 181    13972  31321  14093  -2069   -915  -2667       O  
ATOM   1214  OD2 ASP A 181      21.142   7.689  45.626  1.00166.47           O  
ANISOU 1214  OD2 ASP A 181    14765  33726  14761  -2235   -962  -3120       O  
ATOM   1215  N   ASP A 182      23.664  11.490  44.187  1.00145.48           N  
ANISOU 1215  N   ASP A 182    11372  30384  13518  -1998   -973  -4576       N  
ATOM   1216  CA  ASP A 182      24.760  12.279  43.639  1.00144.35           C  
ANISOU 1216  CA  ASP A 182    11098  29977  13773  -1924   -982  -4832       C  
ATOM   1217  C   ASP A 182      25.022  11.951  42.159  1.00143.41           C  
ANISOU 1217  C   ASP A 182    11309  29125  14055  -1794   -946  -4480       C  
ATOM   1218  O   ASP A 182      25.662  12.727  41.445  1.00141.81           O  
ANISOU 1218  O   ASP A 182    11049  28562  14272  -1769   -898  -4691       O  
ATOM   1219  CB  ASP A 182      26.022  12.126  44.505  1.00149.24           C  
ANISOU 1219  CB  ASP A 182    11470  31150  14085  -1861  -1123  -4901       C  
ATOM   1220  CG  ASP A 182      25.865  12.607  45.941  1.00163.47           C  
ANISOU 1220  CG  ASP A 182    12897  33711  15505  -1988  -1157  -5330       C  
ATOM   1221  OD1 ASP A 182      26.560  12.070  46.824  1.00167.25           O  
ANISOU 1221  OD1 ASP A 182    13247  34767  15534  -1922  -1297  -5223       O  
ATOM   1222  OD2 ASP A 182      25.084  13.557  46.172  1.00169.50           O  
ANISOU 1222  OD2 ASP A 182    13479  34501  16424  -2137  -1051  -5797       O  
ATOM   1223  N   ARG A 183      24.481  10.794  41.713  1.00137.50           N  
ANISOU 1223  N   ARG A 183    10907  28169  13169  -1731   -958  -3950       N  
ATOM   1224  CA  ARG A 183      24.505  10.300  40.346  1.00133.77           C  
ANISOU 1224  CA  ARG A 183    10770  27051  13006  -1612   -925  -3584       C  
ATOM   1225  C   ARG A 183      23.199  10.743  39.668  1.00134.99           C  
ANISOU 1225  C   ARG A 183    11048  26815  13428  -1690   -795  -3686       C  
ATOM   1226  O   ARG A 183      22.101  10.417  40.138  1.00135.21           O  
ANISOU 1226  O   ARG A 183    11109  27040  13224  -1793   -763  -3651       O  
ATOM   1227  CB  ARG A 183      24.654   8.765  40.309  1.00133.93           C  
ANISOU 1227  CB  ARG A 183    11082  27086  12721  -1498  -1020  -2988       C  
ATOM   1228  CG  ARG A 183      24.984   8.225  38.918  1.00140.08           C  
ANISOU 1228  CG  ARG A 183    12162  27250  13813  -1346  -1008  -2648       C  
ATOM   1229  CD  ARG A 183      24.742   6.735  38.791  1.00147.70           C  
ANISOU 1229  CD  ARG A 183    13457  28124  14538  -1264  -1069  -2092       C  
ATOM   1230  NE  ARG A 183      25.075   6.255  37.446  1.00152.41           N  
ANISOU 1230  NE  ARG A 183    14313  28153  15444  -1114  -1058  -1823       N  
ATOM   1231  CZ  ARG A 183      25.110   4.976  37.088  1.00165.28           C  
ANISOU 1231  CZ  ARG A 183    16240  29588  16970  -1001  -1116  -1360       C  
ATOM   1232  NH1 ARG A 183      25.429   4.639  35.847  1.00150.23           N  
ANISOU 1232  NH1 ARG A 183    14529  27192  15359   -865  -1100  -1185       N  
ATOM   1233  NH2 ARG A 183      24.836   4.023  37.970  1.00153.20           N  
ANISOU 1233  NH2 ARG A 183    14820  28347  15040  -1025  -1186  -1069       N  
ATOM   1234  N   TYR A 184      23.339  11.507  38.579  1.00128.61           N  
ANISOU 1234  N   TYR A 184    10293  25479  13095  -1640   -719  -3822       N  
ATOM   1235  CA  TYR A 184      22.238  12.058  37.802  1.00126.05           C  
ANISOU 1235  CA  TYR A 184    10079  24742  13073  -1660   -614  -3937       C  
ATOM   1236  C   TYR A 184      21.845  11.108  36.684  1.00126.19           C  
ANISOU 1236  C   TYR A 184    10457  24327  13163  -1558   -603  -3471       C  
ATOM   1237  O   TYR A 184      22.715  10.598  35.972  1.00124.55           O  
ANISOU 1237  O   TYR A 184    10406  23869  13049  -1441   -636  -3183       O  
ATOM   1238  CB  TYR A 184      22.602  13.458  37.262  1.00127.08           C  
ANISOU 1238  CB  TYR A 184    10084  24533  13667  -1656   -539  -4331       C  
ATOM   1239  CG  TYR A 184      22.709  14.560  38.306  1.00131.91           C  
ANISOU 1239  CG  TYR A 184    10331  25507  14281  -1779   -526  -4891       C  
ATOM   1240  CD1 TYR A 184      22.899  15.886  37.931  1.00134.51           C  
ANISOU 1240  CD1 TYR A 184    10549  25513  15044  -1803   -445  -5289       C  
ATOM   1241  CD2 TYR A 184      22.629  14.274  39.669  1.00135.29           C  
ANISOU 1241  CD2 TYR A 184    10531  26600  14275  -1873   -591  -5027       C  
ATOM   1242  CE1 TYR A 184      23.016  16.900  38.883  1.00138.54           C  
ANISOU 1242  CE1 TYR A 184    10718  26333  15587  -1921   -430  -5842       C  
ATOM   1243  CE2 TYR A 184      22.744  15.279  40.629  1.00139.18           C  
ANISOU 1243  CE2 TYR A 184    10664  27458  14759  -1984   -581  -5580       C  
ATOM   1244  CZ  TYR A 184      22.931  16.592  40.232  1.00147.25           C  
ANISOU 1244  CZ  TYR A 184    11569  28131  16249  -2009   -501  -6005       C  
ATOM   1245  OH  TYR A 184      23.020  17.585  41.177  1.00151.61           O  
ANISOU 1245  OH  TYR A 184    11763  29022  16820  -2124   -487  -6588       O  
ATOM   1246  N   ILE A 185      20.524  10.855  36.551  1.00121.29           N  
ANISOU 1246  N   ILE A 185     9943  23653  12490  -1608   -556  -3429       N  
ATOM   1247  CA  ILE A 185      19.925   9.953  35.561  1.00118.29           C  
ANISOU 1247  CA  ILE A 185     9876  22910  12157  -1542   -538  -3048       C  
ATOM   1248  C   ILE A 185      19.106  10.744  34.522  1.00119.28           C  
ANISOU 1248  C   ILE A 185    10067  22601  12654  -1484   -461  -3224       C  
ATOM   1249  O   ILE A 185      18.066  11.312  34.862  1.00119.49           O  
ANISOU 1249  O   ILE A 185     9964  22753  12684  -1553   -421  -3521       O  
ATOM   1250  CB  ILE A 185      19.094   8.817  36.259  1.00122.31           C  
ANISOU 1250  CB  ILE A 185    10470  23742  12258  -1662   -547  -2808       C  
ATOM   1251  CG1 ILE A 185      19.828   8.165  37.476  1.00125.28           C  
ANISOU 1251  CG1 ILE A 185    10765  24618  12217  -1714   -631  -2656       C  
ATOM   1252  CG2 ILE A 185      18.565   7.769  35.267  1.00120.83           C  
ANISOU 1252  CG2 ILE A 185    10605  23184  12119  -1614   -528  -2417       C  
ATOM   1253  CD1 ILE A 185      21.234   7.470  37.222  1.00131.46           C  
ANISOU 1253  CD1 ILE A 185    11675  25294  12981  -1553   -734  -2319       C  
ATOM   1254  N   CYS A 186      19.588  10.785  33.262  1.00112.98           N  
ANISOU 1254  N   CYS A 186     9460  21315  12152  -1343   -447  -3046       N  
ATOM   1255  CA  CYS A 186      18.899  11.468  32.165  1.00111.05           C  
ANISOU 1255  CA  CYS A 186     9316  20638  12239  -1250   -389  -3143       C  
ATOM   1256  C   CYS A 186      18.094  10.461  31.346  1.00111.51           C  
ANISOU 1256  C   CYS A 186     9623  20506  12242  -1196   -388  -2830       C  
ATOM   1257  O   CYS A 186      18.676   9.592  30.690  1.00109.30           O  
ANISOU 1257  O   CYS A 186     9541  20037  11950  -1123   -410  -2482       O  
ATOM   1258  CB  CYS A 186      19.870  12.275  31.298  1.00110.92           C  
ANISOU 1258  CB  CYS A 186     9343  20230  12572  -1150   -355  -3175       C  
ATOM   1259  SG  CYS A 186      19.298  12.586  29.599  1.00112.77           S  
ANISOU 1259  SG  CYS A 186     9837  19871  13138   -978   -304  -3040       S  
ATOM   1260  N   ASP A 187      16.748  10.557  31.437  1.00107.51           N  
ANISOU 1260  N   ASP A 187     9077  20081  11690  -1239   -364  -2987       N  
ATOM   1261  CA  ASP A 187      15.768   9.754  30.698  1.00105.51           C  
ANISOU 1261  CA  ASP A 187     9004  19685  11399  -1213   -352  -2795       C  
ATOM   1262  C   ASP A 187      14.355  10.323  30.733  1.00109.18           C  
ANISOU 1262  C   ASP A 187     9348  20233  11903  -1226   -325  -3110       C  
ATOM   1263  O   ASP A 187      14.116  11.352  31.369  1.00109.85           O  
ANISOU 1263  O   ASP A 187     9210  20479  12047  -1246   -317  -3485       O  
ATOM   1264  CB  ASP A 187      15.823   8.240  31.016  1.00107.12           C  
ANISOU 1264  CB  ASP A 187     9350  20049  11300  -1319   -369  -2433       C  
ATOM   1265  CG  ASP A 187      15.154   7.761  32.280  1.00117.31           C  
ANISOU 1265  CG  ASP A 187    10516  21816  12240  -1533   -351  -2492       C  
ATOM   1266  OD1 ASP A 187      15.464   8.306  33.356  1.00119.79           O  
ANISOU 1266  OD1 ASP A 187    10615  22476  12422  -1614   -361  -2705       O  
ATOM   1267  OD2 ASP A 187      14.410   6.763  32.209  1.00122.68           O  
ANISOU 1267  OD2 ASP A 187    11320  22533  12759  -1634   -323  -2304       O  
ATOM   1268  N   ARG A 188      13.426   9.668  30.013  1.00104.68           N  
ANISOU 1268  N   ARG A 188     8908  19552  11313  -1202   -314  -2988       N  
ATOM   1269  CA  ARG A 188      12.030  10.082  29.899  1.00104.86           C  
ANISOU 1269  CA  ARG A 188     8814  19660  11367  -1187   -298  -3278       C  
ATOM   1270  C   ARG A 188      11.225   9.674  31.124  1.00110.30           C  
ANISOU 1270  C   ARG A 188     9312  20860  11736  -1426   -259  -3438       C  
ATOM   1271  O   ARG A 188      11.143   8.485  31.448  1.00109.60           O  
ANISOU 1271  O   ARG A 188     9318  20933  11390  -1597   -230  -3175       O  
ATOM   1272  CB  ARG A 188      11.400   9.521  28.615  1.00102.91           C  
ANISOU 1272  CB  ARG A 188     8758  19130  11212  -1070   -305  -3105       C  
ATOM   1273  CG  ARG A 188      12.149   9.888  27.335  1.00110.10           C  
ANISOU 1273  CG  ARG A 188     9866  19566  12401   -837   -334  -2928       C  
ATOM   1274  CD  ARG A 188      11.956   8.872  26.221  1.00116.81           C  
ANISOU 1274  CD  ARG A 188    10938  20203  13243   -774   -340  -2637       C  
ATOM   1275  NE  ARG A 188      12.476   7.548  26.573  1.00122.92           N  
ANISOU 1275  NE  ARG A 188    11828  21064  13811   -932   -325  -2330       N  
ATOM   1276  CZ  ARG A 188      12.285   6.447  25.855  1.00134.97           C  
ANISOU 1276  CZ  ARG A 188    13532  22457  15292   -937   -321  -2093       C  
ATOM   1277  NH1 ARG A 188      12.790   5.290  26.259  1.00122.57           N  
ANISOU 1277  NH1 ARG A 188    12078  20936  13555  -1069   -312  -1818       N  
ATOM   1278  NH2 ARG A 188      11.583   6.492  24.728  1.00120.63           N  
ANISOU 1278  NH2 ARG A 188    11780  20459  13597   -798   -332  -2137       N  
ATOM   1279  N   PHE A 189      10.656  10.673  31.815  1.00109.13           N  
ANISOU 1279  N   PHE A 189     8897  20960  11606  -1441   -251  -3872       N  
ATOM   1280  CA  PHE A 189       9.824  10.479  32.997  1.00111.54           C  
ANISOU 1280  CA  PHE A 189     8971  21803  11607  -1667   -202  -4103       C  
ATOM   1281  C   PHE A 189       8.370  10.822  32.668  1.00118.03           C  
ANISOU 1281  C   PHE A 189     9651  22703  12491  -1620   -186  -4428       C  
ATOM   1282  O   PHE A 189       7.966  11.986  32.737  1.00118.66           O  
ANISOU 1282  O   PHE A 189     9538  22790  12757  -1481   -214  -4838       O  
ATOM   1283  CB  PHE A 189      10.356  11.286  34.197  1.00114.96           C  
ANISOU 1283  CB  PHE A 189     9160  22558  11963  -1738   -205  -4393       C  
ATOM   1284  CG  PHE A 189      11.658  10.765  34.757  1.00116.00           C  
ANISOU 1284  CG  PHE A 189     9375  22773  11925  -1823   -224  -4095       C  
ATOM   1285  CD1 PHE A 189      11.676   9.682  35.628  1.00119.90           C  
ANISOU 1285  CD1 PHE A 189     9891  23651  12014  -2045   -195  -3856       C  
ATOM   1286  CD2 PHE A 189      12.867  11.363  34.421  1.00116.92           C  
ANISOU 1286  CD2 PHE A 189     9546  22596  12282  -1679   -271  -4055       C  
ATOM   1287  CE1 PHE A 189      12.883   9.193  36.137  1.00120.99           C  
ANISOU 1287  CE1 PHE A 189    10108  23877  11985  -2078   -237  -3574       C  
ATOM   1288  CE2 PHE A 189      14.075  10.875  34.934  1.00119.69           C  
ANISOU 1288  CE2 PHE A 189     9943  23065  12469  -1736   -302  -3810       C  
ATOM   1289  CZ  PHE A 189      14.073   9.798  35.794  1.00118.93           C  
ANISOU 1289  CZ  PHE A 189     9867  23355  11965  -1914   -297  -3573       C  
ATOM   1290  N   TYR A 190       7.578   9.817  32.299  1.00115.98           N  
ANISOU 1290  N   TYR A 190     9479  22498  12090  -1727   -145  -4268       N  
ATOM   1291  CA  TYR A 190       6.162  10.032  31.987  1.00117.85           C  
ANISOU 1291  CA  TYR A 190     9554  22869  12355  -1694   -132  -4590       C  
ATOM   1292  C   TYR A 190       5.323   9.921  33.257  1.00126.64           C  
ANISOU 1292  C   TYR A 190    10376  24590  13152  -1969    -47  -4886       C  
ATOM   1293  O   TYR A 190       5.862   9.611  34.320  1.00127.59           O  
ANISOU 1293  O   TYR A 190    10458  25005  13017  -2181     -1  -4789       O  
ATOM   1294  CB  TYR A 190       5.681   9.020  30.946  1.00117.93           C  
ANISOU 1294  CB  TYR A 190     9766  22671  12371  -1696   -119  -4326       C  
ATOM   1295  CG  TYR A 190       6.491   9.022  29.669  1.00117.21           C  
ANISOU 1295  CG  TYR A 190     9958  22029  12546  -1442   -192  -4024       C  
ATOM   1296  CD1 TYR A 190       7.544   8.134  29.491  1.00117.47           C  
ANISOU 1296  CD1 TYR A 190    10250  21854  12529  -1505   -184  -3576       C  
ATOM   1297  CD2 TYR A 190       6.204   9.911  28.642  1.00117.49           C  
ANISOU 1297  CD2 TYR A 190    10003  21768  12871  -1127   -270  -4184       C  
ATOM   1298  CE1 TYR A 190       8.288   8.132  28.327  1.00115.97           C  
ANISOU 1298  CE1 TYR A 190    10295  21204  12565  -1283   -239  -3326       C  
ATOM   1299  CE2 TYR A 190       6.942   9.916  27.474  1.00116.29           C  
ANISOU 1299  CE2 TYR A 190    10109  21149  12928   -911   -322  -3898       C  
ATOM   1300  CZ  TYR A 190       7.983   9.025  27.322  1.00121.69           C  
ANISOU 1300  CZ  TYR A 190    11021  21663  13551  -1001   -300  -3483       C  
ATOM   1301  OH  TYR A 190       8.720   9.026  26.160  1.00120.17           O  
ANISOU 1301  OH  TYR A 190    11060  21046  13551   -796   -340  -3224       O  
ATOM   1302  N   PRO A 191       4.015  10.167  33.171  1.00125.97           N  
ANISOU 1302  N   PRO A 191    10072  24730  13060  -1965    -26  -5254       N  
ATOM   1303  CA  PRO A 191       3.194  10.065  34.405  1.00129.41           C  
ANISOU 1303  CA  PRO A 191    10201  25798  13170  -2252     74  -5565       C  
ATOM   1304  C   PRO A 191       2.379   8.943  35.090  1.00137.36           C  
ANISOU 1304  C   PRO A 191    11128  27280  13782  -2654    221  -5507       C  
ATOM   1305  O   PRO A 191       2.022   9.095  36.261  1.00139.93           O  
ANISOU 1305  O   PRO A 191    11196  28138  13834  -2874    300  -5761       O  
ATOM   1306  CB  PRO A 191       1.945  10.878  34.102  1.00132.52           C  
ANISOU 1306  CB  PRO A 191    10313  26328  13709  -2082     42  -6092       C  
ATOM   1307  CG  PRO A 191       2.206  11.568  32.804  1.00134.65           C  
ANISOU 1307  CG  PRO A 191    10750  26023  14387  -1674    -92  -6057       C  
ATOM   1308  CD  PRO A 191       3.206  10.741  32.077  1.00127.20           C  
ANISOU 1308  CD  PRO A 191    10189  24651  13489  -1676   -102  -5486       C  
ATOM   1309  N   ASN A 192       2.205   7.859  34.374  1.00134.01           N  
ANISOU 1309  N   ASN A 192    10938  26644  13336  -2752    260  -5165       N  
ATOM   1310  CA  ASN A 192       1.339   6.812  34.788  1.00136.34           C  
ANISOU 1310  CA  ASN A 192    11185  27291  13327  -3127    409  -5117       C  
ATOM   1311  C   ASN A 192       2.336   5.938  34.098  1.00138.67           C  
ANISOU 1311  C   ASN A 192    11894  27083  13713  -3085    374  -4548       C  
ATOM   1312  O   ASN A 192       3.356   6.408  33.640  1.00136.03           O  
ANISOU 1312  O   ASN A 192    11715  26368  13603  -2810    258  -4393       O  
ATOM   1313  CB  ASN A 192       0.139   6.836  33.860  1.00136.81           C  
ANISOU 1313  CB  ASN A 192    11120  27323  13537  -3039    405  -5401       C  
ATOM   1314  CG  ASN A 192      -0.180   8.251  33.368  1.00155.53           C  
ANISOU 1314  CG  ASN A 192    13278  29607  16211  -2629    265  -5858       C  
ATOM   1315  OD1 ASN A 192       0.718   9.045  33.097  1.00151.02           O  
ANISOU 1315  OD1 ASN A 192    12815  28691  15875  -2337    148  -5798       O  
ATOM   1316  ND2 ASN A 192      -1.459   8.572  33.267  1.00145.35           N  
ANISOU 1316  ND2 ASN A 192    11682  28627  14916  -2609    279  -6322       N  
ATOM   1317  N   ASP A 193       2.014   4.672  33.993  1.00136.23           N  
ANISOU 1317  N   ASP A 193    11753  26764  13244  -3361    480  -4260       N  
ATOM   1318  CA  ASP A 193       2.660   3.739  33.078  1.00133.85           C  
ANISOU 1318  CA  ASP A 193    11826  25955  13078  -3305    449  -3794       C  
ATOM   1319  C   ASP A 193       1.780   3.743  31.831  1.00136.34           C  
ANISOU 1319  C   ASP A 193    12102  26078  13622  -3164    422  -3997       C  
ATOM   1320  O   ASP A 193       2.275   3.596  30.713  1.00133.39           O  
ANISOU 1320  O   ASP A 193    11950  25242  13492  -2924    332  -3797       O  
ATOM   1321  CB  ASP A 193       2.358   2.503  33.928  1.00138.50           C  
ANISOU 1321  CB  ASP A 193    12503  26806  13315  -3757    615  -3538       C  
ATOM   1322  CG  ASP A 193       3.545   1.565  34.034  1.00148.13           C  
ANISOU 1322  CG  ASP A 193    14100  27708  14473  -3794    597  -2958       C  
ATOM   1323  OD1 ASP A 193       4.532   1.927  34.709  1.00148.87           O  
ANISOU 1323  OD1 ASP A 193    14222  27860  14480  -3702    530  -2823       O  
ATOM   1324  OD2 ASP A 193       3.490   0.466  33.443  1.00152.77           O  
ANISOU 1324  OD2 ASP A 193    14946  27995  15105  -3906    644  -2661       O  
ATOM   1325  N   LEU A 194       0.475   3.908  32.025  1.00134.86           N  
ANISOU 1325  N   LEU A 194    11616  26286  13340  -3309    498  -4411       N  
ATOM   1326  CA  LEU A 194      -0.469   3.875  30.907  1.00134.35           C  
ANISOU 1326  CA  LEU A 194    11468  26128  13450  -3186    470  -4648       C  
ATOM   1327  C   LEU A 194      -0.068   4.858  29.786  1.00135.45           C  
ANISOU 1327  C   LEU A 194    11655  25874  13934  -2679    279  -4729       C  
ATOM   1328  O   LEU A 194      -0.611   4.777  28.684  1.00134.66           O  
ANISOU 1328  O   LEU A 194    11559  25615  13989  -2511    223  -4828       O  
ATOM   1329  CB  LEU A 194      -1.931   4.031  31.394  1.00137.62           C  
ANISOU 1329  CB  LEU A 194    11488  27104  13697  -3402    573  -5150       C  
ATOM   1330  CG  LEU A 194      -2.403   3.084  32.524  1.00145.33           C  
ANISOU 1330  CG  LEU A 194    12406  28509  14303  -3949    793  -5077       C  
ATOM   1331  CD1 LEU A 194      -3.752   3.511  33.071  1.00148.80           C  
ANISOU 1331  CD1 LEU A 194    12394  29559  14583  -4118    886  -5646       C  
ATOM   1332  CD2 LEU A 194      -2.448   1.627  32.066  1.00147.44           C  
ANISOU 1332  CD2 LEU A 194    12959  28529  14532  -4240    905  -4702       C  
ATOM   1333  N   TRP A 195       0.898   5.761  30.062  1.00130.22           N  
ANISOU 1333  N   TRP A 195    11036  25061  13381  -2449    186  -4676       N  
ATOM   1334  CA  TRP A 195       1.467   6.710  29.094  1.00127.52           C  
ANISOU 1334  CA  TRP A 195    10789  24304  13359  -2004     28  -4680       C  
ATOM   1335  C   TRP A 195       2.679   6.075  28.407  1.00127.35           C  
ANISOU 1335  C   TRP A 195    11143  23801  13441  -1929     -5  -4172       C  
ATOM   1336  O   TRP A 195       3.060   6.479  27.309  1.00124.69           O  
ANISOU 1336  O   TRP A 195    10945  23087  13346  -1612   -108  -4091       O  
ATOM   1337  CB  TRP A 195       1.918   7.997  29.808  1.00126.91           C  
ANISOU 1337  CB  TRP A 195    10557  24305  13357  -1845    -30  -4907       C  
ATOM   1338  CG  TRP A 195       0.958   9.147  29.711  1.00129.61           C  
ANISOU 1338  CG  TRP A 195    10598  24818  13828  -1611   -100  -5431       C  
ATOM   1339  CD1 TRP A 195       0.043   9.530  30.646  1.00135.50           C  
ANISOU 1339  CD1 TRP A 195    10992  26072  14418  -1748    -47  -5876       C  
ATOM   1340  CD2 TRP A 195       0.878  10.112  28.654  1.00128.70           C  
ANISOU 1340  CD2 TRP A 195    10513  24362  14025  -1178   -244  -5563       C  
ATOM   1341  NE1 TRP A 195      -0.632  10.649  30.221  1.00136.02           N  
ANISOU 1341  NE1 TRP A 195    10858  26126  14699  -1407   -159  -6299       N  
ATOM   1342  CE2 TRP A 195      -0.138  11.031  29.002  1.00135.27           C  
ANISOU 1342  CE2 TRP A 195    11007  25498  14891  -1048   -284  -6098       C  
ATOM   1343  CE3 TRP A 195       1.543  10.273  27.427  1.00127.58           C  
ANISOU 1343  CE3 TRP A 195    10654  23698  14123   -882   -339  -5277       C  
ATOM   1344  CZ2 TRP A 195      -0.495  12.101  28.176  1.00134.95           C  
ANISOU 1344  CZ2 TRP A 195    10925  25220  15128   -612   -431  -6330       C  
ATOM   1345  CZ3 TRP A 195       1.187  11.334  26.608  1.00129.41           C  
ANISOU 1345  CZ3 TRP A 195    10850  23714  14605   -478   -469  -5488       C  
ATOM   1346  CH2 TRP A 195       0.179  12.232  26.983  1.00132.75           C  
ANISOU 1346  CH2 TRP A 195    10958  24413  15069   -335   -521  -5998       C  
ATOM   1347  N   VAL A 196       3.287   5.087  29.084  1.00123.58           N  
ANISOU 1347  N   VAL A 196    10828  23359  12770  -2215     81  -3829       N  
ATOM   1348  CA  VAL A 196       4.471   4.348  28.650  1.00121.12           C  
ANISOU 1348  CA  VAL A 196    10852  22651  12515  -2179     58  -3351       C  
ATOM   1349  C   VAL A 196       4.133   3.384  27.505  1.00123.41           C  
ANISOU 1349  C   VAL A 196    11322  22680  12888  -2176     67  -3195       C  
ATOM   1350  O   VAL A 196       4.773   3.457  26.453  1.00120.62           O  
ANISOU 1350  O   VAL A 196    11149  21941  12740  -1914    -17  -3029       O  
ATOM   1351  CB  VAL A 196       5.165   3.647  29.860  1.00126.12           C  
ANISOU 1351  CB  VAL A 196    11579  23449  12890  -2459    130  -3062       C  
ATOM   1352  CG1 VAL A 196       6.293   2.717  29.415  1.00124.37           C  
ANISOU 1352  CG1 VAL A 196    11702  22835  12718  -2420    102  -2577       C  
ATOM   1353  CG2 VAL A 196       5.682   4.670  30.870  1.00126.51           C  
ANISOU 1353  CG2 VAL A 196    11452  23738  12879  -2412     98  -3226       C  
ATOM   1354  N   VAL A 197       3.139   2.491  27.717  1.00121.73           N  
ANISOU 1354  N   VAL A 197    11049  22691  12512  -2484    180  -3265       N  
ATOM   1355  CA  VAL A 197       2.709   1.477  26.742  1.00121.34           C  
ANISOU 1355  CA  VAL A 197    11139  22440  12526  -2548    211  -3170       C  
ATOM   1356  C   VAL A 197       2.116   2.102  25.467  1.00123.34           C  
ANISOU 1356  C   VAL A 197    11287  22592  12984  -2227    108  -3445       C  
ATOM   1357  O   VAL A 197       2.338   1.557  24.386  1.00121.41           O  
ANISOU 1357  O   VAL A 197    11224  22040  12866  -2108     69  -3290       O  
ATOM   1358  CB  VAL A 197       1.795   0.373  27.352  1.00128.39           C  
ANISOU 1358  CB  VAL A 197    11988  23598  13198  -3006    381  -3191       C  
ATOM   1359  CG1 VAL A 197       1.770  -0.873  26.466  1.00128.21           C  
ANISOU 1359  CG1 VAL A 197    12202  23252  13259  -3104    420  -2975       C  
ATOM   1360  CG2 VAL A 197       2.237   0.002  28.765  1.00129.90           C  
ANISOU 1360  CG2 VAL A 197    12235  23988  13133  -3303    478  -2963       C  
ATOM   1361  N   VAL A 198       1.413   3.257  25.584  1.00120.26           N  
ANISOU 1361  N   VAL A 198    10612  22456  12624  -2060     52  -3847       N  
ATOM   1362  CA  VAL A 198       0.815   3.968  24.436  1.00119.45           C  
ANISOU 1362  CA  VAL A 198    10403  22286  12697  -1707    -68  -4110       C  
ATOM   1363  C   VAL A 198       1.862   4.548  23.472  1.00120.29           C  
ANISOU 1363  C   VAL A 198    10735  21947  13025  -1319   -196  -3877       C  
ATOM   1364  O   VAL A 198       1.564   4.764  22.296  1.00119.15           O  
ANISOU 1364  O   VAL A 198    10612  21659  13002  -1046   -287  -3945       O  
ATOM   1365  CB  VAL A 198      -0.284   4.999  24.810  1.00125.49           C  
ANISOU 1365  CB  VAL A 198    10803  23438  13440  -1609   -103  -4616       C  
ATOM   1366  CG1 VAL A 198      -1.409   4.354  25.614  1.00128.03           C  
ANISOU 1366  CG1 VAL A 198    10876  24238  13531  -2012     41  -4878       C  
ATOM   1367  CG2 VAL A 198       0.295   6.206  25.537  1.00125.20           C  
ANISOU 1367  CG2 VAL A 198    10697  23405  13467  -1446   -158  -4691       C  
ATOM   1368  N   PHE A 199       3.079   4.811  23.980  1.00115.55           N  
ANISOU 1368  N   PHE A 199    10288  21160  12458  -1301   -199  -3612       N  
ATOM   1369  CA  PHE A 199       4.198   5.309  23.188  1.00112.98           C  
ANISOU 1369  CA  PHE A 199    10175  20427  12325   -998   -287  -3369       C  
ATOM   1370  C   PHE A 199       5.082   4.149  22.768  1.00115.56           C  
ANISOU 1370  C   PHE A 199    10782  20483  12643  -1092   -253  -2967       C  
ATOM   1371  O   PHE A 199       5.662   4.194  21.685  1.00113.36           O  
ANISOU 1371  O   PHE A 199    10672  19896  12505   -857   -314  -2801       O  
ATOM   1372  CB  PHE A 199       4.997   6.368  23.956  1.00114.39           C  
ANISOU 1372  CB  PHE A 199    10315  20580  12568   -917   -310  -3382       C  
ATOM   1373  CG  PHE A 199       4.400   7.758  23.953  1.00116.86           C  
ANISOU 1373  CG  PHE A 199    10422  20975  13003   -677   -384  -3748       C  
ATOM   1374  CD1 PHE A 199       3.656   8.214  22.869  1.00120.17           C  
ANISOU 1374  CD1 PHE A 199    10808  21311  13541   -389   -473  -3912       C  
ATOM   1375  CD2 PHE A 199       4.629   8.631  25.009  1.00119.79           C  
ANISOU 1375  CD2 PHE A 199    10642  21493  13380   -711   -375  -3928       C  
ATOM   1376  CE1 PHE A 199       3.118   9.502  22.863  1.00122.42           C  
ANISOU 1376  CE1 PHE A 199    10925  21633  13954   -130   -557  -4235       C  
ATOM   1377  CE2 PHE A 199       4.107   9.927  24.992  1.00123.87           C  
ANISOU 1377  CE2 PHE A 199    10984  22035  14047   -468   -449  -4278       C  
ATOM   1378  CZ  PHE A 199       3.344  10.349  23.925  1.00122.43           C  
ANISOU 1378  CZ  PHE A 199    10785  21742  13989   -172   -541  -4420       C  
ATOM   1379  N   GLN A 200       5.160   3.091  23.606  1.00113.75           N  
ANISOU 1379  N   GLN A 200    10606  20371  12245  -1430   -154  -2812       N  
ATOM   1380  CA  GLN A 200       5.928   1.886  23.290  1.00113.42           C  
ANISOU 1380  CA  GLN A 200    10833  20064  12199  -1522   -125  -2443       C  
ATOM   1381  C   GLN A 200       5.168   0.949  22.330  1.00118.64           C  
ANISOU 1381  C   GLN A 200    11544  20652  12882  -1577   -100  -2488       C  
ATOM   1382  O   GLN A 200       5.675  -0.113  21.969  1.00117.86           O  
ANISOU 1382  O   GLN A 200    11662  20315  12804  -1651    -75  -2229       O  
ATOM   1383  CB  GLN A 200       6.448   1.174  24.556  1.00116.04           C  
ANISOU 1383  CB  GLN A 200    11244  20497  12351  -1815    -47  -2210       C  
ATOM   1384  CG  GLN A 200       7.759   1.774  25.089  1.00136.77           C  
ANISOU 1384  CG  GLN A 200    13928  23038  15000  -1686   -101  -2030       C  
ATOM   1385  CD  GLN A 200       9.039   1.160  24.536  1.00157.88           C  
ANISOU 1385  CD  GLN A 200    16866  25352  17770  -1557   -145  -1667       C  
ATOM   1386  OE1 GLN A 200       9.927   0.754  25.295  1.00154.85           O  
ANISOU 1386  OE1 GLN A 200    16581  24965  17290  -1634   -145  -1423       O  
ATOM   1387  NE2 GLN A 200       9.214   1.138  23.215  1.00147.38           N  
ANISOU 1387  NE2 GLN A 200    15639  23741  16619  -1333   -193  -1636       N  
ATOM   1388  N   PHE A 201       3.959   1.375  21.907  1.00117.14           N  
ANISOU 1388  N   PHE A 201    11137  20675  12696  -1523   -117  -2846       N  
ATOM   1389  CA  PHE A 201       3.087   0.723  20.930  1.00118.16           C  
ANISOU 1389  CA  PHE A 201    11236  20811  12847  -1536   -112  -2997       C  
ATOM   1390  C   PHE A 201       3.195   1.555  19.649  1.00120.95           C  
ANISOU 1390  C   PHE A 201    11595  21011  13350  -1108   -248  -3070       C  
ATOM   1391  O   PHE A 201       3.203   0.993  18.553  1.00120.36           O  
ANISOU 1391  O   PHE A 201    11623  20775  13332  -1006   -278  -3021       O  
ATOM   1392  CB  PHE A 201       1.631   0.701  21.424  1.00122.72           C  
ANISOU 1392  CB  PHE A 201    11522  21810  13295  -1764    -43  -3384       C  
ATOM   1393  CG  PHE A 201       0.767  -0.385  20.829  1.00126.02           C  
ANISOU 1393  CG  PHE A 201    11913  22282  13688  -1967     25  -3511       C  
ATOM   1394  CD1 PHE A 201       0.652  -1.624  21.450  1.00130.79           C  
ANISOU 1394  CD1 PHE A 201    12616  22884  14193  -2396    178  -3373       C  
ATOM   1395  CD2 PHE A 201       0.037  -0.158  19.669  1.00128.40           C  
ANISOU 1395  CD2 PHE A 201    12084  22645  14056  -1735    -63  -3783       C  
ATOM   1396  CE1 PHE A 201      -0.164  -2.624  20.908  1.00133.49           C  
ANISOU 1396  CE1 PHE A 201    12926  23257  14536  -2618    257  -3522       C  
ATOM   1397  CE2 PHE A 201      -0.778  -1.158  19.129  1.00132.91           C  
ANISOU 1397  CE2 PHE A 201    12598  23298  14605  -1940      2  -3951       C  
ATOM   1398  CZ  PHE A 201      -0.873  -2.383  19.752  1.00132.63           C  
ANISOU 1398  CZ  PHE A 201    12659  23233  14501  -2394    169  -3831       C  
ATOM   1399  N   GLN A 202       3.316   2.903  19.807  1.00116.95           N  
ANISOU 1399  N   GLN A 202    10988  20544  12903   -858   -327  -3180       N  
ATOM   1400  CA  GLN A 202       3.519   3.902  18.750  1.00115.73           C  
ANISOU 1400  CA  GLN A 202    10867  20218  12887   -441   -452  -3201       C  
ATOM   1401  C   GLN A 202       4.881   3.627  18.088  1.00117.38           C  
ANISOU 1401  C   GLN A 202    11362  20047  13190   -322   -464  -2818       C  
ATOM   1402  O   GLN A 202       5.027   3.813  16.879  1.00116.19           O  
ANISOU 1402  O   GLN A 202    11301  19735  13108    -55   -534  -2764       O  
ATOM   1403  CB  GLN A 202       3.498   5.321  19.358  1.00117.44           C  
ANISOU 1403  CB  GLN A 202    10948  20508  13165   -277   -504  -3365       C  
ATOM   1404  CG  GLN A 202       3.524   6.463  18.343  1.00131.29           C  
ANISOU 1404  CG  GLN A 202    12735  22086  15063    152   -629  -3407       C  
ATOM   1405  CD  GLN A 202       3.933   7.769  18.978  1.00150.03           C  
ANISOU 1405  CD  GLN A 202    15067  24386  17552    282   -658  -3466       C  
ATOM   1406  OE1 GLN A 202       5.121   8.100  19.070  1.00144.22           O  
ANISOU 1406  OE1 GLN A 202    14499  23386  16912    311   -637  -3215       O  
ATOM   1407  NE2 GLN A 202       2.957   8.544  19.430  1.00143.77           N  
ANISOU 1407  NE2 GLN A 202    14031  23832  16761    363   -704  -3830       N  
ATOM   1408  N   HIS A 203       5.858   3.159  18.898  1.00113.22           N  
ANISOU 1408  N   HIS A 203    10961  19414  12642   -518   -395  -2564       N  
ATOM   1409  CA  HIS A 203       7.205   2.777  18.481  1.00111.26           C  
ANISOU 1409  CA  HIS A 203    10954  18854  12468   -447   -395  -2219       C  
ATOM   1410  C   HIS A 203       7.169   1.496  17.640  1.00114.15           C  
ANISOU 1410  C   HIS A 203    11453  19095  12823   -502   -376  -2113       C  
ATOM   1411  O   HIS A 203       7.903   1.409  16.659  1.00112.59           O  
ANISOU 1411  O   HIS A 203    11403  18670  12706   -306   -412  -1952       O  
ATOM   1412  CB  HIS A 203       8.135   2.636  19.708  1.00111.84           C  
ANISOU 1412  CB  HIS A 203    11078  18918  12496   -633   -345  -2028       C  
ATOM   1413  CG  HIS A 203       9.401   1.871  19.447  1.00114.15           C  
ANISOU 1413  CG  HIS A 203    11594  18949  12828   -621   -337  -1694       C  
ATOM   1414  ND1 HIS A 203      10.397   2.376  18.630  1.00114.53           N  
ANISOU 1414  ND1 HIS A 203    11750  18765  13003   -373   -380  -1552       N  
ATOM   1415  CD2 HIS A 203       9.787   0.657  19.909  1.00116.31           C  
ANISOU 1415  CD2 HIS A 203    11995  19168  13031   -822   -293  -1491       C  
ATOM   1416  CE1 HIS A 203      11.345   1.453  18.613  1.00113.53           C  
ANISOU 1416  CE1 HIS A 203    11783  18478  12876   -421   -365  -1300       C  
ATOM   1417  NE2 HIS A 203      11.024   0.404  19.370  1.00114.94           N  
ANISOU 1417  NE2 HIS A 203    11989  18737  12945   -671   -322  -1247       N  
ATOM   1418  N   ILE A 204       6.327   0.512  18.020  1.00111.39           N  
ANISOU 1418  N   ILE A 204    11048  18896  12379   -782   -309  -2219       N  
ATOM   1419  CA  ILE A 204       6.187  -0.754  17.291  1.00111.20           C  
ANISOU 1419  CA  ILE A 204    11138  18746  12366   -874   -278  -2168       C  
ATOM   1420  C   ILE A 204       5.407  -0.511  15.987  1.00114.30           C  
ANISOU 1420  C   ILE A 204    11435  19207  12787   -652   -348  -2406       C  
ATOM   1421  O   ILE A 204       5.738  -1.102  14.959  1.00113.20           O  
ANISOU 1421  O   ILE A 204    11416  18896  12699   -544   -369  -2331       O  
ATOM   1422  CB  ILE A 204       5.582  -1.889  18.188  1.00116.20           C  
ANISOU 1422  CB  ILE A 204    11766  19485  12901  -1286   -163  -2186       C  
ATOM   1423  CG1 ILE A 204       6.328  -2.042  19.545  1.00116.96           C  
ANISOU 1423  CG1 ILE A 204    11953  19563  12921  -1478   -109  -1934       C  
ATOM   1424  CG2 ILE A 204       5.479  -3.242  17.464  1.00117.58           C  
ANISOU 1424  CG2 ILE A 204    12079  19471  13126  -1404   -121  -2142       C  
ATOM   1425  CD1 ILE A 204       7.886  -2.390  19.525  1.00124.13           C  
ANISOU 1425  CD1 ILE A 204    13109  20152  13902  -1356   -145  -1557       C  
ATOM   1426  N   MET A 205       4.410   0.397  16.029  1.00111.30           N  
ANISOU 1426  N   MET A 205    10829  19093  12365   -557   -393  -2700       N  
ATOM   1427  CA  MET A 205       3.562   0.754  14.890  1.00111.72           C  
ANISOU 1427  CA  MET A 205    10758  19277  12412   -312   -483  -2950       C  
ATOM   1428  C   MET A 205       4.332   1.525  13.807  1.00112.88           C  
ANISOU 1428  C   MET A 205    11038  19220  12633     84   -583  -2786       C  
ATOM   1429  O   MET A 205       4.545   0.997  12.715  1.00112.44           O  
ANISOU 1429  O   MET A 205    11079  19063  12582    202   -609  -2728       O  
ATOM   1430  CB  MET A 205       2.312   1.533  15.365  1.00115.80           C  
ANISOU 1430  CB  MET A 205    10987  20148  12864   -301   -515  -3315       C  
ATOM   1431  CG  MET A 205       1.197   1.612  14.334  1.00121.21           C  
ANISOU 1431  CG  MET A 205    11494  21056  13504   -112   -603  -3633       C  
ATOM   1432  SD  MET A 205       0.501  -0.001  13.893  1.00127.23           S  
ANISOU 1432  SD  MET A 205    12210  21922  14210   -427   -516  -3795       S  
ATOM   1433  CE  MET A 205      -0.570   0.468  12.528  1.00125.68           C  
ANISOU 1433  CE  MET A 205    11798  22001  13954    -62   -673  -4155       C  
ATOM   1434  N   VAL A 206       4.754   2.759  14.124  1.00107.31           N  
ANISOU 1434  N   VAL A 206    10337  18455  11980    269   -626  -2719       N  
ATOM   1435  CA  VAL A 206       5.472   3.662  13.222  1.00105.53           C  
ANISOU 1435  CA  VAL A 206    10244  18027  11826    616   -699  -2549       C  
ATOM   1436  C   VAL A 206       6.924   3.202  12.939  1.00105.84           C  
ANISOU 1436  C   VAL A 206    10519  17772  11924    599   -647  -2201       C  
ATOM   1437  O   VAL A 206       7.443   3.460  11.852  1.00105.02           O  
ANISOU 1437  O   VAL A 206    10535  17530  11838    838   -684  -2064       O  
ATOM   1438  CB  VAL A 206       5.343   5.137  13.719  1.00109.93           C  
ANISOU 1438  CB  VAL A 206    10721  18599  12449    788   -750  -2632       C  
ATOM   1439  CG1 VAL A 206       6.276   6.094  12.980  1.00109.21           C  
ANISOU 1439  CG1 VAL A 206    10809  18231  12454   1078   -788  -2396       C  
ATOM   1440  CG2 VAL A 206       3.896   5.621  13.616  1.00111.68           C  
ANISOU 1440  CG2 VAL A 206    10709  19109  12615    920   -837  -2995       C  
ATOM   1441  N   GLY A 207       7.540   2.509  13.896  1.00100.37           N  
ANISOU 1441  N   GLY A 207     9882  17012  11242    328   -565  -2066       N  
ATOM   1442  CA  GLY A 207       8.913   2.025  13.785  1.00 98.00           C  
ANISOU 1442  CA  GLY A 207     9773  16467  10996    310   -524  -1767       C  
ATOM   1443  C   GLY A 207       9.093   0.683  13.104  1.00 99.86           C  
ANISOU 1443  C   GLY A 207    10113  16611  11217    247   -502  -1700       C  
ATOM   1444  O   GLY A 207      10.088   0.489  12.406  1.00 98.85           O  
ANISOU 1444  O   GLY A 207    10123  16302  11134    375   -502  -1514       O  
ATOM   1445  N   LEU A 208       8.163  -0.265  13.313  1.00 95.82           N  
ANISOU 1445  N   LEU A 208     9533  16222  10653     34   -473  -1866       N  
ATOM   1446  CA  LEU A 208       8.282  -1.594  12.709  1.00 95.27           C  
ANISOU 1446  CA  LEU A 208     9566  16034  10600    -50   -445  -1837       C  
ATOM   1447  C   LEU A 208       7.121  -2.132  11.870  1.00100.39           C  
ANISOU 1447  C   LEU A 208    10104  16837  11202    -62   -462  -2120       C  
ATOM   1448  O   LEU A 208       7.380  -2.825  10.887  1.00100.57           O  
ANISOU 1448  O   LEU A 208    10204  16758  11250     19   -472  -2117       O  
ATOM   1449  CB  LEU A 208       8.494  -2.686  13.780  1.00 95.58           C  
ANISOU 1449  CB  LEU A 208     9691  15978  10648   -374   -365  -1718       C  
ATOM   1450  CG  LEU A 208       9.493  -3.816  13.477  1.00 99.60           C  
ANISOU 1450  CG  LEU A 208    10404  16204  11237   -389   -345  -1505       C  
ATOM   1451  CD1 LEU A 208       9.721  -4.656  14.700  1.00100.44           C  
ANISOU 1451  CD1 LEU A 208    10611  16214  11336   -671   -282  -1341       C  
ATOM   1452  CD2 LEU A 208       8.998  -4.749  12.373  1.00102.77           C  
ANISOU 1452  CD2 LEU A 208    10819  16558  11672   -383   -343  -1671       C  
ATOM   1453  N   ILE A 209       5.856  -1.857  12.279  1.00 97.11           N  
ANISOU 1453  N   ILE A 209     9489  16691  10718   -174   -462  -2393       N  
ATOM   1454  CA  ILE A 209       4.630  -2.355  11.636  1.00 98.05           C  
ANISOU 1454  CA  ILE A 209     9448  17024  10783   -225   -474  -2722       C  
ATOM   1455  C   ILE A 209       4.427  -1.628  10.302  1.00 99.53           C  
ANISOU 1455  C   ILE A 209     9576  17317  10923    161   -593  -2829       C  
ATOM   1456  O   ILE A 209       4.499  -2.271   9.255  1.00 99.14           O  
ANISOU 1456  O   ILE A 209     9567  17235  10866    244   -612  -2877       O  
ATOM   1457  CB  ILE A 209       3.371  -2.338  12.567  1.00103.06           C  
ANISOU 1457  CB  ILE A 209     9861  17949  11348   -492   -423  -2998       C  
ATOM   1458  CG1 ILE A 209       3.541  -3.311  13.764  1.00104.15           C  
ANISOU 1458  CG1 ILE A 209    10091  17980  11499   -913   -286  -2865       C  
ATOM   1459  CG2 ILE A 209       2.069  -2.641  11.782  1.00105.90           C  
ANISOU 1459  CG2 ILE A 209    10001  18592  11643   -492   -454  -3396       C  
ATOM   1460  CD1 ILE A 209       2.679  -2.988  14.983  1.00113.10           C  
ANISOU 1460  CD1 ILE A 209    11038  19393  12541  -1168   -220  -3030       C  
ATOM   1461  N   LEU A 210       4.195  -0.301  10.346  1.00 94.57           N  
ANISOU 1461  N   LEU A 210     8862  16809  10261    401   -673  -2862       N  
ATOM   1462  CA  LEU A 210       3.958   0.541   9.171  1.00 94.26           C  
ANISOU 1462  CA  LEU A 210     8787  16871  10159    795   -796  -2924       C  
ATOM   1463  C   LEU A 210       5.089   0.528   8.110  1.00 96.13           C  
ANISOU 1463  C   LEU A 210     9232  16889  10405   1019   -813  -2655       C  
ATOM   1464  O   LEU A 210       4.766   0.259   6.950  1.00 96.58           O  
ANISOU 1464  O   LEU A 210     9257  17066  10373   1191   -873  -2769       O  
ATOM   1465  CB  LEU A 210       3.514   1.967   9.558  1.00 94.57           C  
ANISOU 1465  CB  LEU A 210     8722  17021  10190   1000   -874  -2992       C  
ATOM   1466  CG  LEU A 210       2.134   2.120  10.221  1.00100.78           C  
ANISOU 1466  CG  LEU A 210     9231  18137  10925    890   -895  -3364       C  
ATOM   1467  CD1 LEU A 210       2.072   3.386  11.054  1.00100.69           C  
ANISOU 1467  CD1 LEU A 210     9161  18134  10964    995   -929  -3372       C  
ATOM   1468  CD2 LEU A 210       0.999   2.093   9.188  1.00105.23           C  
ANISOU 1468  CD2 LEU A 210     9605  19007  11372   1101  -1009  -3683       C  
ATOM   1469  N   PRO A 211       6.395   0.749   8.433  1.00 90.21           N  
ANISOU 1469  N   PRO A 211     8672  15863   9742   1013   -758  -2329       N  
ATOM   1470  CA  PRO A 211       7.421   0.660   7.376  1.00 89.13           C  
ANISOU 1470  CA  PRO A 211     8699  15569   9596   1203   -759  -2115       C  
ATOM   1471  C   PRO A 211       7.758  -0.780   6.959  1.00 92.49           C  
ANISOU 1471  C   PRO A 211     9182  15920  10038   1056   -708  -2135       C  
ATOM   1472  O   PRO A 211       8.069  -1.011   5.787  1.00 92.34           O  
ANISOU 1472  O   PRO A 211     9211  15915   9958   1236   -733  -2122       O  
ATOM   1473  CB  PRO A 211       8.627   1.392   7.970  1.00 89.29           C  
ANISOU 1473  CB  PRO A 211     8858  15357   9712   1214   -709  -1817       C  
ATOM   1474  CG  PRO A 211       8.434   1.354   9.418  1.00 93.28           C  
ANISOU 1474  CG  PRO A 211     9300  15860  10283    954   -665  -1855       C  
ATOM   1475  CD  PRO A 211       7.001   1.067   9.743  1.00 90.30           C  
ANISOU 1475  CD  PRO A 211     8731  15733   9844    833   -692  -2169       C  
ATOM   1476  N   GLY A 212       7.669  -1.723   7.906  1.00 88.48           N  
ANISOU 1476  N   GLY A 212     8674  15337   9609    737   -636  -2171       N  
ATOM   1477  CA  GLY A 212       7.922  -3.146   7.688  1.00 88.74           C  
ANISOU 1477  CA  GLY A 212     8778  15242   9698    567   -583  -2200       C  
ATOM   1478  C   GLY A 212       6.998  -3.789   6.674  1.00 94.83           C  
ANISOU 1478  C   GLY A 212     9431  16196  10403    596   -617  -2509       C  
ATOM   1479  O   GLY A 212       7.445  -4.631   5.884  1.00 94.71           O  
ANISOU 1479  O   GLY A 212     9486  16086  10415    628   -605  -2528       O  
ATOM   1480  N   ILE A 213       5.700  -3.378   6.678  1.00 92.82           N  
ANISOU 1480  N   ILE A 213     8976  16233  10060    596   -665  -2786       N  
ATOM   1481  CA  ILE A 213       4.675  -3.853   5.737  1.00 94.59           C  
ANISOU 1481  CA  ILE A 213     9031  16714  10195    635   -713  -3139       C  
ATOM   1482  C   ILE A 213       5.049  -3.423   4.315  1.00 98.26           C  
ANISOU 1482  C   ILE A 213     9522  17269  10542   1013   -804  -3105       C  
ATOM   1483  O   ILE A 213       5.117  -4.275   3.428  1.00 99.12           O  
ANISOU 1483  O   ILE A 213     9628  17402  10633   1027   -803  -3240       O  
ATOM   1484  CB  ILE A 213       3.241  -3.422   6.165  1.00 99.28           C  
ANISOU 1484  CB  ILE A 213     9374  17635  10713    564   -750  -3452       C  
ATOM   1485  CG1 ILE A 213       2.746  -4.309   7.331  1.00100.58           C  
ANISOU 1485  CG1 ILE A 213     9494  17753  10969    108   -625  -3561       C  
ATOM   1486  CG2 ILE A 213       2.249  -3.471   4.986  1.00102.33           C  
ANISOU 1486  CG2 ILE A 213     9554  18368  10958    752   -851  -3809       C  
ATOM   1487  CD1 ILE A 213       1.610  -3.734   8.170  1.00106.77           C  
ANISOU 1487  CD1 ILE A 213    10051  18823  11692    -13   -626  -3787       C  
ATOM   1488  N   VAL A 214       5.352  -2.119   4.128  1.00 93.53           N  
ANISOU 1488  N   VAL A 214     8968  16702   9869   1303   -872  -2912       N  
ATOM   1489  CA  VAL A 214       5.765  -1.504   2.862  1.00 93.74           C  
ANISOU 1489  CA  VAL A 214     9054  16808   9756   1667   -947  -2802       C  
ATOM   1490  C   VAL A 214       6.899  -2.307   2.201  1.00 98.26           C  
ANISOU 1490  C   VAL A 214     9772  17204  10357   1664   -884  -2662       C  
ATOM   1491  O   VAL A 214       6.741  -2.738   1.059  1.00 99.21           O  
ANISOU 1491  O   VAL A 214     9841  17498  10357   1803   -925  -2817       O  
ATOM   1492  CB  VAL A 214       6.105   0.005   3.048  1.00 96.56           C  
ANISOU 1492  CB  VAL A 214     9497  17103  10090   1902   -989  -2542       C  
ATOM   1493  CG1 VAL A 214       6.781   0.595   1.815  1.00 96.69           C  
ANISOU 1493  CG1 VAL A 214     9638  17130   9970   2228  -1027  -2334       C  
ATOM   1494  CG2 VAL A 214       4.857   0.805   3.407  1.00 97.61           C  
ANISOU 1494  CG2 VAL A 214     9454  17464  10169   1997  -1086  -2750       C  
ATOM   1495  N   ILE A 215       8.002  -2.552   2.948  1.00 93.94           N  
ANISOU 1495  N   ILE A 215     9382  16344   9965   1506   -790  -2407       N  
ATOM   1496  CA  ILE A 215       9.186  -3.317   2.513  1.00 93.50           C  
ANISOU 1496  CA  ILE A 215     9458  16096   9970   1497   -727  -2273       C  
ATOM   1497  C   ILE A 215       8.818  -4.757   2.088  1.00 99.87           C  
ANISOU 1497  C   ILE A 215    10206  16920  10820   1353   -711  -2555       C  
ATOM   1498  O   ILE A 215       9.272  -5.214   1.036  1.00100.20           O  
ANISOU 1498  O   ILE A 215    10263  17004  10803   1489   -715  -2611       O  
ATOM   1499  CB  ILE A 215      10.302  -3.276   3.609  1.00 94.43           C  
ANISOU 1499  CB  ILE A 215     9721  15908  10250   1351   -649  -1980       C  
ATOM   1500  CG1 ILE A 215      10.939  -1.870   3.705  1.00 93.63           C  
ANISOU 1500  CG1 ILE A 215     9689  15776  10112   1523   -650  -1711       C  
ATOM   1501  CG2 ILE A 215      11.376  -4.353   3.384  1.00 94.50           C  
ANISOU 1501  CG2 ILE A 215     9836  15712  10359   1299   -593  -1911       C  
ATOM   1502  CD1 ILE A 215      11.433  -1.446   5.111  1.00 98.78           C  
ANISOU 1502  CD1 ILE A 215    10392  16242  10896   1355   -604  -1526       C  
ATOM   1503  N   LEU A 216       8.007  -5.462   2.908  1.00 97.62           N  
ANISOU 1503  N   LEU A 216     9853  16600  10638   1063   -681  -2741       N  
ATOM   1504  CA  LEU A 216       7.608  -6.839   2.620  1.00 99.36           C  
ANISOU 1504  CA  LEU A 216    10031  16783  10940    873   -646  -3018       C  
ATOM   1505  C   LEU A 216       6.601  -6.947   1.480  1.00105.36           C  
ANISOU 1505  C   LEU A 216    10592  17895  11544    996   -718  -3389       C  
ATOM   1506  O   LEU A 216       6.560  -7.982   0.805  1.00106.50           O  
ANISOU 1506  O   LEU A 216    10705  18030  11728    941   -700  -3622       O  
ATOM   1507  CB  LEU A 216       7.131  -7.580   3.878  1.00 99.86           C  
ANISOU 1507  CB  LEU A 216    10111  16670  11162    488   -565  -3063       C  
ATOM   1508  CG  LEU A 216       7.803  -8.938   4.115  1.00105.27           C  
ANISOU 1508  CG  LEU A 216    10956  16998  12044    291   -487  -3017       C  
ATOM   1509  CD1 LEU A 216       8.043  -9.173   5.584  1.00104.71           C  
ANISOU 1509  CD1 LEU A 216    11018  16670  12097     24   -415  -2781       C  
ATOM   1510  CD2 LEU A 216       6.990 -10.083   3.510  1.00110.60           C  
ANISOU 1510  CD2 LEU A 216    11534  17712  12776    126   -461  -3407       C  
ATOM   1511  N   SER A 217       5.808  -5.873   1.249  1.00102.18           N  
ANISOU 1511  N   SER A 217    10051  17806  10965   1185   -808  -3458       N  
ATOM   1512  CA  SER A 217       4.831  -5.804   0.160  1.00104.16           C  
ANISOU 1512  CA  SER A 217    10095  18458  11024   1364   -907  -3798       C  
ATOM   1513  C   SER A 217       5.577  -5.728  -1.169  1.00108.46           C  
ANISOU 1513  C   SER A 217    10697  19092  11420   1670   -950  -3727       C  
ATOM   1514  O   SER A 217       5.314  -6.539  -2.057  1.00109.64           O  
ANISOU 1514  O   SER A 217    10742  19402  11513   1682   -966  -4025       O  
ATOM   1515  CB  SER A 217       3.912  -4.597   0.328  1.00107.76           C  
ANISOU 1515  CB  SER A 217    10414  19196  11335   1538  -1008  -3840       C  
ATOM   1516  OG  SER A 217       3.147  -4.697   1.518  1.00116.10           O  
ANISOU 1516  OG  SER A 217    11375  20234  12503   1246   -962  -3961       O  
ATOM   1517  N   CYS A 218       6.559  -4.798  -1.269  1.00103.87           N  
ANISOU 1517  N   CYS A 218    10282  18401  10783   1885   -951  -3341       N  
ATOM   1518  CA  CYS A 218       7.421  -4.601  -2.440  1.00104.22           C  
ANISOU 1518  CA  CYS A 218    10405  18522  10672   2155   -963  -3204       C  
ATOM   1519  C   CYS A 218       8.181  -5.887  -2.764  1.00108.25           C  
ANISOU 1519  C   CYS A 218    10961  18865  11304   2024   -883  -3304       C  
ATOM   1520  O   CYS A 218       8.165  -6.318  -3.911  1.00109.49           O  
ANISOU 1520  O   CYS A 218    11039  19246  11318   2165   -914  -3507       O  
ATOM   1521  CB  CYS A 218       8.379  -3.430  -2.224  1.00102.86           C  
ANISOU 1521  CB  CYS A 218    10413  18191  10477   2309   -937  -2762       C  
ATOM   1522  SG  CYS A 218       7.563  -1.832  -1.971  1.00106.91           S  
ANISOU 1522  SG  CYS A 218    10901  18857  10865   2520  -1039  -2639       S  
ATOM   1523  N   TYR A 219       8.778  -6.533  -1.741  1.00103.62           N  
ANISOU 1523  N   TYR A 219    10492  17901  10978   1764   -791  -3189       N  
ATOM   1524  CA  TYR A 219       9.538  -7.777  -1.873  1.00104.08           C  
ANISOU 1524  CA  TYR A 219    10619  17724  11203   1645   -723  -3265       C  
ATOM   1525  C   TYR A 219       8.719  -8.966  -2.368  1.00109.80           C  
ANISOU 1525  C   TYR A 219    11204  18541  11973   1510   -730  -3714       C  
ATOM   1526  O   TYR A 219       9.300  -9.926  -2.867  1.00110.66           O  
ANISOU 1526  O   TYR A 219    11344  18527  12176   1499   -695  -3842       O  
ATOM   1527  CB  TYR A 219      10.280  -8.122  -0.573  1.00104.16           C  
ANISOU 1527  CB  TYR A 219    10795  17314  11465   1424   -645  -3014       C  
ATOM   1528  CG  TYR A 219      11.515  -7.287  -0.290  1.00105.05           C  
ANISOU 1528  CG  TYR A 219    11045  17298  11571   1557   -618  -2618       C  
ATOM   1529  CD1 TYR A 219      12.197  -7.404   0.917  1.00105.84           C  
ANISOU 1529  CD1 TYR A 219    11274  17083  11856   1397   -567  -2376       C  
ATOM   1530  CD2 TYR A 219      12.011  -6.390  -1.235  1.00106.01           C  
ANISOU 1530  CD2 TYR A 219    11164  17626  11489   1832   -636  -2489       C  
ATOM   1531  CE1 TYR A 219      13.334  -6.644   1.184  1.00105.45           C  
ANISOU 1531  CE1 TYR A 219    11319  16943  11804   1503   -539  -2056       C  
ATOM   1532  CE2 TYR A 219      13.138  -5.614  -0.974  1.00105.60           C  
ANISOU 1532  CE2 TYR A 219    11225  17455  11443   1915   -589  -2147       C  
ATOM   1533  CZ  TYR A 219      13.798  -5.748   0.237  1.00113.37           C  
ANISOU 1533  CZ  TYR A 219    12309  18140  12628   1747   -543  -1952       C  
ATOM   1534  OH  TYR A 219      14.927  -5.012   0.492  1.00115.41           O  
ANISOU 1534  OH  TYR A 219    12649  18306  12897   1814   -494  -1658       O  
ATOM   1535  N   CYS A 220       7.380  -8.902  -2.242  1.00106.97           N  
ANISOU 1535  N   CYS A 220    10679  18407  11558   1408   -774  -3981       N  
ATOM   1536  CA  CYS A 220       6.500  -9.967  -2.722  1.00109.11           C  
ANISOU 1536  CA  CYS A 220    10783  18806  11869   1253   -774  -4454       C  
ATOM   1537  C   CYS A 220       5.866  -9.644  -4.074  1.00112.83           C  
ANISOU 1537  C   CYS A 220    11042  19780  12047   1524   -882  -4747       C  
ATOM   1538  O   CYS A 220       5.670 -10.554  -4.884  1.00114.89           O  
ANISOU 1538  O   CYS A 220    11189  20157  12307   1500   -883  -5114       O  
ATOM   1539  CB  CYS A 220       5.461 -10.359  -1.677  1.00110.27           C  
ANISOU 1539  CB  CYS A 220    10860  18871  12167    896   -727  -4620       C  
ATOM   1540  SG  CYS A 220       5.248 -12.151  -1.503  1.00116.90           S  
ANISOU 1540  SG  CYS A 220    11715  19398  13303    503   -615  -4957       S  
ATOM   1541  N   ILE A 221       5.565  -8.352  -4.326  1.00106.60           N  
ANISOU 1541  N   ILE A 221    10207  19288  11009   1797   -978  -4587       N  
ATOM   1542  CA  ILE A 221       4.988  -7.858  -5.580  1.00107.38           C  
ANISOU 1542  CA  ILE A 221    10130  19891  10779   2117  -1103  -4785       C  
ATOM   1543  C   ILE A 221       6.041  -7.926  -6.699  1.00109.33           C  
ANISOU 1543  C   ILE A 221    10457  20207  10874   2360  -1097  -4677       C  
ATOM   1544  O   ILE A 221       5.712  -8.353  -7.810  1.00111.22           O  
ANISOU 1544  O   ILE A 221    10535  20795  10930   2490  -1153  -5006       O  
ATOM   1545  CB  ILE A 221       4.342  -6.447  -5.389  1.00109.92           C  
ANISOU 1545  CB  ILE A 221    10412  20444  10909   2342  -1212  -4612       C  
ATOM   1546  CG1 ILE A 221       3.033  -6.553  -4.567  1.00110.96           C  
ANISOU 1546  CG1 ILE A 221    10355  20673  11132   2118  -1235  -4902       C  
ATOM   1547  CG2 ILE A 221       4.079  -5.736  -6.734  1.00112.58           C  
ANISOU 1547  CG2 ILE A 221    10655  21254  10868   2763  -1351  -4652       C  
ATOM   1548  CD1 ILE A 221       2.617  -5.289  -3.786  1.00115.15           C  
ANISOU 1548  CD1 ILE A 221    10902  21222  11627   2222  -1294  -4675       C  
ATOM   1549  N   ILE A 222       7.302  -7.538  -6.388  1.00102.40           N  
ANISOU 1549  N   ILE A 222     9808  19027  10071   2404  -1022  -4246       N  
ATOM   1550  CA  ILE A 222       8.417  -7.569  -7.335  1.00102.13           C  
ANISOU 1550  CA  ILE A 222     9853  19046   9906   2602   -988  -4116       C  
ATOM   1551  C   ILE A 222       8.687  -9.000  -7.792  1.00107.94           C  
ANISOU 1551  C   ILE A 222    10518  19717  10777   2473   -938  -4476       C  
ATOM   1552  O   ILE A 222       8.385  -9.300  -8.944  1.00110.01           O  
ANISOU 1552  O   ILE A 222    10622  20352  10824   2626   -991  -4782       O  
ATOM   1553  CB  ILE A 222       9.691  -6.801  -6.858  1.00102.48           C  
ANISOU 1553  CB  ILE A 222    10127  18804  10007   2653   -909  -3605       C  
ATOM   1554  CG1 ILE A 222       9.438  -5.276  -6.814  1.00102.36           C  
ANISOU 1554  CG1 ILE A 222    10173  18925   9793   2859   -968  -3284       C  
ATOM   1555  CG2 ILE A 222      10.908  -7.113  -7.744  1.00103.40           C  
ANISOU 1555  CG2 ILE A 222    10296  18954  10039   2782   -842  -3541       C  
ATOM   1556  CD1 ILE A 222      10.333  -4.495  -5.806  1.00106.95           C  
ANISOU 1556  CD1 ILE A 222    10957  19140  10539   2786   -887  -2838       C  
ATOM   1557  N   ILE A 223       9.142  -9.904  -6.884  1.00104.03           N  
ANISOU 1557  N   ILE A 223    10128  18762  10636   2195   -847  -4472       N  
ATOM   1558  CA  ILE A 223       9.455 -11.310  -7.224  1.00106.07           C  
ANISOU 1558  CA  ILE A 223    10355  18863  11086   2071   -797  -4804       C  
ATOM   1559  C   ILE A 223       8.349 -12.072  -7.992  1.00113.58           C  
ANISOU 1559  C   ILE A 223    11066  20118  11972   2016   -848  -5367       C  
ATOM   1560  O   ILE A 223       8.643 -13.053  -8.677  1.00115.35           O  
ANISOU 1560  O   ILE A 223    11226  20338  12263   2011   -824  -5686       O  
ATOM   1561  CB  ILE A 223      10.187 -12.147  -6.116  1.00108.13           C  
ANISOU 1561  CB  ILE A 223    10805  18543  11738   1819   -704  -4663       C  
ATOM   1562  CG1 ILE A 223       9.304 -13.181  -5.353  1.00110.09           C  
ANISOU 1562  CG1 ILE A 223    11034  18526  12268   1464   -669  -4937       C  
ATOM   1563  CG2 ILE A 223      11.132 -11.325  -5.230  1.00105.53           C  
ANISOU 1563  CG2 ILE A 223    10671  17965  11459   1853   -667  -4140       C  
ATOM   1564  CD1 ILE A 223       8.186 -12.680  -4.455  1.00117.69           C  
ANISOU 1564  CD1 ILE A 223    11952  19535  13228   1269   -680  -4900       C  
ATOM   1565  N   SER A 224       7.098 -11.587  -7.891  1.00111.26           N  
ANISOU 1565  N   SER A 224    10622  20109  11544   1991   -921  -5511       N  
ATOM   1566  CA  SER A 224       5.940 -12.123  -8.597  1.00114.70           C  
ANISOU 1566  CA  SER A 224    10788  20919  11876   1952   -983  -6057       C  
ATOM   1567  C   SER A 224       5.890 -11.510 -10.002  1.00121.24           C  
ANISOU 1567  C   SER A 224    11469  22322  12275   2339  -1093  -6148       C  
ATOM   1568  O   SER A 224       5.811 -12.251 -10.989  1.00123.99           O  
ANISOU 1568  O   SER A 224    11656  22918  12538   2391  -1111  -6558       O  
ATOM   1569  CB  SER A 224       4.654 -11.820  -7.827  1.00118.39           C  
ANISOU 1569  CB  SER A 224    11137  21474  12373   1768  -1017  -6170       C  
ATOM   1570  OG  SER A 224       3.507 -12.346  -8.477  1.00131.07           O  
ANISOU 1570  OG  SER A 224    12448  23468  13883   1711  -1074  -6736       O  
ATOM   1571  N   LYS A 225       5.994 -10.183 -10.118  1.00116.52           N  
ANISOU 1571  N   LYS A 225    10939  21926  11407   2614  -1162  -5762       N  
ATOM   1572  CA  LYS A 225       5.918  -9.491 -11.426  1.00118.31           C  
ANISOU 1572  CA  LYS A 225    11061  22705  11186   3001  -1270  -5773       C  
ATOM   1573  C   LYS A 225       7.260  -9.333 -12.175  1.00121.37           C  
ANISOU 1573  C   LYS A 225    11589  23101  11427   3201  -1209  -5508       C  
ATOM   1574  O   LYS A 225       7.368  -8.597 -13.157  1.00122.20           O  
ANISOU 1574  O   LYS A 225    11672  23619  11142   3517  -1274  -5383       O  
ATOM   1575  CB  LYS A 225       5.250  -8.123 -11.264  1.00120.55           C  
ANISOU 1575  CB  LYS A 225    11351  23215  11236   3221  -1384  -5506       C  
ATOM   1576  CG  LYS A 225       3.736  -8.153 -11.394  1.00134.66           C  
ANISOU 1576  CG  LYS A 225    12859  25399  12906   3233  -1516  -5933       C  
ATOM   1577  CD  LYS A 225       3.307  -8.801 -12.701  1.00145.45           C  
ANISOU 1577  CD  LYS A 225    13967  27283  14013   3371  -1594  -6429       C  
ATOM   1578  CE  LYS A 225       2.253  -9.871 -12.466  1.00154.39           C  
ANISOU 1578  CE  LYS A 225    14833  28486  15342   3064  -1593  -7039       C  
ATOM   1579  NZ  LYS A 225       2.828 -11.242 -12.544  1.00160.92           N  
ANISOU 1579  NZ  LYS A 225    15670  29021  16452   2784  -1459  -7323       N  
ATOM   1580  N   LEU A 226       8.259 -10.046 -11.678  1.00116.45           N  
ANISOU 1580  N   LEU A 226    11106  22026  11114   3009  -1083  -5426       N  
ATOM   1581  CA  LEU A 226       9.638 -10.147 -12.174  1.00115.95           C  
ANISOU 1581  CA  LEU A 226    11156  21886  11013   3120   -995  -5236       C  
ATOM   1582  C   LEU A 226       9.830 -11.545 -12.778  1.00122.64           C  
ANISOU 1582  C   LEU A 226    11866  22745  11986   3034   -961  -5735       C  
ATOM   1583  O   LEU A 226      10.564 -11.704 -13.752  1.00124.13           O  
ANISOU 1583  O   LEU A 226    12010  23170  11985   3210   -935  -5805       O  
ATOM   1584  CB  LEU A 226      10.572  -9.902 -10.967  1.00112.39           C  
ANISOU 1584  CB  LEU A 226    10953  20884  10866   2967   -895  -4791       C  
ATOM   1585  CG  LEU A 226      12.085 -10.021 -11.129  1.00115.96           C  
ANISOU 1585  CG  LEU A 226    11531  21158  11372   3024   -789  -4566       C  
ATOM   1586  CD1 LEU A 226      12.659  -8.850 -11.899  1.00116.27           C  
ANISOU 1586  CD1 LEU A 226    11624  21518  11037   3290   -777  -4222       C  
ATOM   1587  CD2 LEU A 226      12.749 -10.128  -9.781  1.00114.60           C  
ANISOU 1587  CD2 LEU A 226    11547  20430  11567   2817   -715  -4277       C  
ATOM   1588  N   SER A 227       9.128 -12.548 -12.201  1.00119.73           N  
ANISOU 1588  N   SER A 227    11427  22130  11937   2753   -954  -6097       N  
ATOM   1589  CA  SER A 227       9.104 -13.940 -12.659  1.00122.35           C  
ANISOU 1589  CA  SER A 227    11628  22404  12456   2626   -924  -6629       C  
ATOM   1590  C   SER A 227       8.001 -14.089 -13.721  1.00130.39           C  
ANISOU 1590  C   SER A 227    12345  24015  13182   2725  -1026  -7139       C  
ATOM   1591  O   SER A 227       7.564 -15.195 -14.025  1.00132.67           O  
ANISOU 1591  O   SER A 227    12474  24304  13632   2568  -1016  -7675       O  
ATOM   1592  CB  SER A 227       8.875 -14.880 -11.477  1.00125.09           C  
ANISOU 1592  CB  SER A 227    12075  22162  13290   2254   -854  -6723       C  
ATOM   1593  OG  SER A 227       7.617 -14.621 -10.878  1.00133.63           O  
ANISOU 1593  OG  SER A 227    13078  23306  14387   2078   -895  -6802       O  
ATOM   1594  N   HIS A 228       7.544 -12.950 -14.229  1.00127.74           N  
ANISOU 1594  N   HIS A 228    11943  24165  12429   2986  -1127  -6963       N  
ATOM   1595  CA  HIS A 228       6.567 -12.904 -15.303  1.00131.32           C  
ANISOU 1595  CA  HIS A 228    12108  25268  12519   3159  -1251  -7386       C  
ATOM   1596  C   HIS A 228       7.277 -12.317 -16.508  1.00136.66           C  
ANISOU 1596  C   HIS A 228    12776  26403  12748   3523  -1280  -7226       C  
ATOM   1597  O   HIS A 228       6.989 -12.669 -17.652  1.00139.87           O  
ANISOU 1597  O   HIS A 228    12951  27328  12866   3677  -1343  -7639       O  
ATOM   1598  CB  HIS A 228       5.373 -12.034 -14.912  1.00131.87           C  
ANISOU 1598  CB  HIS A 228    12103  25561  12442   3202  -1366  -7308       C  
ATOM   1599  CG  HIS A 228       4.361 -11.871 -16.002  1.00139.19           C  
ANISOU 1599  CG  HIS A 228    12726  27204  12957   3433  -1521  -7712       C  
ATOM   1600  ND1 HIS A 228       4.393 -10.824 -16.898  1.00142.15           N  
ANISOU 1600  ND1 HIS A 228    13090  28089  12830   3841  -1634  -7469       N  
ATOM   1601  CD2 HIS A 228       3.287 -12.624 -16.341  1.00144.31           C  
ANISOU 1601  CD2 HIS A 228    13065  28156  13609   3314  -1584  -8348       C  
ATOM   1602  CE1 HIS A 228       3.383 -10.939 -17.742  1.00145.32           C  
ANISOU 1602  CE1 HIS A 228    13186  29101  12927   3994  -1776  -7930       C  
ATOM   1603  NE2 HIS A 228       2.696 -12.022 -17.426  1.00146.97           N  
ANISOU 1603  NE2 HIS A 228    13193  29212  13438   3673  -1748  -8490       N  
ATOM   1604  N   ASN A1002       8.221 -11.422 -16.234  1.00101.48           N  
ANISOU 1604  N   ASN A1002    10629  16971  10958    892   -906  -2607       N  
ATOM   1605  CA  ASN A1002       9.088 -10.888 -17.269  1.00 99.71           C  
ANISOU 1605  CA  ASN A1002    10521  16491  10874    970  -1100  -2393       C  
ATOM   1606  C   ASN A1002       9.803 -12.048 -17.940  1.00101.82           C  
ANISOU 1606  C   ASN A1002    10993  16753  10939    894  -1058  -2056       C  
ATOM   1607  O   ASN A1002      10.146 -11.983 -19.121  1.00 99.81           O  
ANISOU 1607  O   ASN A1002    10839  16319  10767    925  -1172  -1861       O  
ATOM   1608  CB  ASN A1002      10.102  -9.911 -16.674  1.00 98.06           C  
ANISOU 1608  CB  ASN A1002    10319  16224  10715   1009  -1173  -2465       C  
ATOM   1609  CG  ASN A1002       9.441  -8.760 -15.941  1.00115.23           C  
ANISOU 1609  CG  ASN A1002    12272  18403  13107   1086  -1212  -2844       C  
ATOM   1610  OD1 ASN A1002       8.291  -8.860 -15.513  1.00114.42           O  
ANISOU 1610  OD1 ASN A1002    12003  18430  13040   1078  -1114  -3091       O  
ATOM   1611  ND2 ASN A1002      10.166  -7.658 -15.792  1.00103.28           N  
ANISOU 1611  ND2 ASN A1002    10736  16740  11766   1156  -1350  -2914       N  
ATOM   1612  N   ILE A1003      10.017 -13.117 -17.178  1.00 99.32           N  
ANISOU 1612  N   ILE A1003    10742  16636  10360    785   -898  -1997       N  
ATOM   1613  CA  ILE A1003      10.592 -14.345 -17.737  1.00 98.05           C  
ANISOU 1613  CA  ILE A1003    10741  16467  10045    714   -856  -1715       C  
ATOM   1614  C   ILE A1003       9.603 -14.960 -18.756  1.00102.29           C  
ANISOU 1614  C   ILE A1003    11258  16959  10647    714   -856  -1660       C  
ATOM   1615  O   ILE A1003      10.040 -15.515 -19.765  1.00101.04           O  
ANISOU 1615  O   ILE A1003    11217  16698  10476    706   -894  -1456       O  
ATOM   1616  CB  ILE A1003      11.044 -15.339 -16.619  1.00101.47           C  
ANISOU 1616  CB  ILE A1003    11250  17092  10212    592   -730  -1649       C  
ATOM   1617  CG1 ILE A1003      12.176 -16.248 -17.106  1.00100.15           C  
ANISOU 1617  CG1 ILE A1003    11237  16840   9974    555   -755  -1376       C  
ATOM   1618  CG2 ILE A1003       9.876 -16.152 -16.025  1.00103.98           C  
ANISOU 1618  CG2 ILE A1003    11502  17607  10399    488   -574  -1733       C  
ATOM   1619  CD1 ILE A1003      12.999 -16.827 -15.997  1.00107.52           C  
ANISOU 1619  CD1 ILE A1003    12253  17882  10716    469   -733  -1301       C  
ATOM   1620  N   PHE A1004       8.276 -14.831 -18.497  1.00100.24           N  
ANISOU 1620  N   PHE A1004    10837  16778  10473    722   -813  -1869       N  
ATOM   1621  CA  PHE A1004       7.216 -15.319 -19.384  1.00100.25           C  
ANISOU 1621  CA  PHE A1004    10783  16733  10575    731   -838  -1863       C  
ATOM   1622  C   PHE A1004       7.251 -14.513 -20.675  1.00102.87           C  
ANISOU 1622  C   PHE A1004    11151  16829  11108    839  -1060  -1796       C  
ATOM   1623  O   PHE A1004       7.371 -15.097 -21.753  1.00101.14           O  
ANISOU 1623  O   PHE A1004    11050  16525  10851    824  -1115  -1610       O  
ATOM   1624  CB  PHE A1004       5.835 -15.235 -18.693  1.00104.45           C  
ANISOU 1624  CB  PHE A1004    11092  17397  11196    714   -739  -2148       C  
ATOM   1625  CG  PHE A1004       4.652 -15.703 -19.512  1.00106.90           C  
ANISOU 1625  CG  PHE A1004    11306  17657  11655    727   -777  -2184       C  
ATOM   1626  CD1 PHE A1004       4.305 -17.049 -19.559  1.00109.89           C  
ANISOU 1626  CD1 PHE A1004    11719  18136  11899    614   -644  -2075       C  
ATOM   1627  CD2 PHE A1004       3.866 -14.793 -20.213  1.00110.34           C  
ANISOU 1627  CD2 PHE A1004    11605  17926  12394    851   -970  -2330       C  
ATOM   1628  CE1 PHE A1004       3.204 -17.479 -20.309  1.00111.44           C  
ANISOU 1628  CE1 PHE A1004    11812  18279  12252    626   -691  -2127       C  
ATOM   1629  CE2 PHE A1004       2.774 -15.226 -20.971  1.00113.90           C  
ANISOU 1629  CE2 PHE A1004    11961  18320  12997    867  -1040  -2371       C  
ATOM   1630  CZ  PHE A1004       2.448 -16.565 -21.011  1.00111.54           C  
ANISOU 1630  CZ  PHE A1004    11692  18135  12553    754   -892  -2278       C  
ATOM   1631  N   GLU A1005       7.207 -13.169 -20.547  1.00100.36           N  
ANISOU 1631  N   GLU A1005    10742  16400  10992    934  -1192  -1945       N  
ATOM   1632  CA  GLU A1005       7.248 -12.213 -21.653  1.00100.47           C  
ANISOU 1632  CA  GLU A1005    10796  16166  11212   1023  -1438  -1871       C  
ATOM   1633  C   GLU A1005       8.523 -12.318 -22.503  1.00102.26           C  
ANISOU 1633  C   GLU A1005    11256  16287  11309    983  -1480  -1577       C  
ATOM   1634  O   GLU A1005       8.456 -12.107 -23.715  1.00102.17           O  
ANISOU 1634  O   GLU A1005    11348  16120  11351    993  -1637  -1430       O  
ATOM   1635  CB  GLU A1005       7.020 -10.782 -21.144  1.00103.67           C  
ANISOU 1635  CB  GLU A1005    11039  16465  11885   1124  -1567  -2103       C  
ATOM   1636  CG  GLU A1005       5.561 -10.469 -20.852  1.00117.68           C  
ANISOU 1636  CG  GLU A1005    12557  18251  13906   1191  -1606  -2408       C  
ATOM   1637  CD  GLU A1005       4.667 -10.337 -22.070  1.00142.34           C  
ANISOU 1637  CD  GLU A1005    15658  21181  17243   1254  -1842  -2356       C  
ATOM   1638  OE1 GLU A1005       3.928 -11.302 -22.374  1.00139.28           O  
ANISOU 1638  OE1 GLU A1005    15249  20882  16790   1211  -1775  -2345       O  
ATOM   1639  OE2 GLU A1005       4.700  -9.264 -22.715  1.00138.35           O  
ANISOU 1639  OE2 GLU A1005    15162  20425  16979   1340  -2114  -2320       O  
ATOM   1640  N   MET A1006       9.667 -12.668 -21.874  1.00 96.82           N  
ANISOU 1640  N   MET A1006    10648  15689  10451    925  -1342  -1499       N  
ATOM   1641  CA  MET A1006      10.957 -12.848 -22.546  1.00 94.98           C  
ANISOU 1641  CA  MET A1006    10596  15377  10117    874  -1336  -1265       C  
ATOM   1642  C   MET A1006      10.905 -14.111 -23.401  1.00 98.18           C  
ANISOU 1642  C   MET A1006    11112  15824  10370    804  -1264  -1108       C  
ATOM   1643  O   MET A1006      11.297 -14.086 -24.571  1.00 97.65           O  
ANISOU 1643  O   MET A1006    11177  15648  10276    774  -1323   -951       O  
ATOM   1644  CB  MET A1006      12.092 -12.970 -21.513  1.00 96.44           C  
ANISOU 1644  CB  MET A1006    10792  15646  10204    841  -1225  -1268       C  
ATOM   1645  CG  MET A1006      13.472 -13.008 -22.135  1.00 98.95           C  
ANISOU 1645  CG  MET A1006    11245  15864  10487    795  -1217  -1076       C  
ATOM   1646  SD  MET A1006      14.616 -14.129 -21.303  1.00101.78           S  
ANISOU 1646  SD  MET A1006    11643  16345  10685    727  -1071  -1011       S  
ATOM   1647  CE  MET A1006      16.096 -13.759 -22.196  1.00 98.12           C  
ANISOU 1647  CE  MET A1006    11274  15716  10292    692  -1081   -859       C  
ATOM   1648  N   LEU A1007      10.420 -15.210 -22.808  1.00 94.52           N  
ANISOU 1648  N   LEU A1007    10596  15517   9799    764  -1131  -1156       N  
ATOM   1649  CA  LEU A1007      10.318 -16.501 -23.471  1.00 93.75           C  
ANISOU 1649  CA  LEU A1007    10575  15458   9588    699  -1061  -1041       C  
ATOM   1650  C   LEU A1007       9.167 -16.633 -24.468  1.00 98.42           C  
ANISOU 1650  C   LEU A1007    11152  16000  10243    719  -1161  -1060       C  
ATOM   1651  O   LEU A1007       9.223 -17.514 -25.328  1.00 97.71           O  
ANISOU 1651  O   LEU A1007    11155  15903  10068    671  -1141   -958       O  
ATOM   1652  CB  LEU A1007      10.329 -17.628 -22.447  1.00 93.48           C  
ANISOU 1652  CB  LEU A1007    10503  15581   9435    632   -905  -1053       C  
ATOM   1653  CG  LEU A1007      11.702 -18.201 -22.189  1.00 97.53           C  
ANISOU 1653  CG  LEU A1007    11109  16091   9855    582   -838   -921       C  
ATOM   1654  CD1 LEU A1007      12.375 -17.530 -21.002  1.00 98.16           C  
ANISOU 1654  CD1 LEU A1007    11160  16215   9920    595   -835   -979       C  
ATOM   1655  CD2 LEU A1007      11.617 -19.662 -21.974  1.00 99.84           C  
ANISOU 1655  CD2 LEU A1007    11418  16456  10062    505   -745   -849       C  
ATOM   1656  N   ARG A1008       8.142 -15.756 -24.377  1.00 95.99           N  
ANISOU 1656  N   ARG A1008    10720  15646  10105    795  -1287  -1209       N  
ATOM   1657  CA  ARG A1008       7.028 -15.747 -25.327  1.00 96.72           C  
ANISOU 1657  CA  ARG A1008    10786  15660  10303    828  -1441  -1238       C  
ATOM   1658  C   ARG A1008       7.542 -15.214 -26.677  1.00100.63           C  
ANISOU 1658  C   ARG A1008    11471  15994  10770    823  -1614  -1057       C  
ATOM   1659  O   ARG A1008       7.174 -15.735 -27.731  1.00100.85           O  
ANISOU 1659  O   ARG A1008    11593  15993  10734    792  -1691   -978       O  
ATOM   1660  CB  ARG A1008       5.843 -14.908 -24.802  1.00 98.90           C  
ANISOU 1660  CB  ARG A1008    10844  15908  10825    917  -1546  -1474       C  
ATOM   1661  CG  ARG A1008       4.664 -14.885 -25.775  1.00111.48           C  
ANISOU 1661  CG  ARG A1008    12390  17395  12574    963  -1750  -1514       C  
ATOM   1662  CD  ARG A1008       3.339 -14.484 -25.170  1.00122.92           C  
ANISOU 1662  CD  ARG A1008    13562  18849  14294   1036  -1797  -1799       C  
ATOM   1663  NE  ARG A1008       2.286 -14.552 -26.186  1.00132.09           N  
ANISOU 1663  NE  ARG A1008    14682  19888  15617   1080  -2027  -1821       N  
ATOM   1664  CZ  ARG A1008       1.064 -14.050 -26.049  1.00148.47           C  
ANISOU 1664  CZ  ARG A1008    16513  21889  18011   1166  -2167  -2062       C  
ATOM   1665  NH1 ARG A1008       0.719 -13.426 -24.927  1.00135.68           N  
ANISOU 1665  NH1 ARG A1008    14657  20319  16577   1212  -2072  -2328       N  
ATOM   1666  NH2 ARG A1008       0.181 -14.158 -27.029  1.00137.98           N  
ANISOU 1666  NH2 ARG A1008    15163  20434  16828   1206  -2411  -2062       N  
ATOM   1667  N   ILE A1009       8.420 -14.198 -26.623  1.00 96.57           N  
ANISOU 1667  N   ILE A1009    11020  15383  10288    836  -1667   -992       N  
ATOM   1668  CA  ILE A1009       9.050 -13.578 -27.787  1.00 96.73           C  
ANISOU 1668  CA  ILE A1009    11234  15256  10263    795  -1802   -800       C  
ATOM   1669  C   ILE A1009      10.033 -14.565 -28.448  1.00100.39           C  
ANISOU 1669  C   ILE A1009    11868  15794  10481    680  -1634   -647       C  
ATOM   1670  O   ILE A1009      10.079 -14.652 -29.676  1.00100.68           O  
ANISOU 1670  O   ILE A1009    12070  15781  10403    612  -1711   -518       O  
ATOM   1671  CB  ILE A1009       9.704 -12.220 -27.377  1.00100.14           C  
ANISOU 1671  CB  ILE A1009    11651  15560  10840    831  -1885   -794       C  
ATOM   1672  CG1 ILE A1009       8.608 -11.186 -27.002  1.00101.95           C  
ANISOU 1672  CG1 ILE A1009    11706  15670  11362    951  -2104   -966       C  
ATOM   1673  CG2 ILE A1009      10.638 -11.670 -28.469  1.00101.66           C  
ANISOU 1673  CG2 ILE A1009    12061  15619  10944    740  -1957   -562       C  
ATOM   1674  CD1 ILE A1009       9.060  -9.937 -26.244  1.00108.53           C  
ANISOU 1674  CD1 ILE A1009    12446  16394  12397   1012  -2168  -1055       C  
ATOM   1675  N   ASP A1010      10.782 -15.325 -27.630  1.00 96.45           N  
ANISOU 1675  N   ASP A1010    11322  15413   9910    654  -1417   -675       N  
ATOM   1676  CA  ASP A1010      11.789 -16.274 -28.107  1.00 95.71           C  
ANISOU 1676  CA  ASP A1010    11338  15372   9654    560  -1253   -578       C  
ATOM   1677  C   ASP A1010      11.262 -17.678 -28.475  1.00 99.66           C  
ANISOU 1677  C   ASP A1010    11839  15964  10064    525  -1178   -602       C  
ATOM   1678  O   ASP A1010      11.455 -18.108 -29.615  1.00 99.48           O  
ANISOU 1678  O   ASP A1010    11944  15931   9922    455  -1171   -536       O  
ATOM   1679  CB  ASP A1010      12.993 -16.341 -27.139  1.00 96.57           C  
ANISOU 1679  CB  ASP A1010    11401  15514   9778    550  -1108   -583       C  
ATOM   1680  CG  ASP A1010      13.716 -15.020 -26.883  1.00106.77           C  
ANISOU 1680  CG  ASP A1010    12698  16703  11168    568  -1170   -559       C  
ATOM   1681  OD1 ASP A1010      13.628 -14.112 -27.740  1.00108.53           O  
ANISOU 1681  OD1 ASP A1010    13012  16807  11416    550  -1298   -478       O  
ATOM   1682  OD2 ASP A1010      14.394 -14.907 -25.838  1.00111.76           O  
ANISOU 1682  OD2 ASP A1010    13251  17363  11850    591  -1106   -611       O  
ATOM   1683  N   GLU A1011      10.614 -18.388 -27.527  1.00 96.27           N  
ANISOU 1683  N   GLU A1011    11271  15625   9681    557  -1116   -702       N  
ATOM   1684  CA  GLU A1011      10.108 -19.747 -27.756  1.00 96.10           C  
ANISOU 1684  CA  GLU A1011    11229  15671   9613    519  -1047   -725       C  
ATOM   1685  C   GLU A1011       8.745 -19.817 -28.447  1.00101.22           C  
ANISOU 1685  C   GLU A1011    11853  16304  10303    543  -1185   -784       C  
ATOM   1686  O   GLU A1011       8.491 -20.774 -29.180  1.00101.02           O  
ANISOU 1686  O   GLU A1011    11869  16295  10218    499  -1171   -781       O  
ATOM   1687  CB  GLU A1011      10.130 -20.583 -26.465  1.00 96.89           C  
ANISOU 1687  CB  GLU A1011    11216  15864   9733    505   -915   -765       C  
ATOM   1688  CG  GLU A1011      10.439 -22.054 -26.704  1.00108.11           C  
ANISOU 1688  CG  GLU A1011    12658  17306  11113    439   -814   -726       C  
ATOM   1689  CD  GLU A1011      11.619 -22.611 -25.930  1.00129.98           C  
ANISOU 1689  CD  GLU A1011    15428  20081  13878    406   -712   -666       C  
ATOM   1690  OE1 GLU A1011      12.683 -22.836 -26.552  1.00122.06           O  
ANISOU 1690  OE1 GLU A1011    14492  19020  12867    382   -672   -625       O  
ATOM   1691  OE2 GLU A1011      11.470 -22.851 -24.710  1.00125.74           O  
ANISOU 1691  OE2 GLU A1011    14822  19606  13346    394   -677   -667       O  
ATOM   1692  N   GLY A1012       7.887 -18.825 -28.203  1.00 98.58           N  
ANISOU 1692  N   GLY A1012    11434  15927  10096    616  -1328   -860       N  
ATOM   1693  CA  GLY A1012       6.554 -18.757 -28.796  1.00 99.50           C  
ANISOU 1693  CA  GLY A1012    11493  16000  10311    655  -1502   -938       C  
ATOM   1694  C   GLY A1012       5.466 -19.428 -27.982  1.00103.36           C  
ANISOU 1694  C   GLY A1012    11777  16576  10917    668  -1429  -1093       C  
ATOM   1695  O   GLY A1012       5.681 -20.506 -27.418  1.00101.99           O  
ANISOU 1695  O   GLY A1012    11572  16501  10679    606  -1244  -1088       O  
ATOM   1696  N   LEU A1013       4.282 -18.790 -27.927  1.00101.45           N  
ANISOU 1696  N   LEU A1013    11388  16284  10873    741  -1582  -1235       N  
ATOM   1697  CA  LEU A1013       3.110 -19.293 -27.204  1.00102.01           C  
ANISOU 1697  CA  LEU A1013    11231  16436  11093    742  -1508  -1419       C  
ATOM   1698  C   LEU A1013       2.058 -19.854 -28.169  1.00106.47           C  
ANISOU 1698  C   LEU A1013    11759  16946  11748    748  -1658  -1467       C  
ATOM   1699  O   LEU A1013       1.506 -19.117 -28.989  1.00107.33           O  
ANISOU 1699  O   LEU A1013    11880  16925  11978    819  -1925  -1489       O  
ATOM   1700  CB  LEU A1013       2.510 -18.197 -26.297  1.00103.32           C  
ANISOU 1700  CB  LEU A1013    11194  16595  11466    819  -1538  -1614       C  
ATOM   1701  CG  LEU A1013       1.198 -18.530 -25.584  1.00109.44           C  
ANISOU 1701  CG  LEU A1013    11698  17454  12428    811  -1452  -1854       C  
ATOM   1702  CD1 LEU A1013       1.322 -18.342 -24.091  1.00109.72           C  
ANISOU 1702  CD1 LEU A1013    11605  17645  12437    769  -1216  -1986       C  
ATOM   1703  CD2 LEU A1013       0.059 -17.686 -26.121  1.00114.27           C  
ANISOU 1703  CD2 LEU A1013    12147  17920  13351    922  -1716  -2027       C  
ATOM   1704  N   ARG A1014       1.786 -21.161 -28.048  1.00102.15           N  
ANISOU 1704  N   ARG A1014    11168  16485  11158    669  -1510  -1479       N  
ATOM   1705  CA  ARG A1014       0.791 -21.892 -28.832  1.00102.67           C  
ANISOU 1705  CA  ARG A1014    11175  16515  11321    660  -1622  -1548       C  
ATOM   1706  C   ARG A1014      -0.207 -22.546 -27.876  1.00106.47           C  
ANISOU 1706  C   ARG A1014    11401  17087  11966    612  -1457  -1715       C  
ATOM   1707  O   ARG A1014       0.159 -23.416 -27.083  1.00104.50           O  
ANISOU 1707  O   ARG A1014    11142  16945  11619    512  -1217  -1665       O  
ATOM   1708  CB  ARG A1014       1.438 -22.892 -29.822  1.00102.07           C  
ANISOU 1708  CB  ARG A1014    11300  16432  11050    595  -1616  -1410       C  
ATOM   1709  CG  ARG A1014       2.612 -23.699 -29.266  1.00112.40           C  
ANISOU 1709  CG  ARG A1014    12696  17820  12190    512  -1369  -1292       C  
ATOM   1710  CD  ARG A1014       3.509 -24.229 -30.368  1.00124.14           C  
ANISOU 1710  CD  ARG A1014    14394  19276  13498    472  -1389  -1183       C  
ATOM   1711  NE  ARG A1014       4.751 -24.792 -29.836  1.00134.26           N  
ANISOU 1711  NE  ARG A1014    15741  20598  14672    416  -1187  -1085       N  
ATOM   1712  CZ  ARG A1014       5.880 -24.106 -29.677  1.00150.76           C  
ANISOU 1712  CZ  ARG A1014    17939  22685  16659    425  -1141   -992       C  
ATOM   1713  NH1 ARG A1014       6.958 -24.697 -29.182  1.00139.24           N  
ANISOU 1713  NH1 ARG A1014    16511  21246  15149    380   -984   -923       N  
ATOM   1714  NH2 ARG A1014       5.938 -22.822 -30.010  1.00138.36           N  
ANISOU 1714  NH2 ARG A1014    16435  21070  15066    478  -1272   -968       N  
ATOM   1715  N   LEU A1015      -1.457 -22.064 -27.907  1.00105.13           N  
ANISOU 1715  N   LEU A1015    11017  16867  12062    675  -1592  -1914       N  
ATOM   1716  CA  LEU A1015      -2.539 -22.522 -27.029  1.00106.19           C  
ANISOU 1716  CA  LEU A1015    10869  17089  12392    619  -1428  -2117       C  
ATOM   1717  C   LEU A1015      -3.147 -23.881 -27.406  1.00109.72           C  
ANISOU 1717  C   LEU A1015    11258  17545  12884    531  -1381  -2126       C  
ATOM   1718  O   LEU A1015      -3.869 -24.477 -26.603  1.00110.19           O  
ANISOU 1718  O   LEU A1015    11112  17695  13059    436  -1183  -2248       O  
ATOM   1719  CB  LEU A1015      -3.610 -21.424 -26.864  1.00108.48           C  
ANISOU 1719  CB  LEU A1015    10904  17309  13005    725  -1579  -2373       C  
ATOM   1720  CG  LEU A1015      -3.141 -20.102 -26.221  1.00113.21           C  
ANISOU 1720  CG  LEU A1015    11491  17903  13622    802  -1586  -2425       C  
ATOM   1721  CD1 LEU A1015      -4.282 -19.115 -26.113  1.00115.99           C  
ANISOU 1721  CD1 LEU A1015    11551  18156  14363    913  -1755  -2718       C  
ATOM   1722  CD2 LEU A1015      -2.507 -20.328 -24.848  1.00114.52           C  
ANISOU 1722  CD2 LEU A1015    11654  18265  13592    694  -1240  -2415       C  
ATOM   1723  N   LYS A1016      -2.826 -24.375 -28.613  1.00105.04           N  
ANISOU 1723  N   LYS A1016    10852  16865  12192    545  -1551  -2003       N  
ATOM   1724  CA  LYS A1016      -3.257 -25.674 -29.133  1.00104.89           C  
ANISOU 1724  CA  LYS A1016    10810  16833  12211    471  -1542  -2010       C  
ATOM   1725  C   LYS A1016      -2.016 -26.556 -29.339  1.00106.36           C  
ANISOU 1725  C   LYS A1016    11231  17046  12134    398  -1420  -1806       C  
ATOM   1726  O   LYS A1016      -0.911 -26.022 -29.465  1.00104.20           O  
ANISOU 1726  O   LYS A1016    11154  16776  11662    428  -1422  -1670       O  
ATOM   1727  CB  LYS A1016      -4.038 -25.509 -30.451  1.00108.70           C  
ANISOU 1727  CB  LYS A1016    11291  17185  12826    554  -1879  -2096       C  
ATOM   1728  CG  LYS A1016      -5.464 -25.014 -30.264  1.00122.44           C  
ANISOU 1728  CG  LYS A1016    12726  18869  14924    614  -2008  -2341       C  
ATOM   1729  CD  LYS A1016      -6.249 -25.025 -31.570  1.00132.50           C  
ANISOU 1729  CD  LYS A1016    14003  20004  16339    686  -2376  -2416       C  
ATOM   1730  CE  LYS A1016      -7.719 -24.752 -31.354  1.00142.33           C  
ANISOU 1730  CE  LYS A1016    14895  21179  18007    739  -2497  -2690       C  
ATOM   1731  NZ  LYS A1016      -8.509 -24.976 -32.595  1.00150.81           N  
ANISOU 1731  NZ  LYS A1016    15962  22114  19226    794  -2867  -2765       N  
ATOM   1732  N   ILE A1017      -2.191 -27.896 -29.352  1.00103.05           N  
ANISOU 1732  N   ILE A1017    10771  16632  11753    299  -1315  -1797       N  
ATOM   1733  CA  ILE A1017      -1.091 -28.852 -29.546  1.00101.44           C  
ANISOU 1733  CA  ILE A1017    10742  16423  11377    234  -1215  -1643       C  
ATOM   1734  C   ILE A1017      -0.480 -28.729 -30.959  1.00105.87           C  
ANISOU 1734  C   ILE A1017    11518  16921  11786    293  -1402  -1607       C  
ATOM   1735  O   ILE A1017      -1.178 -28.924 -31.956  1.00106.68           O  
ANISOU 1735  O   ILE A1017    11612  16968  11955    318  -1592  -1707       O  
ATOM   1736  CB  ILE A1017      -1.485 -30.321 -29.170  1.00104.90           C  
ANISOU 1736  CB  ILE A1017    11063  16850  11943    109  -1077  -1648       C  
ATOM   1737  CG1 ILE A1017      -1.770 -30.463 -27.649  1.00105.50           C  
ANISOU 1737  CG1 ILE A1017    10996  17021  12069     -1   -840  -1619       C  
ATOM   1738  CG2 ILE A1017      -0.407 -31.321 -29.626  1.00104.66           C  
ANISOU 1738  CG2 ILE A1017    11196  16766  11806     68  -1043  -1532       C  
ATOM   1739  CD1 ILE A1017      -2.260 -31.868 -27.147  1.00112.01           C  
ANISOU 1739  CD1 ILE A1017    11700  17826  13032   -162   -698  -1593       C  
ATOM   1740  N   TYR A1018       0.818 -28.380 -31.025  1.00101.78           N  
ANISOU 1740  N   TYR A1018    11193  16422  11059    302  -1344  -1475       N  
ATOM   1741  CA  TYR A1018       1.591 -28.252 -32.262  1.00101.93           C  
ANISOU 1741  CA  TYR A1018    11431  16412  10887    320  -1452  -1433       C  
ATOM   1742  C   TYR A1018       2.829 -29.154 -32.195  1.00104.94           C  
ANISOU 1742  C   TYR A1018    11901  16799  11172    256  -1274  -1358       C  
ATOM   1743  O   TYR A1018       2.964 -29.913 -31.235  1.00104.35           O  
ANISOU 1743  O   TYR A1018    11724  16725  11200    205  -1121  -1321       O  
ATOM   1744  CB  TYR A1018       1.979 -26.781 -32.521  1.00103.56           C  
ANISOU 1744  CB  TYR A1018    11767  16616  10964    386  -1567  -1364       C  
ATOM   1745  CG  TYR A1018       0.891 -25.973 -33.202  1.00108.07           C  
ANISOU 1745  CG  TYR A1018    12316  17130  11617    454  -1847  -1440       C  
ATOM   1746  CD1 TYR A1018       0.008 -25.192 -32.462  1.00110.73           C  
ANISOU 1746  CD1 TYR A1018    12466  17445  12162    521  -1910  -1517       C  
ATOM   1747  CD2 TYR A1018       0.745 -25.989 -34.587  1.00110.43           C  
ANISOU 1747  CD2 TYR A1018    12776  17391  11790    446  -2062  -1448       C  
ATOM   1748  CE1 TYR A1018      -1.003 -24.458 -33.082  1.00113.44           C  
ANISOU 1748  CE1 TYR A1018    12760  17699  12641    596  -2206  -1601       C  
ATOM   1749  CE2 TYR A1018      -0.264 -25.263 -35.217  1.00113.29           C  
ANISOU 1749  CE2 TYR A1018    13127  17677  12242    509  -2373  -1501       C  
ATOM   1750  CZ  TYR A1018      -1.132 -24.493 -34.460  1.00121.65           C  
ANISOU 1750  CZ  TYR A1018    13977  18683  13561    592  -2457  -1576       C  
ATOM   1751  OH  TYR A1018      -2.122 -23.766 -35.077  1.00125.40           O  
ANISOU 1751  OH  TYR A1018    14416  19048  14182    667  -2801  -1639       O  
ATOM   1752  N   LYS A1019       3.711 -29.103 -33.217  1.00101.27           N  
ANISOU 1752  N   LYS A1019    11622  16332  10525    247  -1301  -1342       N  
ATOM   1753  CA  LYS A1019       4.937 -29.905 -33.271  1.00100.14           C  
ANISOU 1753  CA  LYS A1019    11538  16178  10331    196  -1141  -1317       C  
ATOM   1754  C   LYS A1019       6.188 -29.009 -33.300  1.00103.06           C  
ANISOU 1754  C   LYS A1019    12051  16577  10529    203  -1071  -1219       C  
ATOM   1755  O   LYS A1019       7.210 -29.340 -33.903  1.00102.80           O  
ANISOU 1755  O   LYS A1019    12113  16546  10402    162   -985  -1241       O  
ATOM   1756  CB  LYS A1019       4.890 -30.905 -34.443  1.00103.48           C  
ANISOU 1756  CB  LYS A1019    12004  16580  10735    153  -1182  -1453       C  
ATOM   1757  CG  LYS A1019       4.075 -32.157 -34.135  1.00113.57           C  
ANISOU 1757  CG  LYS A1019    13106  17794  12250    125  -1181  -1537       C  
ATOM   1758  CD  LYS A1019       3.690 -32.907 -35.399  1.00123.07           C  
ANISOU 1758  CD  LYS A1019    14342  18979  13440     99  -1286  -1709       C  
ATOM   1759  CE  LYS A1019       2.208 -33.182 -35.475  1.00136.01           C  
ANISOU 1759  CE  LYS A1019    15846  20586  15246    110  -1439  -1799       C  
ATOM   1760  NZ  LYS A1019       1.415 -31.944 -35.717  1.00147.42           N  
ANISOU 1760  NZ  LYS A1019    17332  22070  16610    168  -1623  -1779       N  
ATOM   1761  N   GLY A1023      10.772 -32.224 -33.942  1.00105.27           N  
ANISOU 1761  N   GLY A1023    12297  16692  11007     57   -545  -1435       N  
ATOM   1762  CA  GLY A1023       9.387 -31.790 -34.071  1.00105.14           C  
ANISOU 1762  CA  GLY A1023    12312  16729  10907     74   -683  -1403       C  
ATOM   1763  C   GLY A1023       8.390 -32.730 -33.421  1.00108.54           C  
ANISOU 1763  C   GLY A1023    12595  17092  11554     78   -742  -1402       C  
ATOM   1764  O   GLY A1023       7.695 -33.478 -34.118  1.00108.89           O  
ANISOU 1764  O   GLY A1023    12606  17114  11654     57   -806  -1533       O  
ATOM   1765  N   TYR A1024       8.308 -32.684 -32.074  1.00103.89           N  
ANISOU 1765  N   TYR A1024    11921  16474  11077     89   -719  -1255       N  
ATOM   1766  CA  TYR A1024       7.419 -33.526 -31.257  1.00103.81           C  
ANISOU 1766  CA  TYR A1024    11776  16408  11258     56   -742  -1214       C  
ATOM   1767  C   TYR A1024       6.248 -32.712 -30.686  1.00106.25           C  
ANISOU 1767  C   TYR A1024    12049  16802  11520     69   -789  -1162       C  
ATOM   1768  O   TYR A1024       6.341 -31.486 -30.651  1.00105.42           O  
ANISOU 1768  O   TYR A1024    12016  16773  11267    117   -807  -1126       O  
ATOM   1769  CB  TYR A1024       8.212 -34.198 -30.116  1.00104.96           C  
ANISOU 1769  CB  TYR A1024    11862  16463  11553     23   -678  -1084       C  
ATOM   1770  CG  TYR A1024       9.567 -34.745 -30.521  1.00107.39           C  
ANISOU 1770  CG  TYR A1024    12182  16676  11947     32   -636  -1143       C  
ATOM   1771  CD1 TYR A1024      10.743 -34.185 -30.028  1.00108.69           C  
ANISOU 1771  CD1 TYR A1024    12388  16839  12071     58   -588  -1062       C  
ATOM   1772  CD2 TYR A1024       9.674 -35.824 -31.396  1.00109.57           C  
ANISOU 1772  CD2 TYR A1024    12403  16855  12375     15   -646  -1311       C  
ATOM   1773  CE1 TYR A1024      11.993 -34.686 -30.394  1.00110.19           C  
ANISOU 1773  CE1 TYR A1024    12549  16930  12387     67   -545  -1149       C  
ATOM   1774  CE2 TYR A1024      10.918 -36.326 -31.779  1.00111.20           C  
ANISOU 1774  CE2 TYR A1024    12582  16969  12699     25   -595  -1416       C  
ATOM   1775  CZ  TYR A1024      12.075 -35.757 -31.270  1.00118.10           C  
ANISOU 1775  CZ  TYR A1024    13483  17839  13550     51   -541  -1335       C  
ATOM   1776  OH  TYR A1024      13.303 -36.252 -31.634  1.00119.66           O  
ANISOU 1776  OH  TYR A1024    13617  17935  13912     61   -486  -1467       O  
ATOM   1777  N   TYR A1025       5.157 -33.385 -30.234  1.00102.45           N  
ANISOU 1777  N   TYR A1025    11438  16296  11192     21   -804  -1172       N  
ATOM   1778  CA  TYR A1025       3.957 -32.743 -29.666  1.00102.17           C  
ANISOU 1778  CA  TYR A1025    11314  16337  11167     20   -823  -1174       C  
ATOM   1779  C   TYR A1025       4.283 -31.730 -28.554  1.00104.23           C  
ANISOU 1779  C   TYR A1025    11596  16685  11321     33   -749  -1064       C  
ATOM   1780  O   TYR A1025       4.884 -32.096 -27.543  1.00103.57           O  
ANISOU 1780  O   TYR A1025    11513  16596  11242    -24   -657   -937       O  
ATOM   1781  CB  TYR A1025       2.917 -33.785 -29.210  1.00104.66           C  
ANISOU 1781  CB  TYR A1025    11470  16608  11688    -71   -799  -1194       C  
ATOM   1782  CG  TYR A1025       2.291 -34.578 -30.340  1.00107.67           C  
ANISOU 1782  CG  TYR A1025    11803  16913  12196    -71   -905  -1349       C  
ATOM   1783  CD1 TYR A1025       2.470 -35.955 -30.436  1.00110.49           C  
ANISOU 1783  CD1 TYR A1025    12106  17145  12728   -139   -889  -1356       C  
ATOM   1784  CD2 TYR A1025       1.504 -33.955 -31.305  1.00109.05           C  
ANISOU 1784  CD2 TYR A1025    11981  17122  12330     -4  -1048  -1492       C  
ATOM   1785  CE1 TYR A1025       1.886 -36.692 -31.468  1.00112.50           C  
ANISOU 1785  CE1 TYR A1025    12307  17328  13109   -139   -992  -1527       C  
ATOM   1786  CE2 TYR A1025       0.926 -34.679 -32.348  1.00111.29           C  
ANISOU 1786  CE2 TYR A1025    12230  17344  12713     -8  -1168  -1646       C  
ATOM   1787  CZ  TYR A1025       1.109 -36.050 -32.420  1.00119.10           C  
ANISOU 1787  CZ  TYR A1025    13158  18225  13870    -75  -1128  -1676       C  
ATOM   1788  OH  TYR A1025       0.531 -36.766 -33.443  1.00120.62           O  
ANISOU 1788  OH  TYR A1025    13306  18354  14169    -79  -1252  -1855       O  
ATOM   1789  N   THR A1026       3.939 -30.445 -28.785  1.00 99.83           N  
ANISOU 1789  N   THR A1026    11063  16194  10672    110   -816  -1114       N  
ATOM   1790  CA  THR A1026       4.244 -29.316 -27.893  1.00 98.61           C  
ANISOU 1790  CA  THR A1026    10924  16116  10426    141   -770  -1057       C  
ATOM   1791  C   THR A1026       3.003 -28.430 -27.590  1.00102.99           C  
ANISOU 1791  C   THR A1026    11352  16732  11047    176   -815  -1168       C  
ATOM   1792  O   THR A1026       2.077 -28.355 -28.398  1.00103.16           O  
ANISOU 1792  O   THR A1026    11316  16720  11159    213   -943  -1282       O  
ATOM   1793  CB  THR A1026       5.454 -28.528 -28.461  1.00102.80           C  
ANISOU 1793  CB  THR A1026    11617  16630  10811    206   -805  -1006       C  
ATOM   1794  OG1 THR A1026       6.427 -29.446 -28.967  1.00101.71           O  
ANISOU 1794  OG1 THR A1026    11551  16426  10667    174   -766   -974       O  
ATOM   1795  CG2 THR A1026       6.120 -27.641 -27.436  1.00 99.15           C  
ANISOU 1795  CG2 THR A1026    11177  16220  10275    224   -742   -929       C  
ATOM   1796  N   ILE A1027       2.998 -27.779 -26.412  1.00 99.75           N  
ANISOU 1796  N   ILE A1027    10887  16408  10607    163   -720  -1154       N  
ATOM   1797  CA  ILE A1027       1.936 -26.886 -25.928  1.00100.81           C  
ANISOU 1797  CA  ILE A1027    10867  16607  10831    194   -729  -1298       C  
ATOM   1798  C   ILE A1027       2.559 -25.661 -25.208  1.00104.97           C  
ANISOU 1798  C   ILE A1027    11433  17190  11260    247   -703  -1288       C  
ATOM   1799  O   ILE A1027       3.674 -25.764 -24.692  1.00103.62           O  
ANISOU 1799  O   ILE A1027    11377  17040  10953    217   -628  -1156       O  
ATOM   1800  CB  ILE A1027       0.912 -27.681 -25.041  1.00105.28           C  
ANISOU 1800  CB  ILE A1027    11249  17247  11505     68   -577  -1362       C  
ATOM   1801  CG1 ILE A1027      -0.411 -26.913 -24.819  1.00107.10           C  
ANISOU 1801  CG1 ILE A1027    11261  17526  11906    101   -591  -1585       C  
ATOM   1802  CG2 ILE A1027       1.516 -28.156 -23.708  1.00105.92           C  
ANISOU 1802  CG2 ILE A1027    11371  17423  11451    -61   -384  -1227       C  
ATOM   1803  CD1 ILE A1027      -1.535 -27.221 -25.781  1.00113.81           C  
ANISOU 1803  CD1 ILE A1027    11981  18289  12971    136   -734  -1724       C  
ATOM   1804  N   GLY A1028       1.845 -24.528 -25.212  1.00102.95           N  
ANISOU 1804  N   GLY A1028    11070  16937  11110    330   -790  -1439       N  
ATOM   1805  CA  GLY A1028       2.242 -23.278 -24.561  1.00102.99           C  
ANISOU 1805  CA  GLY A1028    11073  16978  11082    391   -789  -1481       C  
ATOM   1806  C   GLY A1028       3.640 -22.782 -24.869  1.00106.12           C  
ANISOU 1806  C   GLY A1028    11670  17318  11333    437   -843  -1328       C  
ATOM   1807  O   GLY A1028       4.085 -22.846 -26.020  1.00105.31           O  
ANISOU 1807  O   GLY A1028    11703  17117  11194    471   -963  -1240       O  
ATOM   1808  N   ILE A1029       4.354 -22.299 -23.832  1.00102.68           N  
ANISOU 1808  N   ILE A1029    11253  16953  10806    423   -745  -1307       N  
ATOM   1809  CA  ILE A1029       5.729 -21.805 -23.980  1.00101.48           C  
ANISOU 1809  CA  ILE A1029    11262  16748  10547    459   -781  -1178       C  
ATOM   1810  C   ILE A1029       6.703 -23.000 -24.056  1.00103.85           C  
ANISOU 1810  C   ILE A1029    11684  17041  10735    382   -700  -1010       C  
ATOM   1811  O   ILE A1029       7.402 -23.314 -23.085  1.00103.64           O  
ANISOU 1811  O   ILE A1029    11685  17072  10622    326   -605   -939       O  
ATOM   1812  CB  ILE A1029       6.140 -20.734 -22.913  1.00105.03           C  
ANISOU 1812  CB  ILE A1029    11676  17255  10974    489   -748  -1245       C  
ATOM   1813  CG1 ILE A1029       5.006 -19.714 -22.592  1.00107.02           C  
ANISOU 1813  CG1 ILE A1029    11745  17526  11392    554   -799  -1473       C  
ATOM   1814  CG2 ILE A1029       7.483 -20.048 -23.269  1.00104.96           C  
ANISOU 1814  CG2 ILE A1029    11812  17154  10913    538   -819  -1130       C  
ATOM   1815  CD1 ILE A1029       4.951 -18.406 -23.448  1.00115.25           C  
ANISOU 1815  CD1 ILE A1029    12795  18407  12588    681  -1021  -1516       C  
ATOM   1816  N   GLY A1030       6.696 -23.664 -25.209  1.00 99.17           N  
ANISOU 1816  N   GLY A1030    11153  16369  10157    380   -755   -965       N  
ATOM   1817  CA  GLY A1030       7.549 -24.808 -25.510  1.00 97.97           C  
ANISOU 1817  CA  GLY A1030    11087  16177   9961    323   -699   -854       C  
ATOM   1818  C   GLY A1030       7.520 -25.957 -24.522  1.00101.05           C  
ANISOU 1818  C   GLY A1030    11427  16612  10354    226   -591   -794       C  
ATOM   1819  O   GLY A1030       8.582 -26.418 -24.096  1.00 99.99           O  
ANISOU 1819  O   GLY A1030    11356  16450  10185    193   -556   -687       O  
ATOM   1820  N   HIS A1031       6.315 -26.434 -24.150  1.00 98.37           N  
ANISOU 1820  N   HIS A1031    10973  16330  10073    169   -547   -857       N  
ATOM   1821  CA  HIS A1031       6.191 -27.563 -23.227  1.00 98.96           C  
ANISOU 1821  CA  HIS A1031    11015  16442  10142     42   -446   -771       C  
ATOM   1822  C   HIS A1031       6.102 -28.884 -23.988  1.00102.72           C  
ANISOU 1822  C   HIS A1031    11493  16812  10725     -1   -470   -730       C  
ATOM   1823  O   HIS A1031       5.065 -29.205 -24.576  1.00102.57           O  
ANISOU 1823  O   HIS A1031    11387  16779  10805     -7   -491   -827       O  
ATOM   1824  CB  HIS A1031       5.030 -27.386 -22.225  1.00101.24           C  
ANISOU 1824  CB  HIS A1031    11173  16868  10424    -39   -341   -859       C  
ATOM   1825  CG  HIS A1031       4.949 -28.479 -21.196  1.00105.79           C  
ANISOU 1825  CG  HIS A1031    11751  17496  10948   -208   -230   -732       C  
ATOM   1826  ND1 HIS A1031       5.639 -28.398 -19.997  1.00107.89           N  
ANISOU 1826  ND1 HIS A1031    12099  17844  11049   -287   -177   -619       N  
ATOM   1827  CD2 HIS A1031       4.269 -29.651 -21.229  1.00108.47           C  
ANISOU 1827  CD2 HIS A1031    12031  17802  11379   -323   -184   -690       C  
ATOM   1828  CE1 HIS A1031       5.366 -29.521 -19.351  1.00108.55           C  
ANISOU 1828  CE1 HIS A1031    12191  17942  11111   -455   -108   -488       C  
ATOM   1829  NE2 HIS A1031       4.542 -30.302 -20.048  1.00109.35           N  
ANISOU 1829  NE2 HIS A1031    12201  17970  11377   -484   -101   -525       N  
ATOM   1830  N   LEU A1032       7.211 -29.637 -23.979  1.00 99.25           N  
ANISOU 1830  N   LEU A1032    11135  16282  10293    -23   -481   -608       N  
ATOM   1831  CA  LEU A1032       7.327 -30.946 -24.619  1.00 99.59           C  
ANISOU 1831  CA  LEU A1032    11171  16199  10471    -61   -509   -584       C  
ATOM   1832  C   LEU A1032       6.516 -31.961 -23.812  1.00104.50           C  
ANISOU 1832  C   LEU A1032    11717  16826  11164   -199   -456   -510       C  
ATOM   1833  O   LEU A1032       6.826 -32.227 -22.647  1.00104.61           O  
ANISOU 1833  O   LEU A1032    11763  16868  11117   -294   -418   -365       O  
ATOM   1834  CB  LEU A1032       8.805 -31.387 -24.775  1.00 99.36           C  
ANISOU 1834  CB  LEU A1032    11218  16054  10482    -37   -543   -506       C  
ATOM   1835  CG  LEU A1032       9.881 -30.606 -23.987  1.00104.05           C  
ANISOU 1835  CG  LEU A1032    11881  16679  10974     -8   -544   -423       C  
ATOM   1836  CD1 LEU A1032       9.985 -31.079 -22.532  1.00105.00           C  
ANISOU 1836  CD1 LEU A1032    12013  16821  11060   -113   -541   -261       C  
ATOM   1837  CD2 LEU A1032      11.236 -30.710 -24.663  1.00107.19           C  
ANISOU 1837  CD2 LEU A1032    12319  16962  11445     53   -576   -439       C  
ATOM   1838  N   LEU A1033       5.433 -32.469 -24.414  1.00101.52           N  
ANISOU 1838  N   LEU A1033    11243  16427  10903   -224   -459   -608       N  
ATOM   1839  CA  LEU A1033       4.529 -33.421 -23.768  1.00102.74           C  
ANISOU 1839  CA  LEU A1033    11304  16579  11152   -372   -394   -554       C  
ATOM   1840  C   LEU A1033       5.064 -34.841 -23.861  1.00106.59           C  
ANISOU 1840  C   LEU A1033    11812  16890  11796   -442   -446   -435       C  
ATOM   1841  O   LEU A1033       5.325 -35.472 -22.835  1.00107.22           O  
ANISOU 1841  O   LEU A1033    11925  16941  11872   -569   -424   -248       O  
ATOM   1842  CB  LEU A1033       3.123 -33.342 -24.384  1.00103.51           C  
ANISOU 1842  CB  LEU A1033    11261  16710  11357   -366   -390   -733       C  
ATOM   1843  CG  LEU A1033       2.396 -32.024 -24.211  1.00108.07           C  
ANISOU 1843  CG  LEU A1033    11771  17432  11858   -306   -359   -872       C  
ATOM   1844  CD1 LEU A1033       2.182 -31.353 -25.538  1.00107.65           C  
ANISOU 1844  CD1 LEU A1033    11720  17338  11843   -154   -502  -1027       C  
ATOM   1845  CD2 LEU A1033       1.090 -32.234 -23.536  1.00112.03           C  
ANISOU 1845  CD2 LEU A1033    12103  18019  12443   -429   -242   -943       C  
ATOM   1846  N   THR A1034       5.219 -35.340 -25.097  1.00102.50           N  
ANISOU 1846  N   THR A1034    11276  16250  11420   -365   -528   -549       N  
ATOM   1847  CA  THR A1034       5.705 -36.686 -25.379  1.00103.01           C  
ANISOU 1847  CA  THR A1034    11326  16120  11695   -406   -593   -502       C  
ATOM   1848  C   THR A1034       6.445 -36.774 -26.727  1.00105.86           C  
ANISOU 1848  C   THR A1034    11711  16394  12117   -283   -661   -666       C  
ATOM   1849  O   THR A1034       6.109 -36.053 -27.670  1.00104.64           O  
ANISOU 1849  O   THR A1034    11572  16324  11863   -199   -671   -826       O  
ATOM   1850  CB  THR A1034       4.565 -37.725 -25.191  1.00111.19           C  
ANISOU 1850  CB  THR A1034    12244  17090  12912   -541   -578   -484       C  
ATOM   1851  OG1 THR A1034       5.116 -39.035 -25.103  1.00112.19           O  
ANISOU 1851  OG1 THR A1034    12361  17003  13262   -606   -654   -379       O  
ATOM   1852  CG2 THR A1034       3.487 -37.655 -26.280  1.00108.83           C  
ANISOU 1852  CG2 THR A1034    11844  16816  12692   -490   -601   -710       C  
ATOM   1853  N   LYS A1035       7.457 -37.657 -26.801  1.00102.70           N  
ANISOU 1853  N   LYS A1035    11315  15823  11885   -283   -714   -630       N  
ATOM   1854  CA  LYS A1035       8.233 -37.936 -28.011  1.00102.35           C  
ANISOU 1854  CA  LYS A1035    11267  15691  11929   -196   -746   -816       C  
ATOM   1855  C   LYS A1035       7.497 -39.019 -28.808  1.00108.47           C  
ANISOU 1855  C   LYS A1035    11942  16357  12915   -227   -794   -964       C  
ATOM   1856  O   LYS A1035       7.875 -39.321 -29.943  1.00108.37           O  
ANISOU 1856  O   LYS A1035    11915  16297  12962   -172   -810  -1173       O  
ATOM   1857  CB  LYS A1035       9.644 -38.428 -27.645  1.00104.70           C  
ANISOU 1857  CB  LYS A1035    11569  15835  12379   -180   -786   -747       C  
ATOM   1858  CG  LYS A1035      10.760 -37.627 -28.299  1.00112.98           C  
ANISOU 1858  CG  LYS A1035    12673  16937  13316    -82   -739   -868       C  
ATOM   1859  CD  LYS A1035      12.077 -38.402 -28.372  1.00120.73           C  
ANISOU 1859  CD  LYS A1035    13588  17723  14560    -54   -782   -918       C  
ATOM   1860  CE  LYS A1035      12.276 -39.066 -29.719  1.00128.23           C  
ANISOU 1860  CE  LYS A1035    14462  18601  15658    -24   -755  -1205       C  
ATOM   1861  NZ  LYS A1035      13.687 -39.489 -29.930  1.00132.22           N  
ANISOU 1861  NZ  LYS A1035    14885  18957  16398     20   -755  -1327       N  
ATOM   1862  N   SER A1036       6.440 -39.599 -28.191  1.00106.94           N  
ANISOU 1862  N   SER A1036    11674  16130  12830   -331   -805   -866       N  
ATOM   1863  CA  SER A1036       5.593 -40.668 -28.721  1.00108.80           C  
ANISOU 1863  CA  SER A1036    11792  16244  13301   -384   -857   -977       C  
ATOM   1864  C   SER A1036       4.846 -40.256 -29.990  1.00113.87           C  
ANISOU 1864  C   SER A1036    12420  16989  13855   -315   -877  -1229       C  
ATOM   1865  O   SER A1036       4.256 -39.174 -30.021  1.00112.45           O  
ANISOU 1865  O   SER A1036    12282  16983  13460   -281   -851  -1240       O  
ATOM   1866  CB  SER A1036       4.597 -41.136 -27.661  1.00113.20           C  
ANISOU 1866  CB  SER A1036    12281  16782  13949   -535   -832   -793       C  
ATOM   1867  OG  SER A1036       5.252 -41.553 -26.474  1.00121.64           O  
ANISOU 1867  OG  SER A1036    13396  17757  15066   -627   -842   -529       O  
ATOM   1868  N   PRO A1037       4.826 -41.109 -31.040  1.00112.87           N  
ANISOU 1868  N   PRO A1037    12233  16749  13902   -295   -945  -1441       N  
ATOM   1869  CA  PRO A1037       4.109 -40.735 -32.268  1.00113.45           C  
ANISOU 1869  CA  PRO A1037    12319  16927  13861   -242   -996  -1675       C  
ATOM   1870  C   PRO A1037       2.613 -41.072 -32.216  1.00119.48           C  
ANISOU 1870  C   PRO A1037    12958  17678  14760   -303  -1052  -1711       C  
ATOM   1871  O   PRO A1037       2.122 -41.866 -33.020  1.00120.31           O  
ANISOU 1871  O   PRO A1037    12980  17694  15037   -312  -1138  -1902       O  
ATOM   1872  CB  PRO A1037       4.877 -41.478 -33.374  1.00116.20           C  
ANISOU 1872  CB  PRO A1037    12664  17178  14307   -204  -1028  -1911       C  
ATOM   1873  CG  PRO A1037       5.702 -42.537 -32.661  1.00121.24           C  
ANISOU 1873  CG  PRO A1037    13217  17597  15251   -243  -1022  -1815       C  
ATOM   1874  CD  PRO A1037       5.462 -42.432 -31.181  1.00116.05           C  
ANISOU 1874  CD  PRO A1037    12552  16919  14624   -319   -997  -1495       C  
ATOM   1875  N   SER A1038       1.890 -40.458 -31.253  1.00116.71           N  
ANISOU 1875  N   SER A1038    12578  17421  14347   -350   -996  -1552       N  
ATOM   1876  CA  SER A1038       0.443 -40.626 -31.057  1.00118.39           C  
ANISOU 1876  CA  SER A1038    12643  17643  14698   -420  -1014  -1590       C  
ATOM   1877  C   SER A1038      -0.156 -39.398 -30.362  1.00122.38           C  
ANISOU 1877  C   SER A1038    13148  18326  15026   -414   -945  -1514       C  
ATOM   1878  O   SER A1038       0.292 -39.024 -29.273  1.00121.25           O  
ANISOU 1878  O   SER A1038    13052  18240  14776   -458   -829  -1322       O  
ATOM   1879  CB  SER A1038       0.138 -41.901 -30.267  1.00123.91           C  
ANISOU 1879  CB  SER A1038    13213  18172  15696   -570   -975  -1469       C  
ATOM   1880  OG  SER A1038      -1.159 -42.388 -30.575  1.00134.57           O  
ANISOU 1880  OG  SER A1038    14395  19476  17258   -630  -1023  -1602       O  
ATOM   1881  N   LEU A1039      -1.148 -38.754 -31.016  1.00119.86           N  
ANISOU 1881  N   LEU A1039    12772  18085  14686   -354  -1037  -1682       N  
ATOM   1882  CA  LEU A1039      -1.829 -37.547 -30.533  1.00119.54           C  
ANISOU 1882  CA  LEU A1039    12691  18188  14541   -325  -1008  -1679       C  
ATOM   1883  C   LEU A1039      -2.641 -37.791 -29.258  1.00125.30           C  
ANISOU 1883  C   LEU A1039    13251  18944  15412   -468   -849  -1594       C  
ATOM   1884  O   LEU A1039      -2.643 -36.932 -28.375  1.00123.92           O  
ANISOU 1884  O   LEU A1039    13083  18896  15105   -480   -736  -1518       O  
ATOM   1885  CB  LEU A1039      -2.706 -36.936 -31.648  1.00120.28           C  
ANISOU 1885  CB  LEU A1039    12750  18309  14643   -223  -1204  -1893       C  
ATOM   1886  CG  LEU A1039      -3.457 -35.627 -31.340  1.00124.86           C  
ANISOU 1886  CG  LEU A1039    13264  18997  15180   -163  -1235  -1938       C  
ATOM   1887  CD1 LEU A1039      -2.510 -34.438 -31.262  1.00123.12           C  
ANISOU 1887  CD1 LEU A1039    13232  18867  14681    -72  -1227  -1836       C  
ATOM   1888  CD2 LEU A1039      -4.523 -35.361 -32.379  1.00128.91           C  
ANISOU 1888  CD2 LEU A1039    13693  19478  15810    -88  -1474  -2148       C  
ATOM   1889  N   ASN A1040      -3.325 -38.952 -29.161  1.00124.85           N  
ANISOU 1889  N   ASN A1040    13043  18774  15620   -591   -830  -1618       N  
ATOM   1890  CA  ASN A1040      -4.124 -39.302 -27.982  1.00126.74           C  
ANISOU 1890  CA  ASN A1040    13124  19041  15991   -774   -652  -1531       C  
ATOM   1891  C   ASN A1040      -3.249 -39.551 -26.751  1.00131.31           C  
ANISOU 1891  C   ASN A1040    13822  19642  16429   -897   -493  -1250       C  
ATOM   1892  O   ASN A1040      -3.701 -39.325 -25.626  1.00131.93           O  
ANISOU 1892  O   ASN A1040    13839  19833  16454  -1038   -314  -1160       O  
ATOM   1893  CB  ASN A1040      -5.051 -40.476 -28.259  1.00130.19           C  
ANISOU 1893  CB  ASN A1040    13372  19333  16760   -887   -682  -1619       C  
ATOM   1894  CG  ASN A1040      -6.380 -40.318 -27.573  1.00158.45           C  
ANISOU 1894  CG  ASN A1040    16719  22992  20493  -1017   -544  -1693       C  
ATOM   1895  OD1 ASN A1040      -6.544 -40.655 -26.396  1.00154.22           O  
ANISOU 1895  OD1 ASN A1040    16139  22498  19959  -1216   -333  -1528       O  
ATOM   1896  ND2 ASN A1040      -7.345 -39.746 -28.279  1.00151.87           N  
ANISOU 1896  ND2 ASN A1040    15733  22188  19783   -916   -660  -1949       N  
ATOM   1897  N   ALA A1041      -1.988 -39.981 -26.974  1.00127.42           N  
ANISOU 1897  N   ALA A1041    13496  19045  15872   -847   -564  -1131       N  
ATOM   1898  CA  ALA A1041      -0.985 -40.202 -25.933  1.00127.16           C  
ANISOU 1898  CA  ALA A1041    13598  19000  15716   -933   -485   -863       C  
ATOM   1899  C   ALA A1041      -0.512 -38.842 -25.403  1.00129.86           C  
ANISOU 1899  C   ALA A1041    14051  19539  15753   -856   -414   -825       C  
ATOM   1900  O   ALA A1041      -0.206 -38.725 -24.214  1.00129.96           O  
ANISOU 1900  O   ALA A1041    14128  19627  15625   -971   -301   -633       O  
ATOM   1901  CB  ALA A1041       0.188 -40.985 -26.499  1.00127.43           C  
ANISOU 1901  CB  ALA A1041    13734  18846  15840   -868   -613   -818       C  
ATOM   1902  N   ALA A1042      -0.484 -37.809 -26.286  1.00125.06           N  
ANISOU 1902  N   ALA A1042    13470  19009  15041   -674   -496  -1006       N  
ATOM   1903  CA  ALA A1042      -0.120 -36.432 -25.940  1.00123.45           C  
ANISOU 1903  CA  ALA A1042    13348  18964  14591   -583   -457  -1005       C  
ATOM   1904  C   ALA A1042      -1.233 -35.783 -25.114  1.00128.50           C  
ANISOU 1904  C   ALA A1042    13847  19760  15220   -660   -324  -1071       C  
ATOM   1905  O   ALA A1042      -0.942 -34.942 -24.264  1.00127.53           O  
ANISOU 1905  O   ALA A1042    13773  19771  14910   -667   -228  -1016       O  
ATOM   1906  CB  ALA A1042       0.152 -35.621 -27.197  1.00122.82           C  
ANISOU 1906  CB  ALA A1042    13339  18889  14437   -394   -605  -1161       C  
ATOM   1907  N   LYS A1043      -2.500 -36.196 -25.349  1.00127.09           N  
ANISOU 1907  N   LYS A1043    13471  19558  15257   -724   -313  -1213       N  
ATOM   1908  CA  LYS A1043      -3.680 -35.723 -24.619  1.00128.69           C  
ANISOU 1908  CA  LYS A1043    13480  19895  15519   -816   -164  -1329       C  
ATOM   1909  C   LYS A1043      -3.634 -36.257 -23.181  1.00134.63           C  
ANISOU 1909  C   LYS A1043    14244  20729  16180  -1055     65  -1132       C  
ATOM   1910  O   LYS A1043      -3.858 -35.491 -22.243  1.00134.82           O  
ANISOU 1910  O   LYS A1043    14236  20933  16057  -1117    227  -1158       O  
ATOM   1911  CB  LYS A1043      -4.977 -36.173 -25.324  1.00132.93           C  
ANISOU 1911  CB  LYS A1043    13791  20357  16361   -829   -229  -1538       C  
ATOM   1912  CG  LYS A1043      -6.235 -35.440 -24.855  1.00149.68           C  
ANISOU 1912  CG  LYS A1043    15667  22604  18601   -866   -117  -1750       C  
ATOM   1913  CD  LYS A1043      -7.393 -36.396 -24.550  1.00160.36           C  
ANISOU 1913  CD  LYS A1043    16781  23923  20226  -1063     13  -1819       C  
ATOM   1914  CE  LYS A1043      -8.720 -35.692 -24.355  1.00169.46           C  
ANISOU 1914  CE  LYS A1043    17635  25170  21582  -1071     91  -2107       C  
ATOM   1915  NZ  LYS A1043      -8.773 -34.895 -23.098  1.00177.78           N  
ANISOU 1915  NZ  LYS A1043    18649  26438  22462  -1167    350  -2123       N  
ATOM   1916  N   SER A1044      -3.330 -37.569 -23.019  1.00132.38           N  
ANISOU 1916  N   SER A1044    14014  20306  15979  -1196     66   -937       N  
ATOM   1917  CA  SER A1044      -3.226 -38.252 -21.726  1.00134.05           C  
ANISOU 1917  CA  SER A1044    14279  20556  16099  -1453    237   -690       C  
ATOM   1918  C   SER A1044      -2.143 -37.611 -20.863  1.00136.89           C  
ANISOU 1918  C   SER A1044    14846  21031  16134  -1446    273   -517       C  
ATOM   1919  O   SER A1044      -2.354 -37.435 -19.666  1.00137.92           O  
ANISOU 1919  O   SER A1044    14996  21327  16080  -1633    460   -423       O  
ATOM   1920  CB  SER A1044      -2.946 -39.741 -21.925  1.00138.61           C  
ANISOU 1920  CB  SER A1044    14894  20897  16873  -1562    145   -505       C  
ATOM   1921  OG  SER A1044      -2.907 -40.438 -20.689  1.00149.09           O  
ANISOU 1921  OG  SER A1044    16289  22239  18117  -1836    280   -230       O  
ATOM   1922  N   GLU A1045      -1.003 -37.230 -21.482  1.00131.25           N  
ANISOU 1922  N   GLU A1045    14281  20243  15346  -1241    101   -496       N  
ATOM   1923  CA  GLU A1045       0.112 -36.561 -20.810  1.00129.91           C  
ANISOU 1923  CA  GLU A1045    14294  20157  14907  -1200     97   -362       C  
ATOM   1924  C   GLU A1045      -0.247 -35.115 -20.452  1.00133.24           C  
ANISOU 1924  C   GLU A1045    14667  20801  15157  -1128    201   -540       C  
ATOM   1925  O   GLU A1045       0.281 -34.585 -19.470  1.00132.68           O  
ANISOU 1925  O   GLU A1045    14703  20863  14845  -1182    276   -444       O  
ATOM   1926  CB  GLU A1045       1.385 -36.614 -21.669  1.00129.08           C  
ANISOU 1926  CB  GLU A1045    14322  19895  14829  -1011   -100   -324       C  
ATOM   1927  CG  GLU A1045       2.410 -37.626 -21.186  1.00140.43           C  
ANISOU 1927  CG  GLU A1045    15894  21175  16290  -1100   -182    -57       C  
ATOM   1928  CD  GLU A1045       3.255 -37.183 -20.008  1.00161.63           C  
ANISOU 1928  CD  GLU A1045    18737  23958  18717  -1162   -159    135       C  
ATOM   1929  OE1 GLU A1045       2.812 -37.374 -18.852  1.00157.51           O  
ANISOU 1929  OE1 GLU A1045    18242  23548  18055  -1376    -38    280       O  
ATOM   1930  OE2 GLU A1045       4.364 -36.652 -20.241  1.00154.05           O  
ANISOU 1930  OE2 GLU A1045    17875  22969  17689  -1010   -259    136       O  
ATOM   1931  N   LEU A1046      -1.154 -34.488 -21.239  1.00129.59           N  
ANISOU 1931  N   LEU A1046    14037  20365  14837  -1008    181   -807       N  
ATOM   1932  CA  LEU A1046      -1.627 -33.122 -21.008  1.00129.27           C  
ANISOU 1932  CA  LEU A1046    13903  20491  14722   -923    246  -1016       C  
ATOM   1933  C   LEU A1046      -2.557 -33.112 -19.798  1.00136.73           C  
ANISOU 1933  C   LEU A1046    14711  21623  15617  -1142    504  -1072       C  
ATOM   1934  O   LEU A1046      -2.257 -32.424 -18.824  1.00136.61           O  
ANISOU 1934  O   LEU A1046    14754  21777  15374  -1194    624  -1062       O  
ATOM   1935  CB  LEU A1046      -2.312 -32.542 -22.270  1.00128.48           C  
ANISOU 1935  CB  LEU A1046    13668  20319  14831   -731     92  -1265       C  
ATOM   1936  CG  LEU A1046      -2.775 -31.073 -22.256  1.00132.82           C  
ANISOU 1936  CG  LEU A1046    14108  20972  15384   -600     79  -1496       C  
ATOM   1937  CD1 LEU A1046      -1.617 -30.104 -22.063  1.00131.17           C  
ANISOU 1937  CD1 LEU A1046    14081  20802  14955   -483     23  -1419       C  
ATOM   1938  CD2 LEU A1046      -3.481 -30.725 -23.546  1.00134.57           C  
ANISOU 1938  CD2 LEU A1046    14215  21080  15834   -437   -129  -1691       C  
ATOM   1939  N   ASP A1047      -3.629 -33.938 -19.831  1.00136.26           N  
ANISOU 1939  N   ASP A1047    14478  21537  15759  -1291    599  -1127       N  
ATOM   1940  CA  ASP A1047      -4.621 -34.077 -18.756  1.00139.61           C  
ANISOU 1940  CA  ASP A1047    14745  22140  16161  -1543    883  -1195       C  
ATOM   1941  C   ASP A1047      -4.011 -34.539 -17.421  1.00145.35           C  
ANISOU 1941  C   ASP A1047    15667  22987  16572  -1793   1045   -913       C  
ATOM   1942  O   ASP A1047      -4.522 -34.162 -16.363  1.00147.00           O  
ANISOU 1942  O   ASP A1047    15811  23426  16617  -1976   1297   -992       O  
ATOM   1943  CB  ASP A1047      -5.764 -35.027 -19.176  1.00143.59           C  
ANISOU 1943  CB  ASP A1047    15034  22546  16977  -1662    929  -1276       C  
ATOM   1944  CG  ASP A1047      -6.398 -34.754 -20.533  1.00153.46           C  
ANISOU 1944  CG  ASP A1047    16106  23654  18545  -1436    725  -1531       C  
ATOM   1945  OD1 ASP A1047      -7.067 -35.663 -21.069  1.00155.19           O  
ANISOU 1945  OD1 ASP A1047    16197  23742  19026  -1498    686  -1562       O  
ATOM   1946  OD2 ASP A1047      -6.190 -33.647 -21.079  1.00157.72           O  
ANISOU 1946  OD2 ASP A1047    16652  24203  19073  -1202    578  -1686       O  
ATOM   1947  N   LYS A1048      -2.919 -35.342 -17.478  1.00141.24           N  
ANISOU 1947  N   LYS A1048    15381  22310  15972  -1803    889   -599       N  
ATOM   1948  CA  LYS A1048      -2.209 -35.873 -16.309  1.00142.52           C  
ANISOU 1948  CA  LYS A1048    15765  22531  15853  -2026    952   -280       C  
ATOM   1949  C   LYS A1048      -1.570 -34.784 -15.447  1.00146.22           C  
ANISOU 1949  C   LYS A1048    16363  23211  15984  -2000   1010   -297       C  
ATOM   1950  O   LYS A1048      -1.540 -34.925 -14.223  1.00148.37           O  
ANISOU 1950  O   LYS A1048    16744  23655  15975  -2250   1169   -152       O  
ATOM   1951  CB  LYS A1048      -1.149 -36.899 -16.730  1.00143.92           C  
ANISOU 1951  CB  LYS A1048    16127  22443  16114  -1986    709     12       C  
ATOM   1952  CG  LYS A1048      -1.326 -38.254 -16.062  1.00160.83           C  
ANISOU 1952  CG  LYS A1048    18336  24495  18275  -2289    755    309       C  
ATOM   1953  CD  LYS A1048      -0.165 -39.195 -16.362  1.00169.61           C  
ANISOU 1953  CD  LYS A1048    19624  25325  19495  -2237    485    587       C  
ATOM   1954  CE  LYS A1048       0.005 -40.268 -15.309  1.00183.07           C  
ANISOU 1954  CE  LYS A1048    21488  26967  21104  -2551    486    965       C  
ATOM   1955  NZ  LYS A1048      -1.038 -41.328 -15.395  1.00194.03           N  
ANISOU 1955  NZ  LYS A1048    22738  28251  22733  -2769    581   1015       N  
ATOM   1956  N   ALA A1049      -1.062 -33.708 -16.077  1.00140.00           N  
ANISOU 1956  N   ALA A1049    15571  22409  15214  -1716    876   -469       N  
ATOM   1957  CA  ALA A1049      -0.411 -32.608 -15.368  1.00139.30           C  
ANISOU 1957  CA  ALA A1049    15586  22489  14852  -1660    901   -515       C  
ATOM   1958  C   ALA A1049      -1.101 -31.228 -15.352  1.00143.28           C  
ANISOU 1958  C   ALA A1049    15898  23163  15378  -1543   1013   -883       C  
ATOM   1959  O   ALA A1049      -0.519 -30.245 -14.884  1.00142.21           O  
ANISOU 1959  O   ALA A1049    15835  23139  15060  -1463   1004   -950       O  
ATOM   1960  CB  ALA A1049       1.082 -32.599 -15.677  1.00137.62           C  
ANISOU 1960  CB  ALA A1049    15592  22121  14577  -1499    656   -316       C  
ATOM   1961  N   ILE A1050      -2.354 -31.168 -15.846  1.00140.91           N  
ANISOU 1961  N   ILE A1050    15337  22867  15336  -1533   1102  -1133       N  
ATOM   1962  CA  ILE A1050      -3.153 -29.936 -15.875  1.00141.34           C  
ANISOU 1962  CA  ILE A1050    15158  23042  15502  -1422   1185  -1512       C  
ATOM   1963  C   ILE A1050      -4.470 -29.871 -15.082  1.00148.74           C  
ANISOU 1963  C   ILE A1050    15843  24193  16479  -1636   1500  -1763       C  
ATOM   1964  O   ILE A1050      -4.838 -28.797 -14.602  1.00149.46           O  
ANISOU 1964  O   ILE A1050    15791  24447  16551  -1600   1619  -2055       O  
ATOM   1965  CB  ILE A1050      -3.302 -29.594 -17.389  1.00142.24           C  
ANISOU 1965  CB  ILE A1050    15176  22932  15938  -1138    924  -1638       C  
ATOM   1966  CG1 ILE A1050      -3.242 -28.076 -17.648  1.00141.68           C  
ANISOU 1966  CG1 ILE A1050    15026  22880  15926   -908    822  -1888       C  
ATOM   1967  CG2 ILE A1050      -4.530 -30.254 -18.034  1.00144.41           C  
ANISOU 1967  CG2 ILE A1050    15218  23121  16529  -1181    944  -1771       C  
ATOM   1968  CD1 ILE A1050      -2.602 -27.681 -18.998  1.00145.54           C  
ANISOU 1968  CD1 ILE A1050    15614  23146  16537   -641    506  -1837       C  
ATOM   1969  N   GLY A1051      -5.146 -31.017 -14.949  1.00147.22           N  
ANISOU 1969  N   GLY A1051    15586  23989  16359  -1863   1637  -1662       N  
ATOM   1970  CA  GLY A1051      -6.407 -31.140 -14.225  1.00150.73           C  
ANISOU 1970  CA  GLY A1051    15783  24630  16855  -2113   1969  -1882       C  
ATOM   1971  C   GLY A1051      -7.532 -31.764 -15.024  1.00155.36           C  
ANISOU 1971  C   GLY A1051    16104  25077  17848  -2122   1968  -2018       C  
ATOM   1972  O   GLY A1051      -7.798 -32.962 -14.896  1.00156.44           O  
ANISOU 1972  O   GLY A1051    16269  25163  18009  -2346   2053  -1812       O  
ATOM   1973  N   ARG A1052      -8.209 -30.942 -15.841  1.00151.13           N  
ANISOU 1973  N   ARG A1052    15306  24463  17653  -1882   1851  -2364       N  
ATOM   1974  CA  ARG A1052      -9.354 -31.343 -16.670  1.00151.94           C  
ANISOU 1974  CA  ARG A1052    15117  24426  18188  -1850   1804  -2562       C  
ATOM   1975  C   ARG A1052      -8.952 -31.984 -18.004  1.00153.03           C  
ANISOU 1975  C   ARG A1052    15374  24272  18500  -1663   1455  -2377       C  
ATOM   1976  O   ARG A1052      -7.790 -31.895 -18.411  1.00149.49           O  
ANISOU 1976  O   ARG A1052    15202  23725  17873  -1509   1238  -2153       O  
ATOM   1977  CB  ARG A1052     -10.336 -30.167 -16.924  1.00153.27           C  
ANISOU 1977  CB  ARG A1052    14927  24626  18681  -1683   1801  -3038       C  
ATOM   1978  CG  ARG A1052     -10.054 -28.839 -16.195  1.00162.37           C  
ANISOU 1978  CG  ARG A1052    16062  25961  19669  -1608   1893  -3248       C  
ATOM   1979  CD  ARG A1052      -9.055 -27.942 -16.916  1.00164.64           C  
ANISOU 1979  CD  ARG A1052    16547  26101  19908  -1286   1543  -3172       C  
ATOM   1980  NE  ARG A1052      -9.479 -27.612 -18.279  1.00169.78           N  
ANISOU 1980  NE  ARG A1052    17064  26501  20944  -1018   1202  -3304       N  
ATOM   1981  CZ  ARG A1052      -8.738 -26.935 -19.149  1.00179.85           C  
ANISOU 1981  CZ  ARG A1052    18504  27610  22220   -752    867  -3222       C  
ATOM   1982  NH1 ARG A1052      -7.528 -26.507 -18.811  1.00164.85           N  
ANISOU 1982  NH1 ARG A1052    16881  25757  19996   -704    836  -3027       N  
ATOM   1983  NH2 ARG A1052      -9.201 -26.682 -20.365  1.00164.92           N  
ANISOU 1983  NH2 ARG A1052    16509  25506  20649   -545    556  -3330       N  
ATOM   1984  N   ASN A1053      -9.932 -32.613 -18.691  1.00151.05           N  
ANISOU 1984  N   ASN A1053    14895  23890  18608  -1681   1410  -2502       N  
ATOM   1985  CA  ASN A1053      -9.749 -33.239 -20.002  1.00149.06           C  
ANISOU 1985  CA  ASN A1053    14710  23375  18549  -1518   1091  -2400       C  
ATOM   1986  C   ASN A1053      -9.890 -32.151 -21.086  1.00151.75           C  
ANISOU 1986  C   ASN A1053    14969  23606  19082  -1191    783  -2637       C  
ATOM   1987  O   ASN A1053     -10.901 -32.077 -21.792  1.00152.60           O  
ANISOU 1987  O   ASN A1053    14820  23614  19549  -1109    660  -2887       O  
ATOM   1988  CB  ASN A1053     -10.738 -34.407 -20.206  1.00152.22           C  
ANISOU 1988  CB  ASN A1053    14906  23683  19246  -1699   1169  -2432       C  
ATOM   1989  CG  ASN A1053     -10.723 -35.467 -19.125  1.00177.48           C  
ANISOU 1989  CG  ASN A1053    18175  26976  22284  -2056   1469  -2187       C  
ATOM   1990  OD1 ASN A1053     -11.774 -35.877 -18.621  1.00175.24           O  
ANISOU 1990  OD1 ASN A1053    17644  26770  22171  -2291   1722  -2317       O  
ATOM   1991  ND2 ASN A1053      -9.544 -35.953 -18.754  1.00166.95           N  
ANISOU 1991  ND2 ASN A1053    17176  25624  20634  -2119   1437  -1822       N  
ATOM   1992  N   THR A1054      -8.861 -31.286 -21.167  1.00146.19           N  
ANISOU 1992  N   THR A1054    14488  22916  18140  -1018    651  -2547       N  
ATOM   1993  CA  THR A1054      -8.722 -30.127 -22.064  1.00144.56           C  
ANISOU 1993  CA  THR A1054    14286  22613  18027   -728    356  -2693       C  
ATOM   1994  C   THR A1054      -8.969 -30.402 -23.543  1.00147.38           C  
ANISOU 1994  C   THR A1054    14643  22751  18605   -562     18  -2720       C  
ATOM   1995  O   THR A1054      -9.555 -29.556 -24.223  1.00147.41           O  
ANISOU 1995  O   THR A1054    14504  22672  18835   -384   -205  -2941       O  
ATOM   1996  CB  THR A1054      -7.384 -29.398 -21.817  1.00151.08           C  
ANISOU 1996  CB  THR A1054    15399  23486  18519   -628    305  -2513       C  
ATOM   1997  OG1 THR A1054      -6.904 -28.831 -23.037  1.00149.20           O  
ANISOU 1997  OG1 THR A1054    15292  23084  18315   -386    -32  -2489       O  
ATOM   1998  CG2 THR A1054      -6.318 -30.305 -21.247  1.00148.76           C  
ANISOU 1998  CG2 THR A1054    15376  23234  17914   -781    429  -2174       C  
ATOM   1999  N   ASN A1055      -8.498 -31.564 -24.036  1.00142.73           N  
ANISOU 1999  N   ASN A1055    14219  22060  17950   -621    -39  -2501       N  
ATOM   2000  CA  ASN A1055      -8.597 -31.998 -25.431  1.00141.85           C  
ANISOU 2000  CA  ASN A1055    14151  21762  17985   -494   -340  -2512       C  
ATOM   2001  C   ASN A1055      -7.787 -31.356 -26.579  1.00143.06           C  
ANISOU 2001  C   ASN A1055    14541  21815  18002   -271   -654  -2450       C  
ATOM   2002  O   ASN A1055      -8.242 -31.300 -27.724  1.00143.27           O  
ANISOU 2002  O   ASN A1055    14536  21717  18181   -152   -930  -2562       O  
ATOM   2003  CB  ASN A1055     -10.059 -32.312 -25.845  1.00145.51           C  
ANISOU 2003  CB  ASN A1055    14288  22149  18850   -515   -405  -2778       C  
ATOM   2004  CG  ASN A1055     -10.207 -33.287 -26.995  1.00168.63           C  
ANISOU 2004  CG  ASN A1055    17252  24905  21913   -487   -627  -2758       C  
ATOM   2005  OD1 ASN A1055      -9.648 -33.114 -28.087  1.00161.68           O  
ANISOU 2005  OD1 ASN A1055    16572  23929  20931   -327   -906  -2708       O  
ATOM   2006  ND2 ASN A1055     -11.022 -34.312 -26.793  1.00161.65           N  
ANISOU 2006  ND2 ASN A1055    16165  23984  21271   -652   -506  -2821       N  
ATOM   2007  N   GLY A1056      -6.628 -30.808 -26.218  1.00136.95           N  
ANISOU 2007  N   GLY A1056    13995  21105  16935   -230   -608  -2280       N  
ATOM   2008  CA  GLY A1056      -5.663 -30.212 -27.138  1.00134.51           C  
ANISOU 2008  CA  GLY A1056    13937  20727  16443    -66   -836  -2179       C  
ATOM   2009  C   GLY A1056      -5.669 -28.696 -27.141  1.00137.52           C  
ANISOU 2009  C   GLY A1056    14309  21128  16814     80   -954  -2276       C  
ATOM   2010  O   GLY A1056      -4.911 -28.100 -27.907  1.00135.62           O  
ANISOU 2010  O   GLY A1056    14278  20829  16425    200  -1144  -2185       O  
ATOM   2011  N   VAL A1057      -6.537 -28.054 -26.337  1.00135.42           N  
ANISOU 2011  N   VAL A1057    13791  20936  16725     65   -848  -2476       N  
ATOM   2012  CA  VAL A1057      -6.653 -26.589 -26.317  1.00135.42           C  
ANISOU 2012  CA  VAL A1057    13736  20923  16794    213   -983  -2610       C  
ATOM   2013  C   VAL A1057      -6.560 -26.077 -24.861  1.00139.46           C  
ANISOU 2013  C   VAL A1057    14146  21607  17237    132   -690  -2680       C  
ATOM   2014  O   VAL A1057      -7.330 -26.503 -23.999  1.00141.11           O  
ANISOU 2014  O   VAL A1057    14133  21929  17556    -13   -442  -2819       O  
ATOM   2015  CB  VAL A1057      -7.778 -25.909 -27.160  1.00141.26           C  
ANISOU 2015  CB  VAL A1057    14274  21521  17877    357  -1292  -2847       C  
ATOM   2016  CG1 VAL A1057      -9.178 -26.280 -26.667  1.00143.85           C  
ANISOU 2016  CG1 VAL A1057    14223  21878  18555    275  -1166  -3124       C  
ATOM   2017  CG2 VAL A1057      -7.602 -24.393 -27.235  1.00141.13           C  
ANISOU 2017  CG2 VAL A1057    14271  21445  17908    519  -1483  -2915       C  
ATOM   2018  N   ILE A1058      -5.613 -25.151 -24.609  1.00134.03           N  
ANISOU 2018  N   ILE A1058    13623  20944  16359    212   -716  -2593       N  
ATOM   2019  CA  ILE A1058      -5.403 -24.484 -23.315  1.00134.04           C  
ANISOU 2019  CA  ILE A1058    13559  21104  16267    160   -486  -2677       C  
ATOM   2020  C   ILE A1058      -5.546 -22.955 -23.493  1.00138.12           C  
ANISOU 2020  C   ILE A1058    13986  21540  16952    343   -685  -2859       C  
ATOM   2021  O   ILE A1058      -5.722 -22.502 -24.626  1.00137.60           O  
ANISOU 2021  O   ILE A1058    13951  21291  17038    493  -1008  -2861       O  
ATOM   2022  CB  ILE A1058      -4.081 -24.916 -22.604  1.00135.23           C  
ANISOU 2022  CB  ILE A1058    13975  21365  16042     55   -307  -2405       C  
ATOM   2023  CG1 ILE A1058      -2.817 -24.472 -23.376  1.00133.25           C  
ANISOU 2023  CG1 ILE A1058    14007  21000  15622    187   -516  -2195       C  
ATOM   2024  CG2 ILE A1058      -4.071 -26.425 -22.298  1.00135.89           C  
ANISOU 2024  CG2 ILE A1058    14107  21502  16023   -140   -125  -2241       C  
ATOM   2025  CD1 ILE A1058      -1.606 -24.137 -22.501  1.00138.70           C  
ANISOU 2025  CD1 ILE A1058    14870  21788  16041    154   -391  -2053       C  
ATOM   2026  N   THR A1059      -5.509 -22.170 -22.394  1.00135.27           N  
ANISOU 2026  N   THR A1059    13515  21307  16573    325   -511  -3019       N  
ATOM   2027  CA  THR A1059      -5.638 -20.704 -22.465  1.00135.78           C  
ANISOU 2027  CA  THR A1059    13470  21278  16843    497   -699  -3215       C  
ATOM   2028  C   THR A1059      -4.447 -19.936 -21.878  1.00138.25           C  
ANISOU 2028  C   THR A1059    13971  21646  16913    527   -654  -3109       C  
ATOM   2029  O   THR A1059      -3.726 -20.474 -21.040  1.00136.77           O  
ANISOU 2029  O   THR A1059    13923  21629  16415    388   -408  -2970       O  
ATOM   2030  CB  THR A1059      -7.005 -20.216 -21.959  1.00145.72           C  
ANISOU 2030  CB  THR A1059    14318  22566  18483    507   -627  -3634       C  
ATOM   2031  OG1 THR A1059      -7.365 -20.927 -20.775  1.00145.97           O  
ANISOU 2031  OG1 THR A1059    14219  22847  18395    289   -218  -3741       O  
ATOM   2032  CG2 THR A1059      -8.094 -20.360 -23.011  1.00145.80           C  
ANISOU 2032  CG2 THR A1059    14144  22387  18868    600   -896  -3759       C  
ATOM   2033  N   LYS A1060      -4.244 -18.681 -22.352  1.00135.06           N  
ANISOU 2033  N   LYS A1060    13572  21075  16668    704   -924  -3165       N  
ATOM   2034  CA  LYS A1060      -3.177 -17.734 -21.993  1.00133.81           C  
ANISOU 2034  CA  LYS A1060    13564  20906  16370    767   -957  -3092       C  
ATOM   2035  C   LYS A1060      -2.895 -17.640 -20.484  1.00138.17           C  
ANISOU 2035  C   LYS A1060    14054  21700  16745    651   -629  -3225       C  
ATOM   2036  O   LYS A1060      -1.730 -17.700 -20.082  1.00135.90           O  
ANISOU 2036  O   LYS A1060    13996  21484  16156    606   -551  -3022       O  
ATOM   2037  CB  LYS A1060      -3.498 -16.340 -22.569  1.00137.77           C  
ANISOU 2037  CB  LYS A1060    13955  21179  17213    960  -1289  -3243       C  
ATOM   2038  CG  LYS A1060      -2.310 -15.375 -22.611  1.00151.55           C  
ANISOU 2038  CG  LYS A1060    15906  22835  18843   1038  -1414  -3091       C  
ATOM   2039  CD  LYS A1060      -2.724 -13.904 -22.472  1.00164.58           C  
ANISOU 2039  CD  LYS A1060    17345  24323  20864   1190  -1619  -3357       C  
ATOM   2040  CE  LYS A1060      -3.121 -13.242 -23.775  1.00176.03           C  
ANISOU 2040  CE  LYS A1060    18813  25465  22605   1335  -2059  -3290       C  
ATOM   2041  NZ  LYS A1060      -4.548 -13.487 -24.120  1.00185.79           N  
ANISOU 2041  NZ  LYS A1060    19774  26632  24187   1377  -2175  -3523       N  
ATOM   2042  N   ASP A1061      -3.958 -17.484 -19.661  1.00137.47           N  
ANISOU 2042  N   ASP A1061    13650  21740  16843    596   -440  -3580       N  
ATOM   2043  CA  ASP A1061      -3.838 -17.381 -18.202  1.00138.41           C  
ANISOU 2043  CA  ASP A1061    13696  22122  16770    458   -110  -3753       C  
ATOM   2044  C   ASP A1061      -3.385 -18.699 -17.560  1.00140.70           C  
ANISOU 2044  C   ASP A1061    14180  22628  16652    227    169  -3506       C  
ATOM   2045  O   ASP A1061      -2.480 -18.681 -16.725  1.00139.77           O  
ANISOU 2045  O   ASP A1061    14236  22654  16216    142    299  -3397       O  
ATOM   2046  CB  ASP A1061      -5.129 -16.834 -17.557  1.00143.87           C  
ANISOU 2046  CB  ASP A1061    13979  22900  17785    447     35  -4240       C  
ATOM   2047  CG  ASP A1061      -5.329 -15.332 -17.715  1.00154.43           C  
ANISOU 2047  CG  ASP A1061    15122  24058  19496    660   -200  -4530       C  
ATOM   2048  OD1 ASP A1061      -4.393 -14.568 -17.388  1.00153.72           O  
ANISOU 2048  OD1 ASP A1061    15173  23956  19277    720   -258  -4481       O  
ATOM   2049  OD2 ASP A1061      -6.441 -14.920 -18.109  1.00162.50           O  
ANISOU 2049  OD2 ASP A1061    15830  24944  20967    761   -331  -4825       O  
ATOM   2050  N   GLU A1062      -3.973 -19.839 -17.979  1.00136.48           N  
ANISOU 2050  N   GLU A1062    13623  22090  16142    128    225  -3403       N  
ATOM   2051  CA  GLU A1062      -3.590 -21.155 -17.455  1.00135.31           C  
ANISOU 2051  CA  GLU A1062    13655  22095  15659    -93    447  -3142       C  
ATOM   2052  C   GLU A1062      -2.286 -21.696 -18.076  1.00134.83           C  
ANISOU 2052  C   GLU A1062    13941  21916  15373    -54    282  -2733       C  
ATOM   2053  O   GLU A1062      -1.707 -22.651 -17.548  1.00133.99           O  
ANISOU 2053  O   GLU A1062    14013  21909  14988   -217    420  -2496       O  
ATOM   2054  CB  GLU A1062      -4.750 -22.166 -17.521  1.00138.47           C  
ANISOU 2054  CB  GLU A1062    13869  22542  16200   -239    599  -3218       C  
ATOM   2055  CG  GLU A1062      -5.161 -22.577 -18.925  1.00147.75           C  
ANISOU 2055  CG  GLU A1062    15022  23480  17636   -115    337  -3140       C  
ATOM   2056  CD  GLU A1062      -5.186 -24.069 -19.191  1.00166.23           C  
ANISOU 2056  CD  GLU A1062    17471  25813  19877   -266    407  -2893       C  
ATOM   2057  OE1 GLU A1062      -4.231 -24.769 -18.782  1.00156.21           O  
ANISOU 2057  OE1 GLU A1062    16455  24605  18291   -381    493  -2602       O  
ATOM   2058  OE2 GLU A1062      -6.140 -24.529 -19.859  1.00160.09           O  
ANISOU 2058  OE2 GLU A1062    16519  24941  19369   -258    342  -2994       O  
ATOM   2059  N   ALA A1063      -1.825 -21.069 -19.187  1.00128.56           N  
ANISOU 2059  N   ALA A1063    13236  20903  14709    150    -17  -2657       N  
ATOM   2060  CA  ALA A1063      -0.572 -21.400 -19.876  1.00125.05           C  
ANISOU 2060  CA  ALA A1063    13086  20339  14087    200   -167  -2328       C  
ATOM   2061  C   ALA A1063       0.604 -20.908 -19.032  1.00126.68           C  
ANISOU 2061  C   ALA A1063    13450  20631  14051    185   -108  -2240       C  
ATOM   2062  O   ALA A1063       1.667 -21.529 -19.047  1.00124.26           O  
ANISOU 2062  O   ALA A1063    13367  20311  13537    139   -112  -1974       O  
ATOM   2063  CB  ALA A1063      -0.531 -20.742 -21.248  1.00124.80           C  
ANISOU 2063  CB  ALA A1063    13091  20078  14248    389   -476  -2307       C  
ATOM   2064  N   GLU A1064       0.400 -19.786 -18.301  1.00123.93           N  
ANISOU 2064  N   GLU A1064    12966  20358  13763    229    -66  -2489       N  
ATOM   2065  CA  GLU A1064       1.368 -19.163 -17.397  1.00122.99           C  
ANISOU 2065  CA  GLU A1064    12953  20333  13445    218    -16  -2480       C  
ATOM   2066  C   GLU A1064       1.825 -20.159 -16.329  1.00125.52           C  
ANISOU 2066  C   GLU A1064    13411  20856  13425      8    200  -2321       C  
ATOM   2067  O   GLU A1064       3.028 -20.292 -16.102  1.00123.83           O  
ANISOU 2067  O   GLU A1064    13410  20632  13010     -3    150  -2105       O  
ATOM   2068  CB  GLU A1064       0.754 -17.924 -16.723  1.00126.61           C  
ANISOU 2068  CB  GLU A1064    13178  20861  14065    276     27  -2856       C  
ATOM   2069  CG  GLU A1064       0.924 -16.633 -17.501  1.00137.36           C  
ANISOU 2069  CG  GLU A1064    14493  21995  15703    495   -247  -2944       C  
ATOM   2070  CD  GLU A1064       1.247 -15.445 -16.616  1.00160.52           C  
ANISOU 2070  CD  GLU A1064    17346  24985  18657    544   -227  -3178       C  
ATOM   2071  OE1 GLU A1064       2.384 -15.390 -16.093  1.00157.27           O  
ANISOU 2071  OE1 GLU A1064    17125  24634  17996    507   -202  -3030       O  
ATOM   2072  OE2 GLU A1064       0.369 -14.569 -16.444  1.00155.98           O  
ANISOU 2072  OE2 GLU A1064    16505  24385  18374    623   -249  -3528       O  
ATOM   2073  N   LYS A1065       0.858 -20.876 -15.707  1.00122.68           N  
ANISOU 2073  N   LYS A1065    12928  20666  13019   -169    425  -2417       N  
ATOM   2074  CA  LYS A1065       1.080 -21.878 -14.663  1.00122.86           C  
ANISOU 2074  CA  LYS A1065    13079  20884  12719   -411    631  -2255       C  
ATOM   2075  C   LYS A1065       1.996 -23.013 -15.141  1.00123.02           C  
ANISOU 2075  C   LYS A1065    13343  20776  12622   -445    520  -1862       C  
ATOM   2076  O   LYS A1065       3.012 -23.265 -14.494  1.00121.94           O  
ANISOU 2076  O   LYS A1065    13407  20688  12238   -516    508  -1666       O  
ATOM   2077  CB  LYS A1065      -0.258 -22.414 -14.115  1.00128.12           C  
ANISOU 2077  CB  LYS A1065    13544  21726  13410   -604    894  -2436       C  
ATOM   2078  CG  LYS A1065      -0.171 -22.950 -12.688  1.00141.94           C  
ANISOU 2078  CG  LYS A1065    15395  23752  14783   -885   1152  -2376       C  
ATOM   2079  CD  LYS A1065      -1.537 -23.359 -12.163  1.00154.17           C  
ANISOU 2079  CD  LYS A1065    16720  25488  16368  -1095   1448  -2592       C  
ATOM   2080  CE  LYS A1065      -1.458 -23.982 -10.790  1.00167.40           C  
ANISOU 2080  CE  LYS A1065    18538  27447  17621  -1421   1710  -2486       C  
ATOM   2081  NZ  LYS A1065      -2.810 -24.193 -10.206  1.00180.49           N  
ANISOU 2081  NZ  LYS A1065    19949  29322  19307  -1646   2050  -2757       N  
ATOM   2082  N   LEU A1066       1.663 -23.653 -16.292  1.00117.54           N  
ANISOU 2082  N   LEU A1066    12623  19906  12130   -382    415  -1771       N  
ATOM   2083  CA  LEU A1066       2.431 -24.748 -16.911  1.00115.18           C  
ANISOU 2083  CA  LEU A1066    12510  19460  11794   -396    306  -1458       C  
ATOM   2084  C   LEU A1066       3.899 -24.370 -17.124  1.00116.05           C  
ANISOU 2084  C   LEU A1066    12814  19466  11816   -281    142  -1296       C  
ATOM   2085  O   LEU A1066       4.786 -25.181 -16.849  1.00115.01           O  
ANISOU 2085  O   LEU A1066    12847  19301  11548   -357    116  -1055       O  
ATOM   2086  CB  LEU A1066       1.811 -25.151 -18.268  1.00114.33           C  
ANISOU 2086  CB  LEU A1066    12317  19179  11944   -301    191  -1478       C  
ATOM   2087  CG  LEU A1066       1.493 -26.637 -18.516  1.00119.13           C  
ANISOU 2087  CG  LEU A1066    12944  19734  12584   -435    235  -1316       C  
ATOM   2088  CD1 LEU A1066       1.035 -26.851 -19.938  1.00118.32           C  
ANISOU 2088  CD1 LEU A1066    12777  19459  12720   -311     80  -1364       C  
ATOM   2089  CD2 LEU A1066       2.693 -27.533 -18.264  1.00120.41           C  
ANISOU 2089  CD2 LEU A1066    13326  19837  12585   -507    193  -1016       C  
ATOM   2090  N   PHE A1067       4.138 -23.140 -17.620  1.00111.07           N  
ANISOU 2090  N   PHE A1067    12147  18763  11292   -102     22  -1431       N  
ATOM   2091  CA  PHE A1067       5.457 -22.574 -17.891  1.00108.97           C  
ANISOU 2091  CA  PHE A1067    12026  18391  10985     11   -121  -1321       C  
ATOM   2092  C   PHE A1067       6.221 -22.317 -16.594  1.00113.27           C  
ANISOU 2092  C   PHE A1067    12658  19071  11308    -66    -63  -1290       C  
ATOM   2093  O   PHE A1067       7.423 -22.585 -16.539  1.00111.76           O  
ANISOU 2093  O   PHE A1067    12621  18809  11033    -59   -148  -1101       O  
ATOM   2094  CB  PHE A1067       5.311 -21.283 -18.712  1.00110.22           C  
ANISOU 2094  CB  PHE A1067    12109  18436  11334    192   -261  -1478       C  
ATOM   2095  CG  PHE A1067       6.540 -20.409 -18.781  1.00110.70           C  
ANISOU 2095  CG  PHE A1067    12280  18414  11367    289   -375  -1420       C  
ATOM   2096  CD1 PHE A1067       7.576 -20.706 -19.658  1.00112.15           C  
ANISOU 2096  CD1 PHE A1067    12610  18450  11551    334   -478  -1225       C  
ATOM   2097  CD2 PHE A1067       6.653 -19.278 -17.984  1.00113.78           C  
ANISOU 2097  CD2 PHE A1067    12610  18874  11750    328   -369  -1588       C  
ATOM   2098  CE1 PHE A1067       8.703 -19.885 -19.738  1.00112.28           C  
ANISOU 2098  CE1 PHE A1067    12708  18387  11567    408   -566  -1181       C  
ATOM   2099  CE2 PHE A1067       7.792 -18.473 -18.046  1.00115.79           C  
ANISOU 2099  CE2 PHE A1067    12953  19037  12005    411   -479  -1537       C  
ATOM   2100  CZ  PHE A1067       8.801 -18.771 -18.936  1.00112.22           C  
ANISOU 2100  CZ  PHE A1067    12642  18433  11562    447   -575  -1327       C  
ATOM   2101  N   ASN A1068       5.525 -21.787 -15.562  1.00111.63           N  
ANISOU 2101  N   ASN A1068    12343  19058  11014   -142     78  -1499       N  
ATOM   2102  CA  ASN A1068       6.093 -21.493 -14.246  1.00112.36           C  
ANISOU 2102  CA  ASN A1068    12516  19320  10856   -238    143  -1513       C  
ATOM   2103  C   ASN A1068       6.578 -22.761 -13.551  1.00117.11           C  
ANISOU 2103  C   ASN A1068    13295  19988  11215   -428    182  -1238       C  
ATOM   2104  O   ASN A1068       7.548 -22.702 -12.799  1.00116.99           O  
ANISOU 2104  O   ASN A1068    13426  20015  11010   -470    120  -1130       O  
ATOM   2105  CB  ASN A1068       5.095 -20.729 -13.382  1.00114.02           C  
ANISOU 2105  CB  ASN A1068    12550  19741  11030   -297    316  -1842       C  
ATOM   2106  CG  ASN A1068       5.007 -19.262 -13.723  1.00132.00           C  
ANISOU 2106  CG  ASN A1068    14683  21940  13531   -103    221  -2110       C  
ATOM   2107  OD1 ASN A1068       6.008 -18.540 -13.752  1.00124.85           O  
ANISOU 2107  OD1 ASN A1068    13861  20947  12629      5     79  -2078       O  
ATOM   2108  ND2 ASN A1068       3.800 -18.774 -13.946  1.00124.52           N  
ANISOU 2108  ND2 ASN A1068    13501  21010  12802    -60    287  -2391       N  
ATOM   2109  N   GLN A1069       5.931 -23.909 -13.842  1.00114.33           N  
ANISOU 2109  N   GLN A1069    12929  19614  10896   -539    253  -1117       N  
ATOM   2110  CA  GLN A1069       6.300 -25.226 -13.313  1.00115.13           C  
ANISOU 2110  CA  GLN A1069    13192  19724  10828   -725    258   -826       C  
ATOM   2111  C   GLN A1069       7.621 -25.683 -13.949  1.00116.81           C  
ANISOU 2111  C   GLN A1069    13546  19706  11129   -617     39   -588       C  
ATOM   2112  O   GLN A1069       8.497 -26.193 -13.244  1.00117.24           O  
ANISOU 2112  O   GLN A1069    13761  19754  11030   -706    -47   -381       O  
ATOM   2113  CB  GLN A1069       5.188 -26.262 -13.571  1.00117.56           C  
ANISOU 2113  CB  GLN A1069    13413  20037  11216   -860    386   -789       C  
ATOM   2114  CG  GLN A1069       3.853 -25.906 -12.917  1.00136.50           C  
ANISOU 2114  CG  GLN A1069    15641  22670  13555   -993    635  -1044       C  
ATOM   2115  CD  GLN A1069       3.187 -27.057 -12.210  1.00160.48           C  
ANISOU 2115  CD  GLN A1069    18708  25826  16441  -1279    810   -904       C  
ATOM   2116  OE1 GLN A1069       3.119 -28.186 -12.710  1.00156.96           O  
ANISOU 2116  OE1 GLN A1069    18299  25231  16107  -1335    758   -694       O  
ATOM   2117  NE2 GLN A1069       2.617 -26.775 -11.049  1.00155.29           N  
ANISOU 2117  NE2 GLN A1069    18022  25445  15537  -1480   1037  -1041       N  
ATOM   2118  N   ASP A1070       7.772 -25.463 -15.275  1.00110.47           N  
ANISOU 2118  N   ASP A1070    12681  18716  10578   -432    -58   -632       N  
ATOM   2119  CA  ASP A1070       8.975 -25.808 -16.042  1.00108.18           C  
ANISOU 2119  CA  ASP A1070    12484  18214  10406   -325   -227   -472       C  
ATOM   2120  C   ASP A1070      10.169 -24.918 -15.651  1.00110.24           C  
ANISOU 2120  C   ASP A1070    12819  18462  10606   -238   -331   -477       C  
ATOM   2121  O   ASP A1070      11.312 -25.380 -15.705  1.00109.06           O  
ANISOU 2121  O   ASP A1070    12763  18182  10491   -219   -456   -316       O  
ATOM   2122  CB  ASP A1070       8.704 -25.743 -17.559  1.00108.47           C  
ANISOU 2122  CB  ASP A1070    12442  18099  10673   -185   -270   -546       C  
ATOM   2123  CG  ASP A1070       7.473 -26.501 -18.038  1.00120.56           C  
ANISOU 2123  CG  ASP A1070    13876  19631  12299   -248   -191   -583       C  
ATOM   2124  OD1 ASP A1070       7.118 -27.523 -17.408  1.00122.75           O  
ANISOU 2124  OD1 ASP A1070    14172  19954  12513   -411   -122   -466       O  
ATOM   2125  OD2 ASP A1070       6.872 -26.077 -19.051  1.00125.71           O  
ANISOU 2125  OD2 ASP A1070    14439  20230  13096   -143   -215   -720       O  
ATOM   2126  N   VAL A1071       9.892 -23.656 -15.240  1.00106.34           N  
ANISOU 2126  N   VAL A1071    12262  18089  10055   -186   -286   -682       N  
ATOM   2127  CA  VAL A1071      10.881 -22.672 -14.774  1.00105.63           C  
ANISOU 2127  CA  VAL A1071    12217  18001   9916   -111   -376   -731       C  
ATOM   2128  C   VAL A1071      11.473 -23.155 -13.441  1.00110.74           C  
ANISOU 2128  C   VAL A1071    12998  18759  10320   -256   -408   -597       C  
ATOM   2129  O   VAL A1071      12.697 -23.182 -13.293  1.00109.83           O  
ANISOU 2129  O   VAL A1071    12972  18541  10219   -216   -559   -480       O  
ATOM   2130  CB  VAL A1071      10.264 -21.243 -14.676  1.00109.80           C  
ANISOU 2130  CB  VAL A1071    12618  18617  10485    -24   -325  -1014       C  
ATOM   2131  CG1 VAL A1071      11.065 -20.325 -13.751  1.00110.17           C  
ANISOU 2131  CG1 VAL A1071    12705  18733  10422     -4   -384  -1096       C  
ATOM   2132  CG2 VAL A1071      10.121 -20.614 -16.055  1.00108.04           C  
ANISOU 2132  CG2 VAL A1071    12315  18221  10515    139   -392  -1084       C  
ATOM   2133  N   ASP A1072      10.601 -23.563 -12.495  1.00109.21           N  
ANISOU 2133  N   ASP A1072    12819  18770   9907   -437   -272   -608       N  
ATOM   2134  CA  ASP A1072      10.986 -24.081 -11.184  1.00111.23           C  
ANISOU 2134  CA  ASP A1072    13235  19160   9869   -623   -299   -457       C  
ATOM   2135  C   ASP A1072      11.792 -25.373 -11.315  1.00114.87           C  
ANISOU 2135  C   ASP A1072    13828  19437  10379   -676   -464   -134       C  
ATOM   2136  O   ASP A1072      12.783 -25.536 -10.607  1.00115.41           O  
ANISOU 2136  O   ASP A1072    14034  19480  10336   -716   -632     13       O  
ATOM   2137  CB  ASP A1072       9.748 -24.288 -10.296  1.00115.83           C  
ANISOU 2137  CB  ASP A1072    13798  20008  10204   -838    -74   -543       C  
ATOM   2138  CG  ASP A1072       8.953 -23.028  -9.982  1.00128.16           C  
ANISOU 2138  CG  ASP A1072    15203  21764  11730   -801     92   -909       C  
ATOM   2139  OD1 ASP A1072       7.980 -23.120  -9.202  1.00131.34           O  
ANISOU 2139  OD1 ASP A1072    15567  22407  11931   -987    306  -1029       O  
ATOM   2140  OD2 ASP A1072       9.288 -21.954 -10.535  1.00133.03           O  
ANISOU 2140  OD2 ASP A1072    15723  22282  12541   -594     14  -1085       O  
ATOM   2141  N   ALA A1073      11.396 -26.260 -12.256  1.00110.51           N  
ANISOU 2141  N   ALA A1073    13222  18738  10030   -662   -443    -42       N  
ATOM   2142  CA  ALA A1073      12.080 -27.531 -12.535  1.00110.34           C  
ANISOU 2142  CA  ALA A1073    13283  18503  10138   -694   -600    224       C  
ATOM   2143  C   ALA A1073      13.494 -27.295 -13.084  1.00112.33           C  
ANISOU 2143  C   ALA A1073    13542  18544  10595   -518   -795    251       C  
ATOM   2144  O   ALA A1073      14.418 -28.040 -12.740  1.00112.30           O  
ANISOU 2144  O   ALA A1073    13631  18402  10637   -554   -983    450       O  
ATOM   2145  CB  ALA A1073      11.268 -28.358 -13.521  1.00110.38           C  
ANISOU 2145  CB  ALA A1073    13193  18405  10341   -696   -516    237       C  
ATOM   2146  N   ALA A1074      13.654 -26.247 -13.924  1.00107.12           N  
ANISOU 2146  N   ALA A1074    12777  17850  10072   -340   -757     50       N  
ATOM   2147  CA  ALA A1074      14.935 -25.854 -14.513  1.00105.52           C  
ANISOU 2147  CA  ALA A1074    12557  17470  10065   -188   -890     35       C  
ATOM   2148  C   ALA A1074      15.810 -25.183 -13.458  1.00109.61           C  
ANISOU 2148  C   ALA A1074    13148  18047  10453   -192  -1013     36       C  
ATOM   2149  O   ALA A1074      16.994 -25.505 -13.375  1.00109.39           O  
ANISOU 2149  O   ALA A1074    13153  17863  10547   -156  -1189    140       O  
ATOM   2150  CB  ALA A1074      14.715 -24.923 -15.694  1.00104.38           C  
ANISOU 2150  CB  ALA A1074    12304  17288  10069    -40   -803   -153       C  
ATOM   2151  N   VAL A1075      15.218 -24.280 -12.636  1.00106.45           N  
ANISOU 2151  N   VAL A1075    12757  17867   9821   -237   -926   -103       N  
ATOM   2152  CA  VAL A1075      15.904 -23.580 -11.543  1.00107.21           C  
ANISOU 2152  CA  VAL A1075    12925  18058   9751   -256  -1034   -142       C  
ATOM   2153  C   VAL A1075      16.446 -24.600 -10.536  1.00112.37           C  
ANISOU 2153  C   VAL A1075    13743  18707  10245   -406  -1205    107       C  
ATOM   2154  O   VAL A1075      17.637 -24.552 -10.235  1.00112.37           O  
ANISOU 2154  O   VAL A1075    13790  18590  10317   -358  -1418    177       O  
ATOM   2155  CB  VAL A1075      15.035 -22.458 -10.905  1.00111.98           C  
ANISOU 2155  CB  VAL A1075    13485  18909  10151   -283   -883   -387       C  
ATOM   2156  CG1 VAL A1075      15.504 -22.090  -9.499  1.00114.00           C  
ANISOU 2156  CG1 VAL A1075    13858  19328  10127   -380   -976   -405       C  
ATOM   2157  CG2 VAL A1075      15.011 -21.222 -11.797  1.00109.96           C  
ANISOU 2157  CG2 VAL A1075    13083  18578  10120    -98   -839   -611       C  
ATOM   2158  N   ARG A1076      15.601 -25.567 -10.096  1.00110.02           N  
ANISOU 2158  N   ARG A1076    13527  18507   9769   -590  -1131    255       N  
ATOM   2159  CA  ARG A1076      15.993 -26.647  -9.175  1.00112.20           C  
ANISOU 2159  CA  ARG A1076    13983  18758   9888   -766  -1312    543       C  
ATOM   2160  C   ARG A1076      17.129 -27.510  -9.763  1.00114.44           C  
ANISOU 2160  C   ARG A1076    14259  18715  10509   -671  -1559    727       C  
ATOM   2161  O   ARG A1076      18.001 -27.973  -9.019  1.00115.98           O  
ANISOU 2161  O   ARG A1076    14578  18820  10669   -730  -1821    915       O  
ATOM   2162  CB  ARG A1076      14.786 -27.524  -8.785  1.00114.50           C  
ANISOU 2162  CB  ARG A1076    14343  19191   9972   -991  -1153    670       C  
ATOM   2163  CG  ARG A1076      13.828 -26.884  -7.778  1.00126.98           C  
ANISOU 2163  CG  ARG A1076    15971  21123  11152  -1160   -941    524       C  
ATOM   2164  CD  ARG A1076      12.906 -27.912  -7.142  1.00140.78           C  
ANISOU 2164  CD  ARG A1076    17832  23001  12655  -1444   -825    719       C  
ATOM   2165  NE  ARG A1076      13.519 -28.542  -5.968  1.00155.13           N  
ANISOU 2165  NE  ARG A1076    19908  24852  14184  -1651  -1041   1012       N  
ATOM   2166  CZ  ARG A1076      12.965 -29.519  -5.252  1.00172.94           C  
ANISOU 2166  CZ  ARG A1076    22327  27197  16187  -1941  -1010   1267       C  
ATOM   2167  NH1 ARG A1076      11.775 -30.005  -5.587  1.00161.72           N  
ANISOU 2167  NH1 ARG A1076    20815  25841  14790  -2057   -749   1248       N  
ATOM   2168  NH2 ARG A1076      13.599 -30.020  -4.201  1.00161.19           N  
ANISOU 2168  NH2 ARG A1076    21097  25722  14425  -2128  -1254   1554       N  
ATOM   2169  N   GLY A1077      17.112 -27.679 -11.090  1.00107.34           N  
ANISOU 2169  N   GLY A1077    13206  17642   9936   -527  -1481    648       N  
ATOM   2170  CA  GLY A1077      18.118 -28.421 -11.843  1.00105.67           C  
ANISOU 2170  CA  GLY A1077    12932  17128  10091   -421  -1654    736       C  
ATOM   2171  C   GLY A1077      19.443 -27.689 -11.918  1.00106.96           C  
ANISOU 2171  C   GLY A1077    13040  17175  10424   -274  -1806    641       C  
ATOM   2172  O   GLY A1077      20.499 -28.308 -11.761  1.00107.37           O  
ANISOU 2172  O   GLY A1077    13098  17017  10682   -250  -2050    761       O  
ATOM   2173  N   ILE A1078      19.391 -26.355 -12.145  1.00100.92           N  
ANISOU 2173  N   ILE A1078    12208  16529   9606   -176  -1676    418       N  
ATOM   2174  CA  ILE A1078      20.558 -25.465 -12.201  1.00 99.71           C  
ANISOU 2174  CA  ILE A1078    11991  16289   9607    -48  -1785    301       C  
ATOM   2175  C   ILE A1078      21.273 -25.507 -10.836  1.00104.90           C  
ANISOU 2175  C   ILE A1078    12775  16972  10110   -122  -2044    415       C  
ATOM   2176  O   ILE A1078      22.493 -25.687 -10.781  1.00105.01           O  
ANISOU 2176  O   ILE A1078    12752  16789  10358    -56  -2269    456       O  
ATOM   2177  CB  ILE A1078      20.143 -24.012 -12.611  1.00101.10           C  
ANISOU 2177  CB  ILE A1078    12088  16596   9730     41  -1597     60       C  
ATOM   2178  CG1 ILE A1078      19.739 -23.928 -14.102  1.00 99.20           C  
ANISOU 2178  CG1 ILE A1078    11732  16273   9687    129  -1412    -34       C  
ATOM   2179  CG2 ILE A1078      21.251 -23.000 -12.303  1.00101.92           C  
ANISOU 2179  CG2 ILE A1078    12152  16648   9925    131  -1724    -50       C  
ATOM   2180  CD1 ILE A1078      18.755 -22.763 -14.454  1.00104.34           C  
ANISOU 2180  CD1 ILE A1078    12336  17074  10233    170  -1228   -217       C  
ATOM   2181  N   LEU A1079      20.489 -25.404  -9.746  1.00102.23           N  
ANISOU 2181  N   LEU A1079    12585  16880   9378   -274  -2014    462       N  
ATOM   2182  CA  LEU A1079      20.969 -25.432  -8.364  1.00104.48           C  
ANISOU 2182  CA  LEU A1079    13038  17250   9408   -388  -2247    576       C  
ATOM   2183  C   LEU A1079      21.607 -26.780  -7.957  1.00111.51           C  
ANISOU 2183  C   LEU A1079    14039  17941  10390   -474  -2548    881       C  
ATOM   2184  O   LEU A1079      22.150 -26.898  -6.856  1.00113.82           O  
ANISOU 2184  O   LEU A1079    14489  18259  10500   -568  -2812   1014       O  
ATOM   2185  CB  LEU A1079      19.875 -24.922  -7.403  1.00105.63           C  
ANISOU 2185  CB  LEU A1079    13305  17745   9086   -549  -2077    503       C  
ATOM   2186  CG  LEU A1079      19.342 -23.498  -7.633  1.00108.14           C  
ANISOU 2186  CG  LEU A1079    13499  18236   9355   -454  -1843    175       C  
ATOM   2187  CD1 LEU A1079      18.038 -23.291  -6.909  1.00109.64           C  
ANISOU 2187  CD1 LEU A1079    13756  18746   9156   -623  -1616     84       C  
ATOM   2188  CD2 LEU A1079      20.356 -22.433  -7.232  1.00110.26           C  
ANISOU 2188  CD2 LEU A1079    13739  18481   9672   -347  -2005     19       C  
ATOM   2189  N   ARG A1080      21.550 -27.780  -8.854  1.00107.83           N  
ANISOU 2189  N   ARG A1080    13489  17262  10220   -441  -2531    981       N  
ATOM   2190  CA  ARG A1080      22.147 -29.103  -8.689  1.00109.90           C  
ANISOU 2190  CA  ARG A1080    13803  17266  10687   -492  -2821   1243       C  
ATOM   2191  C   ARG A1080      23.395 -29.281  -9.576  1.00112.65           C  
ANISOU 2191  C   ARG A1080    13949  17287  11565   -296  -2969   1155       C  
ATOM   2192  O   ARG A1080      24.332 -29.970  -9.168  1.00114.70           O  
ANISOU 2192  O   ARG A1080    14227  17315  12038   -294  -3311   1306       O  
ATOM   2193  CB  ARG A1080      21.070 -30.181  -8.959  1.00111.59           C  
ANISOU 2193  CB  ARG A1080    14062  17482  10854   -626  -2687   1404       C  
ATOM   2194  CG  ARG A1080      21.557 -31.644  -9.032  1.00127.79           C  
ANISOU 2194  CG  ARG A1080    16129  19216  13211   -665  -2965   1659       C  
ATOM   2195  CD  ARG A1080      22.111 -32.201  -7.723  1.00146.18           C  
ANISOU 2195  CD  ARG A1080    18676  21480  15386   -817  -3353   1960       C  
ATOM   2196  NE  ARG A1080      21.046 -32.585  -6.795  1.00159.60           N  
ANISOU 2196  NE  ARG A1080    20616  23411  16615  -1091  -3283   2185       N  
ATOM   2197  CZ  ARG A1080      20.656 -31.857  -5.753  1.00177.40           C  
ANISOU 2197  CZ  ARG A1080    23052  25991  18362  -1239  -3216   2183       C  
ATOM   2198  NH1 ARG A1080      19.674 -32.284  -4.972  1.00168.64           N  
ANISOU 2198  NH1 ARG A1080    22147  25096  16834  -1515  -3114   2377       N  
ATOM   2199  NH2 ARG A1080      21.244 -30.697  -5.484  1.00164.92           N  
ANISOU 2199  NH2 ARG A1080    21442  24527  16691  -1126  -3239   1971       N  
ATOM   2200  N   ASN A1081      23.410 -28.638 -10.768  1.00105.93           N  
ANISOU 2200  N   ASN A1081    12906  16419  10924   -143  -2719    904       N  
ATOM   2201  CA  ASN A1081      24.523 -28.681 -11.723  1.00104.67           C  
ANISOU 2201  CA  ASN A1081    12535  15998  11239     22  -2771    765       C  
ATOM   2202  C   ASN A1081      25.748 -27.983 -11.126  1.00108.84           C  
ANISOU 2202  C   ASN A1081    13029  16454  11873     95  -3002    700       C  
ATOM   2203  O   ASN A1081      25.642 -26.838 -10.685  1.00107.85           O  
ANISOU 2203  O   ASN A1081    12949  16522  11506    100  -2933    592       O  
ATOM   2204  CB  ASN A1081      24.116 -28.027 -13.048  1.00102.98           C  
ANISOU 2204  CB  ASN A1081    12176  15843  11107    119  -2426    533       C  
ATOM   2205  CG  ASN A1081      24.980 -28.420 -14.219  1.00128.64           C  
ANISOU 2205  CG  ASN A1081    15222  18846  14811    234  -2401    405       C  
ATOM   2206  OD1 ASN A1081      26.017 -27.810 -14.492  1.00125.13           O  
ANISOU 2206  OD1 ASN A1081    14648  18303  14593    329  -2431    259       O  
ATOM   2207  ND2 ASN A1081      24.554 -29.434 -14.956  1.00120.70           N  
ANISOU 2207  ND2 ASN A1081    14168  17742  13950    218  -2325    432       N  
ATOM   2208  N   ALA A1082      26.898 -28.688 -11.086  1.00106.69           N  
ANISOU 2208  N   ALA A1082    12661  15889  11988    152  -3296    753       N  
ATOM   2209  CA  ALA A1082      28.159 -28.191 -10.509  1.00107.78           C  
ANISOU 2209  CA  ALA A1082    12740  15907  12304    223  -3575    695       C  
ATOM   2210  C   ALA A1082      28.728 -26.942 -11.201  1.00108.32           C  
ANISOU 2210  C   ALA A1082    12625  16000  12532    350  -3376    408       C  
ATOM   2211  O   ALA A1082      29.352 -26.113 -10.533  1.00108.59           O  
ANISOU 2211  O   ALA A1082    12666  16066  12527    378  -3524    341       O  
ATOM   2212  CB  ALA A1082      29.200 -29.300 -10.480  1.00110.93           C  
ANISOU 2212  CB  ALA A1082    13028  15950  13170    269  -3924    785       C  
ATOM   2213  N   LYS A1083      28.517 -26.815 -12.528  1.00101.30           N  
ANISOU 2213  N   LYS A1083    11584  15092  11814    412  -3054    245       N  
ATOM   2214  CA  LYS A1083      28.987 -25.674 -13.320  1.00 98.79           C  
ANISOU 2214  CA  LYS A1083    11109  14791  11637    500  -2836      3       C  
ATOM   2215  C   LYS A1083      28.025 -24.483 -13.238  1.00 99.73           C  
ANISOU 2215  C   LYS A1083    11342  15189  11362    471  -2608    -55       C  
ATOM   2216  O   LYS A1083      28.467 -23.340 -13.106  1.00 98.97           O  
ANISOU 2216  O   LYS A1083    11197  15132  11274    515  -2591   -188       O  
ATOM   2217  CB  LYS A1083      29.192 -26.073 -14.795  1.00 99.72           C  
ANISOU 2217  CB  LYS A1083    11038  14776  12075    549  -2595   -137       C  
ATOM   2218  CG  LYS A1083      30.430 -26.911 -15.058  1.00113.28           C  
ANISOU 2218  CG  LYS A1083    12546  16191  14305    610  -2775   -205       C  
ATOM   2219  CD  LYS A1083      30.071 -28.349 -15.389  1.00123.91           C  
ANISOU 2219  CD  LYS A1083    13882  17407  15790    586  -2820   -111       C  
ATOM   2220  CE  LYS A1083      31.294 -29.154 -15.747  1.00138.07           C  
ANISOU 2220  CE  LYS A1083    15424  18881  18157    660  -2982   -235       C  
ATOM   2221  NZ  LYS A1083      30.938 -30.528 -16.194  1.00148.75           N  
ANISOU 2221  NZ  LYS A1083    16737  20085  19694    644  -3009   -185       N  
ATOM   2222  N   LEU A1084      26.716 -24.758 -13.318  1.00 94.55           N  
ANISOU 2222  N   LEU A1084    10816  14707  10401    399  -2445     30       N  
ATOM   2223  CA  LEU A1084      25.658 -23.750 -13.344  1.00 92.60           C  
ANISOU 2223  CA  LEU A1084    10646  14705   9832    377  -2222    -45       C  
ATOM   2224  C   LEU A1084      25.288 -23.122 -12.010  1.00 97.16           C  
ANISOU 2224  C   LEU A1084    11369  15484  10062    315  -2331    -25       C  
ATOM   2225  O   LEU A1084      24.992 -21.924 -11.988  1.00 95.87           O  
ANISOU 2225  O   LEU A1084    11192  15450   9784    346  -2211   -176       O  
ATOM   2226  CB  LEU A1084      24.404 -24.289 -14.052  1.00 91.33           C  
ANISOU 2226  CB  LEU A1084    10527  14636   9538    330  -1999     -2       C  
ATOM   2227  CG  LEU A1084      24.582 -24.863 -15.464  1.00 94.73           C  
ANISOU 2227  CG  LEU A1084    10830  14913  10249    377  -1853    -57       C  
ATOM   2228  CD1 LEU A1084      23.327 -25.561 -15.916  1.00 94.09           C  
ANISOU 2228  CD1 LEU A1084    10811  14919  10021    318  -1705      8       C  
ATOM   2229  CD2 LEU A1084      24.970 -23.792 -16.460  1.00 95.73           C  
ANISOU 2229  CD2 LEU A1084    10849  15020  10502    448  -1676   -235       C  
ATOM   2230  N   LYS A1085      25.259 -23.918 -10.913  1.00 95.63           N  
ANISOU 2230  N   LYS A1085    11321  15321   9693    215  -2554    158       N  
ATOM   2231  CA  LYS A1085      24.905 -23.442  -9.566  1.00 96.90           C  
ANISOU 2231  CA  LYS A1085    11649  15705   9463    118  -2656    181       C  
ATOM   2232  C   LYS A1085      25.628 -22.147  -9.135  1.00100.52           C  
ANISOU 2232  C   LYS A1085    12055  16193   9946    194  -2740    -10       C  
ATOM   2233  O   LYS A1085      24.922 -21.198  -8.786  1.00 99.45           O  
ANISOU 2233  O   LYS A1085    11956  16275   9554    173  -2596   -152       O  
ATOM   2234  CB  LYS A1085      24.996 -24.564  -8.504  1.00102.06           C  
ANISOU 2234  CB  LYS A1085    12487  16348   9946    -21  -2932    444       C  
ATOM   2235  CG  LYS A1085      24.802 -24.110  -7.046  1.00116.99           C  
ANISOU 2235  CG  LYS A1085    14576  18478  11395   -149  -3067    470       C  
ATOM   2236  CD  LYS A1085      24.585 -25.272  -6.065  1.00128.50           C  
ANISOU 2236  CD  LYS A1085    16267  19969  12588   -342  -3287    776       C  
ATOM   2237  CE  LYS A1085      25.843 -26.005  -5.646  1.00140.22           C  
ANISOU 2237  CE  LYS A1085    17782  21179  14315   -324  -3728    962       C  
ATOM   2238  NZ  LYS A1085      25.527 -27.245  -4.883  1.00150.44           N  
ANISOU 2238  NZ  LYS A1085    19307  22462  15393   -523  -3939   1305       N  
ATOM   2239  N   PRO A1086      26.986 -22.036  -9.185  1.00 97.95           N  
ANISOU 2239  N   PRO A1086    11616  15646   9955    285  -2957    -47       N  
ATOM   2240  CA  PRO A1086      27.621 -20.777  -8.753  1.00 98.43           C  
ANISOU 2240  CA  PRO A1086    11619  15734  10047    349  -3036   -238       C  
ATOM   2241  C   PRO A1086      27.352 -19.573  -9.657  1.00100.73           C  
ANISOU 2241  C   PRO A1086    11772  16052  10451    435  -2756   -454       C  
ATOM   2242  O   PRO A1086      27.279 -18.451  -9.158  1.00100.74           O  
ANISOU 2242  O   PRO A1086    11773  16166  10336    451  -2753   -616       O  
ATOM   2243  CB  PRO A1086      29.106 -21.130  -8.687  1.00101.51           C  
ANISOU 2243  CB  PRO A1086    11896  15851  10825    418  -3334   -215       C  
ATOM   2244  CG  PRO A1086      29.272 -22.243  -9.644  1.00105.05           C  
ANISOU 2244  CG  PRO A1086    12248  16098  11570    442  -3280   -111       C  
ATOM   2245  CD  PRO A1086      28.005 -23.036  -9.575  1.00100.17           C  
ANISOU 2245  CD  PRO A1086    11797  15636  10630    333  -3153     56       C  
ATOM   2246  N   VAL A1087      27.194 -19.810 -10.971  1.00 95.73           N  
ANISOU 2246  N   VAL A1087    11028  15308  10036    480  -2537   -455       N  
ATOM   2247  CA  VAL A1087      26.938 -18.764 -11.965  1.00 93.90           C  
ANISOU 2247  CA  VAL A1087    10688  15073   9915    541  -2291   -610       C  
ATOM   2248  C   VAL A1087      25.552 -18.148 -11.754  1.00 97.45           C  
ANISOU 2248  C   VAL A1087    11228  15758  10041    506  -2124   -674       C  
ATOM   2249  O   VAL A1087      25.438 -16.920 -11.705  1.00 96.77           O  
ANISOU 2249  O   VAL A1087    11094  15716   9958    549  -2075   -838       O  
ATOM   2250  CB  VAL A1087      27.176 -19.253 -13.424  1.00 96.49           C  
ANISOU 2250  CB  VAL A1087    10902  15237  10524    572  -2116   -587       C  
ATOM   2251  CG1 VAL A1087      27.016 -18.114 -14.428  1.00 94.97           C  
ANISOU 2251  CG1 VAL A1087    10629  15029  10426    611  -1900   -714       C  
ATOM   2252  CG2 VAL A1087      28.555 -19.895 -13.569  1.00 97.42           C  
ANISOU 2252  CG2 VAL A1087    10893  15121  11002    605  -2274   -573       C  
ATOM   2253  N   TYR A1088      24.514 -18.993 -11.587  1.00 94.25           N  
ANISOU 2253  N   TYR A1088    10934  15489   9388    427  -2048   -560       N  
ATOM   2254  CA  TYR A1088      23.142 -18.539 -11.359  1.00 93.94           C  
ANISOU 2254  CA  TYR A1088    10952  15674   9067    383  -1880   -640       C  
ATOM   2255  C   TYR A1088      23.033 -17.756 -10.052  1.00 99.15           C  
ANISOU 2255  C   TYR A1088    11672  16516   9483    346  -1973   -773       C  
ATOM   2256  O   TYR A1088      22.334 -16.742 -10.015  1.00 98.67           O  
ANISOU 2256  O   TYR A1088    11566  16569   9356    372  -1851   -963       O  
ATOM   2257  CB  TYR A1088      22.162 -19.719 -11.387  1.00 95.47           C  
ANISOU 2257  CB  TYR A1088    11237  15961   9075    285  -1789   -487       C  
ATOM   2258  CG  TYR A1088      20.713 -19.336 -11.169  1.00 97.80           C  
ANISOU 2258  CG  TYR A1088    11559  16484   9117    231  -1599   -590       C  
ATOM   2259  CD1 TYR A1088      19.947 -18.807 -12.202  1.00 98.04           C  
ANISOU 2259  CD1 TYR A1088    11495  16499   9258    298  -1416   -694       C  
ATOM   2260  CD2 TYR A1088      20.099 -19.525  -9.933  1.00100.89           C  
ANISOU 2260  CD2 TYR A1088    12066  17106   9162    101  -1608   -588       C  
ATOM   2261  CE1 TYR A1088      18.614 -18.455 -12.007  1.00 99.09           C  
ANISOU 2261  CE1 TYR A1088    11615  16817   9218    259  -1261   -817       C  
ATOM   2262  CE2 TYR A1088      18.766 -19.175  -9.725  1.00102.19           C  
ANISOU 2262  CE2 TYR A1088    12218  17484   9127     43  -1407   -725       C  
ATOM   2263  CZ  TYR A1088      18.027 -18.640 -10.766  1.00107.66           C  
ANISOU 2263  CZ  TYR A1088    12782  18133   9991    134  -1242   -849       C  
ATOM   2264  OH  TYR A1088      16.713 -18.296 -10.558  1.00109.82           O  
ANISOU 2264  OH  TYR A1088    13008  18594  10123     88  -1063  -1011       O  
ATOM   2265  N   ASP A1089      23.751 -18.205  -8.999  1.00 97.12           N  
ANISOU 2265  N   ASP A1089    11514  16276   9113    286  -2207   -687       N  
ATOM   2266  CA  ASP A1089      23.778 -17.536  -7.698  1.00 98.91           C  
ANISOU 2266  CA  ASP A1089    11821  16686   9073    233  -2325   -816       C  
ATOM   2267  C   ASP A1089      24.509 -16.187  -7.768  1.00101.67           C  
ANISOU 2267  C   ASP A1089    12036  16943   9650    352  -2386  -1043       C  
ATOM   2268  O   ASP A1089      24.193 -15.286  -6.991  1.00102.70           O  
ANISOU 2268  O   ASP A1089    12179  17240   9603    337  -2387  -1249       O  
ATOM   2269  CB  ASP A1089      24.386 -18.447  -6.614  1.00103.37           C  
ANISOU 2269  CB  ASP A1089    12554  17275   9446    123  -2602   -627       C  
ATOM   2270  CG  ASP A1089      23.448 -19.523  -6.084  1.00115.26           C  
ANISOU 2270  CG  ASP A1089    14241  18960  10592    -52  -2546   -434       C  
ATOM   2271  OD1 ASP A1089      22.328 -19.175  -5.641  1.00116.55           O  
ANISOU 2271  OD1 ASP A1089    14457  19389  10437   -146  -2345   -551       O  
ATOM   2272  OD2 ASP A1089      23.862 -20.702  -6.038  1.00121.78           O  
ANISOU 2272  OD2 ASP A1089    15149  19656  11465   -107  -2715   -175       O  
ATOM   2273  N   SER A1090      25.458 -16.046  -8.717  1.00 96.03           N  
ANISOU 2273  N   SER A1090    11184  15965   9339    458  -2420  -1022       N  
ATOM   2274  CA  SER A1090      26.230 -14.821  -8.940  1.00 95.45           C  
ANISOU 2274  CA  SER A1090    10967  15759   9543    557  -2467  -1206       C  
ATOM   2275  C   SER A1090      25.402 -13.769  -9.685  1.00 97.75           C  
ANISOU 2275  C   SER A1090    11168  16067   9904    611  -2242  -1361       C  
ATOM   2276  O   SER A1090      25.403 -12.598  -9.299  1.00 97.67           O  
ANISOU 2276  O   SER A1090    11097  16083   9930    652  -2273  -1571       O  
ATOM   2277  CB  SER A1090      27.527 -15.133  -9.689  1.00 98.08           C  
ANISOU 2277  CB  SER A1090    11179  15812  10276    618  -2556  -1124       C  
ATOM   2278  OG  SER A1090      27.696 -14.398 -10.893  1.00103.77           O  
ANISOU 2278  OG  SER A1090    11755  16381  11292    682  -2383  -1195       O  
ATOM   2279  N   LEU A1091      24.705 -14.198 -10.756  1.00 93.01           N  
ANISOU 2279  N   LEU A1091    10558  15437   9343    611  -2044  -1260       N  
ATOM   2280  CA  LEU A1091      23.882 -13.353 -11.623  1.00 91.69           C  
ANISOU 2280  CA  LEU A1091    10320  15252   9264    658  -1865  -1357       C  
ATOM   2281  C   LEU A1091      22.691 -12.687 -10.931  1.00 96.67           C  
ANISOU 2281  C   LEU A1091    10963  16091   9677    646  -1800  -1548       C  
ATOM   2282  O   LEU A1091      22.246 -13.127  -9.868  1.00 97.84           O  
ANISOU 2282  O   LEU A1091    11203  16453   9520    568  -1821  -1576       O  
ATOM   2283  CB  LEU A1091      23.407 -14.133 -12.865  1.00 89.94           C  
ANISOU 2283  CB  LEU A1091    10110  14968   9095    647  -1703  -1195       C  
ATOM   2284  CG  LEU A1091      24.471 -14.593 -13.860  1.00 93.96           C  
ANISOU 2284  CG  LEU A1091    10566  15263   9870    661  -1697  -1071       C  
ATOM   2285  CD1 LEU A1091      23.868 -15.504 -14.897  1.00 92.71           C  
ANISOU 2285  CD1 LEU A1091    10443  15097   9688    633  -1544   -939       C  
ATOM   2286  CD2 LEU A1091      25.147 -13.420 -14.541  1.00 96.85           C  
ANISOU 2286  CD2 LEU A1091    10827  15459  10514    708  -1682  -1155       C  
ATOM   2287  N   ASP A1092      22.181 -11.618 -11.561  1.00 92.47           N  
ANISOU 2287  N   ASP A1092    10333  15487   9314    714  -1722  -1682       N  
ATOM   2288  CA  ASP A1092      21.035 -10.819 -11.126  1.00 92.99           C  
ANISOU 2288  CA  ASP A1092    10348  15694   9291    731  -1656  -1914       C  
ATOM   2289  C   ASP A1092      19.775 -11.401 -11.784  1.00 95.35           C  
ANISOU 2289  C   ASP A1092    10663  16065   9501    707  -1489  -1845       C  
ATOM   2290  O   ASP A1092      19.885 -12.296 -12.622  1.00 93.55           O  
ANISOU 2290  O   ASP A1092    10488  15761   9295    685  -1439  -1624       O  
ATOM   2291  CB  ASP A1092      21.341  -9.327 -11.320  1.00 95.37           C  
ANISOU 2291  CB  ASP A1092    10521  15832   9885    823  -1733  -2103       C  
ATOM   2292  CG  ASP A1092      21.930  -9.012 -12.678  1.00104.54           C  
ANISOU 2292  CG  ASP A1092    11643  16721  11358    866  -1731  -1947       C  
ATOM   2293  OD1 ASP A1092      23.176  -8.981 -12.789  1.00105.20           O  
ANISOU 2293  OD1 ASP A1092    11714  16664  11594    865  -1815  -1871       O  
ATOM   2294  OD2 ASP A1092      21.148  -8.868 -13.648  1.00108.95           O  
ANISOU 2294  OD2 ASP A1092    12188  17213  11994    885  -1645  -1894       O  
ATOM   2295  N   ALA A1093      18.589 -10.868 -11.419  1.00 92.14           N  
ANISOU 2295  N   ALA A1093    10187  15795   9025    713  -1408  -2063       N  
ATOM   2296  CA  ALA A1093      17.252 -11.263 -11.889  1.00 90.92           C  
ANISOU 2296  CA  ALA A1093    10008  15722   8815    695  -1261  -2068       C  
ATOM   2297  C   ALA A1093      17.131 -11.374 -13.421  1.00 91.28           C  
ANISOU 2297  C   ALA A1093    10047  15559   9078    749  -1245  -1889       C  
ATOM   2298  O   ALA A1093      16.753 -12.435 -13.914  1.00 88.96           O  
ANISOU 2298  O   ALA A1093     9817  15300   8685    698  -1162  -1719       O  
ATOM   2299  CB  ALA A1093      16.230 -10.281 -11.340  1.00 93.37           C  
ANISOU 2299  CB  ALA A1093    10180  16139   9158    729  -1214  -2404       C  
ATOM   2300  N   VAL A1094      17.478 -10.298 -14.160  1.00 87.71           N  
ANISOU 2300  N   VAL A1094     9528  14888   8910    836  -1332  -1920       N  
ATOM   2301  CA  VAL A1094      17.396 -10.229 -15.629  1.00 86.43           C  
ANISOU 2301  CA  VAL A1094     9382  14529   8926    866  -1335  -1752       C  
ATOM   2302  C   VAL A1094      18.406 -11.184 -16.294  1.00 90.07           C  
ANISOU 2302  C   VAL A1094     9950  14918   9353    812  -1305  -1493       C  
ATOM   2303  O   VAL A1094      18.030 -11.928 -17.204  1.00 88.76           O  
ANISOU 2303  O   VAL A1094     9840  14736   9149    785  -1234  -1347       O  
ATOM   2304  CB  VAL A1094      17.511  -8.768 -16.160  1.00 90.82           C  
ANISOU 2304  CB  VAL A1094     9858  14866   9786    945  -1454  -1836       C  
ATOM   2305  CG1 VAL A1094      17.305  -8.694 -17.672  1.00 89.74           C  
ANISOU 2305  CG1 VAL A1094     9773  14547   9776    946  -1469  -1644       C  
ATOM   2306  CG2 VAL A1094      16.533  -7.839 -15.445  1.00 92.34           C  
ANISOU 2306  CG2 VAL A1094     9907  15112  10065   1011  -1496  -2141       C  
ATOM   2307  N   ARG A1095      19.676 -11.169 -15.826  1.00 87.00           N  
ANISOU 2307  N   ARG A1095     9573  14484   9000    800  -1366  -1465       N  
ATOM   2308  CA  ARG A1095      20.755 -12.034 -16.321  1.00 85.78           C  
ANISOU 2308  CA  ARG A1095     9474  14248   8869    755  -1347  -1274       C  
ATOM   2309  C   ARG A1095      20.535 -13.503 -15.912  1.00 88.95           C  
ANISOU 2309  C   ARG A1095     9948  14793   9055    695  -1298  -1172       C  
ATOM   2310  O   ARG A1095      21.063 -14.402 -16.568  1.00 87.62           O  
ANISOU 2310  O   ARG A1095     9814  14555   8924    664  -1258  -1023       O  
ATOM   2311  CB  ARG A1095      22.122 -11.525 -15.844  1.00 86.91           C  
ANISOU 2311  CB  ARG A1095     9572  14288   9162    767  -1452  -1312       C  
ATOM   2312  CG  ARG A1095      22.580 -10.239 -16.523  1.00 96.35           C  
ANISOU 2312  CG  ARG A1095    10703  15285  10622    797  -1486  -1348       C  
ATOM   2313  CD  ARG A1095      23.987  -9.894 -16.099  1.00103.20           C  
ANISOU 2313  CD  ARG A1095    11508  16043  11662    796  -1577  -1380       C  
ATOM   2314  NE  ARG A1095      24.488  -8.683 -16.747  1.00111.06           N  
ANISOU 2314  NE  ARG A1095    12438  16833  12926    800  -1601  -1397       N  
ATOM   2315  CZ  ARG A1095      24.530  -7.486 -16.169  1.00125.56           C  
ANISOU 2315  CZ  ARG A1095    14197  18605  14906    849  -1718  -1563       C  
ATOM   2316  NH1 ARG A1095      24.104  -7.327 -14.922  1.00112.98           N  
ANISOU 2316  NH1 ARG A1095    12578  17161  13188    898  -1806  -1754       N  
ATOM   2317  NH2 ARG A1095      25.011  -6.442 -16.829  1.00112.56           N  
ANISOU 2317  NH2 ARG A1095    12497  16744  13526    835  -1744  -1543       N  
ATOM   2318  N   ARG A1096      19.750 -13.740 -14.832  1.00 86.23           N  
ANISOU 2318  N   ARG A1096     9621  14647   8495    668  -1294  -1263       N  
ATOM   2319  CA  ARG A1096      19.370 -15.071 -14.347  1.00 85.88           C  
ANISOU 2319  CA  ARG A1096     9657  14744   8228    585  -1252  -1154       C  
ATOM   2320  C   ARG A1096      18.381 -15.646 -15.362  1.00 89.37           C  
ANISOU 2320  C   ARG A1096    10105  15183   8668    575  -1129  -1080       C  
ATOM   2321  O   ARG A1096      18.560 -16.774 -15.822  1.00 88.26           O  
ANISOU 2321  O   ARG A1096    10014  15007   8515    533  -1099   -921       O  
ATOM   2322  CB  ARG A1096      18.710 -14.984 -12.954  1.00 85.84           C  
ANISOU 2322  CB  ARG A1096     9675  14972   7969    527  -1250  -1290       C  
ATOM   2323  CG  ARG A1096      19.680 -14.890 -11.785  1.00 92.99           C  
ANISOU 2323  CG  ARG A1096    10629  15925   8779    497  -1397  -1314       C  
ATOM   2324  CD  ARG A1096      18.936 -14.739 -10.472  1.00100.23           C  
ANISOU 2324  CD  ARG A1096    11583  17105   9394    413  -1365  -1471       C  
ATOM   2325  NE  ARG A1096      19.827 -14.311  -9.392  1.00106.01           N  
ANISOU 2325  NE  ARG A1096    12355  17884  10039    398  -1528  -1553       N  
ATOM   2326  CZ  ARG A1096      20.159 -15.055  -8.341  1.00116.80           C  
ANISOU 2326  CZ  ARG A1096    13861  19385  11132    282  -1627  -1454       C  
ATOM   2327  NH1 ARG A1096      19.666 -16.280  -8.201  1.00102.82           N  
ANISOU 2327  NH1 ARG A1096    12204  17708   9157    162  -1570  -1257       N  
ATOM   2328  NH2 ARG A1096      20.980 -14.578  -7.418  1.00102.58           N  
ANISOU 2328  NH2 ARG A1096    12096  17616   9263    277  -1804  -1544       N  
ATOM   2329  N   ALA A1097      17.383 -14.814 -15.757  1.00 86.44           N  
ANISOU 2329  N   ALA A1097     9669  14824   8352    622  -1083  -1211       N  
ATOM   2330  CA  ALA A1097      16.337 -15.099 -16.740  1.00 85.62           C  
ANISOU 2330  CA  ALA A1097     9553  14704   8274    628  -1005  -1180       C  
ATOM   2331  C   ALA A1097      16.922 -15.387 -18.120  1.00 89.09           C  
ANISOU 2331  C   ALA A1097    10038  14971   8840    638  -1002  -1020       C  
ATOM   2332  O   ALA A1097      16.349 -16.190 -18.859  1.00 88.31           O  
ANISOU 2332  O   ALA A1097     9970  14878   8707    611   -941   -939       O  
ATOM   2333  CB  ALA A1097      15.362 -13.933 -16.819  1.00 87.07           C  
ANISOU 2333  CB  ALA A1097     9636  14886   8559    694  -1021  -1373       C  
ATOM   2334  N   ALA A1098      18.054 -14.735 -18.468  1.00 86.10           N  
ANISOU 2334  N   ALA A1098     9660  14448   8606    664  -1058   -992       N  
ATOM   2335  CA  ALA A1098      18.751 -14.955 -19.734  1.00 85.61           C  
ANISOU 2335  CA  ALA A1098     9640  14244   8646    644  -1022   -863       C  
ATOM   2336  C   ALA A1098      19.391 -16.345 -19.734  1.00 89.88           C  
ANISOU 2336  C   ALA A1098    10210  14796   9144    593   -973   -759       C  
ATOM   2337  O   ALA A1098      19.359 -17.021 -20.760  1.00 89.24           O  
ANISOU 2337  O   ALA A1098    10163  14672   9072    561   -899   -683       O  
ATOM   2338  CB  ALA A1098      19.808 -13.886 -19.952  1.00 86.81           C  
ANISOU 2338  CB  ALA A1098     9765  14249   8969    660  -1072   -876       C  
ATOM   2339  N   LEU A1099      19.924 -16.785 -18.574  1.00 87.30           N  
ANISOU 2339  N   LEU A1099     9873  14523   8774    581  -1034   -763       N  
ATOM   2340  CA  LEU A1099      20.525 -18.110 -18.419  1.00 87.47           C  
ANISOU 2340  CA  LEU A1099     9912  14525   8798    539  -1042   -661       C  
ATOM   2341  C   LEU A1099      19.446 -19.196 -18.393  1.00 91.56           C  
ANISOU 2341  C   LEU A1099    10473  15145   9170    493   -988   -600       C  
ATOM   2342  O   LEU A1099      19.676 -20.276 -18.935  1.00 91.17           O  
ANISOU 2342  O   LEU A1099    10431  15032   9176    464   -959   -518       O  
ATOM   2343  CB  LEU A1099      21.415 -18.183 -17.169  1.00 88.68           C  
ANISOU 2343  CB  LEU A1099    10057  14684   8954    536  -1178   -663       C  
ATOM   2344  CG  LEU A1099      22.473 -19.290 -17.186  1.00 93.88           C  
ANISOU 2344  CG  LEU A1099    10698  15226   9746    515  -1243   -568       C  
ATOM   2345  CD1 LEU A1099      23.845 -18.744 -16.861  1.00 94.94           C  
ANISOU 2345  CD1 LEU A1099    10760  15240  10072    549  -1354   -617       C  
ATOM   2346  CD2 LEU A1099      22.110 -20.411 -16.236  1.00 96.99           C  
ANISOU 2346  CD2 LEU A1099    11163  15701   9987    456  -1330   -463       C  
ATOM   2347  N   ILE A1100      18.275 -18.904 -17.779  1.00 88.61           N  
ANISOU 2347  N   ILE A1100    10109  14921   8638    481   -967   -664       N  
ATOM   2348  CA  ILE A1100      17.122 -19.814 -17.714  1.00 88.74           C  
ANISOU 2348  CA  ILE A1100    10147  15043   8527    423   -897   -627       C  
ATOM   2349  C   ILE A1100      16.607 -20.048 -19.141  1.00 92.55           C  
ANISOU 2349  C   ILE A1100    10621  15452   9093    443   -825   -612       C  
ATOM   2350  O   ILE A1100      16.320 -21.192 -19.501  1.00 91.91           O  
ANISOU 2350  O   ILE A1100    10556  15361   9004    398   -787   -534       O  
ATOM   2351  CB  ILE A1100      16.022 -19.290 -16.737  1.00 92.74           C  
ANISOU 2351  CB  ILE A1100    10631  15734   8870    396   -862   -749       C  
ATOM   2352  CG1 ILE A1100      16.519 -19.345 -15.275  1.00 94.58           C  
ANISOU 2352  CG1 ILE A1100    10913  16076   8948    335   -930   -745       C  
ATOM   2353  CG2 ILE A1100      14.700 -20.072 -16.885  1.00 93.28           C  
ANISOU 2353  CG2 ILE A1100    10688  15900   8855    333   -761   -741       C  
ATOM   2354  CD1 ILE A1100      15.916 -18.299 -14.345  1.00102.91           C  
ANISOU 2354  CD1 ILE A1100    11925  17293   9882    334   -905   -946       C  
ATOM   2355  N   ASN A1101      16.558 -18.964 -19.961  1.00 89.54           N  
ANISOU 2355  N   ASN A1101    10221  15004   8794    503   -826   -678       N  
ATOM   2356  CA  ASN A1101      16.138 -18.970 -21.370  1.00 89.26           C  
ANISOU 2356  CA  ASN A1101    10208  14899   8807    512   -790   -659       C  
ATOM   2357  C   ASN A1101      16.952 -19.989 -22.169  1.00 93.54           C  
ANISOU 2357  C   ASN A1101    10784  15358   9401    473   -741   -573       C  
ATOM   2358  O   ASN A1101      16.398 -20.689 -23.021  1.00 92.82           O  
ANISOU 2358  O   ASN A1101    10714  15264   9289    449   -696   -555       O  
ATOM   2359  CB  ASN A1101      16.277 -17.563 -21.981  1.00 89.87           C  
ANISOU 2359  CB  ASN A1101    10290  14890   8966    560   -839   -700       C  
ATOM   2360  CG  ASN A1101      15.955 -17.465 -23.459  1.00107.08           C  
ANISOU 2360  CG  ASN A1101    12532  16995  11157    547   -832   -652       C  
ATOM   2361  OD1 ASN A1101      16.718 -17.910 -24.324  1.00101.50           O  
ANISOU 2361  OD1 ASN A1101    11880  16229  10458    498   -771   -585       O  
ATOM   2362  ND2 ASN A1101      14.848 -16.820 -23.785  1.00 96.17           N  
ANISOU 2362  ND2 ASN A1101    11143  15614   9785    583   -904   -700       N  
ATOM   2363  N   MET A1102      18.263 -20.060 -21.880  1.00 91.06           N  
ANISOU 2363  N   MET A1102    10453  14971   9175    469   -755   -548       N  
ATOM   2364  CA  MET A1102      19.207 -20.974 -22.513  1.00 91.42           C  
ANISOU 2364  CA  MET A1102    10485  14921   9328    438   -707   -515       C  
ATOM   2365  C   MET A1102      18.940 -22.432 -22.136  1.00 97.37           C  
ANISOU 2365  C   MET A1102    11228  15688  10081    407   -720   -464       C  
ATOM   2366  O   MET A1102      19.072 -23.307 -22.994  1.00 97.37           O  
ANISOU 2366  O   MET A1102    11217  15630  10151    383   -661   -469       O  
ATOM   2367  CB  MET A1102      20.649 -20.571 -22.190  1.00 93.90           C  
ANISOU 2367  CB  MET A1102    10748  15141   9789    449   -738   -530       C  
ATOM   2368  CG  MET A1102      21.134 -19.418 -23.027  1.00 97.32           C  
ANISOU 2368  CG  MET A1102    11188  15514  10275    444   -682   -564       C  
ATOM   2369  SD  MET A1102      22.840 -18.946 -22.708  1.00101.91           S  
ANISOU 2369  SD  MET A1102    11676  15971  11074    444   -699   -604       S  
ATOM   2370  CE  MET A1102      23.690 -20.294 -23.463  1.00 98.88           C  
ANISOU 2370  CE  MET A1102    11221  15506  10843    399   -597   -635       C  
ATOM   2371  N   VAL A1103      18.542 -22.690 -20.868  1.00 95.09           N  
ANISOU 2371  N   VAL A1103    10948  15476   9705    393   -795   -418       N  
ATOM   2372  CA  VAL A1103      18.222 -24.041 -20.379  1.00 95.85           C  
ANISOU 2372  CA  VAL A1103    11052  15576   9790    337   -828   -331       C  
ATOM   2373  C   VAL A1103      16.919 -24.524 -21.044  1.00100.09           C  
ANISOU 2373  C   VAL A1103    11598  16172  10260    310   -746   -344       C  
ATOM   2374  O   VAL A1103      16.800 -25.701 -21.381  1.00 99.99           O  
ANISOU 2374  O   VAL A1103    11573  16099  10321    274   -739   -302       O  
ATOM   2375  CB  VAL A1103      18.188 -24.152 -18.823  1.00100.87           C  
ANISOU 2375  CB  VAL A1103    11727  16293  10306    292   -929   -255       C  
ATOM   2376  CG1 VAL A1103      18.129 -25.613 -18.373  1.00101.74           C  
ANISOU 2376  CG1 VAL A1103    11861  16354  10441    214   -997   -117       C  
ATOM   2377  CG2 VAL A1103      19.395 -23.466 -18.186  1.00101.03           C  
ANISOU 2377  CG2 VAL A1103    11738  16265  10385    330  -1036   -269       C  
ATOM   2378  N   PHE A1104      15.983 -23.590 -21.301  1.00 96.73           N  
ANISOU 2378  N   PHE A1104    11178  15840   9737    335   -702   -420       N  
ATOM   2379  CA  PHE A1104      14.710 -23.848 -21.977  1.00 96.45           C  
ANISOU 2379  CA  PHE A1104    11133  15851   9661    323   -651   -458       C  
ATOM   2380  C   PHE A1104      14.911 -24.148 -23.467  1.00 99.75           C  
ANISOU 2380  C   PHE A1104    11568  16180  10153    336   -617   -485       C  
ATOM   2381  O   PHE A1104      13.988 -24.652 -24.113  1.00 99.23           O  
ANISOU 2381  O   PHE A1104    11498  16131  10074    319   -598   -512       O  
ATOM   2382  CB  PHE A1104      13.787 -22.640 -21.816  1.00 98.36           C  
ANISOU 2382  CB  PHE A1104    11354  16185   9833    362   -653   -553       C  
ATOM   2383  CG  PHE A1104      12.675 -22.812 -20.813  1.00100.95           C  
ANISOU 2383  CG  PHE A1104    11635  16650  10072    313   -621   -589       C  
ATOM   2384  CD1 PHE A1104      11.390 -23.147 -21.226  1.00104.80           C  
ANISOU 2384  CD1 PHE A1104    12070  17180  10568    295   -583   -645       C  
ATOM   2385  CD2 PHE A1104      12.896 -22.589 -19.460  1.00103.89           C  
ANISOU 2385  CD2 PHE A1104    12010  17118  10344    274   -622   -587       C  
ATOM   2386  CE1 PHE A1104      10.349 -23.267 -20.300  1.00106.71           C  
ANISOU 2386  CE1 PHE A1104    12244  17559  10742    230   -518   -706       C  
ATOM   2387  CE2 PHE A1104      11.859 -22.726 -18.534  1.00107.92           C  
ANISOU 2387  CE2 PHE A1104    12479  17785  10740    198   -553   -640       C  
ATOM   2388  CZ  PHE A1104      10.591 -23.055 -18.962  1.00106.33           C  
ANISOU 2388  CZ  PHE A1104    12207  17625  10570    174   -487   -704       C  
ATOM   2389  N   GLN A1105      16.113 -23.835 -24.004  1.00 96.28           N  
ANISOU 2389  N   GLN A1105    11144  15655   9785    353   -603   -492       N  
ATOM   2390  CA  GLN A1105      16.490 -24.048 -25.399  1.00 96.36           C  
ANISOU 2390  CA  GLN A1105    11180  15604   9830    337   -538   -536       C  
ATOM   2391  C   GLN A1105      17.537 -25.133 -25.663  1.00102.32           C  
ANISOU 2391  C   GLN A1105    11884  16260  10733    311   -494   -558       C  
ATOM   2392  O   GLN A1105      17.369 -25.917 -26.599  1.00102.81           O  
ANISOU 2392  O   GLN A1105    11945  16300  10820    282   -440   -617       O  
ATOM   2393  CB  GLN A1105      17.059 -22.755 -26.011  1.00 97.40           C  
ANISOU 2393  CB  GLN A1105    11360  15714   9931    346   -519   -553       C  
ATOM   2394  CG  GLN A1105      17.348 -22.854 -27.512  1.00104.29           C  
ANISOU 2394  CG  GLN A1105    12295  16561  10769    291   -432   -594       C  
ATOM   2395  CD  GLN A1105      17.819 -21.565 -28.144  1.00116.17           C  
ANISOU 2395  CD  GLN A1105    13874  18045  12219    264   -414   -573       C  
ATOM   2396  OE1 GLN A1105      18.153 -20.581 -27.476  1.00110.75           O  
ANISOU 2396  OE1 GLN A1105    13172  17334  11575    297   -464   -541       O  
ATOM   2397  NE2 GLN A1105      17.894 -21.555 -29.466  1.00106.56           N  
ANISOU 2397  NE2 GLN A1105    12749  16836  10903    187   -343   -590       N  
ATOM   2398  N   MET A1106      18.619 -25.163 -24.865  1.00 99.58           N  
ANISOU 2398  N   MET A1106    11483  15845  10506    325   -532   -532       N  
ATOM   2399  CA  MET A1106      19.696 -26.138 -25.023  1.00100.42           C  
ANISOU 2399  CA  MET A1106    11505  15826  10825    315   -521   -575       C  
ATOM   2400  C   MET A1106      19.478 -27.253 -24.017  1.00105.02           C  
ANISOU 2400  C   MET A1106    12054  16358  11489    309   -641   -484       C  
ATOM   2401  O   MET A1106      19.466 -28.422 -24.400  1.00105.69           O  
ANISOU 2401  O   MET A1106    12089  16358  11711    290   -641   -513       O  
ATOM   2402  CB  MET A1106      21.098 -25.541 -24.832  1.00103.26           C  
ANISOU 2402  CB  MET A1106    11803  16106  11323    333   -518   -612       C  
ATOM   2403  CG  MET A1106      21.777 -25.179 -26.125  1.00107.47           C  
ANISOU 2403  CG  MET A1106    12318  16619  11894    295   -358   -733       C  
ATOM   2404  SD  MET A1106      22.603 -23.580 -26.029  1.00111.66           S  
ANISOU 2404  SD  MET A1106    12860  17151  12414    292   -328   -729       S  
ATOM   2405  CE  MET A1106      21.180 -22.485 -26.007  1.00107.34           C  
ANISOU 2405  CE  MET A1106    12462  16731  11592    305   -378   -634       C  
ATOM   2406  N   GLY A1107      19.331 -26.882 -22.748  1.00101.18           N  
ANISOU 2406  N   GLY A1107    11603  15922  10917    312   -744   -378       N  
ATOM   2407  CA  GLY A1107      19.185 -27.811 -21.637  1.00101.78           C  
ANISOU 2407  CA  GLY A1107    11687  15964  11020    273   -875   -248       C  
ATOM   2408  C   GLY A1107      20.329 -27.643 -20.660  1.00106.24           C  
ANISOU 2408  C   GLY A1107    12234  16451  11680    291  -1019   -192       C  
ATOM   2409  O   GLY A1107      21.334 -27.006 -20.993  1.00105.75           O  
ANISOU 2409  O   GLY A1107    12115  16331  11736    340  -1001   -281       O  
ATOM   2410  N   GLU A1108      20.188 -28.217 -19.452  1.00103.61           N  
ANISOU 2410  N   GLU A1108    11956  16118  11295    237  -1169    -39       N  
ATOM   2411  CA  GLU A1108      21.176 -28.157 -18.368  1.00104.62           C  
ANISOU 2411  CA  GLU A1108    12095  16175  11482    240  -1364     44       C  
ATOM   2412  C   GLU A1108      22.607 -28.430 -18.841  1.00108.71           C  
ANISOU 2412  C   GLU A1108    12479  16477  12347    310  -1440    -41       C  
ATOM   2413  O   GLU A1108      23.501 -27.642 -18.546  1.00108.58           O  
ANISOU 2413  O   GLU A1108    12427  16437  12391    356  -1496    -95       O  
ATOM   2414  CB  GLU A1108      20.785 -29.121 -17.240  1.00107.72           C  
ANISOU 2414  CB  GLU A1108    12582  16560  11787    138  -1530    253       C  
ATOM   2415  CG  GLU A1108      21.233 -28.668 -15.862  1.00119.43           C  
ANISOU 2415  CG  GLU A1108    14160  18103  13114    101  -1709    358       C  
ATOM   2416  CD  GLU A1108      20.710 -29.523 -14.725  1.00143.32           C  
ANISOU 2416  CD  GLU A1108    17326  21166  15963    -44  -1852    590       C  
ATOM   2417  OE1 GLU A1108      19.471 -29.638 -14.588  1.00138.72           O  
ANISOU 2417  OE1 GLU A1108    16811  20750  15147   -140  -1707    630       O  
ATOM   2418  OE2 GLU A1108      21.540 -30.054 -13.951  1.00139.69           O  
ANISOU 2418  OE2 GLU A1108    16910  20568  15597    -73  -2116    735       O  
ATOM   2419  N   THR A1109      22.806 -29.521 -19.601  1.00105.52           N  
ANISOU 2419  N   THR A1109    11983  15915  12197    316  -1430    -84       N  
ATOM   2420  CA  THR A1109      24.105 -29.924 -20.150  1.00106.16           C  
ANISOU 2420  CA  THR A1109    11894  15782  12660    376  -1472   -218       C  
ATOM   2421  C   THR A1109      24.553 -28.960 -21.257  1.00108.28           C  
ANISOU 2421  C   THR A1109    12086  16106  12948    414  -1241   -425       C  
ATOM   2422  O   THR A1109      25.738 -28.624 -21.332  1.00108.50           O  
ANISOU 2422  O   THR A1109    11994  16029  13203    454  -1263   -533       O  
ATOM   2423  CB  THR A1109      24.048 -31.393 -20.611  1.00116.69           C  
ANISOU 2423  CB  THR A1109    13142  16936  14258    364  -1523   -231       C  
ATOM   2424  OG1 THR A1109      23.555 -32.200 -19.538  1.00117.28           O  
ANISOU 2424  OG1 THR A1109    13319  16963  14281    300  -1741      8       O  
ATOM   2425  CG2 THR A1109      25.401 -31.927 -21.072  1.00117.73           C  
ANISOU 2425  CG2 THR A1109    13062  16825  14846    428  -1586   -402       C  
ATOM   2426  N   GLY A1110      23.599 -28.522 -22.083  1.00102.86           N  
ANISOU 2426  N   GLY A1110    11474  15579  12029    388  -1037   -471       N  
ATOM   2427  CA  GLY A1110      23.826 -27.587 -23.181  1.00101.54           C  
ANISOU 2427  CA  GLY A1110    11289  15483  11810    390   -825   -620       C  
ATOM   2428  C   GLY A1110      24.416 -26.257 -22.749  1.00103.93           C  
ANISOU 2428  C   GLY A1110    11602  15827  12058    411   -834   -620       C  
ATOM   2429  O   GLY A1110      25.288 -25.715 -23.435  1.00103.98           O  
ANISOU 2429  O   GLY A1110    11527  15792  12190    407   -716   -747       O  
ATOM   2430  N   VAL A1111      23.965 -25.738 -21.590  1.00 98.82           N  
ANISOU 2430  N   VAL A1111    11049  15265  11233    421   -968   -493       N  
ATOM   2431  CA  VAL A1111      24.439 -24.471 -21.029  1.00 97.81           C  
ANISOU 2431  CA  VAL A1111    10932  15175  11056    447  -1008   -503       C  
ATOM   2432  C   VAL A1111      25.775 -24.685 -20.317  1.00101.91           C  
ANISOU 2432  C   VAL A1111    11340  15538  11842    479  -1181   -519       C  
ATOM   2433  O   VAL A1111      26.725 -23.949 -20.591  1.00101.75           O  
ANISOU 2433  O   VAL A1111    11227  15455  11980    497  -1137   -623       O  
ATOM   2434  CB  VAL A1111      23.380 -23.784 -20.122  1.00100.87           C  
ANISOU 2434  CB  VAL A1111    11449  15732  11146    441  -1064   -415       C  
ATOM   2435  CG1 VAL A1111      23.818 -22.376 -19.724  1.00100.53           C  
ANISOU 2435  CG1 VAL A1111    11403  15721  11075    472  -1087   -468       C  
ATOM   2436  CG2 VAL A1111      22.022 -23.735 -20.812  1.00 99.63           C  
ANISOU 2436  CG2 VAL A1111    11367  15698  10789    417   -927   -412       C  
ATOM   2437  N   ALA A1112      25.855 -25.728 -19.451  1.00 98.54           N  
ANISOU 2437  N   ALA A1112    10920  15031  11490    478  -1389   -411       N  
ATOM   2438  CA  ALA A1112      27.032 -26.118 -18.660  1.00 99.38           C  
ANISOU 2438  CA  ALA A1112    10934  14962  11865    511  -1632   -396       C  
ATOM   2439  C   ALA A1112      28.311 -26.271 -19.482  1.00103.20           C  
ANISOU 2439  C   ALA A1112    11199  15257  12755    550  -1572   -582       C  
ATOM   2440  O   ALA A1112      29.408 -26.109 -18.939  1.00104.47           O  
ANISOU 2440  O   ALA A1112    11250  15284  13161    590  -1742   -625       O  
ATOM   2441  CB  ALA A1112      26.747 -27.398 -17.888  1.00101.31           C  
ANISOU 2441  CB  ALA A1112    11237  15127  12130    481  -1856   -226       C  
ATOM   2442  N   GLY A1113      28.153 -26.562 -20.775  1.00 98.15           N  
ANISOU 2442  N   GLY A1113    10496  14619  12178    529  -1327   -708       N  
ATOM   2443  CA  GLY A1113      29.248 -26.741 -21.723  1.00 98.52           C  
ANISOU 2443  CA  GLY A1113    10330  14528  12577    535  -1191   -928       C  
ATOM   2444  C   GLY A1113      30.057 -25.492 -22.023  1.00100.89           C  
ANISOU 2444  C   GLY A1113    10555  14847  12933    524  -1059  -1045       C  
ATOM   2445  O   GLY A1113      31.258 -25.592 -22.286  1.00102.31           O  
ANISOU 2445  O   GLY A1113    10522  14874  13476    535  -1038  -1216       O  
ATOM   2446  N   PHE A1114      29.407 -24.309 -22.010  1.00 94.53           N  
ANISOU 2446  N   PHE A1114     9904  14212  11801    497   -970   -969       N  
ATOM   2447  CA  PHE A1114      30.047 -23.019 -22.293  1.00 93.95           C  
ANISOU 2447  CA  PHE A1114     9784  14152  11759    471   -852  -1048       C  
ATOM   2448  C   PHE A1114      30.975 -22.568 -21.145  1.00 97.82           C  
ANISOU 2448  C   PHE A1114    10184  14535  12448    529  -1090  -1051       C  
ATOM   2449  O   PHE A1114      30.705 -21.564 -20.483  1.00 96.54           O  
ANISOU 2449  O   PHE A1114    10120  14453  12108    542  -1171   -981       O  
ATOM   2450  CB  PHE A1114      28.988 -21.946 -22.622  1.00 94.15           C  
ANISOU 2450  CB  PHE A1114    10000  14357  11414    433   -730   -959       C  
ATOM   2451  CG  PHE A1114      28.109 -22.225 -23.817  1.00 95.04           C  
ANISOU 2451  CG  PHE A1114    10211  14573  11327    370   -520   -959       C  
ATOM   2452  CD1 PHE A1114      28.615 -22.143 -25.109  1.00 99.00           C  
ANISOU 2452  CD1 PHE A1114    10652  15064  11897    282   -271  -1086       C  
ATOM   2453  CD2 PHE A1114      26.761 -22.519 -23.655  1.00 95.97           C  
ANISOU 2453  CD2 PHE A1114    10483  14809  11172    385   -567   -843       C  
ATOM   2454  CE1 PHE A1114      27.796 -22.389 -26.215  1.00 99.48           C  
ANISOU 2454  CE1 PHE A1114    10828  15233  11738    214   -102  -1087       C  
ATOM   2455  CE2 PHE A1114      25.944 -22.767 -24.764  1.00 98.15           C  
ANISOU 2455  CE2 PHE A1114    10845  15171  11274    331   -405   -852       C  
ATOM   2456  CZ  PHE A1114      26.464 -22.690 -26.034  1.00 97.00           C  
ANISOU 2456  CZ  PHE A1114    10661  15017  11177    249   -187   -968       C  
ATOM   2457  N   THR A1115      32.084 -23.307 -20.945  1.00 95.67           N  
ANISOU 2457  N   THR A1115     9710  14070  12572    565  -1212  -1156       N  
ATOM   2458  CA  THR A1115      33.095 -23.111 -19.899  1.00 96.74           C  
ANISOU 2458  CA  THR A1115     9726  14060  12969    626  -1488  -1178       C  
ATOM   2459  C   THR A1115      33.598 -21.668 -19.714  1.00100.15           C  
ANISOU 2459  C   THR A1115    10132  14518  13404    614  -1452  -1233       C  
ATOM   2460  O   THR A1115      33.441 -21.118 -18.620  1.00 99.62           O  
ANISOU 2460  O   THR A1115    10163  14494  13195    653  -1676  -1141       O  
ATOM   2461  CB  THR A1115      34.223 -24.138 -20.061  1.00107.36           C  
ANISOU 2461  CB  THR A1115    10811  15167  14815    663  -1579  -1333       C  
ATOM   2462  OG1 THR A1115      33.665 -25.451 -19.986  1.00106.69           O  
ANISOU 2462  OG1 THR A1115    10776  15038  14724    683  -1690  -1247       O  
ATOM   2463  CG2 THR A1115      35.334 -23.972 -19.023  1.00108.55           C  
ANISOU 2463  CG2 THR A1115    10818  15138  15289    732  -1903  -1369       C  
ATOM   2464  N   ASN A1116      34.209 -21.074 -20.767  1.00 96.75           N  
ANISOU 2464  N   ASN A1116     9568  14060  13132    546  -1170  -1387       N  
ATOM   2465  CA  ASN A1116      34.765 -19.715 -20.749  1.00 96.66           C  
ANISOU 2465  CA  ASN A1116     9506  14039  13181    512  -1108  -1444       C  
ATOM   2466  C   ASN A1116      33.727 -18.634 -20.450  1.00 98.11           C  
ANISOU 2466  C   ASN A1116     9922  14388  12968    505  -1112  -1301       C  
ATOM   2467  O   ASN A1116      33.939 -17.830 -19.542  1.00 98.00           O  
ANISOU 2467  O   ASN A1116     9915  14359  12962    547  -1297  -1292       O  
ATOM   2468  CB  ASN A1116      35.509 -19.402 -22.048  1.00 98.75           C  
ANISOU 2468  CB  ASN A1116     9608  14259  13652    398   -764  -1613       C  
ATOM   2469  CG  ASN A1116      36.954 -19.813 -22.042  1.00127.79           C  
ANISOU 2469  CG  ASN A1116    12969  17734  17853    409   -789  -1831       C  
ATOM   2470  OD1 ASN A1116      37.745 -19.399 -21.184  1.00122.99           O  
ANISOU 2470  OD1 ASN A1116    12233  17000  17499    467  -1014  -1879       O  
ATOM   2471  ND2 ASN A1116      37.342 -20.588 -23.043  1.00122.72           N  
ANISOU 2471  ND2 ASN A1116    12174  17054  17399    346   -549  -1997       N  
ATOM   2472  N   SER A1117      32.607 -18.634 -21.200  1.00 92.54           N  
ANISOU 2472  N   SER A1117     9390  13830  11941    456   -926  -1211       N  
ATOM   2473  CA  SER A1117      31.503 -17.682 -21.061  1.00 90.70           C  
ANISOU 2473  CA  SER A1117     9356  13739  11367    453   -922  -1096       C  
ATOM   2474  C   SER A1117      30.821 -17.741 -19.691  1.00 93.79           C  
ANISOU 2474  C   SER A1117     9861  14211  11563    538  -1189  -1009       C  
ATOM   2475  O   SER A1117      30.514 -16.688 -19.134  1.00 93.10           O  
ANISOU 2475  O   SER A1117     9835  14175  11363    559  -1265  -1002       O  
ATOM   2476  CB  SER A1117      30.489 -17.857 -22.185  1.00 93.16           C  
ANISOU 2476  CB  SER A1117     9808  14167  11422    387   -704  -1031       C  
ATOM   2477  OG  SER A1117      30.617 -19.111 -22.833  1.00102.60           O  
ANISOU 2477  OG  SER A1117    10947  15343  12694    363   -599  -1079       O  
ATOM   2478  N   LEU A1118      30.616 -18.959 -19.135  1.00 90.34           N  
ANISOU 2478  N   LEU A1118     9448  13781  11097    575  -1331   -951       N  
ATOM   2479  CA  LEU A1118      30.022 -19.157 -17.805  1.00 90.12           C  
ANISOU 2479  CA  LEU A1118     9543  13845  10854    618  -1573   -856       C  
ATOM   2480  C   LEU A1118      30.929 -18.584 -16.720  1.00 96.05           C  
ANISOU 2480  C   LEU A1118    10225  14523  11747    660  -1814   -912       C  
ATOM   2481  O   LEU A1118      30.440 -18.004 -15.751  1.00 95.59           O  
ANISOU 2481  O   LEU A1118    10276  14581  11464    675  -1946   -890       O  
ATOM   2482  CB  LEU A1118      29.783 -20.645 -17.523  1.00 90.44           C  
ANISOU 2482  CB  LEU A1118     9616  13865  10881    620  -1683   -759       C  
ATOM   2483  CG  LEU A1118      28.471 -21.237 -18.008  1.00 93.61           C  
ANISOU 2483  CG  LEU A1118    10151  14398  11018    584  -1542   -666       C  
ATOM   2484  CD1 LEU A1118      28.577 -22.736 -18.096  1.00 94.37           C  
ANISOU 2484  CD1 LEU A1118    10212  14396  11248    579  -1613   -610       C  
ATOM   2485  CD2 LEU A1118      27.313 -20.852 -17.092  1.00 95.30           C  
ANISOU 2485  CD2 LEU A1118    10539  14805  10867    573  -1610   -578       C  
ATOM   2486  N   ARG A1119      32.252 -18.758 -16.892  1.00 94.90           N  
ANISOU 2486  N   ARG A1119     9883  14186  11989    676  -1869  -1012       N  
ATOM   2487  CA  ARG A1119      33.283 -18.250 -15.994  1.00 96.92           C  
ANISOU 2487  CA  ARG A1119    10032  14333  12460    718  -2111  -1092       C  
ATOM   2488  C   ARG A1119      33.303 -16.719 -16.090  1.00101.74           C  
ANISOU 2488  C   ARG A1119    10633  14980  13043    707  -2014  -1177       C  
ATOM   2489  O   ARG A1119      33.408 -16.050 -15.062  1.00102.28           O  
ANISOU 2489  O   ARG A1119    10735  15079  13049    741  -2220  -1209       O  
ATOM   2490  CB  ARG A1119      34.647 -18.861 -16.366  1.00 99.04           C  
ANISOU 2490  CB  ARG A1119    10050  14369  13212    734  -2153  -1207       C  
ATOM   2491  CG  ARG A1119      35.805 -18.484 -15.438  1.00112.13           C  
ANISOU 2491  CG  ARG A1119    11565  15878  15159    787  -2450  -1301       C  
ATOM   2492  CD  ARG A1119      37.140 -19.004 -15.948  1.00124.41           C  
ANISOU 2492  CD  ARG A1119    12824  17191  17255    801  -2453  -1460       C  
ATOM   2493  NE  ARG A1119      37.405 -18.575 -17.325  1.00133.89           N  
ANISOU 2493  NE  ARG A1119    13887  18373  18610    724  -2051  -1588       N  
ATOM   2494  CZ  ARG A1119      38.515 -17.971 -17.733  1.00151.33           C  
ANISOU 2494  CZ  ARG A1119    15854  20443  21202    692  -1948  -1770       C  
ATOM   2495  NH1 ARG A1119      38.651 -17.611 -19.000  1.00138.96           N  
ANISOU 2495  NH1 ARG A1119    14206  18893  19698    585  -1558  -1858       N  
ATOM   2496  NH2 ARG A1119      39.503 -17.728 -16.877  1.00141.06           N  
ANISOU 2496  NH2 ARG A1119    14392  18986  20219    753  -2239  -1867       N  
ATOM   2497  N   MET A1120      33.162 -16.179 -17.322  1.00 98.16           N  
ANISOU 2497  N   MET A1120    10149  14524  12622    647  -1713  -1207       N  
ATOM   2498  CA  MET A1120      33.130 -14.740 -17.602  1.00 98.24           C  
ANISOU 2498  CA  MET A1120    10158  14536  12635    618  -1610  -1257       C  
ATOM   2499  C   MET A1120      31.854 -14.084 -17.069  1.00101.52           C  
ANISOU 2499  C   MET A1120    10761  15119  12692    645  -1659  -1199       C  
ATOM   2500  O   MET A1120      31.892 -12.918 -16.674  1.00101.64           O  
ANISOU 2500  O   MET A1120    10766  15121  12733    660  -1724  -1268       O  
ATOM   2501  CB  MET A1120      33.309 -14.462 -19.098  1.00100.66           C  
ANISOU 2501  CB  MET A1120    10412  14791  13042    517  -1290  -1267       C  
ATOM   2502  CG  MET A1120      34.741 -14.567 -19.556  1.00106.50           C  
ANISOU 2502  CG  MET A1120    10914  15356  14196    468  -1208  -1397       C  
ATOM   2503  SD  MET A1120      34.875 -14.673 -21.352  1.00111.51           S  
ANISOU 2503  SD  MET A1120    11518  15988  14861    311   -791  -1410       S  
ATOM   2504  CE  MET A1120      36.610 -15.032 -21.513  1.00110.86           C  
ANISOU 2504  CE  MET A1120    11102  15709  15313    275   -737  -1623       C  
ATOM   2505  N   LEU A1121      30.731 -14.834 -17.044  1.00 97.12           N  
ANISOU 2505  N   LEU A1121    10355  14711  11836    649  -1629  -1096       N  
ATOM   2506  CA  LEU A1121      29.463 -14.346 -16.497  1.00 96.26           C  
ANISOU 2506  CA  LEU A1121    10396  14772  11406    671  -1662  -1073       C  
ATOM   2507  C   LEU A1121      29.563 -14.307 -14.969  1.00101.91           C  
ANISOU 2507  C   LEU A1121    11144  15561  12017    713  -1921  -1120       C  
ATOM   2508  O   LEU A1121      29.083 -13.359 -14.345  1.00102.40           O  
ANISOU 2508  O   LEU A1121    11246  15709  11954    735  -1978  -1205       O  
ATOM   2509  CB  LEU A1121      28.276 -15.226 -16.938  1.00 94.91           C  
ANISOU 2509  CB  LEU A1121    10351  14732  10979    648  -1543   -963       C  
ATOM   2510  CG  LEU A1121      27.800 -15.092 -18.389  1.00 98.49           C  
ANISOU 2510  CG  LEU A1121    10829  15169  11424    601  -1306   -919       C  
ATOM   2511  CD1 LEU A1121      26.811 -16.182 -18.734  1.00 97.63           C  
ANISOU 2511  CD1 LEU A1121    10817  15167  11111    585  -1229   -828       C  
ATOM   2512  CD2 LEU A1121      27.196 -13.718 -18.670  1.00100.62           C  
ANISOU 2512  CD2 LEU A1121    11137  15450  11645    603  -1264   -951       C  
ATOM   2513  N   GLN A1122      30.220 -15.328 -14.381  1.00 99.04           N  
ANISOU 2513  N   GLN A1122    10762  15153  11717    719  -2091  -1073       N  
ATOM   2514  CA  GLN A1122      30.453 -15.474 -12.945  1.00100.32           C  
ANISOU 2514  CA  GLN A1122    10981  15375  11762    735  -2375  -1084       C  
ATOM   2515  C   GLN A1122      31.391 -14.370 -12.440  1.00105.67           C  
ANISOU 2515  C   GLN A1122    11544  15956  12648    773  -2523  -1241       C  
ATOM   2516  O   GLN A1122      31.208 -13.877 -11.325  1.00106.68           O  
ANISOU 2516  O   GLN A1122    11745  16197  12590    782  -2696  -1313       O  
ATOM   2517  CB  GLN A1122      31.055 -16.860 -12.661  1.00102.60           C  
ANISOU 2517  CB  GLN A1122    11262  15573  12150    728  -2549   -971       C  
ATOM   2518  CG  GLN A1122      31.086 -17.267 -11.195  1.00117.71           C  
ANISOU 2518  CG  GLN A1122    13304  17571  13849    711  -2863   -908       C  
ATOM   2519  CD  GLN A1122      31.834 -18.562 -11.033  1.00140.38           C  
ANISOU 2519  CD  GLN A1122    16141  20280  16919    711  -3078   -788       C  
ATOM   2520  OE1 GLN A1122      33.063 -18.588 -10.912  1.00138.53           O  
ANISOU 2520  OE1 GLN A1122    15752  19845  17038    758  -3272   -855       O  
ATOM   2521  NE2 GLN A1122      31.116 -19.673 -11.080  1.00132.50           N  
ANISOU 2521  NE2 GLN A1122    15262  19337  15744    661  -3053   -618       N  
ATOM   2522  N   GLN A1123      32.383 -13.981 -13.269  1.00101.96           N  
ANISOU 2522  N   GLN A1123    10892  15287  12562    781  -2440  -1310       N  
ATOM   2523  CA  GLN A1123      33.376 -12.953 -12.947  1.00102.95           C  
ANISOU 2523  CA  GLN A1123    10871  15281  12964    808  -2559  -1463       C  
ATOM   2524  C   GLN A1123      32.968 -11.541 -13.401  1.00105.88           C  
ANISOU 2524  C   GLN A1123    11226  15654  13349    798  -2403  -1549       C  
ATOM   2525  O   GLN A1123      33.811 -10.639 -13.416  1.00106.58           O  
ANISOU 2525  O   GLN A1123    11171  15597  13729    803  -2447  -1667       O  
ATOM   2526  CB  GLN A1123      34.760 -13.340 -13.499  1.00105.29           C  
ANISOU 2526  CB  GLN A1123    10949  15345  13712    804  -2566  -1507       C  
ATOM   2527  CG  GLN A1123      35.382 -14.554 -12.810  1.00119.83           C  
ANISOU 2527  CG  GLN A1123    12764  17120  15645    837  -2834  -1461       C  
ATOM   2528  CD  GLN A1123      36.661 -15.020 -13.462  1.00139.27           C  
ANISOU 2528  CD  GLN A1123    14973  19343  18599    839  -2814  -1539       C  
ATOM   2529  OE1 GLN A1123      37.671 -15.256 -12.788  1.00138.22           O  
ANISOU 2529  OE1 GLN A1123    14710  19063  18744    884  -3100  -1611       O  
ATOM   2530  NE2 GLN A1123      36.650 -15.188 -14.781  1.00127.88           N  
ANISOU 2530  NE2 GLN A1123    13450  17859  17281    785  -2481  -1544       N  
ATOM   2531  N   LYS A1124      31.674 -11.349 -13.756  1.00100.58           N  
ANISOU 2531  N   LYS A1124    10691  15128  12396    785  -2241  -1491       N  
ATOM   2532  CA  LYS A1124      31.084 -10.074 -14.199  1.00 99.88           C  
ANISOU 2532  CA  LYS A1124    10607  15030  12315    782  -2127  -1551       C  
ATOM   2533  C   LYS A1124      31.642  -9.497 -15.518  1.00103.54           C  
ANISOU 2533  C   LYS A1124    10968  15305  13067    721  -1935  -1517       C  
ATOM   2534  O   LYS A1124      31.245  -8.397 -15.915  1.00103.02           O  
ANISOU 2534  O   LYS A1124    10907  15188  13048    708  -1877  -1539       O  
ATOM   2535  CB  LYS A1124      31.076  -9.020 -13.065  1.00103.84           C  
ANISOU 2535  CB  LYS A1124    11086  15563  12804    833  -2323  -1734       C  
ATOM   2536  CG  LYS A1124      29.847  -9.061 -12.164  1.00118.08           C  
ANISOU 2536  CG  LYS A1124    13031  17608  14228    858  -2375  -1789       C  
ATOM   2537  CD  LYS A1124      29.947 -10.096 -11.045  1.00129.37           C  
ANISOU 2537  CD  LYS A1124    14556  19188  15409    848  -2547  -1758       C  
ATOM   2538  CE  LYS A1124      28.642 -10.264 -10.306  1.00140.95           C  
ANISOU 2538  CE  LYS A1124    16171  20920  16462    829  -2523  -1792       C  
ATOM   2539  NZ  LYS A1124      27.633 -11.005 -11.114  1.00149.53           N  
ANISOU 2539  NZ  LYS A1124    17338  22082  17395    798  -2310  -1638       N  
ATOM   2540  N   ARG A1125      32.531 -10.243 -16.209  1.00100.45           N  
ANISOU 2540  N   ARG A1125    10485  14811  12869    671  -1834  -1464       N  
ATOM   2541  CA  ARG A1125      33.124  -9.848 -17.492  1.00100.60           C  
ANISOU 2541  CA  ARG A1125    10415  14683  13124    573  -1609  -1433       C  
ATOM   2542  C   ARG A1125      32.064  -9.999 -18.597  1.00102.84           C  
ANISOU 2542  C   ARG A1125    10851  15053  13170    514  -1391  -1292       C  
ATOM   2543  O   ARG A1125      32.065 -11.001 -19.316  1.00101.52           O  
ANISOU 2543  O   ARG A1125    10704  14922  12948    470  -1241  -1226       O  
ATOM   2544  CB  ARG A1125      34.368 -10.709 -17.788  1.00102.00           C  
ANISOU 2544  CB  ARG A1125    10425  14749  13580    538  -1562  -1474       C  
ATOM   2545  CG  ARG A1125      35.664 -10.157 -17.206  1.00116.68           C  
ANISOU 2545  CG  ARG A1125    12078  16440  15815    551  -1712  -1622       C  
ATOM   2546  CD  ARG A1125      36.486  -9.457 -18.274  1.00130.91           C  
ANISOU 2546  CD  ARG A1125    13737  18083  17921    423  -1478  -1652       C  
ATOM   2547  NE  ARG A1125      37.522  -8.590 -17.707  1.00143.20           N  
ANISOU 2547  NE  ARG A1125    15104  19472  19833    430  -1622  -1797       N  
ATOM   2548  CZ  ARG A1125      38.233  -7.713 -18.409  1.00158.52           C  
ANISOU 2548  CZ  ARG A1125    16913  21258  22058    309  -1457  -1830       C  
ATOM   2549  NH1 ARG A1125      39.151  -6.965 -17.812  1.00147.54           N  
ANISOU 2549  NH1 ARG A1125    15339  19710  21011    322  -1612  -1974       N  
ATOM   2550  NH2 ARG A1125      38.028  -7.574 -19.715  1.00144.73           N  
ANISOU 2550  NH2 ARG A1125    15228  19517  20246    158  -1141  -1716       N  
ATOM   2551  N   TRP A1126      31.132  -9.016 -18.690  1.00 99.29           N  
ANISOU 2551  N   TRP A1126    10501  14629  12596    523  -1402  -1265       N  
ATOM   2552  CA  TRP A1126      30.001  -9.028 -19.631  1.00 98.19           C  
ANISOU 2552  CA  TRP A1126    10513  14560  12233    483  -1264  -1136       C  
ATOM   2553  C   TRP A1126      30.367  -9.053 -21.113  1.00102.16           C  
ANISOU 2553  C   TRP A1126    11037  14985  12795    340  -1028  -1023       C  
ATOM   2554  O   TRP A1126      30.015 -10.018 -21.794  1.00100.68           O  
ANISOU 2554  O   TRP A1126    10923  14889  12442    302   -892   -951       O  
ATOM   2555  CB  TRP A1126      28.943  -7.939 -19.320  1.00 96.97           C  
ANISOU 2555  CB  TRP A1126    10429  14419  11997    538  -1376  -1160       C  
ATOM   2556  CG  TRP A1126      28.516  -7.829 -17.880  1.00 98.07           C  
ANISOU 2556  CG  TRP A1126    10551  14668  12045    655  -1572  -1310       C  
ATOM   2557  CD1 TRP A1126      28.443  -6.687 -17.139  1.00102.01           C  
ANISOU 2557  CD1 TRP A1126    10990  15112  12656    712  -1723  -1455       C  
ATOM   2558  CD2 TRP A1126      28.090  -8.896 -17.017  1.00 97.22           C  
ANISOU 2558  CD2 TRP A1126    10493  14748  11698    708  -1629  -1335       C  
ATOM   2559  NE1 TRP A1126      28.014  -6.975 -15.864  1.00101.57           N  
ANISOU 2559  NE1 TRP A1126    10947  15226  12419    791  -1854  -1590       N  
ATOM   2560  CE2 TRP A1126      27.801  -8.325 -15.757  1.00101.92           C  
ANISOU 2560  CE2 TRP A1126    11069  15421  12235    780  -1800  -1500       C  
ATOM   2561  CE3 TRP A1126      27.947 -10.286 -17.176  1.00 97.51           C  
ANISOU 2561  CE3 TRP A1126    10591  14890  11570    689  -1556  -1237       C  
ATOM   2562  CZ2 TRP A1126      27.355  -9.091 -14.673  1.00101.14           C  
ANISOU 2562  CZ2 TRP A1126    11033  15521  11876    811  -1884  -1547       C  
ATOM   2563  CZ3 TRP A1126      27.528 -11.044 -16.094  1.00 98.86           C  
ANISOU 2563  CZ3 TRP A1126    10814  15223  11524    729  -1663  -1265       C  
ATOM   2564  CH2 TRP A1126      27.255 -10.450 -14.855  1.00100.36           C  
ANISOU 2564  CH2 TRP A1126    11006  15507  11621    778  -1819  -1408       C  
ATOM   2565  N   ASP A1127      31.070  -8.008 -21.610  1.00100.24           N  
ANISOU 2565  N   ASP A1127    10733  14579  12776    244   -974  -1012       N  
ATOM   2566  CA  ASP A1127      31.477  -7.894 -23.015  1.00101.06           C  
ANISOU 2566  CA  ASP A1127    10872  14618  12909     64   -731   -899       C  
ATOM   2567  C   ASP A1127      32.297  -9.087 -23.488  1.00104.55           C  
ANISOU 2567  C   ASP A1127    11224  15102  13396     -2   -537   -948       C  
ATOM   2568  O   ASP A1127      32.100  -9.535 -24.614  1.00104.17           O  
ANISOU 2568  O   ASP A1127    11271  15116  13195   -120   -327   -866       O  
ATOM   2569  CB  ASP A1127      32.213  -6.570 -23.280  1.00105.17           C  
ANISOU 2569  CB  ASP A1127    11323  14943  13694    -44   -719   -883       C  
ATOM   2570  CG  ASP A1127      31.335  -5.328 -23.240  1.00117.80           C  
ANISOU 2570  CG  ASP A1127    13030  16458  15271    -20   -879   -801       C  
ATOM   2571  OD1 ASP A1127      30.141  -5.425 -23.612  1.00117.44           O  
ANISOU 2571  OD1 ASP A1127    13151  16497  14976      9   -911   -698       O  
ATOM   2572  OD2 ASP A1127      31.852  -4.249 -22.880  1.00126.12           O  
ANISOU 2572  OD2 ASP A1127    13987  17342  16591    -32   -981   -848       O  
ATOM   2573  N   GLU A1128      33.172  -9.626 -22.613  1.00101.15           N  
ANISOU 2573  N   GLU A1128    10613  14640  13180     78   -628  -1097       N  
ATOM   2574  CA  GLU A1128      33.999 -10.801 -22.888  1.00101.29           C  
ANISOU 2574  CA  GLU A1128    10497  14663  13327     48   -497  -1187       C  
ATOM   2575  C   GLU A1128      33.133 -12.051 -23.030  1.00103.50           C  
ANISOU 2575  C   GLU A1128    10892  15094  13339    105   -481  -1139       C  
ATOM   2576  O   GLU A1128      33.374 -12.842 -23.939  1.00103.59           O  
ANISOU 2576  O   GLU A1128    10880  15135  13343     18   -268  -1160       O  
ATOM   2577  CB  GLU A1128      35.061 -10.995 -21.795  1.00103.54           C  
ANISOU 2577  CB  GLU A1128    10563  14843  13934    141   -685  -1347       C  
ATOM   2578  CG  GLU A1128      36.449 -10.525 -22.197  1.00116.23           C  
ANISOU 2578  CG  GLU A1128    11946  16286  15931     26   -548  -1463       C  
ATOM   2579  CD  GLU A1128      37.590 -11.425 -21.756  1.00138.58           C  
ANISOU 2579  CD  GLU A1128    14525  19027  19102     77   -610  -1641       C  
ATOM   2580  OE1 GLU A1128      37.705 -11.700 -20.539  1.00130.47           O  
ANISOU 2580  OE1 GLU A1128    13452  17975  18145    227   -920  -1694       O  
ATOM   2581  OE2 GLU A1128      38.389 -11.833 -22.629  1.00134.70           O  
ANISOU 2581  OE2 GLU A1128    13878  18485  18817    -43   -355  -1739       O  
ATOM   2582  N   ALA A1129      32.112 -12.210 -22.153  1.00 98.62           N  
ANISOU 2582  N   ALA A1129    10392  14575  12504    236   -688  -1090       N  
ATOM   2583  CA  ALA A1129      31.178 -13.342 -22.171  1.00 97.06           C  
ANISOU 2583  CA  ALA A1129    10306  14515  12055    288   -694  -1033       C  
ATOM   2584  C   ALA A1129      30.324 -13.322 -23.434  1.00100.83           C  
ANISOU 2584  C   ALA A1129    10942  15071  12297    194   -501   -927       C  
ATOM   2585  O   ALA A1129      30.171 -14.363 -24.070  1.00100.64           O  
ANISOU 2585  O   ALA A1129    10940  15108  12192    161   -375   -927       O  
ATOM   2586  CB  ALA A1129      30.287 -13.321 -20.937  1.00 96.66           C  
ANISOU 2586  CB  ALA A1129    10341  14559  11824    413   -931  -1013       C  
ATOM   2587  N   ALA A1130      29.800 -12.132 -23.808  1.00 96.97           N  
ANISOU 2587  N   ALA A1130    10560  14563  11722    150   -500   -843       N  
ATOM   2588  CA  ALA A1130      28.964 -11.916 -24.989  1.00 96.28           C  
ANISOU 2588  CA  ALA A1130    10646  14527  11409     55   -377   -717       C  
ATOM   2589  C   ALA A1130      29.731 -12.178 -26.289  1.00101.26           C  
ANISOU 2589  C   ALA A1130    11269  15140  12066   -126   -105   -712       C  
ATOM   2590  O   ALA A1130      29.189 -12.822 -27.188  1.00101.04           O  
ANISOU 2590  O   ALA A1130    11356  15210  11825   -190     19   -667       O  
ATOM   2591  CB  ALA A1130      28.402 -10.504 -24.981  1.00 97.29           C  
ANISOU 2591  CB  ALA A1130    10862  14584  11520     52   -494   -632       C  
ATOM   2592  N   VAL A1131      30.988 -11.699 -26.382  1.00 98.94           N  
ANISOU 2592  N   VAL A1131    10831  14731  12031   -218     -4   -780       N  
ATOM   2593  CA  VAL A1131      31.849 -11.895 -27.553  1.00100.58           C  
ANISOU 2593  CA  VAL A1131    10997  14932  12288   -417    296   -816       C  
ATOM   2594  C   VAL A1131      32.200 -13.385 -27.704  1.00104.83           C  
ANISOU 2594  C   VAL A1131    11421  15543  12868   -393    418   -968       C  
ATOM   2595  O   VAL A1131      32.125 -13.917 -28.814  1.00105.04           O  
ANISOU 2595  O   VAL A1131    11515  15658  12737   -524    646   -982       O  
ATOM   2596  CB  VAL A1131      33.083 -10.946 -27.527  1.00106.32           C  
ANISOU 2596  CB  VAL A1131    11571  15507  13321   -528    375   -865       C  
ATOM   2597  CG1 VAL A1131      34.234 -11.460 -28.389  1.00108.23           C  
ANISOU 2597  CG1 VAL A1131    11663  15749  13711   -708    700  -1003       C  
ATOM   2598  CG2 VAL A1131      32.688  -9.533 -27.951  1.00106.99           C  
ANISOU 2598  CG2 VAL A1131    11818  15517  13318   -636    337   -677       C  
ATOM   2599  N   ASN A1132      32.512 -14.057 -26.577  1.00101.34           N  
ANISOU 2599  N   ASN A1132    10820  15059  12625   -226    240  -1079       N  
ATOM   2600  CA  ASN A1132      32.838 -15.485 -26.529  1.00101.51           C  
ANISOU 2600  CA  ASN A1132    10713  15099  12757   -173    277  -1217       C  
ATOM   2601  C   ASN A1132      31.619 -16.342 -26.913  1.00104.38           C  
ANISOU 2601  C   ASN A1132    11251  15601  12807   -139    276  -1142       C  
ATOM   2602  O   ASN A1132      31.767 -17.297 -27.679  1.00104.68           O  
ANISOU 2602  O   ASN A1132    11249  15681  12842   -199    451  -1241       O  
ATOM   2603  CB  ASN A1132      33.371 -15.868 -25.146  1.00102.34           C  
ANISOU 2603  CB  ASN A1132    10649  15104  13129     -9     14  -1298       C  
ATOM   2604  CG  ASN A1132      34.085 -17.192 -25.110  1.00128.11           C  
ANISOU 2604  CG  ASN A1132    13719  18308  16650     28     32  -1461       C  
ATOM   2605  OD1 ASN A1132      35.295 -17.278 -25.340  1.00121.70           O  
ANISOU 2605  OD1 ASN A1132    12676  17383  16181    -27    145  -1635       O  
ATOM   2606  ND2 ASN A1132      33.351 -18.253 -24.809  1.00121.64           N  
ANISOU 2606  ND2 ASN A1132    12970  17543  15704    121    -88  -1418       N  
ATOM   2607  N   LEU A1133      30.417 -15.980 -26.404  1.00 99.31           N  
ANISOU 2607  N   LEU A1133    10785  15025  11923    -48     87   -993       N  
ATOM   2608  CA  LEU A1133      29.155 -16.669 -26.700  1.00 97.81           C  
ANISOU 2608  CA  LEU A1133    10754  14959  11451    -13     64   -917       C  
ATOM   2609  C   LEU A1133      28.746 -16.488 -28.164  1.00103.66           C  
ANISOU 2609  C   LEU A1133    11648  15779  11961   -168    274   -865       C  
ATOM   2610  O   LEU A1133      28.095 -17.370 -28.723  1.00103.22           O  
ANISOU 2610  O   LEU A1133    11665  15813  11740   -177    329   -875       O  
ATOM   2611  CB  LEU A1133      28.022 -16.170 -25.787  1.00 96.00           C  
ANISOU 2611  CB  LEU A1133    10642  14777  11058    105   -169   -803       C  
ATOM   2612  CG  LEU A1133      27.782 -16.893 -24.465  1.00 99.31           C  
ANISOU 2612  CG  LEU A1133    11005  15211  11515    244   -373   -821       C  
ATOM   2613  CD1 LEU A1133      26.922 -16.055 -23.552  1.00 98.35           C  
ANISOU 2613  CD1 LEU A1133    10966  15138  11264    325   -554   -759       C  
ATOM   2614  CD2 LEU A1133      27.119 -18.245 -24.677  1.00100.99           C  
ANISOU 2614  CD2 LEU A1133    11256  15498  11617    264   -353   -814       C  
ATOM   2615  N   ALA A1134      29.115 -15.341 -28.777  1.00101.76           N  
ANISOU 2615  N   ALA A1134    11465  15499  11701   -301    374   -801       N  
ATOM   2616  CA  ALA A1134      28.825 -15.050 -30.182  1.00102.88           C  
ANISOU 2616  CA  ALA A1134    11784  15713  11593   -487    558   -721       C  
ATOM   2617  C   ALA A1134      29.621 -16.001 -31.092  1.00108.09           C  
ANISOU 2617  C   ALA A1134    12353  16431  12286   -620    849   -892       C  
ATOM   2618  O   ALA A1134      29.137 -16.369 -32.162  1.00108.50           O  
ANISOU 2618  O   ALA A1134    12553  16598  12074   -735    984   -878       O  
ATOM   2619  CB  ALA A1134      29.163 -13.602 -30.497  1.00105.07           C  
ANISOU 2619  CB  ALA A1134    12134  15904  11882   -614    577   -595       C  
ATOM   2620  N   LYS A1135      30.823 -16.422 -30.646  1.00104.85           N  
ANISOU 2620  N   LYS A1135    11686  15937  12214   -600    931  -1077       N  
ATOM   2621  CA  LYS A1135      31.679 -17.369 -31.361  1.00106.03           C  
ANISOU 2621  CA  LYS A1135    11678  16117  12493   -703   1201  -1307       C  
ATOM   2622  C   LYS A1135      31.280 -18.795 -30.949  1.00107.86           C  
ANISOU 2622  C   LYS A1135    11827  16362  12794   -544   1091  -1416       C  
ATOM   2623  O   LYS A1135      32.065 -19.509 -30.319  1.00107.81           O  
ANISOU 2623  O   LYS A1135    11579  16249  13136   -451   1045  -1581       O  
ATOM   2624  CB  LYS A1135      33.169 -17.084 -31.079  1.00110.14           C  
ANISOU 2624  CB  LYS A1135    11928  16509  13409   -755   1320  -1471       C  
ATOM   2625  CG  LYS A1135      33.737 -15.931 -31.893  1.00125.42           C  
ANISOU 2625  CG  LYS A1135    13923  18450  15279   -995   1553  -1413       C  
ATOM   2626  CD  LYS A1135      35.261 -15.966 -31.933  1.00137.86           C  
ANISOU 2626  CD  LYS A1135    15192  19932  17258  -1092   1774  -1654       C  
ATOM   2627  CE  LYS A1135      35.836 -14.929 -32.869  1.00151.83           C  
ANISOU 2627  CE  LYS A1135    17024  21726  18941  -1381   2065  -1602       C  
ATOM   2628  NZ  LYS A1135      37.316 -15.043 -32.982  1.00163.68           N  
ANISOU 2628  NZ  LYS A1135    18192  23147  20852  -1495   2326  -1878       N  
ATOM   2629  N   SER A1136      30.033 -19.193 -31.282  1.00102.61           N  
ANISOU 2629  N   SER A1136    11362  15807  11818   -513   1019  -1314       N  
ATOM   2630  CA  SER A1136      29.502 -20.508 -30.921  1.00101.23           C  
ANISOU 2630  CA  SER A1136    11136  15640  11689   -379    904  -1384       C  
ATOM   2631  C   SER A1136      28.544 -21.121 -31.949  1.00105.40           C  
ANISOU 2631  C   SER A1136    11831  16307  11910   -445    994  -1389       C  
ATOM   2632  O   SER A1136      28.161 -20.478 -32.927  1.00106.00           O  
ANISOU 2632  O   SER A1136    12102  16487  11685   -591   1112  -1307       O  
ATOM   2633  CB  SER A1136      28.823 -20.447 -29.556  1.00102.31           C  
ANISOU 2633  CB  SER A1136    11297  15724  11852   -189    582  -1236       C  
ATOM   2634  OG  SER A1136      27.566 -19.796 -29.644  1.00109.16           O  
ANISOU 2634  OG  SER A1136    12394  16682  12402   -179    478  -1047       O  
ATOM   2635  N   ARG A1137      28.164 -22.383 -31.687  1.00101.34           N  
ANISOU 2635  N   ARG A1137    11242  15778  11485   -339    910  -1477       N  
ATOM   2636  CA  ARG A1137      27.237 -23.237 -32.440  1.00101.12           C  
ANISOU 2636  CA  ARG A1137    11322  15851  11247   -359    943  -1517       C  
ATOM   2637  C   ARG A1137      25.825 -22.667 -32.438  1.00102.51           C  
ANISOU 2637  C   ARG A1137    11745  16114  11090   -330    778  -1290       C  
ATOM   2638  O   ARG A1137      25.101 -22.803 -33.423  1.00102.30           O  
ANISOU 2638  O   ARG A1137    11876  16200  10792   -413    841  -1287       O  
ATOM   2639  CB  ARG A1137      27.183 -24.649 -31.803  1.00102.00           C  
ANISOU 2639  CB  ARG A1137    11267  15867  11623   -223    818  -1626       C  
ATOM   2640  CG  ARG A1137      27.750 -24.771 -30.372  1.00113.78           C  
ANISOU 2640  CG  ARG A1137    12593  17197  13442    -81    605  -1580       C  
ATOM   2641  CD  ARG A1137      26.809 -24.299 -29.272  1.00122.58           C  
ANISOU 2641  CD  ARG A1137    13840  18324  14412     27    346  -1334       C  
ATOM   2642  NE  ARG A1137      25.960 -25.374 -28.754  1.00132.90           N  
ANISOU 2642  NE  ARG A1137    15158  19612  15726    114    182  -1283       N  
ATOM   2643  CZ  ARG A1137      24.710 -25.602 -29.143  1.00148.76           C  
ANISOU 2643  CZ  ARG A1137    17314  21725  17484    106    165  -1213       C  
ATOM   2644  NH1 ARG A1137      24.017 -26.596 -28.610  1.00138.47           N  
ANISOU 2644  NH1 ARG A1137    15998  20388  16226    170     24  -1168       N  
ATOM   2645  NH2 ARG A1137      24.144 -24.840 -30.072  1.00135.52           N  
ANISOU 2645  NH2 ARG A1137    15798  20173  15521     24    272  -1180       N  
ATOM   2646  N   TRP A1138      25.443 -22.058 -31.304  1.00 96.77           N  
ANISOU 2646  N   TRP A1138    11035  15333  10402   -209    558  -1123       N  
ATOM   2647  CA  TRP A1138      24.143 -21.486 -30.984  1.00 94.65           C  
ANISOU 2647  CA  TRP A1138    10931  15114   9916   -146    370   -939       C  
ATOM   2648  C   TRP A1138      23.852 -20.156 -31.682  1.00 99.28           C  
ANISOU 2648  C   TRP A1138    11703  15743  10278   -246    386   -808       C  
ATOM   2649  O   TRP A1138      22.717 -19.934 -32.105  1.00 98.24           O  
ANISOU 2649  O   TRP A1138    11731  15673   9924   -248    289   -711       O  
ATOM   2650  CB  TRP A1138      24.022 -21.384 -29.455  1.00 91.46           C  
ANISOU 2650  CB  TRP A1138    10443  14642   9667      3    162   -865       C  
ATOM   2651  CG  TRP A1138      22.795 -20.698 -28.947  1.00 90.95           C  
ANISOU 2651  CG  TRP A1138    10498  14625   9435     72    -13   -723       C  
ATOM   2652  CD1 TRP A1138      21.498 -20.976 -29.269  1.00 93.14           C  
ANISOU 2652  CD1 TRP A1138    10879  14977   9531     89    -79   -678       C  
ATOM   2653  CD2 TRP A1138      22.751 -19.660 -27.963  1.00 89.92           C  
ANISOU 2653  CD2 TRP A1138    10360  14461   9343    139   -149   -645       C  
ATOM   2654  NE1 TRP A1138      20.652 -20.143 -28.579  1.00 91.71           N  
ANISOU 2654  NE1 TRP A1138    10746  14811   9289    160   -234   -586       N  
ATOM   2655  CE2 TRP A1138      21.394 -19.326 -27.766  1.00 92.98           C  
ANISOU 2655  CE2 TRP A1138    10843  14911   9574    192   -276   -571       C  
ATOM   2656  CE3 TRP A1138      23.733 -18.964 -27.234  1.00 91.31           C  
ANISOU 2656  CE3 TRP A1138    10446  14557   9690    160   -179   -656       C  
ATOM   2657  CZ2 TRP A1138      20.990 -18.338 -26.865  1.00 91.70           C  
ANISOU 2657  CZ2 TRP A1138    10680  14740   9422    264   -415   -527       C  
ATOM   2658  CZ3 TRP A1138      23.331 -17.977 -26.349  1.00 92.10           C  
ANISOU 2658  CZ3 TRP A1138    10564  14651   9778    230   -329   -598       C  
ATOM   2659  CH2 TRP A1138      21.976 -17.668 -26.177  1.00 91.99           C  
ANISOU 2659  CH2 TRP A1138    10640  14706   9607    280   -437   -544       C  
ATOM   2660  N   TYR A1139      24.872 -19.286 -31.810  1.00 97.69           N  
ANISOU 2660  N   TYR A1139    11470  15489  10158   -335    492   -802       N  
ATOM   2661  CA  TYR A1139      24.768 -17.977 -32.463  1.00 99.07           C  
ANISOU 2661  CA  TYR A1139    11817  15666  10158   -456    502   -654       C  
ATOM   2662  C   TYR A1139      24.438 -18.103 -33.957  1.00105.23           C  
ANISOU 2662  C   TYR A1139    12791  16560  10634   -635    640   -640       C  
ATOM   2663  O   TYR A1139      23.768 -17.225 -34.496  1.00105.73           O  
ANISOU 2663  O   TYR A1139    13058  16632  10481   -703    538   -466       O  
ATOM   2664  CB  TYR A1139      26.046 -17.152 -32.241  1.00101.72           C  
ANISOU 2664  CB  TYR A1139    12048  15908  10691   -529    606   -667       C  
ATOM   2665  CG  TYR A1139      25.956 -15.706 -32.686  1.00104.89           C  
ANISOU 2665  CG  TYR A1139    12613  16266  10973   -644    568   -483       C  
ATOM   2666  CD1 TYR A1139      25.426 -14.729 -31.845  1.00105.88           C  
ANISOU 2666  CD1 TYR A1139    12759  16299  11170   -526    324   -358       C  
ATOM   2667  CD2 TYR A1139      26.438 -15.305 -33.928  1.00108.15           C  
ANISOU 2667  CD2 TYR A1139    13155  16722  11215   -884    778   -441       C  
ATOM   2668  CE1 TYR A1139      25.355 -13.393 -32.243  1.00107.98           C  
ANISOU 2668  CE1 TYR A1139    13162  16484  11380   -626    257   -187       C  
ATOM   2669  CE2 TYR A1139      26.370 -13.974 -34.338  1.00110.49           C  
ANISOU 2669  CE2 TYR A1139    13616  16951  11413  -1009    719   -236       C  
ATOM   2670  CZ  TYR A1139      25.831 -13.020 -33.489  1.00117.01           C  
ANISOU 2670  CZ  TYR A1139    14449  17651  12357   -870    443   -106       C  
ATOM   2671  OH  TYR A1139      25.763 -11.706 -33.883  1.00119.88           O  
ANISOU 2671  OH  TYR A1139    14964  17910  12675   -986    353     97       O  
ATOM   2672  N   ASN A1140      24.903 -19.181 -34.623  1.00102.90           N  
ANISOU 2672  N   ASN A1140    12431  16341  10324   -714    853   -830       N  
ATOM   2673  CA  ASN A1140      24.608 -19.414 -36.040  1.00104.64           C  
ANISOU 2673  CA  ASN A1140    12838  16698  10222   -896    996   -855       C  
ATOM   2674  C   ASN A1140      23.423 -20.373 -36.238  1.00106.89           C  
ANISOU 2674  C   ASN A1140    13185  17054  10374   -805    868   -894       C  
ATOM   2675  O   ASN A1140      22.919 -20.506 -37.356  1.00108.32           O  
ANISOU 2675  O   ASN A1140    13554  17349  10252   -934    910   -892       O  
ATOM   2676  CB  ASN A1140      25.862 -19.821 -36.831  1.00109.07           C  
ANISOU 2676  CB  ASN A1140    13305  17323  10815  -1085   1348  -1069       C  
ATOM   2677  CG  ASN A1140      26.424 -21.183 -36.501  1.00138.16           C  
ANISOU 2677  CG  ASN A1140    16724  20986  14786   -992   1458  -1354       C  
ATOM   2678  OD1 ASN A1140      26.342 -22.124 -37.299  1.00135.28           O  
ANISOU 2678  OD1 ASN A1140    16357  20721  14322  -1061   1602  -1544       O  
ATOM   2679  ND2 ASN A1140      27.059 -21.309 -35.346  1.00130.26           N  
ANISOU 2679  ND2 ASN A1140    15488  19843  14161   -843   1382  -1400       N  
ATOM   2680  N   GLN A1141      22.953 -20.994 -35.134  1.00100.34           N  
ANISOU 2680  N   GLN A1141    12209  16155   9759   -597    697   -916       N  
ATOM   2681  CA  GLN A1141      21.803 -21.898 -35.098  1.00 98.84           C  
ANISOU 2681  CA  GLN A1141    12041  16004   9509   -497    559   -943       C  
ATOM   2682  C   GLN A1141      20.527 -21.059 -35.034  1.00100.24           C  
ANISOU 2682  C   GLN A1141    12390  16184   9512   -446    314   -741       C  
ATOM   2683  O   GLN A1141      19.609 -21.280 -35.825  1.00100.46           O  
ANISOU 2683  O   GLN A1141    12562  16285   9325   -484    242   -726       O  
ATOM   2684  CB  GLN A1141      21.876 -22.827 -33.870  1.00 98.78           C  
ANISOU 2684  CB  GLN A1141    11815  15910   9808   -326    479  -1019       C  
ATOM   2685  CG  GLN A1141      21.420 -24.247 -34.156  1.00120.08           C  
ANISOU 2685  CG  GLN A1141    14452  18634  12541   -296    492  -1168       C  
ATOM   2686  CD  GLN A1141      22.576 -25.087 -34.635  1.00146.22           C  
ANISOU 2686  CD  GLN A1141    17610  21928  16018   -368    717  -1408       C  
ATOM   2687  OE1 GLN A1141      23.450 -25.487 -33.855  1.00141.50           O  
ANISOU 2687  OE1 GLN A1141    16812  21218  15735   -300    731  -1484       O  
ATOM   2688  NE2 GLN A1141      22.633 -25.338 -35.937  1.00143.05           N  
ANISOU 2688  NE2 GLN A1141    17298  21639  15415   -514    892  -1547       N  
ATOM   2689  N   THR A1142      20.476 -20.102 -34.085  1.00 94.33           N  
ANISOU 2689  N   THR A1142    11610  15350   8882   -356    174   -609       N  
ATOM   2690  CA  THR A1142      19.366 -19.166 -33.883  1.00 92.93           C  
ANISOU 2690  CA  THR A1142    11545  15143   8623   -291    -65   -449       C  
ATOM   2691  C   THR A1142      20.006 -17.776 -33.790  1.00 95.80           C  
ANISOU 2691  C   THR A1142    11957  15423   9022   -348    -79   -324       C  
ATOM   2692  O   THR A1142      20.366 -17.353 -32.695  1.00 93.75           O  
ANISOU 2692  O   THR A1142    11564  15087   8969   -249   -127   -323       O  
ATOM   2693  CB  THR A1142      18.525 -19.553 -32.652  1.00 97.54           C  
ANISOU 2693  CB  THR A1142    11996  15704   9362   -108   -224   -469       C  
ATOM   2694  OG1 THR A1142      19.402 -19.797 -31.555  1.00 94.68           O  
ANISOU 2694  OG1 THR A1142    11461  15294   9218    -42   -162   -525       O  
ATOM   2695  CG2 THR A1142      17.641 -20.774 -32.897  1.00 95.92           C  
ANISOU 2695  CG2 THR A1142    11776  15564   9106    -74   -248   -553       C  
ATOM   2696  N   PRO A1143      20.242 -17.097 -34.936  1.00 93.89           N  
ANISOU 2696  N   PRO A1143    11905  15194   8576   -527    -26   -222       N  
ATOM   2697  CA  PRO A1143      20.945 -15.805 -34.900  1.00 94.42           C  
ANISOU 2697  CA  PRO A1143    12015  15162   8699   -610    -24    -93       C  
ATOM   2698  C   PRO A1143      20.319 -14.709 -34.043  1.00 96.24           C  
ANISOU 2698  C   PRO A1143    12225  15262   9081   -474   -290     22       C  
ATOM   2699  O   PRO A1143      21.039 -14.035 -33.310  1.00 95.20           O  
ANISOU 2699  O   PRO A1143    11985  15037   9150   -444   -278     27       O  
ATOM   2700  CB  PRO A1143      21.019 -15.401 -36.377  1.00 99.02           C  
ANISOU 2700  CB  PRO A1143    12854  15798   8972   -849     46     27       C  
ATOM   2701  CG  PRO A1143      19.897 -16.142 -37.031  1.00103.73           C  
ANISOU 2701  CG  PRO A1143    13571  16492   9350   -832    -61      5       C  
ATOM   2702  CD  PRO A1143      19.880 -17.462 -36.320  1.00 97.27           C  
ANISOU 2702  CD  PRO A1143    12533  15728   8697   -682     25   -212       C  
ATOM   2703  N   ASN A1144      18.991 -14.520 -34.162  1.00 91.82           N  
ANISOU 2703  N   ASN A1144    11752  14688   8446   -394   -531     90       N  
ATOM   2704  CA  ASN A1144      18.245 -13.475 -33.460  1.00 90.50           C  
ANISOU 2704  CA  ASN A1144    11552  14393   8440   -265   -796    161       C  
ATOM   2705  C   ASN A1144      17.923 -13.774 -32.006  1.00 90.19           C  
ANISOU 2705  C   ASN A1144    11289  14360   8618    -64   -843     17       C  
ATOM   2706  O   ASN A1144      17.972 -12.843 -31.202  1.00 89.80           O  
ANISOU 2706  O   ASN A1144    11157  14210   8754     15   -954     19       O  
ATOM   2707  CB  ASN A1144      17.026 -13.038 -34.263  1.00 92.52           C  
ANISOU 2707  CB  ASN A1144    11982  14606   8565   -277  -1051    284       C  
ATOM   2708  CG  ASN A1144      17.391 -12.520 -35.638  1.00112.77           C  
ANISOU 2708  CG  ASN A1144    14811  17152  10887   -506  -1042    473       C  
ATOM   2709  OD1 ASN A1144      18.101 -11.519 -35.791  1.00106.68           O  
ANISOU 2709  OD1 ASN A1144    14107  16271  10156   -615  -1036    608       O  
ATOM   2710  ND2 ASN A1144      16.922 -13.205 -36.665  1.00104.98           N  
ANISOU 2710  ND2 ASN A1144    13984  16276   9629   -600  -1038    486       N  
ATOM   2711  N   ARG A1145      17.624 -15.051 -31.652  1.00 83.63           N  
ANISOU 2711  N   ARG A1145    10365  13646   7765      3   -759   -110       N  
ATOM   2712  CA  ARG A1145      17.364 -15.446 -30.259  1.00 80.78           C  
ANISOU 2712  CA  ARG A1145     9817  13313   7562    154   -782   -227       C  
ATOM   2713  C   ARG A1145      18.654 -15.309 -29.439  1.00 82.82           C  
ANISOU 2713  C   ARG A1145     9962  13540   7966    157   -668   -270       C  
ATOM   2714  O   ARG A1145      18.613 -14.742 -28.348  1.00 81.98           O  
ANISOU 2714  O   ARG A1145     9754  13399   7997    253   -757   -311       O  
ATOM   2715  CB  ARG A1145      16.770 -16.864 -30.152  1.00 78.79           C  
ANISOU 2715  CB  ARG A1145     9513  13173   7252    192   -727   -317       C  
ATOM   2716  CG  ARG A1145      16.395 -17.253 -28.725  1.00 83.32           C  
ANISOU 2716  CG  ARG A1145     9927  13786   7945    311   -757   -405       C  
ATOM   2717  CD  ARG A1145      15.680 -18.582 -28.636  1.00 90.12           C  
ANISOU 2717  CD  ARG A1145    10745  14734   8763    330   -723   -464       C  
ATOM   2718  NE  ARG A1145      15.498 -18.987 -27.241  1.00 93.50           N  
ANISOU 2718  NE  ARG A1145    11044  15209   9273    400   -725   -519       N  
ATOM   2719  CZ  ARG A1145      14.765 -20.023 -26.846  1.00104.96           C  
ANISOU 2719  CZ  ARG A1145    12439  16728  10712    414   -711   -557       C  
ATOM   2720  NH1 ARG A1145      14.124 -20.770 -27.735  1.00 93.25           N  
ANISOU 2720  NH1 ARG A1145    10996  15264   9170    383   -705   -567       N  
ATOM   2721  NH2 ARG A1145      14.660 -20.315 -25.556  1.00 90.61           N  
ANISOU 2721  NH2 ARG A1145    10533  14962   8931    444   -708   -581       N  
ATOM   2722  N   ALA A1146      19.798 -15.764 -29.995  1.00 78.76           N  
ANISOU 2722  N   ALA A1146     9458  13035   7433     47   -479   -279       N  
ATOM   2723  CA  ALA A1146      21.105 -15.643 -29.355  1.00 78.08           C  
ANISOU 2723  CA  ALA A1146     9249  12898   7519     41   -380   -330       C  
ATOM   2724  C   ALA A1146      21.510 -14.174 -29.273  1.00 83.12           C  
ANISOU 2724  C   ALA A1146     9910  13419   8251     12   -452   -253       C  
ATOM   2725  O   ALA A1146      21.974 -13.756 -28.221  1.00 82.53           O  
ANISOU 2725  O   ALA A1146     9714  13292   8350     89   -507   -306       O  
ATOM   2726  CB  ALA A1146      22.152 -16.441 -30.111  1.00 79.47           C  
ANISOU 2726  CB  ALA A1146     9407  13102   7687    -79   -154   -391       C  
ATOM   2727  N   LYS A1147      21.258 -13.377 -30.342  1.00 81.14           N  
ANISOU 2727  N   LYS A1147     9824  13119   7886   -100   -485   -122       N  
ATOM   2728  CA  LYS A1147      21.550 -11.935 -30.408  1.00 82.03           C  
ANISOU 2728  CA  LYS A1147     9982  13087   8099   -149   -581    -14       C  
ATOM   2729  C   LYS A1147      20.904 -11.184 -29.241  1.00 84.46           C  
ANISOU 2729  C   LYS A1147    10187  13322   8583     22   -803    -63       C  
ATOM   2730  O   LYS A1147      21.566 -10.364 -28.604  1.00 84.20           O  
ANISOU 2730  O   LYS A1147    10065  13186   8741     42   -838    -87       O  
ATOM   2731  CB  LYS A1147      21.057 -11.339 -31.735  1.00 86.39           C  
ANISOU 2731  CB  LYS A1147    10762  13598   8463   -292   -647    168       C  
ATOM   2732  CG  LYS A1147      22.044 -10.397 -32.399  1.00104.33           C  
ANISOU 2732  CG  LYS A1147    13124  15764  10752   -484   -561    303       C  
ATOM   2733  CD  LYS A1147      21.448  -9.832 -33.673  1.00117.09           C  
ANISOU 2733  CD  LYS A1147    15006  17341  12144   -639   -672    518       C  
ATOM   2734  CE  LYS A1147      22.493  -9.329 -34.632  1.00129.40           C  
ANISOU 2734  CE  LYS A1147    16700  18870  13598   -909   -485    658       C  
ATOM   2735  NZ  LYS A1147      21.888  -8.943 -35.934  1.00140.81           N  
ANISOU 2735  NZ  LYS A1147    18447  20306  14747  -1090   -596    887       N  
ATOM   2736  N   ARG A1148      19.621 -11.493 -28.955  1.00 79.59           N  
ANISOU 2736  N   ARG A1148     9565  12763   7911    139   -939   -107       N  
ATOM   2737  CA  ARG A1148      18.852 -10.896 -27.868  1.00 78.79           C  
ANISOU 2737  CA  ARG A1148     9349  12628   7959    294  -1119   -204       C  
ATOM   2738  C   ARG A1148      19.392 -11.333 -26.512  1.00 81.91           C  
ANISOU 2738  C   ARG A1148     9581  13098   8444    379  -1051   -353       C  
ATOM   2739  O   ARG A1148      19.633 -10.478 -25.666  1.00 81.90           O  
ANISOU 2739  O   ARG A1148     9487  13027   8604    442  -1139   -426       O  
ATOM   2740  CB  ARG A1148      17.358 -11.226 -27.995  1.00 78.38           C  
ANISOU 2740  CB  ARG A1148     9316  12634   7833    372  -1245   -235       C  
ATOM   2741  CG  ARG A1148      16.682 -10.521 -29.166  1.00 90.59           C  
ANISOU 2741  CG  ARG A1148    11017  14065   9339    315  -1415    -89       C  
ATOM   2742  CD  ARG A1148      15.168 -10.619 -29.132  1.00 98.39           C  
ANISOU 2742  CD  ARG A1148    11970  15066  10346    420  -1594   -156       C  
ATOM   2743  NE  ARG A1148      14.684 -11.994 -29.289  1.00102.30           N  
ANISOU 2743  NE  ARG A1148    12466  15730  10675    421  -1480   -210       N  
ATOM   2744  CZ  ARG A1148      14.385 -12.558 -30.455  1.00115.02           C  
ANISOU 2744  CZ  ARG A1148    14227  17374  12100    334  -1481   -116       C  
ATOM   2745  NH1 ARG A1148      14.527 -11.879 -31.587  1.00103.10           N  
ANISOU 2745  NH1 ARG A1148    12907  15762  10505    222  -1585     57       N  
ATOM   2746  NH2 ARG A1148      13.946 -13.807 -30.497  1.00100.33           N  
ANISOU 2746  NH2 ARG A1148    12340  15651  10132    345  -1385   -191       N  
ATOM   2747  N   VAL A1149      19.609 -12.654 -26.315  1.00 77.53           N  
ANISOU 2747  N   VAL A1149     8996  12671   7790    375   -915   -397       N  
ATOM   2748  CA  VAL A1149      20.123 -13.226 -25.065  1.00 76.53           C  
ANISOU 2748  CA  VAL A1149     8745  12614   7721    438   -881   -503       C  
ATOM   2749  C   VAL A1149      21.535 -12.715 -24.752  1.00 82.56           C  
ANISOU 2749  C   VAL A1149     9443  13284   8644    405   -845   -517       C  
ATOM   2750  O   VAL A1149      21.769 -12.247 -23.639  1.00 82.62           O  
ANISOU 2750  O   VAL A1149     9358  13280   8752    477   -932   -606       O  
ATOM   2751  CB  VAL A1149      19.975 -14.770 -25.000  1.00 79.08           C  
ANISOU 2751  CB  VAL A1149     9060  13055   7933    433   -784   -518       C  
ATOM   2752  CG1 VAL A1149      20.591 -15.342 -23.730  1.00 78.39           C  
ANISOU 2752  CG1 VAL A1149     8870  13010   7902    477   -789   -586       C  
ATOM   2753  CG2 VAL A1149      18.509 -15.173 -25.091  1.00 78.45           C  
ANISOU 2753  CG2 VAL A1149     9012  13062   7734    473   -836   -529       C  
ATOM   2754  N   ILE A1150      22.439 -12.735 -25.745  1.00 80.95           N  
ANISOU 2754  N   ILE A1150     9281  13015   8462    288   -716   -447       N  
ATOM   2755  CA  ILE A1150      23.802 -12.223 -25.612  1.00 82.34           C  
ANISOU 2755  CA  ILE A1150     9377  13087   8821    235   -660   -467       C  
ATOM   2756  C   ILE A1150      23.783 -10.737 -25.201  1.00 89.01           C  
ANISOU 2756  C   ILE A1150    10201  13809   9811    266   -806   -465       C  
ATOM   2757  O   ILE A1150      24.478 -10.372 -24.254  1.00 88.91           O  
ANISOU 2757  O   ILE A1150    10069  13749   9963    317   -863   -558       O  
ATOM   2758  CB  ILE A1150      24.643 -12.544 -26.888  1.00 86.50           C  
ANISOU 2758  CB  ILE A1150     9950  13590   9324     72   -451   -412       C  
ATOM   2759  CG1 ILE A1150      25.405 -13.862 -26.712  1.00 86.55           C  
ANISOU 2759  CG1 ILE A1150     9847  13651   9385     73   -322   -514       C  
ATOM   2760  CG2 ILE A1150      25.589 -11.413 -27.320  1.00 88.80           C  
ANISOU 2760  CG2 ILE A1150    10235  13744   9760    -46   -398   -360       C  
ATOM   2761  CD1 ILE A1150      24.981 -14.958 -27.620  1.00 93.82           C  
ANISOU 2761  CD1 ILE A1150    10843  14670  10136     18   -197   -510       C  
ATOM   2762  N   THR A1151      22.940  -9.908 -25.866  1.00 87.73           N  
ANISOU 2762  N   THR A1151    10149  13584   9602    244   -898   -370       N  
ATOM   2763  CA  THR A1151      22.817  -8.478 -25.556  1.00 89.25           C  
ANISOU 2763  CA  THR A1151    10316  13623   9972    277  -1066   -369       C  
ATOM   2764  C   THR A1151      22.143  -8.218 -24.193  1.00 93.78           C  
ANISOU 2764  C   THR A1151    10772  14241  10619    444  -1222   -544       C  
ATOM   2765  O   THR A1151      22.397  -7.183 -23.573  1.00 94.37           O  
ANISOU 2765  O   THR A1151    10763  14203  10890    490  -1339   -623       O  
ATOM   2766  CB  THR A1151      22.344  -7.654 -26.774  1.00 98.06           C  
ANISOU 2766  CB  THR A1151    11590  14612  11057    176  -1137   -188       C  
ATOM   2767  OG1 THR A1151      22.837  -6.319 -26.680  1.00 99.15           O  
ANISOU 2767  OG1 THR A1151    11697  14550  11427    144  -1244   -151       O  
ATOM   2768  CG2 THR A1151      20.837  -7.639 -26.942  1.00 96.47           C  
ANISOU 2768  CG2 THR A1151    11451  14438  10764    262  -1300   -178       C  
ATOM   2769  N   THR A1152      21.326  -9.189 -23.715  1.00 89.70           N  
ANISOU 2769  N   THR A1152    10245  13896   9941    519  -1207   -617       N  
ATOM   2770  CA  THR A1152      20.664  -9.155 -22.405  1.00 89.31           C  
ANISOU 2770  CA  THR A1152    10094  13946   9894    641  -1298   -795       C  
ATOM   2771  C   THR A1152      21.714  -9.440 -21.331  1.00 93.73           C  
ANISOU 2771  C   THR A1152    10564  14552  10496    657  -1274   -889       C  
ATOM   2772  O   THR A1152      21.726  -8.762 -20.308  1.00 94.31           O  
ANISOU 2772  O   THR A1152    10551  14626  10658    725  -1378  -1038       O  
ATOM   2773  CB  THR A1152      19.436 -10.085 -22.387  1.00 95.65           C  
ANISOU 2773  CB  THR A1152    10926  14908  10510    676  -1271   -815       C  
ATOM   2774  OG1 THR A1152      18.437  -9.539 -23.252  1.00 96.15           O  
ANISOU 2774  OG1 THR A1152    11044  14891  10596    683  -1362   -762       O  
ATOM   2775  CG2 THR A1152      18.843 -10.270 -20.996  1.00 93.65           C  
ANISOU 2775  CG2 THR A1152    10575  14802  10204    758  -1303   -999       C  
ATOM   2776  N   PHE A1153      22.625 -10.404 -21.590  1.00 89.80           N  
ANISOU 2776  N   PHE A1153    10080  14080   9958    594  -1155   -816       N  
ATOM   2777  CA  PHE A1153      23.739 -10.734 -20.698  1.00 89.61           C  
ANISOU 2777  CA  PHE A1153     9971  14064  10014    604  -1167   -884       C  
ATOM   2778  C   PHE A1153      24.732  -9.562 -20.656  1.00 95.14           C  
ANISOU 2778  C   PHE A1153    10595  14595  10958    586  -1221   -922       C  
ATOM   2779  O   PHE A1153      25.283  -9.260 -19.599  1.00 95.59           O  
ANISOU 2779  O   PHE A1153    10564  14646  11110    636  -1324  -1042       O  
ATOM   2780  CB  PHE A1153      24.468 -11.996 -21.187  1.00 90.78           C  
ANISOU 2780  CB  PHE A1153    10125  14231  10136    541  -1039   -810       C  
ATOM   2781  CG  PHE A1153      23.915 -13.325 -20.733  1.00 91.37           C  
ANISOU 2781  CG  PHE A1153    10228  14451  10036    567  -1029   -800       C  
ATOM   2782  CD1 PHE A1153      23.711 -13.589 -19.382  1.00 94.51           C  
ANISOU 2782  CD1 PHE A1153    10603  14950  10354    622  -1143   -870       C  
ATOM   2783  CD2 PHE A1153      23.693 -14.350 -21.645  1.00 92.93           C  
ANISOU 2783  CD2 PHE A1153    10479  14678  10151    516   -907   -721       C  
ATOM   2784  CE1 PHE A1153      23.256 -14.839 -18.957  1.00 95.00           C  
ANISOU 2784  CE1 PHE A1153    10705  15130  10260    617  -1138   -829       C  
ATOM   2785  CE2 PHE A1153      23.235 -15.601 -21.218  1.00 95.31           C  
ANISOU 2785  CE2 PHE A1153    10798  15084  10332    531   -910   -703       C  
ATOM   2786  CZ  PHE A1153      23.014 -15.835 -19.878  1.00 93.58           C  
ANISOU 2786  CZ  PHE A1153    10564  14952  10039    576  -1027   -741       C  
ATOM   2787  N   ARG A1154      24.930  -8.903 -21.815  1.00 92.65           N  
ANISOU 2787  N   ARG A1154    10326  14143  10734    500  -1159   -813       N  
ATOM   2788  CA  ARG A1154      25.819  -7.761 -22.031  1.00 94.18           C  
ANISOU 2788  CA  ARG A1154    10463  14149  11171    444  -1185   -806       C  
ATOM   2789  C   ARG A1154      25.407  -6.529 -21.200  1.00 99.15           C  
ANISOU 2789  C   ARG A1154    11028  14700  11942    537  -1380   -929       C  
ATOM   2790  O   ARG A1154      26.244  -5.974 -20.485  1.00 99.69           O  
ANISOU 2790  O   ARG A1154    10984  14689  12205    558  -1454  -1039       O  
ATOM   2791  CB  ARG A1154      25.854  -7.416 -23.536  1.00 95.93           C  
ANISOU 2791  CB  ARG A1154    10799  14269  11380    300  -1073   -622       C  
ATOM   2792  CG  ARG A1154      27.023  -6.543 -23.983  1.00109.19           C  
ANISOU 2792  CG  ARG A1154    12429  15765  13292    176  -1019   -573       C  
ATOM   2793  CD  ARG A1154      26.751  -5.865 -25.321  1.00121.10           C  
ANISOU 2793  CD  ARG A1154    14093  17165  14755     25   -975   -368       C  
ATOM   2794  NE  ARG A1154      25.805  -4.749 -25.199  1.00129.18           N  
ANISOU 2794  NE  ARG A1154    15162  18066  15853     92  -1203   -335       N  
ATOM   2795  CZ  ARG A1154      25.428  -3.959 -26.202  1.00142.15           C  
ANISOU 2795  CZ  ARG A1154    16947  19569  17495    -19  -1263   -142       C  
ATOM   2796  NH1 ARG A1154      25.911  -4.148 -27.425  1.00127.16           N  
ANISOU 2796  NH1 ARG A1154    15185  17664  15466   -226  -1085     46       N  
ATOM   2797  NH2 ARG A1154      24.566  -2.974 -25.989  1.00128.73           N  
ANISOU 2797  NH2 ARG A1154    15254  17730  15926     67  -1509   -141       N  
ATOM   2798  N   THR A1155      24.131  -6.107 -21.299  1.00 95.75           N  
ANISOU 2798  N   THR A1155    10651  14284  11445    595  -1471   -937       N  
ATOM   2799  CA  THR A1155      23.607  -4.925 -20.600  1.00 96.57           C  
ANISOU 2799  CA  THR A1155    10674  14303  11717    689  -1655  -1090       C  
ATOM   2800  C   THR A1155      22.956  -5.223 -19.251  1.00 99.83           C  
ANISOU 2800  C   THR A1155    11011  14904  12017    808  -1716  -1319       C  
ATOM   2801  O   THR A1155      23.155  -4.462 -18.305  1.00100.70           O  
ANISOU 2801  O   THR A1155    11013  14982  12267    872  -1831  -1512       O  
ATOM   2802  CB  THR A1155      22.671  -4.097 -21.505  1.00105.45           C  
ANISOU 2802  CB  THR A1155    11867  15280  12920    680  -1754   -990       C  
ATOM   2803  OG1 THR A1155      21.668  -4.949 -22.069  1.00103.04           O  
ANISOU 2803  OG1 THR A1155    11664  15107  12381    681  -1696   -908       O  
ATOM   2804  CG2 THR A1155      23.423  -3.348 -22.609  1.00105.63           C  
ANISOU 2804  CG2 THR A1155    11960  15073  13101    540  -1746   -782       C  
ATOM   2805  N   GLY A1156      22.171  -6.295 -19.184  1.00 94.82           N  
ANISOU 2805  N   GLY A1156    10434  14463  11128    822  -1634  -1302       N  
ATOM   2806  CA  GLY A1156      21.444  -6.690 -17.981  1.00 94.48           C  
ANISOU 2806  CA  GLY A1156    10345  14629  10923    894  -1653  -1493       C  
ATOM   2807  C   GLY A1156      20.056  -6.084 -17.921  1.00 99.24           C  
ANISOU 2807  C   GLY A1156    10901  15245  11562    964  -1719  -1629       C  
ATOM   2808  O   GLY A1156      19.435  -6.072 -16.855  1.00 99.81           O  
ANISOU 2808  O   GLY A1156    10898  15474  11550   1016  -1732  -1850       O  
ATOM   2809  N   THR A1157      19.561  -5.569 -19.069  1.00 95.75           N  
ANISOU 2809  N   THR A1157    10498  14635  11249    957  -1769  -1506       N  
ATOM   2810  CA  THR A1157      18.246  -4.930 -19.198  1.00 96.21           C  
ANISOU 2810  CA  THR A1157    10493  14643  11419   1032  -1877  -1623       C  
ATOM   2811  C   THR A1157      17.357  -5.625 -20.236  1.00 98.31           C  
ANISOU 2811  C   THR A1157    10859  14936  11558   1004  -1838  -1459       C  
ATOM   2812  O   THR A1157      17.822  -6.476 -20.996  1.00 96.59           O  
ANISOU 2812  O   THR A1157    10771  14751  11177    917  -1729  -1243       O  
ATOM   2813  CB  THR A1157      18.402  -3.436 -19.551  1.00106.69           C  
ANISOU 2813  CB  THR A1157    11762  15682  13092   1064  -2067  -1643       C  
ATOM   2814  OG1 THR A1157      19.127  -3.306 -20.774  1.00106.14           O  
ANISOU 2814  OG1 THR A1157    11828  15434  13065    958  -2067  -1347       O  
ATOM   2815  CG2 THR A1157      19.070  -2.629 -18.444  1.00107.25           C  
ANISOU 2815  CG2 THR A1157    11700  15718  13333   1113  -2135  -1873       C  
ATOM   2816  N   TRP A1158      16.079  -5.221 -20.287  1.00 95.52           N  
ANISOU 2816  N   TRP A1158    10427  14556  11310   1080  -1941  -1586       N  
ATOM   2817  CA  TRP A1158      15.094  -5.731 -21.238  1.00 95.06           C  
ANISOU 2817  CA  TRP A1158    10438  14499  11180   1070  -1958  -1468       C  
ATOM   2818  C   TRP A1158      15.081  -4.872 -22.517  1.00 99.92           C  
ANISOU 2818  C   TRP A1158    11149  14836  11978   1043  -2147  -1263       C  
ATOM   2819  O   TRP A1158      14.092  -4.884 -23.259  1.00 99.95           O  
ANISOU 2819  O   TRP A1158    11182  14777  12016   1062  -2262  -1210       O  
ATOM   2820  CB  TRP A1158      13.703  -5.785 -20.587  1.00 94.61           C  
ANISOU 2820  CB  TRP A1158    10222  14558  11168   1160  -1976  -1733       C  
ATOM   2821  CG  TRP A1158      13.665  -6.592 -19.324  1.00 95.02           C  
ANISOU 2821  CG  TRP A1158    10206  14894  11003   1149  -1786  -1913       C  
ATOM   2822  CD1 TRP A1158      13.599  -6.117 -18.048  1.00 99.07           C  
ANISOU 2822  CD1 TRP A1158    10574  15509  11559   1193  -1766  -2204       C  
ATOM   2823  CD2 TRP A1158      13.754  -8.020 -19.218  1.00 93.25           C  
ANISOU 2823  CD2 TRP A1158    10076  14882  10471   1070  -1601  -1798       C  
ATOM   2824  NE1 TRP A1158      13.603  -7.162 -17.151  1.00 97.85           N  
ANISOU 2824  NE1 TRP A1158    10438  15632  11106   1131  -1580  -2257       N  
ATOM   2825  CE2 TRP A1158      13.702  -8.342 -17.842  1.00 97.56           C  
ANISOU 2825  CE2 TRP A1158    10544  15652  10873   1058  -1488  -2001       C  
ATOM   2826  CE3 TRP A1158      13.855  -9.063 -20.155  1.00 92.83           C  
ANISOU 2826  CE3 TRP A1158    10166  14850  10255   1000  -1529  -1553       C  
ATOM   2827  CZ2 TRP A1158      13.745  -9.664 -17.381  1.00 95.88           C  
ANISOU 2827  CZ2 TRP A1158    10403  15657  10370    975  -1326  -1927       C  
ATOM   2828  CZ3 TRP A1158      13.901 -10.370 -19.697  1.00 93.25           C  
ANISOU 2828  CZ3 TRP A1158    10262  15108  10061    936  -1365  -1514       C  
ATOM   2829  CH2 TRP A1158      13.847 -10.661 -18.327  1.00 94.28           C  
ANISOU 2829  CH2 TRP A1158    10323  15434  10064    922  -1275  -1681       C  
ATOM   2830  N   ASP A1159      16.206  -4.156 -22.787  1.00 96.94           N  
ANISOU 2830  N   ASP A1159    10830  14290  11713    981  -2185  -1135       N  
ATOM   2831  CA  ASP A1159      16.403  -3.279 -23.948  1.00 98.24           C  
ANISOU 2831  CA  ASP A1159    11114  14183  12029    911  -2354   -901       C  
ATOM   2832  C   ASP A1159      16.340  -4.009 -25.294  1.00100.36           C  
ANISOU 2832  C   ASP A1159    11601  14477  12053    787  -2299   -617       C  
ATOM   2833  O   ASP A1159      16.110  -3.367 -26.321  1.00101.57           O  
ANISOU 2833  O   ASP A1159    11880  14430  12282    725  -2477   -419       O  
ATOM   2834  CB  ASP A1159      17.694  -2.447 -23.808  1.00101.25           C  
ANISOU 2834  CB  ASP A1159    11492  14405  12575    848  -2361   -845       C  
ATOM   2835  CG  ASP A1159      17.581  -1.204 -22.932  1.00116.13           C  
ANISOU 2835  CG  ASP A1159    13189  16122  14814    961  -2546  -1079       C  
ATOM   2836  OD1 ASP A1159      16.436  -0.806 -22.595  1.00117.40           O  
ANISOU 2836  OD1 ASP A1159    13222  16244  15139   1086  -2700  -1276       O  
ATOM   2837  OD2 ASP A1159      18.633  -0.602 -22.618  1.00125.02           O  
ANISOU 2837  OD2 ASP A1159    14277  17141  16084    923  -2542  -1084       O  
ATOM   2838  N   ALA A1160      16.484  -5.351 -25.274  1.00 94.10           N  
ANISOU 2838  N   ALA A1160    10856  13926  10972    748  -2074   -605       N  
ATOM   2839  CA  ALA A1160      16.388  -6.230 -26.443  1.00 92.99           C  
ANISOU 2839  CA  ALA A1160    10899  13856  10577    638  -1990   -400       C  
ATOM   2840  C   ALA A1160      14.916  -6.590 -26.747  1.00 96.25           C  
ANISOU 2840  C   ALA A1160    11306  14310  10954    712  -2114   -448       C  
ATOM   2841  O   ALA A1160      14.655  -7.409 -27.632  1.00 95.40           O  
ANISOU 2841  O   ALA A1160    11334  14283  10631    639  -2061   -321       O  
ATOM   2842  CB  ALA A1160      17.196  -7.495 -26.202  1.00 91.75           C  
ANISOU 2842  CB  ALA A1160    10756  13909  10198    582  -1717   -408       C  
ATOM   2843  N   TYR A1161      13.960  -5.976 -26.009  1.00 93.00           N  
ANISOU 2843  N   TYR A1161    10719  13844  10774    854  -2276   -658       N  
ATOM   2844  CA  TYR A1161      12.519  -6.193 -26.166  1.00109.00           C  
ANISOU 2844  CA  TYR A1161    12677  15887  12851    939  -2408   -758       C  
ATOM   2845  C   TYR A1161      11.731  -4.881 -26.064  1.00122.77           C  
ANISOU 2845  C   TYR A1161    14293  17389  14966   1050  -2712   -873       C  
ATOM   2846  O   TYR A1161      11.859  -4.136 -25.091  1.00 75.77           O  
ANISOU 2846  O   TYR A1161     8166  11386   9238   1134  -2739  -1083       O  
ATOM   2847  CB  TYR A1161      12.002  -7.230 -25.151  1.00108.35           C  
ANISOU 2847  CB  TYR A1161    12447  16067  12655   1000  -2212   -985       C  
ATOM   2848  CG  TYR A1161      12.806  -8.513 -25.112  1.00107.54           C  
ANISOU 2848  CG  TYR A1161    12444  16168  12249    905  -1946   -889       C  
ATOM   2849  CD1 TYR A1161      12.589  -9.524 -26.043  1.00108.99           C  
ANISOU 2849  CD1 TYR A1161    12760  16426  12225    832  -1883   -745       C  
ATOM   2850  CD2 TYR A1161      13.796  -8.710 -24.155  1.00106.93           C  
ANISOU 2850  CD2 TYR A1161    12320  16192  12118    891  -1783   -952       C  
ATOM   2851  CE1 TYR A1161      13.324 -10.708 -26.010  1.00107.95           C  
ANISOU 2851  CE1 TYR A1161    12694  16452  11870    754  -1656   -682       C  
ATOM   2852  CE2 TYR A1161      14.553  -9.880 -24.127  1.00106.03           C  
ANISOU 2852  CE2 TYR A1161    12281  16225  11782    813  -1580   -866       C  
ATOM   2853  CZ  TYR A1161      14.310 -10.879 -25.055  1.00111.44           C  
ANISOU 2853  CZ  TYR A1161    13079  16969  12294    748  -1513   -738       C  
ATOM   2854  OH  TYR A1161      15.043 -12.043 -25.032  1.00109.45           O  
ANISOU 2854  OH  TYR A1161    12874  16835  11874    680  -1329   -679       O  
ATOM   2855  N   LYS A 236      18.853  -1.751 -13.768  1.00 98.20           N  
ANISOU 2855  N   LYS A 236    10331  17626   9353   1844   1113   -147       N  
ATOM   2856  CA  LYS A 236      18.423  -1.413 -12.410  1.00 95.89           C  
ANISOU 2856  CA  LYS A 236    10098  17009   9325   1614   1042   -107       C  
ATOM   2857  C   LYS A 236      18.646  -2.574 -11.416  1.00 98.92           C  
ANISOU 2857  C   LYS A 236    10446  17196   9942   1490    922   -329       C  
ATOM   2858  O   LYS A 236      17.881  -3.547 -11.406  1.00 98.13           O  
ANISOU 2858  O   LYS A 236    10356  17079   9848   1531    769   -585       O  
ATOM   2859  CB  LYS A 236      16.960  -0.928 -12.399  1.00 97.73           C  
ANISOU 2859  CB  LYS A 236    10421  17213   9498   1645    945   -120       C  
ATOM   2860  N   ALA A 237      19.704  -2.460 -10.582  1.00 94.90           N  
ANISOU 2860  N   ALA A 237     9895  16539   9623   1334    991   -222       N  
ATOM   2861  CA  ALA A 237      20.082  -3.476  -9.596  1.00 93.58           C  
ANISOU 2861  CA  ALA A 237     9697  16188   9672   1227    897   -388       C  
ATOM   2862  C   ALA A 237      19.340  -3.349  -8.263  1.00 95.19           C  
ANISOU 2862  C   ALA A 237     9968  16106  10094   1034    791   -398       C  
ATOM   2863  O   ALA A 237      19.466  -2.336  -7.570  1.00 94.07           O  
ANISOU 2863  O   ALA A 237     9856  15833  10054    894    848   -202       O  
ATOM   2864  CB  ALA A 237      21.588  -3.467  -9.373  1.00 94.90           C  
ANISOU 2864  CB  ALA A 237     9766  16377   9915   1178   1013   -283       C  
ATOM   2865  N   LEU A 238      18.582  -4.401  -7.907  1.00 90.68           N  
ANISOU 2865  N   LEU A 238     9419  15442   9594   1026    635   -630       N  
ATOM   2866  CA  LEU A 238      17.802  -4.496  -6.672  1.00 88.47           C  
ANISOU 2866  CA  LEU A 238     9188  14923   9503    859    528   -664       C  
ATOM   2867  C   LEU A 238      18.527  -5.291  -5.571  1.00 91.80           C  
ANISOU 2867  C   LEU A 238     9587  15149  10143    740    486   -724       C  
ATOM   2868  O   LEU A 238      18.205  -5.130  -4.395  1.00 89.70           O  
ANISOU 2868  O   LEU A 238     9351  14690  10040    587    438   -681       O  
ATOM   2869  CB  LEU A 238      16.397  -5.069  -6.946  1.00 88.46           C  
ANISOU 2869  CB  LEU A 238     9218  14952   9443    901    388   -853       C  
ATOM   2870  CG  LEU A 238      16.330  -6.443  -7.611  1.00 94.26           C  
ANISOU 2870  CG  LEU A 238     9931  15757  10125   1008    289  -1119       C  
ATOM   2871  N   LYS A 239      19.510  -6.125  -5.953  1.00 90.17           N  
ANISOU 2871  N   LYS A 239     9327  15008   9924    831    505   -818       N  
ATOM   2872  CA  LYS A 239      20.315  -6.966  -5.053  1.00 89.84           C  
ANISOU 2872  CA  LYS A 239     9263  14812  10062    768    468   -881       C  
ATOM   2873  C   LYS A 239      21.016  -6.263  -3.860  1.00 90.80           C  
ANISOU 2873  C   LYS A 239     9358  14795  10348    603    523   -698       C  
ATOM   2874  O   LYS A 239      20.998  -6.859  -2.782  1.00 89.35           O  
ANISOU 2874  O   LYS A 239     9196  14423  10331    509    441   -752       O  
ATOM   2875  CB  LYS A 239      21.313  -7.840  -5.837  1.00 95.45           C  
ANISOU 2875  CB  LYS A 239     9914  15663  10688    944    495  -1002       C  
ATOM   2876  CG  LYS A 239      20.666  -8.944  -6.684  1.00120.49           C  
ANISOU 2876  CG  LYS A 239    13131  18889  13760   1093    384  -1262       C  
ATOM   2877  CD  LYS A 239      20.788 -10.311  -6.012  1.00133.85           C  
ANISOU 2877  CD  LYS A 239    14869  20372  15617   1079    259  -1449       C  
ATOM   2878  CE  LYS A 239      19.446 -10.945  -5.729  1.00143.60           C  
ANISOU 2878  CE  LYS A 239    16191  21442  16928    989    105  -1602       C  
ATOM   2879  NZ  LYS A 239      19.550 -12.008  -4.691  1.00151.72           N  
ANISOU 2879  NZ  LYS A 239    17277  22200  18170    901      4  -1690       N  
ATOM   2880  N   PRO A 240      21.640  -5.051  -3.975  1.00 86.23           N  
ANISOU 2880  N   PRO A 240     8737  14293   9734    557    653   -486       N  
ATOM   2881  CA  PRO A 240      22.287  -4.457  -2.788  1.00 84.55           C  
ANISOU 2881  CA  PRO A 240     8499  13936   9690    388    679   -350       C  
ATOM   2882  C   PRO A 240      21.290  -3.924  -1.764  1.00 86.25           C  
ANISOU 2882  C   PRO A 240     8804  13958  10010    249    606   -308       C  
ATOM   2883  O   PRO A 240      21.610  -3.832  -0.582  1.00 84.50           O  
ANISOU 2883  O   PRO A 240     8578  13587   9942    125    574   -271       O  
ATOM   2884  CB  PRO A 240      23.145  -3.339  -3.371  1.00 87.44           C  
ANISOU 2884  CB  PRO A 240     8800  14442   9981    373    833   -149       C  
ATOM   2885  CG  PRO A 240      22.450  -2.936  -4.613  1.00 92.97           C  
ANISOU 2885  CG  PRO A 240     9544  15300  10480    497    880   -123       C  
ATOM   2886  CD  PRO A 240      21.785  -4.168  -5.155  1.00 88.91           C  
ANISOU 2886  CD  PRO A 240     9054  14844   9884    647    777   -358       C  
ATOM   2887  N   THR A 241      20.079  -3.584  -2.236  1.00 82.75           N  
ANISOU 2887  N   THR A 241     8433  13543   9466    289    577   -321       N  
ATOM   2888  CA  THR A 241      18.961  -3.098  -1.437  1.00 80.96           C  
ANISOU 2888  CA  THR A 241     8284  13182   9297    200    508   -297       C  
ATOM   2889  C   THR A 241      18.488  -4.199  -0.486  1.00 82.70           C  
ANISOU 2889  C   THR A 241     8514  13264   9646    139    384   -441       C  
ATOM   2890  O   THR A 241      18.250  -3.932   0.693  1.00 81.04           O  
ANISOU 2890  O   THR A 241     8331  12910   9553     23    345   -395       O  
ATOM   2891  CB  THR A 241      17.901  -2.529  -2.380  1.00 89.91           C  
ANISOU 2891  CB  THR A 241     9466  14436  10258    298    516   -281       C  
ATOM   2892  OG1 THR A 241      18.270  -1.187  -2.685  1.00 90.66           O  
ANISOU 2892  OG1 THR A 241     9589  14559  10297    291    627    -79       O  
ATOM   2893  CG2 THR A 241      16.496  -2.563  -1.804  1.00 87.52           C  
ANISOU 2893  CG2 THR A 241     9215  14061   9977    262    411   -345       C  
ATOM   2894  N   VAL A 242      18.408  -5.438  -1.001  1.00 79.30           N  
ANISOU 2894  N   VAL A 242     8067  12874   9191    219    325   -612       N  
ATOM   2895  CA  VAL A 242      18.023  -6.642  -0.265  1.00 78.41           C  
ANISOU 2895  CA  VAL A 242     7974  12620   9200    166    211   -749       C  
ATOM   2896  C   VAL A 242      19.012  -6.895   0.889  1.00 81.14           C  
ANISOU 2896  C   VAL A 242     8299  12826   9703     87    214   -697       C  
ATOM   2897  O   VAL A 242      18.575  -7.168   2.009  1.00 79.55           O  
ANISOU 2897  O   VAL A 242     8129  12478   9619    -16    147   -693       O  
ATOM   2898  CB  VAL A 242      17.876  -7.860  -1.217  1.00 83.52           C  
ANISOU 2898  CB  VAL A 242     8622  13328   9784    283    150   -950       C  
ATOM   2899  CG1 VAL A 242      17.556  -9.140  -0.452  1.00 83.24           C  
ANISOU 2899  CG1 VAL A 242     8624  13107   9896    213     33  -1078       C  
ATOM   2900  CG2 VAL A 242      16.812  -7.601  -2.279  1.00 83.96           C  
ANISOU 2900  CG2 VAL A 242     8687  13537   9675    359    129  -1015       C  
ATOM   2901  N   ILE A 243      20.326  -6.747   0.628  1.00 78.29           N  
ANISOU 2901  N   ILE A 243     7877  12536   9333    138    293   -645       N  
ATOM   2902  CA  ILE A 243      21.373  -6.929   1.643  1.00 77.85           C  
ANISOU 2902  CA  ILE A 243     7780  12392   9409     81    296   -597       C  
ATOM   2903  C   ILE A 243      21.230  -5.880   2.761  1.00 80.60           C  
ANISOU 2903  C   ILE A 243     8142  12646   9838    -65    303   -458       C  
ATOM   2904  O   ILE A 243      21.190  -6.259   3.931  1.00 80.03           O  
ANISOU 2904  O   ILE A 243     8087  12440   9879   -136    238   -463       O  
ATOM   2905  CB  ILE A 243      22.818  -6.973   1.032  1.00 82.15           C  
ANISOU 2905  CB  ILE A 243     8224  13081   9910    175    384   -576       C  
ATOM   2906  CG1 ILE A 243      22.965  -7.962  -0.171  1.00 83.85           C  
ANISOU 2906  CG1 ILE A 243     8429  13416  10014    358    380   -730       C  
ATOM   2907  CG2 ILE A 243      23.901  -7.200   2.100  1.00 82.54           C  
ANISOU 2907  CG2 ILE A 243     8211  13063  10088    128    374   -538       C  
ATOM   2908  CD1 ILE A 243      22.554  -9.484   0.059  1.00 90.41           C  
ANISOU 2908  CD1 ILE A 243     9334  14104  10914    417    252   -922       C  
ATOM   2909  N   LEU A 244      21.114  -4.579   2.389  1.00 76.47           N  
ANISOU 2909  N   LEU A 244     7623  12185   9247    -98    378   -336       N  
ATOM   2910  CA  LEU A 244      20.972  -3.432   3.301  1.00 75.10           C  
ANISOU 2910  CA  LEU A 244     7481  11918   9136   -220    385   -214       C  
ATOM   2911  C   LEU A 244      19.835  -3.601   4.320  1.00 77.55           C  
ANISOU 2911  C   LEU A 244     7861  12103   9500   -277    290   -251       C  
ATOM   2912  O   LEU A 244      20.072  -3.479   5.529  1.00 76.19           O  
ANISOU 2912  O   LEU A 244     7691  11829   9428   -360    252   -220       O  
ATOM   2913  CB  LEU A 244      20.829  -2.116   2.493  1.00 75.56           C  
ANISOU 2913  CB  LEU A 244     7567  12048   9095   -216    475    -91       C  
ATOM   2914  CG  LEU A 244      20.541  -0.815   3.260  1.00 79.44           C  
ANISOU 2914  CG  LEU A 244     8126  12425   9635   -320    477     25       C  
ATOM   2915  CD1 LEU A 244      21.747  -0.363   4.066  1.00 80.08           C  
ANISOU 2915  CD1 LEU A 244     8151  12441   9836   -437    497     93       C  
ATOM   2916  CD2 LEU A 244      20.147   0.289   2.309  1.00 81.54           C  
ANISOU 2916  CD2 LEU A 244     8451  12744   9785   -279    554    134       C  
ATOM   2917  N   ILE A 245      18.616  -3.899   3.822  1.00 73.82           N  
ANISOU 2917  N   ILE A 245     7432  11662   8952   -229    251   -319       N  
ATOM   2918  CA  ILE A 245      17.415  -4.113   4.630  1.00 72.82           C  
ANISOU 2918  CA  ILE A 245     7349  11463   8856   -279    171   -352       C  
ATOM   2919  C   ILE A 245      17.567  -5.340   5.542  1.00 76.89           C  
ANISOU 2919  C   ILE A 245     7853  11874   9487   -326     99   -420       C  
ATOM   2920  O   ILE A 245      17.332  -5.228   6.747  1.00 75.26           O  
ANISOU 2920  O   ILE A 245     7663  11582   9351   -400     62   -378       O  
ATOM   2921  CB  ILE A 245      16.135  -4.104   3.739  1.00 76.12           C  
ANISOU 2921  CB  ILE A 245     7788  11979   9154   -216    150   -410       C  
ATOM   2922  CG1 ILE A 245      15.797  -2.644   3.341  1.00 76.53           C  
ANISOU 2922  CG1 ILE A 245     7881  12091   9106   -179    210   -298       C  
ATOM   2923  CG2 ILE A 245      14.936  -4.786   4.433  1.00 76.16           C  
ANISOU 2923  CG2 ILE A 245     7798  11940   9198   -274     60   -479       C  
ATOM   2924  CD1 ILE A 245      14.756  -2.417   2.270  1.00 82.49           C  
ANISOU 2924  CD1 ILE A 245     8649  12984   9708    -79    207   -331       C  
ATOM   2925  N   LEU A 246      18.003  -6.486   4.974  1.00 75.09           N  
ANISOU 2925  N   LEU A 246     7607  11652   9274   -268     80   -521       N  
ATOM   2926  CA  LEU A 246      18.220  -7.731   5.721  1.00 75.18           C  
ANISOU 2926  CA  LEU A 246     7628  11541   9395   -292     13   -580       C  
ATOM   2927  C   LEU A 246      19.266  -7.589   6.825  1.00 77.49           C  
ANISOU 2927  C   LEU A 246     7897  11769   9778   -326     22   -501       C  
ATOM   2928  O   LEU A 246      19.075  -8.138   7.909  1.00 76.12           O  
ANISOU 2928  O   LEU A 246     7748  11488   9686   -378    -34   -487       O  
ATOM   2929  CB  LEU A 246      18.589  -8.876   4.779  1.00 76.65           C  
ANISOU 2929  CB  LEU A 246     7816  11740   9569   -194     -8   -713       C  
ATOM   2930  CG  LEU A 246      17.513  -9.917   4.570  1.00 82.20           C  
ANISOU 2930  CG  LEU A 246     8566  12374  10291   -217    -94   -835       C  
ATOM   2931  CD1 LEU A 246      17.517 -10.406   3.150  1.00 83.63           C  
ANISOU 2931  CD1 LEU A 246     8747  12646  10380   -102   -101   -977       C  
ATOM   2932  CD2 LEU A 246      17.695 -11.087   5.525  1.00 85.64           C  
ANISOU 2932  CD2 LEU A 246     9046  12626  10865   -261   -162   -856       C  
ATOM   2933  N   ALA A 247      20.355  -6.836   6.557  1.00 74.12           N  
ANISOU 2933  N   ALA A 247     7415  11418   9331   -301     91   -442       N  
ATOM   2934  CA  ALA A 247      21.404  -6.584   7.546  1.00 73.78           C  
ANISOU 2934  CA  ALA A 247     7325  11343   9364   -339     93   -376       C  
ATOM   2935  C   ALA A 247      20.848  -5.701   8.675  1.00 76.86           C  
ANISOU 2935  C   ALA A 247     7750  11672   9783   -440     68   -298       C  
ATOM   2936  O   ALA A 247      21.099  -6.000   9.844  1.00 76.13           O  
ANISOU 2936  O   ALA A 247     7655  11512   9758   -471     19   -280       O  
ATOM   2937  CB  ALA A 247      22.621  -5.944   6.895  1.00 75.14           C  
ANISOU 2937  CB  ALA A 247     7410  11632   9507   -313    176   -333       C  
ATOM   2938  N   PHE A 248      20.029  -4.673   8.324  1.00 73.20           N  
ANISOU 2938  N   PHE A 248     7325  11236   9252   -468     96   -258       N  
ATOM   2939  CA  PHE A 248      19.353  -3.787   9.284  1.00 72.41           C  
ANISOU 2939  CA  PHE A 248     7272  11086   9156   -532     70   -202       C  
ATOM   2940  C   PHE A 248      18.404  -4.614  10.170  1.00 76.30           C  
ANISOU 2940  C   PHE A 248     7794  11524   9673   -550      0   -232       C  
ATOM   2941  O   PHE A 248      18.377  -4.415  11.384  1.00 74.67           O  
ANISOU 2941  O   PHE A 248     7597  11273   9501   -589    -37   -195       O  
ATOM   2942  CB  PHE A 248      18.574  -2.681   8.545  1.00 74.14           C  
ANISOU 2942  CB  PHE A 248     7537  11348   9283   -517    112   -165       C  
ATOM   2943  CG  PHE A 248      17.940  -1.628   9.427  1.00 75.06           C  
ANISOU 2943  CG  PHE A 248     7713  11415   9390   -553     89   -115       C  
ATOM   2944  CD1 PHE A 248      18.571  -0.409   9.643  1.00 78.31           C  
ANISOU 2944  CD1 PHE A 248     8149  11783   9823   -594    116    -50       C  
ATOM   2945  CD2 PHE A 248      16.689  -1.835   9.999  1.00 76.56           C  
ANISOU 2945  CD2 PHE A 248     7934  11609   9548   -543     40   -138       C  
ATOM   2946  CE1 PHE A 248      17.977   0.570  10.449  1.00 79.04           C  
ANISOU 2946  CE1 PHE A 248     8314  11815   9902   -606     83    -25       C  
ATOM   2947  CE2 PHE A 248      16.102  -0.860  10.810  1.00 79.03           C  
ANISOU 2947  CE2 PHE A 248     8299  11895   9835   -545     18   -103       C  
ATOM   2948  CZ  PHE A 248      16.749   0.336  11.030  1.00 77.36           C  
ANISOU 2948  CZ  PHE A 248     8131  11622   9642   -566     35    -55       C  
ATOM   2949  N   PHE A 249      17.640  -5.541   9.548  1.00 74.81           N  
ANISOU 2949  N   PHE A 249     7615  11346   9463   -525    -19   -297       N  
ATOM   2950  CA  PHE A 249      16.712  -6.467  10.203  1.00 75.30           C  
ANISOU 2950  CA  PHE A 249     7696  11357   9558   -565    -78   -319       C  
ATOM   2951  C   PHE A 249      17.486  -7.401  11.132  1.00 77.49           C  
ANISOU 2951  C   PHE A 249     7973  11540   9930   -575   -114   -306       C  
ATOM   2952  O   PHE A 249      17.027  -7.666  12.239  1.00 76.11           O  
ANISOU 2952  O   PHE A 249     7813  11322   9784   -621   -149   -259       O  
ATOM   2953  CB  PHE A 249      15.875  -7.244   9.147  1.00 78.61           C  
ANISOU 2953  CB  PHE A 249     8118  11804   9944   -551    -96   -411       C  
ATOM   2954  CG  PHE A 249      15.666  -8.735   9.352  1.00 82.04           C  
ANISOU 2954  CG  PHE A 249     8571  12139  10461   -585   -154   -469       C  
ATOM   2955  CD1 PHE A 249      16.491  -9.665   8.724  1.00 86.70           C  
ANISOU 2955  CD1 PHE A 249     9175  12674  11093   -523   -166   -549       C  
ATOM   2956  CD2 PHE A 249      14.621  -9.207  10.139  1.00 85.21           C  
ANISOU 2956  CD2 PHE A 249     8978  12501  10895   -674   -196   -443       C  
ATOM   2957  CE1 PHE A 249      16.299 -11.041   8.913  1.00 88.80           C  
ANISOU 2957  CE1 PHE A 249     9484  12809  11446   -551   -227   -605       C  
ATOM   2958  CE2 PHE A 249      14.423 -10.583  10.319  1.00 89.36           C  
ANISOU 2958  CE2 PHE A 249     9535  12905  11512   -726   -248   -481       C  
ATOM   2959  CZ  PHE A 249      15.265 -11.490   9.705  1.00 88.38           C  
ANISOU 2959  CZ  PHE A 249     9448  12691  11441   -663   -268   -565       C  
ATOM   2960  N   ALA A 250      18.664  -7.876  10.685  1.00 74.39           N  
ANISOU 2960  N   ALA A 250     7558  11135   9573   -516   -102   -341       N  
ATOM   2961  CA  ALA A 250      19.522  -8.762  11.470  1.00 74.83           C  
ANISOU 2961  CA  ALA A 250     7613  11113   9707   -490   -137   -331       C  
ATOM   2962  C   ALA A 250      20.069  -8.058  12.716  1.00 78.47           C  
ANISOU 2962  C   ALA A 250     8048  11585  10183   -517   -147   -250       C  
ATOM   2963  O   ALA A 250      20.102  -8.671  13.781  1.00 77.83           O  
ANISOU 2963  O   ALA A 250     7987  11443  10143   -519   -191   -211       O  
ATOM   2964  CB  ALA A 250      20.661  -9.292  10.616  1.00 76.46           C  
ANISOU 2964  CB  ALA A 250     7785  11341   9924   -393   -118   -395       C  
ATOM   2965  N   CYS A 251      20.464  -6.768  12.581  1.00 75.22           N  
ANISOU 2965  N   CYS A 251     7598  11246   9735   -537   -109   -225       N  
ATOM   2966  CA  CYS A 251      20.998  -5.919  13.658  1.00 74.84           C  
ANISOU 2966  CA  CYS A 251     7525  11212   9699   -572   -128   -174       C  
ATOM   2967  C   CYS A 251      19.980  -5.744  14.791  1.00 79.40           C  
ANISOU 2967  C   CYS A 251     8153  11762  10253   -607   -169   -135       C  
ATOM   2968  O   CYS A 251      20.314  -5.929  15.964  1.00 79.61           O  
ANISOU 2968  O   CYS A 251     8173  11778  10297   -601   -214   -105       O  
ATOM   2969  CB  CYS A 251      21.443  -4.565  13.104  1.00 74.84           C  
ANISOU 2969  CB  CYS A 251     7497  11264   9676   -609    -79   -160       C  
ATOM   2970  SG  CYS A 251      22.968  -4.619  12.131  1.00 79.39           S  
ANISOU 2970  SG  CYS A 251     7971  11918  10277   -580    -22   -174       S  
ATOM   2971  N   TRP A 252      18.737  -5.403  14.424  1.00 75.87           N  
ANISOU 2971  N   TRP A 252     7747  11328   9752   -629   -153   -135       N  
ATOM   2972  CA  TRP A 252      17.641  -5.153  15.345  1.00 75.62           C  
ANISOU 2972  CA  TRP A 252     7747  11310   9676   -650   -178    -99       C  
ATOM   2973  C   TRP A 252      16.905  -6.398  15.844  1.00 80.87           C  
ANISOU 2973  C   TRP A 252     8422  11945  10359   -668   -203    -74       C  
ATOM   2974  O   TRP A 252      16.212  -6.304  16.859  1.00 80.32           O  
ANISOU 2974  O   TRP A 252     8359  11906  10251   -682   -221    -23       O  
ATOM   2975  CB  TRP A 252      16.671  -4.159  14.719  1.00 74.17           C  
ANISOU 2975  CB  TRP A 252     7588  11176   9416   -649   -149   -109       C  
ATOM   2976  CG  TRP A 252      17.149  -2.743  14.767  1.00 75.24           C  
ANISOU 2976  CG  TRP A 252     7745  11312   9531   -643   -137   -102       C  
ATOM   2977  CD1 TRP A 252      17.688  -2.023  13.743  1.00 78.49           C  
ANISOU 2977  CD1 TRP A 252     8161  11719   9943   -643    -92   -106       C  
ATOM   2978  CD2 TRP A 252      17.133  -1.875  15.906  1.00 75.20           C  
ANISOU 2978  CD2 TRP A 252     7767  11301   9502   -640   -173    -88       C  
ATOM   2979  NE1 TRP A 252      17.996  -0.751  14.169  1.00 78.27           N  
ANISOU 2979  NE1 TRP A 252     8171  11659   9911   -659    -99    -89       N  
ATOM   2980  CE2 TRP A 252      17.663  -0.632  15.494  1.00 79.66           C  
ANISOU 2980  CE2 TRP A 252     8364  11831  10072   -652   -156    -93       C  
ATOM   2981  CE3 TRP A 252      16.720  -2.025  17.240  1.00 76.49           C  
ANISOU 2981  CE3 TRP A 252     7936  11490   9635   -624   -220    -72       C  
ATOM   2982  CZ2 TRP A 252      17.789   0.455  16.370  1.00 79.33           C  
ANISOU 2982  CZ2 TRP A 252     8369  11754  10018   -653   -196   -103       C  
ATOM   2983  CZ3 TRP A 252      16.848  -0.950  18.106  1.00 78.17           C  
ANISOU 2983  CZ3 TRP A 252     8186  11701   9816   -605   -257    -86       C  
ATOM   2984  CH2 TRP A 252      17.384   0.270  17.673  1.00 79.19           C  
ANISOU 2984  CH2 TRP A 252     8355  11770   9963   -622   -252   -112       C  
ATOM   2985  N   LEU A 253      17.059  -7.557  15.157  1.00 79.08           N  
ANISOU 2985  N   LEU A 253     8199  11658  10189   -667   -205   -107       N  
ATOM   2986  CA  LEU A 253      16.409  -8.829  15.522  1.00 80.03           C  
ANISOU 2986  CA  LEU A 253     8345  11709  10352   -706   -231    -81       C  
ATOM   2987  C   LEU A 253      16.668  -9.316  16.967  1.00 85.22           C  
ANISOU 2987  C   LEU A 253     9017  12331  11031   -703   -260     11       C  
ATOM   2988  O   LEU A 253      15.680  -9.638  17.631  1.00 85.09           O  
ANISOU 2988  O   LEU A 253     9008  12326  10997   -758   -263     78       O  
ATOM   2989  CB  LEU A 253      16.664  -9.944  14.484  1.00 80.82           C  
ANISOU 2989  CB  LEU A 253     8468  11721  10518   -693   -240   -156       C  
ATOM   2990  CG  LEU A 253      15.792 -11.198  14.577  1.00 86.41           C  
ANISOU 2990  CG  LEU A 253     9215  12331  11285   -765   -271   -149       C  
ATOM   2991  CD1 LEU A 253      14.405 -10.960  13.996  1.00 86.48           C  
ANISOU 2991  CD1 LEU A 253     9196  12414  11249   -844   -265   -183       C  
ATOM   2992  CD2 LEU A 253      16.452 -12.359  13.879  1.00 89.67           C  
ANISOU 2992  CD2 LEU A 253     9679  12614  11779   -719   -299   -225       C  
ATOM   2993  N   PRO A 254      17.926  -9.363  17.500  1.00 82.75           N  
ANISOU 2993  N   PRO A 254     8698  12000  10743   -637   -280     25       N  
ATOM   2994  CA  PRO A 254      18.112  -9.817  18.891  1.00 83.41           C  
ANISOU 2994  CA  PRO A 254     8798  12072  10824   -614   -312    119       C  
ATOM   2995  C   PRO A 254      17.437  -8.905  19.918  1.00 87.54           C  
ANISOU 2995  C   PRO A 254     9304  12703  11255   -630   -312    172       C  
ATOM   2996  O   PRO A 254      16.946  -9.391  20.936  1.00 87.55           O  
ANISOU 2996  O   PRO A 254     9321  12715  11228   -637   -320    267       O  
ATOM   2997  CB  PRO A 254      19.633  -9.833  19.059  1.00 85.38           C  
ANISOU 2997  CB  PRO A 254     9019  12321  11101   -525   -338     95       C  
ATOM   2998  CG  PRO A 254      20.137  -8.858  18.060  1.00 88.87           C  
ANISOU 2998  CG  PRO A 254     9411  12819  11536   -529   -310      7       C  
ATOM   2999  CD  PRO A 254      19.227  -9.021  16.887  1.00 84.13           C  
ANISOU 2999  CD  PRO A 254     8836  12189  10940   -576   -274    -37       C  
ATOM   3000  N   TYR A 255      17.395  -7.590  19.623  1.00 84.06           N  
ANISOU 3000  N   TYR A 255     8839  12339  10762   -630   -300    114       N  
ATOM   3001  CA  TYR A 255      16.756  -6.575  20.456  1.00 83.92           C  
ANISOU 3001  CA  TYR A 255     8817  12419  10649   -621   -306    133       C  
ATOM   3002  C   TYR A 255      15.249  -6.828  20.494  1.00 88.51           C  
ANISOU 3002  C   TYR A 255     9399  13050  11182   -666   -277    180       C  
ATOM   3003  O   TYR A 255      14.657  -6.748  21.569  1.00 88.39           O  
ANISOU 3003  O   TYR A 255     9376  13118  11092   -650   -281    246       O  
ATOM   3004  CB  TYR A 255      17.074  -5.161  19.931  1.00 84.36           C  
ANISOU 3004  CB  TYR A 255     8872  12501  10682   -612   -302     55       C  
ATOM   3005  CG  TYR A 255      16.400  -4.049  20.705  1.00 85.81           C  
ANISOU 3005  CG  TYR A 255     9074  12765  10767   -581   -317     51       C  
ATOM   3006  CD1 TYR A 255      16.886  -3.641  21.944  1.00 88.38           C  
ANISOU 3006  CD1 TYR A 255     9400  13133  11048   -534   -368     51       C  
ATOM   3007  CD2 TYR A 255      15.280  -3.399  20.195  1.00 86.03           C  
ANISOU 3007  CD2 TYR A 255     9118  12835  10734   -579   -287     35       C  
ATOM   3008  CE1 TYR A 255      16.269  -2.617  22.660  1.00 89.44           C  
ANISOU 3008  CE1 TYR A 255     9562  13340  11082   -485   -390     27       C  
ATOM   3009  CE2 TYR A 255      14.661  -2.367  20.897  1.00 87.09           C  
ANISOU 3009  CE2 TYR A 255     9278  13043  10769   -521   -304     20       C  
ATOM   3010  CZ  TYR A 255      15.167  -1.971  22.125  1.00 96.20           C  
ANISOU 3010  CZ  TYR A 255    10442  14226  11882   -473   -356     11       C  
ATOM   3011  OH  TYR A 255      14.559  -0.964  22.835  1.00 99.13           O  
ANISOU 3011  OH  TYR A 255    10850  14670  12146   -396   -381    -22       O  
ATOM   3012  N   TYR A 256      14.641  -7.161  19.327  1.00 85.20           N  
ANISOU 3012  N   TYR A 256     8975  12601  10797   -718   -250    143       N  
ATOM   3013  CA  TYR A 256      13.218  -7.476  19.212  1.00 85.46           C  
ANISOU 3013  CA  TYR A 256     8982  12695  10795   -779   -227    174       C  
ATOM   3014  C   TYR A 256      12.914  -8.773  19.964  1.00 89.71           C  
ANISOU 3014  C   TYR A 256     9522  13187  11377   -840   -230    277       C  
ATOM   3015  O   TYR A 256      11.880  -8.861  20.628  1.00 89.66           O  
ANISOU 3015  O   TYR A 256     9477  13277  11311   -880   -211    354       O  
ATOM   3016  CB  TYR A 256      12.774  -7.569  17.741  1.00 87.09           C  
ANISOU 3016  CB  TYR A 256     9178  12885  11028   -816   -213     92       C  
ATOM   3017  CG  TYR A 256      12.929  -6.305  16.915  1.00 89.52           C  
ANISOU 3017  CG  TYR A 256     9491  13240  11282   -755   -198     18       C  
ATOM   3018  CD1 TYR A 256      12.603  -5.055  17.444  1.00 91.41           C  
ANISOU 3018  CD1 TYR A 256     9736  13567  11428   -697   -195     26       C  
ATOM   3019  CD2 TYR A 256      13.288  -6.366  15.572  1.00 90.72           C  
ANISOU 3019  CD2 TYR A 256     9651  13352  11466   -749   -187    -57       C  
ATOM   3020  CE1 TYR A 256      12.722  -3.892  16.680  1.00 92.25           C  
ANISOU 3020  CE1 TYR A 256     9871  13687  11494   -644   -181    -25       C  
ATOM   3021  CE2 TYR A 256      13.385  -5.214  14.791  1.00 91.55           C  
ANISOU 3021  CE2 TYR A 256     9769  13501  11515   -696   -164    -97       C  
ATOM   3022  CZ  TYR A 256      13.116  -3.976  15.354  1.00 99.93           C  
ANISOU 3022  CZ  TYR A 256    10850  14618  12502   -649   -160    -74       C  
ATOM   3023  OH  TYR A 256      13.210  -2.843  14.577  1.00101.33           O  
ANISOU 3023  OH  TYR A 256    11060  14808  12633   -598   -137    -99       O  
ATOM   3024  N   ILE A 257      13.846  -9.757  19.903  1.00 86.78           N  
ANISOU 3024  N   ILE A 257     9195  12673  11104   -838   -252    288       N  
ATOM   3025  CA  ILE A 257      13.765 -11.037  20.624  1.00 87.96           C  
ANISOU 3025  CA  ILE A 257     9378  12732  11310   -882   -258    400       C  
ATOM   3026  C   ILE A 257      13.790 -10.754  22.145  1.00 93.17           C  
ANISOU 3026  C   ILE A 257    10028  13493  11878   -829   -256    516       C  
ATOM   3027  O   ILE A 257      13.000 -11.340  22.892  1.00 93.86           O  
ANISOU 3027  O   ILE A 257    10107  13612  11944   -887   -233    642       O  
ATOM   3028  CB  ILE A 257      14.871 -12.032  20.142  1.00 91.27           C  
ANISOU 3028  CB  ILE A 257     9864  12971  11844   -846   -289    366       C  
ATOM   3029  CG1 ILE A 257      14.505 -12.618  18.756  1.00 91.69           C  
ANISOU 3029  CG1 ILE A 257     9934  12927  11979   -912   -293    264       C  
ATOM   3030  CG2 ILE A 257      15.129 -13.163  21.158  1.00 93.11           C  
ANISOU 3030  CG2 ILE A 257    10157  13101  12121   -839   -303    503       C  
ATOM   3031  CD1 ILE A 257      15.692 -13.092  17.904  1.00 97.45           C  
ANISOU 3031  CD1 ILE A 257    10708  13539  12781   -828   -319    165       C  
ATOM   3032  N   GLY A 258      14.645  -9.810  22.556  1.00 89.22           N  
ANISOU 3032  N   GLY A 258     9521  13059  11318   -726   -280    470       N  
ATOM   3033  CA  GLY A 258      14.784  -9.374  23.942  1.00 89.44           C  
ANISOU 3033  CA  GLY A 258     9540  13204  11241   -650   -294    541       C  
ATOM   3034  C   GLY A 258      13.580  -8.611  24.457  1.00 93.86           C  
ANISOU 3034  C   GLY A 258    10054  13932  11675   -655   -264    568       C  
ATOM   3035  O   GLY A 258      12.960  -9.028  25.439  1.00 94.26           O  
ANISOU 3035  O   GLY A 258    10088  14069  11655   -658   -241    693       O  
ATOM   3036  N   ILE A 259      13.235  -7.497  23.781  1.00 90.15           N  
ANISOU 3036  N   ILE A 259     9566  13518  11170   -644   -260    458       N  
ATOM   3037  CA  ILE A 259      12.108  -6.618  24.113  1.00 90.37           C  
ANISOU 3037  CA  ILE A 259     9554  13712  11071   -615   -238    454       C  
ATOM   3038  C   ILE A 259      10.775  -7.362  24.269  1.00 96.79           C  
ANISOU 3038  C   ILE A 259    10307  14613  11856   -699   -185    561       C  
ATOM   3039  O   ILE A 259      10.003  -7.033  25.176  1.00 97.34           O  
ANISOU 3039  O   ILE A 259    10331  14858  11797   -654   -162    624       O  
ATOM   3040  CB  ILE A 259      12.074  -5.374  23.173  1.00 92.48           C  
ANISOU 3040  CB  ILE A 259     9835  13979  11325   -581   -246    321       C  
ATOM   3041  CG1 ILE A 259      13.037  -4.256  23.667  1.00 92.62           C  
ANISOU 3041  CG1 ILE A 259     9897  13988  11306   -487   -297    242       C  
ATOM   3042  CG2 ILE A 259      10.673  -4.844  22.857  1.00 93.37           C  
ANISOU 3042  CG2 ILE A 259     9903  14226  11348   -575   -211    311       C  
ATOM   3043  CD1 ILE A 259      12.737  -3.551  25.057  1.00 99.76           C  
ANISOU 3043  CD1 ILE A 259    10803  15037  12063   -379   -324    251       C  
ATOM   3044  N   SER A 260      10.530  -8.387  23.420  1.00 94.50           N  
ANISOU 3044  N   SER A 260    10012  14210  11685   -822   -170    580       N  
ATOM   3045  CA  SER A 260       9.321  -9.216  23.490  1.00 95.81           C  
ANISOU 3045  CA  SER A 260    10112  14434  11857   -945   -127    680       C  
ATOM   3046  C   SER A 260       9.265  -9.975  24.823  1.00101.34           C  
ANISOU 3046  C   SER A 260    10812  15170  12523   -958   -102    858       C  
ATOM   3047  O   SER A 260       8.230  -9.930  25.481  1.00101.97           O  
ANISOU 3047  O   SER A 260    10811  15431  12503   -984    -55    955       O  
ATOM   3048  CB  SER A 260       9.238 -10.176  22.306  1.00 99.68           C  
ANISOU 3048  CB  SER A 260    10617  14761  12496  -1075   -136    637       C  
ATOM   3049  OG  SER A 260      10.404 -10.975  22.197  1.00109.18           O  
ANISOU 3049  OG  SER A 260    11912  15755  13815  -1068   -168    639       O  
ATOM   3050  N   ILE A 261      10.397 -10.606  25.248  1.00 97.97           N  
ANISOU 3050  N   ILE A 261    10470  14595  12161   -921   -132    904       N  
ATOM   3051  CA  ILE A 261      10.538 -11.340  26.520  1.00 99.16           C  
ANISOU 3051  CA  ILE A 261    10642  14764  12272   -904   -114   1084       C  
ATOM   3052  C   ILE A 261      10.245 -10.411  27.718  1.00103.54           C  
ANISOU 3052  C   ILE A 261    11146  15566  12628   -778    -99   1124       C  
ATOM   3053  O   ILE A 261       9.571 -10.834  28.659  1.00104.66           O  
ANISOU 3053  O   ILE A 261    11247  15836  12684   -798    -47   1290       O  
ATOM   3054  CB  ILE A 261      11.912 -12.082  26.624  1.00102.39           C  
ANISOU 3054  CB  ILE A 261    11154  14973  12776   -848   -161   1100       C  
ATOM   3055  CG1 ILE A 261      12.045 -13.179  25.532  1.00103.18           C  
ANISOU 3055  CG1 ILE A 261    11313  14829  13063   -963   -173   1074       C  
ATOM   3056  CG2 ILE A 261      12.146 -12.682  28.028  1.00104.34           C  
ANISOU 3056  CG2 ILE A 261    11432  15264  12949   -785   -149   1290       C  
ATOM   3057  CD1 ILE A 261      13.509 -13.654  25.218  1.00109.82           C  
ANISOU 3057  CD1 ILE A 261    12245  15482  13999   -870   -230   1014       C  
ATOM   3058  N   ASP A 262      10.713  -9.141  27.655  1.00 99.00           N  
ANISOU 3058  N   ASP A 262    10575  15060  11979   -652   -143    971       N  
ATOM   3059  CA  ASP A 262      10.458  -8.131  28.689  1.00 99.12           C  
ANISOU 3059  CA  ASP A 262    10559  15297  11806   -513   -148    960       C  
ATOM   3060  C   ASP A 262       8.969  -7.811  28.734  1.00103.01           C  
ANISOU 3060  C   ASP A 262    10955  15990  12194   -542    -84    999       C  
ATOM   3061  O   ASP A 262       8.425  -7.636  29.819  1.00103.66           O  
ANISOU 3061  O   ASP A 262    10989  16283  12116   -464    -52   1088       O  
ATOM   3062  CB  ASP A 262      11.279  -6.853  28.447  1.00100.08           C  
ANISOU 3062  CB  ASP A 262    10723  15396  11907   -401   -218    771       C  
ATOM   3063  CG  ASP A 262      10.835  -5.663  29.281  1.00112.91           C  
ANISOU 3063  CG  ASP A 262    12328  17226  13346   -259   -234    712       C  
ATOM   3064  OD1 ASP A 262      11.032  -5.696  30.520  1.00114.90           O  
ANISOU 3064  OD1 ASP A 262    12579  17604  13473   -158   -248    774       O  
ATOM   3065  OD2 ASP A 262      10.253  -4.715  28.702  1.00119.01           O  
ANISOU 3065  OD2 ASP A 262    13092  18041  14087   -234   -232    604       O  
ATOM   3066  N   SER A 263       8.313  -7.761  27.560  1.00 98.93           N  
ANISOU 3066  N   SER A 263    10401  15432  11756   -642    -66    931       N  
ATOM   3067  CA  SER A 263       6.875  -7.524  27.468  1.00 99.28           C  
ANISOU 3067  CA  SER A 263    10331  15681  11710   -676     -9    960       C  
ATOM   3068  C   SER A 263       6.124  -8.786  27.919  1.00104.54           C  
ANISOU 3068  C   SER A 263    10923  16398  12402   -829     59   1162       C  
ATOM   3069  O   SER A 263       5.029  -8.666  28.465  1.00105.46           O  
ANISOU 3069  O   SER A 263    10923  16758  12390   -829    120   1249       O  
ATOM   3070  CB  SER A 263       6.478  -7.126  26.050  1.00101.64           C  
ANISOU 3070  CB  SER A 263    10611  15925  12082   -728    -22    824       C  
ATOM   3071  OG  SER A 263       5.333  -6.288  26.075  1.00110.27           O  
ANISOU 3071  OG  SER A 263    11610  17255  13031   -655      6    790       O  
ATOM   3072  N   PHE A 264       6.734  -9.987  27.727  1.00101.15           N  
ANISOU 3072  N   PHE A 264    10561  15738  12133   -952     51   1242       N  
ATOM   3073  CA  PHE A 264       6.176 -11.276  28.151  1.00102.70           C  
ANISOU 3073  CA  PHE A 264    10722  15913  12386  -1116    110   1448       C  
ATOM   3074  C   PHE A 264       6.171 -11.387  29.676  1.00107.77           C  
ANISOU 3074  C   PHE A 264    11352  16722  12875  -1026    156   1632       C  
ATOM   3075  O   PHE A 264       5.182 -11.849  30.240  1.00109.25           O  
ANISOU 3075  O   PHE A 264    11438  17071  13000  -1119    236   1806       O  
ATOM   3076  CB  PHE A 264       6.902 -12.469  27.494  1.00104.55           C  
ANISOU 3076  CB  PHE A 264    11067  15821  12838  -1242     76   1463       C  
ATOM   3077  CG  PHE A 264       6.289 -12.930  26.190  1.00106.08           C  
ANISOU 3077  CG  PHE A 264    11225  15903  13178  -1420     66   1377       C  
ATOM   3078  CD1 PHE A 264       5.191 -13.780  26.180  1.00110.94           C  
ANISOU 3078  CD1 PHE A 264    11754  16549  13849  -1628    116   1502       C  
ATOM   3079  CD2 PHE A 264       6.817 -12.524  24.970  1.00106.51           C  
ANISOU 3079  CD2 PHE A 264    11328  15831  13311  -1385      5   1172       C  
ATOM   3080  CE1 PHE A 264       4.611 -14.190  24.975  1.00111.93           C  
ANISOU 3080  CE1 PHE A 264    11839  16584  14104  -1794     90   1399       C  
ATOM   3081  CE2 PHE A 264       6.237 -12.933  23.765  1.00109.41           C  
ANISOU 3081  CE2 PHE A 264    11660  16121  13790  -1530    -12   1079       C  
ATOM   3082  CZ  PHE A 264       5.141 -13.767  23.776  1.00109.26           C  
ANISOU 3082  CZ  PHE A 264    11554  16133  13826  -1733     23   1182       C  
ATOM   3083  N   ILE A 265       7.248 -10.931  30.345  1.00103.59           N  
ANISOU 3083  N   ILE A 265    10910  16179  12272   -844    106   1593       N  
ATOM   3084  CA  ILE A 265       7.317 -10.931  31.810  1.00104.86           C  
ANISOU 3084  CA  ILE A 265    11062  16526  12255   -720    136   1744       C  
ATOM   3085  C   ILE A 265       6.431  -9.813  32.399  1.00109.54           C  
ANISOU 3085  C   ILE A 265    11544  17454  12621   -590    169   1704       C  
ATOM   3086  O   ILE A 265       5.870  -9.997  33.482  1.00111.45           O  
ANISOU 3086  O   ILE A 265    11718  17925  12702   -546    237   1874       O  
ATOM   3087  CB  ILE A 265       8.774 -10.983  32.380  1.00107.60           C  
ANISOU 3087  CB  ILE A 265    11530  16755  12597   -573     62   1724       C  
ATOM   3088  CG1 ILE A 265       8.793 -11.380  33.879  1.00110.26           C  
ANISOU 3088  CG1 ILE A 265    11864  17264  12764   -472    102   1934       C  
ATOM   3089  CG2 ILE A 265       9.559  -9.688  32.130  1.00106.18           C  
ANISOU 3089  CG2 ILE A 265    11384  16584  12376   -418    -28   1478       C  
ATOM   3090  CD1 ILE A 265       9.933 -12.316  34.302  1.00118.88           C  
ANISOU 3090  CD1 ILE A 265    13073  18171  13925   -431     65   2043       C  
ATOM   3091  N   LEU A 266       6.272  -8.686  31.662  1.00104.43           N  
ANISOU 3091  N   LEU A 266    10881  16838  11958   -524    126   1488       N  
ATOM   3092  CA  LEU A 266       5.439  -7.548  32.070  1.00104.57           C  
ANISOU 3092  CA  LEU A 266    10814  17147  11772   -375    144   1416       C  
ATOM   3093  C   LEU A 266       3.956  -7.918  32.131  1.00109.56           C  
ANISOU 3093  C   LEU A 266    11281  18012  12335   -480    247   1553       C  
ATOM   3094  O   LEU A 266       3.246  -7.454  33.026  1.00110.32           O  
ANISOU 3094  O   LEU A 266    11285  18415  12218   -353    297   1609       O  
ATOM   3095  CB  LEU A 266       5.659  -6.325  31.148  1.00102.85           C  
ANISOU 3095  CB  LEU A 266    10645  16855  11580   -289     71   1166       C  
ATOM   3096  CG  LEU A 266       6.273  -5.041  31.763  1.00107.17           C  
ANISOU 3096  CG  LEU A 266    11268  17463  11988    -58     -5   1007       C  
ATOM   3097  CD1 LEU A 266       5.532  -4.583  33.023  1.00108.95           C  
ANISOU 3097  CD1 LEU A 266    11421  18019  11957    114     33   1062       C  
ATOM   3098  CD2 LEU A 266       7.766  -5.193  32.037  1.00109.44           C  
ANISOU 3098  CD2 LEU A 266    11673  17552  12355    -30    -84    967       C  
ATOM   3099  N   LEU A 267       3.508  -8.779  31.197  1.00105.99           N  
ANISOU 3099  N   LEU A 267    10784  17426  12061   -710    276   1605       N  
ATOM   3100  CA  LEU A 267       2.134  -9.279  31.130  1.00107.54           C  
ANISOU 3100  CA  LEU A 267    10806  17820  12235   -865    367   1737       C  
ATOM   3101  C   LEU A 267       1.935 -10.493  32.057  1.00114.46           C  
ANISOU 3101  C   LEU A 267    11646  18729  13113  -1000    451   2020       C  
ATOM   3102  O   LEU A 267       0.812 -10.988  32.180  1.00116.16           O  
ANISOU 3102  O   LEU A 267    11703  19128  13306  -1151    539   2168       O  
ATOM   3103  CB  LEU A 267       1.752  -9.638  29.679  1.00106.74           C  
ANISOU 3103  CB  LEU A 267    10672  17557  12326  -1060    343   1642       C  
ATOM   3104  CG  LEU A 267       1.660  -8.492  28.665  1.00109.46           C  
ANISOU 3104  CG  LEU A 267    11022  17913  12654   -946    282   1399       C  
ATOM   3105  CD1 LEU A 267       1.563  -9.031  27.256  1.00108.97           C  
ANISOU 3105  CD1 LEU A 267    10962  17651  12791  -1131    247   1314       C  
ATOM   3106  CD2 LEU A 267       0.471  -7.587  28.945  1.00112.51           C  
ANISOU 3106  CD2 LEU A 267    11251  18666  12831   -819    325   1374       C  
ATOM   3107  N   GLU A 268       3.021 -10.937  32.736  1.00110.99           N  
ANISOU 3107  N   GLU A 268    11349  18131  12693   -938    426   2101       N  
ATOM   3108  CA  GLU A 268       3.070 -12.076  33.660  1.00112.86           C  
ANISOU 3108  CA  GLU A 268    11600  18351  12930  -1028    495   2381       C  
ATOM   3109  C   GLU A 268       2.859 -13.407  32.915  1.00118.01           C  
ANISOU 3109  C   GLU A 268    12271  18731  13836  -1326    516   2494       C  
ATOM   3110  O   GLU A 268       1.931 -14.157  33.222  1.00120.09           O  
ANISOU 3110  O   GLU A 268    12426  19095  14108  -1512    611   2707       O  
ATOM   3111  CB  GLU A 268       2.103 -11.907  34.861  1.00116.47           C  
ANISOU 3111  CB  GLU A 268    11903  19213  13138   -959    606   2570       C  
ATOM   3112  CG  GLU A 268       2.367 -10.695  35.740  1.00126.39           C  
ANISOU 3112  CG  GLU A 268    13163  20729  14130   -643    577   2460       C  
ATOM   3113  CD  GLU A 268       1.242 -10.370  36.706  1.00150.32           C  
ANISOU 3113  CD  GLU A 268    16014  24204  16896   -554    686   2596       C  
ATOM   3114  OE1 GLU A 268       0.529  -9.369  36.467  1.00142.34           O  
ANISOU 3114  OE1 GLU A 268    14899  23420  15764   -442    684   2441       O  
ATOM   3115  OE2 GLU A 268       1.078 -11.106  37.707  1.00148.48           O  
ANISOU 3115  OE2 GLU A 268    15747  24101  16567   -580    776   2864       O  
ATOM   3116  N   ILE A 269       3.718 -13.681  31.914  1.00113.29           N  
ANISOU 3116  N   ILE A 269    11810  17790  13445  -1374    425   2343       N  
ATOM   3117  CA  ILE A 269       3.686 -14.917  31.119  1.00114.03           C  
ANISOU 3117  CA  ILE A 269    11960  17576  13790  -1626    417   2400       C  
ATOM   3118  C   ILE A 269       4.834 -15.855  31.558  1.00119.59           C  
ANISOU 3118  C   ILE A 269    12854  17993  14592  -1598    388   2521       C  
ATOM   3119  O   ILE A 269       4.626 -17.066  31.658  1.00121.67           O  
ANISOU 3119  O   ILE A 269    13162  18078  14988  -1786    426   2713       O  
ATOM   3120  CB  ILE A 269       3.553 -14.659  29.577  1.00115.18           C  
ANISOU 3120  CB  ILE A 269    12095  17583  14085  -1715    347   2149       C  
ATOM   3121  CG1 ILE A 269       2.212 -13.940  29.267  1.00115.62           C  
ANISOU 3121  CG1 ILE A 269    11943  17953  14034  -1760    390   2089       C  
ATOM   3122  CG2 ILE A 269       3.665 -15.957  28.759  1.00116.47           C  
ANISOU 3122  CG2 ILE A 269    12344  17402  14507  -1948    317   2173       C  
ATOM   3123  CD1 ILE A 269       2.195 -13.013  28.063  1.00118.45           C  
ANISOU 3123  CD1 ILE A 269    12284  18313  14408  -1689    319   1814       C  
ATOM   3124  N   ILE A 270       6.016 -15.284  31.883  1.00114.81           N  
ANISOU 3124  N   ILE A 270    12353  17356  13913  -1361    321   2418       N  
ATOM   3125  CA  ILE A 270       7.179 -16.026  32.400  1.00115.24           C  
ANISOU 3125  CA  ILE A 270    12571  17197  14018  -1275    285   2521       C  
ATOM   3126  C   ILE A 270       7.562 -15.458  33.794  1.00119.47           C  
ANISOU 3126  C   ILE A 270    13098  17987  14307  -1040    300   2611       C  
ATOM   3127  O   ILE A 270       7.205 -14.316  34.100  1.00118.27           O  
ANISOU 3127  O   ILE A 270    12846  18116  13976   -916    304   2506       O  
ATOM   3128  CB  ILE A 270       8.394 -16.092  31.415  1.00116.56           C  
ANISOU 3128  CB  ILE A 270    12871  17066  14350  -1218    177   2311       C  
ATOM   3129  CG1 ILE A 270       7.978 -15.965  29.930  1.00115.57           C  
ANISOU 3129  CG1 ILE A 270    12710  16821  14379  -1365    146   2110       C  
ATOM   3130  CG2 ILE A 270       9.209 -17.374  31.650  1.00119.11           C  
ANISOU 3130  CG2 ILE A 270    13356  17099  14801  -1227    157   2460       C  
ATOM   3131  CD1 ILE A 270       9.049 -15.366  29.011  1.00119.57           C  
ANISOU 3131  CD1 ILE A 270    13284  17198  14949  -1244     53   1854       C  
ATOM   3132  N   LYS A 271       8.238 -16.265  34.647  1.00117.26           N  
ANISOU 3132  N   LYS A 271    12926  17617  14009   -970    305   2807       N  
ATOM   3133  CA  LYS A 271       8.661 -15.875  36.001  1.00117.55           C  
ANISOU 3133  CA  LYS A 271    12965  17894  13806   -739    311   2905       C  
ATOM   3134  C   LYS A 271      10.100 -16.310  36.286  1.00121.13           C  
ANISOU 3134  C   LYS A 271    13571  18159  14295   -579    225   2905       C  
ATOM   3135  O   LYS A 271      10.746 -15.779  37.190  1.00120.54           O  
ANISOU 3135  O   LYS A 271    13502  18265  14035   -354    184   2887       O  
ATOM   3136  CB  LYS A 271       7.708 -16.457  37.060  1.00122.62           C  
ANISOU 3136  CB  LYS A 271    13539  18737  14313   -804    440   3228       C  
ATOM   3137  CG  LYS A 271       6.399 -15.690  37.209  1.00134.03           C  
ANISOU 3137  CG  LYS A 271    14792  20526  15608   -849    522   3219       C  
ATOM   3138  CD  LYS A 271       5.249 -16.345  36.447  1.00142.35           C  
ANISOU 3138  CD  LYS A 271    15758  21499  16830  -1159    599   3309       C  
ATOM   3139  CE  LYS A 271       3.952 -15.604  36.651  1.00149.72           C  
ANISOU 3139  CE  LYS A 271    16479  22815  17594  -1183    684   3311       C  
ATOM   3140  NZ  LYS A 271       2.804 -16.320  36.037  1.00157.57           N  
ANISOU 3140  NZ  LYS A 271    17360  23769  18739  -1498    762   3425       N  
ATOM   3141  N   CYS A 274      12.517 -13.105  39.253  1.00135.90           N  
ANISOU 3141  N   CYS A 274    15384  20820  15433    297    -27   2512       N  
ATOM   3142  CA  CYS A 274      13.164 -11.816  39.485  1.00134.50           C  
ANISOU 3142  CA  CYS A 274    15178  20790  15136    473   -140   2241       C  
ATOM   3143  C   CYS A 274      14.619 -11.813  39.024  1.00136.57           C  
ANISOU 3143  C   CYS A 274    15505  20853  15532    529   -265   2077       C  
ATOM   3144  O   CYS A 274      15.096 -10.787  38.533  1.00134.05           O  
ANISOU 3144  O   CYS A 274    15163  20522  15249    552   -352   1812       O  
ATOM   3145  CB  CYS A 274      13.038 -11.391  40.945  1.00136.80           C  
ANISOU 3145  CB  CYS A 274    15430  21429  15119    692   -143   2307       C  
ATOM   3146  SG  CYS A 274      13.411  -9.643  41.246  1.00139.70           S  
ANISOU 3146  SG  CYS A 274    15753  22002  15325    879   -273   1953       S  
ATOM   3147  N   GLU A 275      15.326 -12.953  39.199  1.00134.20           N  
ANISOU 3147  N   GLU A 275    15285  20404  15301    555   -273   2241       N  
ATOM   3148  CA  GLU A 275      16.720 -13.134  38.780  1.00133.26           C  
ANISOU 3148  CA  GLU A 275    15216  20113  15305    622   -382   2115       C  
ATOM   3149  C   GLU A 275      16.775 -13.140  37.250  1.00134.02           C  
ANISOU 3149  C   GLU A 275    15324  19939  15660    439   -382   1967       C  
ATOM   3150  O   GLU A 275      17.648 -12.497  36.666  1.00131.90           O  
ANISOU 3150  O   GLU A 275    15034  19618  15466    465   -471   1741       O  
ATOM   3151  CB  GLU A 275      17.292 -14.444  39.356  1.00136.91           C  
ANISOU 3151  CB  GLU A 275    15771  20486  15765    713   -376   2358       C  
ATOM   3152  CG  GLU A 275      18.809 -14.469  39.470  1.00149.59           C  
ANISOU 3152  CG  GLU A 275    17394  22065  17377    886   -505   2240       C  
ATOM   3153  CD  GLU A 275      19.536 -15.246  38.390  1.00173.13           C  
ANISOU 3153  CD  GLU A 275    20443  24734  20604    822   -529   2205       C  
ATOM   3154  OE1 GLU A 275      20.085 -16.326  38.707  1.00170.01           O  
ANISOU 3154  OE1 GLU A 275    20139  24230  20226    923   -538   2376       O  
ATOM   3155  OE2 GLU A 275      19.581 -14.763  37.235  1.00165.17           O  
ANISOU 3155  OE2 GLU A 275    19402  23598  19758    690   -543   2005       O  
ATOM   3156  N   PHE A 276      15.799 -13.824  36.614  1.00130.13           N  
ANISOU 3156  N   PHE A 276    14854  19296  15293    249   -282   2094       N  
ATOM   3157  CA  PHE A 276      15.645 -13.914  35.163  1.00127.99           C  
ANISOU 3157  CA  PHE A 276    14594  18789  15248     72   -272   1970       C  
ATOM   3158  C   PHE A 276      15.195 -12.570  34.596  1.00129.19           C  
ANISOU 3158  C   PHE A 276    14660  19051  15377     26   -284   1746       C  
ATOM   3159  O   PHE A 276      15.552 -12.248  33.467  1.00127.42           O  
ANISOU 3159  O   PHE A 276    14435  18681  15298    -43   -318   1571       O  
ATOM   3160  CB  PHE A 276      14.644 -15.024  34.791  1.00130.88           C  
ANISOU 3160  CB  PHE A 276    15002  18994  15734   -119   -172   2170       C  
ATOM   3161  CG  PHE A 276      14.553 -15.358  33.318  1.00131.28           C  
ANISOU 3161  CG  PHE A 276    15081  18783  16017   -287   -174   2053       C  
ATOM   3162  CD1 PHE A 276      15.456 -16.237  32.730  1.00134.67           C  
ANISOU 3162  CD1 PHE A 276    15611  18948  16608   -272   -220   2039       C  
ATOM   3163  CD2 PHE A 276      13.535 -14.834  32.531  1.00132.39           C  
ANISOU 3163  CD2 PHE A 276    15146  18956  16201   -442   -130   1959       C  
ATOM   3164  CE1 PHE A 276      15.363 -16.556  31.371  1.00134.76           C  
ANISOU 3164  CE1 PHE A 276    15651  18736  16816   -409   -225   1919       C  
ATOM   3165  CE2 PHE A 276      13.441 -15.155  31.174  1.00134.40           C  
ANISOU 3165  CE2 PHE A 276    15424  18991  16650   -584   -138   1846       C  
ATOM   3166  CZ  PHE A 276      14.356 -16.014  30.603  1.00132.75           C  
ANISOU 3166  CZ  PHE A 276    15319  18523  16596   -568   -185   1822       C  
ATOM   3167  N   GLU A 277      14.429 -11.789  35.387  1.00125.28           N  
ANISOU 3167  N   GLU A 277    14097  18815  14689     83   -256   1757       N  
ATOM   3168  CA  GLU A 277      13.904 -10.474  35.010  1.00123.30           C  
ANISOU 3168  CA  GLU A 277    13780  18681  14387     74   -267   1561       C  
ATOM   3169  C   GLU A 277      15.028  -9.453  34.799  1.00124.95           C  
ANISOU 3169  C   GLU A 277    13995  18874  14607    171   -383   1314       C  
ATOM   3170  O   GLU A 277      15.074  -8.823  33.744  1.00123.16           O  
ANISOU 3170  O   GLU A 277    13761  18539  14495     91   -401   1147       O  
ATOM   3171  CB  GLU A 277      12.888  -9.971  36.055  1.00125.88           C  
ANISOU 3171  CB  GLU A 277    14042  19307  14481    156   -214   1640       C  
ATOM   3172  CG  GLU A 277      12.105  -8.741  35.624  1.00134.95           C  
ANISOU 3172  CG  GLU A 277    15131  20566  15577    150   -210   1465       C  
ATOM   3173  CD  GLU A 277      11.926  -7.695  36.706  1.00155.40           C  
ANISOU 3173  CD  GLU A 277    17689  23435  17920    345   -245   1385       C  
ATOM   3174  OE1 GLU A 277      10.808  -7.601  37.263  1.00149.56           O  
ANISOU 3174  OE1 GLU A 277    16882  22922  17021    376   -165   1487       O  
ATOM   3175  OE2 GLU A 277      12.899  -6.959  36.988  1.00147.55           O  
ANISOU 3175  OE2 GLU A 277    16731  22442  16888    467   -357   1211       O  
ATOM   3176  N   ASN A 278      15.928  -9.299  35.788  1.00121.72           N  
ANISOU 3176  N   ASN A 278    13593  18578  14078    336   -462   1296       N  
ATOM   3177  CA  ASN A 278      17.035  -8.346  35.698  1.00120.56           C  
ANISOU 3177  CA  ASN A 278    13435  18431  13941    411   -581   1065       C  
ATOM   3178  C   ASN A 278      18.145  -8.792  34.746  1.00122.31           C  
ANISOU 3178  C   ASN A 278    13674  18432  14365    349   -623   1000       C  
ATOM   3179  O   ASN A 278      18.812  -7.938  34.161  1.00120.69           O  
ANISOU 3179  O   ASN A 278    13446  18179  14233    327   -688    802       O  
ATOM   3180  CB  ASN A 278      17.587  -7.993  37.078  1.00124.48           C  
ANISOU 3180  CB  ASN A 278    13917  19150  14231    607   -665   1045       C  
ATOM   3181  CG  ASN A 278      18.033  -6.553  37.205  1.00153.54           C  
ANISOU 3181  CG  ASN A 278    17572  22911  17855    667   -773    782       C  
ATOM   3182  OD1 ASN A 278      17.350  -5.612  36.774  1.00148.03           O  
ANISOU 3182  OD1 ASN A 278    16873  22211  17159    617   -759    662       O  
ATOM   3183  ND2 ASN A 278      19.171  -6.343  37.847  1.00147.73           N  
ANISOU 3183  ND2 ASN A 278    16817  22252  17061    782   -891    687       N  
ATOM   3184  N   THR A 279      18.331 -10.119  34.575  1.00118.64           N  
ANISOU 3184  N   THR A 279    13254  17833  13991    324   -582   1168       N  
ATOM   3185  CA  THR A 279      19.338 -10.668  33.664  1.00117.45           C  
ANISOU 3185  CA  THR A 279    13123  17483  14020    292   -615   1115       C  
ATOM   3186  C   THR A 279      18.927 -10.495  32.188  1.00118.41           C  
ANISOU 3186  C   THR A 279    13245  17432  14312    124   -567   1019       C  
ATOM   3187  O   THR A 279      19.793 -10.425  31.319  1.00116.92           O  
ANISOU 3187  O   THR A 279    13045  17133  14248    104   -603    899       O  
ATOM   3188  CB  THR A 279      19.781 -12.080  34.092  1.00127.89           C  
ANISOU 3188  CB  THR A 279    14509  18721  15361    368   -607   1309       C  
ATOM   3189  OG1 THR A 279      21.138 -12.291  33.707  1.00128.70           O  
ANISOU 3189  OG1 THR A 279    14601  18748  15550    443   -684   1213       O  
ATOM   3190  CG2 THR A 279      18.896 -13.185  33.535  1.00126.72           C  
ANISOU 3190  CG2 THR A 279    14436  18382  15331    234   -510   1476       C  
ATOM   3191  N   VAL A 280      17.606 -10.423  31.919  1.00113.98           N  
ANISOU 3191  N   VAL A 280    12687  16876  13745     15   -486   1073       N  
ATOM   3192  CA  VAL A 280      17.030 -10.200  30.588  1.00111.93           C  
ANISOU 3192  CA  VAL A 280    12422  16494  13613   -131   -442    986       C  
ATOM   3193  C   VAL A 280      17.257  -8.720  30.217  1.00113.54           C  
ANISOU 3193  C   VAL A 280    12583  16766  13791   -120   -486    782       C  
ATOM   3194  O   VAL A 280      17.650  -8.425  29.086  1.00111.99           O  
ANISOU 3194  O   VAL A 280    12382  16453  13714   -185   -493    664       O  
ATOM   3195  CB  VAL A 280      15.538 -10.656  30.537  1.00116.03           C  
ANISOU 3195  CB  VAL A 280    12939  17029  14119   -245   -349   1120       C  
ATOM   3196  CG1 VAL A 280      14.684  -9.794  29.611  1.00114.59           C  
ANISOU 3196  CG1 VAL A 280    12714  16868  13958   -337   -319    998       C  
ATOM   3197  CG2 VAL A 280      15.433 -12.129  30.151  1.00116.63           C  
ANISOU 3197  CG2 VAL A 280    13076  16910  14329   -335   -311   1262       C  
ATOM   3198  N   HIS A 281      17.067  -7.811  31.203  1.00109.75           N  
ANISOU 3198  N   HIS A 281    12080  16470  13151    -27   -520    742       N  
ATOM   3199  CA  HIS A 281      17.283  -6.364  31.108  1.00108.72           C  
ANISOU 3199  CA  HIS A 281    11932  16395  12981      0   -577    554       C  
ATOM   3200  C   HIS A 281      18.724  -6.084  30.640  1.00109.86           C  
ANISOU 3200  C   HIS A 281    12062  16448  13232     -3   -652    425       C  
ATOM   3201  O   HIS A 281      18.938  -5.179  29.831  1.00108.14           O  
ANISOU 3201  O   HIS A 281    11840  16164  13086    -64   -667    289       O  
ATOM   3202  CB  HIS A 281      17.035  -5.728  32.488  1.00111.20           C  
ANISOU 3202  CB  HIS A 281    12237  16921  13091    136   -620    543       C  
ATOM   3203  CG  HIS A 281      17.019  -4.229  32.506  1.00114.79           C  
ANISOU 3203  CG  HIS A 281    12699  17424  13493    172   -680    351       C  
ATOM   3204  ND1 HIS A 281      15.852  -3.527  32.757  1.00116.97           N  
ANISOU 3204  ND1 HIS A 281    12983  17813  13647    215   -647    332       N  
ATOM   3205  CD2 HIS A 281      18.035  -3.345  32.348  1.00116.68           C  
ANISOU 3205  CD2 HIS A 281    12940  17608  13784    173   -773    177       C  
ATOM   3206  CE1 HIS A 281      16.192  -2.249  32.725  1.00116.42           C  
ANISOU 3206  CE1 HIS A 281    12944  17727  13565    251   -725    143       C  
ATOM   3207  NE2 HIS A 281      17.491  -2.090  32.476  1.00116.59           N  
ANISOU 3207  NE2 HIS A 281    12961  17640  13696    210   -802     48       N  
ATOM   3208  N   LYS A 282      19.696  -6.888  31.141  1.00105.91           N  
ANISOU 3208  N   LYS A 282    11549  15952  12740     67   -695    482       N  
ATOM   3209  CA  LYS A 282      21.127  -6.852  30.819  1.00104.91           C  
ANISOU 3209  CA  LYS A 282    11380  15778  12702     82   -765    386       C  
ATOM   3210  C   LYS A 282      21.337  -7.053  29.306  1.00105.16           C  
ANISOU 3210  C   LYS A 282    11409  15640  12907    -32   -715    345       C  
ATOM   3211  O   LYS A 282      22.037  -6.258  28.678  1.00103.68           O  
ANISOU 3211  O   LYS A 282    11179  15428  12787    -81   -746    212       O  
ATOM   3212  CB  LYS A 282      21.870  -7.934  31.647  1.00108.77           C  
ANISOU 3212  CB  LYS A 282    11863  16315  13148    205   -803    498       C  
ATOM   3213  CG  LYS A 282      23.347  -8.135  31.314  1.00122.76           C  
ANISOU 3213  CG  LYS A 282    13573  18063  15006    243   -869    421       C  
ATOM   3214  CD  LYS A 282      23.628  -9.481  30.624  1.00131.55           C  
ANISOU 3214  CD  LYS A 282    14723  19027  16234    252   -822    525       C  
ATOM   3215  CE  LYS A 282      24.134  -9.306  29.205  1.00137.77           C  
ANISOU 3215  CE  LYS A 282    15472  19699  17174    159   -798    415       C  
ATOM   3216  NZ  LYS A 282      25.005 -10.434  28.773  1.00144.07           N  
ANISOU 3216  NZ  LYS A 282    16270  20416  18053    239   -803    454       N  
ATOM   3217  N   TRP A 283      20.729  -8.115  28.737  1.00100.41           N  
ANISOU 3217  N   TRP A 283    10854  14926  12371    -77   -641    458       N  
ATOM   3218  CA  TRP A 283      20.814  -8.430  27.312  1.00 98.93           C  
ANISOU 3218  CA  TRP A 283    10673  14590  12327   -166   -595    418       C  
ATOM   3219  C   TRP A 283      20.177  -7.335  26.453  1.00 98.32           C  
ANISOU 3219  C   TRP A 283    10590  14501  12267   -263   -561    319       C  
ATOM   3220  O   TRP A 283      20.727  -7.015  25.401  1.00 97.55           O  
ANISOU 3220  O   TRP A 283    10468  14339  12258   -311   -552    231       O  
ATOM   3221  CB  TRP A 283      20.230  -9.817  27.004  1.00 98.70           C  
ANISOU 3221  CB  TRP A 283    10706  14436  12358   -193   -539    548       C  
ATOM   3222  CG  TRP A 283      21.076 -10.950  27.505  1.00101.47           C  
ANISOU 3222  CG  TRP A 283    11083  14741  12729    -89   -573    635       C  
ATOM   3223  CD1 TRP A 283      20.917 -11.635  28.672  1.00105.83           C  
ANISOU 3223  CD1 TRP A 283    11676  15334  13200     -9   -582    785       C  
ATOM   3224  CD2 TRP A 283      22.221 -11.521  26.857  1.00101.83           C  
ANISOU 3224  CD2 TRP A 283    11118  14702  12869    -31   -600    583       C  
ATOM   3225  NE1 TRP A 283      21.893 -12.597  28.796  1.00106.56           N  
ANISOU 3225  NE1 TRP A 283    11797  15357  13336    100   -619    833       N  
ATOM   3226  CE2 TRP A 283      22.706 -12.551  27.694  1.00107.47           C  
ANISOU 3226  CE2 TRP A 283    11877  15399  13559     95   -632    703       C  
ATOM   3227  CE3 TRP A 283      22.886 -11.265  25.645  1.00102.61           C  
ANISOU 3227  CE3 TRP A 283    11171  14754  13061    -59   -595    455       C  
ATOM   3228  CZ2 TRP A 283      23.828 -13.322  27.361  1.00107.71           C  
ANISOU 3228  CZ2 TRP A 283    11908  15362  13654    206   -667    685       C  
ATOM   3229  CZ3 TRP A 283      23.999 -12.027  25.317  1.00104.89           C  
ANISOU 3229  CZ3 TRP A 283    11448  14997  13410     43   -623    436       C  
ATOM   3230  CH2 TRP A 283      24.458 -13.042  26.166  1.00107.10           C  
ANISOU 3230  CH2 TRP A 283    11774  15256  13665    180   -662    543       C  
ATOM   3231  N   ILE A 284      19.066  -6.719  26.928  1.00 91.65           N  
ANISOU 3231  N   ILE A 284     9764  13735  11324   -273   -541    335       N  
ATOM   3232  CA  ILE A 284      18.388  -5.603  26.255  1.00 88.98           C  
ANISOU 3232  CA  ILE A 284     9432  13398  10978   -330   -516    247       C  
ATOM   3233  C   ILE A 284      19.349  -4.409  26.106  1.00 89.64           C  
ANISOU 3233  C   ILE A 284     9496  13480  11083   -329   -574    110       C  
ATOM   3234  O   ILE A 284      19.386  -3.798  25.040  1.00 88.76           O  
ANISOU 3234  O   ILE A 284     9390  13297  11039   -395   -548     44       O  
ATOM   3235  CB  ILE A 284      17.025  -5.261  26.942  1.00 92.00           C  
ANISOU 3235  CB  ILE A 284     9830  13895  11231   -305   -489    296       C  
ATOM   3236  CG1 ILE A 284      15.871  -6.038  26.288  1.00 91.78           C  
ANISOU 3236  CG1 ILE A 284     9803  13833  11234   -383   -410    384       C  
ATOM   3237  CG2 ILE A 284      16.708  -3.759  26.987  1.00 92.25           C  
ANISOU 3237  CG2 ILE A 284     9879  13981  11193   -276   -515    179       C  
ATOM   3238  CD1 ILE A 284      15.161  -6.923  27.218  1.00 97.07           C  
ANISOU 3238  CD1 ILE A 284    10467  14582  11834   -372   -379    535       C  
ATOM   3239  N   SER A 285      20.161  -4.128  27.150  1.00 84.53           N  
ANISOU 3239  N   SER A 285     8823  12913  10383   -261   -654     73       N  
ATOM   3240  CA  SER A 285      21.158  -3.054  27.137  1.00 83.39           C  
ANISOU 3240  CA  SER A 285     8648  12767  10271   -282   -724    -60       C  
ATOM   3241  C   SER A 285      22.228  -3.307  26.073  1.00 83.22           C  
ANISOU 3241  C   SER A 285     8569  12666  10386   -351   -708    -87       C  
ATOM   3242  O   SER A 285      22.543  -2.394  25.306  1.00 82.10           O  
ANISOU 3242  O   SER A 285     8419  12467  10309   -433   -701   -164       O  
ATOM   3243  CB  SER A 285      21.805  -2.890  28.511  1.00 88.56           C  
ANISOU 3243  CB  SER A 285     9271  13545  10833   -191   -825    -98       C  
ATOM   3244  OG  SER A 285      20.992  -2.121  29.380  1.00 98.45           O  
ANISOU 3244  OG  SER A 285    10574  14879  11954   -129   -856   -136       O  
ATOM   3245  N   ILE A 286      22.746  -4.554  25.995  1.00 77.60           N  
ANISOU 3245  N   ILE A 286     7823  11949   9713   -310   -696    -14       N  
ATOM   3246  CA  ILE A 286      23.773  -4.916  25.014  1.00 76.42           C  
ANISOU 3246  CA  ILE A 286     7609  11753   9674   -342   -677    -40       C  
ATOM   3247  C   ILE A 286      23.261  -5.067  23.570  1.00 76.85           C  
ANISOU 3247  C   ILE A 286     7694  11704   9802   -413   -587    -31       C  
ATOM   3248  O   ILE A 286      23.960  -4.661  22.640  1.00 75.76           O  
ANISOU 3248  O   ILE A 286     7504  11549   9733   -468   -564    -84       O  
ATOM   3249  CB  ILE A 286      24.762  -6.030  25.472  1.00 80.34           C  
ANISOU 3249  CB  ILE A 286     8051  12295  10179   -240   -717      2       C  
ATOM   3250  CG1 ILE A 286      24.144  -7.439  25.448  1.00 80.67           C  
ANISOU 3250  CG1 ILE A 286     8167  12261  10223   -181   -673    123       C  
ATOM   3251  CG2 ILE A 286      25.408  -5.703  26.831  1.00 81.96           C  
ANISOU 3251  CG2 ILE A 286     8206  12635  10301   -165   -820    -30       C  
ATOM   3252  CD1 ILE A 286      25.146  -8.529  25.052  1.00 86.58           C  
ANISOU 3252  CD1 ILE A 286     8881  12979  11038    -99   -679    141       C  
ATOM   3253  N   THR A 287      22.043  -5.626  23.389  1.00 71.26           N  
ANISOU 3253  N   THR A 287     7060  10946   9070   -417   -536     37       N  
ATOM   3254  CA  THR A 287      21.439  -5.820  22.069  1.00 69.52           C  
ANISOU 3254  CA  THR A 287     6867  10646   8900   -474   -463     35       C  
ATOM   3255  C   THR A 287      21.040  -4.505  21.424  1.00 71.76           C  
ANISOU 3255  C   THR A 287     7165  10928   9174   -539   -436    -24       C  
ATOM   3256  O   THR A 287      21.098  -4.401  20.199  1.00 71.14           O  
ANISOU 3256  O   THR A 287     7081  10808   9142   -578   -385    -49       O  
ATOM   3257  CB  THR A 287      20.284  -6.823  22.094  1.00 75.59           C  
ANISOU 3257  CB  THR A 287     7695  11370   9655   -476   -429    116       C  
ATOM   3258  OG1 THR A 287      19.319  -6.422  23.064  1.00 74.87           O  
ANISOU 3258  OG1 THR A 287     7630  11348   9469   -470   -437    160       O  
ATOM   3259  CG2 THR A 287      20.752  -8.254  22.338  1.00 74.02           C  
ANISOU 3259  CG2 THR A 287     7508  11113   9502   -420   -442    180       C  
ATOM   3260  N   GLU A 288      20.647  -3.502  22.235  1.00 67.51           N  
ANISOU 3260  N   GLU A 288     6653  10433   8566   -535   -473    -48       N  
ATOM   3261  CA  GLU A 288      20.288  -2.165  21.756  1.00 66.85           C  
ANISOU 3261  CA  GLU A 288     6607  10323   8469   -578   -460   -103       C  
ATOM   3262  C   GLU A 288      21.552  -1.480  21.227  1.00 70.68           C  
ANISOU 3262  C   GLU A 288     7044  10777   9035   -640   -470   -159       C  
ATOM   3263  O   GLU A 288      21.496  -0.761  20.229  1.00 69.75           O  
ANISOU 3263  O   GLU A 288     6947  10607   8949   -694   -424   -172       O  
ATOM   3264  CB  GLU A 288      19.671  -1.338  22.892  1.00 68.58           C  
ANISOU 3264  CB  GLU A 288     6874  10592   8590   -531   -512   -130       C  
ATOM   3265  CG  GLU A 288      18.987  -0.063  22.433  1.00 80.06           C  
ANISOU 3265  CG  GLU A 288     8399  12003  10016   -543   -497   -176       C  
ATOM   3266  CD  GLU A 288      19.027   1.112  23.393  1.00106.04           C  
ANISOU 3266  CD  GLU A 288    11741  15300  13250   -506   -573   -256       C  
ATOM   3267  OE1 GLU A 288      18.195   2.030  23.216  1.00106.54           O  
ANISOU 3267  OE1 GLU A 288    11884  15334  13262   -473   -565   -285       O  
ATOM   3268  OE2 GLU A 288      19.903   1.143  24.288  1.00100.37           O  
ANISOU 3268  OE2 GLU A 288    10986  14615  12535   -500   -649   -301       O  
ATOM   3269  N   ALA A 289      22.692  -1.731  21.897  1.00 68.08           N  
ANISOU 3269  N   ALA A 289     6639  10494   8733   -630   -529   -181       N  
ATOM   3270  CA  ALA A 289      23.996  -1.194  21.530  1.00 68.51           C  
ANISOU 3270  CA  ALA A 289     6611  10554   8867   -701   -544   -230       C  
ATOM   3271  C   ALA A 289      24.604  -1.976  20.370  1.00 71.44           C  
ANISOU 3271  C   ALA A 289     6912  10930   9301   -708   -475   -198       C  
ATOM   3272  O   ALA A 289      25.272  -1.374  19.541  1.00 71.24           O  
ANISOU 3272  O   ALA A 289     6836  10900   9334   -786   -438   -213       O  
ATOM   3273  CB  ALA A 289      24.922  -1.202  22.728  1.00 70.30           C  
ANISOU 3273  CB  ALA A 289     6764  10863   9082   -674   -644   -276       C  
ATOM   3274  N   LEU A 290      24.355  -3.299  20.284  1.00 67.39           N  
ANISOU 3274  N   LEU A 290     6405  10422   8778   -627   -455   -153       N  
ATOM   3275  CA  LEU A 290      24.841  -4.103  19.158  1.00 67.27           C  
ANISOU 3275  CA  LEU A 290     6343  10406   8810   -605   -395   -143       C  
ATOM   3276  C   LEU A 290      24.024  -3.783  17.901  1.00 71.95           C  
ANISOU 3276  C   LEU A 290     6993  10945   9399   -647   -314   -136       C  
ATOM   3277  O   LEU A 290      24.552  -3.884  16.796  1.00 71.94           O  
ANISOU 3277  O   LEU A 290     6943  10964   9426   -654   -257   -144       O  
ATOM   3278  CB  LEU A 290      24.805  -5.609  19.466  1.00 67.30           C  
ANISOU 3278  CB  LEU A 290     6362  10397   8812   -500   -411   -108       C  
ATOM   3279  CG  LEU A 290      25.989  -6.156  20.271  1.00 73.01           C  
ANISOU 3279  CG  LEU A 290     7001  11195   9545   -420   -475   -112       C  
ATOM   3280  CD1 LEU A 290      25.573  -7.347  21.110  1.00 73.33           C  
ANISOU 3280  CD1 LEU A 290     7111  11196   9557   -321   -510    -48       C  
ATOM   3281  CD2 LEU A 290      27.180  -6.504  19.369  1.00 75.52           C  
ANISOU 3281  CD2 LEU A 290     7210  11571   9912   -385   -445   -146       C  
ATOM   3282  N   ALA A 291      22.744  -3.375  18.082  1.00 68.92           N  
ANISOU 3282  N   ALA A 291     6703  10518   8964   -662   -310   -121       N  
ATOM   3283  CA  ALA A 291      21.821  -2.992  17.015  1.00 68.69           C  
ANISOU 3283  CA  ALA A 291     6732  10458   8910   -684   -247   -115       C  
ATOM   3284  C   ALA A 291      22.221  -1.662  16.387  1.00 74.86           C  
ANISOU 3284  C   ALA A 291     7510  11229   9703   -750   -214   -123       C  
ATOM   3285  O   ALA A 291      21.886  -1.421  15.227  1.00 74.57           O  
ANISOU 3285  O   ALA A 291     7496  11187   9651   -757   -149   -109       O  
ATOM   3286  CB  ALA A 291      20.405  -2.901  17.553  1.00 68.83           C  
ANISOU 3286  CB  ALA A 291     6828  10464   8859   -668   -262    -97       C  
ATOM   3287  N   PHE A 292      22.945  -0.806  17.145  1.00 73.47           N  
ANISOU 3287  N   PHE A 292     7311  11049   9557   -802   -263   -143       N  
ATOM   3288  CA  PHE A 292      23.439   0.498  16.688  1.00 74.84           C  
ANISOU 3288  CA  PHE A 292     7486  11182   9765   -894   -240   -143       C  
ATOM   3289  C   PHE A 292      24.414   0.385  15.522  1.00 80.62           C  
ANISOU 3289  C   PHE A 292     8125  11961  10546   -937   -165   -114       C  
ATOM   3290  O   PHE A 292      24.643   1.378  14.834  1.00 80.71           O  
ANISOU 3290  O   PHE A 292     8150  11936  10580  -1016   -116    -81       O  
ATOM   3291  CB  PHE A 292      24.085   1.286  17.841  1.00 77.83           C  
ANISOU 3291  CB  PHE A 292     7849  11545  10178   -952   -328   -192       C  
ATOM   3292  CG  PHE A 292      23.133   1.884  18.850  1.00 79.75           C  
ANISOU 3292  CG  PHE A 292     8202  11739  10359   -912   -395   -229       C  
ATOM   3293  CD1 PHE A 292      21.785   2.052  18.548  1.00 82.58           C  
ANISOU 3293  CD1 PHE A 292     8668  12065  10645   -850   -361   -205       C  
ATOM   3294  CD2 PHE A 292      23.591   2.324  20.087  1.00 82.97           C  
ANISOU 3294  CD2 PHE A 292     8599  12156  10770   -925   -495   -296       C  
ATOM   3295  CE1 PHE A 292      20.907   2.603  19.481  1.00 83.62           C  
ANISOU 3295  CE1 PHE A 292     8888  12180  10703   -791   -418   -241       C  
ATOM   3296  CE2 PHE A 292      22.712   2.891  21.015  1.00 85.84           C  
ANISOU 3296  CE2 PHE A 292     9065  12493  11056   -864   -556   -341       C  
ATOM   3297  CZ  PHE A 292      21.379   3.031  20.703  1.00 83.27           C  
ANISOU 3297  CZ  PHE A 292     8842  12141  10656   -793   -513   -310       C  
ATOM   3298  N   PHE A 293      24.957  -0.830  15.282  1.00 78.70           N  
ANISOU 3298  N   PHE A 293     7795  11797  10312   -875   -151   -120       N  
ATOM   3299  CA  PHE A 293      25.880  -1.152  14.194  1.00 79.84           C  
ANISOU 3299  CA  PHE A 293     7834  12022  10478   -875    -78   -103       C  
ATOM   3300  C   PHE A 293      25.278  -0.856  12.811  1.00 84.58           C  
ANISOU 3300  C   PHE A 293     8489  12615  11031   -868     17    -62       C  
ATOM   3301  O   PHE A 293      26.033  -0.725  11.844  1.00 84.99           O  
ANISOU 3301  O   PHE A 293     8460  12745  11088   -887     93    -30       O  
ATOM   3302  CB  PHE A 293      26.323  -2.620  14.284  1.00 81.89           C  
ANISOU 3302  CB  PHE A 293     8029  12348  10738   -763    -96   -133       C  
ATOM   3303  CG  PHE A 293      27.814  -2.820  14.168  1.00 85.36           C  
ANISOU 3303  CG  PHE A 293     8306  12909  11219   -762    -86   -142       C  
ATOM   3304  CD1 PHE A 293      28.433  -2.856  12.921  1.00 89.73           C  
ANISOU 3304  CD1 PHE A 293     8773  13556  11762   -753      6   -123       C  
ATOM   3305  CD2 PHE A 293      28.600  -2.988  15.303  1.00 88.46           C  
ANISOU 3305  CD2 PHE A 293     8618  13350  11644   -757   -169   -170       C  
ATOM   3306  CE1 PHE A 293      29.815  -3.048  12.814  1.00 92.10           C  
ANISOU 3306  CE1 PHE A 293     8898  14004  12090   -744     21   -129       C  
ATOM   3307  CE2 PHE A 293      29.982  -3.188  15.196  1.00 92.69           C  
ANISOU 3307  CE2 PHE A 293     8979  14028  12209   -747   -164   -183       C  
ATOM   3308  CZ  PHE A 293      30.580  -3.213  13.952  1.00 91.77           C  
ANISOU 3308  CZ  PHE A 293     8768  14011  12088   -743    -66   -161       C  
ATOM   3309  N   HIS A 294      23.927  -0.704  12.733  1.00 81.07           N  
ANISOU 3309  N   HIS A 294     8171  12102  10531   -835     13    -60       N  
ATOM   3310  CA  HIS A 294      23.178  -0.377  11.514  1.00 81.45           C  
ANISOU 3310  CA  HIS A 294     8282  12153  10514   -809     86    -27       C  
ATOM   3311  C   HIS A 294      23.624   0.964  10.917  1.00 88.23           C  
ANISOU 3311  C   HIS A 294     9148  12991  11384   -895    149     45       C  
ATOM   3312  O   HIS A 294      23.438   1.193   9.721  1.00 88.38           O  
ANISOU 3312  O   HIS A 294     9184  13050  11347   -868    230     94       O  
ATOM   3313  CB  HIS A 294      21.654  -0.392  11.772  1.00 81.23           C  
ANISOU 3313  CB  HIS A 294     8366  12074  10423   -759     52    -43       C  
ATOM   3314  CG  HIS A 294      21.120   0.841  12.447  1.00 84.57           C  
ANISOU 3314  CG  HIS A 294     8878  12416  10838   -798     20    -24       C  
ATOM   3315  ND1 HIS A 294      20.866   1.072  13.756  1.00 86.06           N  
ANISOU 3315  ND1 HIS A 294     9101  12560  11038   -807    -57    -53       N  
ATOM   3316  CD2 HIS A 294      20.773   1.972  11.723  1.00 86.60           C  
ANISOU 3316  CD2 HIS A 294     9211  12633  11059   -808     69     28       C  
ATOM   3317  CE1 HIS A 294      20.384   2.361  13.846  1.00 85.67           C  
ANISOU 3317  CE1 HIS A 294     9150  12435  10966   -820    -63    -36       C  
ATOM   3318  NE2 HIS A 294      20.350   2.854  12.613  1.00 86.34           N  
ANISOU 3318  NE2 HIS A 294     9262  12515  11028   -823     14     18       N  
ATOM   3319  N   CYS A 295      24.181   1.855  11.762  1.00 86.84           N  
ANISOU 3319  N   CYS A 295     8970  12748  11278   -999    106     53       N  
ATOM   3320  CA  CYS A 295      24.679   3.171  11.366  1.00 88.83           C  
ANISOU 3320  CA  CYS A 295     9240  12940  11571  -1115    153    126       C  
ATOM   3321  C   CYS A 295      25.909   3.005  10.481  1.00 95.42           C  
ANISOU 3321  C   CYS A 295     9928  13894  12434  -1169    240    181       C  
ATOM   3322  O   CYS A 295      25.955   3.583   9.396  1.00 95.90           O  
ANISOU 3322  O   CYS A 295    10006  13967  12464  -1193    338    273       O  
ATOM   3323  CB  CYS A 295      24.966   4.037  12.589  1.00 89.89           C  
ANISOU 3323  CB  CYS A 295     9406  12965  11782  -1216     62     89       C  
ATOM   3324  SG  CYS A 295      23.522   4.323  13.642  1.00 92.75           S  
ANISOU 3324  SG  CYS A 295     9935  13220  12086  -1127    -33     24       S  
ATOM   3325  N   CYS A 296      26.883   2.226  10.940  1.00 93.61           N  
ANISOU 3325  N   CYS A 296     9553  13765  12251  -1172    210    132       N  
ATOM   3326  CA  CYS A 296      28.107   2.000  10.181  1.00 95.45           C  
ANISOU 3326  CA  CYS A 296     9617  14149  12500  -1205    291    175       C  
ATOM   3327  C   CYS A 296      27.986   0.776   9.279  1.00 99.61           C  
ANISOU 3327  C   CYS A 296    10104  14804  12941  -1042    345    151       C  
ATOM   3328  O   CYS A 296      28.834  -0.116   9.309  1.00100.28           O  
ANISOU 3328  O   CYS A 296    10054  15015  13032   -981    342    108       O  
ATOM   3329  CB  CYS A 296      29.301   1.840  11.125  1.00 96.68           C  
ANISOU 3329  CB  CYS A 296     9619  14374  12742  -1277    225    127       C  
ATOM   3330  SG  CYS A 296      28.987   0.776  12.553  1.00 99.30           S  
ANISOU 3330  SG  CYS A 296     9972  14685  13073  -1162     85      8       S  
ATOM   3331  N   LEU A 297      26.927   0.741   8.476  1.00 95.34           N  
ANISOU 3331  N   LEU A 297     9681  14232  12312   -962    386    168       N  
ATOM   3332  CA  LEU A 297      26.698  -0.366   7.555  1.00 95.08           C  
ANISOU 3332  CA  LEU A 297     9629  14306  12192   -809    425    124       C  
ATOM   3333  C   LEU A 297      26.391   0.150   6.154  1.00 98.50           C  
ANISOU 3333  C   LEU A 297    10095  14804  12526   -779    535    204       C  
ATOM   3334  O   LEU A 297      26.807  -0.442   5.157  1.00 98.88           O  
ANISOU 3334  O   LEU A 297    10065  15004  12500   -683    605    197       O  
ATOM   3335  CB  LEU A 297      25.553  -1.250   8.053  1.00 94.03           C  
ANISOU 3335  CB  LEU A 297     9603  14089  12036   -714    338     32       C  
ATOM   3336  CG  LEU A 297      25.269  -2.514   7.239  1.00 99.34           C  
ANISOU 3336  CG  LEU A 297    10272  14835  12638   -567    348    -45       C  
ATOM   3337  CD1 LEU A 297      25.961  -3.719   7.858  1.00 99.94           C  
ANISOU 3337  CD1 LEU A 297    10277  14928  12767   -500    289   -122       C  
ATOM   3338  CD2 LEU A 297      23.771  -2.753   7.122  1.00100.86           C  
ANISOU 3338  CD2 LEU A 297    10594  14951  12777   -521    307    -87       C  
ATOM   3339  N   ASN A 298      25.661   1.258   6.087  1.00 93.76           N  
ANISOU 3339  N   ASN A 298     9616  14096  11914   -841    548    278       N  
ATOM   3340  CA  ASN A 298      25.303   1.873   4.811  1.00 93.70           C  
ANISOU 3340  CA  ASN A 298     9659  14140  11802   -805    651    376       C  
ATOM   3341  C   ASN A 298      26.695   2.183   4.210  1.00 97.74           C  
ANISOU 3341  C   ASN A 298    10020  14786  12332   -881    759    474       C  
ATOM   3342  O   ASN A 298      26.932   1.719   3.097  1.00 97.95           O  
ANISOU 3342  O   ASN A 298     9982  14984  12253   -777    844    491       O  
ATOM   3343  CB  ASN A 298      24.426   3.132   4.985  1.00 93.43           C  
ANISOU 3343  CB  ASN A 298     9787  13946  11767   -860    641    453       C  
ATOM   3344  CG  ASN A 298      24.297   4.036   3.773  1.00109.96           C  
ANISOU 3344  CG  ASN A 298    11937  16073  13771   -847    755    598       C  
ATOM   3345  OD1 ASN A 298      24.425   3.624   2.614  1.00103.36           O  
ANISOU 3345  OD1 ASN A 298    11048  15404  12822   -749    840    628       O  
ATOM   3346  ND2 ASN A 298      24.015   5.306   4.026  1.00100.37           N  
ANISOU 3346  ND2 ASN A 298    10845  14694  12596   -933    757    694       N  
ATOM   3347  N   PRO A 299      27.670   2.802   4.942  1.00 94.41           N  
ANISOU 3347  N   PRO A 299     9515  14320  12035  -1050    751    520       N  
ATOM   3348  CA  PRO A 299      29.012   3.001   4.355  1.00 96.04           C  
ANISOU 3348  CA  PRO A 299     9541  14692  12256  -1131    858    614       C  
ATOM   3349  C   PRO A 299      29.774   1.692   4.099  1.00 99.10           C  
ANISOU 3349  C   PRO A 299     9758  15295  12600  -1000    870    523       C  
ATOM   3350  O   PRO A 299      30.560   1.624   3.153  1.00100.21           O  
ANISOU 3350  O   PRO A 299     9763  15636  12675   -975    986    595       O  
ATOM   3351  CB  PRO A 299      29.727   3.874   5.395  1.00 98.58           C  
ANISOU 3351  CB  PRO A 299     9819  14900  12736  -1349    808    643       C  
ATOM   3352  CG  PRO A 299      28.635   4.472   6.219  1.00101.66           C  
ANISOU 3352  CG  PRO A 299    10413  15047  13167  -1374    706    605       C  
ATOM   3353  CD  PRO A 299      27.614   3.395   6.293  1.00 95.33           C  
ANISOU 3353  CD  PRO A 299     9688  14256  12277  -1179    645    486       C  
ATOM   3354  N   ILE A 300      29.531   0.661   4.941  1.00 93.53           N  
ANISOU 3354  N   ILE A 300     9066  14548  11924   -907    753    374       N  
ATOM   3355  CA  ILE A 300      30.132  -0.678   4.849  1.00 93.17           C  
ANISOU 3355  CA  ILE A 300     8900  14654  11845   -754    737    268       C  
ATOM   3356  C   ILE A 300      29.673  -1.357   3.539  1.00 97.05           C  
ANISOU 3356  C   ILE A 300     9425  15262  12187   -569    803    237       C  
ATOM   3357  O   ILE A 300      30.457  -2.086   2.927  1.00 97.72           O  
ANISOU 3357  O   ILE A 300     9380  15541  12210   -449    854    201       O  
ATOM   3358  CB  ILE A 300      29.850  -1.522   6.147  1.00 94.72           C  
ANISOU 3358  CB  ILE A 300     9144  14730  12116   -710    590    139       C  
ATOM   3359  N   LEU A 301      28.437  -1.062   3.077  1.00 93.02           N  
ANISOU 3359  N   LEU A 301     9078  14656  11608   -537    802    248       N  
ATOM   3360  CA  LEU A 301      27.921  -1.611   1.821  1.00 93.46           C  
ANISOU 3360  CA  LEU A 301     9171  14829  11511   -366    852    208       C  
ATOM   3361  C   LEU A 301      28.648  -1.434   0.477  1.00100.40           C  
ANISOU 3361  C   LEU A 301     9937  15950  12260   -295    998    292       C  
ATOM   3362  O   LEU A 301      28.435  -2.171  -0.491  1.00100.93           O  
ANISOU 3362  O   LEU A 301    10005  16152  12191   -114   1023    214       O  
ATOM   3363  CB  LEU A 301      26.409  -1.901   1.856  1.00 91.97           C  
ANISOU 3363  CB  LEU A 301     9156  14504  11282   -302    768    124       C  
ATOM   3364  CG  LEU A 301      25.959  -3.227   2.482  1.00 95.56           C  
ANISOU 3364  CG  LEU A 301     9653  14874  11781   -216    645    -45       C  
ATOM   3365  CD1 LEU A 301      24.495  -3.438   2.246  1.00 94.86           C  
ANISOU 3365  CD1 LEU A 301     9702  14705  11634   -167    587   -112       C  
ATOM   3366  CD2 LEU A 301      26.716  -4.427   1.908  1.00 98.72           C  
ANISOU 3366  CD2 LEU A 301     9961  15416  12132    -57    656   -152       C  
ATOM   3367  N   TYR A 302      29.513  -0.420   0.452  1.00 98.61           N  
ANISOU 3367  N   TYR A 302     9610  15779  12077   -448   1093    453       N  
ATOM   3368  CA  TYR A 302      30.393  -0.024  -0.641  1.00100.69           C  
ANISOU 3368  CA  TYR A 302     9735  16282  12242   -439   1252    586       C  
ATOM   3369  C   TYR A 302      31.708  -0.819  -0.746  1.00105.58           C  
ANISOU 3369  C   TYR A 302    10130  17136  12848   -363   1292    536       C  
ATOM   3370  O   TYR A 302      32.807  -0.264  -0.670  1.00106.75           O  
ANISOU 3370  O   TYR A 302    10105  17404  13049   -497   1374    653       O  
ATOM   3371  CB  TYR A 302      30.609   1.477  -0.343  1.00102.76           C  
ANISOU 3371  CB  TYR A 302    10014  16428  12602   -686   1310    782       C  
ATOM   3372  CG  TYR A 302      29.367   2.318  -0.558  1.00104.18           C  
ANISOU 3372  CG  TYR A 302    10411  16425  12746   -707   1301    855       C  
ATOM   3373  CD1 TYR A 302      28.992   2.730  -1.834  1.00107.58           C  
ANISOU 3373  CD1 TYR A 302    10894  16967  13013   -618   1416    973       C  
ATOM   3374  CD2 TYR A 302      28.575   2.716   0.514  1.00103.23           C  
ANISOU 3374  CD2 TYR A 302    10442  16040  12742   -796   1179    808       C  
ATOM   3375  CE1 TYR A 302      27.844   3.495  -2.041  1.00107.67           C  
ANISOU 3375  CE1 TYR A 302    11106  16825  12979   -609   1403   1041       C  
ATOM   3376  CE2 TYR A 302      27.430   3.490   0.321  1.00103.61           C  
ANISOU 3376  CE2 TYR A 302    10684  15936  12746   -788   1169    869       C  
ATOM   3377  CZ  TYR A 302      27.072   3.881  -0.959  1.00111.69           C  
ANISOU 3377  CZ  TYR A 302    11758  17069  13610   -693   1279    987       C  
ATOM   3378  OH  TYR A 302      25.942   4.632  -1.171  1.00110.95           O  
ANISOU 3378  OH  TYR A 302    11853  16842  13459   -658   1266   1048       O  
ATOM   3379  N   ALA A 303      31.558  -2.155  -0.879  1.00101.33           N  
ANISOU 3379  N   ALA A 303     9599  16655  12247   -144   1224    350       N  
ATOM   3380  CA  ALA A 303      32.626  -3.145  -1.000  1.00122.19           C  
ANISOU 3380  CA  ALA A 303    12065  19506  14854      5   1236    256       C  
ATOM   3381  C   ALA A 303      32.455  -3.909  -2.318  1.00141.59           C  
ANISOU 3381  C   ALA A 303    14527  22159  17110    261   1292    172       C  
ATOM   3382  O   ALA A 303      31.382  -3.884  -2.923  1.00 99.45           O  
ANISOU 3382  O   ALA A 303     9348  16757  11683    326   1279    143       O  
ATOM   3383  CB  ALA A 303      32.606  -4.117   0.173  1.00121.45           C  
ANISOU 3383  CB  ALA A 303    12008  19258  14881     51   1080     94       C  
TER    3384      ALA A 303                                                      
ATOM   3385  N   ASN B  35     -29.766   4.380  33.929  1.00115.04           N  
ANISOU 3385  N   ASN B  35    16853  14541  12314  -1709   2569  -1849       N  
ATOM   3386  CA  ASN B  35     -31.048   3.683  34.039  1.00114.73           C  
ANISOU 3386  CA  ASN B  35    16528  14772  12290  -1466   2651  -1613       C  
ATOM   3387  C   ASN B  35     -31.833   3.701  32.724  1.00117.02           C  
ANISOU 3387  C   ASN B  35    16595  14981  12885  -1142   2701  -1405       C  
ATOM   3388  O   ASN B  35     -32.434   2.691  32.364  1.00115.15           O  
ANISOU 3388  O   ASN B  35    16010  14989  12752  -1098   2562  -1150       O  
ATOM   3389  CB  ASN B  35     -31.892   4.266  35.174  1.00118.87           C  
ANISOU 3389  CB  ASN B  35    17236  15387  12542  -1318   2992  -1750       C  
ATOM   3390  CG  ASN B  35     -33.189   3.528  35.396  1.00140.73           C  
ANISOU 3390  CG  ASN B  35    19673  18497  15300  -1102   3080  -1480       C  
ATOM   3391  OD1 ASN B  35     -33.220   2.445  35.985  1.00135.10           O  
ANISOU 3391  OD1 ASN B  35    18745  18103  14485  -1283   2903  -1321       O  
ATOM   3392  ND2 ASN B  35     -34.282   4.083  34.895  1.00133.55           N  
ANISOU 3392  ND2 ASN B  35    18695  17544  14506   -710   3357  -1387       N  
ATOM   3393  N   PHE B  36     -31.838   4.855  32.028  1.00113.95           N  
ANISOU 3393  N   PHE B  36    16414  14258  12622   -930   2907  -1510       N  
ATOM   3394  CA  PHE B  36     -32.521   5.076  30.752  1.00112.54           C  
ANISOU 3394  CA  PHE B  36    16051  14010  12699   -594   2980  -1314       C  
ATOM   3395  C   PHE B  36     -32.061   4.097  29.656  1.00110.33           C  
ANISOU 3395  C   PHE B  36    15476  13817  12628   -717   2618  -1124       C  
ATOM   3396  O   PHE B  36     -32.862   3.737  28.790  1.00109.02           O  
ANISOU 3396  O   PHE B  36    15020  13798  12604   -508   2590   -905       O  
ATOM   3397  CB  PHE B  36     -32.359   6.550  30.321  1.00116.81           C  
ANISOU 3397  CB  PHE B  36    16941  14124  13318   -381   3275  -1469       C  
ATOM   3398  CG  PHE B  36     -32.688   6.889  28.885  1.00117.72           C  
ANISOU 3398  CG  PHE B  36    16908  14126  13694    -73   3313  -1267       C  
ATOM   3399  CD1 PHE B  36     -33.995   6.815  28.416  1.00121.91           C  
ANISOU 3399  CD1 PHE B  36    17146  14888  14287    315   3459  -1012       C  
ATOM   3400  CD2 PHE B  36     -31.695   7.312  28.009  1.00118.63           C  
ANISOU 3400  CD2 PHE B  36    17156  13946  13972   -170   3210  -1312       C  
ATOM   3401  CE1 PHE B  36     -34.297   7.131  27.088  1.00122.34           C  
ANISOU 3401  CE1 PHE B  36    17041  14900  14543    602   3481   -807       C  
ATOM   3402  CE2 PHE B  36     -32.002   7.643  26.685  1.00120.85           C  
ANISOU 3402  CE2 PHE B  36    17300  14153  14465    132   3255  -1107       C  
ATOM   3403  CZ  PHE B  36     -33.302   7.559  26.237  1.00119.86           C  
ANISOU 3403  CZ  PHE B  36    16888  14276  14380    520   3387   -860       C  
ATOM   3404  N   ASN B  37     -30.795   3.636  29.732  1.00103.13           N  
ANISOU 3404  N   ASN B  37    14629  12851  11706  -1057   2346  -1204       N  
ATOM   3405  CA  ASN B  37     -30.190   2.682  28.799  1.00 98.77           C  
ANISOU 3405  CA  ASN B  37    13856  12350  11320  -1178   2022  -1054       C  
ATOM   3406  C   ASN B  37     -30.821   1.275  28.864  1.00 98.60           C  
ANISOU 3406  C   ASN B  37    13512  12641  11309  -1232   1842   -845       C  
ATOM   3407  O   ASN B  37     -30.540   0.448  28.000  1.00 95.54           O  
ANISOU 3407  O   ASN B  37    12955  12279  11066  -1286   1613   -721       O  
ATOM   3408  CB  ASN B  37     -28.667   2.633  28.990  1.00 99.52           C  
ANISOU 3408  CB  ASN B  37    14104  12334  11375  -1492   1825  -1172       C  
ATOM   3409  CG  ASN B  37     -27.950   3.931  28.669  1.00127.54           C  
ANISOU 3409  CG  ASN B  37    17941  15553  14965  -1502   1959  -1352       C  
ATOM   3410  OD1 ASN B  37     -28.558   4.957  28.329  1.00124.61           O  
ANISOU 3410  OD1 ASN B  37    17714  14972  14658  -1249   2233  -1401       O  
ATOM   3411  ND2 ASN B  37     -26.628   3.914  28.768  1.00119.21           N  
ANISOU 3411  ND2 ASN B  37    16970  14448  13876  -1795   1781  -1429       N  
ATOM   3412  N   LYS B  38     -31.697   1.022  29.863  1.00 95.08           N  
ANISOU 3412  N   LYS B  38    12999  12418  10709  -1217   1967   -806       N  
ATOM   3413  CA  LYS B  38     -32.456  -0.226  30.019  1.00 93.45           C  
ANISOU 3413  CA  LYS B  38    12494  12501  10513  -1283   1849   -593       C  
ATOM   3414  C   LYS B  38     -33.660  -0.188  29.049  1.00 94.68           C  
ANISOU 3414  C   LYS B  38    12392  12772  10811  -1034   1922   -432       C  
ATOM   3415  O   LYS B  38     -34.254  -1.225  28.759  1.00 93.40           O  
ANISOU 3415  O   LYS B  38    11957  12815  10715  -1121   1779   -254       O  
ATOM   3416  CB  LYS B  38     -32.956  -0.359  31.471  1.00 98.36           C  
ANISOU 3416  CB  LYS B  38    13136  13340  10894  -1345   1994   -596       C  
ATOM   3417  CG  LYS B  38     -33.309  -1.780  31.909  1.00110.54           C  
ANISOU 3417  CG  LYS B  38    14436  15141  12421  -1535   1834   -380       C  
ATOM   3418  CD  LYS B  38     -34.264  -1.814  33.120  1.00121.46           C  
ANISOU 3418  CD  LYS B  38    15751  16807  13592  -1495   2047   -311       C  
ATOM   3419  CE  LYS B  38     -33.618  -1.486  34.454  1.00133.44           C  
ANISOU 3419  CE  LYS B  38    17519  18363  14820  -1616   2123   -470       C  
ATOM   3420  NZ  LYS B  38     -32.794  -2.608  34.981  1.00141.14           N  
ANISOU 3420  NZ  LYS B  38    18459  19432  15736  -1908   1874   -359       N  
ATOM   3421  N   ILE B  39     -34.009   1.025  28.563  1.00 90.54           N  
ANISOU 3421  N   ILE B  39    11957  12121  10324   -733   2153   -485       N  
ATOM   3422  CA  ILE B  39     -35.105   1.322  27.630  1.00 90.29           C  
ANISOU 3422  CA  ILE B  39    11683  12229  10396   -432   2260   -315       C  
ATOM   3423  C   ILE B  39     -34.529   1.668  26.237  1.00 89.54           C  
ANISOU 3423  C   ILE B  39    11614  11933  10472   -339   2149   -317       C  
ATOM   3424  O   ILE B  39     -35.055   1.204  25.223  1.00 87.85           O  
ANISOU 3424  O   ILE B  39    11126  11899  10354   -276   2019   -156       O  
ATOM   3425  CB  ILE B  39     -36.013   2.473  28.187  1.00 96.89           C  
ANISOU 3425  CB  ILE B  39    12596  13093  11124    -78   2667   -319       C  
ATOM   3426  CG1 ILE B  39     -36.505   2.195  29.620  1.00 99.37           C  
ANISOU 3426  CG1 ILE B  39    12915  13611  11229   -155   2804   -334       C  
ATOM   3427  CG2 ILE B  39     -37.192   2.788  27.263  1.00 99.27           C  
ANISOU 3427  CG2 ILE B  39    12592  13615  11510    278   2792    -82       C  
ATOM   3428  CD1 ILE B  39     -35.844   3.064  30.670  1.00109.18           C  
ANISOU 3428  CD1 ILE B  39    14591  14598  12296   -179   3008   -611       C  
ATOM   3429  N   PHE B  40     -33.455   2.486  26.201  1.00 84.04           N  
ANISOU 3429  N   PHE B  40    11244  10891   9798   -354   2201   -495       N  
ATOM   3430  CA  PHE B  40     -32.830   2.934  24.960  1.00 81.64           C  
ANISOU 3430  CA  PHE B  40    10992  10382   9644   -259   2136   -487       C  
ATOM   3431  C   PHE B  40     -31.912   1.955  24.239  1.00 78.89           C  
ANISOU 3431  C   PHE B  40    10565  10026   9384   -497   1794   -471       C  
ATOM   3432  O   PHE B  40     -31.840   2.008  23.014  1.00 77.53           O  
ANISOU 3432  O   PHE B  40    10297   9839   9322   -372   1716   -387       O  
ATOM   3433  CB  PHE B  40     -32.221   4.335  25.076  1.00 85.33           C  
ANISOU 3433  CB  PHE B  40    11822  10478  10123   -145   2382   -645       C  
ATOM   3434  CG  PHE B  40     -32.355   5.098  23.778  1.00 88.10           C  
ANISOU 3434  CG  PHE B  40    12147  10704  10622    160   2483   -522       C  
ATOM   3435  CD1 PHE B  40     -31.271   5.231  22.915  1.00 90.09           C  
ANISOU 3435  CD1 PHE B  40    12489  10752  10987     67   2341   -544       C  
ATOM   3436  CD2 PHE B  40     -33.586   5.616  23.378  1.00 93.07           C  
ANISOU 3436  CD2 PHE B  40    12617  11477  11267    558   2715   -339       C  
ATOM   3437  CE1 PHE B  40     -31.405   5.901  21.693  1.00 91.61           C  
ANISOU 3437  CE1 PHE B  40    12643  10863  11302    359   2436   -397       C  
ATOM   3438  CE2 PHE B  40     -33.720   6.282  22.154  1.00 96.66           C  
ANISOU 3438  CE2 PHE B  40    13021  11866  11841    863   2802   -179       C  
ATOM   3439  CZ  PHE B  40     -32.628   6.419  21.320  1.00 93.07           C  
ANISOU 3439  CZ  PHE B  40    12681  11188  11494    756   2662   -213       C  
ATOM   3440  N   LEU B  41     -31.209   1.073  24.964  1.00 72.12           N  
ANISOU 3440  N   LEU B  41     9750   9188   8466   -807   1607   -535       N  
ATOM   3441  CA  LEU B  41     -30.362   0.077  24.304  1.00 68.60           C  
ANISOU 3441  CA  LEU B  41     9238   8725   8101   -985   1317   -499       C  
ATOM   3442  C   LEU B  41     -31.202  -0.995  23.612  1.00 70.25           C  
ANISOU 3442  C   LEU B  41     9172   9155   8365   -987   1165   -355       C  
ATOM   3443  O   LEU B  41     -30.945  -1.219  22.431  1.00 68.91           O  
ANISOU 3443  O   LEU B  41     8941   8956   8286   -934   1037   -320       O  
ATOM   3444  CB  LEU B  41     -29.307  -0.554  25.222  1.00 67.75           C  
ANISOU 3444  CB  LEU B  41     9245   8582   7914  -1273   1176   -563       C  
ATOM   3445  CG  LEU B  41     -28.093   0.301  25.564  1.00 72.31           C  
ANISOU 3445  CG  LEU B  41    10065   8962   8447  -1368   1216   -705       C  
ATOM   3446  CD1 LEU B  41     -27.395  -0.229  26.791  1.00 72.79           C  
ANISOU 3446  CD1 LEU B  41    10190   9115   8354  -1635   1119   -745       C  
ATOM   3447  CD2 LEU B  41     -27.116   0.360  24.413  1.00 72.48           C  
ANISOU 3447  CD2 LEU B  41    10096   8843   8599  -1346   1091   -678       C  
ATOM   3448  N   PRO B  42     -32.243  -1.619  24.242  1.00 66.24           N  
ANISOU 3448  N   PRO B  42     8490   8881   7796  -1053   1183   -270       N  
ATOM   3449  CA  PRO B  42     -33.047  -2.604  23.498  1.00 65.71           C  
ANISOU 3449  CA  PRO B  42     8163   9021   7782  -1115   1027   -148       C  
ATOM   3450  C   PRO B  42     -33.784  -2.008  22.299  1.00 69.85           C  
ANISOU 3450  C   PRO B  42     8514   9679   8347   -865   1073    -73       C  
ATOM   3451  O   PRO B  42     -34.061  -2.735  21.354  1.00 69.75           O  
ANISOU 3451  O   PRO B  42     8341   9789   8370   -939    891    -23       O  
ATOM   3452  CB  PRO B  42     -34.010  -3.142  24.551  1.00 68.96           C  
ANISOU 3452  CB  PRO B  42     8427   9663   8112  -1235   1090    -57       C  
ATOM   3453  CG  PRO B  42     -34.121  -2.067  25.532  1.00 74.59           C  
ANISOU 3453  CG  PRO B  42     9269  10355   8718  -1078   1353   -114       C  
ATOM   3454  CD  PRO B  42     -32.753  -1.481  25.622  1.00 68.87           C  
ANISOU 3454  CD  PRO B  42     8847   9323   7995  -1095   1346   -278       C  
ATOM   3455  N   THR B  43     -34.076  -0.686  22.337  1.00 66.24           N  
ANISOU 3455  N   THR B  43     8107   9193   7870   -568   1325    -63       N  
ATOM   3456  CA  THR B  43     -34.718   0.077  21.260  1.00 66.32           C  
ANISOU 3456  CA  THR B  43     7965   9327   7906   -255   1420     54       C  
ATOM   3457  C   THR B  43     -33.794   0.059  20.037  1.00 67.34           C  
ANISOU 3457  C   THR B  43     8177   9296   8112   -243   1259     14       C  
ATOM   3458  O   THR B  43     -34.226  -0.259  18.927  1.00 67.04           O  
ANISOU 3458  O   THR B  43     7932   9466   8073   -186   1130    106       O  
ATOM   3459  CB  THR B  43     -35.020   1.508  21.765  1.00 72.46           C  
ANISOU 3459  CB  THR B  43     8879   9993   8657     70   1776     63       C  
ATOM   3460  OG1 THR B  43     -36.082   1.447  22.714  1.00 72.69           O  
ANISOU 3460  OG1 THR B  43     8763  10263   8592    114   1933    141       O  
ATOM   3461  CG2 THR B  43     -35.400   2.467  20.656  1.00 71.55           C  
ANISOU 3461  CG2 THR B  43     8684   9913   8588    446   1916    204       C  
ATOM   3462  N   ILE B  44     -32.516   0.378  20.265  1.00 62.25           N  
ANISOU 3462  N   ILE B  44     7821   8320   7512   -314   1263   -119       N  
ATOM   3463  CA  ILE B  44     -31.486   0.403  19.235  1.00 60.65           C  
ANISOU 3463  CA  ILE B  44     7713   7954   7376   -303   1139   -148       C  
ATOM   3464  C   ILE B  44     -31.156  -1.025  18.774  1.00 64.13           C  
ANISOU 3464  C   ILE B  44     8076   8471   7820   -539    849   -173       C  
ATOM   3465  O   ILE B  44     -30.980  -1.239  17.578  1.00 63.61           O  
ANISOU 3465  O   ILE B  44     7950   8452   7766   -470    732   -146       O  
ATOM   3466  CB  ILE B  44     -30.257   1.279  19.656  1.00 62.87           C  
ANISOU 3466  CB  ILE B  44     8296   7894   7698   -322   1254   -258       C  
ATOM   3467  CG1 ILE B  44     -30.650   2.769  19.914  1.00 64.98           C  
ANISOU 3467  CG1 ILE B  44     8696   8018   7975    -66   1580   -248       C  
ATOM   3468  CG2 ILE B  44     -29.082   1.171  18.679  1.00 61.90           C  
ANISOU 3468  CG2 ILE B  44     8243   7636   7640   -346   1116   -264       C  
ATOM   3469  CD1 ILE B  44     -31.356   3.580  18.740  1.00 72.13           C  
ANISOU 3469  CD1 ILE B  44     9479   9001   8927    314   1726    -70       C  
ATOM   3470  N   TYR B  45     -31.156  -2.000  19.696  1.00 60.96           N  
ANISOU 3470  N   TYR B  45     7684   8085   7394   -796    753   -213       N  
ATOM   3471  CA  TYR B  45     -30.906  -3.399  19.360  1.00 60.35           C  
ANISOU 3471  CA  TYR B  45     7580   8019   7331  -1015    521   -232       C  
ATOM   3472  C   TYR B  45     -32.034  -3.991  18.513  1.00 64.93           C  
ANISOU 3472  C   TYR B  45     7924   8864   7882  -1042    413   -176       C  
ATOM   3473  O   TYR B  45     -31.742  -4.595  17.486  1.00 63.75           O  
ANISOU 3473  O   TYR B  45     7784   8703   7735  -1081    255   -217       O  
ATOM   3474  CB  TYR B  45     -30.679  -4.247  20.622  1.00 62.00           C  
ANISOU 3474  CB  TYR B  45     7862   8170   7525  -1263    482   -245       C  
ATOM   3475  CG  TYR B  45     -29.452  -3.867  21.422  1.00 63.68           C  
ANISOU 3475  CG  TYR B  45     8282   8186   7728  -1297    528   -299       C  
ATOM   3476  CD1 TYR B  45     -28.283  -3.447  20.789  1.00 64.72           C  
ANISOU 3476  CD1 TYR B  45     8537   8153   7901  -1215    500   -337       C  
ATOM   3477  CD2 TYR B  45     -29.437  -3.980  22.808  1.00 65.20           C  
ANISOU 3477  CD2 TYR B  45     8525   8401   7848  -1434    589   -297       C  
ATOM   3478  CE1 TYR B  45     -27.143  -3.116  21.519  1.00 65.48           C  
ANISOU 3478  CE1 TYR B  45     8781   8128   7971  -1294    520   -372       C  
ATOM   3479  CE2 TYR B  45     -28.306  -3.645  23.549  1.00 65.71           C  
ANISOU 3479  CE2 TYR B  45     8754   8350   7862  -1503    605   -347       C  
ATOM   3480  CZ  TYR B  45     -27.160  -3.214  22.899  1.00 73.47           C  
ANISOU 3480  CZ  TYR B  45     9836   9186   8892  -1447    563   -385       C  
ATOM   3481  OH  TYR B  45     -26.036  -2.878  23.613  1.00 76.51           O  
ANISOU 3481  OH  TYR B  45    10344   9513   9213  -1556    560   -421       O  
ATOM   3482  N   SER B  46     -33.314  -3.799  18.924  1.00 63.21           N  
ANISOU 3482  N   SER B  46     7489   8913   7616  -1024    502    -83       N  
ATOM   3483  CA  SER B  46     -34.490  -4.321  18.219  1.00 64.72           C  
ANISOU 3483  CA  SER B  46     7394   9442   7754  -1095    392     -6       C  
ATOM   3484  C   SER B  46     -34.526  -3.895  16.762  1.00 68.70           C  
ANISOU 3484  C   SER B  46     7809  10074   8219   -900    330     14       C  
ATOM   3485  O   SER B  46     -34.559  -4.763  15.887  1.00 68.41           O  
ANISOU 3485  O   SER B  46     7733  10116   8143  -1066    124    -47       O  
ATOM   3486  CB  SER B  46     -35.781  -3.927  18.927  1.00 70.52           C  
ANISOU 3486  CB  SER B  46     7874  10485   8434  -1034    545    139       C  
ATOM   3487  OG  SER B  46     -35.771  -4.399  20.264  1.00 80.52           O  
ANISOU 3487  OG  SER B  46     9215  11668   9710  -1226    599    129       O  
ATOM   3488  N   ILE B  47     -34.470  -2.568  16.504  1.00 65.67           N  
ANISOU 3488  N   ILE B  47     7427   9687   7837   -549    520     95       N  
ATOM   3489  CA  ILE B  47     -34.475  -1.982  15.160  1.00 66.21           C  
ANISOU 3489  CA  ILE B  47     7411   9886   7861   -300    505    165       C  
ATOM   3490  C   ILE B  47     -33.375  -2.612  14.318  1.00 69.30           C  
ANISOU 3490  C   ILE B  47     7988  10083   8261   -406    321     29       C  
ATOM   3491  O   ILE B  47     -33.674  -3.221  13.292  1.00 69.67           O  
ANISOU 3491  O   ILE B  47     7916  10345   8212   -479    141      9       O  
ATOM   3492  CB  ILE B  47     -34.380  -0.428  15.207  1.00 69.56           C  
ANISOU 3492  CB  ILE B  47     7899  10205   8326     94    791    281       C  
ATOM   3493  CG1 ILE B  47     -35.683   0.190  15.755  1.00 72.42           C  
ANISOU 3493  CG1 ILE B  47     8027  10843   8645    289    995    455       C  
ATOM   3494  CG2 ILE B  47     -34.024   0.160  13.821  1.00 70.23           C  
ANISOU 3494  CG2 ILE B  47     7969  10330   8385    349    783    362       C  
ATOM   3495  CD1 ILE B  47     -35.514   1.531  16.398  1.00 79.19           C  
ANISOU 3495  CD1 ILE B  47     9076  11444   9567    591   1331    497       C  
ATOM   3496  N   ILE B  48     -32.118  -2.518  14.800  1.00 64.67           N  
ANISOU 3496  N   ILE B  48     7686   9119   7768   -434    367    -65       N  
ATOM   3497  CA  ILE B  48     -30.930  -3.055  14.138  1.00 63.49           C  
ANISOU 3497  CA  ILE B  48     7721   8767   7634   -488    239   -166       C  
ATOM   3498  C   ILE B  48     -30.989  -4.587  13.929  1.00 67.76           C  
ANISOU 3498  C   ILE B  48     8285   9324   8137   -776     18   -283       C  
ATOM   3499  O   ILE B  48     -30.453  -5.071  12.936  1.00 67.38           O  
ANISOU 3499  O   ILE B  48     8319   9241   8042   -766    -95   -355       O  
ATOM   3500  CB  ILE B  48     -29.614  -2.484  14.760  1.00 65.12           C  
ANISOU 3500  CB  ILE B  48     8168   8636   7938   -446    353   -195       C  
ATOM   3501  CG1 ILE B  48     -28.513  -2.196  13.724  1.00 65.23           C  
ANISOU 3501  CG1 ILE B  48     8288   8535   7962   -298    336   -189       C  
ATOM   3502  CG2 ILE B  48     -29.108  -3.251  15.971  1.00 65.55           C  
ANISOU 3502  CG2 ILE B  48     8352   8518   8035   -697    309   -271       C  
ATOM   3503  CD1 ILE B  48     -27.687  -3.409  13.242  1.00 75.72           C  
ANISOU 3503  CD1 ILE B  48     9722   9777   9269   -423    161   -281       C  
ATOM   3504  N   PHE B  49     -31.706  -5.328  14.805  1.00 65.23           N  
ANISOU 3504  N   PHE B  49     7898   9059   7826  -1026    -23   -295       N  
ATOM   3505  CA  PHE B  49     -31.893  -6.776  14.661  1.00 65.89           C  
ANISOU 3505  CA  PHE B  49     8025   9118   7891  -1333   -204   -397       C  
ATOM   3506  C   PHE B  49     -32.828  -7.057  13.471  1.00 71.79           C  
ANISOU 3506  C   PHE B  49     8579  10194   8504  -1392   -347   -424       C  
ATOM   3507  O   PHE B  49     -32.434  -7.766  12.553  1.00 71.48           O  
ANISOU 3507  O   PHE B  49     8668  10087   8404  -1468   -480   -555       O  
ATOM   3508  CB  PHE B  49     -32.448  -7.405  15.959  1.00 68.19           C  
ANISOU 3508  CB  PHE B  49     8284   9391   8235  -1589   -185   -362       C  
ATOM   3509  CG  PHE B  49     -32.809  -8.870  15.863  1.00 71.44           C  
ANISOU 3509  CG  PHE B  49     8741   9756   8645  -1939   -343   -443       C  
ATOM   3510  CD1 PHE B  49     -34.133  -9.269  15.723  1.00 77.33           C  
ANISOU 3510  CD1 PHE B  49     9242  10810   9328  -2169   -426   -414       C  
ATOM   3511  CD2 PHE B  49     -31.828  -9.851  15.925  1.00 73.05           C  
ANISOU 3511  CD2 PHE B  49     9236   9606   8915  -2044   -394   -532       C  
ATOM   3512  CE1 PHE B  49     -34.466 -10.625  15.635  1.00 80.43           C  
ANISOU 3512  CE1 PHE B  49     9711  11120   9730  -2551   -564   -504       C  
ATOM   3513  CE2 PHE B  49     -32.161 -11.207  15.839  1.00 78.10           C  
ANISOU 3513  CE2 PHE B  49     9977  10128   9570  -2368   -504   -612       C  
ATOM   3514  CZ  PHE B  49     -33.477 -11.583  15.695  1.00 79.04           C  
ANISOU 3514  CZ  PHE B  49     9880  10518   9633  -2645   -592   -612       C  
ATOM   3515  N   LEU B  50     -34.052  -6.487  13.493  1.00 70.13           N  
ANISOU 3515  N   LEU B  50     8055  10365   8228  -1347   -311   -293       N  
ATOM   3516  CA  LEU B  50     -35.072  -6.660  12.455  1.00 72.72           C  
ANISOU 3516  CA  LEU B  50     8115  11122   8393  -1418   -455   -274       C  
ATOM   3517  C   LEU B  50     -34.584  -6.159  11.096  1.00 76.70           C  
ANISOU 3517  C   LEU B  50     8648  11709   8787  -1162   -494   -293       C  
ATOM   3518  O   LEU B  50     -34.632  -6.911  10.127  1.00 78.08           O  
ANISOU 3518  O   LEU B  50     8849  11991   8827  -1327   -680   -431       O  
ATOM   3519  CB  LEU B  50     -36.400  -5.970  12.851  1.00 74.86           C  
ANISOU 3519  CB  LEU B  50     8002  11825   8617  -1331   -362    -59       C  
ATOM   3520  CG  LEU B  50     -37.052  -6.374  14.196  1.00 80.32           C  
ANISOU 3520  CG  LEU B  50     8603  12528   9386  -1556   -297      4       C  
ATOM   3521  CD1 LEU B  50     -38.054  -5.326  14.653  1.00 81.92           C  
ANISOU 3521  CD1 LEU B  50     8486  13083   9557  -1293   -104    245       C  
ATOM   3522  CD2 LEU B  50     -37.733  -7.740  14.117  1.00 85.18           C  
ANISOU 3522  CD2 LEU B  50     9126  13283   9956  -2043   -512    -79       C  
ATOM   3523  N   THR B  51     -34.073  -4.913  11.034  1.00 71.65           N  
ANISOU 3523  N   THR B  51     8033  10995   8195   -777   -309   -166       N  
ATOM   3524  CA  THR B  51     -33.540  -4.312   9.804  1.00 71.38           C  
ANISOU 3524  CA  THR B  51     8026  11025   8070   -496   -305   -133       C  
ATOM   3525  C   THR B  51     -32.360  -5.135   9.291  1.00 74.85           C  
ANISOU 3525  C   THR B  51     8772  11162   8506   -597   -412   -334       C  
ATOM   3526  O   THR B  51     -32.247  -5.345   8.088  1.00 75.43           O  
ANISOU 3526  O   THR B  51     8845  11397   8418   -547   -522   -394       O  
ATOM   3527  CB  THR B  51     -33.119  -2.845  10.035  1.00 75.94           C  
ANISOU 3527  CB  THR B  51     8632  11471   8751   -109    -48     46       C  
ATOM   3528  OG1 THR B  51     -34.065  -2.179  10.870  1.00 75.41           O  
ANISOU 3528  OG1 THR B  51     8376  11549   8729    -16    109    202       O  
ATOM   3529  CG2 THR B  51     -32.919  -2.074   8.739  1.00 75.53           C  
ANISOU 3529  CG2 THR B  51     8514  11595   8590    213    -15    170       C  
ATOM   3530  N   GLY B  52     -31.514  -5.594  10.213  1.00 70.17           N  
ANISOU 3530  N   GLY B  52     8426  10165   8069   -718   -368   -421       N  
ATOM   3531  CA  GLY B  52     -30.325  -6.382   9.916  1.00 69.10           C  
ANISOU 3531  CA  GLY B  52     8582   9717   7955   -768   -423   -570       C  
ATOM   3532  C   GLY B  52     -30.581  -7.817   9.510  1.00 75.30           C  
ANISOU 3532  C   GLY B  52     9479  10481   8651  -1069   -605   -770       C  
ATOM   3533  O   GLY B  52     -29.869  -8.336   8.653  1.00 75.48           O  
ANISOU 3533  O   GLY B  52     9695  10390   8593  -1024   -658   -896       O  
ATOM   3534  N   ILE B  53     -31.561  -8.485  10.130  1.00 73.82           N  
ANISOU 3534  N   ILE B  53     9195  10377   8477  -1384   -683   -803       N  
ATOM   3535  CA  ILE B  53     -31.855  -9.879   9.802  1.00 76.26           C  
ANISOU 3535  CA  ILE B  53     9646  10612   8717  -1735   -843  -1006       C  
ATOM   3536  C   ILE B  53     -32.643 -10.010   8.494  1.00 82.57           C  
ANISOU 3536  C   ILE B  53    10296  11807   9270  -1826  -1011  -1107       C  
ATOM   3537  O   ILE B  53     -32.309 -10.856   7.664  1.00 83.80           O  
ANISOU 3537  O   ILE B  53    10682  11850   9307  -1944  -1112  -1324       O  
ATOM   3538  CB  ILE B  53     -32.414 -10.688  11.011  1.00 80.29           C  
ANISOU 3538  CB  ILE B  53    10164  10986   9357  -2081   -851   -999       C  
ATOM   3539  CG1 ILE B  53     -31.916 -12.138  11.002  1.00 82.30           C  
ANISOU 3539  CG1 ILE B  53    10774  10841   9654  -2337   -908  -1189       C  
ATOM   3540  CG2 ILE B  53     -33.936 -10.572  11.190  1.00 83.10           C  
ANISOU 3540  CG2 ILE B  53    10158  11776   9642  -2308   -927   -915       C  
ATOM   3541  CD1 ILE B  53     -31.604 -12.671  12.387  1.00 89.03           C  
ANISOU 3541  CD1 ILE B  53    11758  11366  10704  -2453   -810  -1099       C  
ATOM   3542  N   VAL B  54     -33.647  -9.138   8.294  1.00 79.64           N  
ANISOU 3542  N   VAL B  54     9545  11912   8802  -1740  -1026   -940       N  
ATOM   3543  CA  VAL B  54     -34.480  -9.109   7.093  1.00 82.57           C  
ANISOU 3543  CA  VAL B  54     9687  12783   8903  -1804  -1194   -974       C  
ATOM   3544  C   VAL B  54     -33.629  -8.559   5.949  1.00 86.15           C  
ANISOU 3544  C   VAL B  54    10250  13258   9226  -1448  -1163   -988       C  
ATOM   3545  O   VAL B  54     -33.675  -9.095   4.844  1.00 88.14           O  
ANISOU 3545  O   VAL B  54    10569  13677   9243  -1553  -1315  -1166       O  
ATOM   3546  CB  VAL B  54     -35.791  -8.304   7.320  1.00 87.81           C  
ANISOU 3546  CB  VAL B  54     9870  13982   9509  -1759  -1187   -721       C  
ATOM   3547  CG1 VAL B  54     -36.626  -8.209   6.044  1.00 91.34           C  
ANISOU 3547  CG1 VAL B  54    10025  15035   9643  -1796  -1371   -708       C  
ATOM   3548  CG2 VAL B  54     -36.616  -8.911   8.451  1.00 88.54           C  
ANISOU 3548  CG2 VAL B  54     9846  14074   9720  -2122  -1207   -696       C  
ATOM   3549  N   GLY B  55     -32.822  -7.543   6.257  1.00 80.04           N  
ANISOU 3549  N   GLY B  55     9517  12294   8599  -1061   -962   -812       N  
ATOM   3550  CA  GLY B  55     -31.924  -6.888   5.314  1.00 79.13           C  
ANISOU 3550  CA  GLY B  55     9492  12170   8404   -699   -888   -763       C  
ATOM   3551  C   GLY B  55     -30.838  -7.791   4.776  1.00 83.68           C  
ANISOU 3551  C   GLY B  55    10433  12426   8934   -738   -926   -996       C  
ATOM   3552  O   GLY B  55     -30.846  -8.101   3.582  1.00 85.68           O  
ANISOU 3552  O   GLY B  55    10727  12892   8938   -725  -1034  -1121       O  
ATOM   3553  N   ASN B  56     -29.878  -8.195   5.642  1.00 78.57           N  
ANISOU 3553  N   ASN B  56    10051  11297   8507   -758   -824  -1039       N  
ATOM   3554  CA  ASN B  56     -28.740  -9.053   5.271  1.00 78.62           C  
ANISOU 3554  CA  ASN B  56    10411  10961   8501   -730   -809  -1213       C  
ATOM   3555  C   ASN B  56     -29.179 -10.432   4.771  1.00 87.33           C  
ANISOU 3555  C   ASN B  56    11710  12025   9447  -1062   -970  -1510       C  
ATOM   3556  O   ASN B  56     -28.564 -10.973   3.846  1.00 88.29           O  
ANISOU 3556  O   ASN B  56    12075  12059   9412   -982   -981  -1682       O  
ATOM   3557  CB  ASN B  56     -27.701  -9.150   6.395  1.00 75.14           C  
ANISOU 3557  CB  ASN B  56    10144  10085   8319   -672   -666  -1137       C  
ATOM   3558  CG  ASN B  56     -27.024  -7.833   6.727  1.00 89.46           C  
ANISOU 3558  CG  ASN B  56    11838  11894  10257   -373   -507   -897       C  
ATOM   3559  OD1 ASN B  56     -26.112  -7.377   6.026  1.00 87.43           O  
ANISOU 3559  OD1 ASN B  56    11633  11629   9956   -106   -428   -831       O  
ATOM   3560  ND2 ASN B  56     -27.443  -7.197   7.814  1.00 72.92           N  
ANISOU 3560  ND2 ASN B  56     9597   9795   8315   -428   -443   -764       N  
ATOM   3561  N   GLY B  57     -30.280 -10.937   5.333  1.00 86.62           N  
ANISOU 3561  N   GLY B  57    11509  12023   9381  -1434  -1082  -1567       N  
ATOM   3562  CA  GLY B  57     -30.892 -12.200   4.940  1.00 90.64           C  
ANISOU 3562  CA  GLY B  57    12182  12507   9749  -1847  -1245  -1850       C  
ATOM   3563  C   GLY B  57     -31.195 -12.251   3.459  1.00 98.70           C  
ANISOU 3563  C   GLY B  57    13184  13893  10424  -1852  -1386  -2020       C  
ATOM   3564  O   GLY B  57     -30.798 -13.206   2.790  1.00101.03           O  
ANISOU 3564  O   GLY B  57    13829  13976  10580  -1964  -1424  -2303       O  
ATOM   3565  N   LEU B  58     -31.835 -11.185   2.927  1.00 96.10           N  
ANISOU 3565  N   LEU B  58    12463  14111   9939  -1685  -1440  -1833       N  
ATOM   3566  CA  LEU B  58     -32.181 -11.043   1.507  1.00 99.46           C  
ANISOU 3566  CA  LEU B  58    12788  15009   9994  -1643  -1579  -1928       C  
ATOM   3567  C   LEU B  58     -30.927 -11.113   0.629  1.00103.77           C  
ANISOU 3567  C   LEU B  58    13656  15345  10428  -1320  -1479  -2037       C  
ATOM   3568  O   LEU B  58     -30.879 -11.914  -0.304  1.00106.66           O  
ANISOU 3568  O   LEU B  58    14259  15746  10523  -1469  -1583  -2334       O  
ATOM   3569  CB  LEU B  58     -32.915  -9.710   1.250  1.00 99.39           C  
ANISOU 3569  CB  LEU B  58    12287  15583   9894  -1392  -1585  -1597       C  
ATOM   3570  CG  LEU B  58     -34.393  -9.614   1.630  1.00106.44           C  
ANISOU 3570  CG  LEU B  58    12766  16936  10742  -1682  -1725  -1484       C  
ATOM   3571  CD1 LEU B  58     -34.808  -8.167   1.782  1.00105.42           C  
ANISOU 3571  CD1 LEU B  58    12224  17169  10660  -1286  -1602  -1078       C  
ATOM   3572  CD2 LEU B  58     -35.286 -10.306   0.609  1.00113.97           C  
ANISOU 3572  CD2 LEU B  58    13610  18382  11311  -2058  -2002  -1702       C  
ATOM   3573  N   VAL B  59     -29.905 -10.296   0.970  1.00 97.17           N  
ANISOU 3573  N   VAL B  59    12837  14288   9796   -901  -1267  -1802       N  
ATOM   3574  CA  VAL B  59     -28.618 -10.167   0.275  1.00 96.46           C  
ANISOU 3574  CA  VAL B  59    12979  14024   9646   -534  -1129  -1807       C  
ATOM   3575  C   VAL B  59     -27.908 -11.515   0.087  1.00103.67           C  
ANISOU 3575  C   VAL B  59    14364  14506  10519   -655  -1109  -2131       C  
ATOM   3576  O   VAL B  59     -27.409 -11.779  -1.009  1.00105.54           O  
ANISOU 3576  O   VAL B  59    14792  14809  10497   -497  -1097  -2283       O  
ATOM   3577  CB  VAL B  59     -27.724  -9.086   0.938  1.00 95.87           C  
ANISOU 3577  CB  VAL B  59    12809  13765   9851   -171   -913  -1481       C  
ATOM   3578  CG1 VAL B  59     -26.406  -8.909   0.190  1.00 95.09           C  
ANISOU 3578  CG1 VAL B  59    12892  13554   9686    196   -768  -1442       C  
ATOM   3579  CG2 VAL B  59     -28.460  -7.754   1.020  1.00 94.80           C  
ANISOU 3579  CG2 VAL B  59    12270  14011   9738    -25   -895  -1181       C  
ATOM   3580  N   ILE B  60     -27.902 -12.376   1.134  1.00100.47           N  
ANISOU 3580  N   ILE B  60    14156  13667  10352   -919  -1090  -2227       N  
ATOM   3581  CA  ILE B  60     -27.291 -13.713   1.088  1.00102.39           C  
ANISOU 3581  CA  ILE B  60    14877  13429  10597  -1027  -1036  -2507       C  
ATOM   3582  C   ILE B  60     -28.026 -14.599   0.069  1.00112.20           C  
ANISOU 3582  C   ILE B  60    16311  14818  11500  -1359  -1210  -2888       C  
ATOM   3583  O   ILE B  60     -27.389 -15.111  -0.851  1.00113.83           O  
ANISOU 3583  O   ILE B  60    16846  14911  11493  -1213  -1152  -3107       O  
ATOM   3584  CB  ILE B  60     -27.190 -14.379   2.495  1.00104.03           C  
ANISOU 3584  CB  ILE B  60    15222  13161  11142  -1226   -965  -2465       C  
ATOM   3585  CG1 ILE B  60     -26.384 -13.505   3.480  1.00100.03           C  
ANISOU 3585  CG1 ILE B  60    14541  12545  10920   -918   -804  -2115       C  
ATOM   3586  CG2 ILE B  60     -26.592 -15.796   2.403  1.00107.25           C  
ANISOU 3586  CG2 ILE B  60    16155  13039  11555  -1305   -876  -2730       C  
ATOM   3587  CD1 ILE B  60     -26.786 -13.652   4.966  1.00106.39           C  
ANISOU 3587  CD1 ILE B  60    15255  13159  12007  -1155   -797  -1985       C  
ATOM   3588  N   LEU B  61     -29.362 -14.738   0.214  1.00111.88           N  
ANISOU 3588  N   LEU B  61    16052  15068  11388  -1805  -1419  -2963       N  
ATOM   3589  CA  LEU B  61     -30.179 -15.561  -0.681  1.00117.61           C  
ANISOU 3589  CA  LEU B  61    16917  15991  11777  -2226  -1623  -3333       C  
ATOM   3590  C   LEU B  61     -30.246 -15.100  -2.147  1.00125.37           C  
ANISOU 3590  C   LEU B  61    17805  17506  12324  -2054  -1722  -3424       C  
ATOM   3591  O   LEU B  61     -30.601 -15.904  -3.012  1.00129.90           O  
ANISOU 3591  O   LEU B  61    18621  18166  12570  -2356  -1858  -3798       O  
ATOM   3592  CB  LEU B  61     -31.557 -15.918  -0.086  1.00119.68           C  
ANISOU 3592  CB  LEU B  61    16952  16439  12083  -2798  -1822  -3372       C  
ATOM   3593  CG  LEU B  61     -32.581 -14.798   0.092  1.00123.31           C  
ANISOU 3593  CG  LEU B  61    16788  17553  12514  -2799  -1949  -3056       C  
ATOM   3594  CD1 LEU B  61     -33.629 -14.845  -1.013  1.00128.52           C  
ANISOU 3594  CD1 LEU B  61    17222  18869  12741  -3103  -2217  -3220       C  
ATOM   3595  CD2 LEU B  61     -33.285 -14.931   1.424  1.00124.60           C  
ANISOU 3595  CD2 LEU B  61    16760  17603  12981  -3096  -1955  -2898       C  
ATOM   3596  N   VAL B  62     -29.878 -13.830  -2.426  1.00120.01           N  
ANISOU 3596  N   VAL B  62    16804  17165  11630  -1581  -1644  -3089       N  
ATOM   3597  CA  VAL B  62     -29.843 -13.280  -3.785  1.00122.44           C  
ANISOU 3597  CA  VAL B  62    16994  17992  11535  -1338  -1703  -3094       C  
ATOM   3598  C   VAL B  62     -28.626 -13.864  -4.538  1.00129.84           C  
ANISOU 3598  C   VAL B  62    18415  18593  12324  -1068  -1542  -3323       C  
ATOM   3599  O   VAL B  62     -28.811 -14.528  -5.564  1.00134.03           O  
ANISOU 3599  O   VAL B  62    19186  19277  12463  -1232  -1648  -3674       O  
ATOM   3600  CB  VAL B  62     -29.927 -11.724  -3.804  1.00122.89           C  
ANISOU 3600  CB  VAL B  62    16554  18494  11647   -934  -1648  -2626       C  
ATOM   3601  CG1 VAL B  62     -29.498 -11.145  -5.152  1.00124.19           C  
ANISOU 3601  CG1 VAL B  62    16671  19066  11451   -558  -1622  -2567       C  
ATOM   3602  CG2 VAL B  62     -31.336 -11.254  -3.454  1.00123.44           C  
ANISOU 3602  CG2 VAL B  62    16148  19053  11702  -1199  -1831  -2458       C  
ATOM   3603  N   MET B  63     -27.399 -13.661  -4.002  1.00124.42           N  
ANISOU 3603  N   MET B  63    17875  17462  11935   -673  -1284  -3132       N  
ATOM   3604  CA  MET B  63     -26.179 -14.207  -4.609  1.00126.10           C  
ANISOU 3604  CA  MET B  63    18517  17354  12043   -360  -1090  -3289       C  
ATOM   3605  C   MET B  63     -25.597 -15.458  -3.928  1.00131.92           C  
ANISOU 3605  C   MET B  63    19744  17379  13001   -474   -950  -3508       C  
ATOM   3606  O   MET B  63     -24.385 -15.702  -3.961  1.00130.63           O  
ANISOU 3606  O   MET B  63    19845  16871  12917    -98   -713  -3465       O  
ATOM   3607  CB  MET B  63     -25.131 -13.148  -5.026  1.00125.87           C  
ANISOU 3607  CB  MET B  63    18317  17487  12019    219   -898  -2946       C  
ATOM   3608  CG  MET B  63     -24.804 -12.131  -3.967  1.00124.48           C  
ANISOU 3608  CG  MET B  63    17814  17231  12251    403   -793  -2512       C  
ATOM   3609  SD  MET B  63     -26.022 -10.808  -3.932  1.00127.67           S  
ANISOU 3609  SD  MET B  63    17645  18232  12631    327   -957  -2220       S  
ATOM   3610  CE  MET B  63     -25.039  -9.508  -3.284  1.00119.52           C  
ANISOU 3610  CE  MET B  63    16391  17074  11948    747   -722  -1749       C  
ATOM   3611  N   GLY B  64     -26.499 -16.260  -3.358  1.00131.51           N  
ANISOU 3611  N   GLY B  64    19798  17140  13029   -991  -1092  -3724       N  
ATOM   3612  CA  GLY B  64     -26.190 -17.553  -2.759  1.00133.55           C  
ANISOU 3612  CA  GLY B  64    20546  16724  13472  -1182   -979  -3954       C  
ATOM   3613  C   GLY B  64     -26.059 -18.576  -3.868  1.00144.40           C  
ANISOU 3613  C   GLY B  64    22443  17938  14483  -1272   -959  -4425       C  
ATOM   3614  O   GLY B  64     -25.471 -19.645  -3.681  1.00146.13           O  
ANISOU 3614  O   GLY B  64    23182  17545  14797  -1253   -774  -4628       O  
ATOM   3615  N   TYR B  65     -26.601 -18.215  -5.049  1.00144.64           N  
ANISOU 3615  N   TYR B  65    22339  18543  14076  -1344  -1137  -4589       N  
ATOM   3616  CA  TYR B  65     -26.582 -18.956  -6.307  1.00150.76           C  
ANISOU 3616  CA  TYR B  65    23543  19351  14388  -1431  -1159  -5054       C  
ATOM   3617  C   TYR B  65     -26.496 -18.004  -7.510  1.00154.74           C  
ANISOU 3617  C   TYR B  65    23759  20553  14482  -1106  -1225  -4959       C  
ATOM   3618  O   TYR B  65     -26.861 -16.828  -7.423  1.00151.12           O  
ANISOU 3618  O   TYR B  65    22734  20620  14063   -982  -1332  -4582       O  
ATOM   3619  CB  TYR B  65     -27.785 -19.915  -6.443  1.00157.80           C  
ANISOU 3619  CB  TYR B  65    24642  20222  15093  -2170  -1404  -5501       C  
ATOM   3620  CG  TYR B  65     -29.104 -19.462  -5.843  1.00158.96           C  
ANISOU 3620  CG  TYR B  65    24255  20801  15341  -2649  -1693  -5335       C  
ATOM   3621  CD1 TYR B  65     -29.671 -18.238  -6.191  1.00159.02           C  
ANISOU 3621  CD1 TYR B  65    23638  21594  15189  -2533  -1872  -5033       C  
ATOM   3622  CD2 TYR B  65     -29.846 -20.312  -5.028  1.00161.67           C  
ANISOU 3622  CD2 TYR B  65    24733  20797  15898  -3231  -1782  -5491       C  
ATOM   3623  CE1 TYR B  65     -30.899 -17.835  -5.669  1.00159.13           C  
ANISOU 3623  CE1 TYR B  65    23152  22034  15275  -2928  -2112  -4862       C  
ATOM   3624  CE2 TYR B  65     -31.085 -19.928  -4.516  1.00162.17           C  
ANISOU 3624  CE2 TYR B  65    24285  21307  16025  -3670  -2038  -5330       C  
ATOM   3625  CZ  TYR B  65     -31.607 -18.687  -4.838  1.00167.25           C  
ANISOU 3625  CZ  TYR B  65    24294  22740  16513  -3500  -2199  -5015       C  
ATOM   3626  OH  TYR B  65     -32.828 -18.303  -4.338  1.00168.36           O  
ANISOU 3626  OH  TYR B  65    23915  23345  16708  -3880  -2423  -4827       O  
ATOM   3627  N   ARG B  70     -23.027 -11.155  -9.682  1.00141.90           N  
ANISOU 3627  N   ARG B  70    20199  20941  12776   1722   -562  -2598       N  
ATOM   3628  CA  ARG B  70     -21.604 -11.438  -9.828  1.00141.31           C  
ANISOU 3628  CA  ARG B  70    20394  20535  12761   2120   -276  -2554       C  
ATOM   3629  C   ARG B  70     -20.871 -10.265 -10.470  1.00143.95           C  
ANISOU 3629  C   ARG B  70    20440  21225  13028   2594   -109  -2122       C  
ATOM   3630  O   ARG B  70     -20.758 -10.185 -11.693  1.00146.93           O  
ANISOU 3630  O   ARG B  70    20857  22002  12968   2810    -85  -2173       O  
ATOM   3631  CB  ARG B  70     -21.392 -12.707 -10.656  1.00146.09           C  
ANISOU 3631  CB  ARG B  70    21521  21006  12981   2097   -241  -3046       C  
ATOM   3632  CG  ARG B  70     -21.572 -13.997  -9.873  1.00154.80           C  
ANISOU 3632  CG  ARG B  70    23038  21509  14270   1745   -263  -3420       C  
ATOM   3633  CD  ARG B  70     -20.238 -14.681  -9.621  1.00162.99           C  
ANISOU 3633  CD  ARG B  70    24448  22006  15473   2095     53  -3427       C  
ATOM   3634  NE  ARG B  70     -19.770 -15.415 -10.794  1.00175.46           N  
ANISOU 3634  NE  ARG B  70    26462  23600  16604   2317    190  -3762       N  
ATOM   3635  CZ  ARG B  70     -19.637 -16.736 -10.845  1.00192.30           C  
ANISOU 3635  CZ  ARG B  70    29172  25245  18647   2214    287  -4197       C  
ATOM   3636  NH1 ARG B  70     -19.937 -17.476  -9.786  1.00178.70           N  
ANISOU 3636  NH1 ARG B  70    27642  22988  17268   1885    255  -4321       N  
ATOM   3637  NH2 ARG B  70     -19.205 -17.319 -11.954  1.00184.17           N  
ANISOU 3637  NH2 ARG B  70    28550  24247  17178   2449    435  -4506       N  
ATOM   3638  N   SER B  71     -20.376  -9.355  -9.637  1.00135.68           N  
ANISOU 3638  N   SER B  71    19114  20035  12403   2734     10  -1698       N  
ATOM   3639  CA  SER B  71     -19.654  -8.185 -10.121  1.00134.13           C  
ANISOU 3639  CA  SER B  71    18642  20111  12212   3134    186  -1251       C  
ATOM   3640  C   SER B  71     -18.346  -7.910  -9.387  1.00133.64           C  
ANISOU 3640  C   SER B  71    18555  19684  12537   3357    430   -959       C  
ATOM   3641  O   SER B  71     -17.645  -6.943  -9.687  1.00132.29           O  
ANISOU 3641  O   SER B  71    18158  19686  12421   3648    594   -568       O  
ATOM   3642  CB  SER B  71     -20.604  -6.996 -10.278  1.00137.33           C  
ANISOU 3642  CB  SER B  71    18636  20948  12595   3089     61   -968       C  
ATOM   3643  OG  SER B  71     -21.719  -7.337 -11.083  1.00150.63           O  
ANISOU 3643  OG  SER B  71    20320  23064  13849   2909   -168  -1228       O  
ATOM   3644  N   MET B  72     -18.036  -8.737  -8.390  1.00127.80           N  
ANISOU 3644  N   MET B  72    18027  18459  12071   3197    450  -1120       N  
ATOM   3645  CA  MET B  72     -16.775  -8.629  -7.649  1.00124.82           C  
ANISOU 3645  CA  MET B  72    17623  17775  12028   3385    661   -857       C  
ATOM   3646  C   MET B  72     -16.726  -7.513  -6.593  1.00122.68           C  
ANISOU 3646  C   MET B  72    17010  17431  12174   3267    660   -492       C  
ATOM   3647  O   MET B  72     -15.823  -7.483  -5.757  1.00120.69           O  
ANISOU 3647  O   MET B  72    16720  16921  12216   3308    780   -311       O  
ATOM   3648  CB  MET B  72     -15.601  -8.473  -8.620  1.00129.30           C  
ANISOU 3648  CB  MET B  72    18202  18537  12388   3841    902   -669       C  
ATOM   3649  CG  MET B  72     -14.235  -8.639  -7.974  1.00132.01           C  
ANISOU 3649  CG  MET B  72    18543  18612  13005   4047   1123   -437       C  
ATOM   3650  SD  MET B  72     -13.196  -9.830  -8.841  1.00140.93           S  
ANISOU 3650  SD  MET B  72    20047  19677  13822   4473   1370   -613       S  
ATOM   3651  CE  MET B  72     -14.275 -11.259  -8.875  1.00140.20           C  
ANISOU 3651  CE  MET B  72    20450  19288  13532   4175   1198  -1242       C  
ATOM   3652  N   THR B  73     -17.693  -6.603  -6.639  1.00116.33           N  
ANISOU 3652  N   THR B  73    15962  16865  11372   3129    534   -385       N  
ATOM   3653  CA  THR B  73     -17.746  -5.467  -5.741  1.00111.71           C  
ANISOU 3653  CA  THR B  73    15099  16205  11143   3031    556    -68       C  
ATOM   3654  C   THR B  73     -18.988  -5.814  -4.959  1.00111.08           C  
ANISOU 3654  C   THR B  73    15037  16011  11157   2662    346   -299       C  
ATOM   3655  O   THR B  73     -19.288  -5.228  -3.919  1.00108.76           O  
ANISOU 3655  O   THR B  73    14597  15561  11166   2484    325   -169       O  
ATOM   3656  CB  THR B  73     -17.942  -4.124  -6.456  1.00122.20           C  
ANISOU 3656  CB  THR B  73    16152  17884  12394   3215    621    267       C  
ATOM   3657  OG1 THR B  73     -16.684  -3.445  -6.557  1.00123.32           O  
ANISOU 3657  OG1 THR B  73    16187  17998  12669   3448    844    611       O  
ATOM   3658  CG2 THR B  73     -18.924  -3.251  -5.689  1.00118.91           C  
ANISOU 3658  CG2 THR B  73    15534  17441  12206   3004    536    388       C  
ATOM   3659  N   ASP B  74     -19.703  -6.798  -5.492  1.00106.65           N  
ANISOU 3659  N   ASP B  74    14670  15541  10312   2536    198   -655       N  
ATOM   3660  CA  ASP B  74     -20.879  -7.352  -4.834  1.00104.68           C  
ANISOU 3660  CA  ASP B  74    14459  15201  10113   2150     -9   -908       C  
ATOM   3661  C   ASP B  74     -20.517  -8.612  -4.056  1.00104.96           C  
ANISOU 3661  C   ASP B  74    14807  14778  10296   1975     -5  -1165       C  
ATOM   3662  O   ASP B  74     -20.998  -8.826  -2.943  1.00103.03           O  
ANISOU 3662  O   ASP B  74    14546  14299  10300   1693    -84  -1208       O  
ATOM   3663  CB  ASP B  74     -21.972  -7.662  -5.859  1.00109.77           C  
ANISOU 3663  CB  ASP B  74    15107  16252  10351   2038   -197  -1141       C  
ATOM   3664  CG  ASP B  74     -22.495  -6.417  -6.547  1.00118.52           C  
ANISOU 3664  CG  ASP B  74    15869  17850  11314   2214   -211   -843       C  
ATOM   3665  OD1 ASP B  74     -22.324  -5.312  -5.991  1.00115.81           O  
ANISOU 3665  OD1 ASP B  74    15295  17457  11253   2326    -98   -492       O  
ATOM   3666  OD2 ASP B  74     -23.077  -6.543  -7.645  1.00126.95           O  
ANISOU 3666  OD2 ASP B  74    16908  19353  11974   2240   -325   -957       O  
ATOM   3667  N   LYS B  75     -19.664  -9.442  -4.648  1.00101.03           N  
ANISOU 3667  N   LYS B  75    14600  14154   9635   2174    111  -1313       N  
ATOM   3668  CA  LYS B  75     -19.218 -10.675  -3.997  1.00100.17           C  
ANISOU 3668  CA  LYS B  75    14823  13582   9656   2087    166  -1521       C  
ATOM   3669  C   LYS B  75     -18.638 -10.377  -2.593  1.00 97.39           C  
ANISOU 3669  C   LYS B  75    14337  12939   9729   2051    243  -1258       C  
ATOM   3670  O   LYS B  75     -18.874 -11.155  -1.668  1.00 96.18           O  
ANISOU 3670  O   LYS B  75    14335  12456   9752   1818    197  -1389       O  
ATOM   3671  CB  LYS B  75     -18.244 -11.464  -4.887  1.00105.86           C  
ANISOU 3671  CB  LYS B  75    15866  14218  10139   2414    346  -1654       C  
ATOM   3672  CG  LYS B  75     -18.603 -12.941  -5.012  1.00126.62           C  
ANISOU 3672  CG  LYS B  75    18959  16529  12623   2229    310  -2103       C  
ATOM   3673  CD  LYS B  75     -17.622 -13.834  -4.256  1.00137.47           C  
ANISOU 3673  CD  LYS B  75    20601  17402  14230   2376    509  -2078       C  
ATOM   3674  CE  LYS B  75     -18.110 -15.254  -4.099  1.00149.17           C  
ANISOU 3674  CE  LYS B  75    22552  18459  15667   2121    481  -2490       C  
ATOM   3675  NZ  LYS B  75     -17.088 -16.115  -3.443  1.00158.55           N  
ANISOU 3675  NZ  LYS B  75    24009  19167  17066   2354    720  -2412       N  
ATOM   3676  N   TYR B  76     -17.918  -9.239  -2.426  1.00 89.51           N  
ANISOU 3676  N   TYR B  76    13052  12076   8881   2250    354   -886       N  
ATOM   3677  CA  TYR B  76     -17.399  -8.812  -1.121  1.00 85.15           C  
ANISOU 3677  CA  TYR B  76    12344  11321   8689   2171    404   -643       C  
ATOM   3678  C   TYR B  76     -18.574  -8.327  -0.271  1.00 84.43           C  
ANISOU 3678  C   TYR B  76    12094  11228   8756   1827    243   -665       C  
ATOM   3679  O   TYR B  76     -18.558  -8.491   0.948  1.00 82.16           O  
ANISOU 3679  O   TYR B  76    11797  10706   8715   1638    223   -632       O  
ATOM   3680  CB  TYR B  76     -16.403  -7.654  -1.251  1.00 85.35           C  
ANISOU 3680  CB  TYR B  76    12111  11511   8806   2405    554   -266       C  
ATOM   3681  CG  TYR B  76     -15.079  -7.973  -1.906  1.00 89.30           C  
ANISOU 3681  CG  TYR B  76    12680  12051   9199   2766    747   -142       C  
ATOM   3682  CD1 TYR B  76     -14.090  -8.676  -1.219  1.00 91.49           C  
ANISOU 3682  CD1 TYR B  76    13041  12100   9618   2853    853    -67       C  
ATOM   3683  CD2 TYR B  76     -14.762  -7.466  -3.162  1.00 91.64           C  
ANISOU 3683  CD2 TYR B  76    12907  12654   9258   3047    843    -32       C  
ATOM   3684  CE1 TYR B  76     -12.850  -8.935  -1.802  1.00 94.45           C  
ANISOU 3684  CE1 TYR B  76    13438  12555   9895   3223   1055     95       C  
ATOM   3685  CE2 TYR B  76     -13.523  -7.707  -3.749  1.00 94.31           C  
ANISOU 3685  CE2 TYR B  76    13276  13065   9493   3400   1045    119       C  
ATOM   3686  CZ  TYR B  76     -12.566  -8.436  -3.062  1.00102.84           C  
ANISOU 3686  CZ  TYR B  76    14436  13921  10720   3492   1154    185       C  
ATOM   3687  OH  TYR B  76     -11.345  -8.683  -3.642  1.00107.54           O  
ANISOU 3687  OH  TYR B  76    15031  14625  11205   3877   1372    366       O  
ATOM   3688  N   ARG B  77     -19.592  -7.714  -0.924  1.00 79.37           N  
ANISOU 3688  N   ARG B  77    11312  10890   7955   1774    138   -696       N  
ATOM   3689  CA  ARG B  77     -20.809  -7.218  -0.279  1.00 76.55           C  
ANISOU 3689  CA  ARG B  77    10778  10604   7702   1505      5   -697       C  
ATOM   3690  C   ARG B  77     -21.633  -8.386   0.271  1.00 81.67           C  
ANISOU 3690  C   ARG B  77    11602  11073   8355   1173   -143   -996       C  
ATOM   3691  O   ARG B  77     -22.394  -8.201   1.224  1.00 80.46           O  
ANISOU 3691  O   ARG B  77    11331  10868   8371    929   -219   -978       O  
ATOM   3692  CB  ARG B  77     -21.617  -6.325  -1.226  1.00 73.89           C  
ANISOU 3692  CB  ARG B  77    10228  10686   7161   1599    -46   -606       C  
ATOM   3693  CG  ARG B  77     -20.941  -4.979  -1.476  1.00 74.65           C  
ANISOU 3693  CG  ARG B  77    10128  10892   7344   1871    123   -248       C  
ATOM   3694  CD  ARG B  77     -21.764  -4.079  -2.372  1.00 81.50           C  
ANISOU 3694  CD  ARG B  77    10782  12163   8020   2004     98   -105       C  
ATOM   3695  NE  ARG B  77     -22.830  -3.399  -1.635  1.00 86.86           N  
ANISOU 3695  NE  ARG B  77    11272  12880   8852   1852     49    -15       N  
ATOM   3696  CZ  ARG B  77     -23.792  -2.675  -2.197  1.00102.76           C  
ANISOU 3696  CZ  ARG B  77    13070  15251  10724   1946     17    125       C  
ATOM   3697  NH1 ARG B  77     -23.855  -2.552  -3.518  1.00 93.27           N  
ANISOU 3697  NH1 ARG B  77    11807  14428   9203   2164      2    182       N  
ATOM   3698  NH2 ARG B  77     -24.717  -2.099  -1.448  1.00 91.15           N  
ANISOU 3698  NH2 ARG B  77    11436  13792   9405   1843      6    219       N  
ATOM   3699  N   LEU B  78     -21.425  -9.597  -0.293  1.00 80.47           N  
ANISOU 3699  N   LEU B  78    11754  10795   8024   1169   -158  -1264       N  
ATOM   3700  CA  LEU B  78     -22.036 -10.842   0.161  1.00 81.48           C  
ANISOU 3700  CA  LEU B  78    12125  10669   8164    849   -262  -1556       C  
ATOM   3701  C   LEU B  78     -21.279 -11.301   1.409  1.00 83.56           C  
ANISOU 3701  C   LEU B  78    12497  10519   8731    832   -156  -1457       C  
ATOM   3702  O   LEU B  78     -21.910 -11.790   2.348  1.00 82.31           O  
ANISOU 3702  O   LEU B  78    12374  10177   8724    531   -234  -1531       O  
ATOM   3703  CB  LEU B  78     -21.982 -11.914  -0.946  1.00 85.39           C  
ANISOU 3703  CB  LEU B  78    12964  11131   8350    873   -275  -1885       C  
ATOM   3704  CG  LEU B  78     -22.448 -13.328  -0.580  1.00 92.14           C  
ANISOU 3704  CG  LEU B  78    14167  11625   9215    543   -339  -2214       C  
ATOM   3705  CD1 LEU B  78     -23.958 -13.446  -0.627  1.00 93.89           C  
ANISOU 3705  CD1 LEU B  78    14275  12075   9325    103   -579  -2403       C  
ATOM   3706  CD2 LEU B  78     -21.824 -14.354  -1.487  1.00 97.77           C  
ANISOU 3706  CD2 LEU B  78    15313  12135   9698    702   -231  -2484       C  
ATOM   3707  N   HIS B  79     -19.930 -11.110   1.430  1.00 80.00           N  
ANISOU 3707  N   HIS B  79    12066   9974   8359   1156     23  -1255       N  
ATOM   3708  CA  HIS B  79     -19.066 -11.455   2.574  1.00 78.66           C  
ANISOU 3708  CA  HIS B  79    11940   9501   8444   1189    129  -1097       C  
ATOM   3709  C   HIS B  79     -19.477 -10.642   3.789  1.00 79.87           C  
ANISOU 3709  C   HIS B  79    11828   9687   8831    974     65   -921       C  
ATOM   3710  O   HIS B  79     -19.488 -11.176   4.897  1.00 79.17           O  
ANISOU 3710  O   HIS B  79    11798   9366   8915    809     57   -906       O  
ATOM   3711  CB  HIS B  79     -17.573 -11.206   2.275  1.00 79.46           C  
ANISOU 3711  CB  HIS B  79    12012   9628   8553   1577    319   -861       C  
ATOM   3712  CG  HIS B  79     -16.850 -12.342   1.614  1.00 86.07           C  
ANISOU 3712  CG  HIS B  79    13178  10278   9246   1833    456   -988       C  
ATOM   3713  ND1 HIS B  79     -17.026 -13.654   2.021  1.00 89.92           N  
ANISOU 3713  ND1 HIS B  79    13999  10394   9772   1726    474  -1186       N  
ATOM   3714  CD2 HIS B  79     -15.912 -12.312   0.642  1.00 89.48           C  
ANISOU 3714  CD2 HIS B  79    13657  10830   9510   2210    614   -914       C  
ATOM   3715  CE1 HIS B  79     -16.230 -14.376   1.254  1.00 92.12           C  
ANISOU 3715  CE1 HIS B  79    14545  10557   9900   2053    647  -1251       C  
ATOM   3716  NE2 HIS B  79     -15.538 -13.616   0.413  1.00 92.39           N  
ANISOU 3716  NE2 HIS B  79    14408  10898   9798   2359    735  -1092       N  
ATOM   3717  N   LEU B  80     -19.847  -9.362   3.571  1.00 74.91           N  
ANISOU 3717  N   LEU B  80    10928   9340   8195    987     35   -788       N  
ATOM   3718  CA  LEU B  80     -20.305  -8.443   4.609  1.00 72.39           C  
ANISOU 3718  CA  LEU B  80    10382   9058   8065    813      4   -643       C  
ATOM   3719  C   LEU B  80     -21.609  -8.903   5.241  1.00 76.31           C  
ANISOU 3719  C   LEU B  80    10887   9513   8593    488   -132   -807       C  
ATOM   3720  O   LEU B  80     -21.736  -8.809   6.455  1.00 74.66           O  
ANISOU 3720  O   LEU B  80    10620   9184   8564    322   -133   -735       O  
ATOM   3721  CB  LEU B  80     -20.476  -7.026   4.049  1.00 71.92           C  
ANISOU 3721  CB  LEU B  80    10089   9270   7969    943     41   -476       C  
ATOM   3722  CG  LEU B  80     -19.425  -6.000   4.450  1.00 75.32           C  
ANISOU 3722  CG  LEU B  80    10385   9681   8554   1066    176   -206       C  
ATOM   3723  CD1 LEU B  80     -19.532  -4.761   3.580  1.00 75.78           C  
ANISOU 3723  CD1 LEU B  80    10281   9968   8544   1241    246    -46       C  
ATOM   3724  CD2 LEU B  80     -19.564  -5.612   5.913  1.00 76.66           C  
ANISOU 3724  CD2 LEU B  80    10481   9707   8940    837    171   -144       C  
ATOM   3725  N   SER B  81     -22.571  -9.402   4.430  1.00 74.46           N  
ANISOU 3725  N   SER B  81    10713   9412   8167    379   -248  -1021       N  
ATOM   3726  CA  SER B  81     -23.860  -9.883   4.935  1.00 74.54           C  
ANISOU 3726  CA  SER B  81    10698   9436   8187     35   -387  -1166       C  
ATOM   3727  C   SER B  81     -23.725 -11.122   5.808  1.00 78.15           C  
ANISOU 3727  C   SER B  81    11393   9529   8772   -169   -387  -1273       C  
ATOM   3728  O   SER B  81     -24.427 -11.216   6.810  1.00 77.29           O  
ANISOU 3728  O   SER B  81    11201   9374   8792   -420   -436  -1251       O  
ATOM   3729  CB  SER B  81     -24.857 -10.102   3.804  1.00 80.16           C  
ANISOU 3729  CB  SER B  81    11387  10437   8633    -66   -527  -1356       C  
ATOM   3730  OG  SER B  81     -25.285  -8.844   3.307  1.00 86.74           O  
ANISOU 3730  OG  SER B  81    11926  11646   9387     89   -530  -1186       O  
ATOM   3731  N   VAL B  82     -22.789 -12.034   5.476  1.00 75.20           N  
ANISOU 3731  N   VAL B  82    11310   8893   8369    -28   -303  -1354       N  
ATOM   3732  CA  VAL B  82     -22.505 -13.230   6.279  1.00 75.41           C  
ANISOU 3732  CA  VAL B  82    11596   8529   8529   -148   -256  -1405       C  
ATOM   3733  C   VAL B  82     -21.898 -12.761   7.611  1.00 75.71           C  
ANISOU 3733  C   VAL B  82    11478   8494   8794   -103   -181  -1130       C  
ATOM   3734  O   VAL B  82     -22.257 -13.285   8.666  1.00 75.60           O  
ANISOU 3734  O   VAL B  82    11500   8310   8915   -322   -198  -1107       O  
ATOM   3735  CB  VAL B  82     -21.593 -14.251   5.532  1.00 81.86           C  
ANISOU 3735  CB  VAL B  82    12775   9080   9247     76   -137  -1529       C  
ATOM   3736  CG1 VAL B  82     -21.341 -15.500   6.375  1.00 83.11           C  
ANISOU 3736  CG1 VAL B  82    13222   8798   9559    -17    -56  -1547       C  
ATOM   3737  CG2 VAL B  82     -22.182 -14.641   4.174  1.00 84.66           C  
ANISOU 3737  CG2 VAL B  82    13301   9542   9325     14   -216  -1837       C  
ATOM   3738  N   ALA B  83     -21.031 -11.726   7.552  1.00 69.69           N  
ANISOU 3738  N   ALA B  83    10530   7892   8056    148   -103   -922       N  
ATOM   3739  CA  ALA B  83     -20.383 -11.111   8.711  1.00 67.24           C  
ANISOU 3739  CA  ALA B  83    10053   7581   7915    167    -46   -679       C  
ATOM   3740  C   ALA B  83     -21.373 -10.339   9.591  1.00 69.29           C  
ANISOU 3740  C   ALA B  83    10106   7966   8256    -81   -120   -649       C  
ATOM   3741  O   ALA B  83     -21.347 -10.504  10.809  1.00 68.04           O  
ANISOU 3741  O   ALA B  83     9924   7712   8216   -222   -114   -563       O  
ATOM   3742  CB  ALA B  83     -19.259 -10.192   8.257  1.00 66.98           C  
ANISOU 3742  CB  ALA B  83     9885   7700   7865    445     49   -492       C  
ATOM   3743  N   ASP B  84     -22.253  -9.523   8.980  1.00 66.08           N  
ANISOU 3743  N   ASP B  84     9549   7791   7767   -108   -174   -704       N  
ATOM   3744  CA  ASP B  84     -23.235  -8.701   9.688  1.00 65.38           C  
ANISOU 3744  CA  ASP B  84     9260   7844   7738   -273   -205   -661       C  
ATOM   3745  C   ASP B  84     -24.423  -9.475  10.236  1.00 70.43           C  
ANISOU 3745  C   ASP B  84     9915   8458   8388   -568   -300   -779       C  
ATOM   3746  O   ASP B  84     -24.844  -9.195  11.359  1.00 69.22           O  
ANISOU 3746  O   ASP B  84     9661   8308   8332   -712   -285   -706       O  
ATOM   3747  CB  ASP B  84     -23.696  -7.512   8.832  1.00 67.77           C  
ANISOU 3747  CB  ASP B  84     9383   8413   7954   -132   -192   -616       C  
ATOM   3748  CG  ASP B  84     -22.601  -6.500   8.499  1.00 83.49           C  
ANISOU 3748  CG  ASP B  84    11323  10426   9974    115    -72   -448       C  
ATOM   3749  OD1 ASP B  84     -21.834  -6.121   9.417  1.00 83.64           O  
ANISOU 3749  OD1 ASP B  84    11330  10328  10121     91     -1   -332       O  
ATOM   3750  OD2 ASP B  84     -22.575  -6.013   7.349  1.00 91.67           O  
ANISOU 3750  OD2 ASP B  84    12308  11626  10894    305    -52   -421       O  
ATOM   3751  N   LEU B  85     -24.962 -10.446   9.462  1.00 69.20           N  
ANISOU 3751  N   LEU B  85     9890   8284   8120   -681   -392   -967       N  
ATOM   3752  CA  LEU B  85     -26.103 -11.279   9.864  1.00 70.55           C  
ANISOU 3752  CA  LEU B  85    10079   8434   8294  -1019   -491  -1086       C  
ATOM   3753  C   LEU B  85     -25.772 -12.087  11.118  1.00 74.26           C  
ANISOU 3753  C   LEU B  85    10687   8603   8924  -1158   -441  -1023       C  
ATOM   3754  O   LEU B  85     -26.598 -12.157  12.029  1.00 73.53           O  
ANISOU 3754  O   LEU B  85    10484   8554   8901  -1391   -467   -981       O  
ATOM   3755  CB  LEU B  85     -26.545 -12.203   8.719  1.00 73.65           C  
ANISOU 3755  CB  LEU B  85    10640   8827   8517  -1143   -595  -1328       C  
ATOM   3756  CG  LEU B  85     -27.776 -13.052   8.968  1.00 81.18           C  
ANISOU 3756  CG  LEU B  85    11599   9792   9454  -1557   -716  -1466       C  
ATOM   3757  CD1 LEU B  85     -28.915 -12.622   8.082  1.00 83.42           C  
ANISOU 3757  CD1 LEU B  85    11646  10510   9540  -1675   -859  -1548       C  
ATOM   3758  CD2 LEU B  85     -27.469 -14.517   8.754  1.00 86.48           C  
ANISOU 3758  CD2 LEU B  85    12661  10075  10122  -1714   -713  -1664       C  
ATOM   3759  N   LEU B  86     -24.555 -12.672  11.172  1.00 71.39           N  
ANISOU 3759  N   LEU B  86    10545   7970   8611   -987   -353   -983       N  
ATOM   3760  CA  LEU B  86     -24.092 -13.444  12.324  1.00 71.68           C  
ANISOU 3760  CA  LEU B  86    10708   7743   8785  -1053   -288   -869       C  
ATOM   3761  C   LEU B  86     -24.081 -12.555  13.567  1.00 73.17           C  
ANISOU 3761  C   LEU B  86    10665   8077   9058  -1083   -260   -678       C  
ATOM   3762  O   LEU B  86     -24.506 -13.002  14.635  1.00 73.12           O  
ANISOU 3762  O   LEU B  86    10654   8001   9127  -1281   -258   -612       O  
ATOM   3763  CB  LEU B  86     -22.695 -14.030  12.066  1.00 72.44           C  
ANISOU 3763  CB  LEU B  86    11022   7605   8897   -772   -177   -802       C  
ATOM   3764  CG  LEU B  86     -22.566 -15.538  12.262  1.00 79.84           C  
ANISOU 3764  CG  LEU B  86    12287   8158   9892   -840   -118   -849       C  
ATOM   3765  CD1 LEU B  86     -21.333 -16.060  11.579  1.00 81.55           C  
ANISOU 3765  CD1 LEU B  86    12729   8182  10072   -494      9   -827       C  
ATOM   3766  CD2 LEU B  86     -22.540 -15.913  13.737  1.00 81.00           C  
ANISOU 3766  CD2 LEU B  86    12402   8194  10179   -963    -78   -645       C  
ATOM   3767  N   PHE B  87     -23.653 -11.280  13.407  1.00 67.22           N  
ANISOU 3767  N   PHE B  87     9734   7525   8279   -905   -230   -599       N  
ATOM   3768  CA  PHE B  87     -23.652 -10.315  14.493  1.00 65.01           C  
ANISOU 3768  CA  PHE B  87     9277   7374   8051   -945   -191   -468       C  
ATOM   3769  C   PHE B  87     -25.072  -9.918  14.892  1.00 69.58           C  
ANISOU 3769  C   PHE B  87     9701   8116   8620  -1142   -226   -515       C  
ATOM   3770  O   PHE B  87     -25.336  -9.819  16.093  1.00 69.00           O  
ANISOU 3770  O   PHE B  87     9567   8060   8589  -1273   -196   -438       O  
ATOM   3771  CB  PHE B  87     -22.789  -9.085  14.193  1.00 65.13           C  
ANISOU 3771  CB  PHE B  87     9190   7503   8053   -738   -130   -383       C  
ATOM   3772  CG  PHE B  87     -22.835  -8.085  15.328  1.00 65.48           C  
ANISOU 3772  CG  PHE B  87     9106   7641   8134   -824    -81   -298       C  
ATOM   3773  CD1 PHE B  87     -23.508  -6.880  15.186  1.00 68.25           C  
ANISOU 3773  CD1 PHE B  87     9333   8127   8470   -804    -37   -322       C  
ATOM   3774  CD2 PHE B  87     -22.275  -8.386  16.566  1.00 67.13           C  
ANISOU 3774  CD2 PHE B  87     9331   7802   8371   -923    -67   -195       C  
ATOM   3775  CE1 PHE B  87     -23.588  -5.978  16.247  1.00 68.62           C  
ANISOU 3775  CE1 PHE B  87     9321   8216   8537   -885     36   -281       C  
ATOM   3776  CE2 PHE B  87     -22.372  -7.492  17.629  1.00 69.30           C  
ANISOU 3776  CE2 PHE B  87     9518   8173   8639  -1031    -23   -159       C  
ATOM   3777  CZ  PHE B  87     -23.015  -6.289  17.459  1.00 67.18           C  
ANISOU 3777  CZ  PHE B  87     9173   7992   8362  -1015     36   -221       C  
ATOM   3778  N   VAL B  88     -25.984  -9.689  13.912  1.00 66.86           N  
ANISOU 3778  N   VAL B  88     9273   7933   8199  -1151   -284   -621       N  
ATOM   3779  CA  VAL B  88     -27.368  -9.340  14.255  1.00 67.05           C  
ANISOU 3779  CA  VAL B  88     9102   8171   8201  -1311   -308   -626       C  
ATOM   3780  C   VAL B  88     -28.066 -10.474  15.011  1.00 72.82           C  
ANISOU 3780  C   VAL B  88     9875   8818   8974  -1612   -358   -645       C  
ATOM   3781  O   VAL B  88     -28.755 -10.198  15.991  1.00 73.20           O  
ANISOU 3781  O   VAL B  88     9784   8978   9049  -1729   -318   -565       O  
ATOM   3782  CB  VAL B  88     -28.237  -8.646  13.170  1.00 71.62           C  
ANISOU 3782  CB  VAL B  88     9502   9040   8672  -1228   -349   -665       C  
ATOM   3783  CG1 VAL B  88     -27.585  -7.366  12.667  1.00 69.88           C  
ANISOU 3783  CG1 VAL B  88     9232   8880   8439   -927   -254   -585       C  
ATOM   3784  CG2 VAL B  88     -28.577  -9.577  12.017  1.00 73.65           C  
ANISOU 3784  CG2 VAL B  88     9837   9330   8818  -1331   -483   -822       C  
ATOM   3785  N   ILE B  89     -27.768 -11.751  14.633  1.00 70.38           N  
ANISOU 3785  N   ILE B  89     9792   8273   8676  -1719   -412   -738       N  
ATOM   3786  CA  ILE B  89     -28.257 -12.983  15.276  1.00 72.00           C  
ANISOU 3786  CA  ILE B  89    10110   8301   8946  -2014   -437   -747       C  
ATOM   3787  C   ILE B  89     -27.955 -12.996  16.802  1.00 74.01           C  
ANISOU 3787  C   ILE B  89    10345   8481   9294  -2045   -347   -560       C  
ATOM   3788  O   ILE B  89     -28.721 -13.585  17.561  1.00 75.10           O  
ANISOU 3788  O   ILE B  89    10450   8610   9473  -2297   -350   -509       O  
ATOM   3789  CB  ILE B  89     -27.721 -14.246  14.516  1.00 77.14           C  
ANISOU 3789  CB  ILE B  89    11089   8622   9598  -2045   -460   -884       C  
ATOM   3790  CG1 ILE B  89     -28.771 -14.796  13.530  1.00 80.35           C  
ANISOU 3790  CG1 ILE B  89    11515   9110   9905  -2310   -587  -1097       C  
ATOM   3791  CG2 ILE B  89     -27.200 -15.361  15.447  1.00 78.96           C  
ANISOU 3791  CG2 ILE B  89    11550   8495   9955  -2122   -379   -780       C  
ATOM   3792  CD1 ILE B  89     -28.200 -15.607  12.331  1.00 89.36           C  
ANISOU 3792  CD1 ILE B  89    12982  10006  10966  -2251   -605  -1310       C  
ATOM   3793  N   THR B  90     -26.855 -12.337  17.234  1.00 67.43           N  
ANISOU 3793  N   THR B  90     9517   7630   8473  -1810   -272   -454       N  
ATOM   3794  CA  THR B  90     -26.457 -12.256  18.642  1.00 66.10           C  
ANISOU 3794  CA  THR B  90     9322   7455   8340  -1831   -202   -286       C  
ATOM   3795  C   THR B  90     -27.109 -11.097  19.387  1.00 69.07           C  
ANISOU 3795  C   THR B  90     9479   8096   8670  -1858   -157   -250       C  
ATOM   3796  O   THR B  90     -27.111 -11.103  20.619  1.00 69.63           O  
ANISOU 3796  O   THR B  90     9517   8207   8733  -1940   -105   -139       O  
ATOM   3797  CB  THR B  90     -24.935 -12.205  18.801  1.00 70.23           C  
ANISOU 3797  CB  THR B  90     9944   7870   8871  -1612   -158   -182       C  
ATOM   3798  OG1 THR B  90     -24.439 -10.958  18.321  1.00 66.10           O  
ANISOU 3798  OG1 THR B  90     9318   7494   8302  -1433   -143   -212       O  
ATOM   3799  CG2 THR B  90     -24.234 -13.373  18.144  1.00 70.29           C  
ANISOU 3799  CG2 THR B  90    10185   7600   8921  -1519   -153   -187       C  
ATOM   3800  N   LEU B  91     -27.668 -10.107  18.659  1.00 64.08           N  
ANISOU 3800  N   LEU B  91     8708   7646   7992  -1768   -158   -333       N  
ATOM   3801  CA  LEU B  91     -28.314  -8.941  19.275  1.00 62.87           C  
ANISOU 3801  CA  LEU B  91     8381   7709   7796  -1736    -71   -302       C  
ATOM   3802  C   LEU B  91     -29.460  -9.179  20.293  1.00 67.69           C  
ANISOU 3802  C   LEU B  91     8864   8465   8392  -1930    -32   -237       C  
ATOM   3803  O   LEU B  91     -29.580  -8.344  21.193  1.00 67.62           O  
ANISOU 3803  O   LEU B  91     8793   8562   8337  -1881     79   -195       O  
ATOM   3804  CB  LEU B  91     -28.591  -7.800  18.291  1.00 62.15           C  
ANISOU 3804  CB  LEU B  91     8185   7759   7670  -1539    -42   -355       C  
ATOM   3805  CG  LEU B  91     -27.337  -7.060  17.826  1.00 64.85           C  
ANISOU 3805  CG  LEU B  91     8625   7993   8022  -1331     -5   -361       C  
ATOM   3806  CD1 LEU B  91     -27.562  -6.375  16.529  1.00 64.77           C  
ANISOU 3806  CD1 LEU B  91     8544   8082   7982  -1146     -5   -394       C  
ATOM   3807  CD2 LEU B  91     -26.829  -6.087  18.871  1.00 65.70           C  
ANISOU 3807  CD2 LEU B  91     8752   8088   8123  -1303    112   -320       C  
ATOM   3808  N   PRO B  92     -30.264 -10.285  20.267  1.00 64.74           N  
ANISOU 3808  N   PRO B  92     8462   8092   8045  -2165   -102   -225       N  
ATOM   3809  CA  PRO B  92     -31.242 -10.483  21.352  1.00 65.54           C  
ANISOU 3809  CA  PRO B  92     8423   8350   8129  -2347    -43   -120       C  
ATOM   3810  C   PRO B  92     -30.526 -10.677  22.693  1.00 67.65           C  
ANISOU 3810  C   PRO B  92     8798   8518   8388  -2366     31    -10       C  
ATOM   3811  O   PRO B  92     -30.983 -10.145  23.702  1.00 67.25           O  
ANISOU 3811  O   PRO B  92     8642   8645   8267  -2373    135     58       O  
ATOM   3812  CB  PRO B  92     -31.995 -11.756  20.934  1.00 69.80           C  
ANISOU 3812  CB  PRO B  92     8957   8846   8718  -2638   -149   -131       C  
ATOM   3813  CG  PRO B  92     -31.696 -11.943  19.498  1.00 74.20           C  
ANISOU 3813  CG  PRO B  92     9609   9309   9277  -2584   -261   -284       C  
ATOM   3814  CD  PRO B  92     -30.328 -11.404  19.303  1.00 67.46           C  
ANISOU 3814  CD  PRO B  92     8917   8287   8427  -2300   -224   -311       C  
ATOM   3815  N   PHE B  93     -29.353 -11.372  22.689  1.00 63.45           N  
ANISOU 3815  N   PHE B  93     8471   7733   7902  -2339    -12     16       N  
ATOM   3816  CA  PHE B  93     -28.517 -11.615  23.879  1.00 63.06           C  
ANISOU 3816  CA  PHE B  93     8507   7632   7819  -2336     37    155       C  
ATOM   3817  C   PHE B  93     -28.057 -10.308  24.502  1.00 64.69           C  
ANISOU 3817  C   PHE B  93     8662   8003   7914  -2202    109    130       C  
ATOM   3818  O   PHE B  93     -28.059 -10.184  25.725  1.00 65.03           O  
ANISOU 3818  O   PHE B  93     8679   8168   7861  -2264    174    217       O  
ATOM   3819  CB  PHE B  93     -27.296 -12.490  23.559  1.00 65.01           C  
ANISOU 3819  CB  PHE B  93     8953   7618   8131  -2258    -10    212       C  
ATOM   3820  CG  PHE B  93     -27.619 -13.889  23.102  1.00 68.87           C  
ANISOU 3820  CG  PHE B  93     9581   7856   8730  -2399    -44    231       C  
ATOM   3821  CD1 PHE B  93     -27.671 -14.937  24.009  1.00 73.84           C  
ANISOU 3821  CD1 PHE B  93    10290   8364   9400  -2536      1    416       C  
ATOM   3822  CD2 PHE B  93     -27.816 -14.170  21.755  1.00 71.40           C  
ANISOU 3822  CD2 PHE B  93     9983   8045   9102  -2397   -112     62       C  
ATOM   3823  CE1 PHE B  93     -27.952 -16.239  23.582  1.00 77.08           C  
ANISOU 3823  CE1 PHE B  93    10884   8472   9930  -2688     -5    424       C  
ATOM   3824  CE2 PHE B  93     -28.093 -15.472  21.330  1.00 76.49           C  
ANISOU 3824  CE2 PHE B  93    10813   8414   9835  -2565   -134     37       C  
ATOM   3825  CZ  PHE B  93     -28.154 -16.498  22.245  1.00 76.51           C  
ANISOU 3825  CZ  PHE B  93    10920   8243   9905  -2715    -73    214       C  
ATOM   3826  N   TRP B  94     -27.698  -9.327  23.656  1.00 59.23           N  
ANISOU 3826  N   TRP B  94     7969   7312   7223  -2036    108      5       N  
ATOM   3827  CA  TRP B  94     -27.292  -7.985  24.071  1.00 58.18           C  
ANISOU 3827  CA  TRP B  94     7829   7275   7003  -1934    192    -55       C  
ATOM   3828  C   TRP B  94     -28.457  -7.304  24.800  1.00 63.46           C  
ANISOU 3828  C   TRP B  94     8392   8129   7592  -1963    319    -77       C  
ATOM   3829  O   TRP B  94     -28.247  -6.733  25.871  1.00 64.00           O  
ANISOU 3829  O   TRP B  94     8495   8281   7541  -1989    406    -84       O  
ATOM   3830  CB  TRP B  94     -26.887  -7.147  22.846  1.00 55.66           C  
ANISOU 3830  CB  TRP B  94     7527   6889   6731  -1756    185   -158       C  
ATOM   3831  CG  TRP B  94     -25.572  -7.523  22.226  1.00 55.83           C  
ANISOU 3831  CG  TRP B  94     7645   6771   6798  -1680    101   -132       C  
ATOM   3832  CD1 TRP B  94     -25.305  -8.623  21.464  1.00 58.99           C  
ANISOU 3832  CD1 TRP B  94     8107   7038   7269  -1658     15   -102       C  
ATOM   3833  CD2 TRP B  94     -24.367  -6.741  22.241  1.00 54.84           C  
ANISOU 3833  CD2 TRP B  94     7562   6633   6642  -1607    115   -133       C  
ATOM   3834  NE1 TRP B  94     -23.996  -8.598  21.040  1.00 57.79           N  
ANISOU 3834  NE1 TRP B  94     8020   6809   7127  -1532    -11    -63       N  
ATOM   3835  CE2 TRP B  94     -23.399  -7.448  21.495  1.00 58.42           C  
ANISOU 3835  CE2 TRP B  94     8065   6984   7149  -1515     38    -69       C  
ATOM   3836  CE3 TRP B  94     -24.009  -5.509  22.819  1.00 55.66           C  
ANISOU 3836  CE3 TRP B  94     7679   6798   6673  -1630    195   -188       C  
ATOM   3837  CZ2 TRP B  94     -22.095  -6.965  21.313  1.00 57.12           C  
ANISOU 3837  CZ2 TRP B  94     7906   6828   6968  -1440     29    -21       C  
ATOM   3838  CZ3 TRP B  94     -22.721  -5.034  22.638  1.00 56.62           C  
ANISOU 3838  CZ3 TRP B  94     7829   6900   6783  -1609    172   -167       C  
ATOM   3839  CH2 TRP B  94     -21.779  -5.757  21.895  1.00 56.85           C  
ANISOU 3839  CH2 TRP B  94     7852   6880   6867  -1513     85    -66       C  
ATOM   3840  N   ALA B  95     -29.684  -7.408  24.230  1.00 60.08           N  
ANISOU 3840  N   ALA B  95     7825   7794   7208  -1964    330    -81       N  
ATOM   3841  CA  ALA B  95     -30.906  -6.818  24.770  1.00 61.10           C  
ANISOU 3841  CA  ALA B  95     7807   8139   7268  -1944    469    -62       C  
ATOM   3842  C   ALA B  95     -31.303  -7.438  26.106  1.00 67.81           C  
ANISOU 3842  C   ALA B  95     8622   9104   8039  -2114    519     51       C  
ATOM   3843  O   ALA B  95     -31.524  -6.693  27.066  1.00 68.42           O  
ANISOU 3843  O   ALA B  95     8703   9305   7990  -2063    669     37       O  
ATOM   3844  CB  ALA B  95     -32.039  -6.936  23.764  1.00 62.55           C  
ANISOU 3844  CB  ALA B  95     7799   8460   7507  -1922    436    -47       C  
ATOM   3845  N   VAL B  96     -31.365  -8.794  26.179  1.00 65.18           N  
ANISOU 3845  N   VAL B  96     8282   8711   7772  -2312    411    161       N  
ATOM   3846  CA  VAL B  96     -31.710  -9.532  27.401  1.00 66.40           C  
ANISOU 3846  CA  VAL B  96     8403   8960   7866  -2485    458    317       C  
ATOM   3847  C   VAL B  96     -30.748  -9.129  28.521  1.00 70.73           C  
ANISOU 3847  C   VAL B  96     9079   9527   8269  -2441    513    327       C  
ATOM   3848  O   VAL B  96     -31.210  -8.735  29.589  1.00 72.15           O  
ANISOU 3848  O   VAL B  96     9210   9906   8299  -2454    641    363       O  
ATOM   3849  CB  VAL B  96     -31.769 -11.072  27.200  1.00 71.04           C  
ANISOU 3849  CB  VAL B  96     9025   9389   8578  -2702    348    440       C  
ATOM   3850  CG1 VAL B  96     -32.133 -11.782  28.503  1.00 72.63           C  
ANISOU 3850  CG1 VAL B  96     9187   9692   8718  -2869    422    645       C  
ATOM   3851  CG2 VAL B  96     -32.758 -11.448  26.099  1.00 71.78           C  
ANISOU 3851  CG2 VAL B  96     8994   9503   8777  -2813    275    394       C  
ATOM   3852  N   ASP B  97     -29.427  -9.150  28.242  1.00 66.13           N  
ANISOU 3852  N   ASP B  97     8645   8777   7706  -2385    421    290       N  
ATOM   3853  CA  ASP B  97     -28.373  -8.763  29.182  1.00 66.35           C  
ANISOU 3853  CA  ASP B  97     8766   8866   7577  -2377    431    300       C  
ATOM   3854  C   ASP B  97     -28.272  -7.245  29.458  1.00 70.86           C  
ANISOU 3854  C   ASP B  97     9383   9526   8013  -2290    539    110       C  
ATOM   3855  O   ASP B  97     -27.509  -6.833  30.331  1.00 70.15           O  
ANISOU 3855  O   ASP B  97     9372   9529   7751  -2340    550     83       O  
ATOM   3856  CB  ASP B  97     -27.001  -9.257  28.682  1.00 67.19           C  
ANISOU 3856  CB  ASP B  97     8970   8807   7752  -2336    300    349       C  
ATOM   3857  CG  ASP B  97     -25.886  -8.233  28.675  1.00 77.38           C  
ANISOU 3857  CG  ASP B  97    10323  10125   8952  -2269    282    238       C  
ATOM   3858  OD1 ASP B  97     -25.810  -7.440  27.701  1.00 77.00           O  
ANISOU 3858  OD1 ASP B  97    10296   9975   8984  -2166    288     88       O  
ATOM   3859  OD2 ASP B  97     -25.078  -8.231  29.633  1.00 82.68           O  
ANISOU 3859  OD2 ASP B  97    11011  10940   9463  -2337    257    315       O  
ATOM   3860  N   ALA B  98     -29.041  -6.424  28.727  1.00 68.69           N  
ANISOU 3860  N   ALA B  98     9069   9227   7803  -2165    626    -14       N  
ATOM   3861  CA  ALA B  98     -29.051  -4.977  28.938  1.00 69.48           C  
ANISOU 3861  CA  ALA B  98     9256   9340   7801  -2057    777   -189       C  
ATOM   3862  C   ALA B  98     -30.289  -4.632  29.767  1.00 76.70           C  
ANISOU 3862  C   ALA B  98    10101  10447   8595  -2022    970   -182       C  
ATOM   3863  O   ALA B  98     -30.298  -3.608  30.454  1.00 77.85           O  
ANISOU 3863  O   ALA B  98    10369  10625   8585  -1968   1134   -317       O  
ATOM   3864  CB  ALA B  98     -29.169  -4.199  27.635  1.00 69.03           C  
ANISOU 3864  CB  ALA B  98     9203   9140   7885  -1878    803   -286       C  
ATOM   3865  N   VAL B  99     -31.266  -5.511  29.711  1.00 74.26           N  
ANISOU 3865  N   VAL B  99     9608  10257   8349  -2068    954    -26       N  
ATOM   3866  CA  VAL B  99     -32.527  -5.310  30.357  1.00 76.35           C  
ANISOU 3866  CA  VAL B  99     9741  10750   8519  -2021   1135     34       C  
ATOM   3867  C   VAL B  99     -32.427  -6.022  31.667  1.00 80.65           C  
ANISOU 3867  C   VAL B  99    10291  11444   8908  -2191   1142    153       C  
ATOM   3868  O   VAL B  99     -32.616  -5.430  32.704  1.00 82.50           O  
ANISOU 3868  O   VAL B  99    10587  11828   8932  -2155   1306    102       O  
ATOM   3869  CB  VAL B  99     -33.615  -5.888  29.507  1.00 81.20           C  
ANISOU 3869  CB  VAL B  99    10113  11454   9284  -2024   1094    160       C  
ATOM   3870  CG1 VAL B  99     -33.778  -5.088  28.284  1.00 80.33           C  
ANISOU 3870  CG1 VAL B  99     9976  11266   9278  -1822   1106     66       C  
ATOM   3871  CG2 VAL B  99     -33.271  -7.302  29.155  1.00 80.47           C  
ANISOU 3871  CG2 VAL B  99     9997  11258   9321  -2247    880    275       C  
ATOM   3872  N   ALA B 100     -32.140  -7.307  31.631  1.00 75.35           N  
ANISOU 3872  N   ALA B 100     9573  10729   8327  -2366    980    320       N  
ATOM   3873  CA  ALA B 100     -32.158  -8.067  32.854  1.00 76.18           C  
ANISOU 3873  CA  ALA B 100     9659  10995   8294  -2511   1003    496       C  
ATOM   3874  C   ALA B 100     -31.292  -8.974  33.672  1.00 80.37           C  
ANISOU 3874  C   ALA B 100    10259  11538   8741  -2649    910    661       C  
ATOM   3875  O   ALA B 100     -31.200  -8.874  34.873  1.00 81.74           O  
ANISOU 3875  O   ALA B 100    10454  11924   8679  -2685    990    717       O  
ATOM   3876  CB  ALA B 100     -33.183  -9.155  32.730  1.00 77.97           C  
ANISOU 3876  CB  ALA B 100     9693  11286   8646  -2648    992    711       C  
ATOM   3877  N   ASN B 101     -30.616  -9.868  32.939  1.00 75.20           N  
ANISOU 3877  N   ASN B 101     9647  10652   8274  -2701    744    745       N  
ATOM   3878  CA  ASN B 101     -29.642 -10.835  33.462  1.00 75.29           C  
ANISOU 3878  CA  ASN B 101     9730  10621   8258  -2773    649    945       C  
ATOM   3879  C   ASN B 101     -28.920 -11.572  32.309  1.00 78.03           C  
ANISOU 3879  C   ASN B 101    10158  10648   8843  -2745    504    969       C  
ATOM   3880  O   ASN B 101     -29.316 -11.450  31.150  1.00 75.90           O  
ANISOU 3880  O   ASN B 101     9879  10214   8747  -2714    469    834       O  
ATOM   3881  CB  ASN B 101     -30.297 -11.755  34.493  1.00 76.19           C  
ANISOU 3881  CB  ASN B 101     9758  10891   8301  -2903    729   1217       C  
ATOM   3882  CG  ASN B 101     -29.315 -12.732  35.109  1.00 91.24           C  
ANISOU 3882  CG  ASN B 101    11732  12773  10161  -2933    662   1477       C  
ATOM   3883  OD1 ASN B 101     -28.152 -12.795  34.712  1.00 83.17           O  
ANISOU 3883  OD1 ASN B 101    10802  11625   9174  -2851    549   1464       O  
ATOM   3884  ND2 ASN B 101     -29.780 -13.501  36.087  1.00 86.07           N  
ANISOU 3884  ND2 ASN B 101    11015  12263   9425  -3032    745   1749       N  
ATOM   3885  N   TRP B 102     -27.869 -12.330  32.633  1.00 75.83           N  
ANISOU 3885  N   TRP B 102     9954  10308   8550  -2734    434   1152       N  
ATOM   3886  CA  TRP B 102     -27.089 -13.078  31.654  1.00 74.80           C  
ANISOU 3886  CA  TRP B 102     9927   9878   8618  -2661    335   1199       C  
ATOM   3887  C   TRP B 102     -27.700 -14.373  32.177  1.00 80.72           C  
ANISOU 3887  C   TRP B 102    10679  10549   9441  -2790    392   1465       C  
ATOM   3888  O   TRP B 102     -27.699 -14.629  33.381  1.00 83.64           O  
ANISOU 3888  O   TRP B 102    11002  11128   9650  -2837    452   1674       O  
ATOM   3889  CB  TRP B 102     -25.563 -13.143  31.739  1.00 73.55           C  
ANISOU 3889  CB  TRP B 102     9826   9727   8394  -2532    255   1294       C  
ATOM   3890  CG  TRP B 102     -24.940 -14.011  30.690  1.00 74.55           C  
ANISOU 3890  CG  TRP B 102    10066   9526   8734  -2417    202   1358       C  
ATOM   3891  CD1 TRP B 102     -24.315 -15.209  30.882  1.00 79.27           C  
ANISOU 3891  CD1 TRP B 102    10746   9976   9396  -2342    214   1639       C  
ATOM   3892  CD2 TRP B 102     -24.883 -13.750  29.282  1.00 72.83           C  
ANISOU 3892  CD2 TRP B 102     9911   9084   8677  -2335    154   1143       C  
ATOM   3893  NE1 TRP B 102     -23.871 -15.709  29.682  1.00 78.25           N  
ANISOU 3893  NE1 TRP B 102    10751   9522   9459  -2213    189   1588       N  
ATOM   3894  CE2 TRP B 102     -24.207 -14.832  28.684  1.00 77.59           C  
ANISOU 3894  CE2 TRP B 102    10650   9406   9425  -2218    142   1280       C  
ATOM   3895  CE3 TRP B 102     -25.336 -12.706  28.470  1.00 72.43           C  
ANISOU 3895  CE3 TRP B 102     9821   9049   8651  -2325    137    867       C  
ATOM   3896  CZ2 TRP B 102     -23.975 -14.900  27.312  1.00 76.08           C  
ANISOU 3896  CZ2 TRP B 102    10560   8969   9377  -2109    105   1120       C  
ATOM   3897  CZ3 TRP B 102     -25.105 -12.776  27.108  1.00 72.90           C  
ANISOU 3897  CZ3 TRP B 102     9955   8887   8856  -2220     87    739       C  
ATOM   3898  CH2 TRP B 102     -24.430 -13.865  26.543  1.00 74.31           C  
ANISOU 3898  CH2 TRP B 102    10274   8808   9154  -2122     67    852       C  
ATOM   3899  N   TYR B 103     -28.222 -15.187  31.265  1.00 75.56           N  
ANISOU 3899  N   TYR B 103    10093   9597   9021  -2866    377   1455       N  
ATOM   3900  CA  TYR B 103     -28.855 -16.454  31.640  1.00 77.20           C  
ANISOU 3900  CA  TYR B 103    10337   9658   9338  -3040    441   1693       C  
ATOM   3901  C   TYR B 103     -28.210 -17.559  30.801  1.00 79.52           C  
ANISOU 3901  C   TYR B 103    10855   9517   9843  -2992    409   1754       C  
ATOM   3902  O   TYR B 103     -28.357 -18.739  31.116  1.00 81.95           O  
ANISOU 3902  O   TYR B 103    11277   9602  10260  -3093    479   1987       O  
ATOM   3903  CB  TYR B 103     -30.370 -16.495  31.374  1.00 79.23           C  
ANISOU 3903  CB  TYR B 103    10469   9959   9676  -3270    475   1615       C  
ATOM   3904  CG  TYR B 103     -31.187 -15.398  32.022  1.00 80.60           C  
ANISOU 3904  CG  TYR B 103    10424  10537   9663  -3277    546   1540       C  
ATOM   3905  CD1 TYR B 103     -31.500 -14.232  31.329  1.00 80.17           C  
ANISOU 3905  CD1 TYR B 103    10282  10601   9578  -3177    522   1269       C  
ATOM   3906  CD2 TYR B 103     -31.726 -15.563  33.295  1.00 83.79           C  
ANISOU 3906  CD2 TYR B 103    10717  11198   9924  -3368    664   1757       C  
ATOM   3907  CE1 TYR B 103     -32.288 -13.236  31.904  1.00 80.34           C  
ANISOU 3907  CE1 TYR B 103    10134  10955   9436  -3140    630   1209       C  
ATOM   3908  CE2 TYR B 103     -32.525 -14.579  33.876  1.00 84.93           C  
ANISOU 3908  CE2 TYR B 103    10680  11704   9885  -3343    764   1683       C  
ATOM   3909  CZ  TYR B 103     -32.803 -13.416  33.176  1.00 88.54           C  
ANISOU 3909  CZ  TYR B 103    11075  12241  10323  -3219    755   1405       C  
ATOM   3910  OH  TYR B 103     -33.581 -12.440  33.751  1.00 88.92           O  
ANISOU 3910  OH  TYR B 103    10978  12613  10194  -3146    895   1342       O  
ATOM   3911  N   PHE B 104     -27.530 -17.164  29.725  1.00 72.38           N  
ANISOU 3911  N   PHE B 104    10031   8477   8995  -2833    326   1546       N  
ATOM   3912  CA  PHE B 104     -26.952 -17.987  28.661  1.00 71.87           C  
ANISOU 3912  CA  PHE B 104    10193   8006   9108  -2744    304   1510       C  
ATOM   3913  C   PHE B 104     -25.652 -18.772  28.912  1.00 76.50           C  
ANISOU 3913  C   PHE B 104    10939   8411   9716  -2512    353   1766       C  
ATOM   3914  O   PHE B 104     -25.119 -19.382  27.982  1.00 76.32           O  
ANISOU 3914  O   PHE B 104    11123   8046   9827  -2385    362   1721       O  
ATOM   3915  CB  PHE B 104     -26.937 -17.192  27.338  1.00 70.82           C  
ANISOU 3915  CB  PHE B 104    10052   7851   9005  -2669    210   1181       C  
ATOM   3916  CG  PHE B 104     -28.127 -16.265  27.206  1.00 70.66           C  
ANISOU 3916  CG  PHE B 104     9828   8090   8930  -2821    181    990       C  
ATOM   3917  CD1 PHE B 104     -28.011 -14.912  27.504  1.00 71.21           C  
ANISOU 3917  CD1 PHE B 104     9737   8473   8848  -2710    175    890       C  
ATOM   3918  CD2 PHE B 104     -29.380 -16.758  26.852  1.00 73.76           C  
ANISOU 3918  CD2 PHE B 104    10186   8426   9415  -3082    176    933       C  
ATOM   3919  CE1 PHE B 104     -29.120 -14.063  27.417  1.00 71.61           C  
ANISOU 3919  CE1 PHE B 104     9610   8751   8850  -2790    191    751       C  
ATOM   3920  CE2 PHE B 104     -30.489 -15.907  26.769  1.00 75.80           C  
ANISOU 3920  CE2 PHE B 104    10209   8985   9608  -3182    165    812       C  
ATOM   3921  CZ  PHE B 104     -30.349 -14.566  27.049  1.00 71.89           C  
ANISOU 3921  CZ  PHE B 104     9570   8775   8971  -3002    186    732       C  
ATOM   3922  N   GLY B 105     -25.188 -18.803  30.155  1.00 74.00           N  
ANISOU 3922  N   GLY B 105    10527   8336   9254  -2448    396   2048       N  
ATOM   3923  CA  GLY B 105     -24.004 -19.568  30.535  1.00 75.56           C  
ANISOU 3923  CA  GLY B 105    10821   8444   9446  -2206    454   2371       C  
ATOM   3924  C   GLY B 105     -22.675 -19.036  30.046  1.00 77.65           C  
ANISOU 3924  C   GLY B 105    11050   8813   9642  -1924    387   2339       C  
ATOM   3925  O   GLY B 105     -22.618 -18.042  29.319  1.00 74.43           O  
ANISOU 3925  O   GLY B 105    10571   8505   9205  -1920    295   2043       O  
ATOM   3926  N   ASN B 106     -21.596 -19.717  30.446  1.00 76.82           N  
ANISOU 3926  N   ASN B 106    10979   8699   9509  -1676    447   2681       N  
ATOM   3927  CA  ASN B 106     -20.219 -19.334  30.139  1.00 76.21           C  
ANISOU 3927  CA  ASN B 106    10816   8795   9347  -1393    396   2752       C  
ATOM   3928  C   ASN B 106     -19.796 -19.448  28.678  1.00 79.09           C  
ANISOU 3928  C   ASN B 106    11345   8828   9876  -1212    406   2555       C  
ATOM   3929  O   ASN B 106     -19.130 -18.540  28.174  1.00 76.04           O  
ANISOU 3929  O   ASN B 106    10827   8652   9411  -1120    316   2414       O  
ATOM   3930  CB  ASN B 106     -19.241 -20.059  31.055  1.00 80.94           C  
ANISOU 3930  CB  ASN B 106    11354   9554   9845  -1158    467   3234       C  
ATOM   3931  CG  ASN B 106     -18.140 -19.165  31.545  1.00104.93           C  
ANISOU 3931  CG  ASN B 106    14103  13140  12624  -1062    345   3333       C  
ATOM   3932  OD1 ASN B 106     -18.254 -18.513  32.588  1.00 97.63           O  
ANISOU 3932  OD1 ASN B 106    12980  12657  11459  -1238    264   3361       O  
ATOM   3933  ND2 ASN B 106     -17.064 -19.089  30.782  1.00 98.78           N  
ANISOU 3933  ND2 ASN B 106    13296  12361  11876   -803    332   3369       N  
ATOM   3934  N   PHE B 107     -20.158 -20.569  28.010  1.00 78.02           N  
ANISOU 3934  N   PHE B 107    11512   8174   9957  -1172    526   2548       N  
ATOM   3935  CA  PHE B 107     -19.805 -20.853  26.611  1.00 77.61           C  
ANISOU 3935  CA  PHE B 107    11678   7767  10043   -992    565   2354       C  
ATOM   3936  C   PHE B 107     -20.387 -19.834  25.647  1.00 77.32           C  
ANISOU 3936  C   PHE B 107    11580   7800   9998  -1159    435   1920       C  
ATOM   3937  O   PHE B 107     -19.658 -19.297  24.809  1.00 75.46           O  
ANISOU 3937  O   PHE B 107    11307   7631   9734   -966    398   1805       O  
ATOM   3938  CB  PHE B 107     -20.207 -22.286  26.210  1.00 82.91           C  
ANISOU 3938  CB  PHE B 107    12738   7841  10925   -985    732   2398       C  
ATOM   3939  CG  PHE B 107     -19.937 -22.634  24.764  1.00 85.08           C  
ANISOU 3939  CG  PHE B 107    13289   7727  11310   -822    786   2151       C  
ATOM   3940  CD1 PHE B 107     -20.967 -22.647  23.830  1.00 87.80           C  
ANISOU 3940  CD1 PHE B 107    13801   7825  11736  -1103    731   1754       C  
ATOM   3941  CD2 PHE B 107     -18.650 -22.935  24.332  1.00 88.75           C  
ANISOU 3941  CD2 PHE B 107    13829   8122  11769   -382    893   2325       C  
ATOM   3942  CE1 PHE B 107     -20.716 -22.958  22.490  1.00 89.51           C  
ANISOU 3942  CE1 PHE B 107    14284   7719  12008   -962    776   1505       C  
ATOM   3943  CE2 PHE B 107     -18.400 -23.250  22.992  1.00 92.29           C  
ANISOU 3943  CE2 PHE B 107    14550   8226  12290   -210    964   2086       C  
ATOM   3944  CZ  PHE B 107     -19.435 -23.260  22.081  1.00 89.80           C  
ANISOU 3944  CZ  PHE B 107    14427   7657  12037   -509    902   1663       C  
ATOM   3945  N   LEU B 108     -21.695 -19.564  25.776  1.00 72.45           N  
ANISOU 3945  N   LEU B 108    10930   7199   9399  -1500    378   1717       N  
ATOM   3946  CA  LEU B 108     -22.395 -18.593  24.945  1.00 69.60           C  
ANISOU 3946  CA  LEU B 108    10482   6942   9021  -1652    267   1351       C  
ATOM   3947  C   LEU B 108     -21.918 -17.164  25.205  1.00 70.43           C  
ANISOU 3947  C   LEU B 108    10316   7481   8964  -1596    175   1297       C  
ATOM   3948  O   LEU B 108     -22.100 -16.309  24.338  1.00 67.93           O  
ANISOU 3948  O   LEU B 108     9946   7228   8638  -1599    110   1042       O  
ATOM   3949  CB  LEU B 108     -23.915 -18.729  25.113  1.00 70.18           C  
ANISOU 3949  CB  LEU B 108    10547   6974   9144  -2009    247   1217       C  
ATOM   3950  CG  LEU B 108     -24.731 -19.001  23.849  1.00 75.04           C  
ANISOU 3950  CG  LEU B 108    11311   7340   9861  -2163    208    915       C  
ATOM   3951  CD1 LEU B 108     -24.125 -20.123  23.006  1.00 77.61           C  
ANISOU 3951  CD1 LEU B 108    11982   7205  10302  -2011    292    902       C  
ATOM   3952  CD2 LEU B 108     -26.158 -19.349  24.202  1.00 78.26           C  
ANISOU 3952  CD2 LEU B 108    11678   7741  10317  -2539    199    876       C  
ATOM   3953  N   CYS B 109     -21.276 -16.912  26.375  1.00 67.16           N  
ANISOU 3953  N   CYS B 109     9742   7363   8412  -1550    174   1541       N  
ATOM   3954  CA  CYS B 109     -20.700 -15.605  26.703  1.00 65.14           C  
ANISOU 3954  CA  CYS B 109     9265   7498   7987  -1539     92   1487       C  
ATOM   3955  C   CYS B 109     -19.475 -15.378  25.817  1.00 70.00           C  
ANISOU 3955  C   CYS B 109     9873   8109   8614  -1285     74   1497       C  
ATOM   3956  O   CYS B 109     -19.310 -14.288  25.266  1.00 67.92           O  
ANISOU 3956  O   CYS B 109     9517   7977   8312  -1295     14   1301       O  
ATOM   3957  CB  CYS B 109     -20.349 -15.503  28.186  1.00 66.33           C  
ANISOU 3957  CB  CYS B 109     9263   7988   7951  -1599     85   1733       C  
ATOM   3958  SG  CYS B 109     -19.474 -13.977  28.639  1.00 68.65           S  
ANISOU 3958  SG  CYS B 109     9327   8747   8010  -1640    -19   1656       S  
ATOM   3959  N   LYS B 110     -18.637 -16.431  25.667  1.00 68.69           N  
ANISOU 3959  N   LYS B 110     9811   7778   8509  -1037    150   1747       N  
ATOM   3960  CA  LYS B 110     -17.431 -16.440  24.844  1.00 68.33           C  
ANISOU 3960  CA  LYS B 110     9758   7727   8476   -739    171   1822       C  
ATOM   3961  C   LYS B 110     -17.826 -16.316  23.375  1.00 71.69           C  
ANISOU 3961  C   LYS B 110    10346   7877   9018   -697    179   1513       C  
ATOM   3962  O   LYS B 110     -17.238 -15.500  22.664  1.00 69.94           O  
ANISOU 3962  O   LYS B 110    10021   7796   8758   -597    139   1419       O  
ATOM   3963  CB  LYS B 110     -16.639 -17.738  25.059  1.00 73.30           C  
ANISOU 3963  CB  LYS B 110    10500   8197   9155   -445    300   2181       C  
ATOM   3964  CG  LYS B 110     -16.125 -17.944  26.472  1.00 81.05           C  
ANISOU 3964  CG  LYS B 110    11294   9506   9993   -433    295   2555       C  
ATOM   3965  CD  LYS B 110     -15.647 -19.372  26.682  1.00 86.50           C  
ANISOU 3965  CD  LYS B 110    12151   9946  10770   -134    465   2927       C  
ATOM   3966  CE  LYS B 110     -14.968 -19.565  28.012  1.00 88.53           C  
ANISOU 3966  CE  LYS B 110    12177  10607  10853    -56    458   3363       C  
ATOM   3967  NZ  LYS B 110     -13.679 -18.829  28.090  1.00 93.59           N  
ANISOU 3967  NZ  LYS B 110    12491  11756  11312     88    363   3526       N  
ATOM   3968  N   ALA B 111     -18.845 -17.100  22.934  1.00 69.26           N  
ANISOU 3968  N   ALA B 111    10279   7202   8834   -803    226   1357       N  
ATOM   3969  CA  ALA B 111     -19.341 -17.100  21.553  1.00 68.50           C  
ANISOU 3969  CA  ALA B 111    10349   6869   8811   -802    219   1051       C  
ATOM   3970  C   ALA B 111     -19.843 -15.717  21.093  1.00 69.24           C  
ANISOU 3970  C   ALA B 111    10259   7210   8840   -941    107    798       C  
ATOM   3971  O   ALA B 111     -19.489 -15.302  19.989  1.00 68.02           O  
ANISOU 3971  O   ALA B 111    10120   7048   8676   -794     98    663       O  
ATOM   3972  CB  ALA B 111     -20.414 -18.160  21.365  1.00 71.21           C  
ANISOU 3972  CB  ALA B 111    10952   6836   9267   -989    264    936       C  
ATOM   3973  N   VAL B 112     -20.605 -14.979  21.941  1.00 64.10           N  
ANISOU 3973  N   VAL B 112     9440   6782   8134  -1185     47    757       N  
ATOM   3974  CA  VAL B 112     -21.062 -13.631  21.565  1.00 61.38           C  
ANISOU 3974  CA  VAL B 112     8943   6643   7736  -1270    -17    549       C  
ATOM   3975  C   VAL B 112     -19.886 -12.664  21.430  1.00 64.15           C  
ANISOU 3975  C   VAL B 112     9157   7204   8014  -1117    -32    606       C  
ATOM   3976  O   VAL B 112     -19.906 -11.790  20.558  1.00 62.33           O  
ANISOU 3976  O   VAL B 112     8883   7021   7780  -1069    -49    453       O  
ATOM   3977  CB  VAL B 112     -22.232 -13.032  22.395  1.00 64.41           C  
ANISOU 3977  CB  VAL B 112     9207   7190   8075  -1525    -38    473       C  
ATOM   3978  CG1 VAL B 112     -23.480 -13.900  22.312  1.00 65.56           C  
ANISOU 3978  CG1 VAL B 112     9445   7165   8298  -1710    -33    406       C  
ATOM   3979  CG2 VAL B 112     -21.838 -12.770  23.845  1.00 64.63           C  
ANISOU 3979  CG2 VAL B 112     9121   7441   7995  -1596    -28    651       C  
ATOM   3980  N   HIS B 113     -18.852 -12.848  22.277  1.00 61.53           N  
ANISOU 3980  N   HIS B 113     8744   7016   7617  -1047    -24    852       N  
ATOM   3981  CA  HIS B 113     -17.644 -12.033  22.250  1.00 60.96           C  
ANISOU 3981  CA  HIS B 113     8511   7187   7465   -952    -49    946       C  
ATOM   3982  C   HIS B 113     -16.847 -12.301  20.975  1.00 66.11           C  
ANISOU 3982  C   HIS B 113     9219   7725   8176   -673     -6    969       C  
ATOM   3983  O   HIS B 113     -16.347 -11.348  20.375  1.00 64.99           O  
ANISOU 3983  O   HIS B 113     8971   7713   8008   -633    -23    912       O  
ATOM   3984  CB  HIS B 113     -16.796 -12.248  23.515  1.00 63.03           C  
ANISOU 3984  CB  HIS B 113     8635   7705   7609   -972    -69   1226       C  
ATOM   3985  CG  HIS B 113     -17.229 -11.398  24.673  1.00 65.88           C  
ANISOU 3985  CG  HIS B 113     8886   8308   7837  -1252   -123   1160       C  
ATOM   3986  ND1 HIS B 113     -18.116 -11.662  25.661  1.00 67.95           N  
ANISOU 3986  ND1 HIS B 113     9178   8589   8051  -1422   -115   1158       N  
ATOM   3987  CD2 HIS B 113     -16.737 -10.117  24.853  1.00 66.78           C  
ANISOU 3987  CD2 HIS B 113     8866   8663   7844  -1383   -174   1075       C  
ATOM   3988  CE1 HIS B 113     -18.165 -10.547  26.460  1.00 66.89           C  
ANISOU 3988  CE1 HIS B 113     8940   8715   7760  -1631   -154   1056       C  
ATOM   3989  NE2 HIS B 113     -17.326  -9.656  25.943  1.00 66.62           N  
ANISOU 3989  NE2 HIS B 113     8826   8785   7702  -1614   -189   1000       N  
ATOM   3990  N   VAL B 114     -16.786 -13.577  20.525  1.00 64.34           N  
ANISOU 3990  N   VAL B 114     9187   7233   8028   -485     68   1037       N  
ATOM   3991  CA  VAL B 114     -16.059 -13.928  19.302  1.00 64.92           C  
ANISOU 3991  CA  VAL B 114     9355   7180   8133   -185    140   1045       C  
ATOM   3992  C   VAL B 114     -16.748 -13.428  18.038  1.00 67.69           C  
ANISOU 3992  C   VAL B 114     9792   7424   8505   -206    120    745       C  
ATOM   3993  O   VAL B 114     -16.076 -12.891  17.157  1.00 67.02           O  
ANISOU 3993  O   VAL B 114     9642   7433   8389    -33    141    739       O  
ATOM   3994  CB  VAL B 114     -15.557 -15.396  19.211  1.00 71.82           C  
ANISOU 3994  CB  VAL B 114    10434   7792   9060     82    268   1231       C  
ATOM   3995  CG1 VAL B 114     -14.817 -15.808  20.479  1.00 73.25           C  
ANISOU 3995  CG1 VAL B 114    10478   8154   9198    142    290   1593       C  
ATOM   3996  CG2 VAL B 114     -16.672 -16.382  18.880  1.00 72.85           C  
ANISOU 3996  CG2 VAL B 114    10881   7512   9285    -20    310   1035       C  
ATOM   3997  N   ILE B 115     -18.090 -13.574  17.968  1.00 63.63           N  
ANISOU 3997  N   ILE B 115     9388   6760   8027   -424     79    525       N  
ATOM   3998  CA  ILE B 115     -18.904 -13.128  16.839  1.00 62.23           C  
ANISOU 3998  CA  ILE B 115     9259   6544   7841   -469     41    259       C  
ATOM   3999  C   ILE B 115     -18.759 -11.620  16.673  1.00 65.63           C  
ANISOU 3999  C   ILE B 115     9472   7238   8224   -488      4    229       C  
ATOM   4000  O   ILE B 115     -18.543 -11.163  15.554  1.00 65.00           O  
ANISOU 4000  O   ILE B 115     9389   7192   8116   -342     18    152       O  
ATOM   4001  CB  ILE B 115     -20.368 -13.621  16.965  1.00 65.43           C  
ANISOU 4001  CB  ILE B 115     9767   6813   8282   -733     -7     83       C  
ATOM   4002  CG1 ILE B 115     -20.421 -15.158  16.772  1.00 68.23           C  
ANISOU 4002  CG1 ILE B 115    10413   6819   8693   -708     55     74       C  
ATOM   4003  CG2 ILE B 115     -21.282 -12.909  15.953  1.00 65.23           C  
ANISOU 4003  CG2 ILE B 115     9692   6883   8211   -803    -71   -150       C  
ATOM   4004  CD1 ILE B 115     -21.603 -15.885  17.374  1.00 74.39           C  
ANISOU 4004  CD1 ILE B 115    11282   7450   9533  -1015     28     16       C  
ATOM   4005  N   TYR B 116     -18.791 -10.862  17.791  1.00 62.55           N  
ANISOU 4005  N   TYR B 116     8923   7026   7817   -657    -23    302       N  
ATOM   4006  CA  TYR B 116     -18.601  -9.409  17.790  1.00 61.29           C  
ANISOU 4006  CA  TYR B 116     8604   7059   7623   -706    -29    274       C  
ATOM   4007  C   TYR B 116     -17.221  -9.051  17.248  1.00 65.20           C  
ANISOU 4007  C   TYR B 116     9017   7657   8098   -518      1    414       C  
ATOM   4008  O   TYR B 116     -17.137  -8.205  16.364  1.00 64.05           O  
ANISOU 4008  O   TYR B 116     8829   7553   7952   -446     24    352       O  
ATOM   4009  CB  TYR B 116     -18.820  -8.813  19.198  1.00 62.51           C  
ANISOU 4009  CB  TYR B 116     8661   7353   7736   -937    -48    305       C  
ATOM   4010  CG  TYR B 116     -18.668  -7.307  19.302  1.00 63.95           C  
ANISOU 4010  CG  TYR B 116     8744   7667   7886  -1024    -27    246       C  
ATOM   4011  CD1 TYR B 116     -19.274  -6.456  18.382  1.00 65.22           C  
ANISOU 4011  CD1 TYR B 116     8914   7784   8081   -968     13    110       C  
ATOM   4012  CD2 TYR B 116     -17.989  -6.729  20.371  1.00 65.49           C  
ANISOU 4012  CD2 TYR B 116     8852   8028   8003  -1181    -41    323       C  
ATOM   4013  CE1 TYR B 116     -19.178  -5.068  18.500  1.00 65.98           C  
ANISOU 4013  CE1 TYR B 116     8966   7934   8168  -1040     70     64       C  
ATOM   4014  CE2 TYR B 116     -17.883  -5.342  20.497  1.00 66.38           C  
ANISOU 4014  CE2 TYR B 116     8931   8199   8089  -1303     -3    234       C  
ATOM   4015  CZ  TYR B 116     -18.484  -4.515  19.563  1.00 73.20           C  
ANISOU 4015  CZ  TYR B 116     9839   8954   9022  -1223     68    109       C  
ATOM   4016  OH  TYR B 116     -18.373  -3.150  19.680  1.00 75.17           O  
ANISOU 4016  OH  TYR B 116    10098   9198   9265  -1329    141     35       O  
ATOM   4017  N   THR B 117     -16.162  -9.738  17.732  1.00 63.11           N  
ANISOU 4017  N   THR B 117     8716   7450   7814   -419     13    632       N  
ATOM   4018  CA  THR B 117     -14.766  -9.544  17.318  1.00 63.88           C  
ANISOU 4018  CA  THR B 117     8686   7705   7881   -230     48    827       C  
ATOM   4019  C   THR B 117     -14.578  -9.834  15.816  1.00 69.01           C  
ANISOU 4019  C   THR B 117     9438   8237   8547     52    120    773       C  
ATOM   4020  O   THR B 117     -14.018  -8.997  15.102  1.00 68.26           O  
ANISOU 4020  O   THR B 117     9232   8271   8434    129    146    805       O  
ATOM   4021  CB  THR B 117     -13.845 -10.375  18.218  1.00 72.20           C  
ANISOU 4021  CB  THR B 117     9662   8874   8896   -154     53   1104       C  
ATOM   4022  OG1 THR B 117     -14.111 -10.041  19.579  1.00 73.32           O  
ANISOU 4022  OG1 THR B 117     9714   9162   8982   -434    -21   1128       O  
ATOM   4023  CG2 THR B 117     -12.382 -10.162  17.916  1.00 70.92           C  
ANISOU 4023  CG2 THR B 117     9301   8960   8687     30     86   1355       C  
ATOM   4024  N   VAL B 118     -15.060 -11.007  15.348  1.00 67.14           N  
ANISOU 4024  N   VAL B 118     9428   7751   8331    184    158    685       N  
ATOM   4025  CA  VAL B 118     -15.022 -11.419  13.941  1.00 67.99           C  
ANISOU 4025  CA  VAL B 118     9693   7727   8414    431    226    577       C  
ATOM   4026  C   VAL B 118     -15.666 -10.310  13.084  1.00 71.48           C  
ANISOU 4026  C   VAL B 118    10078   8254   8827    358    187    396       C  
ATOM   4027  O   VAL B 118     -15.006  -9.791  12.188  1.00 71.45           O  
ANISOU 4027  O   VAL B 118    10001   8366   8779    543    241    453       O  
ATOM   4028  CB  VAL B 118     -15.671 -12.821  13.730  1.00 73.38           C  
ANISOU 4028  CB  VAL B 118    10681   8082   9116    472    260    442       C  
ATOM   4029  CG1 VAL B 118     -16.036 -13.065  12.269  1.00 73.83           C  
ANISOU 4029  CG1 VAL B 118    10930   8017   9105    609    292    214       C  
ATOM   4030  CG2 VAL B 118     -14.762 -13.933  14.250  1.00 75.49           C  
ANISOU 4030  CG2 VAL B 118    11035   8236   9411    687    367    680       C  
ATOM   4031  N   ASN B 119     -16.906  -9.895  13.433  1.00 67.58           N  
ANISOU 4031  N   ASN B 119     9586   7734   8355    104    109    226       N  
ATOM   4032  CA  ASN B 119     -17.662  -8.824  12.772  1.00 66.58           C  
ANISOU 4032  CA  ASN B 119     9390   7701   8206     47     85     94       C  
ATOM   4033  C   ASN B 119     -16.900  -7.486  12.757  1.00 71.07           C  
ANISOU 4033  C   ASN B 119     9773   8446   8786     67    128    228       C  
ATOM   4034  O   ASN B 119     -16.903  -6.814  11.730  1.00 70.60           O  
ANISOU 4034  O   ASN B 119     9680   8453   8693    191    166    211       O  
ATOM   4035  CB  ASN B 119     -19.047  -8.665  13.414  1.00 65.75           C  
ANISOU 4035  CB  ASN B 119     9282   7571   8127   -208     19    -46       C  
ATOM   4036  CG  ASN B 119     -19.729  -7.349  13.127  1.00 88.41           C  
ANISOU 4036  CG  ASN B 119    12032  10569  10990   -254     27   -101       C  
ATOM   4037  OD1 ASN B 119     -19.657  -6.402  13.918  1.00 86.33           O  
ANISOU 4037  OD1 ASN B 119    11672  10364  10765   -365     57    -45       O  
ATOM   4038  ND2 ASN B 119     -20.387  -7.254  11.983  1.00 78.04           N  
ANISOU 4038  ND2 ASN B 119    10736   9302   9613   -159     12   -207       N  
ATOM   4039  N   LEU B 120     -16.267  -7.101  13.889  1.00 68.58           N  
ANISOU 4039  N   LEU B 120     9343   8211   8503    -78    121    362       N  
ATOM   4040  CA  LEU B 120     -15.499  -5.856  14.009  1.00 68.51           C  
ANISOU 4040  CA  LEU B 120     9177   8347   8505   -144    156    476       C  
ATOM   4041  C   LEU B 120     -14.356  -5.782  12.995  1.00 74.27           C  
ANISOU 4041  C   LEU B 120     9827   9181   9210     93    223    636       C  
ATOM   4042  O   LEU B 120     -14.162  -4.736  12.367  1.00 73.77           O  
ANISOU 4042  O   LEU B 120     9692   9179   9160    109    278    669       O  
ATOM   4043  CB  LEU B 120     -14.914  -5.699  15.429  1.00 68.80           C  
ANISOU 4043  CB  LEU B 120     9113   8493   8536   -370    113    583       C  
ATOM   4044  CG  LEU B 120     -15.835  -5.212  16.542  1.00 72.43           C  
ANISOU 4044  CG  LEU B 120     9609   8915   8997   -644     81    446       C  
ATOM   4045  CD1 LEU B 120     -15.205  -5.464  17.894  1.00 73.09           C  
ANISOU 4045  CD1 LEU B 120     9611   9142   9020   -826     22    560       C  
ATOM   4046  CD2 LEU B 120     -16.163  -3.741  16.397  1.00 74.31           C  
ANISOU 4046  CD2 LEU B 120     9840   9130   9263   -760    144    354       C  
ATOM   4047  N   TYR B 121     -13.601  -6.889  12.847  1.00 72.64           N  
ANISOU 4047  N   TYR B 121     9640   8991   8970    296    241    757       N  
ATOM   4048  CA  TYR B 121     -12.437  -6.955  11.966  1.00 73.96           C  
ANISOU 4048  CA  TYR B 121     9715   9291   9096    564    328    944       C  
ATOM   4049  C   TYR B 121     -12.708  -7.330  10.519  1.00 75.83           C  
ANISOU 4049  C   TYR B 121    10095   9448   9268    849    398    841       C  
ATOM   4050  O   TYR B 121     -12.055  -6.774   9.637  1.00 75.33           O  
ANISOU 4050  O   TYR B 121     9931   9525   9168   1011    477    957       O  
ATOM   4051  CB  TYR B 121     -11.311  -7.797  12.581  1.00 77.84           C  
ANISOU 4051  CB  TYR B 121    10109   9900   9566    682    348   1190       C  
ATOM   4052  CG  TYR B 121     -10.840  -7.301  13.934  1.00 81.24           C  
ANISOU 4052  CG  TYR B 121    10342  10520  10006    391    266   1328       C  
ATOM   4053  CD1 TYR B 121     -10.418  -5.983  14.109  1.00 83.70           C  
ANISOU 4053  CD1 TYR B 121    10470  11008  10326    153    244   1381       C  
ATOM   4054  CD2 TYR B 121     -10.778  -8.156  15.029  1.00 82.88           C  
ANISOU 4054  CD2 TYR B 121    10555  10737  10197    345    218   1413       C  
ATOM   4055  CE1 TYR B 121      -9.981  -5.522  15.351  1.00 85.88           C  
ANISOU 4055  CE1 TYR B 121    10586  11473  10573   -161    158   1468       C  
ATOM   4056  CE2 TYR B 121     -10.331  -7.710  16.271  1.00 84.48           C  
ANISOU 4056  CE2 TYR B 121    10567  11172  10360     69    130   1537       C  
ATOM   4057  CZ  TYR B 121      -9.937  -6.390  16.429  1.00 93.29           C  
ANISOU 4057  CZ  TYR B 121    11512  12472  11462   -199     91   1543       C  
ATOM   4058  OH  TYR B 121      -9.503  -5.949  17.655  1.00 96.52           O  
ANISOU 4058  OH  TYR B 121    11756  13122  11795   -516     -6   1625       O  
ATOM   4059  N   SER B 122     -13.663  -8.249  10.266  1.00 71.43           N  
ANISOU 4059  N   SER B 122     9770   8687   8683    886    369    625       N  
ATOM   4060  CA  SER B 122     -14.011  -8.652   8.905  1.00 71.63           C  
ANISOU 4060  CA  SER B 122     9959   8654   8603   1110    415    476       C  
ATOM   4061  C   SER B 122     -14.675  -7.513   8.124  1.00 73.37           C  
ANISOU 4061  C   SER B 122    10106   8985   8786   1064    397    395       C  
ATOM   4062  O   SER B 122     -14.207  -7.201   7.033  1.00 74.28           O  
ANISOU 4062  O   SER B 122    10188   9223   8812   1289    476    459       O  
ATOM   4063  CB  SER B 122     -14.870  -9.913   8.894  1.00 75.99           C  
ANISOU 4063  CB  SER B 122    10786   8960   9127   1083    376    249       C  
ATOM   4064  OG  SER B 122     -16.134  -9.691   9.495  1.00 83.75           O  
ANISOU 4064  OG  SER B 122    11777   9883  10161    775    259     87       O  
ATOM   4065  N   SER B 123     -15.717  -6.862   8.702  1.00 67.03           N  
ANISOU 4065  N   SER B 123     9265   8157   8047    804    315    290       N  
ATOM   4066  CA  SER B 123     -16.455  -5.750   8.079  1.00 65.55           C  
ANISOU 4066  CA  SER B 123     9004   8065   7838    784    319    249       C  
ATOM   4067  C   SER B 123     -15.543  -4.655   7.539  1.00 67.97           C  
ANISOU 4067  C   SER B 123     9160   8510   8156    904    425    460       C  
ATOM   4068  O   SER B 123     -15.647  -4.315   6.362  1.00 68.55           O  
ANISOU 4068  O   SER B 123     9224   8690   8132   1095    476    477       O  
ATOM   4069  CB  SER B 123     -17.497  -5.163   9.030  1.00 67.74           C  
ANISOU 4069  CB  SER B 123     9243   8292   8202    520    262    169       C  
ATOM   4070  OG  SER B 123     -16.910  -4.414  10.083  1.00 76.54           O  
ANISOU 4070  OG  SER B 123    10260   9397   9427    355    293    292       O  
ATOM   4071  N   VAL B 124     -14.632  -4.137   8.383  1.00 62.80           N  
ANISOU 4071  N   VAL B 124     8381   7876   7605    775    457    629       N  
ATOM   4072  CA  VAL B 124     -13.691  -3.087   7.996  1.00 62.88           C  
ANISOU 4072  CA  VAL B 124     8237   8008   7648    812    558    847       C  
ATOM   4073  C   VAL B 124     -12.644  -3.574   6.975  1.00 67.48           C  
ANISOU 4073  C   VAL B 124     8769   8739   8131   1118    642   1004       C  
ATOM   4074  O   VAL B 124     -12.264  -2.810   6.084  1.00 67.57           O  
ANISOU 4074  O   VAL B 124     8692   8867   8116   1244    740   1146       O  
ATOM   4075  CB  VAL B 124     -13.093  -2.321   9.212  1.00 66.52           C  
ANISOU 4075  CB  VAL B 124     8580   8468   8225    507    552    953       C  
ATOM   4076  CG1 VAL B 124     -12.048  -3.146   9.970  1.00 66.84           C  
ANISOU 4076  CG1 VAL B 124     8532   8611   8254    475    506   1077       C  
ATOM   4077  CG2 VAL B 124     -12.538  -0.959   8.799  1.00 67.17           C  
ANISOU 4077  CG2 VAL B 124     8551   8603   8369    449    662   1121       C  
ATOM   4078  N   TRP B 125     -12.200  -4.844   7.093  1.00 64.29           N  
ANISOU 4078  N   TRP B 125     8435   8324   7670   1261    627    993       N  
ATOM   4079  CA  TRP B 125     -11.221  -5.402   6.166  1.00 65.59           C  
ANISOU 4079  CA  TRP B 125     8577   8618   7724   1602    739   1137       C  
ATOM   4080  C   TRP B 125     -11.779  -5.830   4.821  1.00 69.84           C  
ANISOU 4080  C   TRP B 125     9292   9148   8094   1867    780    975       C  
ATOM   4081  O   TRP B 125     -11.031  -5.856   3.845  1.00 70.97           O  
ANISOU 4081  O   TRP B 125     9392   9447   8125   2154    902   1109       O  
ATOM   4082  CB  TRP B 125     -10.291  -6.416   6.829  1.00 65.41           C  
ANISOU 4082  CB  TRP B 125     8529   8614   7711   1700    760   1270       C  
ATOM   4083  CG  TRP B 125      -9.151  -5.720   7.505  1.00 66.97           C  
ANISOU 4083  CG  TRP B 125     8429   9032   7986   1564    776   1569       C  
ATOM   4084  CD1 TRP B 125      -9.113  -5.261   8.790  1.00 68.94           C  
ANISOU 4084  CD1 TRP B 125     8561   9298   8335   1211    674   1606       C  
ATOM   4085  CD2 TRP B 125      -7.964  -5.231   6.869  1.00 68.53           C  
ANISOU 4085  CD2 TRP B 125     8393   9497   8148   1723    894   1862       C  
ATOM   4086  NE1 TRP B 125      -7.937  -4.584   9.017  1.00 69.65           N  
ANISOU 4086  NE1 TRP B 125     8363   9652   8446   1115    705   1890       N  
ATOM   4087  CE2 TRP B 125      -7.212  -4.549   7.853  1.00 72.78           C  
ANISOU 4087  CE2 TRP B 125     8668  10211   8775   1422    842   2068       C  
ATOM   4088  CE3 TRP B 125      -7.436  -5.344   5.570  1.00 71.29           C  
ANISOU 4088  CE3 TRP B 125     8724   9982   8380   2088   1044   1976       C  
ATOM   4089  CZ2 TRP B 125      -5.961  -3.980   7.576  1.00 74.12           C  
ANISOU 4089  CZ2 TRP B 125     8535  10692   8937   1445    925   2397       C  
ATOM   4090  CZ3 TRP B 125      -6.199  -4.781   5.299  1.00 74.49           C  
ANISOU 4090  CZ3 TRP B 125     8829  10691   8781   2153   1147   2319       C  
ATOM   4091  CH2 TRP B 125      -5.479  -4.100   6.290  1.00 75.50           C  
ANISOU 4091  CH2 TRP B 125     8676  10994   9017   1818   1083   2533       C  
ATOM   4092  N   ILE B 126     -13.104  -6.084   4.751  1.00 65.45           N  
ANISOU 4092  N   ILE B 126     8909   8457   7502   1754    677    699       N  
ATOM   4093  CA  ILE B 126     -13.812  -6.385   3.508  1.00 66.43           C  
ANISOU 4093  CA  ILE B 126     9184   8624   7433   1924    674    513       C  
ATOM   4094  C   ILE B 126     -13.880  -5.056   2.737  1.00 70.81           C  
ANISOU 4094  C   ILE B 126     9569   9380   7957   1983    730    662       C  
ATOM   4095  O   ILE B 126     -13.610  -5.033   1.537  1.00 72.43           O  
ANISOU 4095  O   ILE B 126     9785   9751   7985   2247    813    705       O  
ATOM   4096  CB  ILE B 126     -15.210  -7.039   3.762  1.00 69.28           C  
ANISOU 4096  CB  ILE B 126     9727   8831   7764   1723    528    202       C  
ATOM   4097  CG1 ILE B 126     -15.070  -8.541   4.103  1.00 71.01           C  
ANISOU 4097  CG1 ILE B 126    10190   8825   7966   1747    522     52       C  
ATOM   4098  CG2 ILE B 126     -16.143  -6.873   2.553  1.00 71.26           C  
ANISOU 4098  CG2 ILE B 126    10031   9234   7809   1795    483     42       C  
ATOM   4099  CD1 ILE B 126     -16.145  -9.118   5.061  1.00 76.65           C  
ANISOU 4099  CD1 ILE B 126    11014   9337   8774   1430    387   -143       C  
ATOM   4100  N   LEU B 127     -14.155  -3.947   3.453  1.00 66.16           N  
ANISOU 4100  N   LEU B 127     8838   8764   7537   1752    711    760       N  
ATOM   4101  CA  LEU B 127     -14.202  -2.598   2.876  1.00 66.37           C  
ANISOU 4101  CA  LEU B 127     8725   8910   7582   1791    798    938       C  
ATOM   4102  C   LEU B 127     -12.830  -2.150   2.366  1.00 72.94           C  
ANISOU 4102  C   LEU B 127     9411   9887   8414   1953    947   1230       C  
ATOM   4103  O   LEU B 127     -12.757  -1.384   1.404  1.00 73.98           O  
ANISOU 4103  O   LEU B 127     9468  10163   8478   2112   1049   1385       O  
ATOM   4104  CB  LEU B 127     -14.780  -1.573   3.860  1.00 64.74           C  
ANISOU 4104  CB  LEU B 127     8462   8568   7567   1508    780    954       C  
ATOM   4105  CG  LEU B 127     -16.224  -1.781   4.311  1.00 68.10           C  
ANISOU 4105  CG  LEU B 127     8976   8906   7992   1368    663    723       C  
ATOM   4106  CD1 LEU B 127     -16.618  -0.717   5.260  1.00 67.42           C  
ANISOU 4106  CD1 LEU B 127     8847   8685   8083   1147    699    765       C  
ATOM   4107  CD2 LEU B 127     -17.191  -1.776   3.150  1.00 71.60           C  
ANISOU 4107  CD2 LEU B 127     9436   9518   8252   1553    639    653       C  
ATOM   4108  N   ALA B 128     -11.747  -2.644   3.004  1.00 70.29           N  
ANISOU 4108  N   ALA B 128     9012   9549   8145   1922    965   1335       N  
ATOM   4109  CA  ALA B 128     -10.374  -2.382   2.590  1.00 72.16           C  
ANISOU 4109  CA  ALA B 128     9067   9978   8372   2071   1101   1636       C  
ATOM   4110  C   ALA B 128     -10.146  -3.109   1.258  1.00 79.45           C  
ANISOU 4110  C   ALA B 128    10073  11058   9058   2481   1193   1626       C  
ATOM   4111  O   ALA B 128      -9.630  -2.509   0.314  1.00 80.80           O  
ANISOU 4111  O   ALA B 128    10125  11427   9149   2668   1325   1839       O  
ATOM   4112  CB  ALA B 128      -9.406  -2.887   3.646  1.00 73.02           C  
ANISOU 4112  CB  ALA B 128     9069  10099   8576   1955   1076   1747       C  
ATOM   4113  N   PHE B 129     -10.614  -4.374   1.168  1.00 76.94           N  
ANISOU 4113  N   PHE B 129     9985  10633   8615   2602   1131   1361       N  
ATOM   4114  CA  PHE B 129     -10.537  -5.219  -0.024  1.00 79.08           C  
ANISOU 4114  CA  PHE B 129    10424  10995   8627   2962   1211   1256       C  
ATOM   4115  C   PHE B 129     -11.434  -4.678  -1.133  1.00 83.54           C  
ANISOU 4115  C   PHE B 129    11035  11692   9014   3037   1194   1158       C  
ATOM   4116  O   PHE B 129     -11.130  -4.881  -2.308  1.00 85.75           O  
ANISOU 4116  O   PHE B 129    11361  12163   9057   3347   1301   1183       O  
ATOM   4117  CB  PHE B 129     -10.888  -6.674   0.325  1.00 81.41           C  
ANISOU 4117  CB  PHE B 129    11003  11063   8868   2988   1149    968       C  
ATOM   4118  CG  PHE B 129      -9.718  -7.534   0.744  1.00 84.72           C  
ANISOU 4118  CG  PHE B 129    11423  11446   9321   3186   1266   1117       C  
ATOM   4119  CD1 PHE B 129      -8.900  -7.159   1.805  1.00 87.20           C  
ANISOU 4119  CD1 PHE B 129    11484  11810   9837   3043   1267   1392       C  
ATOM   4120  CD2 PHE B 129      -9.450  -8.734   0.098  1.00 89.85           C  
ANISOU 4120  CD2 PHE B 129    12335  12018   9786   3518   1382    984       C  
ATOM   4121  CE1 PHE B 129      -7.821  -7.956   2.194  1.00 90.18           C  
ANISOU 4121  CE1 PHE B 129    11817  12220  10229   3257   1376   1581       C  
ATOM   4122  CE2 PHE B 129      -8.373  -9.535   0.494  1.00 94.61           C  
ANISOU 4122  CE2 PHE B 129    12937  12586  10424   3762   1524   1163       C  
ATOM   4123  CZ  PHE B 129      -7.570  -9.143   1.542  1.00 91.97           C  
ANISOU 4123  CZ  PHE B 129    12298  12356  10290   3641   1516   1482       C  
ATOM   4124  N   ILE B 130     -12.523  -3.972  -0.754  1.00 77.73           N  
ANISOU 4124  N   ILE B 130    10272  10886   8376   2776   1073   1072       N  
ATOM   4125  CA  ILE B 130     -13.456  -3.304  -1.667  1.00 77.81           C  
ANISOU 4125  CA  ILE B 130    10265  11060   8238   2834   1050   1043       C  
ATOM   4126  C   ILE B 130     -12.696  -2.129  -2.324  1.00 82.05           C  
ANISOU 4126  C   ILE B 130    10592  11794   8791   2992   1223   1412       C  
ATOM   4127  O   ILE B 130     -12.741  -1.977  -3.546  1.00 83.28           O  
ANISOU 4127  O   ILE B 130    10739  12194   8709   3254   1295   1477       O  
ATOM   4128  CB  ILE B 130     -14.730  -2.866  -0.877  1.00 79.00           C  
ANISOU 4128  CB  ILE B 130    10412  11074   8530   2532    906    909       C  
ATOM   4129  CG1 ILE B 130     -15.777  -4.002  -0.774  1.00 79.50           C  
ANISOU 4129  CG1 ILE B 130    10675  11063   8469   2422    734    543       C  
ATOM   4130  CG2 ILE B 130     -15.336  -1.543  -1.360  1.00 80.01           C  
ANISOU 4130  CG2 ILE B 130    10396  11340   8664   2563    955   1090       C  
ATOM   4131  CD1 ILE B 130     -16.809  -4.114  -1.920  1.00 90.70           C  
ANISOU 4131  CD1 ILE B 130    12140  12730   9593   2520    653    388       C  
ATOM   4132  N   SER B 131     -11.954  -1.349  -1.499  1.00 77.47           N  
ANISOU 4132  N   SER B 131     9847  11113   8473   2813   1290   1652       N  
ATOM   4133  CA  SER B 131     -11.129  -0.214  -1.921  1.00 78.18           C  
ANISOU 4133  CA  SER B 131     9736  11332   8637   2870   1462   2021       C  
ATOM   4134  C   SER B 131      -9.960  -0.711  -2.772  1.00 84.14           C  
ANISOU 4134  C   SER B 131    10420  12330   9219   3188   1602   2195       C  
ATOM   4135  O   SER B 131      -9.632  -0.088  -3.782  1.00 85.46           O  
ANISOU 4135  O   SER B 131    10482  12715   9275   3396   1747   2436       O  
ATOM   4136  CB  SER B 131     -10.606   0.553  -0.709  1.00 79.75           C  
ANISOU 4136  CB  SER B 131     9811  11348   9140   2522   1472   2167       C  
ATOM   4137  OG  SER B 131     -11.668   1.026   0.099  1.00 85.73           O  
ANISOU 4137  OG  SER B 131    10656  11875  10044   2260   1375   2002       O  
ATOM   4138  N   LEU B 132      -9.359  -1.849  -2.373  1.00 80.62           N  
ANISOU 4138  N   LEU B 132    10037  11852   8742   3255   1581   2093       N  
ATOM   4139  CA  LEU B 132      -8.240  -2.484  -3.063  1.00 82.76           C  
ANISOU 4139  CA  LEU B 132    10260  12339   8846   3602   1736   2245       C  
ATOM   4140  C   LEU B 132      -8.639  -2.945  -4.463  1.00 88.66           C  
ANISOU 4140  C   LEU B 132    11176  13264   9248   3962   1797   2108       C  
ATOM   4141  O   LEU B 132      -7.882  -2.723  -5.408  1.00 90.97           O  
ANISOU 4141  O   LEU B 132    11355  13826   9383   4256   1976   2350       O  
ATOM   4142  CB  LEU B 132      -7.700  -3.652  -2.220  1.00 82.72           C  
ANISOU 4142  CB  LEU B 132    10327  12208   8893   3613   1704   2148       C  
ATOM   4143  CG  LEU B 132      -6.193  -3.884  -2.246  1.00 89.85           C  
ANISOU 4143  CG  LEU B 132    11015  13329   9796   3830   1875   2481       C  
ATOM   4144  CD1 LEU B 132      -5.435  -2.703  -1.650  1.00 89.87           C  
ANISOU 4144  CD1 LEU B 132    10667  13452  10028   3540   1897   2842       C  
ATOM   4145  CD2 LEU B 132      -5.834  -5.121  -1.457  1.00 93.14           C  
ANISOU 4145  CD2 LEU B 132    11538  13610  10242   3901   1852   2383       C  
ATOM   4146  N   ASP B 133      -9.850  -3.534  -4.597  1.00 84.17           N  
ANISOU 4146  N   ASP B 133    10861  12575   8545   3913   1644   1729       N  
ATOM   4147  CA  ASP B 133     -10.427  -4.019  -5.858  1.00 85.86           C  
ANISOU 4147  CA  ASP B 133    11265  12967   8392   4170   1648   1520       C  
ATOM   4148  C   ASP B 133     -10.680  -2.868  -6.828  1.00 90.10           C  
ANISOU 4148  C   ASP B 133    11634  13794   8806   4280   1714   1754       C  
ATOM   4149  O   ASP B 133     -10.381  -3.000  -8.013  1.00 92.46           O  
ANISOU 4149  O   ASP B 133    11959  14376   8797   4608   1835   1811       O  
ATOM   4150  CB  ASP B 133     -11.736  -4.791  -5.596  1.00 86.78           C  
ANISOU 4150  CB  ASP B 133    11641  12898   8433   3969   1432   1077       C  
ATOM   4151  CG  ASP B 133     -12.472  -5.252  -6.844  1.00 95.93           C  
ANISOU 4151  CG  ASP B 133    12991  14272   9187   4138   1388    820       C  
ATOM   4152  OD1 ASP B 133     -13.366  -4.515  -7.314  1.00 95.38           O  
ANISOU 4152  OD1 ASP B 133    12820  14401   9018   4073   1299    843       O  
ATOM   4153  OD2 ASP B 133     -12.165  -6.354  -7.337  1.00102.57           O  
ANISOU 4153  OD2 ASP B 133    14088  15087   9796   4335   1448    594       O  
ATOM   4154  N   ARG B 134     -11.243  -1.753  -6.327  1.00 84.36           N  
ANISOU 4154  N   ARG B 134    10755  12991   8308   4028   1655   1896       N  
ATOM   4155  CA  ARG B 134     -11.542  -0.568  -7.128  1.00 84.99           C  
ANISOU 4155  CA  ARG B 134    10679  13290   8322   4129   1739   2168       C  
ATOM   4156  C   ARG B 134     -10.269   0.093  -7.654  1.00 90.27           C  
ANISOU 4156  C   ARG B 134    11144  14142   9014   4322   1978   2596       C  
ATOM   4157  O   ARG B 134     -10.255   0.530  -8.802  1.00 91.95           O  
ANISOU 4157  O   ARG B 134    11290  14652   8994   4588   2094   2788       O  
ATOM   4158  CB  ARG B 134     -12.440   0.419  -6.357  1.00 82.49           C  
ANISOU 4158  CB  ARG B 134    10293  12776   8273   3834   1656   2213       C  
ATOM   4159  CG  ARG B 134     -13.870  -0.088  -6.102  1.00 87.94           C  
ANISOU 4159  CG  ARG B 134    11126  13409   8878   3693   1436   1853       C  
ATOM   4160  CD  ARG B 134     -14.710  -0.204  -7.369  1.00 97.62           C  
ANISOU 4160  CD  ARG B 134    12379  14996   9716   3920   1384   1778       C  
ATOM   4161  NE  ARG B 134     -14.762  -1.573  -7.892  1.00103.30           N  
ANISOU 4161  NE  ARG B 134    13309  15821  10118   4013   1288   1422       N  
ATOM   4162  CZ  ARG B 134     -15.200  -1.902  -9.105  1.00114.77           C  
ANISOU 4162  CZ  ARG B 134    14823  17630  11153   4220   1253   1311       C  
ATOM   4163  NH1 ARG B 134     -15.217  -3.170  -9.491  1.00101.27           N  
ANISOU 4163  NH1 ARG B 134    13364  15945   9168   4261   1179    942       N  
ATOM   4164  NH2 ARG B 134     -15.622  -0.963  -9.943  1.00100.52           N  
ANISOU 4164  NH2 ARG B 134    12846  16158   9190   4388   1300   1570       N  
ATOM   4165  N   TYR B 135      -9.187   0.097  -6.840  1.00 86.11           N  
ANISOU 4165  N   TYR B 135    10499  13482   8737   4191   2048   2756       N  
ATOM   4166  CA  TYR B 135      -7.867   0.618  -7.202  1.00 87.77           C  
ANISOU 4166  CA  TYR B 135    10474  13886   8990   4320   2266   3175       C  
ATOM   4167  C   TYR B 135      -7.325  -0.194  -8.373  1.00 94.49           C  
ANISOU 4167  C   TYR B 135    11375  15058   9469   4774   2399   3180       C  
ATOM   4168  O   TYR B 135      -6.837   0.388  -9.340  1.00 97.13           O  
ANISOU 4168  O   TYR B 135    11561  15682   9662   5008   2582   3499       O  
ATOM   4169  CB  TYR B 135      -6.903   0.574  -5.992  1.00 88.10           C  
ANISOU 4169  CB  TYR B 135    10371  13771   9332   4052   2263   3291       C  
ATOM   4170  CG  TYR B 135      -5.431   0.571  -6.358  1.00 92.91           C  
ANISOU 4170  CG  TYR B 135    10735  14658   9908   4240   2465   3661       C  
ATOM   4171  CD1 TYR B 135      -4.745   1.758  -6.592  1.00 96.30           C  
ANISOU 4171  CD1 TYR B 135    10899  15218  10474   4136   2620   4091       C  
ATOM   4172  CD2 TYR B 135      -4.720  -0.624  -6.452  1.00 95.24           C  
ANISOU 4172  CD2 TYR B 135    11063  15080  10044   4523   2518   3599       C  
ATOM   4173  CE1 TYR B 135      -3.393   1.759  -6.935  1.00 99.45           C  
ANISOU 4173  CE1 TYR B 135    11026  15923  10836   4291   2807   4464       C  
ATOM   4174  CE2 TYR B 135      -3.371  -0.636  -6.808  1.00 99.04           C  
ANISOU 4174  CE2 TYR B 135    11281  15870  10479   4739   2724   3975       C  
ATOM   4175  CZ  TYR B 135      -2.708   0.557  -7.038  1.00107.79           C  
ANISOU 4175  CZ  TYR B 135    12082  17158  11716   4607   2857   4413       C  
ATOM   4176  OH  TYR B 135      -1.369   0.538  -7.363  1.00112.29           O  
ANISOU 4176  OH  TYR B 135    12347  18076  12240   4796   3057   4812       O  
ATOM   4177  N   LEU B 136      -7.430  -1.534  -8.288  1.00 90.39           N  
ANISOU 4177  N   LEU B 136    11090  14469   8786   4901   2324   2827       N  
ATOM   4178  CA  LEU B 136      -6.975  -2.442  -9.340  1.00 92.97           C  
ANISOU 4178  CA  LEU B 136    11550  15037   8737   5342   2464   2749       C  
ATOM   4179  C   LEU B 136      -7.871  -2.374 -10.588  1.00 99.22           C  
ANISOU 4179  C   LEU B 136    12486  16067   9147   5539   2440   2596       C  
ATOM   4180  O   LEU B 136      -7.407  -2.697 -11.681  1.00102.20           O  
ANISOU 4180  O   LEU B 136    12907  16744   9181   5922   2605   2648       O  
ATOM   4181  CB  LEU B 136      -6.866  -3.889  -8.827  1.00 92.56           C  
ANISOU 4181  CB  LEU B 136    11764  14762   8644   5405   2415   2402       C  
ATOM   4182  CG  LEU B 136      -5.798  -4.196  -7.769  1.00 95.97           C  
ANISOU 4182  CG  LEU B 136    12044  15067   9353   5343   2476   2592       C  
ATOM   4183  CD1 LEU B 136      -5.956  -5.607  -7.258  1.00 96.08           C  
ANISOU 4183  CD1 LEU B 136    12372  14804   9332   5402   2420   2233       C  
ATOM   4184  CD2 LEU B 136      -4.383  -4.026  -8.317  1.00100.37           C  
ANISOU 4184  CD2 LEU B 136    12339  15961   9836   5680   2748   3023       C  
ATOM   4185  N   ALA B 137      -9.143  -1.949 -10.424  1.00 94.05           N  
ANISOU 4185  N   ALA B 137    11887  15320   8530   5289   2241   2424       N  
ATOM   4186  CA  ALA B 137     -10.111  -1.825 -11.517  1.00 95.85           C  
ANISOU 4186  CA  ALA B 137    12200  15828   8391   5429   2177   2300       C  
ATOM   4187  C   ALA B 137     -10.037  -0.469 -12.232  1.00101.82           C  
ANISOU 4187  C   ALA B 137    12692  16867   9129   5550   2314   2760       C  
ATOM   4188  O   ALA B 137     -10.464  -0.368 -13.383  1.00104.37           O  
ANISOU 4188  O   ALA B 137    13034  17552   9072   5793   2336   2774       O  
ATOM   4189  CB  ALA B 137     -11.522  -2.061 -10.999  1.00 94.61           C  
ANISOU 4189  CB  ALA B 137    12186  15494   8269   5122   1903   1935       C  
ATOM   4190  N   ILE B 138      -9.505   0.564 -11.555  1.00 97.05           N  
ANISOU 4190  N   ILE B 138    11856  16098   8922   5369   2411   3133       N  
ATOM   4191  CA  ILE B 138      -9.411   1.919 -12.094  1.00 98.27           C  
ANISOU 4191  CA  ILE B 138    11785  16417   9135   5437   2569   3599       C  
ATOM   4192  C   ILE B 138      -7.983   2.295 -12.511  1.00105.92           C  
ANISOU 4192  C   ILE B 138    12543  17568  10133   5619   2840   4035       C  
ATOM   4193  O   ILE B 138      -7.787   2.785 -13.627  1.00108.47           O  
ANISOU 4193  O   ILE B 138    12760  18238  10216   5910   3009   4333       O  
ATOM   4194  CB  ILE B 138     -10.114   2.929 -11.126  1.00 98.64           C  
ANISOU 4194  CB  ILE B 138    11773  16123   9581   5074   2488   3680       C  
ATOM   4195  CG1 ILE B 138     -11.628   3.055 -11.441  1.00 98.98           C  
ANISOU 4195  CG1 ILE B 138    11905  16254   9451   5090   2325   3495       C  
ATOM   4196  CG2 ILE B 138      -9.455   4.310 -11.087  1.00100.09           C  
ANISOU 4196  CG2 ILE B 138    11741  16241  10048   5000   2710   4195       C  
ATOM   4197  CD1 ILE B 138     -12.553   2.002 -10.820  1.00104.40           C  
ANISOU 4197  CD1 ILE B 138    12794  16791  10084   4899   2053   2972       C  
ATOM   4198  N   VAL B 139      -6.997   2.057 -11.626  1.00102.93           N  
ANISOU 4198  N   VAL B 139    12079  17001  10029   5450   2879   4093       N  
ATOM   4199  CA  VAL B 139      -5.589   2.381 -11.886  1.00105.96           C  
ANISOU 4199  CA  VAL B 139    12208  17585  10467   5571   3123   4528       C  
ATOM   4200  C   VAL B 139      -4.768   1.342 -12.661  1.00114.96           C  
ANISOU 4200  C   VAL B 139    13374  19049  11256   6005   3266   4503       C  
ATOM   4201  O   VAL B 139      -3.774   1.700 -13.298  1.00117.40           O  
ANISOU 4201  O   VAL B 139    13454  19663  11488   6223   3506   4913       O  
ATOM   4202  CB  VAL B 139      -4.769   2.598 -10.576  1.00108.13           C  
ANISOU 4202  CB  VAL B 139    12315  17600  11168   5187   3105   4654       C  
ATOM   4203  CG1 VAL B 139      -3.325   3.009 -10.872  1.00110.71           C  
ANISOU 4203  CG1 VAL B 139    12318  18202  11547   5271   3350   5149       C  
ATOM   4204  CG2 VAL B 139      -5.440   3.623  -9.659  1.00105.60           C  
ANISOU 4204  CG2 VAL B 139    11999  16908  11216   4730   2993   4659       C  
ATOM   4205  N   HIS B 140      -5.192   0.066 -12.612  1.00112.92           N  
ANISOU 4205  N   HIS B 140    13408  18712  10785   6132   3139   4028       N  
ATOM   4206  CA  HIS B 140      -4.497  -1.035 -13.281  1.00116.43           C  
ANISOU 4206  CA  HIS B 140    13968  19381  10891   6563   3291   3929       C  
ATOM   4207  C   HIS B 140      -5.633  -1.802 -13.966  1.00122.73           C  
ANISOU 4207  C   HIS B 140    15135  20203  11294   6703   3151   3435       C  
ATOM   4208  O   HIS B 140      -5.859  -2.979 -13.672  1.00122.32           O  
ANISOU 4208  O   HIS B 140    15380  19948  11148   6729   3062   3007       O  
ATOM   4209  CB  HIS B 140      -3.627  -1.942 -12.389  1.00116.75           C  
ANISOU 4209  CB  HIS B 140    14011  19247  11101   6566   3323   3868       C  
ATOM   4210  CG  HIS B 140      -2.621  -1.180 -11.589  1.00119.62           C  
ANISOU 4210  CG  HIS B 140    13986  19616  11847   6328   3398   4321       C  
ATOM   4211  ND1 HIS B 140      -1.496  -0.634 -12.178  1.00124.47           N  
ANISOU 4211  ND1 HIS B 140    14271  20600  12420   6530   3655   4826       N  
ATOM   4212  CD2 HIS B 140      -2.622  -0.868 -10.274  1.00118.69           C  
ANISOU 4212  CD2 HIS B 140    13762  19205  12130   5876   3239   4329       C  
ATOM   4213  CE1 HIS B 140      -0.853  -0.011 -11.206  1.00122.97           C  
ANISOU 4213  CE1 HIS B 140    13782  20331  12612   6162   3631   5116       C  
ATOM   4214  NE2 HIS B 140      -1.485  -0.132 -10.043  1.00119.83           N  
ANISOU 4214  NE2 HIS B 140    13515  19539  12476   5767   3384   4821       N  
ATOM   4215  N   ALA B 141      -6.323  -1.127 -14.906  1.00121.80           N  
ANISOU 4215  N   ALA B 141    14992  20354  10934   6789   3141   3517       N  
ATOM   4216  CA  ALA B 141      -7.453  -1.666 -15.675  1.00123.65           C  
ANISOU 4216  CA  ALA B 141    15508  20729  10744   6883   2989   3102       C  
ATOM   4217  C   ALA B 141      -6.998  -2.776 -16.642  1.00133.81           C  
ANISOU 4217  C   ALA B 141    17047  22256  11539   7310   3135   2865       C  
ATOM   4218  O   ALA B 141      -7.812  -3.619 -17.030  1.00134.55           O  
ANISOU 4218  O   ALA B 141    17471  22354  11298   7320   2988   2376       O  
ATOM   4219  CB  ALA B 141      -8.152  -0.552 -16.441  1.00125.27           C  
ANISOU 4219  CB  ALA B 141    15547  21239  10810   6909   2974   3364       C  
ATOM   4220  N   THR B 142      -5.703  -2.778 -17.011  1.00134.72           N  
ANISOU 4220  N   THR B 142    17011  22570  11606   7647   3432   3205       N  
ATOM   4221  CA  THR B 142      -5.096  -3.761 -17.908  1.00139.75           C  
ANISOU 4221  CA  THR B 142    17874  23434  11791   8120   3645   3044       C  
ATOM   4222  C   THR B 142      -3.822  -4.400 -17.318  1.00147.08           C  
ANISOU 4222  C   THR B 142    18757  24207  12919   8305   3859   3178       C  
ATOM   4223  O   THR B 142      -3.697  -5.625 -17.373  1.00148.57           O  
ANISOU 4223  O   THR B 142    19301  24242  12908   8519   3919   2798       O  
ATOM   4224  CB  THR B 142      -4.862  -3.165 -19.310  1.00150.31           C  
ANISOU 4224  CB  THR B 142    19073  25338  12700   8493   3846   3354       C  
ATOM   4225  OG1 THR B 142      -4.276  -1.868 -19.180  1.00148.05           O  
ANISOU 4225  OG1 THR B 142    18334  25192  12729   8421   3973   3990       O  
ATOM   4226  CG2 THR B 142      -6.141  -3.087 -20.142  1.00150.33           C  
ANISOU 4226  CG2 THR B 142    19257  25577  12286   8454   3648   3060       C  
ATOM   4227  N   ASN B 143      -2.880  -3.570 -16.774  1.00144.35           N  
ANISOU 4227  N   ASN B 143    17978  23915  12954   8223   3983   3727       N  
ATOM   4228  CA  ASN B 143      -1.587  -3.976 -16.187  1.00145.66           C  
ANISOU 4228  CA  ASN B 143    17966  24051  13329   8379   4183   3986       C  
ATOM   4229  C   ASN B 143      -1.720  -5.192 -15.271  1.00149.54           C  
ANISOU 4229  C   ASN B 143    18770  24105  13945   8314   4076   3562       C  
ATOM   4230  O   ASN B 143      -1.035  -6.197 -15.469  1.00152.37           O  
ANISOU 4230  O   ASN B 143    19297  24476  14120   8721   4289   3482       O  
ATOM   4231  CB  ASN B 143      -0.928  -2.802 -15.438  1.00145.29           C  
ANISOU 4231  CB  ASN B 143    17419  24038  13747   8053   4192   4539       C  
ATOM   4232  CG  ASN B 143       0.425  -2.358 -15.961  1.00173.80           C  
ANISOU 4232  CG  ASN B 143    20631  28092  17313   8352   4518   5131       C  
ATOM   4233  OD1 ASN B 143       0.838  -1.214 -15.750  1.00169.17           O  
ANISOU 4233  OD1 ASN B 143    19654  27621  17001   8089   4550   5599       O  
ATOM   4234  ND2 ASN B 143       1.170  -3.247 -16.615  1.00169.39           N  
ANISOU 4234  ND2 ASN B 143    20161  27779  16420   8896   4783   5136       N  
ATOM   4235  N   SER B 144      -2.627  -5.097 -14.291  1.00142.61           N  
ANISOU 4235  N   SER B 144    17979  22836  13368   7825   3768   3303       N  
ATOM   4236  CA  SER B 144      -2.975  -6.167 -13.369  1.00140.97           C  
ANISOU 4236  CA  SER B 144    18080  22181  13300   7684   3628   2891       C  
ATOM   4237  C   SER B 144      -4.483  -6.387 -13.583  1.00143.92           C  
ANISOU 4237  C   SER B 144    18808  22364  13509   7432   3358   2367       C  
ATOM   4238  O   SER B 144      -5.324  -5.906 -12.814  1.00139.74           O  
ANISOU 4238  O   SER B 144    18225  21615  13254   6977   3096   2277       O  
ATOM   4239  CB  SER B 144      -2.630  -5.782 -11.929  1.00140.81           C  
ANISOU 4239  CB  SER B 144    17774  21934  13792   7297   3507   3121       C  
ATOM   4240  OG  SER B 144      -1.227  -5.770 -11.703  1.00150.44           O  
ANISOU 4240  OG  SER B 144    18667  23369  15125   7525   3741   3576       O  
ATOM   4241  N   GLN B 145      -4.804  -7.044 -14.716  1.00144.07           N  
ANISOU 4241  N   GLN B 145    19166  22534  13041   7739   3436   2049       N  
ATOM   4242  CA  GLN B 145      -6.158  -7.344 -15.192  1.00143.96           C  
ANISOU 4242  CA  GLN B 145    19482  22471  12743   7552   3203   1550       C  
ATOM   4243  C   GLN B 145      -7.056  -8.109 -14.193  1.00144.77           C  
ANISOU 4243  C   GLN B 145    19875  22075  13056   7151   2942   1091       C  
ATOM   4244  O   GLN B 145      -7.997  -7.517 -13.656  1.00140.48           O  
ANISOU 4244  O   GLN B 145    19212  21444  12720   6729   2676   1047       O  
ATOM   4245  CB  GLN B 145      -6.136  -8.012 -16.593  1.00150.44           C  
ANISOU 4245  CB  GLN B 145    20632  23574  12956   7971   3367   1284       C  
ATOM   4246  CG  GLN B 145      -5.133  -9.164 -16.760  1.00166.03           C  
ANISOU 4246  CG  GLN B 145    22891  25418  14775   8427   3676   1178       C  
ATOM   4247  CD  GLN B 145      -5.496 -10.112 -17.875  1.00186.52           C  
ANISOU 4247  CD  GLN B 145    26001  28083  16785   8688   3758    670       C  
ATOM   4248  OE1 GLN B 145      -5.370  -9.791 -19.060  1.00185.36           O  
ANISOU 4248  OE1 GLN B 145    25827  28401  16199   8982   3887    749       O  
ATOM   4249  NE2 GLN B 145      -5.903 -11.325 -17.522  1.00177.18           N  
ANISOU 4249  NE2 GLN B 145    25319  26433  15569   8591   3706    141       N  
ATOM   4250  N   ARG B 146      -6.750  -9.399 -13.921  1.00143.19           N  
ANISOU 4250  N   ARG B 146    20049  21541  12816   7299   3042    784       N  
ATOM   4251  CA  ARG B 146      -7.551 -10.217 -13.017  1.00141.16           C  
ANISOU 4251  CA  ARG B 146    20095  20795  12744   6938   2829    363       C  
ATOM   4252  C   ARG B 146      -6.888 -10.812 -11.749  1.00142.84           C  
ANISOU 4252  C   ARG B 146    20314  20598  13362   6917   2900    468       C  
ATOM   4253  O   ARG B 146      -7.269 -11.920 -11.368  1.00143.26           O  
ANISOU 4253  O   ARG B 146    20776  20238  13417   6836   2864     76       O  
ATOM   4254  CB  ARG B 146      -8.422 -11.236 -13.783  1.00145.48           C  
ANISOU 4254  CB  ARG B 146    21180  21237  12860   6917   2756   -253       C  
ATOM   4255  CG  ARG B 146      -9.600 -10.591 -14.512  1.00156.49           C  
ANISOU 4255  CG  ARG B 146    22506  22973  13978   6657   2502   -412       C  
ATOM   4256  CD  ARG B 146     -10.663 -11.582 -14.962  1.00170.44           C  
ANISOU 4256  CD  ARG B 146    24763  24605  15392   6438   2331  -1056       C  
ATOM   4257  NE  ARG B 146     -11.636 -11.863 -13.905  1.00175.24           N  
ANISOU 4257  NE  ARG B 146    25434  24837  16311   5912   2048  -1295       N  
ATOM   4258  CZ  ARG B 146     -12.735 -11.150 -13.676  1.00185.07           C  
ANISOU 4258  CZ  ARG B 146    26431  26250  17637   5508   1748  -1287       C  
ATOM   4259  NH1 ARG B 146     -13.022 -10.095 -14.431  1.00171.76           N  
ANISOU 4259  NH1 ARG B 146    24425  25085  15751   5575   1689  -1042       N  
ATOM   4260  NH2 ARG B 146     -13.554 -11.483 -12.689  1.00168.58           N  
ANISOU 4260  NH2 ARG B 146    24406  23819  15826   5062   1525  -1493       N  
ATOM   4261  N   PRO B 147      -5.993 -10.104 -10.996  1.00136.71           N  
ANISOU 4261  N   PRO B 147    19093  19910  12940   6924   2972    979       N  
ATOM   4262  CA  PRO B 147      -5.529 -10.662  -9.710  1.00134.72           C  
ANISOU 4262  CA  PRO B 147    18828  19311  13049   6841   2981   1063       C  
ATOM   4263  C   PRO B 147      -6.642 -10.492  -8.668  1.00133.40           C  
ANISOU 4263  C   PRO B 147    18676  18843  13169   6269   2650    851       C  
ATOM   4264  O   PRO B 147      -6.594 -11.058  -7.578  1.00131.70           O  
ANISOU 4264  O   PRO B 147    18528  18295  13218   6121   2600    814       O  
ATOM   4265  CB  PRO B 147      -4.303  -9.809  -9.375  1.00135.90           C  
ANISOU 4265  CB  PRO B 147    18451  19767  13417   6968   3126   1672       C  
ATOM   4266  CG  PRO B 147      -4.511  -8.543 -10.052  1.00139.61           C  
ANISOU 4266  CG  PRO B 147    18629  20604  13812   6866   3074   1882       C  
ATOM   4267  CD  PRO B 147      -5.446  -8.747 -11.206  1.00137.07           C  
ANISOU 4267  CD  PRO B 147    18631  20364  13083   6938   3022   1495       C  
ATOM   4268  N   ARG B 148      -7.659  -9.690  -9.041  1.00127.34           N  
ANISOU 4268  N   ARG B 148    17829  18226  12327   5978   2438    740       N  
ATOM   4269  CA  ARG B 148      -8.887  -9.370  -8.335  1.00123.47           C  
ANISOU 4269  CA  ARG B 148    17331  17557  12024   5473   2134    539       C  
ATOM   4270  C   ARG B 148      -9.730 -10.639  -8.265  1.00128.78           C  
ANISOU 4270  C   ARG B 148    18482  17880  12569   5341   2029      9       C  
ATOM   4271  O   ARG B 148     -10.396 -10.871  -7.258  1.00126.09           O  
ANISOU 4271  O   ARG B 148    18192  17243  12475   4973   1845   -137       O  
ATOM   4272  CB  ARG B 148      -9.666  -8.298  -9.120  1.00122.37           C  
ANISOU 4272  CB  ARG B 148    17016  17758  11721   5360   2012    581       C  
ATOM   4273  CG  ARG B 148      -8.922  -6.979  -9.328  1.00128.27           C  
ANISOU 4273  CG  ARG B 148    17330  18828  12580   5471   2134   1103       C  
ATOM   4274  CD  ARG B 148      -9.489  -6.184 -10.494  1.00135.04           C  
ANISOU 4274  CD  ARG B 148    18099  20066  13146   5554   2114   1159       C  
ATOM   4275  NE  ARG B 148     -10.775  -5.554 -10.182  1.00137.40           N  
ANISOU 4275  NE  ARG B 148    18329  20336  13542   5188   1865   1054       N  
ATOM   4276  CZ  ARG B 148     -11.958  -6.002 -10.597  1.00150.89           C  
ANISOU 4276  CZ  ARG B 148    20248  22087  14997   5057   1677    672       C  
ATOM   4277  NH1 ARG B 148     -12.037  -7.097 -11.344  1.00140.42           N  
ANISOU 4277  NH1 ARG B 148    19263  20794  13298   5220   1698    308       N  
ATOM   4278  NH2 ARG B 148     -13.069  -5.364 -10.262  1.00135.28           N  
ANISOU 4278  NH2 ARG B 148    18145  20128  13127   4756   1474    650       N  
ATOM   4279  N   LYS B 149      -9.686 -11.465  -9.341  1.00129.70           N  
ANISOU 4279  N   LYS B 149    18966  18028  12287   5629   2161   -282       N  
ATOM   4280  CA  LYS B 149     -10.397 -12.745  -9.449  1.00132.14           C  
ANISOU 4280  CA  LYS B 149    19801  17985  12423   5511   2102   -822       C  
ATOM   4281  C   LYS B 149      -9.856 -13.724  -8.401  1.00136.28           C  
ANISOU 4281  C   LYS B 149    20526  18022  13232   5559   2221   -825       C  
ATOM   4282  O   LYS B 149     -10.586 -14.608  -7.949  1.00136.68           O  
ANISOU 4282  O   LYS B 149    20925  17676  13333   5287   2112  -1190       O  
ATOM   4283  CB  LYS B 149     -10.266 -13.321 -10.872  1.00139.77           C  
ANISOU 4283  CB  LYS B 149    21119  19113  12874   5852   2267  -1102       C  
ATOM   4284  CG  LYS B 149     -11.349 -14.336 -11.247  1.00157.19           C  
ANISOU 4284  CG  LYS B 149    23841  21077  14808   5579   2120  -1727       C  
ATOM   4285  CD  LYS B 149     -10.808 -15.763 -11.379  1.00172.20           C  
ANISOU 4285  CD  LYS B 149    26317  22527  16585   5856   2384  -2033       C  
ATOM   4286  CE  LYS B 149     -10.345 -16.086 -12.786  1.00188.90           C  
ANISOU 4286  CE  LYS B 149    28717  24876  18181   6297   2620  -2209       C  
ATOM   4287  NZ  LYS B 149      -9.820 -17.475 -12.899  1.00203.27           N  
ANISOU 4287  NZ  LYS B 149    31147  26200  19886   6599   2918  -2516       N  
ATOM   4288  N   LEU B 150      -8.580 -13.543  -8.005  1.00132.07           N  
ANISOU 4288  N   LEU B 150    19746  17551  12884   5895   2444   -385       N  
ATOM   4289  CA  LEU B 150      -7.923 -14.339  -6.973  1.00131.65           C  
ANISOU 4289  CA  LEU B 150    19783  17135  13104   6003   2574   -263       C  
ATOM   4290  C   LEU B 150      -8.182 -13.676  -5.622  1.00129.77           C  
ANISOU 4290  C   LEU B 150    19179  16851  13277   5581   2349    -33       C  
ATOM   4291  O   LEU B 150      -8.696 -14.331  -4.726  1.00128.54           O  
ANISOU 4291  O   LEU B 150    19215  16316  13309   5324   2244   -208       O  
ATOM   4292  CB  LEU B 150      -6.409 -14.490  -7.239  1.00134.45           C  
ANISOU 4292  CB  LEU B 150    20008  17661  13414   6592   2927    128       C  
ATOM   4293  CG  LEU B 150      -6.007 -15.272  -8.501  1.00144.62           C  
ANISOU 4293  CG  LEU B 150    21703  18957  14287   7099   3221    -87       C  
ATOM   4294  CD1 LEU B 150      -4.690 -14.773  -9.054  1.00146.56           C  
ANISOU 4294  CD1 LEU B 150    21605  19647  14433   7612   3505    392       C  
ATOM   4295  CD2 LEU B 150      -5.938 -16.776  -8.235  1.00150.67           C  
ANISOU 4295  CD2 LEU B 150    23038  19165  15044   7292   3409   -381       C  
ATOM   4296  N   LEU B 151      -7.916 -12.356  -5.510  1.00122.89           N  
ANISOU 4296  N   LEU B 151    17812  16353  12527   5480   2274    332       N  
ATOM   4297  CA  LEU B 151      -8.116 -11.538  -4.304  1.00118.16           C  
ANISOU 4297  CA  LEU B 151    16858  15754  12283   5078   2077    552       C  
ATOM   4298  C   LEU B 151      -9.502 -11.687  -3.658  1.00119.03           C  
ANISOU 4298  C   LEU B 151    17129  15591  12506   4592   1802    210       C  
ATOM   4299  O   LEU B 151      -9.598 -11.693  -2.431  1.00116.27           O  
ANISOU 4299  O   LEU B 151    16676  15062  12440   4333   1698    294       O  
ATOM   4300  CB  LEU B 151      -7.834 -10.059  -4.615  1.00116.52           C  
ANISOU 4300  CB  LEU B 151    16204  15956  12110   5024   2053    894       C  
ATOM   4301  CG  LEU B 151      -7.019  -9.282  -3.586  1.00119.06           C  
ANISOU 4301  CG  LEU B 151    16101  16390  12747   4884   2049   1326       C  
ATOM   4302  CD1 LEU B 151      -5.523  -9.410  -3.853  1.00121.88           C  
ANISOU 4302  CD1 LEU B 151    16256  16993  13059   5305   2314   1713       C  
ATOM   4303  CD2 LEU B 151      -7.393  -7.819  -3.613  1.00119.25           C  
ANISOU 4303  CD2 LEU B 151    15818  16618  12873   4594   1928   1488       C  
ATOM   4304  N   ALA B 152     -10.559 -11.817  -4.483  1.00116.19           N  
ANISOU 4304  N   ALA B 152    17001  15245  11902   4470   1685   -157       N  
ATOM   4305  CA  ALA B 152     -11.948 -11.981  -4.043  1.00114.30           C  
ANISOU 4305  CA  ALA B 152    16892  14819  11717   4016   1427   -483       C  
ATOM   4306  C   ALA B 152     -12.318 -13.450  -3.809  1.00119.89           C  
ANISOU 4306  C   ALA B 152    18074  15088  12389   3949   1440   -855       C  
ATOM   4307  O   ALA B 152     -13.337 -13.721  -3.164  1.00117.97           O  
ANISOU 4307  O   ALA B 152    17921  14640  12263   3545   1244  -1070       O  
ATOM   4308  CB  ALA B 152     -12.893 -11.370  -5.070  1.00115.49           C  
ANISOU 4308  CB  ALA B 152    17005  15277  11598   3908   1288   -653       C  
ATOM   4309  N   GLU B 153     -11.512 -14.394  -4.350  1.00119.56           N  
ANISOU 4309  N   GLU B 153    18350  14893  12185   4347   1689   -924       N  
ATOM   4310  CA  GLU B 153     -11.778 -15.833  -4.249  1.00122.14           C  
ANISOU 4310  CA  GLU B 153    19206  14739  12464   4330   1762  -1284       C  
ATOM   4311  C   GLU B 153     -10.813 -16.484  -3.228  1.00126.01           C  
ANISOU 4311  C   GLU B 153    19729  14921  13229   4557   1958  -1014       C  
ATOM   4312  O   GLU B 153     -11.253 -17.313  -2.426  1.00126.34           O  
ANISOU 4312  O   GLU B 153    20020  14544  13438   4341   1919  -1164       O  
ATOM   4313  CB  GLU B 153     -12.212 -16.390  -5.623  1.00127.67           C  
ANISOU 4313  CB  GLU B 153    20316  15459  12733   4416   1802  -1721       C  
ATOM   4314  CG  GLU B 153     -13.489 -15.771  -6.176  1.00136.50           C  
ANISOU 4314  CG  GLU B 153    21326  16877  13660   4013   1504  -1965       C  
ATOM   4315  CD  GLU B 153     -13.949 -16.242  -7.543  1.00162.13           C  
ANISOU 4315  CD  GLU B 153    24932  20242  16429   4049   1504  -2394       C  
ATOM   4316  OE1 GLU B 153     -13.102 -16.379  -8.457  1.00161.06           O  
ANISOU 4316  OE1 GLU B 153    24931  20235  16029   4510   1745  -2368       O  
ATOM   4317  OE2 GLU B 153     -15.176 -16.415  -7.718  1.00155.68           O  
ANISOU 4317  OE2 GLU B 153    24227  19447  15478   3606   1253  -2744       O  
ATOM   4318  N   LYS B 154      -9.512 -16.107  -3.247  1.00122.04           N  
ANISOU 4318  N   LYS B 154    18949  14656  12767   4985   2168   -587       N  
ATOM   4319  CA  LYS B 154      -8.487 -16.654  -2.344  1.00122.36           C  
ANISOU 4319  CA  LYS B 154    18939  14523  13027   5259   2363   -254       C  
ATOM   4320  C   LYS B 154      -7.897 -15.819  -1.200  1.00122.29           C  
ANISOU 4320  C   LYS B 154    18388  14760  13316   5146   2278    225       C  
ATOM   4321  O   LYS B 154      -7.814 -16.312  -0.072  1.00120.94           O  
ANISOU 4321  O   LYS B 154    18223  14356  13372   5051   2263    341       O  
ATOM   4322  CB  LYS B 154      -7.406 -16.974  -3.412  1.00128.96           C  
ANISOU 4322  CB  LYS B 154    19890  15503  13605   5878   2699   -147       C  
ATOM   4323  CG  LYS B 154      -6.186 -17.742  -2.903  1.00146.38           C  
ANISOU 4323  CG  LYS B 154    22120  17573  15924   6365   3007    193       C  
ATOM   4324  CD  LYS B 154      -5.085 -17.814  -3.965  1.00160.19           C  
ANISOU 4324  CD  LYS B 154    23866  19586  17414   6992   3341    375       C  
ATOM   4325  CE  LYS B 154      -3.857 -18.582  -3.524  1.00172.18           C  
ANISOU 4325  CE  LYS B 154    25380  21019  19020   7544   3678    755       C  
ATOM   4326  NZ  LYS B 154      -3.007 -17.804  -2.580  1.00176.38           N  
ANISOU 4326  NZ  LYS B 154    25252  21966  19799   7519   3615   1344       N  
ATOM   4327  N   VAL B 155      -7.468 -14.572  -1.501  1.00116.95           N  
ANISOU 4327  N   VAL B 155    17259  14552  12624   5151   2233    504       N  
ATOM   4328  CA  VAL B 155      -6.827 -13.660  -0.542  1.00114.00           C  
ANISOU 4328  CA  VAL B 155    16369  14454  12492   5012   2159    942       C  
ATOM   4329  C   VAL B 155      -7.780 -13.238   0.583  1.00114.23           C  
ANISOU 4329  C   VAL B 155    16299  14353  12752   4458   1873    845       C  
ATOM   4330  O   VAL B 155      -7.337 -13.086   1.723  1.00112.58           O  
ANISOU 4330  O   VAL B 155    15842  14183  12751   4334   1827   1112       O  
ATOM   4331  CB  VAL B 155      -6.116 -12.459  -1.231  1.00117.51           C  
ANISOU 4331  CB  VAL B 155    16404  15389  12858   5136   2214   1253       C  
ATOM   4332  CG1 VAL B 155      -5.288 -11.648  -0.235  1.00115.60           C  
ANISOU 4332  CG1 VAL B 155    15659  15415  12849   4988   2166   1705       C  
ATOM   4333  CG2 VAL B 155      -5.230 -12.932  -2.381  1.00121.49           C  
ANISOU 4333  CG2 VAL B 155    17019  16040  13103   5710   2516   1341       C  
ATOM   4334  N   VAL B 156      -9.085 -13.103   0.272  1.00109.56           N  
ANISOU 4334  N   VAL B 156    15897  13633  12097   4138   1689    469       N  
ATOM   4335  CA  VAL B 156     -10.136 -12.727   1.225  1.00106.21           C  
ANISOU 4335  CA  VAL B 156    15404  13093  11857   3638   1436    345       C  
ATOM   4336  C   VAL B 156     -10.247 -13.681   2.443  1.00110.92           C  
ANISOU 4336  C   VAL B 156    16157  13350  12640   3512   1417    330       C  
ATOM   4337  O   VAL B 156     -10.454 -13.214   3.562  1.00108.25           O  
ANISOU 4337  O   VAL B 156    15597  13037  12496   3208   1276    455       O  
ATOM   4338  CB  VAL B 156     -11.492 -12.435   0.522  1.00109.20           C  
ANISOU 4338  CB  VAL B 156    15922  13475  12094   3377   1265    -17       C  
ATOM   4339  CG1 VAL B 156     -12.141 -13.705  -0.026  1.00111.72           C  
ANISOU 4339  CG1 VAL B 156    16726  13482  12240   3396   1286   -426       C  
ATOM   4340  CG2 VAL B 156     -12.448 -11.672   1.437  1.00105.63           C  
ANISOU 4340  CG2 VAL B 156    15271  13033  11830   2918   1035    -37       C  
ATOM   4341  N   TYR B 157     -10.064 -14.997   2.229  1.00110.78           N  
ANISOU 4341  N   TYR B 157    16531  13009  12552   3765   1581    194       N  
ATOM   4342  CA  TYR B 157     -10.146 -15.998   3.297  1.00111.19           C  
ANISOU 4342  CA  TYR B 157    16774  12700  12772   3696   1605    207       C  
ATOM   4343  C   TYR B 157      -8.867 -16.064   4.132  1.00115.31           C  
ANISOU 4343  C   TYR B 157    17026  13361  13425   3964   1741    677       C  
ATOM   4344  O   TYR B 157      -8.949 -16.243   5.345  1.00113.87           O  
ANISOU 4344  O   TYR B 157    16752  13093  13421   3771   1662    816       O  
ATOM   4345  CB  TYR B 157     -10.541 -17.376   2.739  1.00116.25           C  
ANISOU 4345  CB  TYR B 157    17992  12878  13299   3826   1742   -140       C  
ATOM   4346  CG  TYR B 157     -11.774 -17.334   1.858  1.00118.33           C  
ANISOU 4346  CG  TYR B 157    18495  13081  13386   3530   1588   -606       C  
ATOM   4347  CD1 TYR B 157     -11.665 -17.350   0.470  1.00122.78           C  
ANISOU 4347  CD1 TYR B 157    19237  13754  13661   3768   1684   -807       C  
ATOM   4348  CD2 TYR B 157     -13.047 -17.232   2.410  1.00117.07           C  
ANISOU 4348  CD2 TYR B 157    18341  12820  13321   3011   1340   -821       C  
ATOM   4349  CE1 TYR B 157     -12.794 -17.290  -0.346  1.00124.09           C  
ANISOU 4349  CE1 TYR B 157    19581  13945  13623   3481   1519  -1217       C  
ATOM   4350  CE2 TYR B 157     -14.184 -17.171   1.604  1.00118.52           C  
ANISOU 4350  CE2 TYR B 157    18680  13031  13321   2728   1182  -1212       C  
ATOM   4351  CZ  TYR B 157     -14.052 -17.198   0.225  1.00128.81           C  
ANISOU 4351  CZ  TYR B 157    20154  14464  14324   2955   1261  -1410       C  
ATOM   4352  OH  TYR B 157     -15.171 -17.137  -0.573  1.00131.06           O  
ANISOU 4352  OH  TYR B 157    20561  14845  14389   2663   1085  -1781       O  
ATOM   4353  N   VAL B 158      -7.696 -15.882   3.492  1.00113.61           N  
ANISOU 4353  N   VAL B 158    16648  13417  13103   4400   1938    943       N  
ATOM   4354  CA  VAL B 158      -6.384 -15.897   4.156  1.00114.70           C  
ANISOU 4354  CA  VAL B 158    16457  13799  13324   4685   2072   1437       C  
ATOM   4355  C   VAL B 158      -6.045 -14.546   4.846  1.00115.01           C  
ANISOU 4355  C   VAL B 158    15936  14289  13472   4373   1882   1729       C  
ATOM   4356  O   VAL B 158      -5.245 -14.490   5.786  1.00115.28           O  
ANISOU 4356  O   VAL B 158    15661  14535  13604   4397   1886   2099       O  
ATOM   4357  CB  VAL B 158      -5.361 -16.858   3.461  1.00123.67           C  
ANISOU 4357  CB  VAL B 158    17793  14869  14328   5336   2424   1590       C  
ATOM   4358  CG1 VAL B 158      -4.324 -17.378   4.458  1.00125.53           C  
ANISOU 4358  CG1 VAL B 158    17817  15197  14683   5613   2561   2061       C  
ATOM   4359  CG2 VAL B 158      -6.064 -18.028   2.772  1.00126.34           C  
ANISOU 4359  CG2 VAL B 158    18781  14669  14554   5468   2557   1147       C  
ATOM   4360  N   GLY B 159      -6.662 -13.474   4.346  1.00108.50           N  
ANISOU 4360  N   GLY B 159    15003  13609  12615   4081   1727   1557       N  
ATOM   4361  CA  GLY B 159      -6.461 -12.118   4.849  1.00105.67           C  
ANISOU 4361  CA  GLY B 159    14200  13596  12352   3756   1570   1764       C  
ATOM   4362  C   GLY B 159      -7.499 -11.359   5.649  1.00105.56           C  
ANISOU 4362  C   GLY B 159    14125  13513  12469   3219   1319   1588       C  
ATOM   4363  O   GLY B 159      -7.145 -10.496   6.459  1.00103.45           O  
ANISOU 4363  O   GLY B 159    13528  13472  12305   2958   1218   1797       O  
ATOM   4364  N   VAL B 160      -8.786 -11.668   5.416  1.00100.82           N  
ANISOU 4364  N   VAL B 160    13842  12618  11848   3045   1223   1202       N  
ATOM   4365  CA  VAL B 160      -9.905 -11.044   6.123  1.00 97.46           C  
ANISOU 4365  CA  VAL B 160    13385  12115  11530   2582   1012   1022       C  
ATOM   4366  C   VAL B 160     -10.473 -12.032   7.145  1.00100.05           C  
ANISOU 4366  C   VAL B 160    13916  12145  11952   2428    951    910       C  
ATOM   4367  O   VAL B 160     -10.487 -11.721   8.336  1.00 98.60           O  
ANISOU 4367  O   VAL B 160    13557  12016  11889   2173    850   1031       O  
ATOM   4368  CB  VAL B 160     -11.008 -10.481   5.176  1.00100.48           C  
ANISOU 4368  CB  VAL B 160    13877  12482  11818   2458    930    731       C  
ATOM   4369  CG1 VAL B 160     -12.079  -9.730   5.958  1.00 97.55           C  
ANISOU 4369  CG1 VAL B 160    13421  12079  11565   2031    746    612       C  
ATOM   4370  CG2 VAL B 160     -10.414  -9.583   4.096  1.00100.80           C  
ANISOU 4370  CG2 VAL B 160    13737  12810  11751   2657   1022    877       C  
ATOM   4371  N   TRP B 161     -10.932 -13.217   6.680  1.00 96.93           N  
ANISOU 4371  N   TRP B 161    13905  11433  11492   2568   1021    676       N  
ATOM   4372  CA  TRP B 161     -11.549 -14.241   7.525  1.00 96.54           C  
ANISOU 4372  CA  TRP B 161    14101  11046  11536   2416    988    560       C  
ATOM   4373  C   TRP B 161     -10.647 -14.927   8.549  1.00100.22           C  
ANISOU 4373  C   TRP B 161    14508  11472  12100   2582   1089    880       C  
ATOM   4374  O   TRP B 161     -10.912 -14.806   9.748  1.00 98.36           O  
ANISOU 4374  O   TRP B 161    14141  11253  11977   2312    975    974       O  
ATOM   4375  CB  TRP B 161     -12.390 -15.231   6.706  1.00 97.27           C  
ANISOU 4375  CB  TRP B 161    14642  10788  11530   2432   1024    186       C  
ATOM   4376  CG  TRP B 161     -13.649 -14.617   6.167  1.00 96.42           C  
ANISOU 4376  CG  TRP B 161    14542  10742  11350   2111    844   -123       C  
ATOM   4377  CD1 TRP B 161     -13.888 -14.237   4.880  1.00 99.90           C  
ANISOU 4377  CD1 TRP B 161    15029  11325  11602   2202    841   -301       C  
ATOM   4378  CD2 TRP B 161     -14.806 -14.230   6.921  1.00 93.92           C  
ANISOU 4378  CD2 TRP B 161    14135  10419  11132   1676    649   -239       C  
ATOM   4379  NE1 TRP B 161     -15.139 -13.675   4.776  1.00 97.61           N  
ANISOU 4379  NE1 TRP B 161    14677  11122  11288   1856    650   -511       N  
ATOM   4380  CE2 TRP B 161     -15.722 -13.650   6.016  1.00 97.22           C  
ANISOU 4380  CE2 TRP B 161    14539  10980  11419   1537    538   -475       C  
ATOM   4381  CE3 TRP B 161     -15.163 -14.325   8.278  1.00 93.70           C  
ANISOU 4381  CE3 TRP B 161    14025  10307  11272   1410    569   -148       C  
ATOM   4382  CZ2 TRP B 161     -16.974 -13.169   6.422  1.00 94.75           C  
ANISOU 4382  CZ2 TRP B 161    14120  10729  11151   1163    361   -607       C  
ATOM   4383  CZ3 TRP B 161     -16.400 -13.846   8.678  1.00 93.27           C  
ANISOU 4383  CZ3 TRP B 161    13885  10296  11256   1032    400   -301       C  
ATOM   4384  CH2 TRP B 161     -17.292 -13.281   7.757  1.00 93.49           C  
ANISOU 4384  CH2 TRP B 161    13890  10467  11166    920    303   -521       C  
ATOM   4385  N   ILE B 162      -9.599 -15.643   8.091  1.00 98.61           N  
ANISOU 4385  N   ILE B 162    14392  11240  11833   3046   1313   1065       N  
ATOM   4386  CA  ILE B 162      -8.649 -16.343   8.964  1.00 99.96           C  
ANISOU 4386  CA  ILE B 162    14484  11420  12074   3296   1443   1433       C  
ATOM   4387  C   ILE B 162      -7.952 -15.417  10.004  1.00100.59           C  
ANISOU 4387  C   ILE B 162    14053  11954  12211   3133   1321   1797       C  
ATOM   4388  O   ILE B 162      -8.082 -15.714  11.195  1.00 99.91           O  
ANISOU 4388  O   ILE B 162    13911  11838  12212   2964   1250   1924       O  
ATOM   4389  CB  ILE B 162      -7.735 -17.352   8.191  1.00107.29           C  
ANISOU 4389  CB  ILE B 162    15647  12204  12915   3885   1748   1555       C  
ATOM   4390  CG1 ILE B 162      -8.487 -18.682   7.947  1.00110.12           C  
ANISOU 4390  CG1 ILE B 162    16592  11963  13284   3940   1867   1241       C  
ATOM   4391  CG2 ILE B 162      -6.396 -17.606   8.891  1.00110.36           C  
ANISOU 4391  CG2 ILE B 162    15739  12859  13333   4235   1891   2080       C  
ATOM   4392  CD1 ILE B 162      -8.212 -19.372   6.597  1.00118.78           C  
ANISOU 4392  CD1 ILE B 162    18084  12828  14219   4362   2117   1046       C  
ATOM   4393  N   PRO B 163      -7.313 -14.269   9.629  1.00 94.70           N  
ANISOU 4393  N   PRO B 163    12945  11623  11413   3113   1280   1944       N  
ATOM   4394  CA  PRO B 163      -6.696 -13.404  10.656  1.00 93.13           C  
ANISOU 4394  CA  PRO B 163    12297  11833  11256   2874   1150   2244       C  
ATOM   4395  C   PRO B 163      -7.669 -12.814  11.683  1.00 93.83           C  
ANISOU 4395  C   PRO B 163    12349  11877  11425   2349    922   2068       C  
ATOM   4396  O   PRO B 163      -7.249 -12.543  12.807  1.00 93.32           O  
ANISOU 4396  O   PRO B 163    12021  12058  11378   2165    830   2292       O  
ATOM   4397  CB  PRO B 163      -5.989 -12.318   9.836  1.00 94.55           C  
ANISOU 4397  CB  PRO B 163    12185  12370  11370   2920   1171   2364       C  
ATOM   4398  CG  PRO B 163      -5.818 -12.915   8.483  1.00100.85           C  
ANISOU 4398  CG  PRO B 163    13230  13021  12069   3363   1377   2277       C  
ATOM   4399  CD  PRO B 163      -7.052 -13.730   8.280  1.00 96.06           C  
ANISOU 4399  CD  PRO B 163    13100  11926  11475   3303   1362   1871       C  
ATOM   4400  N   ALA B 164      -8.962 -12.642  11.317  1.00 88.25           N  
ANISOU 4400  N   ALA B 164    11895  10892  10745   2119    838   1681       N  
ATOM   4401  CA  ALA B 164      -9.987 -12.131  12.236  1.00 85.41           C  
ANISOU 4401  CA  ALA B 164    11523  10475  10453   1668    656   1506       C  
ATOM   4402  C   ALA B 164     -10.426 -13.239  13.186  1.00 89.58           C  
ANISOU 4402  C   ALA B 164    12237  10763  11036   1625    653   1512       C  
ATOM   4403  O   ALA B 164     -10.575 -12.986  14.382  1.00 87.72           O  
ANISOU 4403  O   ALA B 164    11856  10643  10830   1360    545   1597       O  
ATOM   4404  CB  ALA B 164     -11.183 -11.594  11.467  1.00 84.14           C  
ANISOU 4404  CB  ALA B 164    11521  10161  10289   1489    587   1150       C  
ATOM   4405  N   LEU B 165     -10.598 -14.474  12.659  1.00 88.77           N  
ANISOU 4405  N   LEU B 165    12473  10318  10937   1887    789   1427       N  
ATOM   4406  CA  LEU B 165     -10.978 -15.651  13.445  1.00 90.21           C  
ANISOU 4406  CA  LEU B 165    12886  10201  11190   1882    832   1456       C  
ATOM   4407  C   LEU B 165      -9.828 -16.151  14.329  1.00 96.36           C  
ANISOU 4407  C   LEU B 165    13481  11160  11970   2126    923   1898       C  
ATOM   4408  O   LEU B 165     -10.073 -16.871  15.295  1.00 97.09           O  
ANISOU 4408  O   LEU B 165    13659  11113  12119   2066    930   2010       O  
ATOM   4409  CB  LEU B 165     -11.527 -16.772  12.553  1.00 92.35           C  
ANISOU 4409  CB  LEU B 165    13620  10005  11464   2047    963   1200       C  
ATOM   4410  CG  LEU B 165     -12.924 -17.273  12.922  1.00 96.59           C  
ANISOU 4410  CG  LEU B 165    14420  10207  12075   1689    872    917       C  
ATOM   4411  CD1 LEU B 165     -13.689 -17.709  11.689  1.00 97.85           C  
ANISOU 4411  CD1 LEU B 165    14935  10066  12177   1673    901    529       C  
ATOM   4412  CD2 LEU B 165     -12.860 -18.400  13.944  1.00101.61           C  
ANISOU 4412  CD2 LEU B 165    15212  10588  12807   1733    967   1119       C  
ATOM   4413  N   LEU B 166      -8.582 -15.758  14.010  1.00 93.74           N  
ANISOU 4413  N   LEU B 166    12871  11180  11568   2398    994   2179       N  
ATOM   4414  CA  LEU B 166      -7.414 -16.086  14.822  1.00 95.98           C  
ANISOU 4414  CA  LEU B 166    12880  11769  11821   2627   1059   2649       C  
ATOM   4415  C   LEU B 166      -7.171 -14.976  15.858  1.00 98.44           C  
ANISOU 4415  C   LEU B 166    12761  12553  12087   2238    843   2791       C  
ATOM   4416  O   LEU B 166      -6.420 -15.170  16.811  1.00100.09           O  
ANISOU 4416  O   LEU B 166    12710  13076  12245   2290    828   3155       O  
ATOM   4417  CB  LEU B 166      -6.169 -16.336  13.955  1.00 98.84           C  
ANISOU 4417  CB  LEU B 166    13140  12302  12114   3142   1266   2916       C  
ATOM   4418  CG  LEU B 166      -6.088 -17.693  13.237  1.00106.74           C  
ANISOU 4418  CG  LEU B 166    14570  12853  13131   3635   1546   2895       C  
ATOM   4419  CD1 LEU B 166      -4.909 -17.727  12.306  1.00109.59           C  
ANISOU 4419  CD1 LEU B 166    14802  13439  13399   4135   1754   3131       C  
ATOM   4420  CD2 LEU B 166      -5.975 -18.859  14.226  1.00111.46           C  
ANISOU 4420  CD2 LEU B 166    15302  13253  13794   3816   1660   3161       C  
ATOM   4421  N   LEU B 167      -7.847 -13.828  15.684  1.00 92.28           N  
ANISOU 4421  N   LEU B 167    11930  11819  11314   1846    685   2497       N  
ATOM   4422  CA  LEU B 167      -7.792 -12.671  16.582  1.00 90.82           C  
ANISOU 4422  CA  LEU B 167    11434  11989  11085   1421    494   2525       C  
ATOM   4423  C   LEU B 167      -8.952 -12.756  17.586  1.00 91.21           C  
ANISOU 4423  C   LEU B 167    11634  11853  11168   1075    377   2325       C  
ATOM   4424  O   LEU B 167      -9.091 -11.919  18.482  1.00 89.12           O  
ANISOU 4424  O   LEU B 167    11189  11820  10853    711    233   2301       O  
ATOM   4425  CB  LEU B 167      -7.878 -11.380  15.742  1.00 89.40           C  
ANISOU 4425  CB  LEU B 167    11164  11899  10906   1245    443   2331       C  
ATOM   4426  CG  LEU B 167      -7.339 -10.060  16.322  1.00 94.29           C  
ANISOU 4426  CG  LEU B 167    11436  12918  11470    886    310   2422       C  
ATOM   4427  CD1 LEU B 167      -6.050 -10.251  17.117  1.00 97.57           C  
ANISOU 4427  CD1 LEU B 167    11494  13794  11785    939    286   2843       C  
ATOM   4428  CD2 LEU B 167      -7.096  -9.075  15.219  1.00 96.02           C  
ANISOU 4428  CD2 LEU B 167    11582  13195  11706    884    347   2350       C  
ATOM   4429  N   THR B 168      -9.759 -13.810  17.435  1.00 87.53           N  
ANISOU 4429  N   THR B 168    11511  10968  10779   1191    457   2188       N  
ATOM   4430  CA  THR B 168     -10.905 -14.146  18.265  1.00 86.24           C  
ANISOU 4430  CA  THR B 168    11519  10587  10660    920    388   2028       C  
ATOM   4431  C   THR B 168     -10.442 -14.915  19.528  1.00 92.21           C  
ANISOU 4431  C   THR B 168    12182  11476  11378    981    404   2374       C  
ATOM   4432  O   THR B 168     -11.174 -14.970  20.520  1.00 91.13           O  
ANISOU 4432  O   THR B 168    12071  11318  11236    711    324   2329       O  
ATOM   4433  CB  THR B 168     -11.951 -14.833  17.373  1.00 94.13           C  
ANISOU 4433  CB  THR B 168    12907  11108  11752    970    459   1717       C  
ATOM   4434  OG1 THR B 168     -13.151 -14.068  17.387  1.00 92.91           O  
ANISOU 4434  OG1 THR B 168    12782  10903  11616    608    334   1399       O  
ATOM   4435  CG2 THR B 168     -12.203 -16.307  17.728  1.00 94.93           C  
ANISOU 4435  CG2 THR B 168    13294  10854  11922   1118    580   1807       C  
ATOM   4436  N   ILE B 169      -9.211 -15.484  19.472  1.00 91.26           N  
ANISOU 4436  N   ILE B 169    11929  11529  11216   1360    519   2747       N  
ATOM   4437  CA  ILE B 169      -8.536 -16.241  20.532  1.00 93.69           C  
ANISOU 4437  CA  ILE B 169    12095  12037  11465   1528    563   3173       C  
ATOM   4438  C   ILE B 169      -8.489 -15.486  21.891  1.00 97.22           C  
ANISOU 4438  C   ILE B 169    12224  12942  11772   1141    362   3278       C  
ATOM   4439  O   ILE B 169      -9.000 -16.058  22.854  1.00 97.48           O  
ANISOU 4439  O   ILE B 169    12340  12903  11796   1048    352   3358       O  
ATOM   4440  CB  ILE B 169      -7.166 -16.826  20.054  1.00 99.89           C  
ANISOU 4440  CB  ILE B 169    12745  12993  12216   2054    739   3573       C  
ATOM   4441  CG1 ILE B 169      -7.379 -17.838  18.895  1.00101.41           C  
ANISOU 4441  CG1 ILE B 169    13372  12629  12532   2451    979   3442       C  
ATOM   4442  CG2 ILE B 169      -6.376 -17.460  21.216  1.00103.76           C  
ANISOU 4442  CG2 ILE B 169    12995  13819  12612   2237    768   4086       C  
ATOM   4443  CD1 ILE B 169      -6.144 -18.193  18.040  1.00109.37           C  
ANISOU 4443  CD1 ILE B 169    14296  13758  13503   2995   1186   3722       C  
ATOM   4444  N   PRO B 170      -7.960 -14.228  22.018  1.00 92.99           N  
ANISOU 4444  N   PRO B 170    11361  12850  11120    881    210   3257       N  
ATOM   4445  CA  PRO B 170      -7.979 -13.554  23.336  1.00 92.92           C  
ANISOU 4445  CA  PRO B 170    11115  13240  10948    481     27   3300       C  
ATOM   4446  C   PRO B 170      -9.374 -13.442  23.960  1.00 95.29           C  
ANISOU 4446  C   PRO B 170    11652  13275  11280    153    -33   2984       C  
ATOM   4447  O   PRO B 170      -9.510 -13.630  25.166  1.00 95.98           O  
ANISOU 4447  O   PRO B 170    11659  13565  11245     -1   -100   3118       O  
ATOM   4448  CB  PRO B 170      -7.378 -12.172  23.050  1.00 93.79           C  
ANISOU 4448  CB  PRO B 170    10959  13699  10978    220    -93   3207       C  
ATOM   4449  CG  PRO B 170      -7.456 -12.001  21.583  1.00 96.79           C  
ANISOU 4449  CG  PRO B 170    11494  13776  11507    418     16   3023       C  
ATOM   4450  CD  PRO B 170      -7.306 -13.371  21.009  1.00 93.95           C  
ANISOU 4450  CD  PRO B 170    11327  13128  11241    918    208   3200       C  
ATOM   4451  N   ASP B 171     -10.409 -13.181  23.132  1.00 89.32           N  
ANISOU 4451  N   ASP B 171    11168  12100  10669     71     -1   2596       N  
ATOM   4452  CA  ASP B 171     -11.807 -13.090  23.571  1.00 87.03           C  
ANISOU 4452  CA  ASP B 171    11086  11561  10422   -206    -37   2304       C  
ATOM   4453  C   ASP B 171     -12.329 -14.461  23.999  1.00 91.14           C  
ANISOU 4453  C   ASP B 171    11814  11802  11013    -62     60   2442       C  
ATOM   4454  O   ASP B 171     -13.111 -14.532  24.940  1.00 90.54           O  
ANISOU 4454  O   ASP B 171    11777  11730  10896   -291     19   2400       O  
ATOM   4455  CB  ASP B 171     -12.695 -12.479  22.476  1.00 86.38           C  
ANISOU 4455  CB  ASP B 171    11187  11172  10462   -289    -25   1912       C  
ATOM   4456  CG  ASP B 171     -12.239 -11.096  22.055  1.00 99.20           C  
ANISOU 4456  CG  ASP B 171    12637  13017  12037   -433    -91   1794       C  
ATOM   4457  OD1 ASP B 171     -12.740 -10.106  22.630  1.00 98.96           O  
ANISOU 4457  OD1 ASP B 171    12568  13088  11945   -755   -168   1609       O  
ATOM   4458  OD2 ASP B 171     -11.342 -11.006  21.185  1.00107.04           O  
ANISOU 4458  OD2 ASP B 171    13541  14082  13049   -218    -47   1904       O  
ATOM   4459  N   PHE B 172     -11.862 -15.546  23.342  1.00 88.98           N  
ANISOU 4459  N   PHE B 172    11684  11284  10839    323    209   2622       N  
ATOM   4460  CA  PHE B 172     -12.240 -16.928  23.663  1.00 90.63           C  
ANISOU 4460  CA  PHE B 172    12140  11154  11140    490    343   2781       C  
ATOM   4461  C   PHE B 172     -11.744 -17.345  25.051  1.00 94.78           C  
ANISOU 4461  C   PHE B 172    12472  12005  11536    514    330   3190       C  
ATOM   4462  O   PHE B 172     -12.413 -18.120  25.734  1.00 95.82           O  
ANISOU 4462  O   PHE B 172    12762  11935  11710    460    386   3273       O  
ATOM   4463  CB  PHE B 172     -11.682 -17.912  22.615  1.00 94.91           C  
ANISOU 4463  CB  PHE B 172    12903  11359  11799    935    539   2884       C  
ATOM   4464  CG  PHE B 172     -12.714 -18.757  21.907  1.00 97.16           C  
ANISOU 4464  CG  PHE B 172    13624  11039  12252    930    649   2612       C  
ATOM   4465  CD1 PHE B 172     -12.858 -18.694  20.525  1.00 99.91           C  
ANISOU 4465  CD1 PHE B 172    14171  11126  12664   1032    699   2319       C  
ATOM   4466  CD2 PHE B 172     -13.527 -19.634  22.617  1.00101.07           C  
ANISOU 4466  CD2 PHE B 172    14330  11244  12826    802    704   2657       C  
ATOM   4467  CE1 PHE B 172     -13.822 -19.467  19.869  1.00101.65           C  
ANISOU 4467  CE1 PHE B 172    14793  10825  13004    968    777   2039       C  
ATOM   4468  CE2 PHE B 172     -14.489 -20.408  21.960  1.00104.92           C  
ANISOU 4468  CE2 PHE B 172    15217  11183  13464    725    793   2392       C  
ATOM   4469  CZ  PHE B 172     -14.628 -20.321  20.591  1.00102.45           C  
ANISOU 4469  CZ  PHE B 172    15097  10635  13193    796    820   2072       C  
ATOM   4470  N   ILE B 173     -10.568 -16.832  25.452  1.00 90.31           N  
ANISOU 4470  N   ILE B 173    11547  11970  10799    583    253   3462       N  
ATOM   4471  CA  ILE B 173      -9.919 -17.131  26.728  1.00 91.94           C  
ANISOU 4471  CA  ILE B 173    11493  12620  10821    620    215   3890       C  
ATOM   4472  C   ILE B 173     -10.456 -16.239  27.869  1.00 92.76           C  
ANISOU 4472  C   ILE B 173    11440  13069  10736    147     25   3743       C  
ATOM   4473  O   ILE B 173     -10.922 -16.760  28.883  1.00 93.62           O  
ANISOU 4473  O   ILE B 173    11584  13211  10777     73     35   3892       O  
ATOM   4474  CB  ILE B 173      -8.355 -17.041  26.579  1.00 97.34           C  
ANISOU 4474  CB  ILE B 173    11823  13779  11381    915    216   4278       C  
ATOM   4475  CG1 ILE B 173      -7.779 -17.876  25.388  1.00 99.29           C  
ANISOU 4475  CG1 ILE B 173    12236  13692  11797   1439    441   4418       C  
ATOM   4476  CG2 ILE B 173      -7.594 -17.281  27.893  1.00101.02           C  
ANISOU 4476  CG2 ILE B 173    11947  14829  11607    948    147   4759       C  
ATOM   4477  CD1 ILE B 173      -8.054 -19.432  25.343  1.00110.47           C  
ANISOU 4477  CD1 ILE B 173    14015  14582  13375   1832    697   4626       C  
ATOM   4478  N   PHE B 174     -10.387 -14.904  27.697  1.00 85.66           N  
ANISOU 4478  N   PHE B 174    10392  12408   9747   -160   -124   3456       N  
ATOM   4479  CA  PHE B 174     -10.729 -13.918  28.726  1.00 83.85           C  
ANISOU 4479  CA  PHE B 174    10029  12524   9307   -599   -286   3290       C  
ATOM   4480  C   PHE B 174     -12.192 -13.581  29.022  1.00 83.44           C  
ANISOU 4480  C   PHE B 174    10213  12189   9302   -891   -288   2916       C  
ATOM   4481  O   PHE B 174     -12.459 -13.068  30.111  1.00 83.56           O  
ANISOU 4481  O   PHE B 174    10140  12501   9109  -1180   -378   2866       O  
ATOM   4482  CB  PHE B 174      -9.829 -12.675  28.633  1.00 85.53           C  
ANISOU 4482  CB  PHE B 174     9964  13169   9366   -814   -429   3220       C  
ATOM   4483  CG  PHE B 174      -8.352 -13.011  28.635  1.00 90.23           C  
ANISOU 4483  CG  PHE B 174    10227  14207   9850   -569   -449   3669       C  
ATOM   4484  CD1 PHE B 174      -7.606 -12.945  27.466  1.00 93.23           C  
ANISOU 4484  CD1 PHE B 174    10539  14529  10357   -322   -384   3731       C  
ATOM   4485  CD2 PHE B 174      -7.720 -13.440  29.798  1.00 95.77           C  
ANISOU 4485  CD2 PHE B 174    10665  15418  10306   -555   -520   4067       C  
ATOM   4486  CE1 PHE B 174      -6.250 -13.277  27.462  1.00 97.46           C  
ANISOU 4486  CE1 PHE B 174    10734  15512  10786    -62   -382   4184       C  
ATOM   4487  CE2 PHE B 174      -6.364 -13.778  29.791  1.00101.92           C  
ANISOU 4487  CE2 PHE B 174    11092  16660  10972   -295   -532   4531       C  
ATOM   4488  CZ  PHE B 174      -5.639 -13.694  28.624  1.00 99.95           C  
ANISOU 4488  CZ  PHE B 174    10766  16347  10863    -46   -458   4590       C  
ATOM   4489  N   ALA B 175     -13.134 -13.889  28.108  1.00 76.57           N  
ANISOU 4489  N   ALA B 175     9626  10794   8675   -818   -187   2671       N  
ATOM   4490  CA  ALA B 175     -14.564 -13.642  28.355  1.00 74.21           C  
ANISOU 4490  CA  ALA B 175     9510  10265   8424  -1069   -177   2364       C  
ATOM   4491  C   ALA B 175     -15.135 -14.768  29.207  1.00 78.70           C  
ANISOU 4491  C   ALA B 175    10174  10732   8995  -1035   -103   2585       C  
ATOM   4492  O   ALA B 175     -14.971 -15.938  28.861  1.00 80.14           O  
ANISOU 4492  O   ALA B 175    10487  10640   9321   -769     10   2804       O  
ATOM   4493  CB  ALA B 175     -15.335 -13.534  27.048  1.00 72.64           C  
ANISOU 4493  CB  ALA B 175     9524   9626   8450  -1028   -119   2047       C  
ATOM   4494  N   ASN B 176     -15.779 -14.418  30.332  1.00 74.19           N  
ANISOU 4494  N   ASN B 176     9554  10375   8259  -1296   -145   2538       N  
ATOM   4495  CA  ASN B 176     -16.360 -15.376  31.277  1.00 75.34           C  
ANISOU 4495  CA  ASN B 176     9761  10488   8376  -1304    -73   2770       C  
ATOM   4496  C   ASN B 176     -17.543 -14.768  32.033  1.00 77.38           C  
ANISOU 4496  C   ASN B 176    10042  10831   8527  -1616    -86   2536       C  
ATOM   4497  O   ASN B 176     -17.697 -13.544  32.072  1.00 74.95           O  
ANISOU 4497  O   ASN B 176     9679  10694   8106  -1812   -156   2239       O  
ATOM   4498  CB  ASN B 176     -15.297 -15.867  32.273  1.00 78.58           C  
ANISOU 4498  CB  ASN B 176     9966  11319   8571  -1170   -100   3224       C  
ATOM   4499  CG  ASN B 176     -14.411 -16.969  31.752  1.00101.98           C  
ANISOU 4499  CG  ASN B 176    12956  14118  11673   -773      0   3588       C  
ATOM   4500  OD1 ASN B 176     -14.757 -18.153  31.793  1.00100.37           O  
ANISOU 4500  OD1 ASN B 176    12938  13577  11622   -600    148   3805       O  
ATOM   4501  ND2 ASN B 176     -13.229 -16.608  31.273  1.00 93.00           N  
ANISOU 4501  ND2 ASN B 176    11638  13215  10482   -615    -58   3681       N  
ATOM   4502  N   VAL B 177     -18.363 -15.631  32.658  1.00 75.07           N  
ANISOU 4502  N   VAL B 177     9839  10414   8269  -1649      6   2690       N  
ATOM   4503  CA  VAL B 177     -19.533 -15.216  33.430  1.00 74.22           C  
ANISOU 4503  CA  VAL B 177     9739  10406   8057  -1904     28   2532       C  
ATOM   4504  C   VAL B 177     -19.186 -14.996  34.909  1.00 78.79           C  
ANISOU 4504  C   VAL B 177    10149  11501   8285  -2005    -15   2731       C  
ATOM   4505  O   VAL B 177     -18.811 -15.937  35.616  1.00 81.01           O  
ANISOU 4505  O   VAL B 177    10381  11906   8494  -1888     22   3132       O  
ATOM   4506  CB  VAL B 177     -20.754 -16.153  33.212  1.00 78.57           C  
ANISOU 4506  CB  VAL B 177    10459  10557   8835  -1946    150   2551       C  
ATOM   4507  CG1 VAL B 177     -21.917 -15.796  34.136  1.00 78.60           C  
ANISOU 4507  CG1 VAL B 177    10419  10741   8704  -2182    193   2468       C  
ATOM   4508  CG2 VAL B 177     -21.204 -16.116  31.760  1.00 76.30           C  
ANISOU 4508  CG2 VAL B 177    10320   9850   8821  -1922    159   2265       C  
ATOM   4509  N   SER B 178     -19.321 -13.737  35.357  1.00 73.41           N  
ANISOU 4509  N   SER B 178     9400  11116   7378  -2217    -82   2446       N  
ATOM   4510  CA  SER B 178     -19.098 -13.302  36.731  1.00 74.82           C  
ANISOU 4510  CA  SER B 178     9450  11809   7169  -2374   -132   2519       C  
ATOM   4511  C   SER B 178     -20.385 -13.554  37.515  1.00 77.49           C  
ANISOU 4511  C   SER B 178     9851  12142   7449  -2482    -11   2521       C  
ATOM   4512  O   SER B 178     -21.419 -12.955  37.211  1.00 74.83           O  
ANISOU 4512  O   SER B 178     9609  11623   7198  -2586     59   2206       O  
ATOM   4513  CB  SER B 178     -18.728 -11.819  36.764  1.00 77.55           C  
ANISOU 4513  CB  SER B 178     9764  12385   7315  -2575   -227   2155       C  
ATOM   4514  OG  SER B 178     -18.773 -11.294  38.081  1.00 89.27           O  
ANISOU 4514  OG  SER B 178    11191  14324   8405  -2780   -255   2118       O  
ATOM   4515  N   GLU B 179     -20.324 -14.467  38.500  1.00 75.95           N  
ANISOU 4515  N   GLU B 179     9586  12161   7111  -2433     28   2916       N  
ATOM   4516  CA  GLU B 179     -21.449 -14.844  39.356  1.00 76.85           C  
ANISOU 4516  CA  GLU B 179     9726  12328   7146  -2526    156   3011       C  
ATOM   4517  C   GLU B 179     -21.662 -13.768  40.437  1.00 81.58           C  
ANISOU 4517  C   GLU B 179    10268  13401   7328  -2726    136   2797       C  
ATOM   4518  O   GLU B 179     -21.491 -14.042  41.627  1.00 84.35           O  
ANISOU 4518  O   GLU B 179    10520  14171   7356  -2758    138   3050       O  
ATOM   4519  CB  GLU B 179     -21.177 -16.222  39.991  1.00 81.33           C  
ANISOU 4519  CB  GLU B 179    10247  12947   7709  -2377    218   3556       C  
ATOM   4520  CG  GLU B 179     -22.044 -17.353  39.473  1.00 91.55           C  
ANISOU 4520  CG  GLU B 179    11688  13721   9374  -2321    369   3714       C  
ATOM   4521  CD  GLU B 179     -22.410 -18.370  40.540  1.00120.11           C  
ANISOU 4521  CD  GLU B 179    15278  17458  12901  -2305    495   4169       C  
ATOM   4522  OE1 GLU B 179     -21.614 -19.311  40.760  1.00118.73           O  
ANISOU 4522  OE1 GLU B 179    15089  17279  12744  -2097    522   4606       O  
ATOM   4523  OE2 GLU B 179     -23.479 -18.213  41.176  1.00114.68           O  
ANISOU 4523  OE2 GLU B 179    14573  16888  12114  -2478    583   4117       O  
ATOM   4524  N   ALA B 180     -22.018 -12.536  40.019  1.00 75.87           N  
ANISOU 4524  N   ALA B 180     9625  12607   6596  -2848    132   2332       N  
ATOM   4525  CA  ALA B 180     -22.229 -11.415  40.940  1.00 77.24           C  
ANISOU 4525  CA  ALA B 180     9817  13145   6386  -3033    146   2055       C  
ATOM   4526  C   ALA B 180     -23.526 -11.561  41.756  1.00 83.06           C  
ANISOU 4526  C   ALA B 180    10580  13972   7008  -3074    324   2081       C  
ATOM   4527  O   ALA B 180     -24.401 -12.351  41.385  1.00 82.43           O  
ANISOU 4527  O   ALA B 180    10503  13606   7209  -2998    432   2237       O  
ATOM   4528  CB  ALA B 180     -22.188 -10.089  40.194  1.00 75.89           C  
ANISOU 4528  CB  ALA B 180     9762  12798   6274  -3116    127   1582       C  
ATOM   4529  N   ASP B 181     -23.610 -10.836  42.896  1.00 81.92           N  
ANISOU 4529  N   ASP B 181    10448  14251   6426  -3208    356   1940       N  
ATOM   4530  CA  ASP B 181     -24.694 -10.895  43.888  1.00 83.80           C  
ANISOU 4530  CA  ASP B 181    10692  14703   6446  -3238    535   1985       C  
ATOM   4531  C   ASP B 181     -26.145 -10.916  43.404  1.00 85.68           C  
ANISOU 4531  C   ASP B 181    10971  14622   6962  -3177    730   1890       C  
ATOM   4532  O   ASP B 181     -26.870 -11.848  43.738  1.00 86.58           O  
ANISOU 4532  O   ASP B 181    11000  14743   7154  -3143    835   2206       O  
ATOM   4533  CB  ASP B 181     -24.487  -9.875  45.022  1.00 88.69           C  
ANISOU 4533  CB  ASP B 181    11377  15790   6532  -3395    544   1727       C  
ATOM   4534  CG  ASP B 181     -23.325 -10.213  45.945  1.00103.90           C  
ANISOU 4534  CG  ASP B 181    13176  18233   8067  -3478    371   1983       C  
ATOM   4535  OD1 ASP B 181     -23.410 -11.239  46.662  1.00106.26           O  
ANISOU 4535  OD1 ASP B 181    13339  18776   8258  -3403    398   2428       O  
ATOM   4536  OD2 ASP B 181     -22.340  -9.440  45.968  1.00112.12           O  
ANISOU 4536  OD2 ASP B 181    14242  19460   8898  -3631    211   1755       O  
ATOM   4537  N   ASP B 182     -26.567  -9.900  42.634  1.00 80.06           N  
ANISOU 4537  N   ASP B 182    10372  13655   6393  -3168    785   1489       N  
ATOM   4538  CA  ASP B 182     -27.943  -9.757  42.145  1.00 78.68           C  
ANISOU 4538  CA  ASP B 182    10198  13252   6445  -3097    966   1389       C  
ATOM   4539  C   ASP B 182     -28.157 -10.102  40.666  1.00 76.72           C  
ANISOU 4539  C   ASP B 182     9931  12544   6675  -3026    911   1376       C  
ATOM   4540  O   ASP B 182     -29.298 -10.106  40.196  1.00 75.20           O  
ANISOU 4540  O   ASP B 182     9691  12204   6677  -2985   1034   1342       O  
ATOM   4541  CB  ASP B 182     -28.424  -8.319  42.417  1.00 81.84           C  
ANISOU 4541  CB  ASP B 182    10739  13731   6623  -3089   1119    971       C  
ATOM   4542  CG  ASP B 182     -27.827  -7.237  41.522  1.00 93.89           C  
ANISOU 4542  CG  ASP B 182    12418  14994   8260  -3086   1052    600       C  
ATOM   4543  OD1 ASP B 182     -28.526  -6.233  41.263  1.00 96.20           O  
ANISOU 4543  OD1 ASP B 182    12826  15158   8569  -3007   1222    307       O  
ATOM   4544  OD2 ASP B 182     -26.658  -7.392  41.085  1.00 97.70           O  
ANISOU 4544  OD2 ASP B 182    12900  15408   8813  -3146    847    629       O  
ATOM   4545  N   ARG B 183     -27.066 -10.343  39.931  1.00 70.43           N  
ANISOU 4545  N   ARG B 183     9160  11561   6039  -3010    731   1400       N  
ATOM   4546  CA  ARG B 183     -27.096 -10.585  38.494  1.00 66.75           C  
ANISOU 4546  CA  ARG B 183     8709  10680   5974  -2938    667   1346       C  
ATOM   4547  C   ARG B 183     -25.775 -11.230  38.036  1.00 68.79           C  
ANISOU 4547  C   ARG B 183     8969  10829   6338  -2894    491   1516       C  
ATOM   4548  O   ARG B 183     -24.746 -11.046  38.680  1.00 68.61           O  
ANISOU 4548  O   ARG B 183     8930  11072   6066  -2926    400   1572       O  
ATOM   4549  CB  ARG B 183     -27.292  -9.212  37.809  1.00 63.92           C  
ANISOU 4549  CB  ARG B 183     8442  10196   5649  -2898    709    941       C  
ATOM   4550  CG  ARG B 183     -27.415  -9.213  36.313  1.00 67.81           C  
ANISOU 4550  CG  ARG B 183     8945  10320   6499  -2812    658    841       C  
ATOM   4551  CD  ARG B 183     -26.534  -8.124  35.749  1.00 70.73           C  
ANISOU 4551  CD  ARG B 183     9420  10602   6854  -2785    592    572       C  
ATOM   4552  NE  ARG B 183     -26.073  -8.470  34.409  1.00 74.68           N  
ANISOU 4552  NE  ARG B 183     9918  10805   7651  -2702    479    585       N  
ATOM   4553  CZ  ARG B 183     -26.728  -8.173  33.295  1.00 88.48           C  
ANISOU 4553  CZ  ARG B 183    11669  12323   9626  -2612    516    451       C  
ATOM   4554  NH1 ARG B 183     -26.244  -8.542  32.119  1.00 79.73           N  
ANISOU 4554  NH1 ARG B 183    10570  10979   8745  -2539    411    466       N  
ATOM   4555  NH2 ARG B 183     -27.872  -7.505  33.346  1.00 76.85           N  
ANISOU 4555  NH2 ARG B 183    10182  10885   8134  -2574    668    317       N  
ATOM   4556  N   TYR B 184     -25.813 -11.984  36.927  1.00 63.92           N  
ANISOU 4556  N   TYR B 184     8368   9849   6070  -2821    450   1598       N  
ATOM   4557  CA  TYR B 184     -24.624 -12.586  36.326  1.00 62.84           C  
ANISOU 4557  CA  TYR B 184     8252   9561   6065  -2721    324   1748       C  
ATOM   4558  C   TYR B 184     -24.147 -11.634  35.239  1.00 65.82           C  
ANISOU 4558  C   TYR B 184     8680   9780   6548  -2671    251   1439       C  
ATOM   4559  O   TYR B 184     -24.958 -11.169  34.431  1.00 63.84           O  
ANISOU 4559  O   TYR B 184     8468   9326   6464  -2664    302   1212       O  
ATOM   4560  CB  TYR B 184     -24.926 -13.974  35.722  1.00 63.34           C  
ANISOU 4560  CB  TYR B 184     8360   9275   6432  -2665    351   1990       C  
ATOM   4561  CG  TYR B 184     -25.097 -15.107  36.714  1.00 66.67           C  
ANISOU 4561  CG  TYR B 184     8752   9788   6790  -2689    424   2385       C  
ATOM   4562  CD1 TYR B 184     -25.231 -16.423  36.283  1.00 69.67           C  
ANISOU 4562  CD1 TYR B 184     9221   9812   7437  -2652    470   2632       C  
ATOM   4563  CD2 TYR B 184     -25.140 -14.863  38.085  1.00 68.73           C  
ANISOU 4563  CD2 TYR B 184     8920  10478   6715  -2754    463   2511       C  
ATOM   4564  CE1 TYR B 184     -25.399 -17.468  37.191  1.00 73.40           C  
ANISOU 4564  CE1 TYR B 184     9687  10329   7871  -2671    564   3027       C  
ATOM   4565  CE2 TYR B 184     -25.309 -15.898  38.999  1.00 71.96           C  
ANISOU 4565  CE2 TYR B 184     9293  10990   7058  -2761    544   2912       C  
ATOM   4566  CZ  TYR B 184     -25.450 -17.198  38.548  1.00 78.05           C  
ANISOU 4566  CZ  TYR B 184    10150  11377   8127  -2718    600   3184       C  
ATOM   4567  OH  TYR B 184     -25.620 -18.211  39.458  1.00 79.28           O  
ANISOU 4567  OH  TYR B 184    10288  11603   8232  -2723    705   3608       O  
ATOM   4568  N   ILE B 185     -22.840 -11.333  35.229  1.00 63.51           N  
ANISOU 4568  N   ILE B 185     8363   9619   6149  -2638    137   1460       N  
ATOM   4569  CA  ILE B 185     -22.215 -10.432  34.261  1.00 61.63           C  
ANISOU 4569  CA  ILE B 185     8158   9263   5995  -2605     69   1215       C  
ATOM   4570  C   ILE B 185     -21.402 -11.240  33.263  1.00 65.68           C  
ANISOU 4570  C   ILE B 185     8668   9552   6737  -2433     -1   1386       C  
ATOM   4571  O   ILE B 185     -20.650 -12.127  33.653  1.00 66.17           O  
ANISOU 4571  O   ILE B 185     8671   9717   6755  -2349    -40   1701       O  
ATOM   4572  CB  ILE B 185     -21.362  -9.345  35.004  1.00 65.90           C  
ANISOU 4572  CB  ILE B 185     8667  10149   6221  -2749      1   1081       C  
ATOM   4573  CG1 ILE B 185     -22.244  -8.296  35.726  1.00 67.07           C  
ANISOU 4573  CG1 ILE B 185     8901  10414   6167  -2893    114    795       C  
ATOM   4574  CG2 ILE B 185     -20.307  -8.673  34.111  1.00 65.63           C  
ANISOU 4574  CG2 ILE B 185     8624  10048   6264  -2732    -96    959       C  
ATOM   4575  CD1 ILE B 185     -22.950  -7.207  34.833  1.00 72.87           C  
ANISOU 4575  CD1 ILE B 185     9757  10864   7066  -2861    217    448       C  
ATOM   4576  N   CYS B 186     -21.549 -10.928  31.978  1.00 62.67           N  
ANISOU 4576  N   CYS B 186     8352   8878   6581  -2353      0   1193       N  
ATOM   4577  CA  CYS B 186     -20.759 -11.560  30.929  1.00 62.80           C  
ANISOU 4577  CA  CYS B 186     8390   8681   6791  -2169    -48   1305       C  
ATOM   4578  C   CYS B 186     -19.860 -10.514  30.313  1.00 64.13           C  
ANISOU 4578  C   CYS B 186     8518   8916   6932  -2151   -114   1147       C  
ATOM   4579  O   CYS B 186     -20.370  -9.523  29.800  1.00 62.03           O  
ANISOU 4579  O   CYS B 186     8300   8560   6710  -2206    -84    869       O  
ATOM   4580  CB  CYS B 186     -21.641 -12.224  29.874  1.00 62.83           C  
ANISOU 4580  CB  CYS B 186     8510   8300   7063  -2097      6   1234       C  
ATOM   4581  SG  CYS B 186     -20.813 -12.490  28.281  1.00 65.81           S  
ANISOU 4581  SG  CYS B 186     8960   8399   7645  -1873    -30   1202       S  
ATOM   4582  N   ASP B 187     -18.531 -10.728  30.391  1.00 61.41           N  
ANISOU 4582  N   ASP B 187     8070   8750   6513  -2071   -192   1354       N  
ATOM   4583  CA  ASP B 187     -17.454  -9.930  29.796  1.00 61.00           C  
ANISOU 4583  CA  ASP B 187     7938   8799   6442  -2055   -262   1293       C  
ATOM   4584  C   ASP B 187     -16.045 -10.468  30.011  1.00 66.84           C  
ANISOU 4584  C   ASP B 187     8507   9803   7089  -1939   -338   1625       C  
ATOM   4585  O   ASP B 187     -15.871 -11.516  30.630  1.00 68.71           O  
ANISOU 4585  O   ASP B 187     8702  10129   7278  -1830   -326   1928       O  
ATOM   4586  CB  ASP B 187     -17.577  -8.394  29.965  1.00 62.42           C  
ANISOU 4586  CB  ASP B 187     8132   9083   6501  -2286   -272    981       C  
ATOM   4587  CG  ASP B 187     -17.022  -7.791  31.232  1.00 74.43           C  
ANISOU 4587  CG  ASP B 187     9563  11010   7709  -2535   -344    985       C  
ATOM   4588  OD1 ASP B 187     -17.544  -8.114  32.318  1.00 77.43           O  
ANISOU 4588  OD1 ASP B 187     9950  11550   7920  -2622   -325   1039       O  
ATOM   4589  OD2 ASP B 187     -16.144  -6.911  31.129  1.00 78.89           O  
ANISOU 4589  OD2 ASP B 187    10061  11732   8182  -2675   -413    904       O  
ATOM   4590  N   ARG B 188     -15.047  -9.777  29.452  1.00 62.65           N  
ANISOU 4590  N   ARG B 188     7865   9396   6542  -1940   -400   1602       N  
ATOM   4591  CA  ARG B 188     -13.651 -10.180  29.524  1.00 63.92           C  
ANISOU 4591  CA  ARG B 188     7809   9863   6614  -1813   -469   1935       C  
ATOM   4592  C   ARG B 188     -12.990  -9.687  30.795  1.00 70.24           C  
ANISOU 4592  C   ARG B 188     8408  11194   7087  -2075   -593   2034       C  
ATOM   4593  O   ARG B 188     -13.143  -8.521  31.165  1.00 69.83           O  
ANISOU 4593  O   ARG B 188     8378  11259   6895  -2393   -643   1750       O  
ATOM   4594  CB  ARG B 188     -12.884  -9.718  28.275  1.00 61.20           C  
ANISOU 4594  CB  ARG B 188     7409   9440   6405  -1694   -470   1897       C  
ATOM   4595  CG  ARG B 188     -13.475 -10.210  26.950  1.00 61.92           C  
ANISOU 4595  CG  ARG B 188     7702   9051   6776  -1432   -357   1790       C  
ATOM   4596  CD  ARG B 188     -13.311  -9.188  25.846  1.00 68.72           C  
ANISOU 4596  CD  ARG B 188     8576   9802   7735  -1457   -350   1569       C  
ATOM   4597  NE  ARG B 188     -13.848  -7.881  26.242  1.00 76.94           N  
ANISOU 4597  NE  ARG B 188     9659  10878   8696  -1782   -376   1271       N  
ATOM   4598  CZ  ARG B 188     -13.774  -6.780  25.503  1.00 86.90           C  
ANISOU 4598  CZ  ARG B 188    10945  12052  10020  -1865   -357   1074       C  
ATOM   4599  NH1 ARG B 188     -14.277  -5.641  25.954  1.00 72.86           N  
ANISOU 4599  NH1 ARG B 188     9250  10264   8172  -2139   -346    816       N  
ATOM   4600  NH2 ARG B 188     -13.196  -6.810  24.307  1.00 72.30           N  
ANISOU 4600  NH2 ARG B 188     9056  10114   8301  -1657   -326   1144       N  
ATOM   4601  N   PHE B 189     -12.271 -10.581  31.471  1.00 69.52           N  
ANISOU 4601  N   PHE B 189     8133  11424   6857  -1940   -633   2437       N  
ATOM   4602  CA  PHE B 189     -11.552 -10.252  32.692  1.00 72.72           C  
ANISOU 4602  CA  PHE B 189     8300  12426   6903  -2176   -774   2589       C  
ATOM   4603  C   PHE B 189     -10.113 -10.664  32.475  1.00 81.70           C  
ANISOU 4603  C   PHE B 189     9129  13930   7982  -1982   -843   2996       C  
ATOM   4604  O   PHE B 189      -9.810 -11.856  32.379  1.00 82.60           O  
ANISOU 4604  O   PHE B 189     9191  14011   8182  -1608   -764   3383       O  
ATOM   4605  CB  PHE B 189     -12.173 -10.936  33.923  1.00 75.69           C  
ANISOU 4605  CB  PHE B 189     8708  12948   7104  -2197   -754   2742       C  
ATOM   4606  CG  PHE B 189     -13.655 -10.699  34.103  1.00 74.51           C  
ANISOU 4606  CG  PHE B 189     8836  12442   7031  -2326   -654   2404       C  
ATOM   4607  CD1 PHE B 189     -14.122  -9.537  34.706  1.00 77.03           C  
ANISOU 4607  CD1 PHE B 189     9231  12889   7149  -2677   -690   2042       C  
ATOM   4608  CD2 PHE B 189     -14.583 -11.648  33.687  1.00 74.64           C  
ANISOU 4608  CD2 PHE B 189     9041  12008   7310  -2101   -511   2457       C  
ATOM   4609  CE1 PHE B 189     -15.495  -9.319  34.871  1.00 76.21           C  
ANISOU 4609  CE1 PHE B 189     9354  12493   7108  -2747   -571   1768       C  
ATOM   4610  CE2 PHE B 189     -15.955 -11.429  33.853  1.00 75.71           C  
ANISOU 4610  CE2 PHE B 189     9376  11884   7506  -2227   -422   2182       C  
ATOM   4611  CZ  PHE B 189     -16.401 -10.267  34.445  1.00 73.64           C  
ANISOU 4611  CZ  PHE B 189     9155  11783   7043  -2522   -446   1857       C  
ATOM   4612  N   TYR B 190      -9.244  -9.660  32.306  1.00 81.12           N  
ANISOU 4612  N   TYR B 190     8864  14168   7788  -2225   -965   2909       N  
ATOM   4613  CA  TYR B 190      -7.814  -9.815  32.041  1.00 84.11           C  
ANISOU 4613  CA  TYR B 190     8887  14977   8092  -2099  -1044   3279       C  
ATOM   4614  C   TYR B 190      -7.020  -9.817  33.351  1.00 93.72           C  
ANISOU 4614  C   TYR B 190     9768  16942   8901  -2312  -1221   3564       C  
ATOM   4615  O   TYR B 190      -7.554  -9.352  34.362  1.00 94.03           O  
ANISOU 4615  O   TYR B 190     9888  17138   8700  -2656  -1298   3348       O  
ATOM   4616  CB  TYR B 190      -7.333  -8.687  31.112  1.00 84.28           C  
ANISOU 4616  CB  TYR B 190     8869  14946   8210  -2295  -1080   3037       C  
ATOM   4617  CG  TYR B 190      -8.028  -8.681  29.770  1.00 82.38           C  
ANISOU 4617  CG  TYR B 190     8918  14049   8334  -2061   -915   2800       C  
ATOM   4618  CD1 TYR B 190      -9.129  -7.861  29.537  1.00 81.40           C  
ANISOU 4618  CD1 TYR B 190     9102  13508   8318  -2276   -864   2333       C  
ATOM   4619  CD2 TYR B 190      -7.593  -9.501  28.733  1.00 82.93           C  
ANISOU 4619  CD2 TYR B 190     8956  13938   8617  -1606   -800   3050       C  
ATOM   4620  CE1 TYR B 190      -9.782  -7.859  28.305  1.00 79.00           C  
ANISOU 4620  CE1 TYR B 190     9031  12672   8315  -2062   -728   2139       C  
ATOM   4621  CE2 TYR B 190      -8.241  -9.511  27.498  1.00 80.77           C  
ANISOU 4621  CE2 TYR B 190     8951  13106   8633  -1409   -663   2817       C  
ATOM   4622  CZ  TYR B 190      -9.340  -8.693  27.290  1.00 85.52           C  
ANISOU 4622  CZ  TYR B 190     9820  13347   9325  -1647   -640   2372       C  
ATOM   4623  OH  TYR B 190      -9.971  -8.701  26.069  1.00 84.60           O  
ANISOU 4623  OH  TYR B 190     9932  12753   9461  -1454   -521   2170       O  
ATOM   4624  N   PRO B 191      -5.754 -10.326  33.368  1.00 95.01           N  
ANISOU 4624  N   PRO B 191     9538  17610   8950  -2104  -1284   4057       N  
ATOM   4625  CA  PRO B 191      -4.980 -10.351  34.628  1.00100.15           C  
ANISOU 4625  CA  PRO B 191     9818  19065   9171  -2308  -1473   4369       C  
ATOM   4626  C   PRO B 191      -4.611  -8.974  35.198  1.00107.49           C  
ANISOU 4626  C   PRO B 191    10616  20439   9785  -2963  -1696   4050       C  
ATOM   4627  O   PRO B 191      -4.854  -8.716  36.381  1.00109.50           O  
ANISOU 4627  O   PRO B 191    10864  21045   9697  -3292  -1816   3952       O  
ATOM   4628  CB  PRO B 191      -3.741 -11.191  34.275  1.00104.78           C  
ANISOU 4628  CB  PRO B 191    10010  20039   9764  -1868  -1453   4983       C  
ATOM   4629  CG  PRO B 191      -4.081 -11.890  33.003  1.00105.82           C  
ANISOU 4629  CG  PRO B 191    10405  19470  10331  -1362  -1206   4997       C  
ATOM   4630  CD  PRO B 191      -4.990 -10.958  32.275  1.00 96.77           C  
ANISOU 4630  CD  PRO B 191     9628  17736   9406  -1639  -1170   4384       C  
ATOM   4631  N   ASN B 192      -4.035  -8.091  34.364  1.00104.12           N  
ANISOU 4631  N   ASN B 192    10109  19987   9464  -3165  -1739   3881       N  
ATOM   4632  CA  ASN B 192      -3.642  -6.737  34.768  1.00106.24           C  
ANISOU 4632  CA  ASN B 192    10298  20589   9477  -3823  -1927   3554       C  
ATOM   4633  C   ASN B 192      -4.193  -5.692  33.794  1.00107.36           C  
ANISOU 4633  C   ASN B 192    10787  20088   9915  -4014  -1820   3044       C  
ATOM   4634  O   ASN B 192      -4.764  -6.062  32.760  1.00102.88           O  
ANISOU 4634  O   ASN B 192    10449  18915   9725  -3615  -1627   2997       O  
ATOM   4635  CB  ASN B 192      -2.108  -6.623  34.925  1.00111.22           C  
ANISOU 4635  CB  ASN B 192    10361  22044   9852  -3984  -2127   3962       C  
ATOM   4636  CG  ASN B 192      -1.291  -7.221  33.799  1.00132.07           C  
ANISOU 4636  CG  ASN B 192    12737  24686  12756  -3497  -2025   4390       C  
ATOM   4637  OD1 ASN B 192      -1.415  -6.846  32.632  1.00124.02           O  
ANISOU 4637  OD1 ASN B 192    11889  23166  12066  -3399  -1895   4200       O  
ATOM   4638  ND2 ASN B 192      -0.436  -8.175  34.129  1.00126.83           N  
ANISOU 4638  ND2 ASN B 192    11650  24603  11937  -3148  -2064   4999       N  
ATOM   4639  N   ASP B 193      -4.036  -4.391  34.124  1.00106.32           N  
ANISOU 4639  N   ASP B 193    10713  20081   9603  -4626  -1937   2666       N  
ATOM   4640  CA  ASP B 193      -4.509  -3.303  33.266  1.00103.84           C  
ANISOU 4640  CA  ASP B 193    10731  19172   9551  -4824  -1821   2209       C  
ATOM   4641  C   ASP B 193      -3.660  -3.157  31.994  1.00106.35           C  
ANISOU 4641  C   ASP B 193    10835  19448  10126  -4675  -1783   2414       C  
ATOM   4642  O   ASP B 193      -4.101  -2.515  31.042  1.00102.61           O  
ANISOU 4642  O   ASP B 193    10628  18418   9941  -4661  -1640   2140       O  
ATOM   4643  CB  ASP B 193      -4.622  -1.978  34.039  1.00108.74           C  
ANISOU 4643  CB  ASP B 193    11541  19870   9907  -5513  -1916   1737       C  
ATOM   4644  CG  ASP B 193      -5.942  -1.255  33.812  1.00120.25           C  
ANISOU 4644  CG  ASP B 193    13547  20580  11560  -5555  -1714   1209       C  
ATOM   4645  OD1 ASP B 193      -6.805  -1.294  34.719  1.00121.48           O  
ANISOU 4645  OD1 ASP B 193    13944  20674  11540  -5618  -1682    988       O  
ATOM   4646  OD2 ASP B 193      -6.113  -0.652  32.725  1.00124.70           O  
ANISOU 4646  OD2 ASP B 193    14285  20650  12446  -5500  -1577   1044       O  
ATOM   4647  N   LEU B 194      -2.456  -3.779  31.978  1.00105.86           N  
ANISOU 4647  N   LEU B 194    10277  19998   9946  -4525  -1895   2931       N  
ATOM   4648  CA  LEU B 194      -1.535  -3.795  30.841  1.00105.81           C  
ANISOU 4648  CA  LEU B 194     9993  20071  10140  -4321  -1851   3219       C  
ATOM   4649  C   LEU B 194      -2.158  -4.601  29.703  1.00105.00           C  
ANISOU 4649  C   LEU B 194    10123  19346  10426  -3658  -1606   3284       C  
ATOM   4650  O   LEU B 194      -2.144  -4.128  28.566  1.00102.94           O  
ANISOU 4650  O   LEU B 194     9962  18727  10425  -3584  -1490   3171       O  
ATOM   4651  CB  LEU B 194      -0.191  -4.432  31.238  1.00110.54           C  
ANISOU 4651  CB  LEU B 194     9986  21530  10486  -4233  -2007   3812       C  
ATOM   4652  CG  LEU B 194       1.112  -3.803  30.733  1.00118.80           C  
ANISOU 4652  CG  LEU B 194    10588  23066  11483  -4501  -2109   4039       C  
ATOM   4653  CD1 LEU B 194       2.287  -4.643  31.153  1.00123.62           C  
ANISOU 4653  CD1 LEU B 194    10586  24536  11846  -4279  -2232   4688       C  
ATOM   4654  CD2 LEU B 194       1.150  -3.660  29.208  1.00118.12           C  
ANISOU 4654  CD2 LEU B 194    10603  22483  11794  -4174  -1899   4039       C  
ATOM   4655  N   TRP B 195      -2.710  -5.810  30.012  1.00 99.68           N  
ANISOU 4655  N   TRP B 195     9548  18547   9780  -3202  -1526   3462       N  
ATOM   4656  CA  TRP B 195      -3.369  -6.702  29.045  1.00 95.64           C  
ANISOU 4656  CA  TRP B 195     9295  17441   9602  -2609  -1302   3500       C  
ATOM   4657  C   TRP B 195      -4.489  -5.966  28.321  1.00 94.98           C  
ANISOU 4657  C   TRP B 195     9658  16659   9770  -2708  -1182   2988       C  
ATOM   4658  O   TRP B 195      -4.643  -6.124  27.110  1.00 91.94           O  
ANISOU 4658  O   TRP B 195     9397  15880   9656  -2384  -1032   2968       O  
ATOM   4659  CB  TRP B 195      -3.935  -7.947  29.737  1.00 94.28           C  
ANISOU 4659  CB  TRP B 195     9222  17210   9388  -2269  -1249   3690       C  
ATOM   4660  CG  TRP B 195      -2.958  -9.068  29.918  1.00 98.60           C  
ANISOU 4660  CG  TRP B 195     9409  18214   9840  -1849  -1241   4293       C  
ATOM   4661  CD1 TRP B 195      -2.140  -9.274  30.988  1.00106.00           C  
ANISOU 4661  CD1 TRP B 195     9948  19889  10438  -1970  -1404   4660       C  
ATOM   4662  CD2 TRP B 195      -2.777 -10.196  29.053  1.00 97.94           C  
ANISOU 4662  CD2 TRP B 195     9360  17863   9988  -1207  -1037   4605       C  
ATOM   4663  NE1 TRP B 195      -1.430 -10.439  30.826  1.00107.84           N  
ANISOU 4663  NE1 TRP B 195     9938  20345  10692  -1409  -1304   5224       N  
ATOM   4664  CE2 TRP B 195      -1.795 -11.023  29.642  1.00106.31           C  
ANISOU 4664  CE2 TRP B 195    10027  19513  10853   -930  -1065   5187       C  
ATOM   4665  CE3 TRP B 195      -3.332 -10.579  27.823  1.00 95.87           C  
ANISOU 4665  CE3 TRP B 195     9429  16937  10059   -837   -827   4446       C  
ATOM   4666  CZ2 TRP B 195      -1.356 -12.210  29.041  1.00106.73           C  
ANISOU 4666  CZ2 TRP B 195    10042  19452  11057   -266   -857   5612       C  
ATOM   4667  CZ3 TRP B 195      -2.893 -11.751  27.226  1.00 98.51           C  
ANISOU 4667  CZ3 TRP B 195     9741  17166  10523   -227   -641   4825       C  
ATOM   4668  CH2 TRP B 195      -1.921 -12.555  27.835  1.00103.57           C  
ANISOU 4668  CH2 TRP B 195    10022  18342  10988     69   -640   5400       C  
ATOM   4669  N   VAL B 196      -5.236  -5.129  29.069  1.00 91.18           N  
ANISOU 4669  N   VAL B 196     9408  16063   9174  -3150  -1239   2586       N  
ATOM   4670  CA  VAL B 196      -6.327  -4.286  28.582  1.00 87.80           C  
ANISOU 4670  CA  VAL B 196     9386  15039   8936  -3281  -1124   2108       C  
ATOM   4671  C   VAL B 196      -5.781  -3.342  27.505  1.00 91.34           C  
ANISOU 4671  C   VAL B 196     9793  15370   9544  -3397  -1083   2033       C  
ATOM   4672  O   VAL B 196      -6.280  -3.368  26.386  1.00 87.42           O  
ANISOU 4672  O   VAL B 196     9483  14415   9319  -3105   -931   1943       O  
ATOM   4673  CB  VAL B 196      -7.011  -3.525  29.752  1.00 92.68           C  
ANISOU 4673  CB  VAL B 196    10211  15669   9333  -3739  -1185   1744       C  
ATOM   4674  CG1 VAL B 196      -8.030  -2.506  29.249  1.00 89.95           C  
ANISOU 4674  CG1 VAL B 196    10260  14742   9173  -3868  -1042   1283       C  
ATOM   4675  CG2 VAL B 196      -7.655  -4.494  30.741  1.00 92.57           C  
ANISOU 4675  CG2 VAL B 196    10250  15744   9178  -3584  -1196   1838       C  
ATOM   4676  N   VAL B 197      -4.714  -2.579  27.832  1.00 92.20           N  
ANISOU 4676  N   VAL B 197     9628  15934   9468  -3822  -1222   2106       N  
ATOM   4677  CA  VAL B 197      -4.041  -1.617  26.948  1.00 93.07           C  
ANISOU 4677  CA  VAL B 197     9649  16015   9698  -4023  -1196   2081       C  
ATOM   4678  C   VAL B 197      -3.513  -2.287  25.668  1.00 96.39           C  
ANISOU 4678  C   VAL B 197     9887  16401  10337  -3506  -1086   2421       C  
ATOM   4679  O   VAL B 197      -3.787  -1.782  24.581  1.00 93.30           O  
ANISOU 4679  O   VAL B 197     9665  15606  10179  -3401   -946   2286       O  
ATOM   4680  CB  VAL B 197      -2.964  -0.791  27.708  1.00101.82           C  
ANISOU 4680  CB  VAL B 197    10465  17695  10526  -4645  -1394   2121       C  
ATOM   4681  CG1 VAL B 197      -2.195   0.137  26.773  1.00103.13           C  
ANISOU 4681  CG1 VAL B 197    10505  17850  10830  -4866  -1359   2155       C  
ATOM   4682  CG2 VAL B 197      -3.598   0.014  28.836  1.00102.82           C  
ANISOU 4682  CG2 VAL B 197    10883  17742  10443  -5166  -1460   1686       C  
ATOM   4683  N   VAL B 198      -2.808  -3.438  25.801  1.00 95.84           N  
ANISOU 4683  N   VAL B 198     9496  16739  10181  -3149  -1126   2863       N  
ATOM   4684  CA  VAL B 198      -2.250  -4.220  24.685  1.00 95.84           C  
ANISOU 4684  CA  VAL B 198     9329  16741  10346  -2598   -997   3212       C  
ATOM   4685  C   VAL B 198      -3.339  -4.537  23.648  1.00 97.68           C  
ANISOU 4685  C   VAL B 198     9975  16277  10861  -2196   -797   2977       C  
ATOM   4686  O   VAL B 198      -3.174  -4.195  22.476  1.00 96.36           O  
ANISOU 4686  O   VAL B 198     9832  15917  10864  -2043   -682   2970       O  
ATOM   4687  CB  VAL B 198      -1.491  -5.492  25.175  1.00102.09           C  
ANISOU 4687  CB  VAL B 198     9782  18020  10987  -2229  -1034   3713       C  
ATOM   4688  CG1 VAL B 198      -1.123  -6.421  24.017  1.00101.22           C  
ANISOU 4688  CG1 VAL B 198     9620  17779  11061  -1572   -840   4016       C  
ATOM   4689  CG2 VAL B 198      -0.246  -5.115  25.973  1.00106.71           C  
ANISOU 4689  CG2 VAL B 198     9860  19406  11280  -2610  -1239   4013       C  
ATOM   4690  N   PHE B 199      -4.462  -5.131  24.088  1.00 93.73           N  
ANISOU 4690  N   PHE B 199     9785  15436  10393  -2065   -764   2783       N  
ATOM   4691  CA  PHE B 199      -5.565  -5.463  23.195  1.00 90.60           C  
ANISOU 4691  CA  PHE B 199     9759  14435  10230  -1743   -604   2552       C  
ATOM   4692  C   PHE B 199      -6.412  -4.270  22.799  1.00 93.76           C  
ANISOU 4692  C   PHE B 199    10434  14448  10744  -2017   -560   2137       C  
ATOM   4693  O   PHE B 199      -6.783  -4.174  21.631  1.00 91.28           O  
ANISOU 4693  O   PHE B 199    10271  13797  10614  -1779   -434   2044       O  
ATOM   4694  CB  PHE B 199      -6.419  -6.607  23.750  1.00 91.43           C  
ANISOU 4694  CB  PHE B 199    10062  14338  10338  -1506   -575   2544       C  
ATOM   4695  CG  PHE B 199      -5.705  -7.937  23.797  1.00 95.08           C  
ANISOU 4695  CG  PHE B 199    10346  15016  10765  -1078   -534   2972       C  
ATOM   4696  CD1 PHE B 199      -5.144  -8.488  22.649  1.00 98.62           C  
ANISOU 4696  CD1 PHE B 199    10747  15386  11337   -636   -397   3176       C  
ATOM   4697  CD2 PHE B 199      -5.625  -8.658  24.978  1.00 99.03           C  
ANISOU 4697  CD2 PHE B 199    10748  15778  11102  -1079   -605   3182       C  
ATOM   4698  CE1 PHE B 199      -4.488  -9.721  22.693  1.00101.78           C  
ANISOU 4698  CE1 PHE B 199    11019  15943  11710   -191   -315   3579       C  
ATOM   4699  CE2 PHE B 199      -4.987  -9.898  25.016  1.00104.09           C  
ANISOU 4699  CE2 PHE B 199    11246  16578  11724   -634   -530   3612       C  
ATOM   4700  CZ  PHE B 199      -4.405 -10.413  23.879  1.00102.61           C  
ANISOU 4700  CZ  PHE B 199    11027  16289  11672   -187   -378   3808       C  
ATOM   4701  N   GLN B 200      -6.695  -3.344  23.738  1.00 92.84           N  
ANISOU 4701  N   GLN B 200    10387  14385  10504  -2497   -648   1897       N  
ATOM   4702  CA  GLN B 200      -7.498  -2.155  23.433  1.00 92.38           C  
ANISOU 4702  CA  GLN B 200    10613  13935  10552  -2734   -569   1519       C  
ATOM   4703  C   GLN B 200      -6.783  -1.116  22.538  1.00100.06           C  
ANISOU 4703  C   GLN B 200    11495  14901  11620  -2882   -519   1543       C  
ATOM   4704  O   GLN B 200      -7.383  -0.100  22.177  1.00 99.30           O  
ANISOU 4704  O   GLN B 200    11641  14454  11635  -3036   -421   1275       O  
ATOM   4705  CB  GLN B 200      -8.167  -1.549  24.685  1.00 94.50           C  
ANISOU 4705  CB  GLN B 200    11065  14175  10665  -3137   -624   1222       C  
ATOM   4706  CG  GLN B 200      -9.683  -1.819  24.760  1.00112.07           C  
ANISOU 4706  CG  GLN B 200    13618  15979  12983  -2955   -520    969       C  
ATOM   4707  CD  GLN B 200     -10.093  -2.939  25.702  1.00130.09           C  
ANISOU 4707  CD  GLN B 200    15886  18401  15140  -2839   -581   1062       C  
ATOM   4708  OE1 GLN B 200     -10.514  -2.706  26.845  1.00123.99           O  
ANISOU 4708  OE1 GLN B 200    15198  17723  14189  -3099   -626    910       O  
ATOM   4709  NE2 GLN B 200     -10.062  -4.177  25.220  1.00120.79           N  
ANISOU 4709  NE2 GLN B 200    14642  17195  14058  -2435   -559   1301       N  
ATOM   4710  N   PHE B 201      -5.522  -1.403  22.147  1.00100.35           N  
ANISOU 4710  N   PHE B 201    11180  15325  11622  -2798   -563   1896       N  
ATOM   4711  CA  PHE B 201      -4.719  -0.600  21.220  1.00102.21           C  
ANISOU 4711  CA  PHE B 201    11266  15620  11949  -2889   -506   2010       C  
ATOM   4712  C   PHE B 201      -4.453  -1.388  19.935  1.00105.70           C  
ANISOU 4712  C   PHE B 201    11619  16017  12527  -2327   -384   2259       C  
ATOM   4713  O   PHE B 201      -4.334  -0.784  18.866  1.00105.21           O  
ANISOU 4713  O   PHE B 201    11582  15793  12600  -2258   -268   2263       O  
ATOM   4714  CB  PHE B 201      -3.427  -0.075  21.865  1.00108.50           C  
ANISOU 4714  CB  PHE B 201    11697  16965  12563  -3350   -657   2206       C  
ATOM   4715  CG  PHE B 201      -3.530   1.385  22.236  1.00112.09           C  
ANISOU 4715  CG  PHE B 201    12321  17265  13002  -3954   -670   1901       C  
ATOM   4716  CD1 PHE B 201      -4.230   1.784  23.371  1.00116.01           C  
ANISOU 4716  CD1 PHE B 201    13072  17639  13366  -4305   -732   1563       C  
ATOM   4717  CD2 PHE B 201      -2.956   2.364  21.436  1.00115.96           C  
ANISOU 4717  CD2 PHE B 201    12749  17697  13613  -4160   -592   1948       C  
ATOM   4718  CE1 PHE B 201      -4.351   3.138  23.698  1.00119.06           C  
ANISOU 4718  CE1 PHE B 201    13684  17814  13739  -4844   -705   1250       C  
ATOM   4719  CE2 PHE B 201      -3.070   3.717  21.768  1.00121.04           C  
ANISOU 4719  CE2 PHE B 201    13610  18119  14263  -4724   -570   1656       C  
ATOM   4720  CZ  PHE B 201      -3.772   4.095  22.893  1.00119.75           C  
ANISOU 4720  CZ  PHE B 201    13735  17799  13966  -5057   -621   1295       C  
ATOM   4721  N   GLN B 202      -4.416  -2.740  20.042  1.00102.08           N  
ANISOU 4721  N   GLN B 202    11093  15667  12026  -1915   -389   2454       N  
ATOM   4722  CA  GLN B 202      -4.289  -3.689  18.933  1.00101.19           C  
ANISOU 4722  CA  GLN B 202    10979  15456  12014  -1341   -253   2641       C  
ATOM   4723  C   GLN B 202      -5.557  -3.548  18.085  1.00103.91           C  
ANISOU 4723  C   GLN B 202    11714  15245  12522  -1169   -134   2313       C  
ATOM   4724  O   GLN B 202      -5.494  -3.582  16.857  1.00103.07           O  
ANISOU 4724  O   GLN B 202    11646  15007  12510   -869     -9   2355       O  
ATOM   4725  CB  GLN B 202      -4.179  -5.121  19.483  1.00102.87           C  
ANISOU 4725  CB  GLN B 202    11138  15804  12146  -1007   -270   2854       C  
ATOM   4726  CG  GLN B 202      -4.186  -6.224  18.436  1.00114.22           C  
ANISOU 4726  CG  GLN B 202    12676  17045  13676   -406   -104   2986       C  
ATOM   4727  CD  GLN B 202      -4.619  -7.537  19.032  1.00135.44           C  
ANISOU 4727  CD  GLN B 202    15508  19613  16341   -142    -91   3041       C  
ATOM   4728  OE1 GLN B 202      -5.783  -7.729  19.405  1.00130.04           O  
ANISOU 4728  OE1 GLN B 202    15124  18581  15705   -233   -112   2758       O  
ATOM   4729  NE2 GLN B 202      -3.694  -8.482  19.121  1.00130.67           N  
ANISOU 4729  NE2 GLN B 202    14689  19291  15668    209    -36   3436       N  
ATOM   4730  N   HIS B 203      -6.697  -3.339  18.774  1.00100.21           N  
ANISOU 4730  N   HIS B 203    11510  14504  12062  -1374   -176   2000       N  
ATOM   4731  CA  HIS B 203      -8.035  -3.116  18.239  1.00 97.92           C  
ANISOU 4731  CA  HIS B 203    11556  13753  11895  -1288    -92   1685       C  
ATOM   4732  C   HIS B 203      -8.077  -1.889  17.315  1.00101.86           C  
ANISOU 4732  C   HIS B 203    12108  14096  12499  -1379      3   1591       C  
ATOM   4733  O   HIS B 203      -8.766  -1.923  16.296  1.00 99.62           O  
ANISOU 4733  O   HIS B 203    11991  13546  12312  -1116    104   1489       O  
ATOM   4734  CB  HIS B 203      -9.030  -2.965  19.409  1.00 98.23           C  
ANISOU 4734  CB  HIS B 203    11780  13659  11885  -1559   -159   1430       C  
ATOM   4735  CG  HIS B 203     -10.430  -2.631  18.995  1.00 99.58           C  
ANISOU 4735  CG  HIS B 203    12246  13425  12165  -1503    -75   1132       C  
ATOM   4736  ND1 HIS B 203     -11.227  -3.549  18.334  1.00 99.77           N  
ANISOU 4736  ND1 HIS B 203    12414  13234  12261  -1166    -27   1081       N  
ATOM   4737  CD2 HIS B 203     -11.136  -1.492  19.187  1.00101.14           C  
ANISOU 4737  CD2 HIS B 203    12607  13424  12398  -1744    -25    890       C  
ATOM   4738  CE1 HIS B 203     -12.380  -2.935  18.131  1.00 97.86           C  
ANISOU 4738  CE1 HIS B 203    12366  12732  12086  -1217     30    836       C  
ATOM   4739  NE2 HIS B 203     -12.374  -1.698  18.627  1.00 98.93           N  
ANISOU 4739  NE2 HIS B 203    12525  12854  12208  -1527     49    726       N  
ATOM   4740  N   ILE B 204      -7.329  -0.823  17.671  1.00100.89           N  
ANISOU 4740  N   ILE B 204    11842  14149  12344  -1766    -29   1637       N  
ATOM   4741  CA  ILE B 204      -7.236   0.436  16.922  1.00101.23           C  
ANISOU 4741  CA  ILE B 204    11933  14038  12492  -1914     78   1589       C  
ATOM   4742  C   ILE B 204      -6.314   0.267  15.703  1.00105.91           C  
ANISOU 4742  C   ILE B 204    12307  14806  13127  -1629    158   1886       C  
ATOM   4743  O   ILE B 204      -6.447   1.003  14.730  1.00105.22           O  
ANISOU 4743  O   ILE B 204    12293  14540  13145  -1565    285   1877       O  
ATOM   4744  CB  ILE B 204      -6.798   1.620  17.855  1.00106.89           C  
ANISOU 4744  CB  ILE B 204    12624  14836  13154  -2501     21   1499       C  
ATOM   4745  CG1 ILE B 204      -7.478   1.577  19.260  1.00107.35           C  
ANISOU 4745  CG1 ILE B 204    12845  14850  13093  -2772    -77   1245       C  
ATOM   4746  CG2 ILE B 204      -6.943   3.006  17.192  1.00108.06           C  
ANISOU 4746  CG2 ILE B 204    12927  14687  13442  -2682    170   1399       C  
ATOM   4747  CD1 ILE B 204      -9.085   1.568  19.332  1.00112.04           C  
ANISOU 4747  CD1 ILE B 204    13801  15010  13760  -2608     13    935       C  
ATOM   4748  N   MET B 205      -5.400  -0.707  15.739  1.00103.91           N  
ANISOU 4748  N   MET B 205    11788  14907  12784  -1422    107   2170       N  
ATOM   4749  CA  MET B 205      -4.490  -0.899  14.613  1.00105.26           C  
ANISOU 4749  CA  MET B 205    11743  15280  12973  -1116    209   2468       C  
ATOM   4750  C   MET B 205      -5.082  -1.760  13.505  1.00105.14           C  
ANISOU 4750  C   MET B 205    11913  15039  12997   -569    328   2427       C  
ATOM   4751  O   MET B 205      -5.371  -1.235  12.429  1.00103.79           O  
ANISOU 4751  O   MET B 205    11842  14696  12896   -434    446   2381       O  
ATOM   4752  CB  MET B 205      -3.089  -1.361  15.060  1.00111.24           C  
ANISOU 4752  CB  MET B 205    12083  16576  13607  -1139    135   2845       C  
ATOM   4753  CG  MET B 205      -2.417  -0.424  16.066  1.00118.47           C  
ANISOU 4753  CG  MET B 205    12782  17783  14448  -1751     -3   2885       C  
ATOM   4754  SD  MET B 205      -2.361   1.345  15.636  1.00124.70           S  
ANISOU 4754  SD  MET B 205    13644  18377  15358  -2240     68   2759       S  
ATOM   4755  CE  MET B 205      -1.590   2.017  17.123  1.00125.34           C  
ANISOU 4755  CE  MET B 205    13502  18841  15279  -2977   -141   2760       C  
ATOM   4756  N   VAL B 206      -5.313  -3.045  13.758  1.00 99.73           N  
ANISOU 4756  N   VAL B 206    11300  14336  12259   -274    304   2429       N  
ATOM   4757  CA  VAL B 206      -5.885  -3.934  12.738  1.00 97.60           C  
ANISOU 4757  CA  VAL B 206    11248  13831  12004    199    413   2347       C  
ATOM   4758  C   VAL B 206      -7.345  -3.613  12.381  1.00 97.33           C  
ANISOU 4758  C   VAL B 206    11546  13396  12040    164    422   1989       C  
ATOM   4759  O   VAL B 206      -7.869  -4.089  11.373  1.00 96.72           O  
ANISOU 4759  O   VAL B 206    11643  13149  11958    483    501   1891       O  
ATOM   4760  CB  VAL B 206      -5.789  -5.412  13.164  1.00102.10           C  
ANISOU 4760  CB  VAL B 206    11860  14420  12514    491    405   2431       C  
ATOM   4761  CG1 VAL B 206      -4.546  -6.056  12.568  1.00104.59           C  
ANISOU 4761  CG1 VAL B 206    11950  15028  12764    883    522   2789       C  
ATOM   4762  CG2 VAL B 206      -5.782  -5.527  14.681  1.00102.34           C  
ANISOU 4762  CG2 VAL B 206    11807  14575  12503    175    257   2449       C  
ATOM   4763  N   GLY B 207      -7.986  -2.807  13.219  1.00 90.87           N  
ANISOU 4763  N   GLY B 207    10805  12458  11265   -222    344   1801       N  
ATOM   4764  CA  GLY B 207      -9.382  -2.411  13.075  1.00 87.40           C  
ANISOU 4764  CA  GLY B 207    10632  11691  10886   -276    356   1500       C  
ATOM   4765  C   GLY B 207      -9.636  -1.023  12.522  1.00 88.62           C  
ANISOU 4765  C   GLY B 207    10826  11728  11117   -415    441   1445       C  
ATOM   4766  O   GLY B 207     -10.601  -0.834  11.777  1.00 87.04           O  
ANISOU 4766  O   GLY B 207    10793  11328  10949   -256    503   1302       O  
ATOM   4767  N   LEU B 208      -8.779  -0.042  12.865  1.00 85.05           N  
ANISOU 4767  N   LEU B 208    10219  11406  10689   -718    452   1571       N  
ATOM   4768  CA  LEU B 208      -8.910   1.337  12.380  1.00 84.64           C  
ANISOU 4768  CA  LEU B 208    10228  11199  10732   -874    566   1552       C  
ATOM   4769  C   LEU B 208      -7.769   2.003  11.582  1.00 88.59           C  
ANISOU 4769  C   LEU B 208    10521  11874  11264   -892    661   1829       C  
ATOM   4770  O   LEU B 208      -8.043   2.596  10.539  1.00 88.24           O  
ANISOU 4770  O   LEU B 208    10546  11700  11281   -726    797   1869       O  
ATOM   4771  CB  LEU B 208      -9.156   2.263  13.603  1.00 85.31           C  
ANISOU 4771  CB  LEU B 208    10416  11154  10844  -1347    531   1378       C  
ATOM   4772  CG  LEU B 208      -9.820   3.632  13.371  1.00 90.31           C  
ANISOU 4772  CG  LEU B 208    11263  11458  11594  -1490    680   1247       C  
ATOM   4773  CD1 LEU B 208     -10.409   4.154  14.650  1.00 90.68           C  
ANISOU 4773  CD1 LEU B 208    11499  11327  11629  -1838    654    992       C  
ATOM   4774  CD2 LEU B 208      -8.823   4.680  12.859  1.00 95.48           C  
ANISOU 4774  CD2 LEU B 208    11806  12148  12323  -1687    784   1447       C  
ATOM   4775  N   ILE B 209      -6.506   1.908  12.076  1.00 85.42           N  
ANISOU 4775  N   ILE B 209     9844  11803  10810  -1094    592   2046       N  
ATOM   4776  CA  ILE B 209      -5.309   2.528  11.483  1.00 86.92           C  
ANISOU 4776  CA  ILE B 209     9774  12230  11022  -1186    668   2347       C  
ATOM   4777  C   ILE B 209      -4.921   1.777  10.206  1.00 87.79           C  
ANISOU 4777  C   ILE B 209     9764  12508  11086   -663    767   2568       C  
ATOM   4778  O   ILE B 209      -4.907   2.394   9.146  1.00 87.56           O  
ANISOU 4778  O   ILE B 209     9748  12411  11108   -530    911   2667       O  
ATOM   4779  CB  ILE B 209      -4.120   2.775  12.475  1.00 92.98           C  
ANISOU 4779  CB  ILE B 209    10248  13352  11728  -1638    548   2513       C  
ATOM   4780  CG1 ILE B 209      -4.543   3.580  13.746  1.00 93.98           C  
ANISOU 4780  CG1 ILE B 209    10549  13296  11862  -2188    457   2238       C  
ATOM   4781  CG2 ILE B 209      -2.889   3.398  11.783  1.00 96.66           C  
ANISOU 4781  CG2 ILE B 209    10405  14099  12221  -1745    632   2858       C  
ATOM   4782  CD1 ILE B 209      -5.115   5.048  13.567  1.00102.79           C  
ANISOU 4782  CD1 ILE B 209    11947  13983  13124  -2480    599   2052       C  
ATOM   4783  N   LEU B 210      -4.650   0.459  10.298  1.00 81.86           N  
ANISOU 4783  N   LEU B 210     8926  11949  10229   -349    711   2642       N  
ATOM   4784  CA  LEU B 210      -4.291  -0.365   9.141  1.00 80.96           C  
ANISOU 4784  CA  LEU B 210     8751  11968  10041    176    826   2813       C  
ATOM   4785  C   LEU B 210      -5.355  -0.399   8.023  1.00 81.48           C  
ANISOU 4785  C   LEU B 210     9102  11746  10110    496    924   2618       C  
ATOM   4786  O   LEU B 210      -4.989  -0.052   6.896  1.00 81.77           O  
ANISOU 4786  O   LEU B 210     9065  11878  10125    709   1063   2786       O  
ATOM   4787  CB  LEU B 210      -3.819  -1.776   9.535  1.00 81.37           C  
ANISOU 4787  CB  LEU B 210     8710  12218   9988    458    780   2921       C  
ATOM   4788  CG  LEU B 210      -2.311  -1.999   9.634  1.00 88.90           C  
ANISOU 4788  CG  LEU B 210     9252  13654  10872    513    806   3335       C  
ATOM   4789  CD1 LEU B 210      -2.009  -3.366  10.225  1.00 89.35           C  
ANISOU 4789  CD1 LEU B 210     9262  13848  10838    790    769   3434       C  
ATOM   4790  CD2 LEU B 210      -1.639  -1.856   8.267  1.00 93.24           C  
ANISOU 4790  CD2 LEU B 210     9659  14379  11388    854    996   3585       C  
ATOM   4791  N   PRO B 211      -6.659  -0.722   8.276  1.00 74.93           N  
ANISOU 4791  N   PRO B 211     8567  10609   9292    514    857   2291       N  
ATOM   4792  CA  PRO B 211      -7.639  -0.697   7.170  1.00 73.06           C  
ANISOU 4792  CA  PRO B 211     8546  10187   9026    788    933   2135       C  
ATOM   4793  C   PRO B 211      -7.918   0.704   6.619  1.00 74.96           C  
ANISOU 4793  C   PRO B 211     8802  10328   9352    659   1033   2178       C  
ATOM   4794  O   PRO B 211      -8.093   0.856   5.413  1.00 74.68           O  
ANISOU 4794  O   PRO B 211     8797  10321   9257    945   1143   2240       O  
ATOM   4795  CB  PRO B 211      -8.887  -1.337   7.779  1.00 72.80           C  
ANISOU 4795  CB  PRO B 211     8759   9911   8992    752    818   1815       C  
ATOM   4796  CG  PRO B 211      -8.753  -1.126   9.227  1.00 77.07           C  
ANISOU 4796  CG  PRO B 211     9246  10435   9601    368    710   1781       C  
ATOM   4797  CD  PRO B 211      -7.296  -1.153   9.539  1.00 74.80           C  
ANISOU 4797  CD  PRO B 211     8674  10454   9293    293    712   2075       C  
ATOM   4798  N   GLY B 212      -7.916   1.703   7.501  1.00 70.53           N  
ANISOU 4798  N   GLY B 212     8232   9651   8914    240   1011   2154       N  
ATOM   4799  CA  GLY B 212      -8.122   3.103   7.145  1.00 70.93           C  
ANISOU 4799  CA  GLY B 212     8334   9537   9077     77   1137   2208       C  
ATOM   4800  C   GLY B 212      -7.013   3.645   6.270  1.00 77.01           C  
ANISOU 4800  C   GLY B 212     8888  10515   9857    131   1272   2545       C  
ATOM   4801  O   GLY B 212      -7.286   4.348   5.294  1.00 76.84           O  
ANISOU 4801  O   GLY B 212     8918  10416   9863    285   1420   2645       O  
ATOM   4802  N   ILE B 213      -5.754   3.278   6.594  1.00 75.59           N  
ANISOU 4802  N   ILE B 213     8437  10642   9640     31   1230   2756       N  
ATOM   4803  CA  ILE B 213      -4.563   3.670   5.838  1.00 78.26           C  
ANISOU 4803  CA  ILE B 213     8501  11261   9973     72   1354   3122       C  
ATOM   4804  C   ILE B 213      -4.608   3.101   4.412  1.00 80.99           C  
ANISOU 4804  C   ILE B 213     8843  11741  10188    630   1479   3238       C  
ATOM   4805  O   ILE B 213      -4.238   3.803   3.471  1.00 82.88           O  
ANISOU 4805  O   ILE B 213     8990  12060  10440    718   1639   3476       O  
ATOM   4806  CB  ILE B 213      -3.250   3.397   6.643  1.00 83.88           C  
ANISOU 4806  CB  ILE B 213     8879  12332  10658   -188   1262   3336       C  
ATOM   4807  CG1 ILE B 213      -2.821   4.632   7.494  1.00 86.64           C  
ANISOU 4807  CG1 ILE B 213     9160  12621  11136   -831   1231   3365       C  
ATOM   4808  CG2 ILE B 213      -2.096   2.815   5.816  1.00 86.93           C  
ANISOU 4808  CG2 ILE B 213     8946  13150  10935    154   1357   3702       C  
ATOM   4809  CD1 ILE B 213      -2.585   6.040   6.727  1.00 96.20           C  
ANISOU 4809  CD1 ILE B 213    10374  13693  12486  -1024   1424   3551       C  
ATOM   4810  N   VAL B 214      -5.134   1.871   4.253  1.00 74.26           N  
ANISOU 4810  N   VAL B 214     8126  10887   9204    984   1414   3051       N  
ATOM   4811  CA  VAL B 214      -5.317   1.223   2.952  1.00 73.78           C  
ANISOU 4811  CA  VAL B 214     8133  10925   8975   1497   1516   3069       C  
ATOM   4812  C   VAL B 214      -6.423   1.978   2.169  1.00 77.42           C  
ANISOU 4812  C   VAL B 214     8796  11181   9441   1574   1580   2955       C  
ATOM   4813  O   VAL B 214      -6.159   2.450   1.062  1.00 78.48           O  
ANISOU 4813  O   VAL B 214     8857  11451   9512   1787   1734   3167       O  
ATOM   4814  CB  VAL B 214      -5.599  -0.302   3.109  1.00 76.09           C  
ANISOU 4814  CB  VAL B 214     8567  11210   9133   1782   1430   2861       C  
ATOM   4815  CG1 VAL B 214      -6.067  -0.937   1.803  1.00 76.00           C  
ANISOU 4815  CG1 VAL B 214     8727  11224   8925   2247   1517   2763       C  
ATOM   4816  CG2 VAL B 214      -4.379  -1.035   3.651  1.00 77.50           C  
ANISOU 4816  CG2 VAL B 214     8512  11651   9285   1831   1427   3077       C  
ATOM   4817  N   ILE B 215      -7.635   2.113   2.769  1.00 72.49           N  
ANISOU 4817  N   ILE B 215     8395  10264   8884   1410   1474   2658       N  
ATOM   4818  CA  ILE B 215      -8.821   2.790   2.212  1.00 71.95           C  
ANISOU 4818  CA  ILE B 215     8500  10016   8821   1484   1520   2553       C  
ATOM   4819  C   ILE B 215      -8.501   4.213   1.713  1.00 78.50           C  
ANISOU 4819  C   ILE B 215     9251  10810   9766   1391   1701   2831       C  
ATOM   4820  O   ILE B 215      -8.804   4.539   0.560  1.00 79.01           O  
ANISOU 4820  O   ILE B 215     9328  10956   9736   1680   1820   2956       O  
ATOM   4821  CB  ILE B 215     -10.021   2.738   3.218  1.00 72.89           C  
ANISOU 4821  CB  ILE B 215     8816   9860   9021   1270   1386   2233       C  
ATOM   4822  CG1 ILE B 215     -10.604   1.303   3.304  1.00 72.02           C  
ANISOU 4822  CG1 ILE B 215     8821   9778   8765   1445   1239   1970       C  
ATOM   4823  CG2 ILE B 215     -11.125   3.764   2.878  1.00 73.08           C  
ANISOU 4823  CG2 ILE B 215     8966   9698   9102   1286   1469   2204       C  
ATOM   4824  CD1 ILE B 215     -11.403   0.943   4.603  1.00 76.53           C  
ANISOU 4824  CD1 ILE B 215     9520  10142   9418   1182   1087   1699       C  
ATOM   4825  N   LEU B 216      -7.871   5.039   2.573  1.00 76.27           N  
ANISOU 4825  N   LEU B 216     8894  10412   9674    975   1725   2932       N  
ATOM   4826  CA  LEU B 216      -7.512   6.416   2.243  1.00 78.47           C  
ANISOU 4826  CA  LEU B 216     9134  10581  10099    802   1911   3189       C  
ATOM   4827  C   LEU B 216      -6.491   6.517   1.121  1.00 85.64           C  
ANISOU 4827  C   LEU B 216     9813  11798  10930   1018   2058   3558       C  
ATOM   4828  O   LEU B 216      -6.639   7.385   0.264  1.00 86.69           O  
ANISOU 4828  O   LEU B 216     9967  11878  11094   1135   2239   3768       O  
ATOM   4829  CB  LEU B 216      -7.041   7.180   3.485  1.00 79.41           C  
ANISOU 4829  CB  LEU B 216     9255  10503  10413    243   1885   3160       C  
ATOM   4830  CG  LEU B 216      -8.066   8.129   4.104  1.00 83.66           C  
ANISOU 4830  CG  LEU B 216    10079  10602  11106     22   1939   2962       C  
ATOM   4831  CD1 LEU B 216      -7.838   8.274   5.593  1.00 83.75           C  
ANISOU 4831  CD1 LEU B 216    10145  10470  11206   -482   1819   2757       C  
ATOM   4832  CD2 LEU B 216      -8.042   9.500   3.426  1.00 89.04           C  
ANISOU 4832  CD2 LEU B 216    10834  11065  11932    -12   2193   3209       C  
ATOM   4833  N   SER B 217      -5.468   5.630   1.115  1.00 83.66           N  
ANISOU 4833  N   SER B 217     9337  11880  10568   1104   2004   3667       N  
ATOM   4834  CA  SER B 217      -4.434   5.615   0.074  1.00 86.58           C  
ANISOU 4834  CA  SER B 217     9458  12601  10838   1347   2157   4034       C  
ATOM   4835  C   SER B 217      -5.027   5.174  -1.268  1.00 91.81           C  
ANISOU 4835  C   SER B 217    10219  13388  11277   1892   2242   4027       C  
ATOM   4836  O   SER B 217      -4.755   5.814  -2.282  1.00 93.21           O  
ANISOU 4836  O   SER B 217    10309  13692  11415   2060   2427   4318       O  
ATOM   4837  CB  SER B 217      -3.252   4.738   0.473  1.00 90.55           C  
ANISOU 4837  CB  SER B 217     9692  13443  11269   1348   2093   4158       C  
ATOM   4838  OG  SER B 217      -3.600   3.365   0.453  1.00 96.81           O  
ANISOU 4838  OG  SER B 217    10592  14306  11885   1700   1991   3928       O  
ATOM   4839  N   CYS B 218      -5.876   4.119  -1.261  1.00 87.58           N  
ANISOU 4839  N   CYS B 218     9875  12814  10586   2134   2107   3693       N  
ATOM   4840  CA  CYS B 218      -6.577   3.627  -2.451  1.00 88.00           C  
ANISOU 4840  CA  CYS B 218    10058  12989  10389   2589   2144   3605       C  
ATOM   4841  C   CYS B 218      -7.379   4.765  -3.084  1.00 92.89           C  
ANISOU 4841  C   CYS B 218    10755  13492  11046   2619   2250   3709       C  
ATOM   4842  O   CYS B 218      -7.207   5.040  -4.271  1.00 94.53           O  
ANISOU 4842  O   CYS B 218    10893  13925  11099   2920   2402   3944       O  
ATOM   4843  CB  CYS B 218      -7.471   2.439  -2.107  1.00 86.29           C  
ANISOU 4843  CB  CYS B 218    10062  12674  10051   2690   1957   3190       C  
ATOM   4844  SG  CYS B 218      -6.631   0.841  -2.167  1.00 91.00           S  
ANISOU 4844  SG  CYS B 218    10636  13480  10459   2972   1933   3120       S  
ATOM   4845  N   TYR B 219      -8.200   5.464  -2.266  1.00 88.17           N  
ANISOU 4845  N   TYR B 219    10294  12553  10651   2320   2194   3568       N  
ATOM   4846  CA  TYR B 219      -9.011   6.607  -2.675  1.00 88.88           C  
ANISOU 4846  CA  TYR B 219    10478  12474  10820   2346   2318   3682       C  
ATOM   4847  C   TYR B 219      -8.136   7.739  -3.233  1.00 95.42           C  
ANISOU 4847  C   TYR B 219    11163  13330  11764   2296   2559   4120       C  
ATOM   4848  O   TYR B 219      -8.498   8.319  -4.252  1.00 96.50           O  
ANISOU 4848  O   TYR B 219    11304  13546  11817   2567   2712   4339       O  
ATOM   4849  CB  TYR B 219      -9.893   7.091  -1.504  1.00 88.91           C  
ANISOU 4849  CB  TYR B 219    10661  12083  11037   2025   2242   3448       C  
ATOM   4850  CG  TYR B 219     -10.446   8.492  -1.669  1.00 93.22           C  
ANISOU 4850  CG  TYR B 219    11305  12364  11749   1985   2435   3632       C  
ATOM   4851  CD1 TYR B 219     -11.546   8.738  -2.486  1.00 95.73           C  
ANISOU 4851  CD1 TYR B 219    11693  12740  11942   2329   2492   3674       C  
ATOM   4852  CD2 TYR B 219      -9.870   9.572  -1.004  1.00 95.96           C  
ANISOU 4852  CD2 TYR B 219    11684  12406  12371   1600   2570   3773       C  
ATOM   4853  CE1 TYR B 219     -12.050  10.026  -2.651  1.00 98.91           C  
ANISOU 4853  CE1 TYR B 219    12189  12889  12501   2353   2705   3891       C  
ATOM   4854  CE2 TYR B 219     -10.364  10.866  -1.165  1.00 99.19           C  
ANISOU 4854  CE2 TYR B 219    12236  12504  12948   1585   2791   3950       C  
ATOM   4855  CZ  TYR B 219     -11.455  11.088  -1.988  1.00108.44           C  
ANISOU 4855  CZ  TYR B 219    13473  13724  14006   1992   2871   4026       C  
ATOM   4856  OH  TYR B 219     -11.949  12.361  -2.150  1.00114.10           O  
ANISOU 4856  OH  TYR B 219    14335  14125  14893   2034   3121   4243       O  
ATOM   4857  N   CYS B 220      -6.987   8.030  -2.581  1.00 93.46           N  
ANISOU 4857  N   CYS B 220    10769  13050  11692   1941   2590   4265       N  
ATOM   4858  CA  CYS B 220      -6.031   9.069  -2.994  1.00 96.79           C  
ANISOU 4858  CA  CYS B 220    11030  13499  12247   1794   2809   4688       C  
ATOM   4859  C   CYS B 220      -5.387   8.794  -4.362  1.00101.10           C  
ANISOU 4859  C   CYS B 220    11373  14477  12564   2213   2951   5012       C  
ATOM   4860  O   CYS B 220      -5.097   9.740  -5.096  1.00103.39           O  
ANISOU 4860  O   CYS B 220    11592  14782  12910   2254   3173   5380       O  
ATOM   4861  CB  CYS B 220      -4.974   9.310  -1.919  1.00 98.47           C  
ANISOU 4861  CB  CYS B 220    11105  13650  12661   1267   2763   4732       C  
ATOM   4862  SG  CYS B 220      -5.261  10.787  -0.910  1.00103.84           S  
ANISOU 4862  SG  CYS B 220    12001  13764  13688    681   2846   4687       S  
ATOM   4863  N   ILE B 221      -5.160   7.506  -4.691  1.00 95.55           N  
ANISOU 4863  N   ILE B 221    10597  14105  11601   2529   2845   4879       N  
ATOM   4864  CA  ILE B 221      -4.575   7.082  -5.969  1.00 97.00           C  
ANISOU 4864  CA  ILE B 221    10622  14720  11512   2976   2982   5128       C  
ATOM   4865  C   ILE B 221      -5.661   7.008  -7.067  1.00 99.77           C  
ANISOU 4865  C   ILE B 221    11139  15161  11607   3407   3012   5054       C  
ATOM   4866  O   ILE B 221      -5.393   7.414  -8.203  1.00102.28           O  
ANISOU 4866  O   ILE B 221    11353  15735  11774   3692   3204   5381       O  
ATOM   4867  CB  ILE B 221      -3.684   5.807  -5.838  1.00100.00           C  
ANISOU 4867  CB  ILE B 221    10858  15405  11731   3133   2911   5063       C  
ATOM   4868  CG1 ILE B 221      -2.552   6.022  -4.795  1.00101.37           C  
ANISOU 4868  CG1 ILE B 221    10790  15584  12141   2694   2886   5225       C  
ATOM   4869  CG2 ILE B 221      -3.070   5.418  -7.189  1.00103.16           C  
ANISOU 4869  CG2 ILE B 221    11118  16248  11830   3628   3095   5321       C  
ATOM   4870  CD1 ILE B 221      -2.070   4.743  -4.035  1.00105.61           C  
ANISOU 4870  CD1 ILE B 221    11266  16253  12609   2726   2729   5033       C  
ATOM   4871  N   ILE B 222      -6.891   6.534  -6.719  1.00 92.23           N  
ANISOU 4871  N   ILE B 222    10418  14031  10594   3434   2824   4652       N  
ATOM   4872  CA  ILE B 222      -8.036   6.478  -7.646  1.00 91.29           C  
ANISOU 4872  CA  ILE B 222    10430  14032  10222   3778   2810   4562       C  
ATOM   4873  C   ILE B 222      -8.358   7.909  -8.082  1.00 97.55           C  
ANISOU 4873  C   ILE B 222    11202  14712  11152   3775   3008   4919       C  
ATOM   4874  O   ILE B 222      -8.380   8.181  -9.283  1.00 99.60           O  
ANISOU 4874  O   ILE B 222    11391  15264  11189   4121   3152   5185       O  
ATOM   4875  CB  ILE B 222      -9.278   5.735  -7.057  1.00 90.72           C  
ANISOU 4875  CB  ILE B 222    10572  13803  10095   3726   2561   4084       C  
ATOM   4876  CG1 ILE B 222      -9.030   4.214  -6.958  1.00 89.63           C  
ANISOU 4876  CG1 ILE B 222    10498  13806   9752   3836   2406   3757       C  
ATOM   4877  CG2 ILE B 222     -10.546   6.019  -7.884  1.00 91.46           C  
ANISOU 4877  CG2 ILE B 222    10748  14021   9983   3984   2548   4063       C  
ATOM   4878  CD1 ILE B 222      -9.824   3.494  -5.861  1.00 89.36           C  
ANISOU 4878  CD1 ILE B 222    10636  13507   9809   3599   2170   3328       C  
ATOM   4879  N   ILE B 223      -8.510   8.831  -7.102  1.00 93.75           N  
ANISOU 4879  N   ILE B 223    10789  13801  11030   3388   3040   4945       N  
ATOM   4880  CA  ILE B 223      -8.783  10.253  -7.345  1.00 95.72           C  
ANISOU 4880  CA  ILE B 223    11074  13820  11474   3347   3267   5282       C  
ATOM   4881  C   ILE B 223      -7.687  10.935  -8.183  1.00101.96           C  
ANISOU 4881  C   ILE B 223    11673  14786  12280   3414   3527   5786       C  
ATOM   4882  O   ILE B 223      -7.957  11.950  -8.821  1.00103.51           O  
ANISOU 4882  O   ILE B 223    11889  14911  12529   3548   3746   6130       O  
ATOM   4883  CB  ILE B 223      -9.175  11.027  -6.045  1.00 97.94           C  
ANISOU 4883  CB  ILE B 223    11534  13554  12126   2908   3263   5141       C  
ATOM   4884  CG1 ILE B 223     -10.167  12.171  -6.328  1.00100.38           C  
ANISOU 4884  CG1 ILE B 223    11994  13603  12544   3043   3450   5328       C  
ATOM   4885  CG2 ILE B 223      -7.969  11.501  -5.230  1.00 99.57           C  
ANISOU 4885  CG2 ILE B 223    11669  13548  12616   2418   3326   5250       C  
ATOM   4886  CD1 ILE B 223     -11.669  11.747  -6.303  1.00108.70           C  
ANISOU 4886  CD1 ILE B 223    13164  14699  13436   3293   3296   5047       C  
ATOM   4887  N   SER B 224      -6.467  10.358  -8.190  1.00 99.13           N  
ANISOU 4887  N   SER B 224    11117  14676  11870   3345   3515   5857       N  
ATOM   4888  CA  SER B 224      -5.342  10.865  -8.968  1.00102.81           C  
ANISOU 4888  CA  SER B 224    11351  15386  12327   3404   3754   6343       C  
ATOM   4889  C   SER B 224      -5.372  10.302 -10.389  1.00108.67           C  
ANISOU 4889  C   SER B 224    12001  16641  12649   3978   3825   6485       C  
ATOM   4890  O   SER B 224      -5.147  11.061 -11.334  1.00111.48           O  
ANISOU 4890  O   SER B 224    12257  17148  12950   4169   4064   6921       O  
ATOM   4891  CB  SER B 224      -4.017  10.543  -8.288  1.00106.92           C  
ANISOU 4891  CB  SER B 224    11658  15991  12977   3069   3719   6393       C  
ATOM   4892  OG  SER B 224      -2.944  11.150  -8.990  1.00120.83           O  
ANISOU 4892  OG  SER B 224    13165  17985  14761   3074   3963   6903       O  
ATOM   4893  N   LYS B 225      -5.659   8.983 -10.545  1.00103.39           N  
ANISOU 4893  N   LYS B 225    11387  16226  11669   4243   3631   6115       N  
ATOM   4894  CA  LYS B 225      -5.736   8.328 -11.857  1.00104.75           C  
ANISOU 4894  CA  LYS B 225    11528  16883  11388   4771   3679   6154       C  
ATOM   4895  C   LYS B 225      -6.899   8.847 -12.697  1.00110.16           C  
ANISOU 4895  C   LYS B 225    12319  17650  11887   5050   3714   6228       C  
ATOM   4896  O   LYS B 225      -6.674   9.188 -13.855  1.00113.30           O  
ANISOU 4896  O   LYS B 225    12604  18394  12051   5382   3905   6583       O  
ATOM   4897  CB  LYS B 225      -5.741   6.787 -11.756  1.00104.96           C  
ANISOU 4897  CB  LYS B 225    11647  17087  11147   4942   3481   5707       C  
ATOM   4898  CG  LYS B 225      -5.860   6.027 -13.103  1.00115.39           C  
ANISOU 4898  CG  LYS B 225    13002  18888  11953   5471   3527   5662       C  
ATOM   4899  CD  LYS B 225      -4.725   6.302 -14.119  1.00127.78           C  
ANISOU 4899  CD  LYS B 225    14334  20865  13351   5760   3811   6140       C  
ATOM   4900  CE  LYS B 225      -3.514   5.406 -13.941  1.00139.91           C  
ANISOU 4900  CE  LYS B 225    15750  22575  14834   5843   3866   6130       C  
ATOM   4901  NZ  LYS B 225      -2.388   5.797 -14.838  1.00153.10           N  
ANISOU 4901  NZ  LYS B 225    17142  24649  16379   6091   4164   6652       N  
ATOM   4902  N   LEU B 226      -8.127   8.920 -12.136  1.00104.21           N  
ANISOU 4902  N   LEU B 226    11752  16624  11219   4936   3543   5931       N  
ATOM   4903  CA  LEU B 226      -9.256   9.450 -12.909  1.00105.32           C  
ANISOU 4903  CA  LEU B 226    11946  16894  11178   5216   3579   6051       C  
ATOM   4904  C   LEU B 226      -9.128  10.941 -13.236  1.00112.54           C  
ANISOU 4904  C   LEU B 226    12788  17651  12318   5220   3873   6602       C  
ATOM   4905  O   LEU B 226      -9.635  11.382 -14.267  1.00114.67           O  
ANISOU 4905  O   LEU B 226    13014  18202  12353   5580   3991   6887       O  
ATOM   4906  CB  LEU B 226     -10.649   9.056 -12.379  1.00102.65           C  
ANISOU 4906  CB  LEU B 226    11779  16421  10804   5162   3327   5628       C  
ATOM   4907  CG  LEU B 226     -10.979   9.245 -10.899  1.00104.17           C  
ANISOU 4907  CG  LEU B 226    12099  16077  11404   4728   3216   5372       C  
ATOM   4908  CD1 LEU B 226     -11.370  10.683 -10.589  1.00105.54           C  
ANISOU 4908  CD1 LEU B 226    12314  15877  11908   4617   3416   5687       C  
ATOM   4909  CD2 LEU B 226     -12.123   8.345 -10.504  1.00104.05           C  
ANISOU 4909  CD2 LEU B 226    12210  16085  11237   4716   2931   4890       C  
ATOM   4910  N   SER B 227      -8.400  11.696 -12.388  1.00109.79           N  
ANISOU 4910  N   SER B 227    12431  16875  12409   4813   4000   6766       N  
ATOM   4911  CA  SER B 227      -8.118  13.111 -12.619  1.00113.42           C  
ANISOU 4911  CA  SER B 227    12862  17097  13134   4741   4311   7286       C  
ATOM   4912  C   SER B 227      -6.933  13.254 -13.579  1.00122.53           C  
ANISOU 4912  C   SER B 227    13780  18621  14155   4899   4531   7738       C  
ATOM   4913  O   SER B 227      -6.701  14.354 -14.090  1.00125.63           O  
ANISOU 4913  O   SER B 227    14125  18929  14682   4936   4817   8242       O  
ATOM   4914  CB  SER B 227      -7.829  13.832 -11.306  1.00115.93           C  
ANISOU 4914  CB  SER B 227    13299  16797  13951   4182   4349   7227       C  
ATOM   4915  OG  SER B 227      -7.791  15.237 -11.493  1.00128.33           O  
ANISOU 4915  OG  SER B 227    14930  18037  15794   4107   4660   7680       O  
ATOM   4916  N   HIS B 228      -6.177  12.141 -13.824  1.00119.51           N  
ANISOU 4916  N   HIS B 228    13257  18640  13510   5010   4422   7579       N  
ATOM   4917  CA  HIS B 228      -5.062  12.106 -14.775  1.00123.17           C  
ANISOU 4917  CA  HIS B 228    13475  19542  13782   5228   4629   7984       C  
ATOM   4918  C   HIS B 228      -5.500  12.090 -16.246  1.00131.63           C  
ANISOU 4918  C   HIS B 228    14503  21113  14398   5799   4746   8223       C  
ATOM   4919  O   HIS B 228      -5.716  13.103 -16.830  1.00135.01           O  
ANISOU 4919  O   HIS B 228    14902  21523  14873   5920   4966   8661       O  
ATOM   4920  CB  HIS B 228      -4.118  10.907 -14.559  1.00122.76           C  
ANISOU 4920  CB  HIS B 228    13297  19764  13583   5226   4513   7753       C  
ATOM   4921  CG  HIS B 228      -3.122  10.715 -15.667  1.00129.72           C  
ANISOU 4921  CG  HIS B 228    13934  21182  14171   5574   4730   8136       C  
ATOM   4922  ND1 HIS B 228      -3.411   9.935 -16.775  1.00132.50           N  
ANISOU 4922  ND1 HIS B 228    14316  22025  14003   6111   4726   8041       N  
ATOM   4923  CD2 HIS B 228      -1.871  11.217 -15.802  1.00134.43           C  
ANISOU 4923  CD2 HIS B 228    14254  21905  14916   5438   4960   8605       C  
ATOM   4924  CE1 HIS B 228      -2.331   9.987 -17.537  1.00135.34           C  
ANISOU 4924  CE1 HIS B 228    14430  22784  14210   6322   4968   8455       C  
ATOM   4925  NE2 HIS B 228      -1.380  10.743 -16.992  1.00136.98           N  
ANISOU 4925  NE2 HIS B 228    14426  22803  14815   5932   5115   8821       N  
ATOM   4926  N   ASN B1002      -6.482  10.908 -16.452  1.00 88.77           N  
ANISOU 4926  N   ASN B1002    10930  12187  10612   1115    597   1648       N  
ATOM   4927  CA  ASN B1002      -7.390  10.247 -17.393  1.00 88.15           C  
ANISOU 4927  CA  ASN B1002    10935  11964  10593    914    789   1708       C  
ATOM   4928  C   ASN B1002      -8.112  11.293 -18.247  1.00 91.48           C  
ANISOU 4928  C   ASN B1002    11313  12427  11017    724    789   1582       C  
ATOM   4929  O   ASN B1002      -8.260  11.096 -19.455  1.00 90.63           O  
ANISOU 4929  O   ASN B1002    11229  12193  11014    545    879   1533       O  
ATOM   4930  CB  ASN B1002      -8.386   9.330 -16.673  1.00 89.41           C  
ANISOU 4930  CB  ASN B1002    11211  12125  10635    937    901   1918       C  
ATOM   4931  CG  ASN B1002      -8.275   7.859 -17.022  1.00111.76           C  
ANISOU 4931  CG  ASN B1002    14150  14729  13586    899   1061   2046       C  
ATOM   4932  OD1 ASN B1002      -8.639   6.992 -16.222  1.00107.08           O  
ANISOU 4932  OD1 ASN B1002    13648  14109  12929    989   1144   2243       O  
ATOM   4933  ND2 ASN B1002      -7.809   7.529 -18.228  1.00103.48           N  
ANISOU 4933  ND2 ASN B1002    13117  13492  12709    767   1133   1942       N  
ATOM   4934  N   ILE B1003      -8.540  12.411 -17.609  1.00 87.91           N  
ANISOU 4934  N   ILE B1003    10817  12150  10435    783    689   1532       N  
ATOM   4935  CA  ILE B1003      -9.173  13.577 -18.239  1.00 86.47           C  
ANISOU 4935  CA  ILE B1003    10585  12021  10250    663    677   1429       C  
ATOM   4936  C   ILE B1003      -8.122  14.362 -19.067  1.00 88.32           C  
ANISOU 4936  C   ILE B1003    10736  12183  10638    614    615   1254       C  
ATOM   4937  O   ILE B1003      -8.468  14.930 -20.102  1.00 86.93           O  
ANISOU 4937  O   ILE B1003    10544  11967  10517    471    662   1197       O  
ATOM   4938  CB  ILE B1003      -9.936  14.441 -17.187  1.00 90.40           C  
ANISOU 4938  CB  ILE B1003    11088  12697  10564    780    627   1442       C  
ATOM   4939  CG1 ILE B1003     -10.819  15.530 -17.835  1.00 89.85           C  
ANISOU 4939  CG1 ILE B1003    10970  12669  10499    675    654   1388       C  
ATOM   4940  CG2 ILE B1003      -9.010  15.009 -16.106  1.00 92.71           C  
ANISOU 4940  CG2 ILE B1003    11380  13076  10770    976    463   1340       C  
ATOM   4941  CD1 ILE B1003     -11.811  16.196 -16.875  1.00 98.85           C  
ANISOU 4941  CD1 ILE B1003    12130  13963  11467    797    676   1439       C  
ATOM   4942  N   PHE B1004      -6.843  14.348 -18.615  1.00 84.95           N  
ANISOU 4942  N   PHE B1004    10247  11744  10286    737    514   1191       N  
ATOM   4943  CA  PHE B1004      -5.665  14.930 -19.265  1.00 84.51           C  
ANISOU 4943  CA  PHE B1004    10075  11612  10424    705    472   1054       C  
ATOM   4944  C   PHE B1004      -5.495  14.230 -20.603  1.00 87.85           C  
ANISOU 4944  C   PHE B1004    10531  11867  10981    575    645   1076       C  
ATOM   4945  O   PHE B1004      -5.533  14.897 -21.634  1.00 86.66           O  
ANISOU 4945  O   PHE B1004    10367  11661  10899    448    707   1001       O  
ATOM   4946  CB  PHE B1004      -4.423  14.740 -18.370  1.00 87.99           C  
ANISOU 4946  CB  PHE B1004    10415  12094  10923    873    320   1032       C  
ATOM   4947  CG  PHE B1004      -3.088  15.172 -18.920  1.00 90.31           C  
ANISOU 4947  CG  PHE B1004    10535  12313  11466    851    280    921       C  
ATOM   4948  CD1 PHE B1004      -2.615  16.460 -18.707  1.00 93.87           C  
ANISOU 4948  CD1 PHE B1004    10869  12812  11986    824    132    764       C  
ATOM   4949  CD2 PHE B1004      -2.264  14.267 -19.581  1.00 93.31           C  
ANISOU 4949  CD2 PHE B1004    10861  12564  12027    866    401    980       C  
ATOM   4950  CE1 PHE B1004      -1.357  16.847 -19.179  1.00 95.78           C  
ANISOU 4950  CE1 PHE B1004    10913  12981  12498    788    104    680       C  
ATOM   4951  CE2 PHE B1004      -1.010  14.658 -20.062  1.00 97.03           C  
ANISOU 4951  CE2 PHE B1004    11137  12974  12755    858    393    902       C  
ATOM   4952  CZ  PHE B1004      -0.568  15.947 -19.860  1.00 95.45           C  
ANISOU 4952  CZ  PHE B1004    10792  12832  12643    809    241    759       C  
ATOM   4953  N   GLU B1005      -5.405  12.882 -20.583  1.00 84.86           N  
ANISOU 4953  N   GLU B1005    10230  11399  10613    611    738   1187       N  
ATOM   4954  CA  GLU B1005      -5.282  12.034 -21.768  1.00 84.52           C  
ANISOU 4954  CA  GLU B1005    10276  11171  10665    501    918   1197       C  
ATOM   4955  C   GLU B1005      -6.423  12.277 -22.774  1.00 85.05           C  
ANISOU 4955  C   GLU B1005    10446  11221  10647    291    990   1174       C  
ATOM   4956  O   GLU B1005      -6.167  12.305 -23.981  1.00 84.30           O  
ANISOU 4956  O   GLU B1005    10402  11017  10613    183   1094   1105       O  
ATOM   4957  CB  GLU B1005      -5.208  10.552 -21.360  1.00 87.52           C  
ANISOU 4957  CB  GLU B1005    10758  11445  11052    585   1003   1328       C  
ATOM   4958  CG  GLU B1005      -4.597   9.636 -22.412  1.00101.86           C  
ANISOU 4958  CG  GLU B1005    12662  13033  13007    545   1190   1311       C  
ATOM   4959  CD  GLU B1005      -3.144   9.887 -22.775  1.00129.80           C  
ANISOU 4959  CD  GLU B1005    16062  16516  16742    654   1223   1245       C  
ATOM   4960  OE1 GLU B1005      -2.351  10.251 -21.876  1.00126.98           O  
ANISOU 4960  OE1 GLU B1005    15525  16270  16451    819   1079   1263       O  
ATOM   4961  OE2 GLU B1005      -2.795   9.692 -23.961  1.00127.32           O  
ANISOU 4961  OE2 GLU B1005    15816  16047  16513    575   1396   1179       O  
ATOM   4962  N   MET B1006      -7.663  12.485 -22.270  1.00 79.42           N  
ANISOU 4962  N   MET B1006     9755  10631   9788    247    935   1240       N  
ATOM   4963  CA  MET B1006      -8.849  12.765 -23.084  1.00 77.69           C  
ANISOU 4963  CA  MET B1006     9586  10442   9491     62    960   1246       C  
ATOM   4964  C   MET B1006      -8.642  14.061 -23.869  1.00 80.94           C  
ANISOU 4964  C   MET B1006     9939  10887   9929     17    932   1141       C  
ATOM   4965  O   MET B1006      -8.672  14.038 -25.102  1.00 80.67           O  
ANISOU 4965  O   MET B1006     9977  10773   9902   -113   1002   1098       O  
ATOM   4966  CB  MET B1006     -10.112  12.869 -22.207  1.00 79.50           C  
ANISOU 4966  CB  MET B1006     9788  10822   9597     70    913   1359       C  
ATOM   4967  CG  MET B1006     -11.397  12.909 -23.014  1.00 82.23           C  
ANISOU 4967  CG  MET B1006    10147  11205   9890   -126    929   1402       C  
ATOM   4968  SD  MET B1006     -12.815  13.554 -22.099  1.00 85.61           S  
ANISOU 4968  SD  MET B1006    10465  11847  10214    -81    889   1530       S  
ATOM   4969  CE  MET B1006     -14.110  12.607 -22.842  1.00 83.10           C  
ANISOU 4969  CE  MET B1006    10160  11508   9906   -337    925   1636       C  
ATOM   4970  N   LEU B1007      -8.388  15.173 -23.147  1.00 76.78           N  
ANISOU 4970  N   LEU B1007     9303  10461   9407    131    837   1097       N  
ATOM   4971  CA  LEU B1007      -8.156  16.503 -23.711  1.00 75.67           C  
ANISOU 4971  CA  LEU B1007     9104  10328   9317    106    818   1008       C  
ATOM   4972  C   LEU B1007      -6.863  16.574 -24.514  1.00 79.44           C  
ANISOU 4972  C   LEU B1007     9555  10670   9957     89    893    926       C  
ATOM   4973  O   LEU B1007      -6.779  17.384 -25.432  1.00 79.33           O  
ANISOU 4973  O   LEU B1007     9543  10616   9983     18    946    888       O  
ATOM   4974  CB  LEU B1007      -8.187  17.586 -22.612  1.00 75.67           C  
ANISOU 4974  CB  LEU B1007     9023  10434   9292    230    701    962       C  
ATOM   4975  CG  LEU B1007      -9.532  18.282 -22.282  1.00 79.78           C  
ANISOU 4975  CG  LEU B1007     9553  11079   9680    242    679   1020       C  
ATOM   4976  CD1 LEU B1007     -10.022  19.165 -23.421  1.00 79.45           C  
ANISOU 4976  CD1 LEU B1007     9512  11016   9660    144    725   1022       C  
ATOM   4977  CD2 LEU B1007     -10.600  17.302 -21.810  1.00 82.36           C  
ANISOU 4977  CD2 LEU B1007     9919  11490   9883    236    707   1161       C  
ATOM   4978  N   ARG B1008      -5.868  15.718 -24.185  1.00 75.90           N  
ANISOU 4978  N   ARG B1008     9079  10149   9609    169    916    922       N  
ATOM   4979  CA  ARG B1008      -4.586  15.608 -24.894  1.00 76.02           C  
ANISOU 4979  CA  ARG B1008     9042  10033   9809    178   1024    869       C  
ATOM   4980  C   ARG B1008      -4.865  15.101 -26.314  1.00 79.41           C  
ANISOU 4980  C   ARG B1008     9635  10348  10190     50   1200    877       C  
ATOM   4981  O   ARG B1008      -4.245  15.580 -27.264  1.00 79.26           O  
ANISOU 4981  O   ARG B1008     9609  10249  10258     12   1319    833       O  
ATOM   4982  CB  ARG B1008      -3.644  14.637 -24.153  1.00 76.41           C  
ANISOU 4982  CB  ARG B1008     9024  10045   9963    321   1010    901       C  
ATOM   4983  CG  ARG B1008      -2.204  14.657 -24.632  1.00 85.13           C  
ANISOU 4983  CG  ARG B1008     9995  11045  11307    372   1104    861       C  
ATOM   4984  CD  ARG B1008      -1.562  13.290 -24.517  1.00 96.99           C  
ANISOU 4984  CD  ARG B1008    11518  12447  12886    489   1200    933       C  
ATOM   4985  NE  ARG B1008      -0.422  13.156 -25.427  1.00108.81           N  
ANISOU 4985  NE  ARG B1008    12941  13806  14597    514   1393    912       N  
ATOM   4986  CZ  ARG B1008       0.851  13.160 -25.043  1.00125.24           C  
ANISOU 4986  CZ  ARG B1008    14785  15884  16916    648   1373    926       C  
ATOM   4987  NH1 ARG B1008       1.166  13.273 -23.758  1.00112.93           N  
ANISOU 4987  NH1 ARG B1008    13061  14461  15387    764   1132    948       N  
ATOM   4988  NH2 ARG B1008       1.819  13.034 -25.941  1.00112.81           N  
ANISOU 4988  NH2 ARG B1008    13137  14181  15546    674   1593    925       N  
ATOM   4989  N   ILE B1009      -5.806  14.137 -26.447  1.00 75.47           N  
ANISOU 4989  N   ILE B1009     9290   9838   9546    -24   1219    930       N  
ATOM   4990  CA  ILE B1009      -6.224  13.567 -27.730  1.00 75.42           C  
ANISOU 4990  CA  ILE B1009     9478   9732   9446   -168   1342    913       C  
ATOM   4991  C   ILE B1009      -7.094  14.584 -28.482  1.00 79.09           C  
ANISOU 4991  C   ILE B1009     9971  10294   9786   -285   1293    910       C  
ATOM   4992  O   ILE B1009      -6.999  14.679 -29.708  1.00 79.31           O  
ANISOU 4992  O   ILE B1009    10123  10255   9754   -368   1395    874       O  
ATOM   4993  CB  ILE B1009      -6.864  12.150 -27.555  1.00 78.84           C  
ANISOU 4993  CB  ILE B1009    10057  10093   9804   -229   1361    958       C  
ATOM   4994  CG1 ILE B1009      -5.783  11.115 -27.149  1.00 79.93           C  
ANISOU 4994  CG1 ILE B1009    10205  10079  10086    -89   1471    969       C  
ATOM   4995  CG2 ILE B1009      -7.604  11.677 -28.820  1.00 80.34           C  
ANISOU 4995  CG2 ILE B1009    10462  10212   9853   -426   1418    914       C  
ATOM   4996  CD1 ILE B1009      -6.300   9.874 -26.434  1.00 86.98           C  
ANISOU 4996  CD1 ILE B1009    11186  10908  10953    -84   1469   1054       C  
ATOM   4997  N   ASP B1010      -7.890  15.379 -27.746  1.00 75.20           N  
ANISOU 4997  N   ASP B1010     9370   9956   9246   -266   1150    957       N  
ATOM   4998  CA  ASP B1010      -8.759  16.395 -28.336  1.00 74.78           C  
ANISOU 4998  CA  ASP B1010     9317  10002   9093   -337   1099    985       C  
ATOM   4999  C   ASP B1010      -8.311  17.852 -28.547  1.00 79.87           C  
ANISOU 4999  C   ASP B1010     9877  10655   9816   -280   1111    962       C  
ATOM   5000  O   ASP B1010      -8.486  18.382 -29.644  1.00 80.45           O  
ANISOU 5000  O   ASP B1010    10026  10715   9827   -345   1167    979       O  
ATOM   5001  CB  ASP B1010     -10.080  16.524 -27.551  1.00 75.80           C  
ANISOU 5001  CB  ASP B1010     9379  10290   9129   -343    970   1073       C  
ATOM   5002  CG  ASP B1010     -10.989  15.308 -27.620  1.00 84.85           C  
ANISOU 5002  CG  ASP B1010    10604  11450  10187   -468    949   1130       C  
ATOM   5003  OD1 ASP B1010     -10.915  14.561 -28.623  1.00 86.13           O  
ANISOU 5003  OD1 ASP B1010    10914  11510  10300   -596   1003   1088       O  
ATOM   5004  OD2 ASP B1010     -11.807  15.125 -26.692  1.00 89.49           O  
ANISOU 5004  OD2 ASP B1010    11112  12140  10752   -445    887   1215       O  
ATOM   5005  N   GLU B1011      -7.717  18.485 -27.524  1.00 76.56           N  
ANISOU 5005  N   GLU B1011     9317  10246   9526   -165   1058    922       N  
ATOM   5006  CA  GLU B1011      -7.268  19.875 -27.579  1.00 76.88           C  
ANISOU 5006  CA  GLU B1011     9274  10259   9678   -127   1065    883       C  
ATOM   5007  C   GLU B1011      -5.735  19.929 -27.772  1.00 82.56           C  
ANISOU 5007  C   GLU B1011     9915  10843  10611   -105   1160    810       C  
ATOM   5008  O   GLU B1011      -5.192  21.020 -27.970  1.00 82.56           O  
ANISOU 5008  O   GLU B1011     9840  10778  10750   -106   1197    776       O  
ATOM   5009  CB  GLU B1011      -7.762  20.774 -26.437  1.00 78.01           C  
ANISOU 5009  CB  GLU B1011     9333  10491   9818    -38    937    868       C  
ATOM   5010  CG  GLU B1011      -9.034  21.519 -26.806  1.00 89.04           C  
ANISOU 5010  CG  GLU B1011    10770  11971  11093    -52    923    955       C  
ATOM   5011  CD  GLU B1011      -9.835  22.170 -25.692  1.00114.99           C  
ANISOU 5011  CD  GLU B1011    14007  15358  14328     55    833    965       C  
ATOM   5012  OE1 GLU B1011      -9.304  22.328 -24.569  1.00114.83           O  
ANISOU 5012  OE1 GLU B1011    13940  15333  14358    144    767    871       O  
ATOM   5013  OE2 GLU B1011     -10.998  22.550 -25.959  1.00110.13           O  
ANISOU 5013  OE2 GLU B1011    13401  14831  13614     61    831   1069       O  
ATOM   5014  N   GLY B1012      -5.065  18.770 -27.731  1.00 80.21           N  
ANISOU 5014  N   GLY B1012     9625  10493  10360    -84   1213    798       N  
ATOM   5015  CA  GLY B1012      -3.625  18.644 -27.952  1.00 81.42           C  
ANISOU 5015  CA  GLY B1012     9673  10528  10734    -47   1325    755       C  
ATOM   5016  C   GLY B1012      -2.710  19.226 -26.890  1.00 87.10           C  
ANISOU 5016  C   GLY B1012    10170  11261  11662     31   1201    689       C  
ATOM   5017  O   GLY B1012      -2.998  20.287 -26.331  1.00 87.04           O  
ANISOU 5017  O   GLY B1012    10106  11302  11664     27   1078    644       O  
ATOM   5018  N   LEU B1013      -1.576  18.546 -26.632  1.00 85.07           N  
ANISOU 5018  N   LEU B1013     9787  10957  11580    103   1231    679       N  
ATOM   5019  CA  LEU B1013      -0.574  18.977 -25.653  1.00 86.36           C  
ANISOU 5019  CA  LEU B1013     9709  11148  11957    169   1078    615       C  
ATOM   5020  C   LEU B1013       0.720  19.438 -26.330  1.00 93.43           C  
ANISOU 5020  C   LEU B1013    10413  11923  13161    135   1224    599       C  
ATOM   5021  O   LEU B1013       1.241  18.747 -27.208  1.00 94.08           O  
ANISOU 5021  O   LEU B1013    10518  11912  13317    153   1450    658       O  
ATOM   5022  CB  LEU B1013      -0.306  17.857 -24.619  1.00 86.84           C  
ANISOU 5022  CB  LEU B1013     9724  11284  11986    306    951    647       C  
ATOM   5023  CG  LEU B1013       0.977  17.919 -23.767  1.00 93.10           C  
ANISOU 5023  CG  LEU B1013    10247  12113  13014    399    799    608       C  
ATOM   5024  CD1 LEU B1013       0.894  18.996 -22.697  1.00 93.67           C  
ANISOU 5024  CD1 LEU B1013    10233  12290  13066    387    528    494       C  
ATOM   5025  CD2 LEU B1013       1.251  16.591 -23.114  1.00 95.69           C  
ANISOU 5025  CD2 LEU B1013    10570  12484  13302    557    753    696       C  
ATOM   5026  N   ARG B1014       1.238  20.607 -25.897  1.00 91.50           N  
ANISOU 5026  N   ARG B1014     9985  11672  13109     85   1106    516       N  
ATOM   5027  CA  ARG B1014       2.481  21.225 -26.377  1.00 93.58           C  
ANISOU 5027  CA  ARG B1014    10010  11822  13724     26   1220    501       C  
ATOM   5028  C   ARG B1014       3.083  22.159 -25.316  1.00 99.76           C  
ANISOU 5028  C   ARG B1014    10558  12638  14709    -14    954    375       C  
ATOM   5029  O   ARG B1014       2.364  22.603 -24.421  1.00 98.04           O  
ANISOU 5029  O   ARG B1014    10434  12504  14314     -8    729    288       O  
ATOM   5030  CB  ARG B1014       2.269  21.963 -27.716  1.00 93.60           C  
ANISOU 5030  CB  ARG B1014    10127  11691  13745    -81   1490    553       C  
ATOM   5031  CG  ARG B1014       1.258  23.099 -27.664  1.00103.40           C  
ANISOU 5031  CG  ARG B1014    11513  12931  14844   -156   1410    516       C  
ATOM   5032  CD  ARG B1014       0.927  23.626 -29.046  1.00112.50           C  
ANISOU 5032  CD  ARG B1014    12822  13973  15948   -224   1679    611       C  
ATOM   5033  NE  ARG B1014      -0.438  24.151 -29.093  1.00113.64           N  
ANISOU 5033  NE  ARG B1014    13184  14172  15824   -234   1608    631       N  
ATOM   5034  CZ  ARG B1014      -0.771  25.409 -28.840  1.00120.68           C  
ANISOU 5034  CZ  ARG B1014    14071  15008  16771   -275   1543    595       C  
ATOM   5035  NH1 ARG B1014      -2.036  25.788 -28.903  1.00106.70           N  
ANISOU 5035  NH1 ARG B1014    12483  13297  14760   -251   1496    638       N  
ATOM   5036  NH2 ARG B1014       0.163  26.303 -28.530  1.00102.57           N  
ANISOU 5036  NH2 ARG B1014    11584  12591  14796   -343   1530    519       N  
ATOM   5037  N   LEU B1015       4.397  22.452 -25.416  1.00 99.99           N  
ANISOU 5037  N   LEU B1015    10281  12598  15112    -59    983    360       N  
ATOM   5038  CA  LEU B1015       5.114  23.327 -24.473  1.00102.19           C  
ANISOU 5038  CA  LEU B1015    10303  12894  15629   -133    709    221       C  
ATOM   5039  C   LEU B1015       5.602  24.639 -25.119  1.00108.86           C  
ANISOU 5039  C   LEU B1015    11020  13556  16785   -319    842    182       C  
ATOM   5040  O   LEU B1015       6.341  25.404 -24.491  1.00110.65           O  
ANISOU 5040  O   LEU B1015    11005  13756  17283   -424    641     58       O  
ATOM   5041  CB  LEU B1015       6.263  22.590 -23.748  1.00104.41           C  
ANISOU 5041  CB  LEU B1015    10272  13281  16119    -40    532    227       C  
ATOM   5042  CG  LEU B1015       6.397  21.075 -23.942  1.00108.49           C  
ANISOU 5042  CG  LEU B1015    10820  13859  16544    146    660    377       C  
ATOM   5043  CD1 LEU B1015       7.846  20.647 -23.828  1.00111.93           C  
ANISOU 5043  CD1 LEU B1015    10858  14312  17357    211    645    436       C  
ATOM   5044  CD2 LEU B1015       5.532  20.300 -22.952  1.00108.79           C  
ANISOU 5044  CD2 LEU B1015    11073  14052  16209    287    443    375       C  
ATOM   5045  N   LYS B1016       5.188  24.881 -26.358  1.00105.56           N  
ANISOU 5045  N   LYS B1016    10774  13012  16323   -361   1172    290       N  
ATOM   5046  CA  LYS B1016       5.584  26.086 -27.077  1.00107.58           C  
ANISOU 5046  CA  LYS B1016    10948  13073  16857   -521   1356    298       C  
ATOM   5047  C   LYS B1016       4.262  26.821 -27.271  1.00110.79           C  
ANISOU 5047  C   LYS B1016    11685  13438  16972   -540   1371    287       C  
ATOM   5048  O   LYS B1016       3.235  26.426 -26.721  1.00108.53           O  
ANISOU 5048  O   LYS B1016    11610  13286  16341   -446   1211    255       O  
ATOM   5049  CB  LYS B1016       5.951  25.751 -28.524  1.00110.72           C  
ANISOU 5049  CB  LYS B1016    11368  13363  17337   -510   1780    480       C  
ATOM   5050  CG  LYS B1016       7.374  26.122 -28.906  1.00127.89           C  
ANISOU 5050  CG  LYS B1016    13176  15411  20005   -604   1953    526       C  
ATOM   5051  CD  LYS B1016       7.420  27.453 -29.639  1.00137.38           C  
ANISOU 5051  CD  LYS B1016    14398  16400  21401   -765   2166    567       C  
ATOM   5052  CE  LYS B1016       8.836  28.003 -29.697  1.00149.93           C  
ANISOU 5052  CE  LYS B1016    15558  17859  23549   -906   2257    580       C  
ATOM   5053  NZ  LYS B1016       8.884  29.451 -29.355  1.00159.29           N  
ANISOU 5053  NZ  LYS B1016    16671  18872  24979  -1113   2144    471       N  
ATOM   5054  N   ILE B1017       4.297  27.892 -28.058  1.00109.39           N  
ANISOU 5054  N   ILE B1017    11539  13072  16953   -653   1579    335       N  
ATOM   5055  CA  ILE B1017       3.102  28.683 -28.326  1.00108.49           C  
ANISOU 5055  CA  ILE B1017    11715  12901  16604   -653   1617    356       C  
ATOM   5056  C   ILE B1017       2.441  28.649 -29.700  1.00112.76           C  
ANISOU 5056  C   ILE B1017    12501  13399  16944   -614   1928    550       C  
ATOM   5057  O   ILE B1017       2.948  28.020 -30.628  1.00112.92           O  
ANISOU 5057  O   ILE B1017    12504  13406  16994   -595   2176    673       O  
ATOM   5058  CB  ILE B1017       3.661  30.095 -28.071  1.00114.28           C  
ANISOU 5058  CB  ILE B1017    12306  13421  17694   -814   1589    257       C  
ATOM   5059  CG1 ILE B1017       3.915  30.306 -26.577  1.00115.61           C  
ANISOU 5059  CG1 ILE B1017    12340  13651  17933   -848   1201     18       C  
ATOM   5060  CG2 ILE B1017       2.706  31.151 -28.608  1.00114.77           C  
ANISOU 5060  CG2 ILE B1017    12628  13341  17640   -822   1727    323       C  
ATOM   5061  CD1 ILE B1017       5.154  31.121 -26.277  1.00126.73           C  
ANISOU 5061  CD1 ILE B1017    13437  14891  19822  -1042   1131   -101       C  
ATOM   5062  N   TYR B1018       1.306  29.330 -29.821  1.00109.22           N  
ANISOU 5062  N   TYR B1018    12287  12932  16278   -589   1914    580       N  
ATOM   5063  CA  TYR B1018       0.558  29.381 -31.106  1.00108.79           C  
ANISOU 5063  CA  TYR B1018    12480  12864  15991   -543   2158    774       C  
ATOM   5064  C   TYR B1018      -0.166  30.714 -31.318  1.00114.67           C  
ANISOU 5064  C   TYR B1018    13368  13475  16726   -553   2204    829       C  
ATOM   5065  O   TYR B1018       0.026  31.620 -30.506  1.00115.51           O  
ANISOU 5065  O   TYR B1018    13383  13459  17045   -611   2080    699       O  
ATOM   5066  CB  TYR B1018      -0.396  28.188 -31.187  1.00107.38           C  
ANISOU 5066  CB  TYR B1018    12483  12906  15412   -437   2074    811       C  
ATOM   5067  CG  TYR B1018      -1.788  28.548 -31.658  1.00107.64           C  
ANISOU 5067  CG  TYR B1018    12766  12999  15132   -379   2071    919       C  
ATOM   5068  CD1 TYR B1018      -2.053  28.760 -33.004  1.00110.20           C  
ANISOU 5068  CD1 TYR B1018    13263  13280  15328   -372   2302   1095       C  
ATOM   5069  CD2 TYR B1018      -2.836  28.674 -30.756  1.00106.83           C  
ANISOU 5069  CD2 TYR B1018    12719  13011  14859   -317   1840    858       C  
ATOM   5070  CE1 TYR B1018      -3.323  29.089 -33.439  1.00110.15           C  
ANISOU 5070  CE1 TYR B1018    13457  13355  15042   -309   2267   1211       C  
ATOM   5071  CE2 TYR B1018      -4.109  29.002 -31.182  1.00106.88           C  
ANISOU 5071  CE2 TYR B1018    12906  13088  14614   -252   1835    977       C  
ATOM   5072  CZ  TYR B1018      -4.347  29.208 -32.524  1.00114.70           C  
ANISOU 5072  CZ  TYR B1018    14043  14046  15492   -251   2031   1155       C  
ATOM   5073  OH  TYR B1018      -5.613  29.535 -32.952  1.00115.61           O  
ANISOU 5073  OH  TYR B1018    14311  14254  15360   -177   1995   1291       O  
ATOM   5074  N   LYS B1019      -0.991  30.889 -32.364  1.00112.04           N  
ANISOU 5074  N   LYS B1019    13264  13153  16151   -491   2367   1013       N  
ATOM   5075  CA  LYS B1019      -1.594  32.203 -32.396  1.00113.40           C  
ANISOU 5075  CA  LYS B1019    13540  13182  16366   -477   2395   1067       C  
ATOM   5076  C   LYS B1019      -2.872  32.026 -33.230  1.00117.81           C  
ANISOU 5076  C   LYS B1019    14349  13882  16532   -357   2434   1254       C  
ATOM   5077  O   LYS B1019      -3.035  30.981 -33.877  1.00117.22           O  
ANISOU 5077  O   LYS B1019    14357  13967  16214   -332   2470   1321       O  
ATOM   5078  CB  LYS B1019      -0.609  33.423 -32.347  1.00118.47           C  
ANISOU 5078  CB  LYS B1019    14043  13520  17450   -604   2532   1033       C  
ATOM   5079  CG  LYS B1019       0.428  33.497 -33.472  1.00132.79           C  
ANISOU 5079  CG  LYS B1019    15787  15188  19480   -684   2867   1186       C  
ATOM   5080  CD  LYS B1019       0.100  34.582 -34.504  1.00143.88           C  
ANISOU 5080  CD  LYS B1019    17375  16398  20895   -661   3142   1412       C  
ATOM   5081  CE  LYS B1019       0.942  35.832 -34.365  1.00157.04           C  
ANISOU 5081  CE  LYS B1019    18901  17730  23037   -808   3284   1393       C  
ATOM   5082  NZ  LYS B1019       0.563  36.645 -33.177  1.00166.16           N  
ANISOU 5082  NZ  LYS B1019    20038  18776  24319   -839   3033   1190       N  
ATOM   5083  N   ASP B1020      -3.746  33.021 -33.112  1.00114.60           N  
ANISOU 5083  N   ASP B1020    14048  13412  16081   -286   2404   1316       N  
ATOM   5084  CA  ASP B1020      -4.932  33.202 -33.923  1.00114.18           C  
ANISOU 5084  CA  ASP B1020    14197  13460  15726   -166   2442   1526       C  
ATOM   5085  C   ASP B1020      -4.796  34.623 -34.447  1.00121.66           C  
ANISOU 5085  C   ASP B1020    15214  14140  16872   -151   2653   1668       C  
ATOM   5086  O   ASP B1020      -4.445  35.538 -33.703  1.00122.95           O  
ANISOU 5086  O   ASP B1020    15300  14086  17328   -193   2646   1552       O  
ATOM   5087  CB  ASP B1020      -6.196  33.061 -33.078  1.00113.91           C  
ANISOU 5087  CB  ASP B1020    14188  13609  15485    -58   2196   1479       C  
ATOM   5088  CG  ASP B1020      -7.091  31.933 -33.553  1.00118.18           C  
ANISOU 5088  CG  ASP B1020    14809  14435  15658    -13   2090   1569       C  
ATOM   5089  OD1 ASP B1020      -8.297  31.953 -33.229  1.00116.57           O  
ANISOU 5089  OD1 ASP B1020    14634  14384  15273     87   1945   1623       O  
ATOM   5090  OD2 ASP B1020      -6.588  31.027 -34.251  1.00123.59           O  
ANISOU 5090  OD2 ASP B1020    15526  15183  16249    -81   2161   1584       O  
ATOM   5091  N   TYR B1024      -3.932  35.104 -30.086  1.00104.76           N  
ANISOU 5091  N   TYR B1024    12679  11856  15270   -290   2031    855       N  
ATOM   5092  CA  TYR B1024      -4.324  34.045 -29.150  1.00102.26           C  
ANISOU 5092  CA  TYR B1024    12321  11806  14726   -233   1784    725       C  
ATOM   5093  C   TYR B1024      -3.086  33.185 -28.880  1.00104.36           C  
ANISOU 5093  C   TYR B1024    12391  12118  15143   -358   1716    598       C  
ATOM   5094  O   TYR B1024      -2.802  32.250 -29.633  1.00102.71           O  
ANISOU 5094  O   TYR B1024    12153  12019  14852   -374   1807    705       O  
ATOM   5095  CB  TYR B1024      -5.535  33.264 -29.695  1.00101.88           C  
ANISOU 5095  CB  TYR B1024    12389  12014  14305   -105   1775    909       C  
ATOM   5096  CG  TYR B1024      -6.864  33.984 -29.600  1.00104.44           C  
ANISOU 5096  CG  TYR B1024    12848  12358  14477     51   1768   1012       C  
ATOM   5097  CD1 TYR B1024      -7.070  35.199 -30.248  1.00108.31           C  
ANISOU 5097  CD1 TYR B1024    13436  12635  15081     97   1944   1151       C  
ATOM   5098  CD2 TYR B1024      -7.951  33.397 -28.962  1.00104.06           C  
ANISOU 5098  CD2 TYR B1024    12820  12547  14172    168   1613   1011       C  
ATOM   5099  CE1 TYR B1024      -8.299  35.852 -30.188  1.00109.64           C  
ANISOU 5099  CE1 TYR B1024    13712  12824  15123    273   1950   1273       C  
ATOM   5100  CE2 TYR B1024      -9.187  34.038 -28.898  1.00105.63           C  
ANISOU 5100  CE2 TYR B1024    13105  12778  14253    332   1626   1131       C  
ATOM   5101  CZ  TYR B1024      -9.358  35.266 -29.515  1.00115.66           C  
ANISOU 5101  CZ  TYR B1024    14465  13837  15645    393   1789   1262       C  
ATOM   5102  OH  TYR B1024     -10.577  35.901 -29.460  1.00118.74           O  
ANISOU 5102  OH  TYR B1024    14923  14257  15935    585   1812   1403       O  
ATOM   5103  N   TYR B1025      -2.358  33.498 -27.793  1.00101.05           N  
ANISOU 5103  N   TYR B1025    11844  11616  14937   -436   1548    365       N  
ATOM   5104  CA  TYR B1025      -1.164  32.757 -27.386  1.00100.67           C  
ANISOU 5104  CA  TYR B1025    11569  11621  15059   -537   1440    244       C  
ATOM   5105  C   TYR B1025      -1.643  31.645 -26.440  1.00102.35           C  
ANISOU 5105  C   TYR B1025    11797  12110  14983   -426   1202    164       C  
ATOM   5106  O   TYR B1025      -2.347  31.932 -25.469  1.00101.53           O  
ANISOU 5106  O   TYR B1025    11795  12060  14724   -343   1036     50       O  
ATOM   5107  CB  TYR B1025      -0.100  33.657 -26.729  1.00104.30           C  
ANISOU 5107  CB  TYR B1025    11861  11865  15903   -695   1346     40       C  
ATOM   5108  CG  TYR B1025       0.649  34.568 -27.686  1.00107.85           C  
ANISOU 5108  CG  TYR B1025    12233  12029  16717   -842   1610    136       C  
ATOM   5109  CD1 TYR B1025       0.600  35.952 -27.545  1.00112.00           C  
ANISOU 5109  CD1 TYR B1025    12832  12268  17456   -919   1657     64       C  
ATOM   5110  CD2 TYR B1025       1.442  34.045 -28.705  1.00108.80           C  
ANISOU 5110  CD2 TYR B1025    12213  12145  16980   -900   1835    300       C  
ATOM   5111  CE1 TYR B1025       1.305  36.793 -28.407  1.00115.11           C  
ANISOU 5111  CE1 TYR B1025    13152  12374  18209  -1063   1922    173       C  
ATOM   5112  CE2 TYR B1025       2.145  34.876 -29.576  1.00112.13           C  
ANISOU 5112  CE2 TYR B1025    12560  12302  17741  -1029   2114    414       C  
ATOM   5113  CZ  TYR B1025       2.079  36.250 -29.419  1.00121.71           C  
ANISOU 5113  CZ  TYR B1025    13837  13230  19179  -1119   2154    357       C  
ATOM   5114  OH  TYR B1025       2.775  37.069 -30.276  1.00125.12           O  
ANISOU 5114  OH  TYR B1025    14196  13379  19967  -1254   2453    490       O  
ATOM   5115  N   THR B1026      -1.301  30.374 -26.750  1.00 97.71           N  
ANISOU 5115  N   THR B1026    11129  11681  14315   -410   1217    238       N  
ATOM   5116  CA  THR B1026      -1.735  29.195 -25.988  1.00 95.77           C  
ANISOU 5116  CA  THR B1026    10906  11677  13807   -305   1037    207       C  
ATOM   5117  C   THR B1026      -0.573  28.272 -25.566  1.00 99.89           C  
ANISOU 5117  C   THR B1026    11216  12268  14470   -332    934    141       C  
ATOM   5118  O   THR B1026       0.415  28.141 -26.289  1.00100.64           O  
ANISOU 5118  O   THR B1026    11159  12272  14808   -410   1084    193       O  
ATOM   5119  CB  THR B1026      -2.859  28.482 -26.769  1.00103.71           C  
ANISOU 5119  CB  THR B1026    12087  12814  14506   -225   1153    392       C  
ATOM   5120  OG1 THR B1026      -3.878  28.082 -25.851  1.00102.43           O  
ANISOU 5120  OG1 THR B1026    12017  12823  14078   -115    987    363       O  
ATOM   5121  CG2 THR B1026      -2.387  27.266 -27.541  1.00103.99           C  
ANISOU 5121  CG2 THR B1026    12088  12912  14513   -241   1268    488       C  
ATOM   5122  N   ILE B1027      -0.713  27.638 -24.383  1.00 95.67           N  
ANISOU 5122  N   ILE B1027    10671  11900  13780   -246    693     44       N  
ATOM   5123  CA  ILE B1027       0.246  26.700 -23.785  1.00 95.97           C  
ANISOU 5123  CA  ILE B1027    10522  12039  13903   -222    549     -2       C  
ATOM   5124  C   ILE B1027      -0.491  25.430 -23.287  1.00 96.96           C  
ANISOU 5124  C   ILE B1027    10768  12368  13705    -78    474     70       C  
ATOM   5125  O   ILE B1027      -1.716  25.450 -23.141  1.00 94.32           O  
ANISOU 5125  O   ILE B1027    10630  12104  13104    -14    480    111       O  
ATOM   5126  CB  ILE B1027       1.067  27.409 -22.654  1.00101.70           C  
ANISOU 5126  CB  ILE B1027    11086  12738  14816   -278    279   -215       C  
ATOM   5127  CG1 ILE B1027       2.411  26.697 -22.356  1.00103.88           C  
ANISOU 5127  CG1 ILE B1027    11071  13076  15322   -290    159   -235       C  
ATOM   5128  CG2 ILE B1027       0.239  27.615 -21.374  1.00102.17           C  
ANISOU 5128  CG2 ILE B1027    11321  12914  14584   -175     43   -345       C  
ATOM   5129  CD1 ILE B1027       3.640  27.282 -23.026  1.00112.88           C  
ANISOU 5129  CD1 ILE B1027    11937  14043  16909   -452    270   -242       C  
ATOM   5130  N   GLY B1028       0.273  24.360 -23.045  1.00 94.07           N  
ANISOU 5130  N   GLY B1028    10268  12082  13395    -26    420    100       N  
ATOM   5131  CA  GLY B1028      -0.200  23.082 -22.526  1.00 92.69           C  
ANISOU 5131  CA  GLY B1028    10183  12064  12973    106    358    177       C  
ATOM   5132  C   GLY B1028      -1.292  22.420 -23.337  1.00 94.16           C  
ANISOU 5132  C   GLY B1028    10574  12265  12937    119    550    321       C  
ATOM   5133  O   GLY B1028      -1.130  22.184 -24.537  1.00 93.24           O  
ANISOU 5133  O   GLY B1028    10477  12055  12894     59    768    404       O  
ATOM   5134  N   ILE B1029      -2.418  22.129 -22.669  1.00 89.54           N  
ANISOU 5134  N   ILE B1029    10144  11801  12074    195    468    349       N  
ATOM   5135  CA  ILE B1029      -3.586  21.478 -23.261  1.00 87.55           C  
ANISOU 5135  CA  ILE B1029    10064  11590  11609    191    597    479       C  
ATOM   5136  C   ILE B1029      -4.573  22.650 -23.344  1.00 90.96           C  
ANISOU 5136  C   ILE B1029    10586  12022  11952    167    603    463       C  
ATOM   5137  O   ILE B1029      -5.221  23.007 -22.350  1.00 90.89           O  
ANISOU 5137  O   ILE B1029    10628  12102  11804    248    486    423       O  
ATOM   5138  CB  ILE B1029      -4.027  20.185 -22.499  1.00 90.11           C  
ANISOU 5138  CB  ILE B1029    10455  12033  11749    289    534    556       C  
ATOM   5139  CG1 ILE B1029      -2.834  19.373 -21.952  1.00 91.60           C  
ANISOU 5139  CG1 ILE B1029    10518  12225  12061    371    458    546       C  
ATOM   5140  CG2 ILE B1029      -4.920  19.313 -23.367  1.00 89.49           C  
ANISOU 5140  CG2 ILE B1029    10515  11947  11540    231    685    681       C  
ATOM   5141  CD1 ILE B1029      -2.442  19.746 -20.548  1.00 99.93           C  
ANISOU 5141  CD1 ILE B1029    11497  13385  13084    475    215    453       C  
ATOM   5142  N   GLY B1030      -4.634  23.247 -24.533  1.00 86.69           N  
ANISOU 5142  N   GLY B1030    10071  11376  11492     77    756    505       N  
ATOM   5143  CA  GLY B1030      -5.514  24.369 -24.851  1.00 85.79           C  
ANISOU 5143  CA  GLY B1030    10037  11235  11324     66    797    529       C  
ATOM   5144  C   GLY B1030      -5.717  25.468 -23.827  1.00 89.16           C  
ANISOU 5144  C   GLY B1030    10464  11651  11762    130    679    413       C  
ATOM   5145  O   GLY B1030      -6.827  25.999 -23.714  1.00 88.44           O  
ANISOU 5145  O   GLY B1030    10466  11601  11535    189    695    462       O  
ATOM   5146  N   HIS B1031      -4.650  25.822 -23.081  1.00 86.31           N  
ANISOU 5146  N   HIS B1031     9999  11231  11566    120    557    255       N  
ATOM   5147  CA  HIS B1031      -4.715  26.880 -22.074  1.00 87.25           C  
ANISOU 5147  CA  HIS B1031    10148  11312  11691    165    427     96       C  
ATOM   5148  C   HIS B1031      -4.325  28.236 -22.668  1.00 91.84           C  
ANISOU 5148  C   HIS B1031    10710  11673  12510     68    515     34       C  
ATOM   5149  O   HIS B1031      -3.142  28.496 -22.910  1.00 92.55           O  
ANISOU 5149  O   HIS B1031    10655  11639  12868    -45    508    -41       O  
ATOM   5150  CB  HIS B1031      -3.897  26.531 -20.815  1.00 89.34           C  
ANISOU 5150  CB  HIS B1031    10336  11654  11956    207    195    -57       C  
ATOM   5151  CG  HIS B1031      -3.803  27.665 -19.840  1.00 94.60           C  
ANISOU 5151  CG  HIS B1031    11056  12256  12631    225     44   -267       C  
ATOM   5152  ND1 HIS B1031      -4.806  27.914 -18.925  1.00 96.48           N  
ANISOU 5152  ND1 HIS B1031    11472  12582  12602    366     -3   -307       N  
ATOM   5153  CD2 HIS B1031      -2.836  28.601 -19.696  1.00 98.38           C  
ANISOU 5153  CD2 HIS B1031    11442  12576  13362    112    -52   -448       C  
ATOM   5154  CE1 HIS B1031      -4.421  28.991 -18.261  1.00 98.08           C  
ANISOU 5154  CE1 HIS B1031    11720  12670  12877    344   -127   -529       C  
ATOM   5155  NE2 HIS B1031      -3.239  29.433 -18.683  1.00 99.70           N  
ANISOU 5155  NE2 HIS B1031    11760  12721  13400    178   -177   -627       N  
ATOM   5156  N   LEU B1032      -5.329  29.097 -22.895  1.00 88.33           N  
ANISOU 5156  N   LEU B1032    10400  11174  11988    118    610     83       N  
ATOM   5157  CA  LEU B1032      -5.142  30.431 -23.455  1.00 89.66           C  
ANISOU 5157  CA  LEU B1032    10591  11109  12367     52    724     57       C  
ATOM   5158  C   LEU B1032      -4.413  31.328 -22.449  1.00 95.31           C  
ANISOU 5158  C   LEU B1032    11286  11683  13245      8    571   -198       C  
ATOM   5159  O   LEU B1032      -4.930  31.584 -21.357  1.00 95.53           O  
ANISOU 5159  O   LEU B1032    11427  11764  13105    116    447   -325       O  
ATOM   5160  CB  LEU B1032      -6.504  31.036 -23.839  1.00 89.38           C  
ANISOU 5160  CB  LEU B1032    10706  11072  12183    163    851    197       C  
ATOM   5161  CG  LEU B1032      -6.537  31.965 -25.052  1.00 94.98           C  
ANISOU 5161  CG  LEU B1032    11450  11587  13050    113   1052    326       C  
ATOM   5162  CD1 LEU B1032      -7.883  31.888 -25.741  1.00 94.11           C  
ANISOU 5162  CD1 LEU B1032    11432  11596  12729    226   1153    555       C  
ATOM   5163  CD2 LEU B1032      -6.246  33.406 -24.661  1.00 99.97           C  
ANISOU 5163  CD2 LEU B1032    12137  11954  13893     98   1075    182       C  
ATOM   5164  N   LEU B1033      -3.205  31.780 -22.815  1.00 92.79           N  
ANISOU 5164  N   LEU B1033    10822  11183  13250   -155    583   -276       N  
ATOM   5165  CA  LEU B1033      -2.392  32.652 -21.971  1.00 95.04           C  
ANISOU 5165  CA  LEU B1033    11059  11310  13742   -251    416   -534       C  
ATOM   5166  C   LEU B1033      -2.974  34.071 -21.936  1.00100.17           C  
ANISOU 5166  C   LEU B1033    11889  11721  14451   -237    510   -604       C  
ATOM   5167  O   LEU B1033      -3.372  34.539 -20.867  1.00100.72           O  
ANISOU 5167  O   LEU B1033    12105  11781  14384   -157    372   -791       O  
ATOM   5168  CB  LEU B1033      -0.921  32.661 -22.440  1.00 96.52           C  
ANISOU 5168  CB  LEU B1033    10987  11378  14308   -449    416   -567       C  
ATOM   5169  CG  LEU B1033      -0.109  31.398 -22.164  1.00100.38           C  
ANISOU 5169  CG  LEU B1033    11272  12072  14798   -451    272   -559       C  
ATOM   5170  CD1 LEU B1033       1.102  31.328 -23.064  1.00101.56           C  
ANISOU 5170  CD1 LEU B1033    11163  12106  15319   -606    407   -483       C  
ATOM   5171  CD2 LEU B1033       0.318  31.325 -20.714  1.00104.50           C  
ANISOU 5171  CD2 LEU B1033    11751  12698  15256   -435    -74   -798       C  
ATOM   5172  N   THR B1034      -3.050  34.732 -23.109  1.00 97.00           N  
ANISOU 5172  N   THR B1034    11502  11124  14232   -293    763   -442       N  
ATOM   5173  CA  THR B1034      -3.577  36.090 -23.275  1.00 98.46           C  
ANISOU 5173  CA  THR B1034    11856  11041  14512   -267    905   -453       C  
ATOM   5174  C   THR B1034      -4.274  36.298 -24.622  1.00101.57           C  
ANISOU 5174  C   THR B1034    12320  11389  14883   -200   1188   -146       C  
ATOM   5175  O   THR B1034      -3.855  35.734 -25.637  1.00100.28           O  
ANISOU 5175  O   THR B1034    12048  11277  14778   -271   1309     31       O  
ATOM   5176  CB  THR B1034      -2.499  37.169 -22.988  1.00107.78           C  
ANISOU 5176  CB  THR B1034    12975  11900  16078   -472    855   -680       C  
ATOM   5177  OG1 THR B1034      -3.079  38.464 -23.158  1.00108.18           O  
ANISOU 5177  OG1 THR B1034    13224  11659  16218   -427   1021   -679       O  
ATOM   5178  CG2 THR B1034      -1.258  37.042 -23.884  1.00105.89           C  
ANISOU 5178  CG2 THR B1034    12486  11557  16192   -684    956   -596       C  
ATOM   5179  N   LYS B1035      -5.336  37.123 -24.621  1.00 98.46           N  
ANISOU 5179  N   LYS B1035    12118  10899  14394    -48   1296    -80       N  
ATOM   5180  CA  LYS B1035      -6.090  37.484 -25.821  1.00 97.80           C  
ANISOU 5180  CA  LYS B1035    12116  10769  14273     46   1536    220       C  
ATOM   5181  C   LYS B1035      -5.407  38.665 -26.520  1.00105.51           C  
ANISOU 5181  C   LYS B1035    13112  11373  15605    -77   1733    255       C  
ATOM   5182  O   LYS B1035      -5.740  38.981 -27.667  1.00105.33           O  
ANISOU 5182  O   LYS B1035    13144  11284  15592    -29   1950    524       O  
ATOM   5183  CB  LYS B1035      -7.537  37.837 -25.463  1.00 99.31           C  
ANISOU 5183  CB  LYS B1035    12471  11034  14229    290   1563    300       C  
ATOM   5184  CG  LYS B1035      -8.560  36.981 -26.174  1.00102.72           C  
ANISOU 5184  CG  LYS B1035    12884  11764  14380    417   1598    577       C  
ATOM   5185  CD  LYS B1035      -9.967  37.417 -25.820  1.00110.46           C  
ANISOU 5185  CD  LYS B1035    13973  12810  15185    661   1638    677       C  
ATOM   5186  CE  LYS B1035     -10.968  36.321 -26.069  1.00119.17           C  
ANISOU 5186  CE  LYS B1035    15007  14274  15999    756   1578    871       C  
ATOM   5187  NZ  LYS B1035     -10.810  35.198 -25.107  1.00128.94           N  
ANISOU 5187  NZ  LYS B1035    16174  15733  17084    716   1397    711       N  
ATOM   5188  N   SER B1036      -4.447  39.308 -25.823  1.00105.38           N  
ANISOU 5188  N   SER B1036    13051  11111  15877   -243   1650    -13       N  
ATOM   5189  CA  SER B1036      -3.673  40.440 -26.325  1.00108.76           C  
ANISOU 5189  CA  SER B1036    13473  11144  16706   -407   1825    -18       C  
ATOM   5190  C   SER B1036      -2.532  39.943 -27.232  1.00113.48           C  
ANISOU 5190  C   SER B1036    13849  11746  17524   -601   1928     98       C  
ATOM   5191  O   SER B1036      -1.914  38.918 -26.924  1.00111.61           O  
ANISOU 5191  O   SER B1036    13428  11734  17246   -677   1761      8       O  
ATOM   5192  CB  SER B1036      -3.124  41.269 -25.165  1.00115.64           C  
ANISOU 5192  CB  SER B1036    14379  11760  17801   -534   1663   -379       C  
ATOM   5193  OG  SER B1036      -4.171  41.782 -24.355  1.00124.97           O  
ANISOU 5193  OG  SER B1036    15801  12910  18773   -331   1618   -489       O  
ATOM   5194  N   PRO B1037      -2.249  40.631 -28.365  1.00112.51           N  
ANISOU 5194  N   PRO B1037    13745  11377  17627   -661   2224    320       N  
ATOM   5195  CA  PRO B1037      -1.182  40.160 -29.261  1.00113.01           C  
ANISOU 5195  CA  PRO B1037    13607  11444  17889   -821   2374    451       C  
ATOM   5196  C   PRO B1037       0.224  40.603 -28.836  1.00120.93           C  
ANISOU 5196  C   PRO B1037    14378  12203  19368  -1102   2328    239       C  
ATOM   5197  O   PRO B1037       0.920  41.294 -29.588  1.00123.30           O  
ANISOU 5197  O   PRO B1037    14611  12219  20018  -1247   2585    363       O  
ATOM   5198  CB  PRO B1037      -1.608  40.696 -30.638  1.00115.38           C  
ANISOU 5198  CB  PRO B1037    14061  11611  18167   -730   2721    805       C  
ATOM   5199  CG  PRO B1037      -2.661  41.745 -30.369  1.00120.65           C  
ANISOU 5199  CG  PRO B1037    14971  12100  18769   -570   2754    828       C  
ATOM   5200  CD  PRO B1037      -2.882  41.855 -28.894  1.00116.05           C  
ANISOU 5200  CD  PRO B1037    14406  11529  18157   -564   2464    485       C  
ATOM   5201  N   SER B1038       0.649  40.182 -27.628  1.00117.98           N  
ANISOU 5201  N   SER B1038    13869  11953  19007  -1181   1993    -68       N  
ATOM   5202  CA  SER B1038       1.966  40.506 -27.072  1.00121.26           C  
ANISOU 5202  CA  SER B1038    14024  12194  19855  -1455   1858   -303       C  
ATOM   5203  C   SER B1038       2.571  39.306 -26.339  1.00124.03           C  
ANISOU 5203  C   SER B1038    14137  12873  20116  -1483   1553   -457       C  
ATOM   5204  O   SER B1038       1.985  38.811 -25.371  1.00121.88           O  
ANISOU 5204  O   SER B1038    13966  12827  19516  -1351   1280   -618       O  
ATOM   5205  CB  SER B1038       1.880  41.725 -26.153  1.00128.28           C  
ANISOU 5205  CB  SER B1038    15049  12770  20920  -1550   1723   -586       C  
ATOM   5206  OG  SER B1038       3.171  42.217 -25.827  1.00141.50           O  
ANISOU 5206  OG  SER B1038    16467  14216  23081  -1862   1625   -785       O  
ATOM   5207  N   LEU B1039       3.738  38.827 -26.824  1.00121.74           N  
ANISOU 5207  N   LEU B1039    13528  12608  20119  -1634   1627   -381       N  
ATOM   5208  CA  LEU B1039       4.458  37.680 -26.259  1.00120.89           C  
ANISOU 5208  CA  LEU B1039    13152  12792  19991  -1650   1377   -479       C  
ATOM   5209  C   LEU B1039       5.007  37.970 -24.863  1.00127.42           C  
ANISOU 5209  C   LEU B1039    13850  13608  20958  -1790    962   -836       C  
ATOM   5210  O   LEU B1039       5.100  37.055 -24.042  1.00125.60           O  
ANISOU 5210  O   LEU B1039    13538  13669  20516  -1708    665   -951       O  
ATOM   5211  CB  LEU B1039       5.571  37.194 -27.203  1.00121.97           C  
ANISOU 5211  CB  LEU B1039    12974  12926  20443  -1754   1615   -283       C  
ATOM   5212  CG  LEU B1039       6.116  35.787 -26.941  1.00125.24           C  
ANISOU 5212  CG  LEU B1039    13156  13667  20762  -1678   1462   -276       C  
ATOM   5213  CD1 LEU B1039       5.187  34.712 -27.500  1.00121.26           C  
ANISOU 5213  CD1 LEU B1039    12882  13414  19778  -1425   1588    -82       C  
ATOM   5214  CD2 LEU B1039       7.495  35.632 -27.523  1.00130.67           C  
ANISOU 5214  CD2 LEU B1039    13450  14281  21917  -1836   1636   -172       C  
ATOM   5215  N   ASN B1040       5.346  39.249 -24.592  1.00128.05           N  
ANISOU 5215  N   ASN B1040    13935  13341  21377  -1999    938  -1012       N  
ATOM   5216  CA  ASN B1040       5.830  39.721 -23.293  1.00131.12           C  
ANISOU 5216  CA  ASN B1040    14253  13668  21897  -2163    532  -1391       C  
ATOM   5217  C   ASN B1040       4.752  39.444 -22.236  1.00132.78           C  
ANISOU 5217  C   ASN B1040    14788  14086  21576  -1933    273  -1567       C  
ATOM   5218  O   ASN B1040       5.082  39.015 -21.132  1.00133.24           O  
ANISOU 5218  O   ASN B1040    14768  14342  21515  -1943   -114  -1804       O  
ATOM   5219  CB  ASN B1040       6.173  41.219 -23.362  1.00136.61           C  
ANISOU 5219  CB  ASN B1040    14985  13894  23028  -2420    624  -1528       C  
ATOM   5220  CG  ASN B1040       6.887  41.780 -22.150  1.00164.66           C  
ANISOU 5220  CG  ASN B1040    18425  17333  26803  -2664    203  -1941       C  
ATOM   5221  OD1 ASN B1040       7.778  41.154 -21.564  1.00160.35           O  
ANISOU 5221  OD1 ASN B1040    17557  17007  26361  -2771   -118  -2069       O  
ATOM   5222  ND2 ASN B1040       6.535  43.002 -21.777  1.00159.10           N  
ANISOU 5222  ND2 ASN B1040    17989  16271  26192  -2762    197  -2156       N  
ATOM   5223  N   ALA B1041       3.465  39.624 -22.615  1.00126.62           N  
ANISOU 5223  N   ALA B1041    14353  13287  20471  -1707    498  -1417       N  
ATOM   5224  CA  ALA B1041       2.296  39.359 -21.775  1.00124.28           C  
ANISOU 5224  CA  ALA B1041    14364  13184  19674  -1456    348  -1513       C  
ATOM   5225  C   ALA B1041       2.004  37.853 -21.707  1.00124.07           C  
ANISOU 5225  C   ALA B1041    14271  13588  19283  -1261    266  -1363       C  
ATOM   5226  O   ALA B1041       1.526  37.376 -20.676  1.00122.90           O  
ANISOU 5226  O   ALA B1041    14247  13662  18787  -1117     21  -1505       O  
ATOM   5227  CB  ALA B1041       1.084  40.106 -22.309  1.00124.00           C  
ANISOU 5227  CB  ALA B1041    14655  12968  19493  -1291    642  -1364       C  
ATOM   5228  N   ALA B1042       2.295  37.110 -22.805  1.00118.40           N  
ANISOU 5228  N   ALA B1042    13376  12969  18641  -1255    489  -1078       N  
ATOM   5229  CA  ALA B1042       2.115  35.654 -22.891  1.00114.84           C  
ANISOU 5229  CA  ALA B1042    12858  12873  17902  -1096    452   -925       C  
ATOM   5230  C   ALA B1042       3.087  34.955 -21.939  1.00119.20           C  
ANISOU 5230  C   ALA B1042    13162  13613  18516  -1158    110  -1102       C  
ATOM   5231  O   ALA B1042       2.709  33.986 -21.279  1.00116.92           O  
ANISOU 5231  O   ALA B1042    12926  13606  17890   -992    -66  -1110       O  
ATOM   5232  CB  ALA B1042       2.337  35.176 -24.317  1.00114.17           C  
ANISOU 5232  CB  ALA B1042    12668  12787  17926  -1101    785   -620       C  
ATOM   5233  N   LYS B1043       4.328  35.481 -21.845  1.00118.69           N  
ANISOU 5233  N   LYS B1043    12818  13386  18894  -1398      9  -1234       N  
ATOM   5234  CA  LYS B1043       5.358  34.981 -20.941  1.00120.36           C  
ANISOU 5234  CA  LYS B1043    12746  13761  19225  -1479   -353  -1407       C  
ATOM   5235  C   LYS B1043       5.001  35.393 -19.508  1.00125.53           C  
ANISOU 5235  C   LYS B1043    13602  14463  19629  -1450   -732  -1728       C  
ATOM   5236  O   LYS B1043       5.066  34.552 -18.616  1.00124.83           O  
ANISOU 5236  O   LYS B1043    13489  14660  19280  -1328  -1019  -1799       O  
ATOM   5237  CB  LYS B1043       6.750  35.490 -21.347  1.00126.35           C  
ANISOU 5237  CB  LYS B1043    13113  14324  20570  -1762   -334  -1434       C  
ATOM   5238  CG  LYS B1043       7.310  34.814 -22.602  1.00137.73           C  
ANISOU 5238  CG  LYS B1043    14308  15791  22233  -1755     11  -1120       C  
ATOM   5239  CD  LYS B1043       8.763  35.205 -22.884  1.00151.72           C  
ANISOU 5239  CD  LYS B1043    15629  17409  24609  -2022     23  -1133       C  
ATOM   5240  CE  LYS B1043       8.900  36.410 -23.789  1.00162.61           C  
ANISOU 5240  CE  LYS B1043    17022  18403  26358  -2222    361  -1061       C  
ATOM   5241  NZ  LYS B1043      10.326  36.753 -24.037  1.00175.94           N  
ANISOU 5241  NZ  LYS B1043    18234  19945  28668  -2496    387  -1058       N  
ATOM   5242  N   SER B1044       4.553  36.662 -19.310  1.00123.55           N  
ANISOU 5242  N   SER B1044    13591  13928  19423  -1533   -701  -1907       N  
ATOM   5243  CA  SER B1044       4.130  37.226 -18.018  1.00125.17           C  
ANISOU 5243  CA  SER B1044    14064  14119  19377  -1499  -1002  -2235       C  
ATOM   5244  C   SER B1044       2.974  36.430 -17.406  1.00125.37           C  
ANISOU 5244  C   SER B1044    14374  14438  18822  -1180  -1041  -2179       C  
ATOM   5245  O   SER B1044       2.942  36.235 -16.190  1.00126.06           O  
ANISOU 5245  O   SER B1044    14572  14694  18632  -1105  -1369  -2400       O  
ATOM   5246  CB  SER B1044       3.733  38.693 -18.178  1.00130.95           C  
ANISOU 5246  CB  SER B1044    15036  14444  20275  -1608   -842  -2374       C  
ATOM   5247  OG  SER B1044       3.381  39.290 -16.941  1.00142.19           O  
ANISOU 5247  OG  SER B1044    16744  15817  21465  -1578  -1112  -2721       O  
ATOM   5248  N   GLU B1045       2.036  35.963 -18.250  1.00118.34           N  
ANISOU 5248  N   GLU B1045    13599  13616  17749   -999   -711  -1878       N  
ATOM   5249  CA  GLU B1045       0.909  35.146 -17.810  1.00115.37           C  
ANISOU 5249  CA  GLU B1045    13447  13513  16877   -718   -703  -1776       C  
ATOM   5250  C   GLU B1045       1.378  33.741 -17.459  1.00117.78           C  
ANISOU 5250  C   GLU B1045    13562  14150  17039   -639   -886  -1688       C  
ATOM   5251  O   GLU B1045       0.868  33.156 -16.504  1.00116.74           O  
ANISOU 5251  O   GLU B1045    13583  14247  16525   -459  -1054  -1737       O  
ATOM   5252  CB  GLU B1045      -0.199  35.096 -18.872  1.00113.60           C  
ANISOU 5252  CB  GLU B1045    13365  13255  16543   -583   -324  -1483       C  
ATOM   5253  CG  GLU B1045      -1.127  36.298 -18.846  1.00127.01           C  
ANISOU 5253  CG  GLU B1045    15352  14715  18191   -520   -169  -1548       C  
ATOM   5254  CD  GLU B1045      -1.884  36.514 -17.549  1.00153.18           C  
ANISOU 5254  CD  GLU B1045    18946  18107  21147   -346   -330  -1757       C  
ATOM   5255  OE1 GLU B1045      -1.527  37.458 -16.808  1.00153.42           O  
ANISOU 5255  OE1 GLU B1045    19091  17937  21266   -439   -487  -2063       O  
ATOM   5256  OE2 GLU B1045      -2.805  35.717 -17.254  1.00146.81           O  
ANISOU 5256  OE2 GLU B1045    18247  17560  19973   -124   -298  -1623       O  
ATOM   5257  N   LEU B1046       2.363  33.217 -18.221  1.00113.98           N  
ANISOU 5257  N   LEU B1046    12754  13682  16873   -761   -832  -1548       N  
ATOM   5258  CA  LEU B1046       2.955  31.894 -18.021  1.00112.89           C  
ANISOU 5258  CA  LEU B1046    12400  13815  16677   -687   -970  -1441       C  
ATOM   5259  C   LEU B1046       3.802  31.871 -16.746  1.00120.17           C  
ANISOU 5259  C   LEU B1046    13199  14861  17599   -732  -1412  -1692       C  
ATOM   5260  O   LEU B1046       3.621  30.972 -15.929  1.00119.33           O  
ANISOU 5260  O   LEU B1046    13152  15020  17168   -553  -1603  -1677       O  
ATOM   5261  CB  LEU B1046       3.775  31.472 -19.260  1.00112.28           C  
ANISOU 5261  CB  LEU B1046    12021  13676  16965   -792   -736  -1225       C  
ATOM   5262  CG  LEU B1046       4.295  30.028 -19.329  1.00115.78           C  
ANISOU 5262  CG  LEU B1046    12261  14359  17372   -680   -768  -1054       C  
ATOM   5263  CD1 LEU B1046       3.161  29.016 -19.395  1.00112.30           C  
ANISOU 5263  CD1 LEU B1046    12066  14097  16507   -453   -640   -876       C  
ATOM   5264  CD2 LEU B1046       5.180  29.842 -20.533  1.00118.35           C  
ANISOU 5264  CD2 LEU B1046    12302  14573  18093   -792   -509   -880       C  
ATOM   5265  N   ASP B1047       4.686  32.879 -16.559  1.00120.45           N  
ANISOU 5265  N   ASP B1047    13078  14701  17987   -974  -1582  -1921       N  
ATOM   5266  CA  ASP B1047       5.545  33.030 -15.380  1.00124.43           C  
ANISOU 5266  CA  ASP B1047    13455  15303  18521  -1065  -2051  -2199       C  
ATOM   5267  C   ASP B1047       4.717  33.011 -14.085  1.00128.73           C  
ANISOU 5267  C   ASP B1047    14375  16008  18530   -872  -2289  -2385       C  
ATOM   5268  O   ASP B1047       5.079  32.307 -13.142  1.00129.73           O  
ANISOU 5268  O   ASP B1047    14452  16404  18436   -767  -2621  -2442       O  
ATOM   5269  CB  ASP B1047       6.373  34.333 -15.469  1.00130.49           C  
ANISOU 5269  CB  ASP B1047    14064  15762  19753  -1391  -2151  -2440       C  
ATOM   5270  CG  ASP B1047       7.543  34.302 -16.440  1.00141.25           C  
ANISOU 5270  CG  ASP B1047    14962  17016  21689  -1606  -2022  -2293       C  
ATOM   5271  OD1 ASP B1047       7.572  35.140 -17.364  1.00141.78           O  
ANISOU 5271  OD1 ASP B1047    15009  16773  22089  -1773  -1717  -2240       O  
ATOM   5272  OD2 ASP B1047       8.464  33.490 -16.233  1.00148.28           O  
ANISOU 5272  OD2 ASP B1047    15504  18123  22711  -1603  -2226  -2229       O  
ATOM   5273  N   LYS B1048       3.585  33.746 -14.070  1.00124.19           N  
ANISOU 5273  N   LYS B1048    14175  15273  17737   -797  -2092  -2449       N  
ATOM   5274  CA  LYS B1048       2.672  33.855 -12.931  1.00124.49           C  
ANISOU 5274  CA  LYS B1048    14607  15422  17271   -595  -2224  -2614       C  
ATOM   5275  C   LYS B1048       1.726  32.658 -12.768  1.00124.84           C  
ANISOU 5275  C   LYS B1048    14798  15755  16879   -292  -2089  -2354       C  
ATOM   5276  O   LYS B1048       1.219  32.441 -11.664  1.00125.37           O  
ANISOU 5276  O   LYS B1048    15121  15999  16515   -106  -2253  -2458       O  
ATOM   5277  CB  LYS B1048       1.900  35.186 -12.977  1.00127.94           C  
ANISOU 5277  CB  LYS B1048    15364  15545  17703   -630  -2044  -2786       C  
ATOM   5278  CG  LYS B1048       2.710  36.359 -12.439  1.00149.63           C  
ANISOU 5278  CG  LYS B1048    18113  18045  20694   -887  -2323  -3175       C  
ATOM   5279  CD  LYS B1048       2.389  37.671 -13.138  1.00161.02           C  
ANISOU 5279  CD  LYS B1048    19688  19060  22433  -1028  -2037  -3241       C  
ATOM   5280  CE  LYS B1048       3.285  38.777 -12.634  1.00177.00           C  
ANISOU 5280  CE  LYS B1048    21689  20810  24753  -1326  -2321  -3634       C  
ATOM   5281  NZ  LYS B1048       3.083  40.044 -13.383  1.00186.31           N  
ANISOU 5281  NZ  LYS B1048    22973  21529  26287  -1482  -2020  -3671       N  
ATOM   5282  N   ALA B1049       1.497  31.881 -13.854  1.00117.83           N  
ANISOU 5282  N   ALA B1049    13762  14908  16101   -248  -1789  -2022       N  
ATOM   5283  CA  ALA B1049       0.622  30.701 -13.836  1.00114.47           C  
ANISOU 5283  CA  ALA B1049    13445  14720  15328     -5  -1641  -1762       C  
ATOM   5284  C   ALA B1049       1.184  29.589 -12.953  1.00119.97           C  
ANISOU 5284  C   ALA B1049    14044  15709  15830    114  -1930  -1735       C  
ATOM   5285  O   ALA B1049       0.429  28.966 -12.205  1.00118.96           O  
ANISOU 5285  O   ALA B1049    14134  15777  15289    334  -1948  -1668       O  
ATOM   5286  CB  ALA B1049       0.393  30.184 -15.248  1.00111.66           C  
ANISOU 5286  CB  ALA B1049    12951  14309  15165    -31  -1291  -1459       C  
ATOM   5287  N   ILE B1050       2.507  29.359 -13.025  1.00118.86           N  
ANISOU 5287  N   ILE B1050    13569  15597  15997    -21  -2145  -1770       N  
ATOM   5288  CA  ILE B1050       3.194  28.333 -12.236  1.00120.39           C  
ANISOU 5288  CA  ILE B1050    13620  16062  16060     97  -2442  -1724       C  
ATOM   5289  C   ILE B1050       4.221  28.901 -11.239  1.00129.51           C  
ANISOU 5289  C   ILE B1050    14663  17269  17274    -14  -2917  -2026       C  
ATOM   5290  O   ILE B1050       5.050  28.159 -10.711  1.00131.16           O  
ANISOU 5290  O   ILE B1050    14662  17693  17480     47  -3203  -1985       O  
ATOM   5291  CB  ILE B1050       3.727  27.140 -13.086  1.00121.54           C  
ANISOU 5291  CB  ILE B1050    13470  16280  16428    132  -2283  -1421       C  
ATOM   5292  CG1 ILE B1050       4.615  27.590 -14.283  1.00122.06           C  
ANISOU 5292  CG1 ILE B1050    13202  16131  17043   -106  -2128  -1393       C  
ATOM   5293  CG2 ILE B1050       2.592  26.172 -13.481  1.00118.47           C  
ANISOU 5293  CG2 ILE B1050    13286  15964  15764    325  -1961  -1147       C  
ATOM   5294  CD1 ILE B1050       3.908  27.800 -15.652  1.00125.43           C  
ANISOU 5294  CD1 ILE B1050    13712  16353  17593   -163  -1667  -1227       C  
ATOM   5295  N   GLY B1051       4.131  30.208 -10.977  1.00128.56           N  
ANISOU 5295  N   GLY B1051    14694  16950  17202   -172  -3004  -2326       N  
ATOM   5296  CA  GLY B1051       4.986  30.918 -10.029  1.00133.65           C  
ANISOU 5296  CA  GLY B1051    15290  17603  17887   -319  -3467  -2672       C  
ATOM   5297  C   GLY B1051       6.415  31.150 -10.480  1.00140.47           C  
ANISOU 5297  C   GLY B1051    15670  18388  19313   -594  -3656  -2726       C  
ATOM   5298  O   GLY B1051       6.870  32.298 -10.522  1.00143.29           O  
ANISOU 5298  O   GLY B1051    15972  18506  19965   -863  -3769  -2991       O  
ATOM   5299  N   ARG B1052       7.139  30.053 -10.798  1.00135.87           N  
ANISOU 5299  N   ARG B1052    14731  17996  18900   -527  -3681  -2468       N  
ATOM   5300  CA  ARG B1052       8.542  30.061 -11.236  1.00138.02           C  
ANISOU 5300  CA  ARG B1052    14475  18243  19723   -741  -3833  -2451       C  
ATOM   5301  C   ARG B1052       8.760  30.738 -12.604  1.00140.40           C  
ANISOU 5301  C   ARG B1052    14580  18213  20553   -983  -3444  -2376       C  
ATOM   5302  O   ARG B1052       7.813  30.858 -13.385  1.00136.00           O  
ANISOU 5302  O   ARG B1052    14264  17498  19911   -925  -3019  -2242       O  
ATOM   5303  CB  ARG B1052       9.125  28.628 -11.236  1.00136.54           C  
ANISOU 5303  CB  ARG B1052    13997  18338  19542   -537  -3890  -2154       C  
ATOM   5304  CG  ARG B1052       8.497  27.679 -12.262  1.00138.01           C  
ANISOU 5304  CG  ARG B1052    14237  18501  19699   -360  -3388  -1793       C  
ATOM   5305  CD  ARG B1052       9.454  26.591 -12.706  1.00144.02           C  
ANISOU 5305  CD  ARG B1052    14580  19392  20750   -277  -3355  -1526       C  
ATOM   5306  NE  ARG B1052       9.179  26.151 -14.077  1.00147.79           N  
ANISOU 5306  NE  ARG B1052    15021  19710  21423   -260  -2832  -1263       N  
ATOM   5307  CZ  ARG B1052      10.011  26.314 -15.102  1.00161.89           C  
ANISOU 5307  CZ  ARG B1052    16447  21342  23722   -419  -2621  -1170       C  
ATOM   5308  NH1 ARG B1052      11.191  26.895 -14.924  1.00154.53           N  
ANISOU 5308  NH1 ARG B1052    15109  20391  23212   -622  -2883  -1300       N  
ATOM   5309  NH2 ARG B1052       9.677  25.882 -16.309  1.00143.17           N  
ANISOU 5309  NH2 ARG B1052    14117  18841  21442   -377  -2146   -943       N  
ATOM   5310  N   ASN B1053      10.018  31.149 -12.897  1.00140.46           N  
ANISOU 5310  N   ASN B1053    14131  18130  21107  -1246  -3591  -2441       N  
ATOM   5311  CA  ASN B1053      10.387  31.765 -14.176  1.00139.72           C  
ANISOU 5311  CA  ASN B1053    13808  17728  21549  -1479  -3219  -2345       C  
ATOM   5312  C   ASN B1053      10.316  30.713 -15.287  1.00139.92           C  
ANISOU 5312  C   ASN B1053    13702  17806  21655  -1309  -2784  -1951       C  
ATOM   5313  O   ASN B1053      10.837  29.609 -15.119  1.00139.94           O  
ANISOU 5313  O   ASN B1053    13473  18056  21643  -1145  -2886  -1780       O  
ATOM   5314  CB  ASN B1053      11.763  32.415 -14.114  1.00144.51           C  
ANISOU 5314  CB  ASN B1053    13936  18243  22729  -1803  -3494  -2504       C  
ATOM   5315  CG  ASN B1053      11.992  33.385 -15.242  1.00161.33           C  
ANISOU 5315  CG  ASN B1053    15936  19992  25371  -2079  -3122  -2474       C  
ATOM   5316  OD1 ASN B1053      12.388  33.007 -16.349  1.00152.10           O  
ANISOU 5316  OD1 ASN B1053    14497  18761  24535  -2085  -2748  -2188       O  
ATOM   5317  ND2 ASN B1053      11.703  34.654 -15.001  1.00153.25           N  
ANISOU 5317  ND2 ASN B1053    15141  18689  24399  -2294  -3185  -2760       N  
ATOM   5318  N   THR B1054       9.645  31.047 -16.401  1.00133.04           N  
ANISOU 5318  N   THR B1054    13006  16701  20841  -1332  -2305  -1811       N  
ATOM   5319  CA  THR B1054       9.415  30.109 -17.503  1.00129.08           C  
ANISOU 5319  CA  THR B1054    12476  16227  20342  -1174  -1875  -1470       C  
ATOM   5320  C   THR B1054      10.238  30.312 -18.767  1.00133.58           C  
ANISOU 5320  C   THR B1054    12706  16602  21446  -1339  -1532  -1299       C  
ATOM   5321  O   THR B1054      10.699  29.316 -19.325  1.00132.47           O  
ANISOU 5321  O   THR B1054    12353  16569  21411  -1216  -1354  -1062       O  
ATOM   5322  CB  THR B1054       7.924  30.025 -17.837  1.00133.18           C  
ANISOU 5322  CB  THR B1054    13473  16708  20422  -1008  -1588  -1382       C  
ATOM   5323  OG1 THR B1054       7.464  31.313 -18.251  1.00133.38           O  
ANISOU 5323  OG1 THR B1054    13680  16443  20554  -1176  -1422  -1496       O  
ATOM   5324  CG2 THR B1054       7.090  29.504 -16.673  1.00130.73           C  
ANISOU 5324  CG2 THR B1054    13473  16632  19566   -785  -1842  -1462       C  
ATOM   5325  N   ASN B1055      10.376  31.543 -19.247  1.00131.53           N  
ANISOU 5325  N   ASN B1055    12426  16046  21502  -1590  -1398  -1398       N  
ATOM   5326  CA  ASN B1055      11.086  31.790 -20.503  1.00132.21           C  
ANISOU 5326  CA  ASN B1055    12226  15928  22078  -1739  -1010  -1207       C  
ATOM   5327  C   ASN B1055      10.358  31.211 -21.721  1.00131.21           C  
ANISOU 5327  C   ASN B1055    12328  15768  21759  -1562   -508   -917       C  
ATOM   5328  O   ASN B1055      10.966  30.960 -22.762  1.00131.40           O  
ANISOU 5328  O   ASN B1055    12129  15714  22084  -1587   -166   -702       O  
ATOM   5329  CB  ASN B1055      12.511  31.239 -20.429  1.00137.41           C  
ANISOU 5329  CB  ASN B1055    12325  16716  23168  -1796  -1148  -1135       C  
ATOM   5330  CG  ASN B1055      13.345  31.616 -21.638  1.00163.85           C  
ANISOU 5330  CG  ASN B1055    15341  19840  27073  -1971   -743   -952       C  
ATOM   5331  OD1 ASN B1055      13.438  32.788 -22.001  1.00161.22           O  
ANISOU 5331  OD1 ASN B1055    15006  19219  27032  -2221   -619  -1032       O  
ATOM   5332  ND2 ASN B1055      13.956  30.620 -22.269  1.00153.93           N  
ANISOU 5332  ND2 ASN B1055    13818  18700  25969  -1828   -508   -695       N  
ATOM   5333  N   GLY B1056       9.054  31.004 -21.573  1.00123.10           N  
ANISOU 5333  N   GLY B1056    11745  14805  20223  -1384   -472   -915       N  
ATOM   5334  CA  GLY B1056       8.193  30.469 -22.624  1.00118.55           C  
ANISOU 5334  CA  GLY B1056    11431  14218  19393  -1225    -69   -676       C  
ATOM   5335  C   GLY B1056       8.006  28.967 -22.722  1.00118.90           C  
ANISOU 5335  C   GLY B1056    11508  14502  19167   -984    -14   -502       C  
ATOM   5336  O   GLY B1056       7.174  28.501 -23.504  1.00115.15           O  
ANISOU 5336  O   GLY B1056    11293  14028  18431   -864    269   -340       O  
ATOM   5337  N   VAL B1057       8.774  28.199 -21.925  1.00116.72           N  
ANISOU 5337  N   VAL B1057    10972  14423  18952   -913   -295   -534       N  
ATOM   5338  CA  VAL B1057       8.739  26.734 -21.926  1.00114.66           C  
ANISOU 5338  CA  VAL B1057    10717  14364  18486   -678   -253   -366       C  
ATOM   5339  C   VAL B1057       8.301  26.133 -20.572  1.00117.88           C  
ANISOU 5339  C   VAL B1057    11259  15013  18518   -514   -640   -465       C  
ATOM   5340  O   VAL B1057       8.582  26.707 -19.515  1.00119.90           O  
ANISOU 5340  O   VAL B1057    11439  15330  18789   -587  -1020   -671       O  
ATOM   5341  CB  VAL B1057      10.073  26.147 -22.481  1.00120.90           C  
ANISOU 5341  CB  VAL B1057    11077  15157  19703   -674   -107   -213       C  
ATOM   5342  CG1 VAL B1057      11.235  26.312 -21.501  1.00124.84           C  
ANISOU 5342  CG1 VAL B1057    11150  15766  20519   -750   -509   -335       C  
ATOM   5343  CG2 VAL B1057       9.920  24.695 -22.927  1.00118.73           C  
ANISOU 5343  CG2 VAL B1057    10887  14987  19237   -431    110     -3       C  
ATOM   5344  N   ILE B1058       7.587  24.989 -20.628  1.00111.43           N  
ANISOU 5344  N   ILE B1058    10665  14319  17354   -299   -532   -317       N  
ATOM   5345  CA  ILE B1058       7.088  24.218 -19.478  1.00110.59           C  
ANISOU 5345  CA  ILE B1058    10719  14435  16866   -108   -808   -338       C  
ATOM   5346  C   ILE B1058       7.325  22.705 -19.678  1.00114.29           C  
ANISOU 5346  C   ILE B1058    11133  15010  17283    101   -686   -119       C  
ATOM   5347  O   ILE B1058       7.675  22.286 -20.781  1.00113.26           O  
ANISOU 5347  O   ILE B1058    10913  14769  17353     99   -355     29       O  
ATOM   5348  CB  ILE B1058       5.604  24.547 -19.123  1.00110.83           C  
ANISOU 5348  CB  ILE B1058    11177  14477  16456    -65   -810   -406       C  
ATOM   5349  CG1 ILE B1058       4.655  24.410 -20.339  1.00107.69           C  
ANISOU 5349  CG1 ILE B1058    11016  13956  15945    -67   -408   -258       C  
ATOM   5350  CG2 ILE B1058       5.479  25.915 -18.451  1.00113.15           C  
ANISOU 5350  CG2 ILE B1058    11533  14704  16755   -207  -1038   -660       C  
ATOM   5351  CD1 ILE B1058       3.267  23.862 -20.001  1.00110.55           C  
ANISOU 5351  CD1 ILE B1058    11725  14425  15856     75   -383   -199       C  
ATOM   5352  N   THR B1059       7.150  21.893 -18.612  1.00111.65           N  
ANISOU 5352  N   THR B1059    10872  14875  16676    289   -936    -96       N  
ATOM   5353  CA  THR B1059       7.330  20.432 -18.657  1.00111.35           C  
ANISOU 5353  CA  THR B1059    10814  14919  16575    508   -836    115       C  
ATOM   5354  C   THR B1059       5.965  19.724 -18.770  1.00112.19           C  
ANISOU 5354  C   THR B1059    11329  15026  16271    614   -654    211       C  
ATOM   5355  O   THR B1059       4.948  20.309 -18.403  1.00110.01           O  
ANISOU 5355  O   THR B1059    11310  14769  15719    567   -716    112       O  
ATOM   5356  CB  THR B1059       8.144  19.931 -17.437  1.00122.51           C  
ANISOU 5356  CB  THR B1059    12008  16546  17996    662  -1223    122       C  
ATOM   5357  OG1 THR B1059       9.040  20.952 -16.988  1.00125.17           O  
ANISOU 5357  OG1 THR B1059    12042  16916  18602    504  -1528    -58       O  
ATOM   5358  CG2 THR B1059       8.923  18.649 -17.734  1.00121.96           C  
ANISOU 5358  CG2 THR B1059    11733  16499  18107    857  -1088    351       C  
ATOM   5359  N   LYS B1060       5.950  18.470 -19.283  1.00108.47           N  
ANISOU 5359  N   LYS B1060    10910  14522  15781    752   -419    403       N  
ATOM   5360  CA  LYS B1060       4.753  17.633 -19.441  1.00105.65           C  
ANISOU 5360  CA  LYS B1060    10902  14148  15090    833   -242    509       C  
ATOM   5361  C   LYS B1060       4.053  17.436 -18.089  1.00109.97           C  
ANISOU 5361  C   LYS B1060    11626  14873  15283    954   -509    496       C  
ATOM   5362  O   LYS B1060       2.829  17.540 -18.019  1.00107.16           O  
ANISOU 5362  O   LYS B1060    11550  14521  14643    927   -444    488       O  
ATOM   5363  CB  LYS B1060       5.134  16.273 -20.057  1.00108.26           C  
ANISOU 5363  CB  LYS B1060    11220  14397  15517    969      8    695       C  
ATOM   5364  CG  LYS B1060       3.950  15.379 -20.437  1.00117.83           C  
ANISOU 5364  CG  LYS B1060    12784  15540  16447   1000    225    793       C  
ATOM   5365  CD  LYS B1060       4.300  13.888 -20.358  1.00128.92           C  
ANISOU 5365  CD  LYS B1060    14210  16903  17872   1199    336    969       C  
ATOM   5366  CE  LYS B1060       4.948  13.337 -21.612  1.00139.67           C  
ANISOU 5366  CE  LYS B1060    15517  18072  19479   1205    674   1031       C  
ATOM   5367  NZ  LYS B1060       5.618  12.032 -21.359  1.00148.99           N  
ANISOU 5367  NZ  LYS B1060    16636  19210  20762   1439    744   1194       N  
ATOM   5368  N   ASP B1061       4.839  17.172 -17.022  1.00109.93           N  
ANISOU 5368  N   ASP B1061    11449  15024  15293   1096   -808    504       N  
ATOM   5369  CA  ASP B1061       4.334  16.995 -15.660  1.00110.65           C  
ANISOU 5369  CA  ASP B1061    11708  15305  15030   1240  -1076    500       C  
ATOM   5370  C   ASP B1061       3.857  18.334 -15.095  1.00114.17           C  
ANISOU 5370  C   ASP B1061    12254  15804  15321   1115  -1277    269       C  
ATOM   5371  O   ASP B1061       2.861  18.371 -14.369  1.00113.25           O  
ANISOU 5371  O   ASP B1061    12411  15775  14845   1185  -1326    256       O  
ATOM   5372  CB  ASP B1061       5.406  16.367 -14.751  1.00116.14           C  
ANISOU 5372  CB  ASP B1061    12181  16162  15785   1436  -1358    582       C  
ATOM   5373  CG  ASP B1061       4.892  15.846 -13.416  1.00129.45           C  
ANISOU 5373  CG  ASP B1061    14082  18040  17062   1645  -1573    654       C  
ATOM   5374  OD1 ASP B1061       3.660  15.649 -13.283  1.00128.29           O  
ANISOU 5374  OD1 ASP B1061    14259  17878  16609   1662  -1420    699       O  
ATOM   5375  OD2 ASP B1061       5.723  15.609 -12.513  1.00139.23           O  
ANISOU 5375  OD2 ASP B1061    15158  19453  18291   1798  -1887    685       O  
ATOM   5376  N   GLU B1062       4.552  19.432 -15.464  1.00110.86           N  
ANISOU 5376  N   GLU B1062    11621  15309  15191    930  -1357     95       N  
ATOM   5377  CA  GLU B1062       4.228  20.804 -15.066  1.00110.66           C  
ANISOU 5377  CA  GLU B1062    11682  15271  15094    786  -1520   -148       C  
ATOM   5378  C   GLU B1062       2.938  21.277 -15.759  1.00110.58           C  
ANISOU 5378  C   GLU B1062    11947  15128  14940    698  -1230   -153       C  
ATOM   5379  O   GLU B1062       2.210  22.093 -15.191  1.00110.37           O  
ANISOU 5379  O   GLU B1062    12121  15120  14696    678  -1319   -296       O  
ATOM   5380  CB  GLU B1062       5.403  21.736 -15.398  1.00114.34           C  
ANISOU 5380  CB  GLU B1062    11815  15649  15982    593  -1644   -302       C  
ATOM   5381  CG  GLU B1062       5.413  23.040 -14.619  1.00125.92           C  
ANISOU 5381  CG  GLU B1062    13328  17122  17394    466  -1939   -585       C  
ATOM   5382  CD  GLU B1062       6.703  23.830 -14.725  1.00146.03           C  
ANISOU 5382  CD  GLU B1062    15503  19603  20378    268  -2135   -737       C  
ATOM   5383  OE1 GLU B1062       7.278  24.158 -13.662  1.00143.17           O  
ANISOU 5383  OE1 GLU B1062    15047  19377  19974    261  -2551   -909       O  
ATOM   5384  OE2 GLU B1062       7.145  24.114 -15.862  1.00134.74           O  
ANISOU 5384  OE2 GLU B1062    13875  17990  19330    117  -1877   -681       O  
ATOM   5385  N   ALA B1063       2.659  20.754 -16.977  1.00103.84           N  
ANISOU 5385  N   ALA B1063    11109  14145  14198    659   -889      4       N  
ATOM   5386  CA  ALA B1063       1.469  21.064 -17.778  1.00100.26           C  
ANISOU 5386  CA  ALA B1063    10884  13586  13625    580   -620     38       C  
ATOM   5387  C   ALA B1063       0.198  20.526 -17.116  1.00102.34           C  
ANISOU 5387  C   ALA B1063    11426  13965  13495    712   -608    119       C  
ATOM   5388  O   ALA B1063      -0.860  21.138 -17.258  1.00100.57           O  
ANISOU 5388  O   ALA B1063    11381  13712  13120    668   -512     89       O  
ATOM   5389  CB  ALA B1063       1.611  20.488 -19.175  1.00 99.44           C  
ANISOU 5389  CB  ALA B1063    10733  13345  13706    520   -304    180       C  
ATOM   5390  N   GLU B1064       0.313  19.390 -16.382  1.00 99.20           N  
ANISOU 5390  N   GLU B1064    11049  13693  12948    883   -692    241       N  
ATOM   5391  CA  GLU B1064      -0.776  18.748 -15.635  1.00 97.82           C  
ANISOU 5391  CA  GLU B1064    11115  13632  12420   1021   -671    351       C  
ATOM   5392  C   GLU B1064      -1.287  19.695 -14.547  1.00100.77           C  
ANISOU 5392  C   GLU B1064    11630  14115  12542   1069   -859    198       C  
ATOM   5393  O   GLU B1064      -2.499  19.798 -14.359  1.00 98.80           O  
ANISOU 5393  O   GLU B1064    11585  13894  12059   1102   -739    241       O  
ATOM   5394  CB  GLU B1064      -0.303  17.439 -14.975  1.00100.77           C  
ANISOU 5394  CB  GLU B1064    11464  14103  12721   1209   -747    514       C  
ATOM   5395  CG  GLU B1064       0.110  16.332 -15.925  1.00112.30           C  
ANISOU 5395  CG  GLU B1064    12840  15438  14390   1207   -531    678       C  
ATOM   5396  CD  GLU B1064       0.095  14.958 -15.284  1.00136.22           C  
ANISOU 5396  CD  GLU B1064    15948  18527  17285   1406   -524    883       C  
ATOM   5397  OE1 GLU B1064      -0.949  14.274 -15.381  1.00128.29           O  
ANISOU 5397  OE1 GLU B1064    15147  17484  16113   1414   -337   1014       O  
ATOM   5398  OE2 GLU B1064       1.115  14.573 -14.667  1.00133.78           O  
ANISOU 5398  OE2 GLU B1064    15486  18299  17044   1554   -710    924       O  
ATOM   5399  N   LYS B1065      -0.354  20.393 -13.847  1.00 98.77           N  
ANISOU 5399  N   LYS B1065    11263  13918  12348   1068  -1152     12       N  
ATOM   5400  CA  LYS B1065      -0.640  21.360 -12.779  1.00 99.75           C  
ANISOU 5400  CA  LYS B1065    11539  14125  12236   1108  -1364   -189       C  
ATOM   5401  C   LYS B1065      -1.550  22.485 -13.297  1.00100.48           C  
ANISOU 5401  C   LYS B1065    11764  14082  12333    990  -1189   -297       C  
ATOM   5402  O   LYS B1065      -2.503  22.863 -12.611  1.00100.14           O  
ANISOU 5402  O   LYS B1065    11955  14099  11996   1086  -1170   -339       O  
ATOM   5403  CB  LYS B1065       0.669  21.921 -12.190  1.00105.36           C  
ANISOU 5403  CB  LYS B1065    12060  14881  13089   1064  -1723   -394       C  
ATOM   5404  CG  LYS B1065       0.511  22.555 -10.806  1.00120.36           C  
ANISOU 5404  CG  LYS B1065    14159  16919  14653   1161  -2012   -595       C  
ATOM   5405  CD  LYS B1065       1.847  22.756 -10.096  1.00132.53           C  
ANISOU 5405  CD  LYS B1065    15501  18565  16290   1143  -2432   -759       C  
ATOM   5406  CE  LYS B1065       2.508  24.076 -10.415  1.00142.32           C  
ANISOU 5406  CE  LYS B1065    16590  19644  17843    895  -2570  -1040       C  
ATOM   5407  NZ  LYS B1065       3.873  23.885 -10.978  1.00152.13           N  
ANISOU 5407  NZ  LYS B1065    17412  20854  19536    767  -2687  -1014       N  
ATOM   5408  N   LEU B1066      -1.274  22.974 -14.524  1.00 94.30           N  
ANISOU 5408  N   LEU B1066    10836  13115  11876    806  -1036   -313       N  
ATOM   5409  CA  LEU B1066      -2.051  24.012 -15.201  1.00 92.10           C  
ANISOU 5409  CA  LEU B1066    10658  12689  11649    700   -851   -372       C  
ATOM   5410  C   LEU B1066      -3.406  23.463 -15.652  1.00 91.91           C  
ANISOU 5410  C   LEU B1066    10788  12692  11440    762   -588   -168       C  
ATOM   5411  O   LEU B1066      -4.400  24.190 -15.627  1.00 90.39           O  
ANISOU 5411  O   LEU B1066    10746  12472  11127    780   -486   -193       O  
ATOM   5412  CB  LEU B1066      -1.283  24.531 -16.429  1.00 91.77           C  
ANISOU 5412  CB  LEU B1066    10412  12454  12003    503   -746   -397       C  
ATOM   5413  CG  LEU B1066      -1.103  26.041 -16.550  1.00 97.72           C  
ANISOU 5413  CG  LEU B1066    11167  13034  12927    367   -781   -604       C  
ATOM   5414  CD1 LEU B1066      -0.305  26.382 -17.782  1.00 97.77           C  
ANISOU 5414  CD1 LEU B1066    10962  12857  13327    185   -637   -573       C  
ATOM   5415  CD2 LEU B1066      -2.431  26.763 -16.603  1.00 98.89           C  
ANISOU 5415  CD2 LEU B1066    11559  13129  12887    413   -622   -604       C  
ATOM   5416  N   PHE B1067      -3.428  22.187 -16.091  1.00 86.54           N  
ANISOU 5416  N   PHE B1067    10059  12056  10764    788   -477     34       N  
ATOM   5417  CA  PHE B1067      -4.631  21.507 -16.566  1.00 83.86           C  
ANISOU 5417  CA  PHE B1067     9835  11742  10287    808   -254    229       C  
ATOM   5418  C   PHE B1067      -5.601  21.246 -15.430  1.00 88.70           C  
ANISOU 5418  C   PHE B1067    10622  12506  10571    972   -273    287       C  
ATOM   5419  O   PHE B1067      -6.799  21.466 -15.605  1.00 87.55           O  
ANISOU 5419  O   PHE B1067    10576  12375  10314    980   -118    364       O  
ATOM   5420  CB  PHE B1067      -4.283  20.207 -17.302  1.00 84.41           C  
ANISOU 5420  CB  PHE B1067     9827  11780  10465    777   -141    393       C  
ATOM   5421  CG  PHE B1067      -5.480  19.495 -17.883  1.00 84.02           C  
ANISOU 5421  CG  PHE B1067     9886  11733  10304    749     65    570       C  
ATOM   5422  CD1 PHE B1067      -6.150  20.011 -18.987  1.00 85.57           C  
ANISOU 5422  CD1 PHE B1067    10102  11850  10561    621    215    590       C  
ATOM   5423  CD2 PHE B1067      -5.936  18.305 -17.332  1.00 86.36           C  
ANISOU 5423  CD2 PHE B1067    10262  12111  10442    843     98    724       C  
ATOM   5424  CE1 PHE B1067      -7.261  19.354 -19.522  1.00 85.27           C  
ANISOU 5424  CE1 PHE B1067    10141  11832  10426    573    361    743       C  
ATOM   5425  CE2 PHE B1067      -7.053  17.654 -17.863  1.00 87.99           C  
ANISOU 5425  CE2 PHE B1067    10546  12308  10577    780    272    877       C  
ATOM   5426  CZ  PHE B1067      -7.697  18.173 -18.965  1.00 84.60           C  
ANISOU 5426  CZ  PHE B1067    10115  11816  10212    637    385    876       C  
ATOM   5427  N   ASN B1068      -5.083  20.781 -14.271  1.00 87.08           N  
ANISOU 5427  N   ASN B1068    10448  12426  10213   1115   -458    266       N  
ATOM   5428  CA  ASN B1068      -5.869  20.516 -13.066  1.00 87.90           C  
ANISOU 5428  CA  ASN B1068    10739  12685   9974   1299   -472    328       C  
ATOM   5429  C   ASN B1068      -6.514  21.814 -12.591  1.00 92.26           C  
ANISOU 5429  C   ASN B1068    11431  13239  10387   1337   -478    163       C  
ATOM   5430  O   ASN B1068      -7.685  21.799 -12.223  1.00 91.93           O  
ANISOU 5430  O   ASN B1068    11527  13265  10137   1437   -321    264       O  
ATOM   5431  CB  ASN B1068      -4.995  19.904 -11.970  1.00 91.41           C  
ANISOU 5431  CB  ASN B1068    11192  13261  10279   1450   -705    322       C  
ATOM   5432  CG  ASN B1068      -4.531  18.490 -12.240  1.00112.20           C  
ANISOU 5432  CG  ASN B1068    13731  15895  13003   1480   -661    530       C  
ATOM   5433  OD1 ASN B1068      -4.728  17.916 -13.321  1.00101.60           O  
ANISOU 5433  OD1 ASN B1068    12317  14435  11852   1365   -463    652       O  
ATOM   5434  ND2 ASN B1068      -3.891  17.897 -11.245  1.00107.86           N  
ANISOU 5434  ND2 ASN B1068    13201  15474  12307   1649   -850    574       N  
ATOM   5435  N   GLN B1069      -5.764  22.944 -12.677  1.00 89.30           N  
ANISOU 5435  N   GLN B1069    11007  12764  10161   1247   -630    -81       N  
ATOM   5436  CA  GLN B1069      -6.223  24.297 -12.350  1.00 89.88           C  
ANISOU 5436  CA  GLN B1069    11219  12771  10162   1262   -631   -275       C  
ATOM   5437  C   GLN B1069      -7.370  24.672 -13.290  1.00 91.29           C  
ANISOU 5437  C   GLN B1069    11409  12859  10418   1213   -347   -151       C  
ATOM   5438  O   GLN B1069      -8.364  25.236 -12.836  1.00 91.48           O  
ANISOU 5438  O   GLN B1069    11589  12906  10262   1331   -234   -158       O  
ATOM   5439  CB  GLN B1069      -5.074  25.312 -12.500  1.00 92.69           C  
ANISOU 5439  CB  GLN B1069    11477  12983  10758   1116   -834   -540       C  
ATOM   5440  CG  GLN B1069      -4.178  25.436 -11.266  1.00110.58           C  
ANISOU 5440  CG  GLN B1069    13792  15350  12874   1183  -1170   -747       C  
ATOM   5441  CD  GLN B1069      -2.930  26.260 -11.508  1.00128.15           C  
ANISOU 5441  CD  GLN B1069    15845  17435  15410    991  -1391   -986       C  
ATOM   5442  OE1 GLN B1069      -1.803  25.764 -11.407  1.00123.56           O  
ANISOU 5442  OE1 GLN B1069    15063  16917  14968    943  -1607   -999       O  
ATOM   5443  NE2 GLN B1069      -3.096  27.550 -11.780  1.00119.94           N  
ANISOU 5443  NE2 GLN B1069    14874  16198  14500    884  -1340  -1173       N  
ATOM   5444  N   ASP B1070      -7.245  24.315 -14.590  1.00 85.11           N  
ANISOU 5444  N   ASP B1070    10464  11987   9888   1058   -230    -25       N  
ATOM   5445  CA  ASP B1070      -8.259  24.570 -15.615  1.00 82.65           C  
ANISOU 5445  CA  ASP B1070    10138  11611   9652    999     -1    114       C  
ATOM   5446  C   ASP B1070      -9.515  23.704 -15.431  1.00 84.55           C  
ANISOU 5446  C   ASP B1070    10431  11996   9696   1094    155    343       C  
ATOM   5447  O   ASP B1070     -10.620  24.202 -15.651  1.00 83.73           O  
ANISOU 5447  O   ASP B1070    10363  11900   9550   1133    305    422       O  
ATOM   5448  CB  ASP B1070      -7.672  24.420 -17.033  1.00 82.87           C  
ANISOU 5448  CB  ASP B1070    10011  11513   9965    811     60    166       C  
ATOM   5449  CG  ASP B1070      -6.763  25.561 -17.478  1.00 95.18           C  
ANISOU 5449  CG  ASP B1070    11504  12890  11768    696      2    -16       C  
ATOM   5450  OD1 ASP B1070      -7.024  26.722 -17.085  1.00 97.12           O  
ANISOU 5450  OD1 ASP B1070    11847  13059  11997    734    -12   -153       O  
ATOM   5451  OD2 ASP B1070      -5.823  25.301 -18.263  1.00101.63           O  
ANISOU 5451  OD2 ASP B1070    12180  13625  12811    569      0    -10       O  
ATOM   5452  N   VAL B1071      -9.352  22.426 -15.014  1.00 80.09           N  
ANISOU 5452  N   VAL B1071     9859  11539   9035   1134    125    464       N  
ATOM   5453  CA  VAL B1071     -10.475  21.507 -14.787  1.00 79.17           C  
ANISOU 5453  CA  VAL B1071     9778  11539   8763   1199    278    693       C  
ATOM   5454  C   VAL B1071     -11.228  21.903 -13.525  1.00 85.52           C  
ANISOU 5454  C   VAL B1071    10734  12463   9296   1405    317    687       C  
ATOM   5455  O   VAL B1071     -12.450  22.041 -13.576  1.00 85.18           O  
ANISOU 5455  O   VAL B1071    10699  12471   9195   1451    498    821       O  
ATOM   5456  CB  VAL B1071     -10.066  20.007 -14.782  1.00 82.39           C  
ANISOU 5456  CB  VAL B1071    10148  11978   9177   1174    267    837       C  
ATOM   5457  CG1 VAL B1071     -11.249  19.105 -14.430  1.00 82.33           C  
ANISOU 5457  CG1 VAL B1071    10185  12070   9027   1228    433   1072       C  
ATOM   5458  CG2 VAL B1071      -9.483  19.592 -16.122  1.00 80.49           C  
ANISOU 5458  CG2 VAL B1071     9787  11608   9189    984    287    851       C  
ATOM   5459  N   ASP B1072     -10.502  22.092 -12.400  1.00 84.64           N  
ANISOU 5459  N   ASP B1072    10741  12404   9014   1535    148    535       N  
ATOM   5460  CA  ASP B1072     -11.084  22.475 -11.109  1.00 87.15           C  
ANISOU 5460  CA  ASP B1072    11258  12837   9018   1756    179    499       C  
ATOM   5461  C   ASP B1072     -11.857  23.797 -11.164  1.00 91.98           C  
ANISOU 5461  C   ASP B1072    11944  13384   9621   1808    299    394       C  
ATOM   5462  O   ASP B1072     -12.917  23.898 -10.545  1.00 92.89           O  
ANISOU 5462  O   ASP B1072    12165  13590   9540   1976    482    495       O  
ATOM   5463  CB  ASP B1072     -10.035  22.458  -9.982  1.00 91.57           C  
ANISOU 5463  CB  ASP B1072    11945  13468   9381   1868    -78    326       C  
ATOM   5464  CG  ASP B1072      -9.650  21.059  -9.524  1.00104.27           C  
ANISOU 5464  CG  ASP B1072    13542  15192  10885   1933   -133    509       C  
ATOM   5465  OD1 ASP B1072     -10.540  20.328  -9.024  1.00105.66           O  
ANISOU 5465  OD1 ASP B1072    13801  15472  10871   2057     52    734       O  
ATOM   5466  OD2 ASP B1072      -8.454  20.708  -9.624  1.00110.93           O  
ANISOU 5466  OD2 ASP B1072    14290  16016  11843   1873   -349    440       O  
ATOM   5467  N   ALA B1073     -11.363  24.779 -11.950  1.00 87.78           N  
ANISOU 5467  N   ALA B1073    11348  12683   9323   1674    231    222       N  
ATOM   5468  CA  ALA B1073     -12.027  26.070 -12.143  1.00 88.04           C  
ANISOU 5468  CA  ALA B1073    11446  12607   9396   1721    356    134       C  
ATOM   5469  C   ALA B1073     -13.285  25.902 -13.004  1.00 90.12           C  
ANISOU 5469  C   ALA B1073    11583  12900   9760   1704    600    397       C  
ATOM   5470  O   ALA B1073     -14.253  26.645 -12.824  1.00 90.51           O  
ANISOU 5470  O   ALA B1073    11693  12945   9753   1842    770    430       O  
ATOM   5471  CB  ALA B1073     -11.077  27.057 -12.794  1.00 88.72           C  
ANISOU 5471  CB  ALA B1073    11489  12485   9734   1564    224    -89       C  
ATOM   5472  N   ALA B1074     -13.267  24.924 -13.938  1.00 84.71           N  
ANISOU 5472  N   ALA B1074    10720  12242   9225   1540    611    579       N  
ATOM   5473  CA  ALA B1074     -14.409  24.621 -14.804  1.00 83.44           C  
ANISOU 5473  CA  ALA B1074    10419  12129   9156   1485    786    824       C  
ATOM   5474  C   ALA B1074     -15.513  23.929 -14.001  1.00 88.52           C  
ANISOU 5474  C   ALA B1074    11075  12947   9612   1628    944   1028       C  
ATOM   5475  O   ALA B1074     -16.689  24.227 -14.218  1.00 88.73           O  
ANISOU 5475  O   ALA B1074    11023  13030   9662   1687   1115   1184       O  
ATOM   5476  CB  ALA B1074     -13.977  23.757 -15.974  1.00 82.15           C  
ANISOU 5476  CB  ALA B1074    10110  11929   9174   1260    731    913       C  
ATOM   5477  N   VAL B1075     -15.127  23.033 -13.055  1.00 85.71           N  
ANISOU 5477  N   VAL B1075    10809  12680   9079   1695    895   1044       N  
ATOM   5478  CA  VAL B1075     -16.038  22.321 -12.143  1.00 86.92           C  
ANISOU 5478  CA  VAL B1075    11002  12988   9034   1844   1063   1246       C  
ATOM   5479  C   VAL B1075     -16.645  23.348 -11.167  1.00 93.65           C  
ANISOU 5479  C   VAL B1075    12016  13885   9683   2099   1192   1172       C  
ATOM   5480  O   VAL B1075     -17.834  23.265 -10.860  1.00 94.32           O  
ANISOU 5480  O   VAL B1075    12059  14073   9706   2218   1427   1371       O  
ATOM   5481  CB  VAL B1075     -15.351  21.119 -11.434  1.00 90.87           C  
ANISOU 5481  CB  VAL B1075    11580  13549   9396   1863    976   1294       C  
ATOM   5482  CG1 VAL B1075     -16.254  20.494 -10.373  1.00 92.49           C  
ANISOU 5482  CG1 VAL B1075    11865  13904   9374   2044   1178   1509       C  
ATOM   5483  CG2 VAL B1075     -14.927  20.060 -12.450  1.00 88.62           C  
ANISOU 5483  CG2 VAL B1075    11146  13197   9331   1630    911   1391       C  
ATOM   5484  N   ARG B1076     -15.839  24.355 -10.750  1.00 91.54           N  
ANISOU 5484  N   ARG B1076    11921  13523   9336   2170   1049    879       N  
ATOM   5485  CA  ARG B1076     -16.268  25.478  -9.909  1.00 93.86           C  
ANISOU 5485  CA  ARG B1076    12418  13801   9443   2402   1155    738       C  
ATOM   5486  C   ARG B1076     -17.299  26.327 -10.670  1.00 97.54           C  
ANISOU 5486  C   ARG B1076    12762  14203  10097   2425   1357    834       C  
ATOM   5487  O   ARG B1076     -18.157  26.943 -10.049  1.00 99.28           O  
ANISOU 5487  O   ARG B1076    13085  14453  10185   2652   1568    860       O  
ATOM   5488  CB  ARG B1076     -15.066  26.345  -9.490  1.00 95.31           C  
ANISOU 5488  CB  ARG B1076    12795  13856   9563   2400    910    374       C  
ATOM   5489  CG  ARG B1076     -14.354  25.867  -8.228  1.00109.80           C  
ANISOU 5489  CG  ARG B1076    14841  15802  11076   2517    744    255       C  
ATOM   5490  CD  ARG B1076     -14.624  26.791  -7.053  1.00126.74           C  
ANISOU 5490  CD  ARG B1076    17303  17950  12902   2767    803     52       C  
ATOM   5491  NE  ARG B1076     -14.014  26.290  -5.817  1.00138.55           N  
ANISOU 5491  NE  ARG B1076    19024  19586  14031   2899    633    -41       N  
ATOM   5492  CZ  ARG B1076     -14.191  26.824  -4.610  1.00154.46           C  
ANISOU 5492  CZ  ARG B1076    21371  21653  15664   3140    665   -207       C  
ATOM   5493  NH1 ARG B1076     -14.969  27.889  -4.452  1.00142.45           N  
ANISOU 5493  NH1 ARG B1076    19999  20031  14094   3287    888   -306       N  
ATOM   5494  NH2 ARG B1076     -13.595  26.293  -3.551  1.00141.78           N  
ANISOU 5494  NH2 ARG B1076    19965  20198  13706   3255    479   -270       N  
ATOM   5495  N   GLY B1077     -17.214  26.328 -12.002  1.00 91.91           N  
ANISOU 5495  N   GLY B1077    11835  13409   9676   2209   1299    901       N  
ATOM   5496  CA  GLY B1077     -18.150  27.024 -12.875  1.00 91.57           C  
ANISOU 5496  CA  GLY B1077    11644  13325   9824   2217   1451   1033       C  
ATOM   5497  C   GLY B1077     -19.467  26.279 -12.964  1.00 96.11           C  
ANISOU 5497  C   GLY B1077    12022  14083  10411   2255   1650   1365       C  
ATOM   5498  O   GLY B1077     -20.530  26.868 -12.747  1.00 97.36           O  
ANISOU 5498  O   GLY B1077    12141  14288  10562   2443   1867   1485       O  
ATOM   5499  N   ILE B1078     -19.389  24.961 -13.261  1.00 91.75           N  
ANISOU 5499  N   ILE B1078    11340  13625   9896   2075   1586   1515       N  
ATOM   5500  CA  ILE B1078     -20.516  24.024 -13.368  1.00 92.17           C  
ANISOU 5500  CA  ILE B1078    11187  13839   9996   2038   1739   1826       C  
ATOM   5501  C   ILE B1078     -21.311  23.970 -12.048  1.00 99.10           C  
ANISOU 5501  C   ILE B1078    12148  14843  10660   2304   1984   1940       C  
ATOM   5502  O   ILE B1078     -22.538  24.083 -12.073  1.00100.20           O  
ANISOU 5502  O   ILE B1078    12114  15087  10872   2394   2198   2166       O  
ATOM   5503  CB  ILE B1078     -20.017  22.611 -13.815  1.00 93.74           C  
ANISOU 5503  CB  ILE B1078    11309  14049  10258   1787   1607   1899       C  
ATOM   5504  CG1 ILE B1078     -19.471  22.629 -15.267  1.00 92.03           C  
ANISOU 5504  CG1 ILE B1078    10988  13723  10255   1533   1425   1833       C  
ATOM   5505  CG2 ILE B1078     -21.108  21.548 -13.647  1.00 95.43           C  
ANISOU 5505  CG2 ILE B1078    11352  14406  10503   1744   1772   2200       C  
ATOM   5506  CD1 ILE B1078     -18.532  21.442 -15.646  1.00 98.44           C  
ANISOU 5506  CD1 ILE B1078    11820  14477  11105   1323   1276   1796       C  
ATOM   5507  N   LEU B1079     -20.608  23.814 -10.903  1.00 96.82           N  
ANISOU 5507  N   LEU B1079    12123  14557  10106   2439   1953   1794       N  
ATOM   5508  CA  LEU B1079     -21.221  23.732  -9.572  1.00 99.47           C  
ANISOU 5508  CA  LEU B1079    12606  15013  10173   2713   2190   1885       C  
ATOM   5509  C   LEU B1079     -21.791  25.054  -9.038  1.00106.60           C  
ANISOU 5509  C   LEU B1079    13644  15890  10968   2996   2381   1791       C  
ATOM   5510  O   LEU B1079     -22.366  25.076  -7.946  1.00109.31           O  
ANISOU 5510  O   LEU B1079    14130  16331  11071   3253   2621   1865       O  
ATOM   5511  CB  LEU B1079     -20.297  23.043  -8.552  1.00100.05           C  
ANISOU 5511  CB  LEU B1079    12931  15119   9963   2772   2076   1786       C  
ATOM   5512  CG  LEU B1079     -19.937  21.573  -8.815  1.00103.11           C  
ANISOU 5512  CG  LEU B1079    13210  15540  10427   2568   1983   1950       C  
ATOM   5513  CD1 LEU B1079     -18.986  21.065  -7.763  1.00104.56           C  
ANISOU 5513  CD1 LEU B1079    13655  15758  10317   2681   1858   1852       C  
ATOM   5514  CD2 LEU B1079     -21.173  20.675  -8.868  1.00106.07           C  
ANISOU 5514  CD2 LEU B1079    13370  16024  10906   2531   2246   2315       C  
ATOM   5515  N   ARG B1080     -21.659  26.137  -9.824  1.00102.76           N  
ANISOU 5515  N   ARG B1080    13123  15261  10661   2959   2304   1644       N  
ATOM   5516  CA  ARG B1080     -22.196  27.469  -9.540  1.00105.10           C  
ANISOU 5516  CA  ARG B1080    13532  15477  10924   3211   2488   1554       C  
ATOM   5517  C   ARG B1080     -23.160  27.880 -10.673  1.00109.10           C  
ANISOU 5517  C   ARG B1080    13719  15985  11749   3168   2595   1775       C  
ATOM   5518  O   ARG B1080     -23.464  29.065 -10.843  1.00110.04           O  
ANISOU 5518  O   ARG B1080    13885  15985  11939   3326   2696   1705       O  
ATOM   5519  CB  ARG B1080     -21.053  28.490  -9.365  1.00105.66           C  
ANISOU 5519  CB  ARG B1080    13896  15334  10916   3221   2287   1156       C  
ATOM   5520  CG  ARG B1080     -20.630  28.745  -7.914  1.00119.20           C  
ANISOU 5520  CG  ARG B1080    15996  17050  12246   3445   2305    920       C  
ATOM   5521  CD  ARG B1080     -19.736  27.653  -7.347  1.00127.87           C  
ANISOU 5521  CD  ARG B1080    17186  18255  13144   3342   2088    874       C  
ATOM   5522  NE  ARG B1080     -18.885  28.141  -6.260  1.00137.66           N  
ANISOU 5522  NE  ARG B1080    18804  19444  14057   3471   1940    539       N  
ATOM   5523  CZ  ARG B1080     -19.214  28.103  -4.972  1.00157.47           C  
ANISOU 5523  CZ  ARG B1080    21593  22064  16176   3746   2096    517       C  
ATOM   5524  NH1 ARG B1080     -20.388  27.611  -4.593  1.00146.86           N  
ANISOU 5524  NH1 ARG B1080    20177  20878  14745   3930   2445    833       N  
ATOM   5525  NH2 ARG B1080     -18.373  28.559  -4.055  1.00149.58           N  
ANISOU 5525  NH2 ARG B1080    20946  21020  14866   3836   1903    183       N  
ATOM   5526  N   ASN B1081     -23.643  26.874 -11.438  1.00104.63           N  
ANISOU 5526  N   ASN B1081    12834  15551  11370   2955   2562   2045       N  
ATOM   5527  CA  ASN B1081     -24.568  27.014 -12.564  1.00104.30           C  
ANISOU 5527  CA  ASN B1081    12449  15564  11615   2870   2601   2287       C  
ATOM   5528  C   ASN B1081     -25.789  26.116 -12.300  1.00109.92           C  
ANISOU 5528  C   ASN B1081    12887  16498  12380   2890   2812   2637       C  
ATOM   5529  O   ASN B1081     -25.635  24.905 -12.143  1.00108.55           O  
ANISOU 5529  O   ASN B1081    12668  16402  12174   2716   2758   2723       O  
ATOM   5530  CB  ASN B1081     -23.859  26.633 -13.876  1.00102.54           C  
ANISOU 5530  CB  ASN B1081    12112  15274  11573   2532   2300   2238       C  
ATOM   5531  CG  ASN B1081     -24.659  26.903 -15.122  1.00129.15           C  
ANISOU 5531  CG  ASN B1081    15181  18694  15196   2441   2278   2443       C  
ATOM   5532  OD1 ASN B1081     -25.582  26.159 -15.473  1.00124.51           O  
ANISOU 5532  OD1 ASN B1081    14304  18278  14726   2341   2318   2712       O  
ATOM   5533  ND2 ASN B1081     -24.300  27.960 -15.833  1.00121.67           N  
ANISOU 5533  ND2 ASN B1081    14294  17596  14341   2462   2198   2326       N  
ATOM   5534  N   ALA B1082     -26.992  26.722 -12.229  1.00109.22           N  
ANISOU 5534  N   ALA B1082    12611  16495  12392   3109   3069   2846       N  
ATOM   5535  CA  ALA B1082     -28.276  26.058 -11.945  1.00111.14           C  
ANISOU 5535  CA  ALA B1082    12543  16950  12733   3160   3317   3204       C  
ATOM   5536  C   ALA B1082     -28.689  24.950 -12.931  1.00113.06           C  
ANISOU 5536  C   ALA B1082    12419  17316  13224   2804   3150   3431       C  
ATOM   5537  O   ALA B1082     -29.375  24.008 -12.529  1.00113.87           O  
ANISOU 5537  O   ALA B1082    12333  17559  13374   2747   3300   3670       O  
ATOM   5538  CB  ALA B1082     -29.381  27.099 -11.840  1.00114.89           C  
ANISOU 5538  CB  ALA B1082    12864  17474  13313   3476   3599   3368       C  
ATOM   5539  N   LYS B1083     -28.298  25.077 -14.212  1.00106.92           N  
ANISOU 5539  N   LYS B1083    11549  16474  12599   2565   2855   3357       N  
ATOM   5540  CA  LYS B1083     -28.647  24.122 -15.269  1.00105.44           C  
ANISOU 5540  CA  LYS B1083    11056  16383  12622   2215   2657   3523       C  
ATOM   5541  C   LYS B1083     -27.692  22.934 -15.352  1.00105.28           C  
ANISOU 5541  C   LYS B1083    11191  16287  12525   1925   2466   3390       C  
ATOM   5542  O   LYS B1083     -28.123  21.834 -15.701  1.00105.16           O  
ANISOU 5542  O   LYS B1083    10966  16351  12638   1672   2414   3554       O  
ATOM   5543  CB  LYS B1083     -28.731  24.831 -16.634  1.00107.22           C  
ANISOU 5543  CB  LYS B1083    11137  16591  13010   2123   2444   3522       C  
ATOM   5544  CG  LYS B1083     -29.915  25.784 -16.762  1.00125.54           C  
ANISOU 5544  CG  LYS B1083    13192  19028  15482   2375   2615   3752       C  
ATOM   5545  CD  LYS B1083     -29.742  26.764 -17.918  1.00135.63           C  
ANISOU 5545  CD  LYS B1083    14455  20232  16846   2381   2431   3705       C  
ATOM   5546  CE  LYS B1083     -30.804  27.839 -17.907  1.00150.53           C  
ANISOU 5546  CE  LYS B1083    16131  22198  18867   2705   2630   3923       C  
ATOM   5547  NZ  LYS B1083     -30.575  28.862 -18.965  1.00158.37           N  
ANISOU 5547  NZ  LYS B1083    17157  23090  19926   2750   2476   3889       N  
ATOM   5548  N   LEU B1084     -26.405  23.156 -15.035  1.00 98.55           N  
ANISOU 5548  N   LEU B1084    10693  15270  11484   1960   2363   3097       N  
ATOM   5549  CA  LEU B1084     -25.355  22.139 -15.130  1.00 95.81           C  
ANISOU 5549  CA  LEU B1084    10505  14830  11068   1728   2180   2957       C  
ATOM   5550  C   LEU B1084     -25.040  21.372 -13.843  1.00100.19           C  
ANISOU 5550  C   LEU B1084    11247  15394  11426   1825   2313   2960       C  
ATOM   5551  O   LEU B1084     -24.645  20.209 -13.933  1.00 98.97           O  
ANISOU 5551  O   LEU B1084    11108  15209  11286   1619   2228   2986       O  
ATOM   5552  CB  LEU B1084     -24.077  22.724 -15.762  1.00 93.24           C  
ANISOU 5552  CB  LEU B1084    10390  14329  10707   1661   1947   2664       C  
ATOM   5553  CG  LEU B1084     -24.229  23.368 -17.152  1.00 96.86           C  
ANISOU 5553  CG  LEU B1084    10706  14761  11336   1541   1800   2668       C  
ATOM   5554  CD1 LEU B1084     -23.132  24.368 -17.405  1.00 95.35           C  
ANISOU 5554  CD1 LEU B1084    10742  14388  11098   1600   1692   2403       C  
ATOM   5555  CD2 LEU B1084     -24.270  22.321 -18.264  1.00 98.13           C  
ANISOU 5555  CD2 LEU B1084    10715  14949  11622   1202   1619   2746       C  
ATOM   5556  N   LYS B1085     -25.214  22.002 -12.656  1.00 98.30           N  
ANISOU 5556  N   LYS B1085    11171  15188  10990   2148   2529   2938       N  
ATOM   5557  CA  LYS B1085     -24.974  21.380 -11.340  1.00 98.99           C  
ANISOU 5557  CA  LYS B1085    11472  15309  10831   2295   2674   2959       C  
ATOM   5558  C   LYS B1085     -25.774  20.065 -11.108  1.00103.56           C  
ANISOU 5558  C   LYS B1085    11851  15994  11503   2172   2840   3277       C  
ATOM   5559  O   LYS B1085     -25.137  19.091 -10.697  1.00102.85           O  
ANISOU 5559  O   LYS B1085    11909  15860  11308   2093   2791   3271       O  
ATOM   5560  CB  LYS B1085     -25.170  22.393 -10.190  1.00103.58           C  
ANISOU 5560  CB  LYS B1085    12275  15917  11164   2677   2895   2879       C  
ATOM   5561  CG  LYS B1085     -24.769  21.884  -8.809  1.00118.01           C  
ANISOU 5561  CG  LYS B1085    14396  17782  12658   2861   3009   2858       C  
ATOM   5562  CD  LYS B1085     -25.086  22.898  -7.713  1.00129.42           C  
ANISOU 5562  CD  LYS B1085    16081  19259  13834   3245   3249   2775       C  
ATOM   5563  CE  LYS B1085     -25.153  22.273  -6.337  1.00141.16           C  
ANISOU 5563  CE  LYS B1085    17798  20847  14988   3456   3462   2879       C  
ATOM   5564  NZ  LYS B1085     -23.821  21.828  -5.841  1.00146.69           N  
ANISOU 5564  NZ  LYS B1085    18808  21496  15433   3421   3197   2661       N  
ATOM   5565  N   PRO B1086     -27.113  19.966 -11.381  1.00101.27           N  
ANISOU 5565  N   PRO B1086    11216  15831  11432   2139   3025   3565       N  
ATOM   5566  CA  PRO B1086     -27.812  18.682 -11.160  1.00102.59           C  
ANISOU 5566  CA  PRO B1086    11187  16068  11723   1980   3178   3860       C  
ATOM   5567  C   PRO B1086     -27.375  17.575 -12.118  1.00104.05           C  
ANISOU 5567  C   PRO B1086    11293  16155  12087   1582   2923   3841       C  
ATOM   5568  O   PRO B1086     -27.452  16.393 -11.774  1.00104.75           O  
ANISOU 5568  O   PRO B1086    11375  16217  12208   1450   3008   3995       O  
ATOM   5569  CB  PRO B1086     -29.291  19.030 -11.377  1.00106.97           C  
ANISOU 5569  CB  PRO B1086    11345  16781  12516   2022   3388   4141       C  
ATOM   5570  CG  PRO B1086     -29.368  20.507 -11.376  1.00111.60           C  
ANISOU 5570  CG  PRO B1086    11992  17383  13028   2305   3424   4010       C  
ATOM   5571  CD  PRO B1086     -28.056  20.984 -11.886  1.00103.81           C  
ANISOU 5571  CD  PRO B1086    11289  16233  11921   2243   3107   3655       C  
ATOM   5572  N   VAL B1087     -26.918  17.966 -13.317  1.00 97.50           N  
ANISOU 5572  N   VAL B1087    10426  15255  11366   1403   2632   3656       N  
ATOM   5573  CA  VAL B1087     -26.456  17.056 -14.362  1.00 95.24           C  
ANISOU 5573  CA  VAL B1087    10101  14861  11225   1041   2383   3593       C  
ATOM   5574  C   VAL B1087     -25.085  16.466 -13.986  1.00 97.57           C  
ANISOU 5574  C   VAL B1087    10732  14999  11342   1036   2280   3402       C  
ATOM   5575  O   VAL B1087     -24.911  15.253 -14.081  1.00 97.51           O  
ANISOU 5575  O   VAL B1087    10738  14906  11405    833   2262   3472       O  
ATOM   5576  CB  VAL B1087     -26.466  17.727 -15.766  1.00 97.22           C  
ANISOU 5576  CB  VAL B1087    10218  15106  11615    886   2135   3480       C  
ATOM   5577  CG1 VAL B1087     -26.168  16.712 -16.868  1.00 95.95           C  
ANISOU 5577  CG1 VAL B1087    10018  14849  11592    507   1909   3433       C  
ATOM   5578  CG2 VAL B1087     -27.799  18.420 -16.038  1.00 99.06           C  
ANISOU 5578  CG2 VAL B1087    10113  15517  12010    955   2231   3688       C  
ATOM   5579  N   TYR B1088     -24.134  17.317 -13.538  1.00 92.71           N  
ANISOU 5579  N   TYR B1088    10374  14339  10512   1261   2216   3170       N  
ATOM   5580  CA  TYR B1088     -22.775  16.930 -13.140  1.00 91.19           C  
ANISOU 5580  CA  TYR B1088    10469  14025  10152   1294   2090   2982       C  
ATOM   5581  C   TYR B1088     -22.760  16.011 -11.913  1.00 96.41           C  
ANISOU 5581  C   TYR B1088    11268  14710  10655   1418   2268   3137       C  
ATOM   5582  O   TYR B1088     -22.019  15.025 -11.903  1.00 95.59           O  
ANISOU 5582  O   TYR B1088    11276  14500  10545   1313   2186   3126       O  
ATOM   5583  CB  TYR B1088     -21.915  18.181 -12.897  1.00 91.83           C  
ANISOU 5583  CB  TYR B1088    10749  14075  10067   1498   1978   2708       C  
ATOM   5584  CG  TYR B1088     -20.477  17.901 -12.510  1.00 93.43           C  
ANISOU 5584  CG  TYR B1088    11201  14177  10122   1533   1810   2506       C  
ATOM   5585  CD1 TYR B1088     -19.533  17.545 -13.470  1.00 93.28           C  
ANISOU 5585  CD1 TYR B1088    11184  14025  10232   1321   1597   2367       C  
ATOM   5586  CD2 TYR B1088     -20.050  18.033 -11.192  1.00 96.04           C  
ANISOU 5586  CD2 TYR B1088    11762  14554  10174   1791   1861   2454       C  
ATOM   5587  CE1 TYR B1088     -18.204  17.299 -13.121  1.00 93.57           C  
ANISOU 5587  CE1 TYR B1088    11402  13981  10168   1365   1446   2202       C  
ATOM   5588  CE2 TYR B1088     -18.727  17.780 -10.830  1.00 96.56           C  
ANISOU 5588  CE2 TYR B1088    12021  14554  10115   1826   1671   2282       C  
ATOM   5589  CZ  TYR B1088     -17.808  17.411 -11.798  1.00102.26           C  
ANISOU 5589  CZ  TYR B1088    12697  15147  11012   1613   1466   2165       C  
ATOM   5590  OH  TYR B1088     -16.502  17.164 -11.452  1.00103.75           O  
ANISOU 5590  OH  TYR B1088    13029  15281  11111   1659   1283   2017       O  
ATOM   5591  N   ASP B1089     -23.571  16.339 -10.885  1.00 94.79           N  
ANISOU 5591  N   ASP B1089    11063  14637  10314   1662   2529   3296       N  
ATOM   5592  CA  ASP B1089     -23.682  15.560  -9.651  1.00 96.52           C  
ANISOU 5592  CA  ASP B1089    11426  14899  10347   1821   2746   3484       C  
ATOM   5593  C   ASP B1089     -24.211  14.152  -9.917  1.00 99.59           C  
ANISOU 5593  C   ASP B1089    11649  15234  10956   1567   2849   3750       C  
ATOM   5594  O   ASP B1089     -23.741  13.199  -9.297  1.00100.29           O  
ANISOU 5594  O   ASP B1089    11908  15259  10940   1594   2901   3840       O  
ATOM   5595  CB  ASP B1089     -24.567  16.288  -8.623  1.00101.49           C  
ANISOU 5595  CB  ASP B1089    12077  15684  10799   2136   3047   3608       C  
ATOM   5596  CG  ASP B1089     -23.930  17.513  -7.987  1.00113.54           C  
ANISOU 5596  CG  ASP B1089    13881  17233  12024   2431   2981   3335       C  
ATOM   5597  OD1 ASP B1089     -22.764  17.415  -7.535  1.00114.03           O  
ANISOU 5597  OD1 ASP B1089    14220  17241  11864   2503   2796   3142       O  
ATOM   5598  OD2 ASP B1089     -24.625  18.547  -7.866  1.00120.08           O  
ANISOU 5598  OD2 ASP B1089    14655  18132  12837   2605   3128   3324       O  
ATOM   5599  N   SER B1090     -25.158  14.024 -10.863  1.00 94.79           N  
ANISOU 5599  N   SER B1090    10715  14642  10657   1314   2860   3870       N  
ATOM   5600  CA  SER B1090     -25.781  12.754 -11.249  1.00 95.35           C  
ANISOU 5600  CA  SER B1090    10593  14645  10990   1014   2936   4100       C  
ATOM   5601  C   SER B1090     -24.875  11.851 -12.096  1.00 96.23           C  
ANISOU 5601  C   SER B1090    10803  14550  11208    736   2694   3957       C  
ATOM   5602  O   SER B1090     -25.089  10.638 -12.135  1.00 97.14           O  
ANISOU 5602  O   SER B1090    10886  14549  11475    533   2774   4120       O  
ATOM   5603  CB  SER B1090     -27.083  13.013 -11.999  1.00 99.41           C  
ANISOU 5603  CB  SER B1090    10710  15267  11794    832   2977   4249       C  
ATOM   5604  OG  SER B1090     -26.817  13.576 -13.271  1.00103.14           O  
ANISOU 5604  OG  SER B1090    11100  15714  12373    662   2678   4033       O  
ATOM   5605  N   LEU B1091     -23.901  12.442 -12.801  1.00 89.31           N  
ANISOU 5605  N   LEU B1091    10044  13615  10276    722   2423   3662       N  
ATOM   5606  CA  LEU B1091     -22.994  11.709 -13.683  1.00 87.01           C  
ANISOU 5606  CA  LEU B1091     9851  13129  10078    489   2212   3506       C  
ATOM   5607  C   LEU B1091     -21.800  11.078 -12.965  1.00 90.11           C  
ANISOU 5607  C   LEU B1091    10533  13403  10300    634   2200   3454       C  
ATOM   5608  O   LEU B1091     -21.344  11.587 -11.939  1.00 89.73           O  
ANISOU 5608  O   LEU B1091    10651  13442  10001    936   2241   3423       O  
ATOM   5609  CB  LEU B1091     -22.516  12.587 -14.862  1.00 84.23           C  
ANISOU 5609  CB  LEU B1091     9471  12764   9770    397   1957   3245       C  
ATOM   5610  CG  LEU B1091     -23.548  12.953 -15.932  1.00 88.91           C  
ANISOU 5610  CG  LEU B1091     9784  13438  10561    181   1890   3290       C  
ATOM   5611  CD1 LEU B1091     -23.085  14.143 -16.736  1.00 87.05           C  
ANISOU 5611  CD1 LEU B1091     9563  13228  10284    226   1700   3069       C  
ATOM   5612  CD2 LEU B1091     -23.859  11.777 -16.848  1.00 91.49           C  
ANISOU 5612  CD2 LEU B1091    10021  13639  11101   -191   1816   3339       C  
ATOM   5613  N   ASP B1092     -21.294   9.969 -13.538  1.00 85.95           N  
ANISOU 5613  N   ASP B1092    10072  12675   9911    421   2134   3439       N  
ATOM   5614  CA  ASP B1092     -20.136   9.203 -13.077  1.00 85.36           C  
ANISOU 5614  CA  ASP B1092    10238  12455   9737    527   2108   3410       C  
ATOM   5615  C   ASP B1092     -18.830   9.861 -13.540  1.00 85.59           C  
ANISOU 5615  C   ASP B1092    10379  12452   9687    605   1864   3114       C  
ATOM   5616  O   ASP B1092     -18.860  10.703 -14.436  1.00 82.90           O  
ANISOU 5616  O   ASP B1092     9940  12148   9411    505   1729   2940       O  
ATOM   5617  CB  ASP B1092     -20.216   7.761 -13.607  1.00 88.43           C  
ANISOU 5617  CB  ASP B1092    10642  12608  10348    258   2166   3516       C  
ATOM   5618  CG  ASP B1092     -20.398   7.675 -15.110  1.00 98.49           C  
ANISOU 5618  CG  ASP B1092    11804  13778  11841    -81   2013   3359       C  
ATOM   5619  OD1 ASP B1092     -21.556   7.588 -15.558  1.00100.51           O  
ANISOU 5619  OD1 ASP B1092    11853  14077  12259   -308   2057   3460       O  
ATOM   5620  OD2 ASP B1092     -19.381   7.737 -15.839  1.00102.17           O  
ANISOU 5620  OD2 ASP B1092    12381  14133  12305   -112   1846   3136       O  
ATOM   5621  N   ALA B1093     -17.688   9.434 -12.955  1.00 81.80           N  
ANISOU 5621  N   ALA B1093    10092  11901   9089    778   1814   3080       N  
ATOM   5622  CA  ALA B1093     -16.330   9.926 -13.227  1.00 79.36           C  
ANISOU 5622  CA  ALA B1093     9869  11559   8727    869   1597   2833       C  
ATOM   5623  C   ALA B1093     -15.974  10.108 -14.718  1.00 80.66           C  
ANISOU 5623  C   ALA B1093     9956  11602   9089    628   1462   2633       C  
ATOM   5624  O   ALA B1093     -15.449  11.162 -15.086  1.00 78.49           O  
ANISOU 5624  O   ALA B1093     9654  11384   8785    669   1318   2430       O  
ATOM   5625  CB  ALA B1093     -15.309   9.029 -12.544  1.00 81.10           C  
ANISOU 5625  CB  ALA B1093    10256  11687   8873   1033   1585   2900       C  
ATOM   5626  N   VAL B1094     -16.267   9.090 -15.563  1.00 77.11           N  
ANISOU 5626  N   VAL B1094     9493  10976   8830    375   1519   2688       N  
ATOM   5627  CA  VAL B1094     -15.976   9.088 -17.005  1.00 75.02           C  
ANISOU 5627  CA  VAL B1094     9203  10584   8716    142   1416   2510       C  
ATOM   5628  C   VAL B1094     -16.890  10.082 -17.724  1.00 78.37           C  
ANISOU 5628  C   VAL B1094     9465  11146   9165      9   1357   2454       C  
ATOM   5629  O   VAL B1094     -16.401  10.921 -18.483  1.00 76.57           O  
ANISOU 5629  O   VAL B1094     9223  10934   8938     -7   1232   2271       O  
ATOM   5630  CB  VAL B1094     -16.044   7.658 -17.626  1.00 79.78           C  
ANISOU 5630  CB  VAL B1094     9887  10940   9486    -83   1498   2569       C  
ATOM   5631  CG1 VAL B1094     -15.734   7.673 -19.119  1.00 78.31           C  
ANISOU 5631  CG1 VAL B1094     9722  10629   9404   -306   1399   2367       C  
ATOM   5632  CG2 VAL B1094     -15.103   6.696 -16.907  1.00 80.76           C  
ANISOU 5632  CG2 VAL B1094    10174  10913   9597     90   1572   2651       C  
ATOM   5633  N   ARG B1095     -18.206  10.001 -17.457  1.00 76.21           N  
ANISOU 5633  N   ARG B1095     9058  10974   8924    -71   1457   2633       N  
ATOM   5634  CA  ARG B1095     -19.233  10.866 -18.046  1.00 75.57           C  
ANISOU 5634  CA  ARG B1095     8783  11045   8884   -175   1413   2638       C  
ATOM   5635  C   ARG B1095     -19.140  12.327 -17.585  1.00 77.55           C  
ANISOU 5635  C   ARG B1095     8999  11470   8998     71   1378   2564       C  
ATOM   5636  O   ARG B1095     -19.593  13.216 -18.307  1.00 75.82           O  
ANISOU 5636  O   ARG B1095     8660  11336   8812     17   1302   2509       O  
ATOM   5637  CB  ARG B1095     -20.625  10.289 -17.788  1.00 78.71           C  
ANISOU 5637  CB  ARG B1095     9013  11504   9391   -315   1547   2878       C  
ATOM   5638  CG  ARG B1095     -20.934   9.062 -18.629  1.00 90.47           C  
ANISOU 5638  CG  ARG B1095    10500  12812  11062   -653   1529   2901       C  
ATOM   5639  CD  ARG B1095     -22.380   8.667 -18.458  1.00101.24           C  
ANISOU 5639  CD  ARG B1095    11632  14257  12575   -827   1634   3132       C  
ATOM   5640  NE  ARG B1095     -22.771   7.583 -19.358  1.00108.52           N  
ANISOU 5640  NE  ARG B1095    12539  15006  13688  -1200   1577   3122       N  
ATOM   5641  CZ  ARG B1095     -22.701   6.291 -19.060  1.00121.45           C  
ANISOU 5641  CZ  ARG B1095    14290  16421  15435  -1325   1702   3213       C  
ATOM   5642  NH1 ARG B1095     -22.228   5.898 -17.882  1.00108.89           N  
ANISOU 5642  NH1 ARG B1095    12833  14771  13768  -1085   1892   3346       N  
ATOM   5643  NH2 ARG B1095     -23.085   5.381 -19.942  1.00107.10           N  
ANISOU 5643  NH2 ARG B1095    12472  14427  13793  -1688   1633   3167       N  
ATOM   5644  N   ARG B1096     -18.553  12.568 -16.388  1.00 74.65           N  
ANISOU 5644  N   ARG B1096     8751  11146   8468    344   1427   2562       N  
ATOM   5645  CA  ARG B1096     -18.320  13.901 -15.819  1.00 73.81           C  
ANISOU 5645  CA  ARG B1096     8669  11164   8213    584   1391   2453       C  
ATOM   5646  C   ARG B1096     -17.236  14.601 -16.644  1.00 75.80           C  
ANISOU 5646  C   ARG B1096     8970  11332   8498    554   1210   2204       C  
ATOM   5647  O   ARG B1096     -17.394  15.772 -16.991  1.00 74.24           O  
ANISOU 5647  O   ARG B1096     8718  11192   8299    593   1161   2109       O  
ATOM   5648  CB  ARG B1096     -17.902  13.807 -14.337  1.00 73.94           C  
ANISOU 5648  CB  ARG B1096     8838  11237   8018    859   1459   2497       C  
ATOM   5649  CG  ARG B1096     -19.071  13.873 -13.356  1.00 82.48           C  
ANISOU 5649  CG  ARG B1096     9874  12467   8998    998   1673   2712       C  
ATOM   5650  CD  ARG B1096     -18.627  13.622 -11.926  1.00 90.00           C  
ANISOU 5650  CD  ARG B1096    11025  13474   9699   1268   1744   2770       C  
ATOM   5651  NE  ARG B1096     -19.389  14.427 -10.966  1.00 97.06           N  
ANISOU 5651  NE  ARG B1096    11942  14534  10403   1504   1901   2836       N  
ATOM   5652  CZ  ARG B1096     -19.662  14.060  -9.717  1.00113.10           C  
ANISOU 5652  CZ  ARG B1096    14104  16653  12218   1719   2079   3006       C  
ATOM   5653  NH1 ARG B1096     -19.260  12.879  -9.259  1.00101.86           N  
ANISOU 5653  NH1 ARG B1096    12787  15166  10750   1727   2117   3151       N  
ATOM   5654  NH2 ARG B1096     -20.353  14.862  -8.921  1.00102.66           N  
ANISOU 5654  NH2 ARG B1096    12819  15473  10713   1945   2243   3045       N  
ATOM   5655  N   ALA B1097     -16.164  13.851 -16.998  1.00 72.34           N  
ANISOU 5655  N   ALA B1097     8629  10746   8113    485   1137   2119       N  
ATOM   5656  CA  ALA B1097     -15.039  14.311 -17.819  1.00 70.80           C  
ANISOU 5656  CA  ALA B1097     8469  10451   7982    443   1004   1910       C  
ATOM   5657  C   ALA B1097     -15.480  14.708 -19.235  1.00 74.12           C  
ANISOU 5657  C   ALA B1097     8805  10844   8513    236    967   1861       C  
ATOM   5658  O   ALA B1097     -14.884  15.623 -19.810  1.00 73.05           O  
ANISOU 5658  O   ALA B1097     8670  10682   8402    247    890   1713       O  
ATOM   5659  CB  ALA B1097     -13.961  13.237 -17.888  1.00 71.49           C  
ANISOU 5659  CB  ALA B1097     8654  10385   8124    424    986   1883       C  
ATOM   5660  N   ALA B1098     -16.518  14.029 -19.790  1.00 71.05           N  
ANISOU 5660  N   ALA B1098     8345  10461   8188     43   1015   1990       N  
ATOM   5661  CA  ALA B1098     -17.060  14.314 -21.125  1.00 70.53           C  
ANISOU 5661  CA  ALA B1098     8205  10401   8191   -159    950   1964       C  
ATOM   5662  C   ALA B1098     -17.793  15.642 -21.134  1.00 75.50           C  
ANISOU 5662  C   ALA B1098     8707  11187   8791    -64    933   1993       C  
ATOM   5663  O   ALA B1098     -17.705  16.378 -22.115  1.00 74.83           O  
ANISOU 5663  O   ALA B1098     8607  11100   8725   -119    857   1916       O  
ATOM   5664  CB  ALA B1098     -17.986  13.199 -21.577  1.00 72.50           C  
ANISOU 5664  CB  ALA B1098     8404  10624   8517   -399    974   2086       C  
ATOM   5665  N   LEU B1099     -18.501  15.951 -20.034  1.00 73.70           N  
ANISOU 5665  N   LEU B1099     8405  11087   8510    100   1026   2114       N  
ATOM   5666  CA  LEU B1099     -19.236  17.197 -19.847  1.00 74.19           C  
ANISOU 5666  CA  LEU B1099     8358  11285   8547    243   1055   2158       C  
ATOM   5667  C   LEU B1099     -18.235  18.344 -19.704  1.00 77.18           C  
ANISOU 5667  C   LEU B1099     8851  11604   8869    409   1004   1965       C  
ATOM   5668  O   LEU B1099     -18.453  19.406 -20.281  1.00 76.40           O  
ANISOU 5668  O   LEU B1099     8703  11523   8800    440    976   1933       O  
ATOM   5669  CB  LEU B1099     -20.115  17.092 -18.593  1.00 76.11           C  
ANISOU 5669  CB  LEU B1099     8532  11654   8731    401   1214   2330       C  
ATOM   5670  CG  LEU B1099     -21.455  17.811 -18.635  1.00 82.37           C  
ANISOU 5670  CG  LEU B1099     9117  12608   9572    460   1293   2491       C  
ATOM   5671  CD1 LEU B1099     -22.514  16.962 -19.336  1.00 83.96           C  
ANISOU 5671  CD1 LEU B1099     9106  12873   9920    206   1278   2674       C  
ATOM   5672  CD2 LEU B1099     -21.925  18.145 -17.232  1.00 86.08           C  
ANISOU 5672  CD2 LEU B1099     9599  13177   9931    727   1485   2588       C  
ATOM   5673  N   ILE B1100     -17.125  18.107 -18.962  1.00 73.91           N  
ANISOU 5673  N   ILE B1100     8582  11112   8390    508    984   1844       N  
ATOM   5674  CA  ILE B1100     -16.027  19.058 -18.734  1.00 73.48           C  
ANISOU 5674  CA  ILE B1100     8625  10984   8308    631    908   1641       C  
ATOM   5675  C   ILE B1100     -15.377  19.388 -20.082  1.00 77.56           C  
ANISOU 5675  C   ILE B1100     9136  11385   8947    479    830   1535       C  
ATOM   5676  O   ILE B1100     -15.182  20.568 -20.385  1.00 77.48           O  
ANISOU 5676  O   ILE B1100     9127  11340   8971    530    808   1444       O  
ATOM   5677  CB  ILE B1100     -15.018  18.518 -17.668  1.00 76.92           C  
ANISOU 5677  CB  ILE B1100     9181  11390   8654    746    868   1565       C  
ATOM   5678  CG1 ILE B1100     -15.661  18.494 -16.261  1.00 78.97           C  
ANISOU 5678  CG1 ILE B1100     9490  11779   8737    948    961   1661       C  
ATOM   5679  CG2 ILE B1100     -13.718  19.331 -17.642  1.00 76.98           C  
ANISOU 5679  CG2 ILE B1100     9250  11308   8692    800    744   1340       C  
ATOM   5680  CD1 ILE B1100     -15.077  17.468 -15.290  1.00 87.49           C  
ANISOU 5680  CD1 ILE B1100    10674  12866   9703   1035    951   1704       C  
ATOM   5681  N   ASN B1101     -15.110  18.342 -20.909  1.00 73.92           N  
ANISOU 5681  N   ASN B1101     8684  10853   8548    295    811   1556       N  
ATOM   5682  CA  ASN B1101     -14.543  18.436 -22.264  1.00 72.87           C  
ANISOU 5682  CA  ASN B1101     8575  10613   8498    146    771   1476       C  
ATOM   5683  C   ASN B1101     -15.377  19.397 -23.122  1.00 76.23           C  
ANISOU 5683  C   ASN B1101     8931  11101   8932    109    762   1531       C  
ATOM   5684  O   ASN B1101     -14.811  20.234 -23.827  1.00 75.23           O  
ANISOU 5684  O   ASN B1101     8836  10899   8851    107    748   1447       O  
ATOM   5685  CB  ASN B1101     -14.468  17.038 -22.914  1.00 74.11           C  
ANISOU 5685  CB  ASN B1101     8782  10696   8682    -36    781   1511       C  
ATOM   5686  CG  ASN B1101     -13.838  17.001 -24.289  1.00 98.11           C  
ANISOU 5686  CG  ASN B1101    11891  13620  11767   -174    768   1421       C  
ATOM   5687  OD1 ASN B1101     -14.407  17.466 -25.281  1.00 93.84           O  
ANISOU 5687  OD1 ASN B1101    11334  13118  11203   -268    741   1449       O  
ATOM   5688  ND2 ASN B1101     -12.670  16.395 -24.390  1.00 90.17           N  
ANISOU 5688  ND2 ASN B1101    10968  12475  10815   -175    797   1329       N  
ATOM   5689  N   MET B1102     -16.718  19.288 -23.027  1.00 73.50           N  
ANISOU 5689  N   MET B1102     8475  10894   8556     91    780   1692       N  
ATOM   5690  CA  MET B1102     -17.672  20.138 -23.737  1.00 73.93           C  
ANISOU 5690  CA  MET B1102     8425  11044   8620     87    761   1792       C  
ATOM   5691  C   MET B1102     -17.584  21.592 -23.273  1.00 79.07           C  
ANISOU 5691  C   MET B1102     9079  11688   9278    300    806   1749       C  
ATOM   5692  O   MET B1102     -17.708  22.497 -24.100  1.00 78.88           O  
ANISOU 5692  O   MET B1102     9041  11646   9283    310    790   1766       O  
ATOM   5693  CB  MET B1102     -19.100  19.605 -23.575  1.00 77.33           C  
ANISOU 5693  CB  MET B1102     8690  11639   9054     28    771   1989       C  
ATOM   5694  CG  MET B1102     -19.465  18.565 -24.604  1.00 81.27           C  
ANISOU 5694  CG  MET B1102     9168  12146   9567   -238    679   2033       C  
ATOM   5695  SD  MET B1102     -21.107  17.842 -24.389  1.00 87.43           S  
ANISOU 5695  SD  MET B1102     9707  13106  10406   -360    672   2263       S  
ATOM   5696  CE  MET B1102     -22.153  19.234 -24.808  1.00 85.07           C  
ANISOU 5696  CE  MET B1102     9204  12990  10127   -229    636   2410       C  
ATOM   5697  N   VAL B1103     -17.359  21.814 -21.957  1.00 76.66           N  
ANISOU 5697  N   VAL B1103     8815  11381   8933    474    864   1691       N  
ATOM   5698  CA  VAL B1103     -17.239  23.154 -21.362  1.00 77.32           C  
ANISOU 5698  CA  VAL B1103     8943  11425   9010    677    910   1609       C  
ATOM   5699  C   VAL B1103     -15.944  23.824 -21.844  1.00 81.83           C  
ANISOU 5699  C   VAL B1103     9619  11817   9657    644    856   1422       C  
ATOM   5700  O   VAL B1103     -15.928  25.030 -22.082  1.00 82.02           O  
ANISOU 5700  O   VAL B1103     9665  11764   9736    724    886   1383       O  
ATOM   5701  CB  VAL B1103     -17.431  23.156 -19.813  1.00 81.81           C  
ANISOU 5701  CB  VAL B1103     9561  12054   9468    871    983   1589       C  
ATOM   5702  CG1 VAL B1103     -17.173  24.534 -19.207  1.00 82.45           C  
ANISOU 5702  CG1 VAL B1103     9743  12054   9529   1066   1019   1448       C  
ATOM   5703  CG2 VAL B1103     -18.832  22.682 -19.440  1.00 82.66           C  
ANISOU 5703  CG2 VAL B1103     9533  12336   9538    916   1088   1815       C  
ATOM   5704  N   PHE B1104     -14.892  23.025 -22.080  1.00 78.49           N  
ANISOU 5704  N   PHE B1104     9245  11316   9263    520    796   1327       N  
ATOM   5705  CA  PHE B1104     -13.622  23.528 -22.605  1.00 78.20           C  
ANISOU 5705  CA  PHE B1104     9265  11114   9334    467    765   1174       C  
ATOM   5706  C   PHE B1104     -13.749  23.949 -24.069  1.00 81.63           C  
ANISOU 5706  C   PHE B1104     9689  11496   9829    361    793   1241       C  
ATOM   5707  O   PHE B1104     -12.902  24.693 -24.563  1.00 81.96           O  
ANISOU 5707  O   PHE B1104     9769  11396   9977    342    813   1152       O  
ATOM   5708  CB  PHE B1104     -12.517  22.478 -22.450  1.00 79.62           C  
ANISOU 5708  CB  PHE B1104     9471  11240   9540    391    716   1088       C  
ATOM   5709  CG  PHE B1104     -11.802  22.541 -21.126  1.00 81.93           C  
ANISOU 5709  CG  PHE B1104     9796  11528   9807    513    651    960       C  
ATOM   5710  CD1 PHE B1104     -10.782  23.458 -20.912  1.00 86.05           C  
ANISOU 5710  CD1 PHE B1104    10329  11934  10432    541    594    786       C  
ATOM   5711  CD2 PHE B1104     -12.134  21.672 -20.097  1.00 84.42           C  
ANISOU 5711  CD2 PHE B1104    10130  11953   9992    593    637   1017       C  
ATOM   5712  CE1 PHE B1104     -10.114  23.510 -19.686  1.00 88.14           C  
ANISOU 5712  CE1 PHE B1104    10624  12213  10652    642    486    652       C  
ATOM   5713  CE2 PHE B1104     -11.464  21.725 -18.872  1.00 88.24           C  
ANISOU 5713  CE2 PHE B1104    10665  12454  10407    721    552    904       C  
ATOM   5714  CZ  PHE B1104     -10.460  22.642 -18.674  1.00 87.14           C  
ANISOU 5714  CZ  PHE B1104    10537  12219  10354    743    458    713       C  
ATOM   5715  N   GLN B1105     -14.811  23.487 -24.748  1.00 77.39           N  
ANISOU 5715  N   GLN B1105     9100  11080   9225    289    790   1404       N  
ATOM   5716  CA  GLN B1105     -15.070  23.787 -26.150  1.00 77.24           C  
ANISOU 5716  CA  GLN B1105     9089  11055   9205    197    788   1490       C  
ATOM   5717  C   GLN B1105     -16.142  24.866 -26.329  1.00 82.96           C  
ANISOU 5717  C   GLN B1105     9743  11856   9923    316    807   1631       C  
ATOM   5718  O   GLN B1105     -15.942  25.794 -27.116  1.00 83.35           O  
ANISOU 5718  O   GLN B1105     9836  11821  10013    341    841   1655       O  
ATOM   5719  CB  GLN B1105     -15.452  22.506 -26.900  1.00 78.15           C  
ANISOU 5719  CB  GLN B1105     9207  11248   9239     15    731   1557       C  
ATOM   5720  CG  GLN B1105     -15.247  22.607 -28.402  1.00 81.40           C  
ANISOU 5720  CG  GLN B1105     9702  11619   9609   -100    722   1580       C  
ATOM   5721  CD  GLN B1105     -15.789  21.416 -29.145  1.00 90.63           C  
ANISOU 5721  CD  GLN B1105    10897  12868  10669   -287    642   1626       C  
ATOM   5722  OE1 GLN B1105     -15.684  20.262 -28.717  1.00 88.09           O  
ANISOU 5722  OE1 GLN B1105    10590  12532  10346   -374    632   1578       O  
ATOM   5723  NE2 GLN B1105     -16.356  21.672 -30.300  1.00 75.57           N  
ANISOU 5723  NE2 GLN B1105     9015  11036   8663   -355    578   1718       N  
ATOM   5724  N   MET B1106     -17.273  24.738 -25.610  1.00 80.12           N  
ANISOU 5724  N   MET B1106     9269  11650   9524    402    808   1745       N  
ATOM   5725  CA  MET B1106     -18.396  25.671 -25.686  1.00 81.18           C  
ANISOU 5725  CA  MET B1106     9300  11877   9670    547    842   1908       C  
ATOM   5726  C   MET B1106     -18.412  26.677 -24.544  1.00 85.76           C  
ANISOU 5726  C   MET B1106     9910  12387  10290    778    950   1844       C  
ATOM   5727  O   MET B1106     -18.627  27.864 -24.781  1.00 86.70           O  
ANISOU 5727  O   MET B1106    10043  12433  10465    914   1014   1886       O  
ATOM   5728  CB  MET B1106     -19.733  24.910 -25.699  1.00 84.44           C  
ANISOU 5728  CB  MET B1106     9529  12514  10041    497    793   2101       C  
ATOM   5729  CG  MET B1106     -20.079  24.303 -27.030  1.00 88.40           C  
ANISOU 5729  CG  MET B1106     9992  13103  10494    292    660   2194       C  
ATOM   5730  SD  MET B1106     -20.835  22.678 -26.827  1.00 93.02           S  
ANISOU 5730  SD  MET B1106    10450  13840  11053     83    575   2264       S  
ATOM   5731  CE  MET B1106     -19.379  21.663 -26.829  1.00 87.99           C  
ANISOU 5731  CE  MET B1106    10036  13012  10385    -69    581   2036       C  
ATOM   5732  N   GLY B1107     -18.217  26.192 -23.322  1.00 81.78           N  
ANISOU 5732  N   GLY B1107     9433  11898   9740    830    976   1747       N  
ATOM   5733  CA  GLY B1107     -18.305  26.999 -22.115  1.00 82.73           C  
ANISOU 5733  CA  GLY B1107     9617  11974   9844   1052   1073   1667       C  
ATOM   5734  C   GLY B1107     -19.639  26.724 -21.460  1.00 88.82           C  
ANISOU 5734  C   GLY B1107    10254  12937  10557   1178   1162   1850       C  
ATOM   5735  O   GLY B1107     -20.504  26.101 -22.085  1.00 88.36           O  
ANISOU 5735  O   GLY B1107    10024  13034  10516   1079   1129   2046       O  
ATOM   5736  N   GLU B1108     -19.814  27.177 -20.203  1.00 87.62           N  
ANISOU 5736  N   GLU B1108    10179  12778  10336   1391   1277   1785       N  
ATOM   5737  CA  GLU B1108     -21.035  26.989 -19.406  1.00 89.54           C  
ANISOU 5737  CA  GLU B1108    10308  13192  10520   1555   1420   1959       C  
ATOM   5738  C   GLU B1108     -22.333  27.248 -20.185  1.00 94.98           C  
ANISOU 5738  C   GLU B1108    10754  14019  11314   1588   1468   2231       C  
ATOM   5739  O   GLU B1108     -23.135  26.327 -20.338  1.00 95.12           O  
ANISOU 5739  O   GLU B1108    10572  14218  11352   1485   1455   2422       O  
ATOM   5740  CB  GLU B1108     -20.998  27.851 -18.134  1.00 92.71           C  
ANISOU 5740  CB  GLU B1108    10884  13520  10822   1826   1565   1825       C  
ATOM   5741  CG  GLU B1108     -20.147  27.282 -17.016  1.00104.94           C  
ANISOU 5741  CG  GLU B1108    12618  15048  12207   1833   1524   1635       C  
ATOM   5742  CD  GLU B1108     -19.982  28.236 -15.849  1.00131.83           C  
ANISOU 5742  CD  GLU B1108    16250  18361  15479   2084   1625   1449       C  
ATOM   5743  OE1 GLU B1108     -20.987  28.504 -15.150  1.00129.58           O  
ANISOU 5743  OE1 GLU B1108    15954  18167  15113   2312   1830   1565       O  
ATOM   5744  OE2 GLU B1108     -18.853  28.739 -15.651  1.00128.41           O  
ANISOU 5744  OE2 GLU B1108    16003  17758  15030   2050   1505   1182       O  
ATOM   5745  N   THR B1109     -22.509  28.479 -20.707  1.00 92.56           N  
ANISOU 5745  N   THR B1109    10459  13621  11090   1721   1510   2256       N  
ATOM   5746  CA  THR B1109     -23.684  28.920 -21.472  1.00 94.23           C  
ANISOU 5746  CA  THR B1109    10440  13957  11405   1800   1541   2525       C  
ATOM   5747  C   THR B1109     -23.990  28.055 -22.698  1.00 97.96           C  
ANISOU 5747  C   THR B1109    10726  14579  11914   1536   1348   2678       C  
ATOM   5748  O   THR B1109     -25.158  27.785 -22.970  1.00 99.05           O  
ANISOU 5748  O   THR B1109    10599  14925  12112   1541   1339   2924       O  
ATOM   5749  CB  THR B1109     -23.566  30.400 -21.843  1.00104.03           C  
ANISOU 5749  CB  THR B1109    11785  15018  12724   1989   1615   2503       C  
ATOM   5750  OG1 THR B1109     -22.336  30.606 -22.543  1.00103.53           O  
ANISOU 5750  OG1 THR B1109    11903  14760  12673   1823   1495   2321       O  
ATOM   5751  CG2 THR B1109     -23.644  31.311 -20.626  1.00104.27           C  
ANISOU 5751  CG2 THR B1109    11973  14920  12725   2285   1831   2389       C  
ATOM   5752  N   GLY B1110     -22.947  27.627 -23.409  1.00 92.82           N  
ANISOU 5752  N   GLY B1110    10214  13823  11229   1309   1198   2528       N  
ATOM   5753  CA  GLY B1110     -23.069  26.785 -24.594  1.00 92.14           C  
ANISOU 5753  CA  GLY B1110    10032  13843  11136   1047   1013   2614       C  
ATOM   5754  C   GLY B1110     -23.602  25.399 -24.296  1.00 96.03           C  
ANISOU 5754  C   GLY B1110    10379  14497  11612    872    961   2686       C  
ATOM   5755  O   GLY B1110     -24.543  24.946 -24.954  1.00 97.26           O  
ANISOU 5755  O   GLY B1110    10318  14832  11805    752    856   2873       O  
ATOM   5756  N   VAL B1111     -23.005  24.726 -23.288  1.00 90.98           N  
ANISOU 5756  N   VAL B1111     9856  13790  10922    853   1028   2545       N  
ATOM   5757  CA  VAL B1111     -23.376  23.374 -22.845  1.00 90.52           C  
ANISOU 5757  CA  VAL B1111     9703  13833  10856    698   1020   2608       C  
ATOM   5758  C   VAL B1111     -24.761  23.398 -22.193  1.00 95.85           C  
ANISOU 5758  C   VAL B1111    10124  14699  11598    827   1149   2846       C  
ATOM   5759  O   VAL B1111     -25.582  22.529 -22.496  1.00 96.42           O  
ANISOU 5759  O   VAL B1111     9981  14913  11742    648   1089   3007       O  
ATOM   5760  CB  VAL B1111     -22.290  22.724 -21.936  1.00 92.76           C  
ANISOU 5760  CB  VAL B1111    10200  13986  11058    685   1063   2416       C  
ATOM   5761  CG1 VAL B1111     -22.627  21.268 -21.610  1.00 92.80           C  
ANISOU 5761  CG1 VAL B1111    10131  14059  11069    512   1064   2501       C  
ATOM   5762  CG2 VAL B1111     -20.910  22.809 -22.583  1.00 90.66           C  
ANISOU 5762  CG2 VAL B1111    10141  13538  10768    584    958   2199       C  
ATOM   5763  N   ALA B1112     -25.038  24.429 -21.355  1.00 93.15           N  
ANISOU 5763  N   ALA B1112     9797  14349  11245   1134   1333   2867       N  
ATOM   5764  CA  ALA B1112     -26.316  24.621 -20.658  1.00 95.58           C  
ANISOU 5764  CA  ALA B1112     9872  14824  11619   1324   1518   3098       C  
ATOM   5765  C   ALA B1112     -27.493  24.821 -21.624  1.00101.93           C  
ANISOU 5765  C   ALA B1112    10341  15812  12574   1279   1433   3357       C  
ATOM   5766  O   ALA B1112     -28.651  24.687 -21.218  1.00103.75           O  
ANISOU 5766  O   ALA B1112    10289  16220  12910   1362   1556   3594       O  
ATOM   5767  CB  ALA B1112     -26.223  25.791 -19.689  1.00 97.09           C  
ANISOU 5767  CB  ALA B1112    10217  14926  11746   1676   1734   3022       C  
ATOM   5768  N   GLY B1113     -27.179  25.115 -22.886  1.00 98.21           N  
ANISOU 5768  N   GLY B1113     9897  15308  12109   1151   1224   3323       N  
ATOM   5769  CA  GLY B1113     -28.159  25.299 -23.947  1.00100.12           C  
ANISOU 5769  CA  GLY B1113     9854  15734  12453   1092   1074   3552       C  
ATOM   5770  C   GLY B1113     -28.825  24.008 -24.383  1.00105.47           C  
ANISOU 5770  C   GLY B1113    10291  16586  13197    773    906   3671       C  
ATOM   5771  O   GLY B1113     -29.992  24.024 -24.776  1.00108.00           O  
ANISOU 5771  O   GLY B1113    10265  17124  13647    756    833   3919       O  
ATOM   5772  N   PHE B1114     -28.098  22.874 -24.305  1.00100.35           N  
ANISOU 5772  N   PHE B1114     9813  15835  12480    516    841   3499       N  
ATOM   5773  CA  PHE B1114     -28.595  21.544 -24.684  1.00101.27           C  
ANISOU 5773  CA  PHE B1114     9763  16050  12663    176    691   3565       C  
ATOM   5774  C   PHE B1114     -29.580  20.989 -23.632  1.00107.23           C  
ANISOU 5774  C   PHE B1114    10246  16932  13564    205    877   3766       C  
ATOM   5775  O   PHE B1114     -29.378  19.886 -23.111  1.00106.53           O  
ANISOU 5775  O   PHE B1114    10217  16775  13486     33    932   3721       O  
ATOM   5776  CB  PHE B1114     -27.418  20.573 -24.905  1.00100.69           C  
ANISOU 5776  CB  PHE B1114    10001  15780  12476    -64    607   3313       C  
ATOM   5777  CG  PHE B1114     -26.411  20.990 -25.949  1.00100.48           C  
ANISOU 5777  CG  PHE B1114    10237  15624  12316   -111    461   3125       C  
ATOM   5778  CD1 PHE B1114     -26.619  20.703 -27.294  1.00104.51           C  
ANISOU 5778  CD1 PHE B1114    10722  16203  12786   -343    210   3132       C  
ATOM   5779  CD2 PHE B1114     -25.228  21.618 -25.584  1.00100.33           C  
ANISOU 5779  CD2 PHE B1114    10499  15413  12208     63    573   2937       C  
ATOM   5780  CE1 PHE B1114     -25.676  21.072 -28.255  1.00104.02           C  
ANISOU 5780  CE1 PHE B1114    10922  16020  12582   -370    116   2975       C  
ATOM   5781  CE2 PHE B1114     -24.287  21.984 -26.545  1.00101.73           C  
ANISOU 5781  CE2 PHE B1114    10898  15464  12291     14    474   2786       C  
ATOM   5782  CZ  PHE B1114     -24.514  21.702 -27.872  1.00100.81           C  
ANISOU 5782  CZ  PHE B1114    10767  15416  12121   -191    266   2814       C  
ATOM   5783  N   THR B1115     -30.653  21.758 -23.339  1.00105.83           N  
ANISOU 5783  N   THR B1115     9767  16932  13512    435    997   4008       N  
ATOM   5784  CA  THR B1115     -31.699  21.461 -22.349  1.00108.02           C  
ANISOU 5784  CA  THR B1115     9744  17351  13948    528   1231   4248       C  
ATOM   5785  C   THR B1115     -32.317  20.065 -22.481  1.00113.20           C  
ANISOU 5785  C   THR B1115    10159  18093  14758    158   1135   4360       C  
ATOM   5786  O   THR B1115     -32.533  19.399 -21.464  1.00113.43           O  
ANISOU 5786  O   THR B1115    10148  18105  14845    161   1366   4440       O  
ATOM   5787  CB  THR B1115     -32.751  22.581 -22.300  1.00117.35           C  
ANISOU 5787  CB  THR B1115    10614  18714  15261    835   1345   4501       C  
ATOM   5788  OG1 THR B1115     -33.322  22.749 -23.596  1.00118.86           O  
ANISOU 5788  OG1 THR B1115    10555  19065  15541    685   1040   4621       O  
ATOM   5789  CG2 THR B1115     -32.178  23.907 -21.800  1.00113.74           C  
ANISOU 5789  CG2 THR B1115    10430  18115  14670   1235   1542   4387       C  
ATOM   5790  N   ASN B1116     -32.572  19.619 -23.727  1.00110.44           N  
ANISOU 5790  N   ASN B1116     9679  17821  14463   -164    799   4359       N  
ATOM   5791  CA  ASN B1116     -33.137  18.301 -24.024  1.00112.22           C  
ANISOU 5791  CA  ASN B1116     9695  18099  14845   -571    653   4427       C  
ATOM   5792  C   ASN B1116     -32.107  17.196 -23.822  1.00113.17           C  
ANISOU 5792  C   ASN B1116    10181  17965  14854   -793    664   4188       C  
ATOM   5793  O   ASN B1116     -32.472  16.096 -23.407  1.00114.05           O  
ANISOU 5793  O   ASN B1116    10183  18043  15106  -1020    731   4262       O  
ATOM   5794  CB  ASN B1116     -33.686  18.248 -25.454  1.00114.94           C  
ANISOU 5794  CB  ASN B1116     9830  18603  15238   -837    256   4463       C  
ATOM   5795  CG  ASN B1116     -34.945  19.046 -25.691  1.00137.69           C  
ANISOU 5795  CG  ASN B1116    12236  21779  18300   -685    203   4768       C  
ATOM   5796  OD1 ASN B1116     -35.699  19.382 -24.771  1.00131.05           O  
ANISOU 5796  OD1 ASN B1116    11111  21049  17633   -452    481   5004       O  
ATOM   5797  ND2 ASN B1116     -35.218  19.334 -26.954  1.00131.66           N  
ANISOU 5797  ND2 ASN B1116    11372  21158  17495   -809   -155   4783       N  
ATOM   5798  N   SER B1117     -30.831  17.483 -24.124  1.00106.18           N  
ANISOU 5798  N   SER B1117     9712  16892  13739   -724    609   3919       N  
ATOM   5799  CA  SER B1117     -29.746  16.520 -23.974  1.00103.76           C  
ANISOU 5799  CA  SER B1117     9759  16339  13326   -886    623   3694       C  
ATOM   5800  C   SER B1117     -29.382  16.308 -22.502  1.00106.42           C  
ANISOU 5800  C   SER B1117    10222  16575  13637   -675    946   3716       C  
ATOM   5801  O   SER B1117     -29.255  15.159 -22.078  1.00106.09           O  
ANISOU 5801  O   SER B1117    10245  16419  13645   -852   1018   3716       O  
ATOM   5802  CB  SER B1117     -28.529  16.955 -24.783  1.00104.59           C  
ANISOU 5802  CB  SER B1117    10219  16299  13223   -861    479   3430       C  
ATOM   5803  OG  SER B1117     -28.838  17.035 -26.166  1.00115.20           O  
ANISOU 5803  OG  SER B1117    11494  17733  14545  -1065    183   3411       O  
ATOM   5804  N   LEU B1118     -29.267  17.412 -21.721  1.00102.32           N  
ANISOU 5804  N   LEU B1118     9747  16097  13034   -293   1140   3743       N  
ATOM   5805  CA  LEU B1118     -28.938  17.407 -20.283  1.00101.69           C  
ANISOU 5805  CA  LEU B1118     9817  15953  12867    -37   1437   3756       C  
ATOM   5806  C   LEU B1118     -29.970  16.629 -19.448  1.00108.26           C  
ANISOU 5806  C   LEU B1118    10390  16882  13861    -85   1654   4024       C  
ATOM   5807  O   LEU B1118     -29.639  16.120 -18.375  1.00107.64           O  
ANISOU 5807  O   LEU B1118    10473  16721  13704     16   1870   4040       O  
ATOM   5808  CB  LEU B1118     -28.802  18.846 -19.734  1.00101.20           C  
ANISOU 5808  CB  LEU B1118     9834  15927  12690    365   1580   3727       C  
ATOM   5809  CG  LEU B1118     -27.665  19.742 -20.265  1.00103.04           C  
ANISOU 5809  CG  LEU B1118    10356  16025  12769    466   1442   3465       C  
ATOM   5810  CD1 LEU B1118     -27.904  21.183 -19.879  1.00103.83           C  
ANISOU 5810  CD1 LEU B1118    10449  16169  12831    820   1580   3490       C  
ATOM   5811  CD2 LEU B1118     -26.296  19.298 -19.754  1.00102.58           C  
ANISOU 5811  CD2 LEU B1118    10660  15768  12548    468   1449   3228       C  
ATOM   5812  N   ARG B1119     -31.215  16.556 -19.955  1.00107.60           N  
ANISOU 5812  N   ARG B1119     9893  16982  14006   -234   1593   4248       N  
ATOM   5813  CA  ARG B1119     -32.357  15.863 -19.368  1.00110.84           C  
ANISOU 5813  CA  ARG B1119     9960  17507  14645   -328   1782   4540       C  
ATOM   5814  C   ARG B1119     -32.078  14.359 -19.269  1.00115.27           C  
ANISOU 5814  C   ARG B1119    10627  17897  15272   -662   1772   4512       C  
ATOM   5815  O   ARG B1119     -32.123  13.802 -18.174  1.00115.78           O  
ANISOU 5815  O   ARG B1119    10745  17906  15339   -577   2058   4635       O  
ATOM   5816  CB  ARG B1119     -33.599  16.135 -20.237  1.00113.63           C  
ANISOU 5816  CB  ARG B1119     9834  18093  15248   -475   1610   4742       C  
ATOM   5817  CG  ARG B1119     -34.906  15.490 -19.764  1.00124.75           C  
ANISOU 5817  CG  ARG B1119    10785  19651  16965   -605   1784   5075       C  
ATOM   5818  CD  ARG B1119     -35.955  15.392 -20.874  1.00128.26           C  
ANISOU 5818  CD  ARG B1119    10764  20295  17673   -901   1482   5218       C  
ATOM   5819  NE  ARG B1119     -36.016  16.592 -21.717  1.00128.33           N  
ANISOU 5819  NE  ARG B1119    10712  20447  17602   -725   1265   5180       N  
ATOM   5820  CZ  ARG B1119     -36.673  17.704 -21.406  1.00142.75           C  
ANISOU 5820  CZ  ARG B1119    12295  22455  19487   -361   1429   5379       C  
ATOM   5821  NH1 ARG B1119     -37.342  17.791 -20.263  1.00134.02           N  
ANISOU 5821  NH1 ARG B1119    10983  21427  18512   -127   1824   5623       N  
ATOM   5822  NH2 ARG B1119     -36.661  18.740 -22.232  1.00128.77           N  
ANISOU 5822  NH2 ARG B1119    10505  20780  17642   -211   1223   5347       N  
ATOM   5823  N   MET B1120     -31.777  13.722 -20.414  1.00111.37           N  
ANISOU 5823  N   MET B1120    10192  17308  14814  -1024   1456   4352       N  
ATOM   5824  CA  MET B1120     -31.498  12.287 -20.537  1.00111.82           C  
ANISOU 5824  CA  MET B1120    10374  17161  14952  -1375   1412   4292       C  
ATOM   5825  C   MET B1120     -30.177  11.850 -19.903  1.00113.41           C  
ANISOU 5825  C   MET B1120    11032  17116  14941  -1248   1537   4113       C  
ATOM   5826  O   MET B1120     -30.069  10.693 -19.487  1.00114.03           O  
ANISOU 5826  O   MET B1120    11200  17028  15100  -1414   1650   4161       O  
ATOM   5827  CB  MET B1120     -31.635  11.799 -21.992  1.00114.86           C  
ANISOU 5827  CB  MET B1120    10701  17520  15419  -1787   1036   4156       C  
ATOM   5828  CG  MET B1120     -31.585  12.911 -23.021  1.00117.37           C  
ANISOU 5828  CG  MET B1120    10989  17988  15618  -1702    773   4051       C  
ATOM   5829  SD  MET B1120     -32.663  12.644 -24.442  1.00125.12           S  
ANISOU 5829  SD  MET B1120    11614  19148  16779  -2117    373   4102       S  
ATOM   5830  CE  MET B1120     -34.230  13.186 -23.765  1.00125.73           C  
ANISOU 5830  CE  MET B1120    11087  19539  17144  -1973    539   4508       C  
ATOM   5831  N   LEU B1121     -29.185  12.775 -19.810  1.00107.16           N  
ANISOU 5831  N   LEU B1121    10516  16299  13900   -953   1517   3921       N  
ATOM   5832  CA  LEU B1121     -27.876  12.517 -19.182  1.00104.49           C  
ANISOU 5832  CA  LEU B1121    10579  15766  13358   -794   1605   3752       C  
ATOM   5833  C   LEU B1121     -28.060  12.294 -17.676  1.00110.03           C  
ANISOU 5833  C   LEU B1121    11306  16485  14015   -556   1935   3942       C  
ATOM   5834  O   LEU B1121     -27.423  11.410 -17.106  1.00109.77           O  
ANISOU 5834  O   LEU B1121    11499  16285  13925   -565   2033   3929       O  
ATOM   5835  CB  LEU B1121     -26.874  13.673 -19.418  1.00101.25           C  
ANISOU 5835  CB  LEU B1121    10393  15346  12731   -548   1500   3519       C  
ATOM   5836  CG  LEU B1121     -26.475  14.010 -20.863  1.00104.18           C  
ANISOU 5836  CG  LEU B1121    10814  15684  13085   -720   1210   3323       C  
ATOM   5837  CD1 LEU B1121     -25.763  15.347 -20.933  1.00101.82           C  
ANISOU 5837  CD1 LEU B1121    10656  15406  12626   -443   1176   3173       C  
ATOM   5838  CD2 LEU B1121     -25.616  12.917 -21.489  1.00105.67           C  
ANISOU 5838  CD2 LEU B1121    11241  15648  13261   -976   1090   3147       C  
ATOM   5839  N   GLN B1122     -28.956  13.078 -17.046  1.00107.91           N  
ANISOU 5839  N   GLN B1122    10811  16419  13769   -328   2121   4135       N  
ATOM   5840  CA  GLN B1122     -29.253  12.953 -15.622  1.00109.35           C  
ANISOU 5840  CA  GLN B1122    11018  16647  13881    -74   2468   4335       C  
ATOM   5841  C   GLN B1122     -30.403  11.973 -15.345  1.00116.43           C  
ANISOU 5841  C   GLN B1122    11610  17580  15047   -287   2658   4650       C  
ATOM   5842  O   GLN B1122     -30.812  11.808 -14.195  1.00118.17           O  
ANISOU 5842  O   GLN B1122    11813  17850  15235    -91   2987   4870       O  
ATOM   5843  CB  GLN B1122     -29.460  14.334 -14.965  1.00110.68           C  
ANISOU 5843  CB  GLN B1122    11184  16978  13891    335   2620   4349       C  
ATOM   5844  CG  GLN B1122     -30.758  15.066 -15.301  1.00125.31           C  
ANISOU 5844  CG  GLN B1122    12624  19045  15943    370   2675   4545       C  
ATOM   5845  CD  GLN B1122     -31.048  16.225 -14.366  1.00145.20           C  
ANISOU 5845  CD  GLN B1122    15173  21687  18310    812   2938   4605       C  
ATOM   5846  OE1 GLN B1122     -31.968  17.017 -14.598  1.00144.19           O  
ANISOU 5846  OE1 GLN B1122    14748  21720  18316    924   2999   4745       O  
ATOM   5847  NE2 GLN B1122     -30.294  16.352 -13.276  1.00133.62           N  
ANISOU 5847  NE2 GLN B1122    14067  20147  16554   1086   3101   4505       N  
ATOM   5848  N   GLN B1123     -30.896  11.311 -16.407  1.00113.66           N  
ANISOU 5848  N   GLN B1123    11034  17195  14956   -697   2448   4664       N  
ATOM   5849  CA  GLN B1123     -31.981  10.332 -16.359  1.00117.14           C  
ANISOU 5849  CA  GLN B1123    11148  17644  15716   -994   2564   4933       C  
ATOM   5850  C   GLN B1123     -31.503   8.916 -16.697  1.00121.09           C  
ANISOU 5850  C   GLN B1123    11830  17866  16312  -1352   2477   4854       C  
ATOM   5851  O   GLN B1123     -32.327   8.004 -16.813  1.00123.52           O  
ANISOU 5851  O   GLN B1123    11890  18125  16916  -1676   2527   5036       O  
ATOM   5852  CB  GLN B1123     -33.120  10.757 -17.297  1.00120.52           C  
ANISOU 5852  CB  GLN B1123    11110  18280  16402  -1196   2375   5031       C  
ATOM   5853  CG  GLN B1123     -34.162  11.645 -16.621  1.00136.38           C  
ANISOU 5853  CG  GLN B1123    12773  20552  18492   -903   2635   5308       C  
ATOM   5854  CD  GLN B1123     -35.268  12.124 -17.538  1.00156.53           C  
ANISOU 5854  CD  GLN B1123    14835  23334  21306  -1061   2433   5429       C  
ATOM   5855  OE1 GLN B1123     -35.915  13.143 -17.270  1.00152.89           O  
ANISOU 5855  OE1 GLN B1123    14133  23090  20869   -766   2567   5584       O  
ATOM   5856  NE2 GLN B1123     -35.538  11.402 -18.623  1.00149.47           N  
ANISOU 5856  NE2 GLN B1123    13780  22402  20612  -1518   2108   5369       N  
ATOM   5857  N   LYS B1124     -30.172   8.733 -16.851  1.00115.05           N  
ANISOU 5857  N   LYS B1124    11490  16905  15320  -1294   2356   4587       N  
ATOM   5858  CA  LYS B1124     -29.519   7.455 -17.175  1.00115.10           C  
ANISOU 5858  CA  LYS B1124    11740  16611  15382  -1567   2289   4479       C  
ATOM   5859  C   LYS B1124     -29.933   6.853 -18.542  1.00120.83           C  
ANISOU 5859  C   LYS B1124    12324  17250  16335  -2046   1997   4364       C  
ATOM   5860  O   LYS B1124     -29.724   5.660 -18.784  1.00121.50           O  
ANISOU 5860  O   LYS B1124    12548  17071  16544  -2331   1986   4323       O  
ATOM   5861  CB  LYS B1124     -29.637   6.438 -16.010  1.00119.98           C  
ANISOU 5861  CB  LYS B1124    12436  17086  16066  -1529   2632   4732       C  
ATOM   5862  CG  LYS B1124     -28.515   6.507 -14.969  1.00128.70           C  
ANISOU 5862  CG  LYS B1124    13927  18117  16858  -1140   2794   4696       C  
ATOM   5863  CD  LYS B1124     -28.661   7.651 -13.961  1.00137.09           C  
ANISOU 5863  CD  LYS B1124    14968  19430  17688   -701   2976   4791       C  
ATOM   5864  CE  LYS B1124     -27.532   8.645 -14.088  1.00143.87           C  
ANISOU 5864  CE  LYS B1124    16087  20330  18247   -434   2782   4493       C  
ATOM   5865  NZ  LYS B1124     -27.617   9.715 -13.059  1.00153.65           N  
ANISOU 5865  NZ  LYS B1124    17364  21772  19244    -14   2958   4551       N  
ATOM   5866  N   ARG B1125     -30.494   7.692 -19.440  1.00118.07           N  
ANISOU 5866  N   ARG B1125    11725  17115  16020  -2122   1753   4304       N  
ATOM   5867  CA  ARG B1125     -30.905   7.289 -20.787  1.00119.64           C  
ANISOU 5867  CA  ARG B1125    11798  17287  16372  -2550   1424   4176       C  
ATOM   5868  C   ARG B1125     -29.843   7.785 -21.769  1.00120.32           C  
ANISOU 5868  C   ARG B1125    12195  17316  16203  -2502   1158   3843       C  
ATOM   5869  O   ARG B1125     -29.949   8.885 -22.315  1.00118.58           O  
ANISOU 5869  O   ARG B1125    11874  17305  15877  -2372    993   3787       O  
ATOM   5870  CB  ARG B1125     -32.315   7.817 -21.126  1.00123.29           C  
ANISOU 5870  CB  ARG B1125    11741  18048  17054  -2670   1323   4378       C  
ATOM   5871  CG  ARG B1125     -33.270   6.738 -21.638  1.00140.38           C  
ANISOU 5871  CG  ARG B1125    13630  20150  19558  -3178   1201   4467       C  
ATOM   5872  CD  ARG B1125     -34.084   6.102 -20.521  1.00157.15           C  
ANISOU 5872  CD  ARG B1125    15495  22256  21959  -3213   1556   4808       C  
ATOM   5873  NE  ARG B1125     -34.916   4.998 -21.008  1.00172.48           N  
ANISOU 5873  NE  ARG B1125    17189  24087  24259  -3742   1439   4874       N  
ATOM   5874  CZ  ARG B1125     -35.772   4.307 -20.258  1.00191.91           C  
ANISOU 5874  CZ  ARG B1125    19359  26512  27046  -3892   1711   5180       C  
ATOM   5875  NH1 ARG B1125     -36.484   3.323 -20.790  1.00183.56           N  
ANISOU 5875  NH1 ARG B1125    18081  25331  26332  -4415   1566   5206       N  
ATOM   5876  NH2 ARG B1125     -35.927   4.600 -18.972  1.00180.52           N  
ANISOU 5876  NH2 ARG B1125    17852  25151  25585  -3527   2135   5461       N  
ATOM   5877  N   TRP B1126     -28.785   6.979 -21.935  1.00115.76           N  
ANISOU 5877  N   TRP B1126    12005  16445  15534  -2577   1155   3643       N  
ATOM   5878  CA  TRP B1126     -27.622   7.296 -22.763  1.00112.56           C  
ANISOU 5878  CA  TRP B1126    11932  15939  14898  -2515    974   3338       C  
ATOM   5879  C   TRP B1126     -27.893   7.238 -24.253  1.00117.74           C  
ANISOU 5879  C   TRP B1126    12566  16613  15559  -2842    640   3158       C  
ATOM   5880  O   TRP B1126     -27.568   8.197 -24.955  1.00115.68           O  
ANISOU 5880  O   TRP B1126    12349  16483  15120  -2719    472   3030       O  
ATOM   5881  CB  TRP B1126     -26.419   6.403 -22.405  1.00110.01           C  
ANISOU 5881  CB  TRP B1126    12004  15295  14499  -2461   1112   3214       C  
ATOM   5882  CG  TRP B1126     -26.286   6.062 -20.950  1.00111.31           C  
ANISOU 5882  CG  TRP B1126    12204  15406  14682  -2225   1426   3424       C  
ATOM   5883  CD1 TRP B1126     -26.323   4.816 -20.397  1.00116.38           C  
ANISOU 5883  CD1 TRP B1126    12937  15811  15470  -2353   1612   3544       C  
ATOM   5884  CD2 TRP B1126     -26.124   6.982 -19.861  1.00109.59           C  
ANISOU 5884  CD2 TRP B1126    11953  15372  14316  -1815   1595   3544       C  
ATOM   5885  NE1 TRP B1126     -26.182   4.899 -19.031  1.00115.75           N  
ANISOU 5885  NE1 TRP B1126    12884  15775  15320  -2033   1885   3750       N  
ATOM   5886  CE2 TRP B1126     -26.070   6.218 -18.673  1.00114.98           C  
ANISOU 5886  CE2 TRP B1126    12716  15941  15031  -1704   1872   3741       C  
ATOM   5887  CE3 TRP B1126     -26.025   8.381 -19.770  1.00108.73           C  
ANISOU 5887  CE3 TRP B1126    11775  15498  14041  -1528   1544   3501       C  
ATOM   5888  CZ2 TRP B1126     -25.891   6.805 -17.414  1.00113.68           C  
ANISOU 5888  CZ2 TRP B1126    12585  15910  14698  -1313   2079   3876       C  
ATOM   5889  CZ3 TRP B1126     -25.876   8.962 -18.521  1.00109.64           C  
ANISOU 5889  CZ3 TRP B1126    11917  15721  14021  -1160   1754   3619       C  
ATOM   5890  CH2 TRP B1126     -25.815   8.179 -17.360  1.00111.72           C  
ANISOU 5890  CH2 TRP B1126    12275  15891  14282  -1054   2010   3799       C  
ATOM   5891  N   ASP B1127     -28.481   6.123 -24.742  1.00117.59           N  
ANISOU 5891  N   ASP B1127    12496  16453  15732  -3261    541   3145       N  
ATOM   5892  CA  ASP B1127     -28.771   5.923 -26.163  1.00119.18           C  
ANISOU 5892  CA  ASP B1127    12713  16658  15913  -3612    197   2951       C  
ATOM   5893  C   ASP B1127     -29.724   6.974 -26.736  1.00123.60           C  
ANISOU 5893  C   ASP B1127    12905  17587  16469  -3614    -43   3049       C  
ATOM   5894  O   ASP B1127     -29.653   7.265 -27.930  1.00123.34           O  
ANISOU 5894  O   ASP B1127    12958  17622  16284  -3741   -338   2870       O  
ATOM   5895  CB  ASP B1127     -29.262   4.492 -26.437  1.00125.13           C  
ANISOU 5895  CB  ASP B1127    13483  17166  16897  -4076    148   2914       C  
ATOM   5896  CG  ASP B1127     -29.055   4.018 -27.865  1.00137.06           C  
ANISOU 5896  CG  ASP B1127    15237  18544  18295  -4412   -166   2603       C  
ATOM   5897  OD1 ASP B1127     -28.023   4.392 -28.475  1.00134.76           O  
ANISOU 5897  OD1 ASP B1127    15285  18190  17726  -4245   -219   2377       O  
ATOM   5898  OD2 ASP B1127     -29.893   3.228 -28.356  1.00146.87           O  
ANISOU 5898  OD2 ASP B1127    16350  19726  19729  -4848   -344   2579       O  
ATOM   5899  N   GLU B1128     -30.579   7.566 -25.872  1.00120.49           N  
ANISOU 5899  N   GLU B1128    12122  17432  16226  -3437    103   3345       N  
ATOM   5900  CA  GLU B1128     -31.535   8.622 -26.213  1.00121.14           C  
ANISOU 5900  CA  GLU B1128    11808  17875  16346  -3362    -63   3502       C  
ATOM   5901  C   GLU B1128     -30.811   9.973 -26.343  1.00121.30           C  
ANISOU 5901  C   GLU B1128    11984  18014  16092  -2952    -60   3427       C  
ATOM   5902  O   GLU B1128     -31.109  10.735 -27.264  1.00121.21           O  
ANISOU 5902  O   GLU B1128    11868  18199  15989  -2951   -316   3402       O  
ATOM   5903  CB  GLU B1128     -32.641   8.702 -25.143  1.00124.71           C  
ANISOU 5903  CB  GLU B1128    11810  18498  17075  -3285    168   3856       C  
ATOM   5904  CG  GLU B1128     -33.976   9.203 -25.672  1.00137.25           C  
ANISOU 5904  CG  GLU B1128    12882  20418  18850  -3416    -58   4049       C  
ATOM   5905  CD  GLU B1128     -35.094   9.318 -24.652  1.00158.16           C  
ANISOU 5905  CD  GLU B1128    15050  23248  21797  -3321    202   4419       C  
ATOM   5906  OE1 GLU B1128     -35.821  10.337 -24.693  1.00152.65           O  
ANISOU 5906  OE1 GLU B1128    13998  22854  21149  -3115    166   4607       O  
ATOM   5907  OE2 GLU B1128     -35.258   8.393 -23.823  1.00151.48           O  
ANISOU 5907  OE2 GLU B1128    14178  22237  21142  -3441    461   4538       O  
ATOM   5908  N   ALA B1129     -29.862  10.256 -25.425  1.00114.67           N  
ANISOU 5908  N   ALA B1129    11395  17049  15126  -2614    218   3395       N  
ATOM   5909  CA  ALA B1129     -29.078  11.491 -25.395  1.00111.25           C  
ANISOU 5909  CA  ALA B1129    11127  16676  14465  -2237    256   3310       C  
ATOM   5910  C   ALA B1129     -28.091  11.575 -26.556  1.00114.06           C  
ANISOU 5910  C   ALA B1129    11825  16910  14604  -2310     51   3027       C  
ATOM   5911  O   ALA B1129     -27.976  12.638 -27.171  1.00113.06           O  
ANISOU 5911  O   ALA B1129    11698  16917  14342  -2156    -70   2993       O  
ATOM   5912  CB  ALA B1129     -28.336  11.612 -24.071  1.00109.64           C  
ANISOU 5912  CB  ALA B1129    11100  16362  14197  -1912    576   3334       C  
ATOM   5913  N   ALA B1130     -27.379  10.457 -26.846  1.00110.23           N  
ANISOU 5913  N   ALA B1130    11639  16155  14089  -2526     41   2837       N  
ATOM   5914  CA  ALA B1130     -26.370  10.347 -27.904  1.00108.27           C  
ANISOU 5914  CA  ALA B1130    11750  15749  13638  -2597    -94   2563       C  
ATOM   5915  C   ALA B1130     -26.928  10.685 -29.288  1.00113.30           C  
ANISOU 5915  C   ALA B1130    12320  16547  14180  -2797   -420   2503       C  
ATOM   5916  O   ALA B1130     -26.305  11.465 -30.014  1.00111.69           O  
ANISOU 5916  O   ALA B1130    12291  16375  13770  -2657   -498   2390       O  
ATOM   5917  CB  ALA B1130     -25.751   8.955 -27.903  1.00109.44           C  
ANISOU 5917  CB  ALA B1130    12184  15576  13823  -2808    -20   2410       C  
ATOM   5918  N   VAL B1131     -28.112  10.127 -29.637  1.00112.24           N  
ANISOU 5918  N   VAL B1131    11922  16526  14199  -3120   -613   2595       N  
ATOM   5919  CA  VAL B1131     -28.771  10.374 -30.924  1.00114.05           C  
ANISOU 5919  CA  VAL B1131    12056  16945  14334  -3333   -974   2557       C  
ATOM   5920  C   VAL B1131     -29.288  11.809 -31.040  1.00116.84           C  
ANISOU 5920  C   VAL B1131    12137  17618  14639  -3058  -1050   2748       C  
ATOM   5921  O   VAL B1131     -29.277  12.371 -32.133  1.00116.99           O  
ANISOU 5921  O   VAL B1131    12230  17761  14459  -3066  -1290   2684       O  
ATOM   5922  CB  VAL B1131     -29.835   9.313 -31.321  1.00122.50           C  
ANISOU 5922  CB  VAL B1131    12924  18033  15587  -3799  -1206   2570       C  
ATOM   5923  CG1 VAL B1131     -29.202   7.941 -31.529  1.00122.95           C  
ANISOU 5923  CG1 VAL B1131    13354  17725  15637  -4084  -1166   2320       C  
ATOM   5924  CG2 VAL B1131     -30.983   9.243 -30.316  1.00124.40           C  
ANISOU 5924  CG2 VAL B1131    12673  18430  16164  -3821  -1097   2878       C  
ATOM   5925  N   ASN B1132     -29.719  12.399 -29.909  1.00112.54           N  
ANISOU 5925  N   ASN B1132    11305  17192  14264  -2795   -827   2985       N  
ATOM   5926  CA  ASN B1132     -30.227  13.771 -29.837  1.00112.22           C  
ANISOU 5926  CA  ASN B1132    11004  17417  14217  -2487   -832   3186       C  
ATOM   5927  C   ASN B1132     -29.093  14.785 -30.029  1.00111.99           C  
ANISOU 5927  C   ASN B1132    11294  17306  13950  -2164   -737   3060       C  
ATOM   5928  O   ASN B1132     -29.294  15.812 -30.678  1.00111.73           O  
ANISOU 5928  O   ASN B1132    11196  17440  13816  -2013   -866   3130       O  
ATOM   5929  CB  ASN B1132     -30.948  14.009 -28.507  1.00113.90           C  
ANISOU 5929  CB  ASN B1132    10874  17735  14670  -2292   -567   3451       C  
ATOM   5930  CG  ASN B1132     -31.712  15.310 -28.456  1.00136.45           C  
ANISOU 5930  CG  ASN B1132    13406  20868  17571  -2002   -572   3686       C  
ATOM   5931  OD1 ASN B1132     -32.761  15.472 -29.093  1.00130.98           O  
ANISOU 5931  OD1 ASN B1132    12368  20421  16978  -2127   -814   3846       O  
ATOM   5932  ND2 ASN B1132     -31.199  16.267 -27.695  1.00126.47           N  
ANISOU 5932  ND2 ASN B1132    12248  19566  16240  -1604   -311   3711       N  
ATOM   5933  N   LEU B1133     -27.908  14.483 -29.470  1.00105.32           N  
ANISOU 5933  N   LEU B1133    10779  16201  13036  -2063   -515   2889       N  
ATOM   5934  CA  LEU B1133     -26.720  15.330 -29.564  1.00101.70           C  
ANISOU 5934  CA  LEU B1133    10614  15629  12398  -1793   -406   2754       C  
ATOM   5935  C   LEU B1133     -26.101  15.333 -30.967  1.00105.04           C  
ANISOU 5935  C   LEU B1133    11319  15990  12599  -1922   -600   2567       C  
ATOM   5936  O   LEU B1133     -25.530  16.347 -31.375  1.00102.97           O  
ANISOU 5936  O   LEU B1133    11186  15735  12204  -1710   -579   2540       O  
ATOM   5937  CB  LEU B1133     -25.691  14.919 -28.512  1.00 99.12           C  
ANISOU 5937  CB  LEU B1133    10504  15068  12087  -1666   -140   2645       C  
ATOM   5938  CG  LEU B1133     -25.954  15.409 -27.092  1.00103.31           C  
ANISOU 5938  CG  LEU B1133    10865  15659  12730  -1390     99   2804       C  
ATOM   5939  CD1 LEU B1133     -25.405  14.434 -26.069  1.00102.63           C  
ANISOU 5939  CD1 LEU B1133    10916  15387  12694  -1402    292   2756       C  
ATOM   5940  CD2 LEU B1133     -25.376  16.803 -26.872  1.00103.96           C  
ANISOU 5940  CD2 LEU B1133    11026  15755  12719  -1047    194   2780       C  
ATOM   5941  N   ALA B1134     -26.242  14.215 -31.716  1.00103.07           N  
ANISOU 5941  N   ALA B1134    11179  15674  12308  -2270   -778   2442       N  
ATOM   5942  CA  ALA B1134     -25.745  14.073 -33.093  1.00103.08           C  
ANISOU 5942  CA  ALA B1134    11481  15621  12064  -2416   -962   2253       C  
ATOM   5943  C   ALA B1134     -26.587  14.898 -34.090  1.00107.87           C  
ANISOU 5943  C   ALA B1134    11922  16513  12550  -2420  -1244   2381       C  
ATOM   5944  O   ALA B1134     -26.220  15.018 -35.260  1.00108.00           O  
ANISOU 5944  O   ALA B1134    12192  16530  12315  -2482  -1395   2262       O  
ATOM   5945  CB  ALA B1134     -25.739  12.602 -33.495  1.00105.79           C  
ANISOU 5945  CB  ALA B1134    11999  15791  12404  -2787  -1060   2071       C  
ATOM   5946  N   LYS B1135     -27.711  15.465 -33.616  1.00105.11           N  
ANISOU 5946  N   LYS B1135    11152  16411  12373  -2332  -1299   2641       N  
ATOM   5947  CA  LYS B1135     -28.639  16.287 -34.395  1.00107.19           C  
ANISOU 5947  CA  LYS B1135    11178  16977  12574  -2291  -1562   2826       C  
ATOM   5948  C   LYS B1135     -28.328  17.790 -34.266  1.00109.11           C  
ANISOU 5948  C   LYS B1135    11414  17277  12766  -1878  -1411   2962       C  
ATOM   5949  O   LYS B1135     -28.841  18.595 -35.049  1.00110.57           O  
ANISOU 5949  O   LYS B1135    11495  17670  12847  -1785  -1601   3108       O  
ATOM   5950  CB  LYS B1135     -30.092  15.999 -33.969  1.00112.43           C  
ANISOU 5950  CB  LYS B1135    11342  17876  13499  -2433  -1699   3055       C  
ATOM   5951  CG  LYS B1135     -30.590  14.617 -34.381  1.00125.82           C  
ANISOU 5951  CG  LYS B1135    13012  19548  15248  -2898  -1936   2936       C  
ATOM   5952  CD  LYS B1135     -31.972  14.311 -33.814  1.00138.06           C  
ANISOU 5952  CD  LYS B1135    14026  21306  17123  -3045  -2020   3180       C  
ATOM   5953  CE  LYS B1135     -32.434  12.924 -34.189  1.00150.73           C  
ANISOU 5953  CE  LYS B1135    15609  22844  18816  -3541  -2248   3047       C  
ATOM   5954  NZ  LYS B1135     -33.815  12.652 -33.707  1.00162.15           N  
ANISOU 5954  NZ  LYS B1135    16487  24508  20615  -3711  -2341   3305       N  
ATOM   5955  N   SER B1136     -27.476  18.157 -33.290  1.00102.11           N  
ANISOU 5955  N   SER B1136    10650  16195  11950  -1635  -1081   2911       N  
ATOM   5956  CA  SER B1136     -27.086  19.543 -33.010  1.00 99.90           C  
ANISOU 5956  CA  SER B1136    10393  15905  11659  -1260   -902   3002       C  
ATOM   5957  C   SER B1136     -26.180  20.163 -34.083  1.00103.45           C  
ANISOU 5957  C   SER B1136    11174  16264  11866  -1184   -933   2898       C  
ATOM   5958  O   SER B1136     -25.638  19.450 -34.933  1.00103.26           O  
ANISOU 5958  O   SER B1136    11422  16152  11662  -1398  -1039   2717       O  
ATOM   5959  CB  SER B1136     -26.405  19.635 -31.647  1.00 99.24           C  
ANISOU 5959  CB  SER B1136    10367  15632  11707  -1070   -578   2937       C  
ATOM   5960  OG  SER B1136     -25.174  18.933 -31.642  1.00102.02           O  
ANISOU 5960  OG  SER B1136    11056  15732  11975  -1172   -483   2687       O  
ATOM   5961  N   ARG B1137     -26.011  21.504 -34.012  1.00 99.26           N  
ANISOU 5961  N   ARG B1137    10635  15738  11341   -868   -810   3018       N  
ATOM   5962  CA  ARG B1137     -25.141  22.317 -34.865  1.00 98.09           C  
ANISOU 5962  CA  ARG B1137    10774  15483  11013   -739   -765   2972       C  
ATOM   5963  C   ARG B1137     -23.689  21.932 -34.542  1.00 99.46           C  
ANISOU 5963  C   ARG B1137    11262  15358  11169   -765   -545   2712       C  
ATOM   5964  O   ARG B1137     -22.866  21.812 -35.448  1.00 99.09           O  
ANISOU 5964  O   ARG B1137    11505  15201  10941   -835   -547   2587       O  
ATOM   5965  CB  ARG B1137     -25.372  23.810 -34.555  1.00 97.22           C  
ANISOU 5965  CB  ARG B1137    10541  15401  10999   -389   -632   3172       C  
ATOM   5966  CG  ARG B1137     -24.596  24.766 -35.445  1.00105.40           C  
ANISOU 5966  CG  ARG B1137    11842  16324  11882   -243   -569   3179       C  
ATOM   5967  CD  ARG B1137     -24.264  26.047 -34.712  1.00113.34           C  
ANISOU 5967  CD  ARG B1137    12836  17180  13049     75   -311   3246       C  
ATOM   5968  NE  ARG B1137     -23.432  26.930 -35.528  1.00124.47           N  
ANISOU 5968  NE  ARG B1137    14507  18436  14350    190   -214   3252       N  
ATOM   5969  CZ  ARG B1137     -23.889  27.983 -36.197  1.00142.19           C  
ANISOU 5969  CZ  ARG B1137    16724  20755  16545    386   -246   3487       C  
ATOM   5970  NH1 ARG B1137     -23.062  28.726 -36.920  1.00129.50           N  
ANISOU 5970  NH1 ARG B1137    15376  18980  14849    477   -124   3497       N  
ATOM   5971  NH2 ARG B1137     -25.176  28.306 -36.144  1.00132.09           N  
ANISOU 5971  NH2 ARG B1137    15146  19716  15324    504   -384   3735       N  
ATOM   5972  N   TRP B1138     -23.400  21.728 -33.241  1.00 94.04           N  
ANISOU 5972  N   TRP B1138    10508  14557  10666   -696   -355   2647       N  
ATOM   5973  CA  TRP B1138     -22.104  21.351 -32.685  1.00 91.14           C  
ANISOU 5973  CA  TRP B1138    10364  13937  10330   -693   -160   2430       C  
ATOM   5974  C   TRP B1138     -21.539  20.069 -33.306  1.00 94.04           C  
ANISOU 5974  C   TRP B1138    10951  14200  10581   -959   -223   2243       C  
ATOM   5975  O   TRP B1138     -20.352  20.039 -33.616  1.00 92.15           O  
ANISOU 5975  O   TRP B1138    10961  13770  10280   -944   -102   2090       O  
ATOM   5976  CB  TRP B1138     -22.203  21.239 -31.148  1.00 88.79           C  
ANISOU 5976  CB  TRP B1138     9915  13604  10217   -582     -8   2434       C  
ATOM   5977  CG  TRP B1138     -21.067  20.515 -30.480  1.00 87.74           C  
ANISOU 5977  CG  TRP B1138     9959  13261  10116   -621    131   2233       C  
ATOM   5978  CD1 TRP B1138     -19.747  20.860 -30.497  1.00 88.83           C  
ANISOU 5978  CD1 TRP B1138    10306  13202  10244   -537    256   2081       C  
ATOM   5979  CD2 TRP B1138     -21.168  19.351 -29.653  1.00 87.38           C  
ANISOU 5979  CD2 TRP B1138     9873  13186  10142   -735    162   2191       C  
ATOM   5980  NE1 TRP B1138     -19.013  19.957 -29.765  1.00 87.00           N  
ANISOU 5980  NE1 TRP B1138    10156  12838  10062   -587    340   1945       N  
ATOM   5981  CE2 TRP B1138     -19.860  19.024 -29.227  1.00 89.35           C  
ANISOU 5981  CE2 TRP B1138    10322  13227  10401   -699    291   2013       C  
ATOM   5982  CE3 TRP B1138     -22.238  18.539 -29.236  1.00 90.28           C  
ANISOU 5982  CE3 TRP B1138    10043  13678  10583   -868    100   2303       C  
ATOM   5983  CZ2 TRP B1138     -19.594  17.927 -28.398  1.00 88.29           C  
ANISOU 5983  CZ2 TRP B1138    10216  13007  10324   -764    357   1955       C  
ATOM   5984  CZ3 TRP B1138     -21.974  17.454 -28.411  1.00 91.33           C  
ANISOU 5984  CZ3 TRP B1138    10215  13706  10781   -950    188   2242       C  
ATOM   5985  CH2 TRP B1138     -20.665  17.151 -28.009  1.00 90.05           C  
ANISOU 5985  CH2 TRP B1138    10275  13336  10602   -888    312   2074       C  
ATOM   5986  N   TYR B1139     -22.372  19.024 -33.490  1.00 91.80           N  
ANISOU 5986  N   TYR B1139    10573  14022  10283  -1202   -398   2254       N  
ATOM   5987  CA  TYR B1139     -21.916  17.751 -34.056  1.00 91.66           C  
ANISOU 5987  CA  TYR B1139    10788  13876  10164  -1462   -451   2062       C  
ATOM   5988  C   TYR B1139     -21.444  17.838 -35.501  1.00 95.33           C  
ANISOU 5988  C   TYR B1139    11536  14315  10370  -1535   -538   1969       C  
ATOM   5989  O   TYR B1139     -20.334  17.403 -35.781  1.00 93.91           O  
ANISOU 5989  O   TYR B1139    11636  13924  10120  -1557   -398   1790       O  
ATOM   5990  CB  TYR B1139     -22.944  16.612 -33.872  1.00 95.04           C  
ANISOU 5990  CB  TYR B1139    11051  14392  10668  -1732   -614   2087       C  
ATOM   5991  CG  TYR B1139     -22.516  15.301 -34.505  1.00 97.84           C  
ANISOU 5991  CG  TYR B1139    11680  14577  10918  -2010   -668   1871       C  
ATOM   5992  CD1 TYR B1139     -21.636  14.442 -33.853  1.00 98.22           C  
ANISOU 5992  CD1 TYR B1139    11889  14373  11055  -2028   -468   1727       C  
ATOM   5993  CD2 TYR B1139     -22.981  14.927 -35.764  1.00101.50           C  
ANISOU 5993  CD2 TYR B1139    12259  15126  11179  -2242   -922   1809       C  
ATOM   5994  CE1 TYR B1139     -21.225  13.245 -34.439  1.00100.22           C  
ANISOU 5994  CE1 TYR B1139    12418  14437  11225  -2258   -486   1529       C  
ATOM   5995  CE2 TYR B1139     -22.574  13.734 -36.361  1.00103.66           C  
ANISOU 5995  CE2 TYR B1139    12832  15215  11341  -2492   -955   1582       C  
ATOM   5996  CZ  TYR B1139     -21.700  12.892 -35.692  1.00108.84           C  
ANISOU 5996  CZ  TYR B1139    13648  15594  12115  -2494   -720   1444       C  
ATOM   5997  OH  TYR B1139     -21.305  11.711 -36.274  1.00110.18           O  
ANISOU 5997  OH  TYR B1139    14126  15549  12188  -2720   -725   1223       O  
ATOM   5998  N   ASN B1140     -22.284  18.349 -36.418  1.00 93.24           N  
ANISOU 5998  N   ASN B1140    11203  14268   9956  -1562   -762   2100       N  
ATOM   5999  CA  ASN B1140     -21.929  18.420 -37.839  1.00 94.12           C  
ANISOU 5999  CA  ASN B1140    11612  14384   9767  -1625   -858   2029       C  
ATOM   6000  C   ASN B1140     -20.795  19.393 -38.147  1.00 94.11           C  
ANISOU 6000  C   ASN B1140    11817  14240   9698  -1386   -622   2023       C  
ATOM   6001  O   ASN B1140     -20.033  19.141 -39.079  1.00 94.73           O  
ANISOU 6001  O   ASN B1140    12219  14210   9564  -1437   -567   1895       O  
ATOM   6002  CB  ASN B1140     -23.157  18.664 -38.728  1.00 99.50           C  
ANISOU 6002  CB  ASN B1140    12161  15360  10282  -1716  -1198   2183       C  
ATOM   6003  CG  ASN B1140     -23.858  19.975 -38.477  1.00125.93           C  
ANISOU 6003  CG  ASN B1140    15216  18904  13728  -1461  -1225   2466       C  
ATOM   6004  OD1 ASN B1140     -23.595  20.988 -39.139  1.00119.52           O  
ANISOU 6004  OD1 ASN B1140    14517  18121  12773  -1268  -1191   2574       O  
ATOM   6005  ND2 ASN B1140     -24.779  19.982 -37.522  1.00119.61           N  
ANISOU 6005  ND2 ASN B1140    14040  18229  13178  -1443  -1264   2606       N  
ATOM   6006  N   GLN B1141     -20.672  20.484 -37.359  1.00 86.73           N  
ANISOU 6006  N   GLN B1141    10707  13292   8955  -1133   -467   2156       N  
ATOM   6007  CA  GLN B1141     -19.631  21.499 -37.547  1.00 84.33           C  
ANISOU 6007  CA  GLN B1141    10556  12833   8651   -921   -236   2164       C  
ATOM   6008  C   GLN B1141     -18.263  20.998 -37.108  1.00 84.24           C  
ANISOU 6008  C   GLN B1141    10715  12554   8738   -929      8   1955       C  
ATOM   6009  O   GLN B1141     -17.252  21.348 -37.720  1.00 82.95           O  
ANISOU 6009  O   GLN B1141    10768  12246   8505   -865    176   1902       O  
ATOM   6010  CB  GLN B1141     -19.992  22.815 -36.839  1.00 84.82           C  
ANISOU 6010  CB  GLN B1141    10390  12941   8897   -666   -162   2352       C  
ATOM   6011  CG  GLN B1141     -19.996  24.030 -37.773  1.00100.64           C  
ANISOU 6011  CG  GLN B1141    12482  14981  10775   -498   -146   2525       C  
ATOM   6012  CD  GLN B1141     -21.310  24.263 -38.488  1.00121.78           C  
ANISOU 6012  CD  GLN B1141    15026  17946  13299   -501   -422   2742       C  
ATOM   6013  OE1 GLN B1141     -21.767  23.458 -39.311  1.00116.82           O  
ANISOU 6013  OE1 GLN B1141    14472  17464  12449   -701   -654   2708       O  
ATOM   6014  NE2 GLN B1141     -21.918  25.414 -38.237  1.00117.56           N  
ANISOU 6014  NE2 GLN B1141    14301  17492  12874   -268   -407   2969       N  
ATOM   6015  N   THR B1142     -18.239  20.172 -36.054  1.00 79.27           N  
ANISOU 6015  N   THR B1142     9976  11865   8278   -999     34   1859       N  
ATOM   6016  CA  THR B1142     -17.020  19.575 -35.504  1.00 76.71           C  
ANISOU 6016  CA  THR B1142     9769  11310   8068   -998    234   1681       C  
ATOM   6017  C   THR B1142     -17.259  18.064 -35.205  1.00 78.93           C  
ANISOU 6017  C   THR B1142    10078  11556   8358  -1205    165   1564       C  
ATOM   6018  O   THR B1142     -17.397  17.679 -34.045  1.00 76.49           O  
ANISOU 6018  O   THR B1142     9613  11228   8224  -1188    195   1567       O  
ATOM   6019  CB  THR B1142     -16.391  20.498 -34.427  1.00 81.59           C  
ANISOU 6019  CB  THR B1142    10256  11835   8909   -782    403   1701       C  
ATOM   6020  OG1 THR B1142     -15.124  19.996 -34.016  1.00 83.28           O  
ANISOU 6020  OG1 THR B1142    10569  11845   9227   -771    572   1542       O  
ATOM   6021  CG2 THR B1142     -17.289  20.719 -33.230  1.00 77.39           C  
ANISOU 6021  CG2 THR B1142     9462  11423   8518   -706    339   1800       C  
ATOM   6022  N   PRO B1143     -17.357  17.209 -36.264  1.00 76.89           N  
ANISOU 6022  N   PRO B1143    10039  11281   7896  -1404     71   1465       N  
ATOM   6023  CA  PRO B1143     -17.689  15.787 -36.052  1.00 77.37           C  
ANISOU 6023  CA  PRO B1143    10141  11280   7977  -1626     -3   1355       C  
ATOM   6024  C   PRO B1143     -16.759  14.892 -35.242  1.00 80.07           C  
ANISOU 6024  C   PRO B1143    10555  11386   8480  -1610    194   1228       C  
ATOM   6025  O   PRO B1143     -17.262  14.168 -34.389  1.00 79.58           O  
ANISOU 6025  O   PRO B1143    10362  11319   8556  -1693    158   1249       O  
ATOM   6026  CB  PRO B1143     -17.897  15.254 -37.473  1.00 81.78           C  
ANISOU 6026  CB  PRO B1143    10970  11852   8249  -1823   -141   1251       C  
ATOM   6027  CG  PRO B1143     -17.107  16.164 -38.334  1.00 86.05           C  
ANISOU 6027  CG  PRO B1143    11697  12369   8630  -1662    -16   1261       C  
ATOM   6028  CD  PRO B1143     -17.282  17.512 -37.708  1.00 80.08           C  
ANISOU 6028  CD  PRO B1143    10676  11728   8023  -1440     16   1456       C  
ATOM   6029  N   ASN B1144     -15.442  14.884 -35.536  1.00 76.16           N  
ANISOU 6029  N   ASN B1144    10262  10701   7973  -1506    406   1115       N  
ATOM   6030  CA  ASN B1144     -14.467  14.001 -34.880  1.00 74.91           C  
ANISOU 6030  CA  ASN B1144    10178  10319   7965  -1468    592   1005       C  
ATOM   6031  C   ASN B1144     -14.496  14.042 -33.358  1.00 77.39           C  
ANISOU 6031  C   ASN B1144    10245  10649   8510  -1352    622   1087       C  
ATOM   6032  O   ASN B1144     -14.708  12.993 -32.742  1.00 77.87           O  
ANISOU 6032  O   ASN B1144    10300  10632   8654  -1437    623   1069       O  
ATOM   6033  CB  ASN B1144     -13.058  14.177 -35.446  1.00 74.23           C  
ANISOU 6033  CB  ASN B1144    10283  10061   7860  -1343    822    909       C  
ATOM   6034  CG  ASN B1144     -12.980  13.990 -36.941  1.00 88.88           C  
ANISOU 6034  CG  ASN B1144    12441  11882   9447  -1444    833    818       C  
ATOM   6035  OD1 ASN B1144     -12.872  14.954 -37.697  1.00 79.83           O  
ANISOU 6035  OD1 ASN B1144    11343  10817   8171  -1372    851    877       O  
ATOM   6036  ND2 ASN B1144     -13.052  12.749 -37.401  1.00 81.41           N  
ANISOU 6036  ND2 ASN B1144    11730  10806   8398  -1610    830    674       N  
ATOM   6037  N   ARG B1145     -14.355  15.246 -32.757  1.00 71.88           N  
ANISOU 6037  N   ARG B1145     9364  10048   7901  -1164    644   1181       N  
ATOM   6038  CA  ARG B1145     -14.394  15.428 -31.301  1.00 69.82           C  
ANISOU 6038  CA  ARG B1145     8897   9822   7811  -1031    664   1248       C  
ATOM   6039  C   ARG B1145     -15.769  15.079 -30.733  1.00 74.41           C  
ANISOU 6039  C   ARG B1145     9316  10553   8405  -1126    532   1366       C  
ATOM   6040  O   ARG B1145     -15.835  14.298 -29.780  1.00 74.07           O  
ANISOU 6040  O   ARG B1145     9224  10462   8456  -1128    571   1385       O  
ATOM   6041  CB  ARG B1145     -13.992  16.855 -30.907  1.00 67.22           C  
ANISOU 6041  CB  ARG B1145     8448   9543   7550   -829    706   1292       C  
ATOM   6042  CG  ARG B1145     -13.695  17.011 -29.427  1.00 69.68           C  
ANISOU 6042  CG  ARG B1145     8619   9853   8004   -674    744   1304       C  
ATOM   6043  CD  ARG B1145     -13.090  18.363 -29.135  1.00 72.79           C  
ANISOU 6043  CD  ARG B1145     8944  10240   8474   -505    788   1291       C  
ATOM   6044  NE  ARG B1145     -12.971  18.613 -27.698  1.00 74.17           N  
ANISOU 6044  NE  ARG B1145     9002  10442   8736   -359    785   1291       N  
ATOM   6045  CZ  ARG B1145     -12.554  19.760 -27.172  1.00 82.49           C  
ANISOU 6045  CZ  ARG B1145     9994  11485   9863   -217    799   1257       C  
ATOM   6046  NH1 ARG B1145     -12.210  20.773 -27.956  1.00 67.40           N  
ANISOU 6046  NH1 ARG B1145     8108   9520   7983   -204    838   1243       N  
ATOM   6047  NH2 ARG B1145     -12.477  19.901 -25.856  1.00 66.32           N  
ANISOU 6047  NH2 ARG B1145     7879   9470   7850    -90    779   1236       N  
ATOM   6048  N   ALA B1146     -16.856  15.636 -31.334  1.00 71.65           N  
ANISOU 6048  N   ALA B1146     8873  10384   7966  -1199    385   1464       N  
ATOM   6049  CA  ALA B1146     -18.245  15.410 -30.914  1.00 72.68           C  
ANISOU 6049  CA  ALA B1146     8794  10685   8135  -1295    257   1603       C  
ATOM   6050  C   ALA B1146     -18.649  13.940 -30.980  1.00 79.66           C  
ANISOU 6050  C   ALA B1146     9740  11490   9038  -1543    209   1558       C  
ATOM   6051  O   ALA B1146     -19.345  13.477 -30.081  1.00 79.91           O  
ANISOU 6051  O   ALA B1146     9605  11569   9189  -1578    214   1662       O  
ATOM   6052  CB  ALA B1146     -19.203  16.264 -31.722  1.00 74.52           C  
ANISOU 6052  CB  ALA B1146     8915  11125   8273  -1320     95   1718       C  
ATOM   6053  N   LYS B1147     -18.171  13.194 -32.002  1.00 77.78           N  
ANISOU 6053  N   LYS B1147     9760  11106   8688  -1706    193   1402       N  
ATOM   6054  CA  LYS B1147     -18.438  11.757 -32.145  1.00 79.52           C  
ANISOU 6054  CA  LYS B1147    10098  11185   8930  -1954    164   1321       C  
ATOM   6055  C   LYS B1147     -17.829  11.004 -30.948  1.00 81.89           C  
ANISOU 6055  C   LYS B1147    10406  11308   9399  -1859    352   1325       C  
ATOM   6056  O   LYS B1147     -18.510  10.176 -30.343  1.00 82.35           O  
ANISOU 6056  O   LYS B1147    10377  11341   9572  -1989    343   1397       O  
ATOM   6057  CB  LYS B1147     -17.875  11.226 -33.480  1.00 83.42           C  
ANISOU 6057  CB  LYS B1147    10925  11528   9241  -2096    149   1123       C  
ATOM   6058  CG  LYS B1147     -18.496   9.914 -33.955  1.00101.04           C  
ANISOU 6058  CG  LYS B1147    13291  13649  11449  -2418     37   1021       C  
ATOM   6059  CD  LYS B1147     -18.023   9.506 -35.359  1.00113.05           C  
ANISOU 6059  CD  LYS B1147    15182  15040  12731  -2546     11    807       C  
ATOM   6060  CE  LYS B1147     -16.655   8.851 -35.394  1.00123.02           C  
ANISOU 6060  CE  LYS B1147    16737  15998  14009  -2435    282    652       C  
ATOM   6061  NZ  LYS B1147     -16.652   7.496 -34.773  1.00132.83           N  
ANISOU 6061  NZ  LYS B1147    18052  16994  15421  -2559    373    600       N  
ATOM   6062  N   ARG B1148     -16.571  11.349 -30.584  1.00 76.34           N  
ANISOU 6062  N   ARG B1148     9786  10499   8720  -1627    516   1271       N  
ATOM   6063  CA  ARG B1148     -15.817  10.762 -29.470  1.00 74.92           C  
ANISOU 6063  CA  ARG B1148     9619  10174   8675  -1484    676   1283       C  
ATOM   6064  C   ARG B1148     -16.436  11.078 -28.114  1.00 78.12           C  
ANISOU 6064  C   ARG B1148     9783  10724   9174  -1365    680   1455       C  
ATOM   6065  O   ARG B1148     -16.426  10.217 -27.235  1.00 78.00           O  
ANISOU 6065  O   ARG B1148     9770  10617   9251  -1351    765   1517       O  
ATOM   6066  CB  ARG B1148     -14.345  11.204 -29.497  1.00 72.11           C  
ANISOU 6066  CB  ARG B1148     9359   9711   8328  -1270    808   1189       C  
ATOM   6067  CG  ARG B1148     -13.512  10.560 -30.602  1.00 76.45           C  
ANISOU 6067  CG  ARG B1148    10179  10053   8816  -1343    900   1028       C  
ATOM   6068  CD  ARG B1148     -12.017  10.775 -30.406  1.00 79.81           C  
ANISOU 6068  CD  ARG B1148    10645  10357   9323  -1123   1066    970       C  
ATOM   6069  NE  ARG B1148     -11.628  12.188 -30.475  1.00 81.07           N  
ANISOU 6069  NE  ARG B1148    10679  10648   9477   -981   1052    989       N  
ATOM   6070  CZ  ARG B1148     -11.291  12.830 -31.591  1.00 88.37           C  
ANISOU 6070  CZ  ARG B1148    11700  11571  10306   -995   1085    929       C  
ATOM   6071  NH1 ARG B1148     -11.297  12.196 -32.759  1.00 72.00           N  
ANISOU 6071  NH1 ARG B1148     9866   9394   8095  -1135   1125    833       N  
ATOM   6072  NH2 ARG B1148     -10.951  14.111 -31.550  1.00 71.37           N  
ANISOU 6072  NH2 ARG B1148     9425   9508   8184   -870   1089    964       N  
ATOM   6073  N   VAL B1149     -16.962  12.306 -27.940  1.00 74.52           N  
ANISOU 6073  N   VAL B1149     9143  10483   8689  -1259    609   1541       N  
ATOM   6074  CA  VAL B1149     -17.607  12.739 -26.690  1.00 74.67           C  
ANISOU 6074  CA  VAL B1149     8951  10652   8768  -1118    635   1699       C  
ATOM   6075  C   VAL B1149     -18.988  12.068 -26.524  1.00 81.29           C  
ANISOU 6075  C   VAL B1149     9640  11578   9669  -1311    585   1844       C  
ATOM   6076  O   VAL B1149     -19.328  11.654 -25.417  1.00 81.15           O  
ANISOU 6076  O   VAL B1149     9533  11573   9726  -1250    681   1968       O  
ATOM   6077  CB  VAL B1149     -17.620  14.290 -26.524  1.00 77.42           C  
ANISOU 6077  CB  VAL B1149     9181  11156   9079   -914    613   1728       C  
ATOM   6078  CG1 VAL B1149     -18.391  14.733 -25.277  1.00 77.21           C  
ANISOU 6078  CG1 VAL B1149     8965  11281   9089   -760    660   1882       C  
ATOM   6079  CG2 VAL B1149     -16.195  14.839 -26.480  1.00 75.64           C  
ANISOU 6079  CG2 VAL B1149     9077  10817   8847   -745    677   1592       C  
ATOM   6080  N   ILE B1150     -19.746  11.914 -27.629  1.00 80.18           N  
ANISOU 6080  N   ILE B1150     9475  11493   9498  -1551    435   1830       N  
ATOM   6081  CA  ILE B1150     -21.047  11.238 -27.650  1.00 82.68           C  
ANISOU 6081  CA  ILE B1150     9623  11887   9904  -1792    351   1951       C  
ATOM   6082  C   ILE B1150     -20.880   9.763 -27.239  1.00 87.85           C  
ANISOU 6082  C   ILE B1150    10404  12313  10662  -1946    453   1931       C  
ATOM   6083  O   ILE B1150     -21.694   9.253 -26.468  1.00 89.14           O  
ANISOU 6083  O   ILE B1150    10400  12509  10959  -2015    510   2094       O  
ATOM   6084  CB  ILE B1150     -21.752  11.453 -29.029  1.00 87.72           C  
ANISOU 6084  CB  ILE B1150    10229  12643  10457  -2017    116   1910       C  
ATOM   6085  CG1 ILE B1150     -22.782  12.595 -28.961  1.00 88.66           C  
ANISOU 6085  CG1 ILE B1150    10040  13056  10593  -1918     19   2094       C  
ATOM   6086  CG2 ILE B1150     -22.382  10.181 -29.621  1.00 91.62           C  
ANISOU 6086  CG2 ILE B1150    10769  13041  11002  -2387     -4   1858       C  
ATOM   6087  CD1 ILE B1150     -22.265  13.954 -29.339  1.00 93.25           C  
ANISOU 6087  CD1 ILE B1150    10662  13718  11050  -1679     13   2069       C  
ATOM   6088  N   THR B1151     -19.795   9.111 -27.712  1.00 84.00           N  
ANISOU 6088  N   THR B1151    10209  11582  10124  -1972    508   1749       N  
ATOM   6089  CA  THR B1151     -19.449   7.719 -27.406  1.00 85.24           C  
ANISOU 6089  CA  THR B1151    10540  11469  10379  -2080    630   1716       C  
ATOM   6090  C   THR B1151     -19.160   7.566 -25.901  1.00 88.53           C  
ANISOU 6090  C   THR B1151    10890  11867  10882  -1842    815   1873       C  
ATOM   6091  O   THR B1151     -19.526   6.547 -25.308  1.00 89.60           O  
ANISOU 6091  O   THR B1151    11029  11874  11141  -1940    914   1978       O  
ATOM   6092  CB  THR B1151     -18.296   7.254 -28.311  1.00 93.29           C  
ANISOU 6092  CB  THR B1151    11885  12250  11313  -2099    668   1490       C  
ATOM   6093  OG1 THR B1151     -18.636   7.539 -29.670  1.00 94.60           O  
ANISOU 6093  OG1 THR B1151    12123  12478  11343  -2291    491   1359       O  
ATOM   6094  CG2 THR B1151     -17.991   5.768 -28.165  1.00 93.56           C  
ANISOU 6094  CG2 THR B1151    12128  11966  11453  -2223    797   1443       C  
ATOM   6095  N   THR B1152     -18.554   8.608 -25.286  1.00 83.02           N  
ANISOU 6095  N   THR B1152    10134  11299  10112  -1536    854   1894       N  
ATOM   6096  CA  THR B1152     -18.238   8.663 -23.853  1.00 82.16           C  
ANISOU 6096  CA  THR B1152     9978  11218  10020  -1276    992   2024       C  
ATOM   6097  C   THR B1152     -19.531   8.652 -23.022  1.00 87.26           C  
ANISOU 6097  C   THR B1152    10399  12023  10733  -1305   1039   2250       C  
ATOM   6098  O   THR B1152     -19.611   7.902 -22.052  1.00 88.02           O  
ANISOU 6098  O   THR B1152    10513  12046  10886  -1251   1183   2390       O  
ATOM   6099  CB  THR B1152     -17.336   9.873 -23.527  1.00 87.11           C  
ANISOU 6099  CB  THR B1152    10600  11949  10546   -986    979   1951       C  
ATOM   6100  OG1 THR B1152     -16.351  10.037 -24.551  1.00 87.26           O  
ANISOU 6100  OG1 THR B1152    10769  11854  10530  -1007    934   1760       O  
ATOM   6101  CG2 THR B1152     -16.662   9.756 -22.167  1.00 83.92           C  
ANISOU 6101  CG2 THR B1152    10231  11532  10124   -721   1087   2023       C  
ATOM   6102  N   PHE B1153     -20.542   9.459 -23.415  1.00 83.82           N  
ANISOU 6102  N   PHE B1153     9748  11802  10296  -1378    933   2305       N  
ATOM   6103  CA  PHE B1153     -21.830   9.508 -22.721  1.00 85.26           C  
ANISOU 6103  CA  PHE B1153     9673  12153  10570  -1404    994   2535       C  
ATOM   6104  C   PHE B1153     -22.596   8.201 -22.920  1.00 92.58           C  
ANISOU 6104  C   PHE B1153    10558  12953  11666  -1728   1011   2621       C  
ATOM   6105  O   PHE B1153     -23.093   7.631 -21.949  1.00 93.45           O  
ANISOU 6105  O   PHE B1153    10584  13048  11875  -1712   1179   2818       O  
ATOM   6106  CB  PHE B1153     -22.686  10.696 -23.199  1.00 86.87           C  
ANISOU 6106  CB  PHE B1153     9640  12612  10755  -1389    871   2580       C  
ATOM   6107  CG  PHE B1153     -22.215  12.085 -22.830  1.00 86.04           C  
ANISOU 6107  CG  PHE B1153     9534  12633  10522  -1068    889   2540       C  
ATOM   6108  CD1 PHE B1153     -21.983  12.432 -21.501  1.00 88.38           C  
ANISOU 6108  CD1 PHE B1153     9844  12973  10763   -783   1053   2617       C  
ATOM   6109  CD2 PHE B1153     -22.099  13.075 -23.798  1.00 86.87           C  
ANISOU 6109  CD2 PHE B1153     9630  12817  10561  -1055    743   2437       C  
ATOM   6110  CE1 PHE B1153     -21.586  13.730 -21.157  1.00 87.68           C  
ANISOU 6110  CE1 PHE B1153     9772  12979  10565   -511   1059   2554       C  
ATOM   6111  CE2 PHE B1153     -21.703  14.372 -23.453  1.00 88.00           C  
ANISOU 6111  CE2 PHE B1153     9777  13041  10618   -777    773   2402       C  
ATOM   6112  CZ  PHE B1153     -21.445  14.689 -22.136  1.00 85.64           C  
ANISOU 6112  CZ  PHE B1153     9498  12762  10277   -517    924   2445       C  
ATOM   6113  N   ARG B1154     -22.661   7.723 -24.180  1.00 90.79           N  
ANISOU 6113  N   ARG B1154    10411  12620  11463  -2026    845   2468       N  
ATOM   6114  CA  ARG B1154     -23.360   6.502 -24.593  1.00 93.91           C  
ANISOU 6114  CA  ARG B1154    10795  12863  12023  -2397    810   2488       C  
ATOM   6115  C   ARG B1154     -22.899   5.223 -23.856  1.00 98.49           C  
ANISOU 6115  C   ARG B1154    11565  13149  12708  -2413   1021   2539       C  
ATOM   6116  O   ARG B1154     -23.742   4.416 -23.454  1.00100.37           O  
ANISOU 6116  O   ARG B1154    11681  13321  13135  -2611   1105   2702       O  
ATOM   6117  CB  ARG B1154     -23.256   6.324 -26.122  1.00 94.91           C  
ANISOU 6117  CB  ARG B1154    11067  12914  12079  -2667    578   2250       C  
ATOM   6118  CG  ARG B1154     -24.229   5.309 -26.713  1.00108.83           C  
ANISOU 6118  CG  ARG B1154    12765  14582  14003  -3103    456   2244       C  
ATOM   6119  CD  ARG B1154     -23.517   4.240 -27.521  1.00121.06           C  
ANISOU 6119  CD  ARG B1154    14688  15791  15518  -3310    436   1997       C  
ATOM   6120  NE  ARG B1154     -23.015   4.751 -28.799  1.00131.71           N  
ANISOU 6120  NE  ARG B1154    16226  17176  16640  -3332    248   1757       N  
ATOM   6121  CZ  ARG B1154     -22.598   3.986 -29.805  1.00149.54           C  
ANISOU 6121  CZ  ARG B1154    18805  19193  18819  -3546    179   1511       C  
ATOM   6122  NH1 ARG B1154     -22.626   2.662 -29.699  1.00137.71           N  
ANISOU 6122  NH1 ARG B1154    17477  17375  17473  -3772    272   1457       N  
ATOM   6123  NH2 ARG B1154     -22.157   4.539 -30.927  1.00138.11           N  
ANISOU 6123  NH2 ARG B1154    17532  17807  17135  -3530     36   1320       N  
ATOM   6124  N   THR B1155     -21.579   5.050 -23.680  1.00 93.26           N  
ANISOU 6124  N   THR B1155    11181  12312  11942  -2201   1113   2421       N  
ATOM   6125  CA  THR B1155     -21.009   3.851 -23.058  1.00 94.18           C  
ANISOU 6125  CA  THR B1155    11505  12135  12145  -2173   1309   2472       C  
ATOM   6126  C   THR B1155     -20.555   4.012 -21.605  1.00 96.56           C  
ANISOU 6126  C   THR B1155    11800  12493  12394  -1812   1501   2660       C  
ATOM   6127  O   THR B1155     -20.702   3.074 -20.818  1.00 98.18           O  
ANISOU 6127  O   THR B1155    12055  12543  12706  -1814   1683   2837       O  
ATOM   6128  CB  THR B1155     -19.880   3.272 -23.930  1.00103.66           C  
ANISOU 6128  CB  THR B1155    13031  13057  13298  -2211   1290   2226       C  
ATOM   6129  OG1 THR B1155     -18.855   4.256 -24.098  1.00 99.17           O  
ANISOU 6129  OG1 THR B1155    12521  12603  12558  -1936   1241   2099       O  
ATOM   6130  CG2 THR B1155     -20.374   2.767 -25.289  1.00105.28           C  
ANISOU 6130  CG2 THR B1155    13323  13139  13542  -2603   1131   2039       C  
ATOM   6131  N   GLY B1156     -19.979   5.167 -21.273  1.00 89.87           N  
ANISOU 6131  N   GLY B1156    10919  11851  11378  -1511   1456   2617       N  
ATOM   6132  CA  GLY B1156     -19.430   5.434 -19.948  1.00 88.76           C  
ANISOU 6132  CA  GLY B1156    10806  11785  11133  -1156   1586   2745       C  
ATOM   6133  C   GLY B1156     -18.023   4.886 -19.821  1.00 92.38           C  
ANISOU 6133  C   GLY B1156    11514  12034  11552   -988   1629   2653       C  
ATOM   6134  O   GLY B1156     -17.490   4.782 -18.713  1.00 92.28           O  
ANISOU 6134  O   GLY B1156    11563  12036  11462   -715   1728   2773       O  
ATOM   6135  N   THR B1157     -17.423   4.514 -20.971  1.00 88.69           N  
ANISOU 6135  N   THR B1157    11194  11374  11129  -1140   1558   2446       N  
ATOM   6136  CA  THR B1157     -16.074   3.961 -21.095  1.00 88.00           C  
ANISOU 6136  CA  THR B1157    11327  11065  11042   -999   1609   2343       C  
ATOM   6137  C   THR B1157     -15.168   4.933 -21.860  1.00 88.71           C  
ANISOU 6137  C   THR B1157    11431  11237  11040   -903   1481   2121       C  
ATOM   6138  O   THR B1157     -15.657   5.843 -22.541  1.00 86.85           O  
ANISOU 6138  O   THR B1157    11083  11167  10747  -1011   1354   2029       O  
ATOM   6139  CB  THR B1157     -16.108   2.581 -21.797  1.00 99.49           C  
ANISOU 6139  CB  THR B1157    12980  12173  12648  -1249   1697   2295       C  
ATOM   6140  OG1 THR B1157     -16.668   2.719 -23.104  1.00101.13           O  
ANISOU 6140  OG1 THR B1157    13189  12370  12865  -1560   1566   2114       O  
ATOM   6141  CG2 THR B1157     -16.876   1.527 -21.012  1.00100.36           C  
ANISOU 6141  CG2 THR B1157    13096  12143  12892  -1345   1857   2529       C  
ATOM   6142  N   TRP B1158     -13.845   4.708 -21.768  1.00 84.60           N  
ANISOU 6142  N   TRP B1158    11035  10588  10520   -700   1527   2055       N  
ATOM   6143  CA  TRP B1158     -12.825   5.510 -22.446  1.00 82.38           C  
ANISOU 6143  CA  TRP B1158    10762  10346  10194   -599   1450   1865       C  
ATOM   6144  C   TRP B1158     -12.519   4.993 -23.862  1.00 87.07           C  
ANISOU 6144  C   TRP B1158    11531  10720  10834   -793   1481   1682       C  
ATOM   6145  O   TRP B1158     -11.600   5.498 -24.515  1.00 85.74           O  
ANISOU 6145  O   TRP B1158    11394  10539  10643   -712   1470   1538       O  
ATOM   6146  CB  TRP B1158     -11.549   5.559 -21.591  1.00 80.45           C  
ANISOU 6146  CB  TRP B1158    10519  10100   9949   -276   1476   1901       C  
ATOM   6147  CG  TRP B1158     -11.695   6.397 -20.359  1.00 80.43           C  
ANISOU 6147  CG  TRP B1158    10370  10354   9836    -72   1398   2007       C  
ATOM   6148  CD1 TRP B1158     -11.724   5.962 -19.068  1.00 84.50           C  
ANISOU 6148  CD1 TRP B1158    10895  10909  10304    114   1447   2196       C  
ATOM   6149  CD2 TRP B1158     -11.870   7.818 -20.309  1.00 78.53           C  
ANISOU 6149  CD2 TRP B1158     9986  10354   9500    -27   1268   1928       C  
ATOM   6150  NE1 TRP B1158     -11.879   7.029 -18.212  1.00 83.15           N  
ANISOU 6150  NE1 TRP B1158    10608  10997   9988    274   1349   2217       N  
ATOM   6151  CE2 TRP B1158     -11.977   8.180 -18.949  1.00 82.82           C  
ANISOU 6151  CE2 TRP B1158    10470  11068   9931    187   1242   2048       C  
ATOM   6152  CE3 TRP B1158     -11.936   8.826 -21.284  1.00 78.23           C  
ANISOU 6152  CE3 TRP B1158     9883  10388   9450   -135   1183   1772       C  
ATOM   6153  CZ2 TRP B1158     -12.150   9.508 -18.540  1.00 81.14           C  
ANISOU 6153  CZ2 TRP B1158    10147  11075   9606    286   1137   1991       C  
ATOM   6154  CZ3 TRP B1158     -12.107  10.138 -20.877  1.00 78.50           C  
ANISOU 6154  CZ3 TRP B1158     9793  10635   9400    -33   1085   1742       C  
ATOM   6155  CH2 TRP B1158     -12.204  10.470 -19.522  1.00 79.47           C  
ANISOU 6155  CH2 TRP B1158     9869  10904   9424    171   1064   1837       C  
ATOM   6156  N   ASP B1159     -13.313   4.005 -24.331  1.00 85.53           N  
ANISOU 6156  N   ASP B1159    11453  10347  10697  -1058   1527   1685       N  
ATOM   6157  CA  ASP B1159     -13.226   3.309 -25.619  1.00 86.81           C  
ANISOU 6157  CA  ASP B1159    11838  10267  10877  -1281   1560   1503       C  
ATOM   6158  C   ASP B1159     -12.962   4.161 -26.864  1.00 88.90           C  
ANISOU 6158  C   ASP B1159    12137  10620  11019  -1345   1464   1303       C  
ATOM   6159  O   ASP B1159     -12.231   3.718 -27.754  1.00 89.52           O  
ANISOU 6159  O   ASP B1159    12435  10493  11087  -1363   1554   1145       O  
ATOM   6160  CB  ASP B1159     -14.451   2.405 -25.818  1.00 91.45           C  
ANISOU 6160  CB  ASP B1159    12480  10731  11536  -1610   1550   1539       C  
ATOM   6161  CG  ASP B1159     -14.521   1.205 -24.885  1.00106.46           C  
ANISOU 6161  CG  ASP B1159    14456  12403  13589  -1581   1719   1713       C  
ATOM   6162  OD1 ASP B1159     -13.709   1.141 -23.926  1.00106.94           O  
ANISOU 6162  OD1 ASP B1159    14502  12458  13672  -1270   1824   1842       O  
ATOM   6163  OD2 ASP B1159     -15.395   0.338 -25.101  1.00115.32           O  
ANISOU 6163  OD2 ASP B1159    15647  13356  14813  -1871   1739   1729       O  
ATOM   6164  N   ALA B1160     -13.529   5.379 -26.915  1.00 82.85           N  
ANISOU 6164  N   ALA B1160    11171  10149  10160  -1356   1309   1323       N  
ATOM   6165  CA  ALA B1160     -13.359   6.310 -28.034  1.00 81.06           C  
ANISOU 6165  CA  ALA B1160    10964  10030   9807  -1398   1220   1179       C  
ATOM   6166  C   ALA B1160     -11.963   6.941 -28.103  1.00 81.65           C  
ANISOU 6166  C   ALA B1160    11048  10094   9882  -1142   1305   1111       C  
ATOM   6167  O   ALA B1160     -11.593   7.464 -29.157  1.00 81.41           O  
ANISOU 6167  O   ALA B1160    11100  10068   9763  -1171   1302    986       O  
ATOM   6168  CB  ALA B1160     -14.414   7.401 -27.961  1.00 80.90           C  
ANISOU 6168  CB  ALA B1160    10714  10310   9716  -1457   1047   1259       C  
ATOM   6169  N   TYR B1161     -11.192   6.880 -26.999  1.00 76.13           N  
ANISOU 6169  N   TYR B1161    10261   9382   9283   -897   1378   1203       N  
ATOM   6170  CA  TYR B1161      -9.858   7.476 -26.877  1.00 85.58           C  
ANISOU 6170  CA  TYR B1161    11401  10587  10528   -656   1433   1160       C  
ATOM   6171  C   TYR B1161      -8.707   6.469 -26.782  1.00101.44           C  
ANISOU 6171  C   TYR B1161    13532  12351  12659   -511   1605   1147       C  
ATOM   6172  O   TYR B1161      -8.910   5.294 -26.479  1.00 63.69           O  
ANISOU 6172  O   TYR B1161     8876   7390   7933   -544   1689   1206       O  
ATOM   6173  CB  TYR B1161      -9.829   8.471 -25.701  1.00 84.90           C  
ANISOU 6173  CB  TYR B1161    11081  10733  10445   -474   1326   1259       C  
ATOM   6174  CG  TYR B1161     -10.749   9.660 -25.897  1.00 84.80           C  
ANISOU 6174  CG  TYR B1161    10944  10943  10332   -561   1192   1260       C  
ATOM   6175  CD1 TYR B1161     -10.286  10.836 -26.480  1.00 85.65           C  
ANISOU 6175  CD1 TYR B1161    10994  11132  10419   -518   1157   1175       C  
ATOM   6176  CD2 TYR B1161     -12.085   9.608 -25.507  1.00 85.52           C  
ANISOU 6176  CD2 TYR B1161    10967  11154  10371   -676   1120   1367       C  
ATOM   6177  CE1 TYR B1161     -11.133  11.924 -26.685  1.00 85.49           C  
ANISOU 6177  CE1 TYR B1161    10874  11294  10316   -574   1051   1195       C  
ATOM   6178  CE2 TYR B1161     -12.944  10.685 -25.718  1.00 85.47           C  
ANISOU 6178  CE2 TYR B1161    10835  11351  10291   -729   1011   1388       C  
ATOM   6179  CZ  TYR B1161     -12.461  11.847 -26.300  1.00 91.02           C  
ANISOU 6179  CZ  TYR B1161    11502  12119  10962   -667    974   1302       C  
ATOM   6180  OH  TYR B1161     -13.289  12.926 -26.502  1.00 89.61           O  
ANISOU 6180  OH  TYR B1161    11208  12120  10720   -691    881   1341       O  
ATOM   6181  N   LYS B 236     -16.716   0.274 -14.830  1.00 97.00           N  
ANISOU 6181  N   LYS B 236    14372  14009   8474   1248    394   -299       N  
ATOM   6182  CA  LYS B 236     -16.447  -0.024 -13.424  1.00 94.43           C  
ANISOU 6182  CA  LYS B 236    14057  13355   8468   1136    466   -307       C  
ATOM   6183  C   LYS B 236     -17.045   1.036 -12.479  1.00 95.73           C  
ANISOU 6183  C   LYS B 236    13748  13629   8996    983    411   -127       C  
ATOM   6184  O   LYS B 236     -16.569   2.178 -12.459  1.00 93.61           O  
ANISOU 6184  O   LYS B 236    13151  13498   8920   1207    512    140       O  
ATOM   6185  CB  LYS B 236     -14.936  -0.205 -13.184  1.00 95.64           C  
ANISOU 6185  CB  LYS B 236    14359  13277   8704   1497    719   -174       C  
ATOM   6186  N   ALA B 237     -18.103   0.650 -11.713  1.00 91.77           N  
ANISOU 6186  N   ALA B 237    13227  13057   8583    606    260   -267       N  
ATOM   6187  CA  ALA B 237     -18.828   1.497 -10.749  1.00 89.14           C  
ANISOU 6187  CA  ALA B 237    12506  12798   8563    437    211   -123       C  
ATOM   6188  C   ALA B 237     -18.095   1.933  -9.483  1.00 89.74           C  
ANISOU 6188  C   ALA B 237    12451  12654   8993    536    362     13       C  
ATOM   6189  O   ALA B 237     -17.555   1.084  -8.776  1.00 89.49           O  
ANISOU 6189  O   ALA B 237    12660  12328   9013    515    428    -98       O  
ATOM   6190  CB  ALA B 237     -20.001   0.731 -10.158  1.00 90.78           C  
ANISOU 6190  CB  ALA B 237    12794  12928   8771     32     34   -305       C  
ATOM   6191  N   LEU B 238     -18.067   3.249  -9.199  1.00 83.71           N  
ANISOU 6191  N   LEU B 238    11312  12032   8462    641    424    254       N  
ATOM   6192  CA  LEU B 238     -17.364   3.788  -8.033  1.00 80.63           C  
ANISOU 6192  CA  LEU B 238    10792  11456   8389    716    552    383       C  
ATOM   6193  C   LEU B 238     -18.164   4.440  -6.893  1.00 82.48           C  
ANISOU 6193  C   LEU B 238    10780  11670   8888    522    522    447       C  
ATOM   6194  O   LEU B 238     -17.731   4.373  -5.745  1.00 80.30           O  
ANISOU 6194  O   LEU B 238    10524  11176   8809    489    584    444       O  
ATOM   6195  CB  LEU B 238     -16.379   4.798  -8.654  1.00 80.18           C  
ANISOU 6195  CB  LEU B 238    10558  11520   8386   1044    687    621       C  
ATOM   6196  CG  LEU B 238     -15.145   5.169  -7.834  1.00 82.92           C  
ANISOU 6196  CG  LEU B 238    10858  11677   8971   1196    832    764       C  
ATOM   6197  CD1 LEU B 238     -14.039   4.124  -7.982  1.00 83.67           C  
ANISOU 6197  CD1 LEU B 238    11263  11599   8928   1353    917    710       C  
ATOM   6198  CD2 LEU B 238     -14.629   6.536  -8.233  1.00 85.18           C  
ANISOU 6198  CD2 LEU B 238    10842  12116   9408   1414    928   1036       C  
ATOM   6199  N   LYS B 239     -19.302   5.089  -7.203  1.00 79.55           N  
ANISOU 6199  N   LYS B 239    10174  11539   8512    413    443    526       N  
ATOM   6200  CA  LYS B 239     -20.152   5.770  -6.215  1.00 78.06           C  
ANISOU 6200  CA  LYS B 239     9755  11352   8552    265    443    622       C  
ATOM   6201  C   LYS B 239     -20.727   4.885  -5.090  1.00 79.77           C  
ANISOU 6201  C   LYS B 239    10104  11368   8836      9    364    469       C  
ATOM   6202  O   LYS B 239     -20.658   5.334  -3.943  1.00 77.53           O  
ANISOU 6202  O   LYS B 239     9733  10942   8785     -6    440    529       O  
ATOM   6203  CB  LYS B 239     -21.244   6.618  -6.882  1.00 82.55           C  
ANISOU 6203  CB  LYS B 239    10036  12249   9079    237    405    790       C  
ATOM   6204  CG  LYS B 239     -20.707   7.857  -7.590  1.00101.57           C  
ANISOU 6204  CG  LYS B 239    12218  14823  11549    513    544   1017       C  
ATOM   6205  CD  LYS B 239     -21.796   8.534  -8.404  1.00113.91           C  
ANISOU 6205  CD  LYS B 239    13506  16751  13023    500    514   1193       C  
ATOM   6206  CE  LYS B 239     -21.329   9.814  -9.049  1.00121.38           C  
ANISOU 6206  CE  LYS B 239    14200  17855  14063    783    680   1446       C  
ATOM   6207  NZ  LYS B 239     -22.460  10.548  -9.677  1.00129.54           N  
ANISOU 6207  NZ  LYS B 239    14926  19250  15044    777    687   1664       N  
ATOM   6208  N   PRO B 240     -21.270   3.653  -5.350  1.00 76.44           N  
ANISOU 6208  N   PRO B 240     9901  10919   8224   -193    221    275       N  
ATOM   6209  CA  PRO B 240     -21.779   2.820  -4.240  1.00 75.61           C  
ANISOU 6209  CA  PRO B 240     9902  10610   8217   -422    163    157       C  
ATOM   6210  C   PRO B 240     -20.703   2.468  -3.201  1.00 76.77           C  
ANISOU 6210  C   PRO B 240    10195  10454   8519   -327    290    103       C  
ATOM   6211  O   PRO B 240     -20.990   2.432  -2.005  1.00 74.69           O  
ANISOU 6211  O   PRO B 240     9878  10062   8437   -425    307    114       O  
ATOM   6212  CB  PRO B 240     -22.296   1.564  -4.950  1.00 79.97           C  
ANISOU 6212  CB  PRO B 240    10703  11168   8515   -626      2    -48       C  
ATOM   6213  CG  PRO B 240     -22.519   1.975  -6.344  1.00 86.10           C  
ANISOU 6213  CG  PRO B 240    11408  12243   9063   -566    -64      0       C  
ATOM   6214  CD  PRO B 240     -21.441   2.952  -6.636  1.00 80.19           C  
ANISOU 6214  CD  PRO B 240    10550  11532   8385   -232    107    149       C  
ATOM   6215  N   THR B 241     -19.461   2.249  -3.675  1.00 72.65           N  
ANISOU 6215  N   THR B 241     9839   9849   7916   -118    386     76       N  
ATOM   6216  CA  THR B 241     -18.268   1.938  -2.886  1.00 70.57           C  
ANISOU 6216  CA  THR B 241     9696   9355   7763      8    519     76       C  
ATOM   6217  C   THR B 241     -17.961   3.069  -1.890  1.00 70.70           C  
ANISOU 6217  C   THR B 241     9467   9358   8037     68    601    241       C  
ATOM   6218  O   THR B 241     -17.796   2.807  -0.697  1.00 68.75           O  
ANISOU 6218  O   THR B 241     9242   8949   7930      0    636    219       O  
ATOM   6219  CB  THR B 241     -17.112   1.667  -3.866  1.00 80.58           C  
ANISOU 6219  CB  THR B 241    11139  10616   8863    252    608     86       C  
ATOM   6220  OG1 THR B 241     -17.408   0.491  -4.621  1.00 84.10           O  
ANISOU 6220  OG1 THR B 241    11883  11012   9058    174    544   -108       O  
ATOM   6221  CG2 THR B 241     -15.753   1.553  -3.184  1.00 77.72           C  
ANISOU 6221  CG2 THR B 241    10834  10083   8612    426    762    175       C  
ATOM   6222  N   VAL B 242     -17.905   4.318  -2.395  1.00 66.19           N  
ANISOU 6222  N   VAL B 242     8674   8957   7519    191    636    404       N  
ATOM   6223  CA  VAL B 242     -17.625   5.542  -1.638  1.00 63.97           C  
ANISOU 6223  CA  VAL B 242     8180   8659   7465    246    721    558       C  
ATOM   6224  C   VAL B 242     -18.721   5.815  -0.593  1.00 66.24           C  
ANISOU 6224  C   VAL B 242     8364   8915   7889     64    689    550       C  
ATOM   6225  O   VAL B 242     -18.398   6.109   0.558  1.00 63.67           O  
ANISOU 6225  O   VAL B 242     8020   8448   7723     40    746    566       O  
ATOM   6226  CB  VAL B 242     -17.364   6.749  -2.585  1.00 67.99           C  
ANISOU 6226  CB  VAL B 242     8494   9348   7992    428    782    739       C  
ATOM   6227  CG1 VAL B 242     -17.088   8.029  -1.806  1.00 66.76           C  
ANISOU 6227  CG1 VAL B 242     8153   9134   8078    461    879    884       C  
ATOM   6228  CG2 VAL B 242     -16.213   6.459  -3.542  1.00 68.24           C  
ANISOU 6228  CG2 VAL B 242     8627   9408   7895    641    828    778       C  
ATOM   6229  N   ILE B 243     -20.004   5.684  -0.982  1.00 64.61           N  
ANISOU 6229  N   ILE B 243     8093   8851   7605    -64    597    537       N  
ATOM   6230  CA  ILE B 243     -21.133   5.880  -0.064  1.00 64.61           C  
ANISOU 6230  CA  ILE B 243     7987   8844   7719   -216    576    571       C  
ATOM   6231  C   ILE B 243     -21.070   4.839   1.073  1.00 69.40           C  
ANISOU 6231  C   ILE B 243     8757   9238   8374   -342    547    433       C  
ATOM   6232  O   ILE B 243     -21.113   5.227   2.239  1.00 67.97           O  
ANISOU 6232  O   ILE B 243     8527   8950   8349   -356    610    470       O  
ATOM   6233  CB  ILE B 243     -22.517   5.948  -0.793  1.00 69.21           C  
ANISOU 6233  CB  ILE B 243     8428   9670   8198   -328    478    644       C  
ATOM   6234  CG1 ILE B 243     -22.560   7.145  -1.779  1.00 70.07           C  
ANISOU 6234  CG1 ILE B 243     8328  10006   8288   -169    548    828       C  
ATOM   6235  CG2 ILE B 243     -23.689   6.037   0.217  1.00 69.25           C  
ANISOU 6235  CG2 ILE B 243     8324   9667   8322   -471    467    717       C  
ATOM   6236  CD1 ILE B 243     -23.488   6.984  -2.992  1.00 79.27           C  
ANISOU 6236  CD1 ILE B 243     9392  11475   9253   -240    432    882       C  
ATOM   6237  N   LEU B 244     -20.892   3.539   0.728  1.00 67.60           N  
ANISOU 6237  N   LEU B 244     8739   8938   8008   -415    473    277       N  
ATOM   6238  CA  LEU B 244     -20.778   2.420   1.675  1.00 67.27           C  
ANISOU 6238  CA  LEU B 244     8862   8692   8006   -517    466    155       C  
ATOM   6239  C   LEU B 244     -19.700   2.677   2.733  1.00 70.13           C  
ANISOU 6239  C   LEU B 244     9237   8905   8506   -405    588    186       C  
ATOM   6240  O   LEU B 244     -19.986   2.565   3.923  1.00 69.02           O  
ANISOU 6240  O   LEU B 244     9067   8672   8485   -476    606    187       O  
ATOM   6241  CB  LEU B 244     -20.504   1.099   0.913  1.00 68.89           C  
ANISOU 6241  CB  LEU B 244     9329   8820   8026   -561    415     -9       C  
ATOM   6242  CG  LEU B 244     -20.362  -0.209   1.706  1.00 73.55           C  
ANISOU 6242  CG  LEU B 244    10120   9182   8643   -655    432   -135       C  
ATOM   6243  CD1 LEU B 244     -21.642  -0.558   2.462  1.00 74.06           C  
ANISOU 6243  CD1 LEU B 244    10102   9236   8803   -875    339   -141       C  
ATOM   6244  CD2 LEU B 244     -19.999  -1.346   0.780  1.00 77.39           C  
ANISOU 6244  CD2 LEU B 244    10899   9576   8930   -661    420   -290       C  
ATOM   6245  N   ILE B 245     -18.489   3.067   2.293  1.00 66.72           N  
ANISOU 6245  N   ILE B 245     8827   8473   8050   -232    665    236       N  
ATOM   6246  CA  ILE B 245     -17.343   3.366   3.146  1.00 65.45           C  
ANISOU 6246  CA  ILE B 245     8658   8215   7996   -139    761    297       C  
ATOM   6247  C   ILE B 245     -17.557   4.612   4.028  1.00 69.68           C  
ANISOU 6247  C   ILE B 245     9017   8762   8697   -159    794    389       C  
ATOM   6248  O   ILE B 245     -17.277   4.547   5.230  1.00 68.89           O  
ANISOU 6248  O   ILE B 245     8927   8562   8685   -202    825    380       O  
ATOM   6249  CB  ILE B 245     -16.031   3.331   2.321  1.00 68.74           C  
ANISOU 6249  CB  ILE B 245     9142   8648   8328     46    827    360       C  
ATOM   6250  CG1 ILE B 245     -15.501   1.885   2.247  1.00 70.01           C  
ANISOU 6250  CG1 ILE B 245     9540   8688   8373     74    864    271       C  
ATOM   6251  CG2 ILE B 245     -14.956   4.271   2.869  1.00 68.39           C  
ANISOU 6251  CG2 ILE B 245     8976   8597   8410    137    899    504       C  
ATOM   6252  CD1 ILE B 245     -15.062   1.436   0.887  1.00 77.73           C  
ANISOU 6252  CD1 ILE B 245    10669   9704   9162    214    886    256       C  
ATOM   6253  N   LEU B 246     -18.089   5.716   3.454  1.00 67.06           N  
ANISOU 6253  N   LEU B 246     8536   8547   8395   -127    798    478       N  
ATOM   6254  CA  LEU B 246     -18.381   6.947   4.210  1.00 66.40           C  
ANISOU 6254  CA  LEU B 246     8324   8445   8460   -135    859    563       C  
ATOM   6255  C   LEU B 246     -19.470   6.714   5.247  1.00 70.74           C  
ANISOU 6255  C   LEU B 246     8870   8945   9062   -256    844    526       C  
ATOM   6256  O   LEU B 246     -19.344   7.188   6.375  1.00 69.60           O  
ANISOU 6256  O   LEU B 246     8726   8702   9016   -274    899    532       O  
ATOM   6257  CB  LEU B 246     -18.784   8.106   3.285  1.00 66.93           C  
ANISOU 6257  CB  LEU B 246     8235   8647   8548    -51    901    692       C  
ATOM   6258  CG  LEU B 246     -17.654   8.805   2.552  1.00 71.66           C  
ANISOU 6258  CG  LEU B 246     8785   9276   9167     93    956    786       C  
ATOM   6259  CD1 LEU B 246     -18.195   9.667   1.445  1.00 72.66           C  
ANISOU 6259  CD1 LEU B 246     8753   9570   9283    188    995    915       C  
ATOM   6260  CD2 LEU B 246     -16.815   9.648   3.503  1.00 73.48           C  
ANISOU 6260  CD2 LEU B 246     9002   9368   9547     90   1026    829       C  
ATOM   6261  N   ALA B 247     -20.521   5.956   4.868  1.00 68.85           N  
ANISOU 6261  N   ALA B 247     8632   8778   8747   -345    763    493       N  
ATOM   6262  CA  ALA B 247     -21.637   5.613   5.747  1.00 69.20           C  
ANISOU 6262  CA  ALA B 247     8652   8799   8842   -455    739    496       C  
ATOM   6263  C   ALA B 247     -21.169   4.722   6.899  1.00 73.90           C  
ANISOU 6263  C   ALA B 247     9369   9237   9474   -501    743    397       C  
ATOM   6264  O   ALA B 247     -21.601   4.935   8.032  1.00 73.61           O  
ANISOU 6264  O   ALA B 247     9303   9143   9523   -522    784    426       O  
ATOM   6265  CB  ALA B 247     -22.747   4.936   4.962  1.00 71.24           C  
ANISOU 6265  CB  ALA B 247     8875   9187   9004   -568    627    500       C  
ATOM   6266  N   PHE B 248     -20.257   3.764   6.623  1.00 70.95           N  
ANISOU 6266  N   PHE B 248     9130   8799   9029   -491    722    302       N  
ATOM   6267  CA  PHE B 248     -19.690   2.875   7.637  1.00 70.60           C  
ANISOU 6267  CA  PHE B 248     9186   8626   9014   -510    752    238       C  
ATOM   6268  C   PHE B 248     -18.878   3.668   8.650  1.00 73.35           C  
ANISOU 6268  C   PHE B 248     9497   8932   9441   -450    828    283       C  
ATOM   6269  O   PHE B 248     -19.013   3.436   9.851  1.00 72.16           O  
ANISOU 6269  O   PHE B 248     9350   8723   9346   -484    852    273       O  
ATOM   6270  CB  PHE B 248     -18.821   1.782   6.992  1.00 73.30           C  
ANISOU 6270  CB  PHE B 248     9686   8911   9253   -474    756    165       C  
ATOM   6271  CG  PHE B 248     -18.130   0.853   7.967  1.00 75.12           C  
ANISOU 6271  CG  PHE B 248    10006   9024   9511   -462    822    139       C  
ATOM   6272  CD1 PHE B 248     -18.734  -0.329   8.374  1.00 79.15           C  
ANISOU 6272  CD1 PHE B 248    10597   9443  10034   -553    810     72       C  
ATOM   6273  CD2 PHE B 248     -16.852   1.135   8.437  1.00 77.32           C  
ANISOU 6273  CD2 PHE B 248    10277   9298   9805   -363    899    205       C  
ATOM   6274  CE1 PHE B 248     -18.091  -1.193   9.263  1.00 80.20           C  
ANISOU 6274  CE1 PHE B 248    10796   9478  10198   -520    897     74       C  
ATOM   6275  CE2 PHE B 248     -16.211   0.272   9.332  1.00 80.15           C  
ANISOU 6275  CE2 PHE B 248    10689   9587  10177   -343    972    217       C  
ATOM   6276  CZ  PHE B 248     -16.833  -0.888   9.736  1.00 78.76           C  
ANISOU 6276  CZ  PHE B 248    10589   9318  10016   -407    982    152       C  
ATOM   6277  N   PHE B 249     -18.019   4.575   8.171  1.00 70.65           N  
ANISOU 6277  N   PHE B 249     9120   8625   9098   -369    859    338       N  
ATOM   6278  CA  PHE B 249     -17.185   5.390   9.045  1.00 70.56           C  
ANISOU 6278  CA  PHE B 249     9081   8576   9151   -352    908    378       C  
ATOM   6279  C   PHE B 249     -17.997   6.435   9.809  1.00 72.25           C  
ANISOU 6279  C   PHE B 249     9241   8764   9446   -387    942    397       C  
ATOM   6280  O   PHE B 249     -17.701   6.676  10.980  1.00 70.82           O  
ANISOU 6280  O   PHE B 249     9090   8524   9296   -421    968    378       O  
ATOM   6281  CB  PHE B 249     -16.008   5.999   8.278  1.00 73.36           C  
ANISOU 6281  CB  PHE B 249     9408   8970   9495   -270    925    454       C  
ATOM   6282  CG  PHE B 249     -14.738   5.179   8.335  1.00 76.15           C  
ANISOU 6282  CG  PHE B 249     9819   9320   9794   -224    939    484       C  
ATOM   6283  CD1 PHE B 249     -14.721   3.858   7.899  1.00 80.36           C  
ANISOU 6283  CD1 PHE B 249    10456   9838  10238   -188    944    440       C  
ATOM   6284  CD2 PHE B 249     -13.548   5.740   8.788  1.00 79.49           C  
ANISOU 6284  CD2 PHE B 249    10195   9756  10250   -218    956    576       C  
ATOM   6285  CE1 PHE B 249     -13.544   3.102   7.942  1.00 82.04           C  
ANISOU 6285  CE1 PHE B 249    10727  10045  10398   -110    999    505       C  
ATOM   6286  CE2 PHE B 249     -12.364   4.987   8.814  1.00 83.05           C  
ANISOU 6286  CE2 PHE B 249    10670  10239  10646   -157    985    662       C  
ATOM   6287  CZ  PHE B 249     -12.372   3.673   8.393  1.00 81.46           C  
ANISOU 6287  CZ  PHE B 249    10575  10019  10358    -85   1023    635       C  
ATOM   6288  N   ALA B 250     -19.062   6.989   9.177  1.00 68.26           N  
ANISOU 6288  N   ALA B 250     8666   8311   8957   -373    951    445       N  
ATOM   6289  CA  ALA B 250     -19.980   7.942   9.811  1.00 67.84           C  
ANISOU 6289  CA  ALA B 250     8573   8231   8972   -370   1023    498       C  
ATOM   6290  C   ALA B 250     -20.724   7.244  10.953  1.00 71.20           C  
ANISOU 6290  C   ALA B 250     9033   8615   9406   -418   1018    467       C  
ATOM   6291  O   ALA B 250     -20.912   7.843  12.008  1.00 70.81           O  
ANISOU 6291  O   ALA B 250     9018   8493   9394   -405   1089    473       O  
ATOM   6292  CB  ALA B 250     -20.976   8.475   8.796  1.00 69.16           C  
ANISOU 6292  CB  ALA B 250     8630   8506   9140   -329   1044    603       C  
ATOM   6293  N   CYS B 251     -21.130   5.974  10.738  1.00 67.34           N  
ANISOU 6293  N   CYS B 251     8546   8162   8879   -470    941    436       N  
ATOM   6294  CA  CYS B 251     -21.800   5.124  11.716  1.00 66.94           C  
ANISOU 6294  CA  CYS B 251     8507   8076   8851   -514    930    426       C  
ATOM   6295  C   CYS B 251     -20.914   5.022  12.968  1.00 69.05           C  
ANISOU 6295  C   CYS B 251     8847   8263   9126   -500    971    368       C  
ATOM   6296  O   CYS B 251     -21.367   5.329  14.069  1.00 68.78           O  
ANISOU 6296  O   CYS B 251     8818   8194   9120   -479   1025    390       O  
ATOM   6297  CB  CYS B 251     -22.065   3.743  11.114  1.00 68.06           C  
ANISOU 6297  CB  CYS B 251     8669   8237   8954   -592    839    382       C  
ATOM   6298  SG  CYS B 251     -23.791   3.439  10.645  1.00 73.25           S  
ANISOU 6298  SG  CYS B 251     9215   8993   9624   -681    768    483       S  
ATOM   6299  N   TRP B 252     -19.635   4.646  12.769  1.00 64.11           N  
ANISOU 6299  N   TRP B 252     8272   7627   8460   -500    953    314       N  
ATOM   6300  CA  TRP B 252     -18.636   4.468  13.815  1.00 62.61           C  
ANISOU 6300  CA  TRP B 252     8124   7412   8255   -500    977    288       C  
ATOM   6301  C   TRP B 252     -18.035   5.762  14.351  1.00 66.40           C  
ANISOU 6301  C   TRP B 252     8620   7874   8737   -506   1006    289       C  
ATOM   6302  O   TRP B 252     -17.405   5.719  15.410  1.00 65.64           O  
ANISOU 6302  O   TRP B 252     8551   7777   8611   -532   1014    269       O  
ATOM   6303  CB  TRP B 252     -17.528   3.527  13.337  1.00 60.79           C  
ANISOU 6303  CB  TRP B 252     7926   7198   7976   -486    963    282       C  
ATOM   6304  CG  TRP B 252     -17.863   2.072  13.454  1.00 61.80           C  
ANISOU 6304  CG  TRP B 252     8087   7293   8100   -494    968    260       C  
ATOM   6305  CD1 TRP B 252     -18.112   1.205  12.429  1.00 65.22           C  
ANISOU 6305  CD1 TRP B 252     8576   7700   8506   -503    944    229       C  
ATOM   6306  CD2 TRP B 252     -17.942   1.300  14.660  1.00 61.51           C  
ANISOU 6306  CD2 TRP B 252     8046   7239   8088   -496   1008    268       C  
ATOM   6307  NE1 TRP B 252     -18.359  -0.058  12.922  1.00 64.98           N  
ANISOU 6307  NE1 TRP B 252     8587   7607   8496   -524    972    211       N  
ATOM   6308  CE2 TRP B 252     -18.256  -0.029  14.289  1.00 66.01           C  
ANISOU 6308  CE2 TRP B 252     8663   7750   8667   -508   1017    248       C  
ATOM   6309  CE3 TRP B 252     -17.793   1.601  16.024  1.00 62.47           C  
ANISOU 6309  CE3 TRP B 252     8132   7388   8214   -489   1041    288       C  
ATOM   6310  CZ2 TRP B 252     -18.422  -1.049  15.235  1.00 65.54           C  
ANISOU 6310  CZ2 TRP B 252     8598   7655   8651   -501   1071    269       C  
ATOM   6311  CZ3 TRP B 252     -17.958   0.590  16.958  1.00 64.04           C  
ANISOU 6311  CZ3 TRP B 252     8314   7584   8436   -470   1087    311       C  
ATOM   6312  CH2 TRP B 252     -18.270  -0.715  16.564  1.00 65.13           C  
ANISOU 6312  CH2 TRP B 252     8477   7658   8610   -470   1108    312       C  
ATOM   6313  N   LEU B 253     -18.211   6.900  13.644  1.00 63.88           N  
ANISOU 6313  N   LEU B 253     8283   7541   8446   -489   1026    316       N  
ATOM   6314  CA  LEU B 253     -17.647   8.194  14.054  1.00 64.61           C  
ANISOU 6314  CA  LEU B 253     8416   7578   8555   -514   1062    310       C  
ATOM   6315  C   LEU B 253     -17.983   8.687  15.475  1.00 70.73           C  
ANISOU 6315  C   LEU B 253     9279   8282   9315   -540   1112    262       C  
ATOM   6316  O   LEU B 253     -17.032   9.027  16.180  1.00 70.83           O  
ANISOU 6316  O   LEU B 253     9345   8279   9287   -614   1088    219       O  
ATOM   6317  CB  LEU B 253     -17.820   9.301  12.988  1.00 64.80           C  
ANISOU 6317  CB  LEU B 253     8401   7586   8633   -474   1103    367       C  
ATOM   6318  CG  LEU B 253     -17.175  10.672  13.259  1.00 69.24           C  
ANISOU 6318  CG  LEU B 253     9016   8056   9235   -515   1149    365       C  
ATOM   6319  CD1 LEU B 253     -15.653  10.589  13.268  1.00 68.73           C  
ANISOU 6319  CD1 LEU B 253     8940   8024   9150   -589   1070    369       C  
ATOM   6320  CD2 LEU B 253     -17.650  11.696  12.254  1.00 71.61           C  
ANISOU 6320  CD2 LEU B 253     9264   8334   9609   -443   1230    446       C  
ATOM   6321  N   PRO B 254     -19.266   8.731  15.938  1.00 68.88           N  
ANISOU 6321  N   PRO B 254     9061   8016   9095   -482   1179    281       N  
ATOM   6322  CA  PRO B 254     -19.534   9.215  17.307  1.00 69.96           C  
ANISOU 6322  CA  PRO B 254     9310   8080   9192   -475   1245    237       C  
ATOM   6323  C   PRO B 254     -18.860   8.382  18.399  1.00 75.24           C  
ANISOU 6323  C   PRO B 254     9999   8802   9786   -524   1188    179       C  
ATOM   6324  O   PRO B 254     -18.383   8.953  19.380  1.00 75.63           O  
ANISOU 6324  O   PRO B 254    10155   8815   9765   -573   1198    111       O  
ATOM   6325  CB  PRO B 254     -21.062   9.157  17.417  1.00 71.94           C  
ANISOU 6325  CB  PRO B 254     9533   8324   9477   -370   1331    327       C  
ATOM   6326  CG  PRO B 254     -21.556   9.119  16.027  1.00 75.78           C  
ANISOU 6326  CG  PRO B 254     9901   8869  10023   -349   1315    416       C  
ATOM   6327  CD  PRO B 254     -20.526   8.365  15.262  1.00 70.43           C  
ANISOU 6327  CD  PRO B 254     9172   8256   9332   -419   1198    365       C  
ATOM   6328  N   TYR B 255     -18.797   7.043  18.205  1.00 72.39           N  
ANISOU 6328  N   TYR B 255     9542   8528   9434   -514   1135    210       N  
ATOM   6329  CA  TYR B 255     -18.152   6.096  19.119  1.00 72.75           C  
ANISOU 6329  CA  TYR B 255     9570   8648   9423   -535   1105    196       C  
ATOM   6330  C   TYR B 255     -16.670   6.442  19.273  1.00 78.76           C  
ANISOU 6330  C   TYR B 255    10347   9461  10118   -629   1049    173       C  
ATOM   6331  O   TYR B 255     -16.168   6.444  20.393  1.00 78.80           O  
ANISOU 6331  O   TYR B 255    10380   9521  10039   -673   1037    148       O  
ATOM   6332  CB  TYR B 255     -18.335   4.641  18.628  1.00 73.29           C  
ANISOU 6332  CB  TYR B 255     9550   8762   9534   -503   1086    245       C  
ATOM   6333  CG  TYR B 255     -17.570   3.613  19.437  1.00 75.22           C  
ANISOU 6333  CG  TYR B 255     9760   9086   9735   -502   1088    265       C  
ATOM   6334  CD1 TYR B 255     -18.028   3.195  20.683  1.00 77.70           C  
ANISOU 6334  CD1 TYR B 255    10062   9431  10032   -457   1131    281       C  
ATOM   6335  CD2 TYR B 255     -16.378   3.072  18.967  1.00 75.78           C  
ANISOU 6335  CD2 TYR B 255     9800   9216   9778   -523   1068    300       C  
ATOM   6336  CE1 TYR B 255     -17.321   2.260  21.439  1.00 78.94           C  
ANISOU 6336  CE1 TYR B 255    10161   9684  10147   -440   1152    326       C  
ATOM   6337  CE2 TYR B 255     -15.670   2.125  19.706  1.00 76.92           C  
ANISOU 6337  CE2 TYR B 255     9893   9451   9880   -502   1100    360       C  
ATOM   6338  CZ  TYR B 255     -16.150   1.716  20.940  1.00 85.31           C  
ANISOU 6338  CZ  TYR B 255    10930  10552  10931   -464   1141    371       C  
ATOM   6339  OH  TYR B 255     -15.454   0.785  21.679  1.00 87.15           O  
ANISOU 6339  OH  TYR B 255    11090  10897  11124   -428   1191    455       O  
ATOM   6340  N   TYR B 256     -15.983   6.745  18.147  1.00 76.78           N  
ANISOU 6340  N   TYR B 256    10062   9211   9898   -661   1011    201       N  
ATOM   6341  CA  TYR B 256     -14.574   7.129  18.120  1.00 77.54           C  
ANISOU 6341  CA  TYR B 256    10141   9367   9952   -753    952    229       C  
ATOM   6342  C   TYR B 256     -14.334   8.446  18.863  1.00 82.98           C  
ANISOU 6342  C   TYR B 256    10934   9994  10601   -864    937    158       C  
ATOM   6343  O   TYR B 256     -13.287   8.577  19.490  1.00 83.34           O  
ANISOU 6343  O   TYR B 256    10973  10122  10570   -980    870    169       O  
ATOM   6344  CB  TYR B 256     -14.025   7.197  16.680  1.00 78.74           C  
ANISOU 6344  CB  TYR B 256    10231   9529  10158   -727    932    302       C  
ATOM   6345  CG  TYR B 256     -14.002   5.886  15.913  1.00 80.66           C  
ANISOU 6345  CG  TYR B 256    10419   9823  10405   -633    946    359       C  
ATOM   6346  CD1 TYR B 256     -13.755   4.676  16.561  1.00 82.77           C  
ANISOU 6346  CD1 TYR B 256    10664  10155  10629   -607    967    390       C  
ATOM   6347  CD2 TYR B 256     -14.131   5.866  14.526  1.00 81.38           C  
ANISOU 6347  CD2 TYR B 256    10493   9895  10533   -568    949    388       C  
ATOM   6348  CE1 TYR B 256     -13.724   3.472  15.858  1.00 84.00           C  
ANISOU 6348  CE1 TYR B 256    10812  10314  10788   -523   1004    431       C  
ATOM   6349  CE2 TYR B 256     -14.074   4.672  13.808  1.00 82.25           C  
ANISOU 6349  CE2 TYR B 256    10602  10027  10621   -491    967    417       C  
ATOM   6350  CZ  TYR B 256     -13.885   3.474  14.479  1.00 91.49           C  
ANISOU 6350  CZ  TYR B 256    11782  11221  11757   -472   1000    432       C  
ATOM   6351  OH  TYR B 256     -13.830   2.298  13.766  1.00 92.92           O  
ANISOU 6351  OH  TYR B 256    12004  11384  11917   -398   1041    450       O  
ATOM   6352  N   ILE B 257     -15.301   9.403  18.826  1.00 80.45           N  
ANISOU 6352  N   ILE B 257    10716   9531  10322   -834   1007     96       N  
ATOM   6353  CA  ILE B 257     -15.211  10.682  19.557  1.00 82.21           C  
ANISOU 6353  CA  ILE B 257    11097   9638  10501   -929   1028      5       C  
ATOM   6354  C   ILE B 257     -15.295  10.382  21.067  1.00 88.39           C  
ANISOU 6354  C   ILE B 257    11968  10465  11153   -957   1023    -69       C  
ATOM   6355  O   ILE B 257     -14.492  10.901  21.840  1.00 89.81           O  
ANISOU 6355  O   ILE B 257    12232  10659  11231  -1107    958   -135       O  
ATOM   6356  CB  ILE B 257     -16.288  11.733  19.120  1.00 85.62           C  
ANISOU 6356  CB  ILE B 257    11628   9894  11011   -845   1156    -11       C  
ATOM   6357  CG1 ILE B 257     -16.464  11.861  17.578  1.00 85.17           C  
ANISOU 6357  CG1 ILE B 257    11447   9838  11076   -773   1177     88       C  
ATOM   6358  CG2 ILE B 257     -16.079  13.101  19.799  1.00 87.98           C  
ANISOU 6358  CG2 ILE B 257    12136  10026  11267   -949   1202   -115       C  
ATOM   6359  CD1 ILE B 257     -15.228  12.334  16.731  1.00 91.83           C  
ANISOU 6359  CD1 ILE B 257    12221  10700  11969   -865   1105    135       C  
ATOM   6360  N   GLY B 258     -16.249   9.530  21.447  1.00 84.59           N  
ANISOU 6360  N   GLY B 258    11453  10018  10671   -820   1081    -45       N  
ATOM   6361  CA  GLY B 258     -16.467   9.094  22.822  1.00 85.13           C  
ANISOU 6361  CA  GLY B 258    11572  10149  10625   -794   1096    -83       C  
ATOM   6362  C   GLY B 258     -15.324   8.271  23.384  1.00 89.35           C  
ANISOU 6362  C   GLY B 258    12002  10878  11070   -881    998    -51       C  
ATOM   6363  O   GLY B 258     -14.890   8.518  24.512  1.00 90.82           O  
ANISOU 6363  O   GLY B 258    12264  11130  11112   -963    962   -111       O  
ATOM   6364  N   ILE B 259     -14.810   7.304  22.597  1.00 84.22           N  
ANISOU 6364  N   ILE B 259    11184  10328  10489   -860    964     57       N  
ATOM   6365  CA  ILE B 259     -13.686   6.453  22.989  1.00 83.86           C  
ANISOU 6365  CA  ILE B 259    11014  10479  10372   -911    907    146       C  
ATOM   6366  C   ILE B 259     -12.397   7.288  23.070  1.00 89.58           C  
ANISOU 6366  C   ILE B 259    11748  11273  11016  -1104    799    150       C  
ATOM   6367  O   ILE B 259     -11.513   6.961  23.863  1.00 90.21           O  
ANISOU 6367  O   ILE B 259    11757  11542  10978  -1190    740    210       O  
ATOM   6368  CB  ILE B 259     -13.612   5.159  22.108  1.00 85.42           C  
ANISOU 6368  CB  ILE B 259    11071  10723  10663   -801    945    266       C  
ATOM   6369  CG1 ILE B 259     -13.974   3.870  22.892  1.00 85.61           C  
ANISOU 6369  CG1 ILE B 259    11018  10835  10675   -693   1013    325       C  
ATOM   6370  CG2 ILE B 259     -12.346   5.013  21.262  1.00 85.79           C  
ANISOU 6370  CG2 ILE B 259    11026  10854  10716   -852    899    379       C  
ATOM   6371  CD1 ILE B 259     -13.044   3.443  24.096  1.00 94.77           C  
ANISOU 6371  CD1 ILE B 259    12095  12214  11701   -732    998    402       C  
ATOM   6372  N   SER B 260     -12.336   8.403  22.292  1.00 86.98           N  
ANISOU 6372  N   SER B 260    11497  10798  10751  -1178    777    100       N  
ATOM   6373  CA  SER B 260     -11.222   9.352  22.272  1.00 88.54           C  
ANISOU 6373  CA  SER B 260    11715  11018  10907  -1383    671    105       C  
ATOM   6374  C   SER B 260     -11.162  10.114  23.594  1.00 94.55           C  
ANISOU 6374  C   SER B 260    12644  11768  11514  -1538    622    -34       C  
ATOM   6375  O   SER B 260     -10.100  10.152  24.215  1.00 95.65           O  
ANISOU 6375  O   SER B 260    12733  12077  11532  -1718    504      8       O  
ATOM   6376  CB  SER B 260     -11.351  10.321  21.098  1.00 92.46           C  
ANISOU 6376  CB  SER B 260    12255  11337  11538  -1390    691     94       C  
ATOM   6377  OG  SER B 260     -10.463  11.421  21.215  1.00105.79           O  
ANISOU 6377  OG  SER B 260    14001  12992  13203  -1606    598     75       O  
ATOM   6378  N   ILE B 261     -12.303  10.697  24.029  1.00 91.55           N  
ANISOU 6378  N   ILE B 261    12462  11199  11122  -1465    718   -184       N  
ATOM   6379  CA  ILE B 261     -12.423  11.443  25.284  1.00 93.70           C  
ANISOU 6379  CA  ILE B 261    12958  11418  11227  -1575    706   -344       C  
ATOM   6380  C   ILE B 261     -12.108  10.528  26.465  1.00 99.69           C  
ANISOU 6380  C   ILE B 261    13638  12424  11815  -1578    655   -315       C  
ATOM   6381  O   ILE B 261     -11.292  10.909  27.295  1.00101.19           O  
ANISOU 6381  O   ILE B 261    13886  12726  11835  -1785    538   -368       O  
ATOM   6382  CB  ILE B 261     -13.779  12.198  25.427  1.00 96.91           C  
ANISOU 6382  CB  ILE B 261    13599  11563  11659  -1433    867   -467       C  
ATOM   6383  CG1 ILE B 261     -14.012  13.156  24.234  1.00 96.95           C  
ANISOU 6383  CG1 ILE B 261    13656  11348  11832  -1430    934   -464       C  
ATOM   6384  CG2 ILE B 261     -13.841  12.976  26.754  1.00 99.99           C  
ANISOU 6384  CG2 ILE B 261    14270  11879  11843  -1535    871   -645       C  
ATOM   6385  CD1 ILE B 261     -15.473  13.522  23.952  1.00101.66           C  
ANISOU 6385  CD1 ILE B 261    14362  11751  12514  -1207   1129   -470       C  
ATOM   6386  N   ASP B 262     -12.693   9.306  26.501  1.00 96.38           N  
ANISOU 6386  N   ASP B 262    13070  12103  11445  -1365    735   -215       N  
ATOM   6387  CA  ASP B 262     -12.456   8.304  27.554  1.00 97.57           C  
ANISOU 6387  CA  ASP B 262    13106  12500  11467  -1321    721   -147       C  
ATOM   6388  C   ASP B 262     -10.967   7.968  27.708  1.00103.78           C  
ANISOU 6388  C   ASP B 262    13718  13554  12161  -1501    587    -20       C  
ATOM   6389  O   ASP B 262     -10.503   7.776  28.831  1.00104.83           O  
ANISOU 6389  O   ASP B 262    13827  13898  12106  -1579    528    -11       O  
ATOM   6390  CB  ASP B 262     -13.273   7.024  27.298  1.00 97.89           C  
ANISOU 6390  CB  ASP B 262    12996  12564  11634  -1074    839    -33       C  
ATOM   6391  CG  ASP B 262     -13.109   5.917  28.336  1.00111.98           C  
ANISOU 6391  CG  ASP B 262    14640  14587  13321   -991    863     67       C  
ATOM   6392  OD1 ASP B 262     -13.231   6.212  29.552  1.00114.34           O  
ANISOU 6392  OD1 ASP B 262    15037  14963  13443  -1007    854    -10       O  
ATOM   6393  OD2 ASP B 262     -12.909   4.747  27.929  1.00117.89           O  
ANISOU 6393  OD2 ASP B 262    15193  15434  14165   -892    908    223       O  
ATOM   6394  N   SER B 263     -10.228   7.907  26.583  1.00100.62           N  
ANISOU 6394  N   SER B 263    13187  13164  11881  -1554    544    103       N  
ATOM   6395  CA  SER B 263      -8.790   7.644  26.581  1.00101.74           C  
ANISOU 6395  CA  SER B 263    13142  13563  11953  -1709    431    283       C  
ATOM   6396  C   SER B 263      -7.988   8.876  27.021  1.00109.06           C  
ANISOU 6396  C   SER B 263    14176  14511  12750  -2019    265    201       C  
ATOM   6397  O   SER B 263      -6.896   8.712  27.566  1.00110.03           O  
ANISOU 6397  O   SER B 263    14160  14911  12734  -2190    145    333       O  
ATOM   6398  CB  SER B 263      -8.321   7.110  25.229  1.00103.57           C  
ANISOU 6398  CB  SER B 263    13208  13793  12351  -1618    467    467       C  
ATOM   6399  OG  SER B 263      -8.896   7.800  24.133  1.00110.20           O  
ANISOU 6399  OG  SER B 263    14157  14369  13346  -1577    500    374       O  
ATOM   6400  N   PHE B 264      -8.545  10.101  26.823  1.00107.36           N  
ANISOU 6400  N   PHE B 264    14209  14008  12573  -2098    265     -6       N  
ATOM   6401  CA  PHE B 264      -7.920  11.364  27.244  1.00110.47           C  
ANISOU 6401  CA  PHE B 264    14770  14347  12856  -2410    122   -127       C  
ATOM   6402  C   PHE B 264      -7.939  11.496  28.771  1.00118.12           C  
ANISOU 6402  C   PHE B 264    15884  15439  13558  -2533     58   -267       C  
ATOM   6403  O   PHE B 264      -6.930  11.907  29.347  1.00120.45           O  
ANISOU 6403  O   PHE B 264    16170  15906  13690  -2829   -120   -256       O  
ATOM   6404  CB  PHE B 264      -8.598  12.587  26.594  1.00112.45           C  
ANISOU 6404  CB  PHE B 264    15266  14223  13237  -2421    192   -300       C  
ATOM   6405  CG  PHE B 264      -8.022  13.019  25.267  1.00113.55           C  
ANISOU 6405  CG  PHE B 264    15291  14281  13573  -2475    162   -175       C  
ATOM   6406  CD1 PHE B 264      -6.768  13.613  25.194  1.00118.63           C  
ANISOU 6406  CD1 PHE B 264    15867  15017  14190  -2770    -10    -90       C  
ATOM   6407  CD2 PHE B 264      -8.757  12.886  24.095  1.00113.60           C  
ANISOU 6407  CD2 PHE B 264    15254  14124  13783  -2238    302   -133       C  
ATOM   6408  CE1 PHE B 264      -6.237  14.018  23.966  1.00119.11           C  
ANISOU 6408  CE1 PHE B 264    15806  15009  14441  -2796    -27     54       C  
ATOM   6409  CE2 PHE B 264      -8.226  13.291  22.866  1.00115.98           C  
ANISOU 6409  CE2 PHE B 264    15446  14369  14254  -2264    283     -8       C  
ATOM   6410  CZ  PHE B 264      -6.972  13.860  22.811  1.00115.93           C  
ANISOU 6410  CZ  PHE B 264    15367  14449  14234  -2529    127     89       C  
ATOM   6411  N   ILE B 265      -9.076  11.141  29.421  1.00114.77           N  
ANISOU 6411  N   ILE B 265    15583  14942  13081  -2308    196   -381       N  
ATOM   6412  CA  ILE B 265      -9.221  11.183  30.883  1.00117.17           C  
ANISOU 6412  CA  ILE B 265    16031  15369  13118  -2360    165   -509       C  
ATOM   6413  C   ILE B 265      -8.407  10.072  31.546  1.00122.79           C  
ANISOU 6413  C   ILE B 265    16453  16507  13695  -2378     85   -306       C  
ATOM   6414  O   ILE B 265      -7.748  10.332  32.555  1.00125.31           O  
ANISOU 6414  O   ILE B 265    16811  17040  13762  -2600    -56   -349       O  
ATOM   6415  CB  ILE B 265     -10.682  11.213  31.425  1.00119.88           C  
ANISOU 6415  CB  ILE B 265    16598  15513  13439  -2093    350   -661       C  
ATOM   6416  CG1 ILE B 265     -11.745  11.461  30.331  1.00118.12           C  
ANISOU 6416  CG1 ILE B 265    16441  14967  13471  -1878    519   -674       C  
ATOM   6417  CG2 ILE B 265     -10.795  12.223  32.579  1.00124.02           C  
ANISOU 6417  CG2 ILE B 265    17478  15947  13696  -2248    311   -909       C  
ATOM   6418  CD1 ILE B 265     -13.148  10.899  30.614  1.00121.82           C  
ANISOU 6418  CD1 ILE B 265    16943  15355  13988  -1544    711   -665       C  
ATOM   6419  N   LEU B 266      -8.452   8.840  30.979  1.00117.90           N  
ANISOU 6419  N   LEU B 266    15551  16011  13234  -2147    184    -81       N  
ATOM   6420  CA  LEU B 266      -7.716   7.653  31.449  1.00118.39           C  
ANISOU 6420  CA  LEU B 266    15308  16460  13214  -2103    170    166       C  
ATOM   6421  C   LEU B 266      -6.197   7.910  31.424  1.00125.60           C  
ANISOU 6421  C   LEU B 266    16056  17646  14022  -2406    -22    332       C  
ATOM   6422  O   LEU B 266      -5.465   7.380  32.264  1.00126.65           O  
ANISOU 6422  O   LEU B 266    16004  18148  13968  -2482    -89    490       O  
ATOM   6423  CB  LEU B 266      -8.094   6.416  30.595  1.00115.59           C  
ANISOU 6423  CB  LEU B 266    14747  16082  13091  -1806    340    354       C  
ATOM   6424  CG  LEU B 266      -7.478   5.038  30.938  1.00120.23           C  
ANISOU 6424  CG  LEU B 266    15026  17010  13645  -1684    404    638       C  
ATOM   6425  CD1 LEU B 266      -7.919   4.540  32.310  1.00121.43           C  
ANISOU 6425  CD1 LEU B 266    15163  17347  13628  -1578    456    619       C  
ATOM   6426  CD2 LEU B 266      -7.844   4.006  29.890  1.00120.12           C  
ANISOU 6426  CD2 LEU B 266    14890  16875  13875  -1431    571    776       C  
ATOM   6427  N   LEU B 267      -5.746   8.747  30.477  1.00123.59           N  
ANISOU 6427  N   LEU B 267    15852  17221  13885  -2577   -106    318       N  
ATOM   6428  CA  LEU B 267      -4.352   9.160  30.325  1.00126.12           C  
ANISOU 6428  CA  LEU B 267    16024  17757  14139  -2886   -299    488       C  
ATOM   6429  C   LEU B 267      -4.023  10.513  30.985  1.00134.25           C  
ANISOU 6429  C   LEU B 267    17299  18722  14987  -3267   -500    267       C  
ATOM   6430  O   LEU B 267      -2.890  11.000  30.906  1.00136.22           O  
ANISOU 6430  O   LEU B 267    17444  19135  15179  -3580   -691    394       O  
ATOM   6431  CB  LEU B 267      -3.874   8.874  28.891  1.00124.40           C  
ANISOU 6431  CB  LEU B 267    15615  17488  14165  -2789   -249    718       C  
ATOM   6432  CG  LEU B 267      -3.066   7.592  28.650  1.00128.30           C  
ANISOU 6432  CG  LEU B 267    15757  18313  14678  -2641   -184   1096       C  
ATOM   6433  CD1 LEU B 267      -3.870   6.325  28.975  1.00126.40           C  
ANISOU 6433  CD1 LEU B 267    15461  18106  14460  -2306     21   1119       C  
ATOM   6434  CD2 LEU B 267      -2.619   7.536  27.225  1.00129.27           C  
ANISOU 6434  CD2 LEU B 267    15765  18339  15014  -2557   -138   1284       C  
ATOM   6435  N   GLU B 268      -5.054  11.098  31.635  1.00131.47           N  
ANISOU 6435  N   GLU B 268    17287  18122  14546  -3230   -442    -55       N  
ATOM   6436  CA  GLU B 268      -5.096  12.368  32.367  1.00134.44           C  
ANISOU 6436  CA  GLU B 268    18014  18336  14731  -3525   -565   -349       C  
ATOM   6437  C   GLU B 268      -5.010  13.821  31.871  1.00139.98           C  
ANISOU 6437  C   GLU B 268    19000  18679  15507  -3785   -638   -547       C  
ATOM   6438  O   GLU B 268      -4.698  14.739  32.632  1.00143.15           O  
ANISOU 6438  O   GLU B 268    19657  19036  15699  -4109   -784   -747       O  
ATOM   6439  CB  GLU B 268      -4.655  12.376  33.852  1.00139.10           C  
ANISOU 6439  CB  GLU B 268    18659  19236  14955  -3744   -719   -421       C  
ATOM   6440  CG  GLU B 268      -3.176  12.129  34.125  1.00152.44           C  
ANISOU 6440  CG  GLU B 268    20041  21381  16499  -4060   -954   -157       C  
ATOM   6441  CD  GLU B 268      -2.808  11.666  35.521  1.00179.90           C  
ANISOU 6441  CD  GLU B 268    23440  25286  19627  -4164  -1061   -124       C  
ATOM   6442  OE1 GLU B 268      -2.167  10.596  35.636  1.00179.12           O  
ANISOU 6442  OE1 GLU B 268    22947  25610  19502  -4076  -1060    215       O  
ATOM   6443  OE2 GLU B 268      -3.164  12.366  36.498  1.00178.20           O  
ANISOU 6443  OE2 GLU B 268    23563  24988  19156  -4316  -1129   -426       O  
ATOM   6444  N   ILE B 269      -5.256  14.004  30.569  1.00134.12           N  
ANISOU 6444  N   ILE B 269    18209  17688  15061  -3647   -532   -480       N  
ATOM   6445  CA  ILE B 269      -5.306  15.306  29.899  1.00134.91           C  
ANISOU 6445  CA  ILE B 269    18544  17417  15300  -3812   -539   -626       C  
ATOM   6446  C   ILE B 269      -6.497  16.225  30.201  1.00139.33           C  
ANISOU 6446  C   ILE B 269    19544  17554  15839  -3725   -379   -954       C  
ATOM   6447  O   ILE B 269      -6.301  17.403  30.502  1.00142.09           O  
ANISOU 6447  O   ILE B 269    20197  17682  16110  -4008   -450  -1156       O  
ATOM   6448  CB  ILE B 269      -5.071  15.008  28.382  1.00135.27           C  
ANISOU 6448  CB  ILE B 269    18316  17426  15656  -3655   -475   -379       C  
ATOM   6449  CG1 ILE B 269      -3.729  14.264  28.181  1.00135.92           C  
ANISOU 6449  CG1 ILE B 269    18001  17921  15722  -3776   -635    -35       C  
ATOM   6450  CG2 ILE B 269      -5.120  16.299  27.536  1.00136.68           C  
ANISOU 6450  CG2 ILE B 269    18677  17235  16022  -3780   -456   -478       C  
ATOM   6451  CD1 ILE B 269      -3.556  13.532  26.862  1.00140.72           C  
ANISOU 6451  CD1 ILE B 269    18318  18575  16574  -3519   -532    242       C  
ATOM   6452  N   ILE B 270      -7.721  15.660  30.192  1.00133.03           N  
ANISOU 6452  N   ILE B 270    18789  16658  15099  -3339   -157   -991       N  
ATOM   6453  CA  ILE B 270      -8.932  16.411  30.530  1.00133.24           C  
ANISOU 6453  CA  ILE B 270    19208  16322  15095  -3193     34  -1242       C  
ATOM   6454  C   ILE B 270      -9.272  16.238  32.026  1.00138.59           C  
ANISOU 6454  C   ILE B 270    20093  17110  15455  -3182     31  -1406       C  
ATOM   6455  O   ILE B 270      -9.043  15.169  32.601  1.00137.43           O  
ANISOU 6455  O   ILE B 270    19709  17316  15191  -3107    -29  -1279       O  
ATOM   6456  CB  ILE B 270     -10.135  16.203  29.554  1.00133.03           C  
ANISOU 6456  CB  ILE B 270    19145  16074  15328  -2808    284  -1177       C  
ATOM   6457  CG1 ILE B 270     -10.998  14.988  29.909  1.00131.12           C  
ANISOU 6457  CG1 ILE B 270    18758  15994  15067  -2468    405  -1089       C  
ATOM   6458  CG2 ILE B 270      -9.709  16.183  28.078  1.00131.57           C  
ANISOU 6458  CG2 ILE B 270    18705  15862  15424  -2800    270   -987       C  
ATOM   6459  CD1 ILE B 270     -12.397  15.351  30.311  1.00139.22           C  
ANISOU 6459  CD1 ILE B 270    20067  16765  16066  -2210    631  -1222       C  
ATOM   6460  N   LYS B 271      -9.853  17.300  32.607  1.00137.31           N  
ANISOU 6460  N   LYS B 271    20381  16630  15161  -3227    123  -1675       N  
ATOM   6461  CA  LYS B 271     -10.216  17.365  34.034  1.00139.37           C  
ANISOU 6461  CA  LYS B 271    20929  16936  15089  -3217    138  -1871       C  
ATOM   6462  C   LYS B 271     -11.401  18.284  34.451  1.00144.54           C  
ANISOU 6462  C   LYS B 271    22080  17173  15668  -3033    387  -2109       C  
ATOM   6463  O   LYS B 271     -11.231  19.476  34.710  1.00147.56           O  
ANISOU 6463  O   LYS B 271    22863  17264  15938  -3270    380  -2343       O  
ATOM   6464  CB  LYS B 271      -8.989  17.738  34.873  1.00145.60           C  
ANISOU 6464  CB  LYS B 271    21795  17933  15591  -3677   -149  -1979       C  
ATOM   6465  CG  LYS B 271      -8.364  19.072  34.499  1.00162.71           C  
ANISOU 6465  CG  LYS B 271    24223  19807  17792  -4066   -255  -2137       C  
ATOM   6466  CD  LYS B 271      -8.700  19.457  33.067  1.00168.05           C  
ANISOU 6466  CD  LYS B 271    24820  20180  18852  -3924   -102  -2031       C  
ATOM   6467  CE  LYS B 271      -9.430  20.789  33.011  1.00178.62           C  
ANISOU 6467  CE  LYS B 271    26659  20992  20218  -3915     99  -2282       C  
ATOM   6468  NZ  LYS B 271      -9.668  21.233  31.610  1.00183.70           N  
ANISOU 6468  NZ  LYS B 271    27200  21371  21226  -3801    241  -2158       N  
ATOM   6469  N   GLN B 272     -12.585  17.679  34.509  1.00138.37           N  
ANISOU 6469  N   GLN B 272    21256  16367  14950  -2606    615  -2023       N  
ATOM   6470  CA  GLN B 272     -13.846  18.171  35.078  1.00139.10           C  
ANISOU 6470  CA  GLN B 272    21732  16176  14944  -2315    886  -2153       C  
ATOM   6471  C   GLN B 272     -14.394  17.375  36.282  1.00142.85           C  
ANISOU 6471  C   GLN B 272    22212  16884  15179  -2071    941  -2141       C  
ATOM   6472  O   GLN B 272     -15.299  17.854  36.976  1.00144.27           O  
ANISOU 6472  O   GLN B 272    22759  16854  15204  -1857   1148  -2262       O  
ATOM   6473  CB  GLN B 272     -14.610  18.498  33.784  1.00137.96           C  
ANISOU 6473  CB  GLN B 272    21530  15745  15143  -2101   1096  -2028       C  
ATOM   6474  CG  GLN B 272     -14.573  19.989  33.446  1.00155.04           C  
ANISOU 6474  CG  GLN B 272    24092  17477  17339  -2269   1192  -2212       C  
ATOM   6475  CD  GLN B 272     -14.682  20.272  31.965  1.00171.94           C  
ANISOU 6475  CD  GLN B 272    26038  19456  19834  -2219   1272  -2055       C  
ATOM   6476  OE1 GLN B 272     -15.524  19.712  31.249  1.00165.35           O  
ANISOU 6476  OE1 GLN B 272    24965  18653  19207  -1900   1423  -1849       O  
ATOM   6477  NE2 GLN B 272     -13.873  21.207  31.484  1.00164.55           N  
ANISOU 6477  NE2 GLN B 272    25215  18335  18970  -2538   1181  -2147       N  
ATOM   6478  N   GLY B 273     -13.805  16.205  36.538  1.00137.40           N  
ANISOU 6478  N   GLY B 273    21128  16623  14455  -2099    770  -1982       N  
ATOM   6479  CA  GLY B 273     -14.131  15.335  37.665  1.00137.11           C  
ANISOU 6479  CA  GLY B 273    21016  16874  14205  -1894    793  -1931       C  
ATOM   6480  C   GLY B 273     -14.970  14.206  37.098  1.00135.98           C  
ANISOU 6480  C   GLY B 273    20509  16820  14336  -1515    944  -1656       C  
ATOM   6481  O   GLY B 273     -15.080  14.046  35.879  1.00132.89           O  
ANISOU 6481  O   GLY B 273    19910  16328  14253  -1478    975  -1522       O  
ATOM   6482  N   CYS B 274     -15.563  13.412  38.010  1.00131.63           N  
ANISOU 6482  N   CYS B 274    19884  16466  13662  -1239   1033  -1570       N  
ATOM   6483  CA  CYS B 274     -16.378  12.235  37.708  1.00127.82           C  
ANISOU 6483  CA  CYS B 274    19062  16098  13407   -891   1166  -1305       C  
ATOM   6484  C   CYS B 274     -17.795  12.447  37.156  1.00129.38           C  
ANISOU 6484  C   CYS B 274    19350  15993  13815   -561   1422  -1219       C  
ATOM   6485  O   CYS B 274     -18.405  11.476  36.696  1.00125.99           O  
ANISOU 6485  O   CYS B 274    18609  15647  13615   -337   1496   -990       O  
ATOM   6486  CB  CYS B 274     -16.372  11.277  38.897  1.00128.67           C  
ANISOU 6486  CB  CYS B 274    19013  16557  13318   -740   1155  -1213       C  
ATOM   6487  SG  CYS B 274     -14.989  10.101  38.895  1.00131.44           S  
ANISOU 6487  SG  CYS B 274    18889  17382  13671   -955    923  -1040       S  
ATOM   6488  N   GLU B 275     -18.313  13.695  37.182  1.00127.56           N  
ANISOU 6488  N   GLU B 275    19538  15416  13511   -538   1562  -1383       N  
ATOM   6489  CA  GLU B 275     -19.657  13.984  36.663  1.00126.26           C  
ANISOU 6489  CA  GLU B 275    19457  14985  13533   -219   1825  -1261       C  
ATOM   6490  C   GLU B 275     -19.748  13.823  35.139  1.00126.19           C  
ANISOU 6490  C   GLU B 275    19177  14892  13877   -254   1815  -1114       C  
ATOM   6491  O   GLU B 275     -20.627  13.106  34.652  1.00123.12           O  
ANISOU 6491  O   GLU B 275    18541  14542  13698     -9   1918   -885       O  
ATOM   6492  CB  GLU B 275     -20.222  15.330  37.170  1.00131.01           C  
ANISOU 6492  CB  GLU B 275    20592  15240  13945   -136   2029  -1443       C  
ATOM   6493  CG  GLU B 275     -19.433  16.575  36.798  1.00144.86           C  
ANISOU 6493  CG  GLU B 275    22659  16736  15646   -478   1956  -1694       C  
ATOM   6494  CD  GLU B 275     -20.307  17.756  36.425  1.00168.61           C  
ANISOU 6494  CD  GLU B 275    26034  19316  18712   -316   2241  -1728       C  
ATOM   6495  OE1 GLU B 275     -20.441  18.683  37.257  1.00168.99           O  
ANISOU 6495  OE1 GLU B 275    26574  19137  18499   -308   2367  -1937       O  
ATOM   6496  OE2 GLU B 275     -20.877  17.744  35.310  1.00160.11           O  
ANISOU 6496  OE2 GLU B 275    24761  18139  17933   -186   2353  -1536       O  
ATOM   6497  N   PHE B 276     -18.805  14.431  34.401  1.00122.53           N  
ANISOU 6497  N   PHE B 276    18743  14340  13472   -568   1674  -1234       N  
ATOM   6498  CA  PHE B 276     -18.751  14.321  32.950  1.00119.59           C  
ANISOU 6498  CA  PHE B 276    18124  13910  13403   -616   1649  -1108       C  
ATOM   6499  C   PHE B 276     -18.120  12.996  32.510  1.00119.16           C  
ANISOU 6499  C   PHE B 276    17630  14168  13476   -681   1472   -954       C  
ATOM   6500  O   PHE B 276     -18.313  12.584  31.368  1.00116.40           O  
ANISOU 6500  O   PHE B 276    17043  13811  13373   -636   1476   -811       O  
ATOM   6501  CB  PHE B 276     -18.065  15.542  32.315  1.00123.02           C  
ANISOU 6501  CB  PHE B 276    18767  14108  13868   -885   1603  -1266       C  
ATOM   6502  CG  PHE B 276     -19.037  16.459  31.609  1.00125.18           C  
ANISOU 6502  CG  PHE B 276    19221  14053  14290   -712   1846  -1227       C  
ATOM   6503  CD1 PHE B 276     -19.643  17.512  32.286  1.00131.36           C  
ANISOU 6503  CD1 PHE B 276    20443  14555  14915   -606   2057  -1355       C  
ATOM   6504  CD2 PHE B 276     -19.366  16.257  30.273  1.00125.19           C  
ANISOU 6504  CD2 PHE B 276    18958  14036  14573   -637   1882  -1047       C  
ATOM   6505  CE1 PHE B 276     -20.554  18.351  31.636  1.00132.76           C  
ANISOU 6505  CE1 PHE B 276    20771  14439  15232   -416   2319  -1274       C  
ATOM   6506  CE2 PHE B 276     -20.279  17.097  29.624  1.00128.44           C  
ANISOU 6506  CE2 PHE B 276    19503  14185  15114   -465   2119   -972       C  
ATOM   6507  CZ  PHE B 276     -20.866  18.138  30.311  1.00129.39           C  
ANISOU 6507  CZ  PHE B 276    20039  14032  15092   -349   2345  -1072       C  
ATOM   6508  N   GLU B 277     -17.416  12.312  33.439  1.00115.01           N  
ANISOU 6508  N   GLU B 277    17009  13921  12770   -765   1337   -972       N  
ATOM   6509  CA  GLU B 277     -16.768  11.013  33.234  1.00112.23           C  
ANISOU 6509  CA  GLU B 277    16265  13875  12501   -802   1206   -812       C  
ATOM   6510  C   GLU B 277     -17.804   9.919  32.986  1.00111.72           C  
ANISOU 6510  C   GLU B 277    15963  13861  12624   -500   1333   -602       C  
ATOM   6511  O   GLU B 277     -17.558   9.018  32.185  1.00109.05           O  
ANISOU 6511  O   GLU B 277    15334  13628  12472   -506   1281   -460       O  
ATOM   6512  CB  GLU B 277     -15.903  10.658  34.448  1.00115.49           C  
ANISOU 6512  CB  GLU B 277    16658  14580  12645   -929   1075   -861       C  
ATOM   6513  CG  GLU B 277     -14.507  10.189  34.090  1.00127.00           C  
ANISOU 6513  CG  GLU B 277    17858  16284  14111  -1191    871   -790       C  
ATOM   6514  CD  GLU B 277     -14.331   8.686  34.021  1.00149.57           C  
ANISOU 6514  CD  GLU B 277    20333  19422  17077  -1056    873   -554       C  
ATOM   6515  OE1 GLU B 277     -13.629   8.134  34.898  1.00146.97           O  
ANISOU 6515  OE1 GLU B 277    19874  19402  16567  -1117    791   -497       O  
ATOM   6516  OE2 GLU B 277     -14.880   8.062  33.084  1.00144.00           O  
ANISOU 6516  OE2 GLU B 277    19459  18627  16627   -897    959   -423       O  
ATOM   6517  N   ASN B 278     -18.964  10.008  33.663  1.00107.48           N  
ANISOU 6517  N   ASN B 278    15561  13241  12035   -238   1505   -573       N  
ATOM   6518  CA  ASN B 278     -20.064   9.065  33.483  1.00104.82           C  
ANISOU 6518  CA  ASN B 278    15010  12936  11880     39   1627   -354       C  
ATOM   6519  C   ASN B 278     -20.926   9.463  32.295  1.00105.16           C  
ANISOU 6519  C   ASN B 278    15051  12754  12149    116   1726   -275       C  
ATOM   6520  O   ASN B 278     -21.518   8.590  31.662  1.00102.60           O  
ANISOU 6520  O   ASN B 278    14478  12475  12032    224   1748    -94       O  
ATOM   6521  CB  ASN B 278     -20.898   8.938  34.752  1.00107.98           C  
ANISOU 6521  CB  ASN B 278    15516  13384  12126    300   1767   -306       C  
ATOM   6522  CG  ASN B 278     -20.362   7.894  35.691  1.00135.62           C  
ANISOU 6522  CG  ASN B 278    18821  17192  15515    322   1695   -245       C  
ATOM   6523  OD1 ASN B 278     -20.858   6.765  35.745  1.00129.89           O  
ANISOU 6523  OD1 ASN B 278    17826  16591  14934    498   1745    -41       O  
ATOM   6524  ND2 ASN B 278     -19.314   8.235  36.430  1.00130.19           N  
ANISOU 6524  ND2 ASN B 278    18252  16644  14572    129   1573   -407       N  
ATOM   6525  N   THR B 279     -20.971  10.778  31.980  1.00101.67           N  
ANISOU 6525  N   THR B 279    14887  12076  11666     46   1784   -406       N  
ATOM   6526  CA  THR B 279     -21.699  11.343  30.840  1.00100.18           C  
ANISOU 6526  CA  THR B 279    14708  11686  11670    109   1890   -326       C  
ATOM   6527  C   THR B 279     -21.024  10.829  29.568  1.00100.26           C  
ANISOU 6527  C   THR B 279    14456  11770  11869    -67   1737   -286       C  
ATOM   6528  O   THR B 279     -21.708  10.478  28.607  1.00 98.68           O  
ANISOU 6528  O   THR B 279    14082  11548  11862     20   1777   -136       O  
ATOM   6529  CB  THR B 279     -21.729  12.883  30.933  1.00112.03           C  
ANISOU 6529  CB  THR B 279    16586  12916  13063     68   2005   -484       C  
ATOM   6530  OG1 THR B 279     -22.184  13.275  32.234  1.00114.84           O  
ANISOU 6530  OG1 THR B 279    17224  13216  13192    223   2138   -549       O  
ATOM   6531  CG2 THR B 279     -22.614  13.524  29.868  1.00110.42           C  
ANISOU 6531  CG2 THR B 279    16391  12518  13044    187   2166   -358       C  
ATOM   6532  N   VAL B 280     -19.678  10.744  29.600  1.00 95.20           N  
ANISOU 6532  N   VAL B 280    13782  11235  11154   -310   1561   -403       N  
ATOM   6533  CA  VAL B 280     -18.833  10.207  28.536  1.00 92.53           C  
ANISOU 6533  CA  VAL B 280    13211  10992  10954   -466   1418   -357       C  
ATOM   6534  C   VAL B 280     -19.056   8.687  28.453  1.00 94.39           C  
ANISOU 6534  C   VAL B 280    13158  11414  11291   -356   1395   -196       C  
ATOM   6535  O   VAL B 280     -19.203   8.164  27.353  1.00 92.40           O  
ANISOU 6535  O   VAL B 280    12736  11159  11214   -348   1376   -102       O  
ATOM   6536  CB  VAL B 280     -17.346  10.617  28.745  1.00 97.12           C  
ANISOU 6536  CB  VAL B 280    13844  11649  11408   -743   1254   -485       C  
ATOM   6537  CG1 VAL B 280     -16.373   9.691  28.018  1.00 95.40           C  
ANISOU 6537  CG1 VAL B 280    13346  11618  11285   -850   1118   -381       C  
ATOM   6538  CG2 VAL B 280     -17.123  12.065  28.322  1.00 98.19           C  
ANISOU 6538  CG2 VAL B 280    14218  11550  11539   -883   1270   -616       C  
ATOM   6539  N   HIS B 281     -19.147   7.997  29.607  1.00 91.72           N  
ANISOU 6539  N   HIS B 281    12781  11227  10842   -263   1412   -163       N  
ATOM   6540  CA  HIS B 281     -19.401   6.553  29.662  1.00 90.39           C  
ANISOU 6540  CA  HIS B 281    12354  11212  10776   -148   1418     -3       C  
ATOM   6541  C   HIS B 281     -20.804   6.177  29.180  1.00 93.22           C  
ANISOU 6541  C   HIS B 281    12634  11473  11314     40   1528    140       C  
ATOM   6542  O   HIS B 281     -20.990   5.086  28.640  1.00 91.41           O  
ANISOU 6542  O   HIS B 281    12195  11299  11236     67   1509    259       O  
ATOM   6543  CB  HIS B 281     -19.099   5.998  31.058  1.00 92.46           C  
ANISOU 6543  CB  HIS B 281    12585  11676  10871    -88   1421     13       C  
ATOM   6544  CG  HIS B 281     -17.650   5.676  31.267  1.00 96.50           C  
ANISOU 6544  CG  HIS B 281    13001  12389  11274   -275   1289    -15       C  
ATOM   6545  ND1 HIS B 281     -17.260   4.565  31.994  1.00 98.44           N  
ANISOU 6545  ND1 HIS B 281    13052  12875  11476   -213   1291    103       N  
ATOM   6546  CD2 HIS B 281     -16.540   6.316  30.817  1.00 98.78           C  
ANISOU 6546  CD2 HIS B 281    13342  12685  11504   -510   1166   -107       C  
ATOM   6547  CE1 HIS B 281     -15.938   4.576  31.977  1.00 98.37           C  
ANISOU 6547  CE1 HIS B 281    12981  13027  11368   -408   1173     89       C  
ATOM   6548  NE2 HIS B 281     -15.460   5.607  31.279  1.00 98.90           N  
ANISOU 6548  NE2 HIS B 281    13189  12964  11426   -597   1085    -33       N  
ATOM   6549  N   LYS B 282     -21.775   7.100  29.349  1.00 90.93           N  
ANISOU 6549  N   LYS B 282    12517  11032  10999    161   1647    140       N  
ATOM   6550  CA  LYS B 282     -23.162   6.984  28.888  1.00 90.25           C  
ANISOU 6550  CA  LYS B 282    12361  10865  11064    332   1758    312       C  
ATOM   6551  C   LYS B 282     -23.156   7.140  27.371  1.00 92.40           C  
ANISOU 6551  C   LYS B 282    12553  11062  11494    219   1702    326       C  
ATOM   6552  O   LYS B 282     -23.899   6.445  26.676  1.00 90.86           O  
ANISOU 6552  O   LYS B 282    12180  10888  11455    262   1700    473       O  
ATOM   6553  CB  LYS B 282     -24.020   8.104  29.498  1.00 94.75           C  
ANISOU 6553  CB  LYS B 282    13171  11298  11533    499   1927    320       C  
ATOM   6554  CG  LYS B 282     -25.000   7.642  30.573  1.00113.46           C  
ANISOU 6554  CG  LYS B 282    15513  13732  13866    753   2053    482       C  
ATOM   6555  CD  LYS B 282     -25.895   8.789  31.064  1.00128.52           C  
ANISOU 6555  CD  LYS B 282    17679  15483  15669    954   2258    522       C  
ATOM   6556  CE  LYS B 282     -27.042   9.107  30.124  1.00141.07           C  
ANISOU 6556  CE  LYS B 282    19191  16982  17429   1064   2370    734       C  
ATOM   6557  NZ  LYS B 282     -27.740  10.365  30.505  1.00152.62           N  
ANISOU 6557  NZ  LYS B 282    20938  18268  18782   1257   2601    772       N  
ATOM   6558  N   TRP B 283     -22.304   8.065  26.869  1.00 89.29           N  
ANISOU 6558  N   TRP B 283    12289  10587  11050     64   1652    177       N  
ATOM   6559  CA  TRP B 283     -22.110   8.367  25.454  1.00 88.24           C  
ANISOU 6559  CA  TRP B 283    12097  10393  11038    -40   1602    177       C  
ATOM   6560  C   TRP B 283     -21.587   7.135  24.722  1.00 87.49           C  
ANISOU 6560  C   TRP B 283    11784  10418  11042   -127   1477    217       C  
ATOM   6561  O   TRP B 283     -22.221   6.703  23.767  1.00 87.00           O  
ANISOU 6561  O   TRP B 283    11596  10352  11107   -105   1470    315       O  
ATOM   6562  CB  TRP B 283     -21.164   9.568  25.278  1.00 88.66           C  
ANISOU 6562  CB  TRP B 283    12330  10342  11013   -188   1574     18       C  
ATOM   6563  CG  TRP B 283     -21.766  10.722  24.535  1.00 90.87           C  
ANISOU 6563  CG  TRP B 283    12715  10453  11358   -143   1688     43       C  
ATOM   6564  CD1 TRP B 283     -22.727  11.580  24.988  1.00 95.39           C  
ANISOU 6564  CD1 TRP B 283    13462  10888  11892     12   1872     85       C  
ATOM   6565  CD2 TRP B 283     -21.409  11.173  23.220  1.00 90.32           C  
ANISOU 6565  CD2 TRP B 283    12584  10338  11395   -234   1650     50       C  
ATOM   6566  NE1 TRP B 283     -23.017  12.517  24.022  1.00 95.39           N  
ANISOU 6566  NE1 TRP B 283    13499  10763  11981     24   1962    130       N  
ATOM   6567  CE2 TRP B 283     -22.222  12.291  22.926  1.00 95.50           C  
ANISOU 6567  CE2 TRP B 283    13361  10838  12086   -128   1820    105       C  
ATOM   6568  CE3 TRP B 283     -20.492  10.727  22.249  1.00 90.35           C  
ANISOU 6568  CE3 TRP B 283    12438  10425  11466   -368   1508     37       C  
ATOM   6569  CZ2 TRP B 283     -22.145  12.972  21.703  1.00 94.54           C  
ANISOU 6569  CZ2 TRP B 283    13195  10655  12071   -161   1845    146       C  
ATOM   6570  CZ3 TRP B 283     -20.423  11.396  21.037  1.00 91.62           C  
ANISOU 6570  CZ3 TRP B 283    12566  10523  11722   -395   1523     69       C  
ATOM   6571  CH2 TRP B 283     -21.238  12.507  20.775  1.00 93.29           C  
ANISOU 6571  CH2 TRP B 283    12879  10592  11973   -297   1685    122       C  
ATOM   6572  N   ILE B 284     -20.483   6.531  25.214  1.00 80.59           N  
ANISOU 6572  N   ILE B 284    10869   9658  10094   -216   1390    157       N  
ATOM   6573  CA  ILE B 284     -19.868   5.323  24.651  1.00 77.78           C  
ANISOU 6573  CA  ILE B 284    10339   9404   9810   -272   1311    205       C  
ATOM   6574  C   ILE B 284     -20.885   4.184  24.505  1.00 78.17           C  
ANISOU 6574  C   ILE B 284    10248   9468   9984   -167   1348    333       C  
ATOM   6575  O   ILE B 284     -20.977   3.598  23.427  1.00 76.33           O  
ANISOU 6575  O   ILE B 284     9929   9216   9857   -209   1307    369       O  
ATOM   6576  CB  ILE B 284     -18.580   4.914  25.428  1.00 81.02           C  
ANISOU 6576  CB  ILE B 284    10722   9962  10101   -351   1251    171       C  
ATOM   6577  CG1 ILE B 284     -17.514   6.032  25.355  1.00 81.81           C  
ANISOU 6577  CG1 ILE B 284    10937  10050  10096   -511   1178     61       C  
ATOM   6578  CG2 ILE B 284     -18.002   3.574  24.928  1.00 81.09           C  
ANISOU 6578  CG2 ILE B 284    10561  10065  10185   -361   1223    258       C  
ATOM   6579  CD1 ILE B 284     -16.668   6.144  26.563  1.00 88.05           C  
ANISOU 6579  CD1 ILE B 284    11769  10979  10709   -587   1132     15       C  
ATOM   6580  N   SER B 285     -21.674   3.919  25.567  1.00 74.25           N  
ANISOU 6580  N   SER B 285     9740   8999   9471    -35   1425    406       N  
ATOM   6581  CA  SER B 285     -22.713   2.880  25.606  1.00 73.41           C  
ANISOU 6581  CA  SER B 285     9491   8906   9494     62   1463    557       C  
ATOM   6582  C   SER B 285     -23.724   3.066  24.488  1.00 75.34           C  
ANISOU 6582  C   SER B 285     9695   9071   9861     50   1456    633       C  
ATOM   6583  O   SER B 285     -24.008   2.107  23.767  1.00 74.22           O  
ANISOU 6583  O   SER B 285     9436   8930   9835     -5   1405    691       O  
ATOM   6584  CB  SER B 285     -23.436   2.875  26.953  1.00 78.15           C  
ANISOU 6584  CB  SER B 285    10100   9550  10045    233   1563    645       C  
ATOM   6585  OG  SER B 285     -22.599   2.423  28.003  1.00 89.15           O  
ANISOU 6585  OG  SER B 285    11478  11064  11330    252   1565    610       O  
ATOM   6586  N   ILE B 286     -24.246   4.304  24.329  1.00 71.35           N  
ANISOU 6586  N   ILE B 286     9294   8497   9319     93   1512    635       N  
ATOM   6587  CA  ILE B 286     -25.234   4.617  23.299  1.00 70.56           C  
ANISOU 6587  CA  ILE B 286     9135   8360   9314     95   1520    745       C  
ATOM   6588  C   ILE B 286     -24.630   4.634  21.894  1.00 71.98           C  
ANISOU 6588  C   ILE B 286     9292   8528   9529    -55   1419    662       C  
ATOM   6589  O   ILE B 286     -25.146   3.949  21.014  1.00 71.41           O  
ANISOU 6589  O   ILE B 286     9103   8484   9546   -113   1355    734       O  
ATOM   6590  CB  ILE B 286     -26.165   5.826  23.624  1.00 74.61           C  
ANISOU 6590  CB  ILE B 286     9741   8815   9791    239   1662    843       C  
ATOM   6591  CG1 ILE B 286     -25.434   7.176  23.650  1.00 75.45           C  
ANISOU 6591  CG1 ILE B 286    10058   8822   9790    217   1713    690       C  
ATOM   6592  CG2 ILE B 286     -26.960   5.600  24.911  1.00 76.12           C  
ANISOU 6592  CG2 ILE B 286     9930   9034   9958    423   1772    978       C  
ATOM   6593  CD1 ILE B 286     -25.990   8.194  22.664  1.00 84.38           C  
ANISOU 6593  CD1 ILE B 286    11207   9889  10966    237   1786    765       C  
ATOM   6594  N   THR B 287     -23.507   5.354  21.711  1.00 66.57           N  
ANISOU 6594  N   THR B 287     8718   7809   8766   -123   1396    516       N  
ATOM   6595  CA  THR B 287     -22.808   5.489  20.433  1.00 64.84           C  
ANISOU 6595  CA  THR B 287     8485   7585   8567   -234   1315    450       C  
ATOM   6596  C   THR B 287     -22.296   4.161  19.862  1.00 67.53           C  
ANISOU 6596  C   THR B 287     8737   7974   8946   -311   1223    432       C  
ATOM   6597  O   THR B 287     -22.264   4.028  18.643  1.00 66.79           O  
ANISOU 6597  O   THR B 287     8610   7883   8885   -369   1166    429       O  
ATOM   6598  CB  THR B 287     -21.745   6.605  20.473  1.00 68.25           C  
ANISOU 6598  CB  THR B 287     9043   7967   8921   -287   1319    333       C  
ATOM   6599  OG1 THR B 287     -20.800   6.328  21.505  1.00 65.84           O  
ANISOU 6599  OG1 THR B 287     8787   7702   8527   -322   1293    255       O  
ATOM   6600  CG2 THR B 287     -22.353   7.989  20.677  1.00 66.30           C  
ANISOU 6600  CG2 THR B 287     8914   7622   8656   -217   1435    350       C  
ATOM   6601  N   GLU B 288     -21.921   3.184  20.721  1.00 63.49           N  
ANISOU 6601  N   GLU B 288     8198   7500   8423   -297   1225    430       N  
ATOM   6602  CA  GLU B 288     -21.459   1.865  20.273  1.00 62.72           C  
ANISOU 6602  CA  GLU B 288     8045   7419   8367   -345   1182    427       C  
ATOM   6603  C   GLU B 288     -22.617   1.080  19.671  1.00 66.13           C  
ANISOU 6603  C   GLU B 288     8403   7822   8902   -368   1155    503       C  
ATOM   6604  O   GLU B 288     -22.429   0.445  18.637  1.00 66.29           O  
ANISOU 6604  O   GLU B 288     8429   7816   8943   -444   1100    469       O  
ATOM   6605  CB  GLU B 288     -20.820   1.063  21.422  1.00 64.31           C  
ANISOU 6605  CB  GLU B 288     8220   7677   8538   -303   1224    441       C  
ATOM   6606  CG  GLU B 288     -20.028  -0.154  20.959  1.00 74.59           C  
ANISOU 6606  CG  GLU B 288     9496   8981   9863   -334   1222    443       C  
ATOM   6607  CD  GLU B 288     -19.482  -1.058  22.047  1.00 92.04           C  
ANISOU 6607  CD  GLU B 288    11648  11264  12060   -272   1294    503       C  
ATOM   6608  OE1 GLU B 288     -18.340  -1.543  21.887  1.00 89.85           O  
ANISOU 6608  OE1 GLU B 288    11368  11030  11739   -278   1318    514       O  
ATOM   6609  OE2 GLU B 288     -20.209  -1.327  23.031  1.00 79.07           O  
ANISOU 6609  OE2 GLU B 288     9946   9644  10452   -199   1342    568       O  
ATOM   6610  N   ALA B 289     -23.802   1.115  20.315  1.00 62.55           N  
ANISOU 6610  N   ALA B 289     7887   7377   8502   -306   1193    616       N  
ATOM   6611  CA  ALA B 289     -24.989   0.426  19.814  1.00 62.83           C  
ANISOU 6611  CA  ALA B 289     7825   7406   8640   -354   1151    725       C  
ATOM   6612  C   ALA B 289     -25.522   1.162  18.596  1.00 67.43           C  
ANISOU 6612  C   ALA B 289     8396   8010   9214   -417   1095    745       C  
ATOM   6613  O   ALA B 289     -25.906   0.522  17.621  1.00 67.41           O  
ANISOU 6613  O   ALA B 289     8355   8011   9246   -532   1006    752       O  
ATOM   6614  CB  ALA B 289     -26.052   0.361  20.890  1.00 64.13           C  
ANISOU 6614  CB  ALA B 289     7904   7600   8864   -247   1218    888       C  
ATOM   6615  N   LEU B 290     -25.506   2.512  18.640  1.00 64.25           N  
ANISOU 6615  N   LEU B 290     8037   7618   8755   -344   1153    751       N  
ATOM   6616  CA  LEU B 290     -25.938   3.393  17.550  1.00 64.06           C  
ANISOU 6616  CA  LEU B 290     7989   7629   8720   -367   1138    795       C  
ATOM   6617  C   LEU B 290     -25.014   3.232  16.333  1.00 66.90           C  
ANISOU 6617  C   LEU B 290     8392   7988   9039   -467   1051    663       C  
ATOM   6618  O   LEU B 290     -25.392   3.606  15.222  1.00 67.45           O  
ANISOU 6618  O   LEU B 290     8416   8113   9098   -508   1009    701       O  
ATOM   6619  CB  LEU B 290     -25.950   4.853  18.024  1.00 64.30           C  
ANISOU 6619  CB  LEU B 290     8093   7632   8707   -249   1261    819       C  
ATOM   6620  CG  LEU B 290     -26.964   5.764  17.362  1.00 69.87           C  
ANISOU 6620  CG  LEU B 290     8728   8387   9431   -199   1320    981       C  
ATOM   6621  CD1 LEU B 290     -28.201   5.915  18.226  1.00 70.64           C  
ANISOU 6621  CD1 LEU B 290     8768   8509   9563    -71   1429   1191       C  
ATOM   6622  CD2 LEU B 290     -26.351   7.117  17.075  1.00 73.08           C  
ANISOU 6622  CD2 LEU B 290     9242   8732   9795   -152   1405    916       C  
ATOM   6623  N   ALA B 291     -23.808   2.667  16.547  1.00 62.15           N  
ANISOU 6623  N   ALA B 291     7869   7340   8404   -487   1035    534       N  
ATOM   6624  CA  ALA B 291     -22.835   2.384  15.497  1.00 61.18           C  
ANISOU 6624  CA  ALA B 291     7798   7211   8235   -545    977    434       C  
ATOM   6625  C   ALA B 291     -22.941   0.930  15.055  1.00 64.45           C  
ANISOU 6625  C   ALA B 291     8224   7596   8668   -625    918    404       C  
ATOM   6626  O   ALA B 291     -21.993   0.406  14.480  1.00 64.16           O  
ANISOU 6626  O   ALA B 291     8266   7528   8584   -641    906    322       O  
ATOM   6627  CB  ALA B 291     -21.420   2.689  15.980  1.00 61.24           C  
ANISOU 6627  CB  ALA B 291     7879   7200   8190   -509   1013    357       C  
ATOM   6628  N   PHE B 292     -24.083   0.269  15.311  1.00 61.28           N  
ANISOU 6628  N   PHE B 292     7752   7194   8336   -675    890    483       N  
ATOM   6629  CA  PHE B 292     -24.287  -1.096  14.818  1.00 61.94           C  
ANISOU 6629  CA  PHE B 292     7869   7219   8446   -787    828    445       C  
ATOM   6630  C   PHE B 292     -25.021  -1.024  13.488  1.00 68.49           C  
ANISOU 6630  C   PHE B 292     8680   8106   9238   -908    715    450       C  
ATOM   6631  O   PHE B 292     -24.962  -1.980  12.721  1.00 69.06           O  
ANISOU 6631  O   PHE B 292     8838   8121   9280  -1021    648    366       O  
ATOM   6632  CB  PHE B 292     -24.993  -2.028  15.830  1.00 63.82           C  
ANISOU 6632  CB  PHE B 292     8041   7413   8793   -800    852    531       C  
ATOM   6633  CG  PHE B 292     -24.149  -2.459  17.011  1.00 64.18           C  
ANISOU 6633  CG  PHE B 292     8112   7415   8859   -691    962    516       C  
ATOM   6634  CD1 PHE B 292     -22.759  -2.446  16.939  1.00 66.06           C  
ANISOU 6634  CD1 PHE B 292     8445   7636   9018   -637   1013    422       C  
ATOM   6635  CD2 PHE B 292     -24.743  -2.908  18.184  1.00 66.31           C  
ANISOU 6635  CD2 PHE B 292     8291   7684   9221   -637   1016    627       C  
ATOM   6636  CE1 PHE B 292     -21.980  -2.834  18.033  1.00 66.17           C  
ANISOU 6636  CE1 PHE B 292     8452   7655   9034   -544   1111    442       C  
ATOM   6637  CE2 PHE B 292     -23.961  -3.307  19.278  1.00 68.44           C  
ANISOU 6637  CE2 PHE B 292     8563   7949   9492   -529   1120    630       C  
ATOM   6638  CZ  PHE B 292     -22.584  -3.260  19.196  1.00 65.48           C  
ANISOU 6638  CZ  PHE B 292     8274   7579   9027   -491   1164    537       C  
ATOM   6639  N   PHE B 293     -25.627   0.151  13.180  1.00 66.55           N  
ANISOU 6639  N   PHE B 293     8335   7975   8975   -878    707    547       N  
ATOM   6640  CA  PHE B 293     -26.343   0.444  11.932  1.00 68.51           C  
ANISOU 6640  CA  PHE B 293     8522   8339   9170   -974    608    594       C  
ATOM   6641  C   PHE B 293     -25.494   0.136  10.683  1.00 73.79           C  
ANISOU 6641  C   PHE B 293     9319   8993   9726  -1021    549    439       C  
ATOM   6642  O   PHE B 293     -26.044  -0.052   9.590  1.00 75.01           O  
ANISOU 6642  O   PHE B 293     9457   9234   9809  -1140    439    438       O  
ATOM   6643  CB  PHE B 293     -26.929   1.863  11.955  1.00 70.70           C  
ANISOU 6643  CB  PHE B 293     8674   8735   9453   -875    671    749       C  
ATOM   6644  CG  PHE B 293     -28.181   2.022  12.788  1.00 73.72           C  
ANISOU 6644  CG  PHE B 293     8916   9174   9921   -850    709    959       C  
ATOM   6645  CD1 PHE B 293     -29.431   2.116  12.185  1.00 78.92           C  
ANISOU 6645  CD1 PHE B 293     9412   9991  10582   -935    639   1150       C  
ATOM   6646  CD2 PHE B 293     -28.108   2.117  14.174  1.00 75.67           C  
ANISOU 6646  CD2 PHE B 293     9182   9339  10232   -729    820    992       C  
ATOM   6647  CE1 PHE B 293     -30.588   2.303  12.958  1.00 80.79           C  
ANISOU 6647  CE1 PHE B 293     9501  10297  10899   -883    694   1399       C  
ATOM   6648  CE2 PHE B 293     -29.264   2.291  14.945  1.00 79.37           C  
ANISOU 6648  CE2 PHE B 293     9526   9862  10770   -666    876   1213       C  
ATOM   6649  CZ  PHE B 293     -30.496   2.385  14.334  1.00 79.02           C  
ANISOU 6649  CZ  PHE B 293     9314   9968  10742   -736    820   1428       C  
ATOM   6650  N   HIS B 294     -24.158   0.054  10.863  1.00 69.38           N  
ANISOU 6650  N   HIS B 294     8884   8338   9139   -926    622    325       N  
ATOM   6651  CA  HIS B 294     -23.185  -0.331   9.847  1.00 69.45           C  
ANISOU 6651  CA  HIS B 294     9035   8311   9041   -919    606    201       C  
ATOM   6652  C   HIS B 294     -23.577  -1.697   9.221  1.00 74.81           C  
ANISOU 6652  C   HIS B 294     9834   8917   9675  -1072    521    111       C  
ATOM   6653  O   HIS B 294     -23.310  -1.935   8.040  1.00 75.98           O  
ANISOU 6653  O   HIS B 294    10093   9077   9700  -1106    468     23       O  
ATOM   6654  CB  HIS B 294     -21.748  -0.341  10.423  1.00 69.08           C  
ANISOU 6654  CB  HIS B 294     9072   8183   8994   -790    715    157       C  
ATOM   6655  CG  HIS B 294     -21.388  -1.575  11.206  1.00 72.58           C  
ANISOU 6655  CG  HIS B 294     9600   8500   9477   -796    772    119       C  
ATOM   6656  ND1 HIS B 294     -21.292  -1.753  12.542  1.00 73.64           N  
ANISOU 6656  ND1 HIS B 294     9684   8603   9695   -752    844    168       N  
ATOM   6657  CD2 HIS B 294     -21.047  -2.765  10.576  1.00 75.16           C  
ANISOU 6657  CD2 HIS B 294    10090   8719   9748   -835    778     30       C  
ATOM   6658  CE1 HIS B 294     -20.912  -3.059  12.745  1.00 73.50           C  
ANISOU 6658  CE1 HIS B 294     9768   8470   9690   -760    900    130       C  
ATOM   6659  NE2 HIS B 294     -20.779  -3.620  11.548  1.00 74.79           N  
ANISOU 6659  NE2 HIS B 294    10070   8575   9771   -811    865     44       N  
ATOM   6660  N   CYS B 295     -24.224  -2.578  10.030  1.00 70.75           N  
ANISOU 6660  N   CYS B 295     9305   8320   9259  -1162    513    134       N  
ATOM   6661  CA  CYS B 295     -24.726  -3.890   9.620  1.00 72.16           C  
ANISOU 6661  CA  CYS B 295     9597   8393   9427  -1341    434     56       C  
ATOM   6662  C   CYS B 295     -25.845  -3.698   8.622  1.00 77.02           C  
ANISOU 6662  C   CYS B 295    10141   9150   9974  -1520    266     88       C  
ATOM   6663  O   CYS B 295     -26.017  -4.518   7.717  1.00 79.02           O  
ANISOU 6663  O   CYS B 295    10542   9350  10130  -1682    168    -30       O  
ATOM   6664  CB  CYS B 295     -25.223  -4.691  10.820  1.00 72.81           C  
ANISOU 6664  CB  CYS B 295     9627   8373   9664  -1382    473    122       C  
ATOM   6665  SG  CYS B 295     -23.943  -5.130  12.018  1.00 75.47           S  
ANISOU 6665  SG  CYS B 295    10033   8576  10065  -1187    671    105       S  
ATOM   6666  N   CYS B 296     -26.629  -2.622   8.825  1.00 72.12           N  
ANISOU 6666  N   CYS B 296     9296   8711   9395  -1492    242    260       N  
ATOM   6667  CA  CYS B 296     -27.794  -2.270   8.024  1.00 72.99           C  
ANISOU 6667  CA  CYS B 296     9263   9019   9450  -1642     99    372       C  
ATOM   6668  C   CYS B 296     -27.473  -1.573   6.719  1.00 75.52           C  
ANISOU 6668  C   CYS B 296     9602   9484   9609  -1613     57    327       C  
ATOM   6669  O   CYS B 296     -28.179  -1.808   5.741  1.00 76.26           O  
ANISOU 6669  O   CYS B 296     9673   9710   9593  -1792    -94    332       O  
ATOM   6670  CB  CYS B 296     -28.792  -1.464   8.850  1.00 73.11           C  
ANISOU 6670  CB  CYS B 296     9028   9168   9584  -1589    134    623       C  
ATOM   6671  SG  CYS B 296     -29.491  -2.366  10.256  1.00 77.26           S  
ANISOU 6671  SG  CYS B 296     9487   9577  10294  -1642    153    732       S  
ATOM   6672  N   LEU B 297     -26.425  -0.720   6.685  1.00 70.33           N  
ANISOU 6672  N   LEU B 297     8976   8817   8931  -1399    180    296       N  
ATOM   6673  CA  LEU B 297     -26.098   0.042   5.475  1.00 70.61           C  
ANISOU 6673  CA  LEU B 297     8997   9000   8831  -1335    161    288       C  
ATOM   6674  C   LEU B 297     -25.657  -0.715   4.230  1.00 77.72           C  
ANISOU 6674  C   LEU B 297    10096   9884   9548  -1412     73    114       C  
ATOM   6675  O   LEU B 297     -25.482  -0.084   3.190  1.00 78.09           O  
ANISOU 6675  O   LEU B 297    10111  10086   9474  -1351     51    129       O  
ATOM   6676  CB  LEU B 297     -25.283   1.325   5.706  1.00 68.59           C  
ANISOU 6676  CB  LEU B 297     8676   8763   8621  -1105    306    351       C  
ATOM   6677  CG  LEU B 297     -24.059   1.248   6.571  1.00 71.74           C  
ANISOU 6677  CG  LEU B 297     9192   8979   9088   -971    428    270       C  
ATOM   6678  CD1 LEU B 297     -22.806   1.142   5.738  1.00 71.83           C  
ANISOU 6678  CD1 LEU B 297     9348   8952   8993   -873    457    164       C  
ATOM   6679  CD2 LEU B 297     -23.960   2.488   7.386  1.00 73.31           C  
ANISOU 6679  CD2 LEU B 297     9269   9194   9392   -841    541    385       C  
ATOM   6680  N   ASN B 298     -25.537  -2.047   4.292  1.00 76.08           N  
ANISOU 6680  N   ASN B 298    10098   9495   9313  -1540     31    -40       N  
ATOM   6681  CA  ASN B 298     -25.218  -2.822   3.096  1.00 77.88           C  
ANISOU 6681  CA  ASN B 298    10564   9683   9342  -1623    -45   -220       C  
ATOM   6682  C   ASN B 298     -26.538  -3.107   2.347  1.00 83.42           C  
ANISOU 6682  C   ASN B 298    11199  10556   9942  -1904   -258   -200       C  
ATOM   6683  O   ASN B 298     -26.677  -2.597   1.234  1.00 83.32           O  
ANISOU 6683  O   ASN B 298    11145  10751   9762  -1909   -336   -189       O  
ATOM   6684  CB  ASN B 298     -24.413  -4.084   3.415  1.00 81.18           C  
ANISOU 6684  CB  ASN B 298    11275   9808   9761  -1615     41   -392       C  
ATOM   6685  CG  ASN B 298     -23.753  -4.709   2.209  1.00107.50           C  
ANISOU 6685  CG  ASN B 298    14907  13067  12872  -1601     37   -574       C  
ATOM   6686  OD1 ASN B 298     -24.278  -5.643   1.590  1.00104.66           O  
ANISOU 6686  OD1 ASN B 298    14738  12636  12390  -1818    -79   -715       O  
ATOM   6687  ND2 ASN B 298     -22.558  -4.238   1.881  1.00 97.61           N  
ANISOU 6687  ND2 ASN B 298    13716  11812  11558  -1344    170   -570       N  
ATOM   6688  N   PRO B 299     -27.555  -3.797   2.940  1.00 81.76           N  
ANISOU 6688  N   PRO B 299    10929  10304   9831  -2134   -358   -155       N  
ATOM   6689  CA  PRO B 299     -28.824  -4.009   2.213  1.00 84.68           C  
ANISOU 6689  CA  PRO B 299    11198  10877  10098  -2430   -583    -97       C  
ATOM   6690  C   PRO B 299     -29.596  -2.718   1.952  1.00 89.43           C  
ANISOU 6690  C   PRO B 299    11456  11828  10695  -2384   -619    167       C  
ATOM   6691  O   PRO B 299     -30.275  -2.614   0.931  1.00 91.34           O  
ANISOU 6691  O   PRO B 299    11621  12317  10769  -2553   -784    210       O  
ATOM   6692  CB  PRO B 299     -29.613  -4.936   3.134  1.00 87.34           C  
ANISOU 6692  CB  PRO B 299    11511  11073  10600  -2642   -644    -53       C  
ATOM   6693  CG  PRO B 299     -28.613  -5.501   4.059  1.00 89.93           C  
ANISOU 6693  CG  PRO B 299    12024  11088  11058  -2473   -456   -171       C  
ATOM   6694  CD  PRO B 299     -27.604  -4.454   4.259  1.00 82.57           C  
ANISOU 6694  CD  PRO B 299    11042  10192  10138  -2146   -279   -135       C  
ATOM   6695  N   ILE B 300     -29.483  -1.733   2.872  1.00 84.09           N  
ANISOU 6695  N   ILE B 300    10585  11174  10192  -2153   -455    347       N  
ATOM   6696  CA  ILE B 300     -30.106  -0.416   2.731  1.00 83.48           C  
ANISOU 6696  CA  ILE B 300    10204  11382  10133  -2048   -419    615       C  
ATOM   6697  C   ILE B 300     -29.457   0.301   1.533  1.00 87.14           C  
ANISOU 6697  C   ILE B 300    10692  11993  10425  -1914   -397    564       C  
ATOM   6698  O   ILE B 300     -30.156   1.020   0.817  1.00 87.65           O  
ANISOU 6698  O   ILE B 300    10539  12358  10406  -1934   -449    748       O  
ATOM   6699  CB  ILE B 300     -30.123   0.388   4.079  1.00 84.28           C  
ANISOU 6699  CB  ILE B 300    10157  11413  10451  -1836   -229    790       C  
ATOM   6700  CG1 ILE B 300     -31.017  -0.300   5.168  1.00 85.33           C  
ANISOU 6700  CG1 ILE B 300    10212  11471  10737  -1969   -267    905       C  
ATOM   6701  CG2 ILE B 300     -30.485   1.872   3.910  1.00 84.25           C  
ANISOU 6701  CG2 ILE B 300     9909  11639  10465  -1658   -118   1041       C  
ATOM   6702  CD1 ILE B 300     -32.561  -0.609   4.824  1.00 95.76           C  
ANISOU 6702  CD1 ILE B 300    11310  13038  12035  -2238   -455   1134       C  
ATOM   6703  N   LEU B 301     -28.169  -0.007   1.230  1.00 83.12           N  
ANISOU 6703  N   LEU B 301    10441  11294   9848  -1787   -328    333       N  
ATOM   6704  CA  LEU B 301     -27.477   0.556   0.065  1.00 83.22           C  
ANISOU 6704  CA  LEU B 301    10493  11432   9694  -1643   -304    287       C  
ATOM   6705  C   LEU B 301     -28.102   0.378  -1.327  1.00 90.32           C  
ANISOU 6705  C   LEU B 301    11373  12599  10346  -1811   -487    276       C  
ATOM   6706  O   LEU B 301     -27.765   1.085  -2.281  1.00 90.42           O  
ANISOU 6706  O   LEU B 301    11325  12798  10231  -1669   -460    317       O  
ATOM   6707  CB  LEU B 301     -25.949   0.571   0.218  1.00 81.28           C  
ANISOU 6707  CB  LEU B 301    10452  10961   9472  -1406   -146    143       C  
ATOM   6708  CG  LEU B 301     -25.236   1.921   0.394  1.00 83.57           C  
ANISOU 6708  CG  LEU B 301    10594  11295   9864  -1131     25    278       C  
ATOM   6709  CD1 LEU B 301     -23.947   1.935  -0.373  1.00 83.27           C  
ANISOU 6709  CD1 LEU B 301    10721  11204   9716   -949     92    172       C  
ATOM   6710  CD2 LEU B 301     -26.092   3.104  -0.050  1.00 86.10           C  
ANISOU 6710  CD2 LEU B 301    10618  11907  10190  -1098     28    513       C  
ATOM   6711  N   TYR B 302     -29.040  -0.556  -1.419  1.00 89.33           N  
ANISOU 6711  N   TYR B 302    11284  12505  10154  -2124   -678    234       N  
ATOM   6712  CA  TYR B 302     -29.823  -0.809  -2.610  1.00 92.53           C  
ANISOU 6712  CA  TYR B 302    11655  13187  10316  -2360   -894    235       C  
ATOM   6713  C   TYR B 302     -31.025   0.145  -2.533  1.00 97.39           C  
ANISOU 6713  C   TYR B 302    11850  14159  10995  -2401   -927    593       C  
ATOM   6714  O   TYR B 302     -32.101  -0.181  -2.019  1.00 98.26           O  
ANISOU 6714  O   TYR B 302    11806  14340  11186  -2625  -1037    743       O  
ATOM   6715  CB  TYR B 302     -30.093  -2.316  -2.541  1.00 95.93           C  
ANISOU 6715  CB  TYR B 302    12365  13402  10684  -2678  -1057      6       C  
ATOM   6716  CG  TYR B 302     -28.818  -3.130  -2.586  1.00 97.33           C  
ANISOU 6716  CG  TYR B 302    12954  13219  10808  -2561   -950   -301       C  
ATOM   6717  CD1 TYR B 302     -28.097  -3.272  -3.768  1.00100.73           C  
ANISOU 6717  CD1 TYR B 302    13623  13671  10977  -2478   -958   -483       C  
ATOM   6718  CD2 TYR B 302     -28.331  -3.761  -1.447  1.00 96.61           C  
ANISOU 6718  CD2 TYR B 302    13006  12781  10920  -2509   -824   -382       C  
ATOM   6719  CE1 TYR B 302     -26.923  -4.021  -3.816  1.00101.24           C  
ANISOU 6719  CE1 TYR B 302    14070  13409  10987  -2338   -828   -723       C  
ATOM   6720  CE2 TYR B 302     -27.164  -4.523  -1.485  1.00 97.28           C  
ANISOU 6720  CE2 TYR B 302    13453  12554  10955  -2384   -698   -618       C  
ATOM   6721  CZ  TYR B 302     -26.466  -4.653  -2.674  1.00106.28           C  
ANISOU 6721  CZ  TYR B 302    14836  13709  11836  -2295   -695   -781       C  
ATOM   6722  OH  TYR B 302     -25.312  -5.394  -2.719  1.00107.47           O  
ANISOU 6722  OH  TYR B 302    15345  13557  11931  -2139   -541   -973       O  
ATOM   6723  N   ALA B 303     -30.778   1.367  -3.047  1.00 92.93           N  
ANISOU 6723  N   ALA B 303    11094  13813  10403  -2152   -804    756       N  
ATOM   6724  CA  ALA B 303     -31.684   2.503  -3.148  1.00117.16           C  
ANISOU 6724  CA  ALA B 303    13769  17231  13515  -2088   -757   1123       C  
ATOM   6725  C   ALA B 303     -31.057   3.421  -4.198  1.00145.84           C  
ANISOU 6725  C   ALA B 303    17338  21056  17019  -1847   -661   1159       C  
ATOM   6726  O   ALA B 303     -29.847   3.655  -4.174  1.00104.72           O  
ANISOU 6726  O   ALA B 303    12303  15632  11854  -1609   -515   1006       O  
ATOM   6727  CB  ALA B 303     -31.911   3.280  -1.857  1.00115.50           C  
ANISOU 6727  CB  ALA B 303    13381  16917  13588  -1911   -552   1347       C  
TER    6728      ALA B 303                                                      
HETATM 6729  C1  ITD A1500      15.447   3.740  25.057  1.00125.07           C  
HETATM 6730  N1  ITD A1500      17.820   3.574  25.506  1.00125.28           N  
HETATM 6731  S1  ITD A1500      19.844   2.575  27.206  1.00124.03           S  
HETATM 6732  C2  ITD A1500      16.639   4.411  25.718  1.00124.99           C  
HETATM 6733  N2  ITD A1500      17.674   3.862  27.649  1.00126.28           N  
HETATM 6734  S2  ITD A1500      18.064   5.878  30.162  1.00122.80           S  
HETATM 6735  C3  ITD A1500      16.876   5.824  25.211  1.00125.26           C  
HETATM 6736  N3  ITD A1500      19.839   5.122  31.662  1.00125.41           N  
HETATM 6737  C4  ITD A1500      18.395   3.354  26.693  1.00124.47           C  
HETATM 6738  N4  ITD A1500      20.659   6.519  29.921  1.00120.74           N  
HETATM 6739  C5  ITD A1500      19.450   2.964  28.852  1.00126.84           C  
HETATM 6740  C6  ITD A1500      16.447   4.519  27.227  1.00125.32           C  
HETATM 6741  C7  ITD A1500      18.219   3.670  28.867  1.00126.87           C  
HETATM 6742  C8  ITD A1500      17.526   4.196  30.094  1.00124.41           C  
HETATM 6743  C9  ITD A1500      19.662   5.871  30.576  1.00122.80           C  
HETATM 6744  C10 ITD A1500      21.020   4.795  32.393  1.00128.09           C  
HETATM 6745  C11 ITD A1500      21.678   6.025  33.010  1.00129.55           C  
HETATM 6746  C12 ITD A1500      22.882   5.605  33.866  1.00129.06           C  
HETATM 6747  C13 ITD A1500      23.839   4.666  33.105  1.00129.27           C  
HETATM 6748  C14 ITD A1500      23.134   3.456  32.484  1.00129.70           C  
HETATM 6749  C15 ITD A1500      21.982   3.911  31.588  1.00128.71           C  
HETATM 6750  C16 ITD A1500      20.776   7.108  28.566  1.00120.23           C  
HETATM 6751  C17 ITD A1500      19.982   6.479  27.402  1.00119.93           C  
HETATM 6752  C18 ITD A1500      20.020   7.267  26.077  1.00118.76           C  
HETATM 6753  C19 ITD A1500      20.008   8.796  26.205  1.00118.17           C  
HETATM 6754  C20 ITD A1500      21.045   9.287  27.212  1.00119.17           C  
HETATM 6755  C21 ITD A1500      20.800   8.647  28.581  1.00120.14           C  
HETATM 6756  C1  ITD B1500     -16.630  -3.829  23.819  1.00 91.72           C  
HETATM 6757  N1  ITD B1500     -18.948  -3.455  24.254  1.00 93.82           N  
HETATM 6758  S1  ITD B1500     -21.358  -3.033  25.651  1.00 93.84           S  
HETATM 6759  C2  ITD B1500     -17.859  -4.384  24.508  1.00 91.88           C  
HETATM 6760  N2  ITD B1500     -19.086  -4.023  26.337  1.00 91.62           N  
HETATM 6761  S2  ITD B1500     -19.914  -6.358  28.742  1.00 83.04           S  
HETATM 6762  C3  ITD B1500     -18.197  -5.792  24.034  1.00 91.71           C  
HETATM 6763  N3  ITD B1500     -21.844  -5.437  30.024  1.00 81.54           N  
HETATM 6764  C4  ITD B1500     -19.729  -3.496  25.333  1.00 92.46           C  
HETATM 6765  N4  ITD B1500     -22.437  -7.064  28.424  1.00 80.64           N  
HETATM 6766  C5  ITD B1500     -21.157  -3.576  27.289  1.00 93.82           C  
HETATM 6767  C6  ITD B1500     -17.718  -4.405  26.032  1.00 91.22           C  
HETATM 6768  C7  ITD B1500     -19.841  -4.098  27.454  1.00 91.26           C  
HETATM 6769  C8  ITD B1500     -19.294  -4.692  28.726  1.00 87.68           C  
HETATM 6770  C9  ITD B1500     -21.533  -6.318  29.067  1.00 81.78           C  
HETATM 6771  C10 ITD B1500     -23.116  -5.043  30.618  1.00 79.91           C  
HETATM 6772  C11 ITD B1500     -23.747  -5.986  31.617  1.00 78.76           C  
HETATM 6773  C12 ITD B1500     -24.605  -5.103  32.516  1.00 77.71           C  
HETATM 6774  C13 ITD B1500     -25.655  -4.327  31.705  1.00 78.66           C  
HETATM 6775  C14 ITD B1500     -25.076  -3.561  30.508  1.00 77.91           C  
HETATM 6776  C15 ITD B1500     -24.169  -4.444  29.670  1.00 79.10           C  
HETATM 6777  C16 ITD B1500     -22.393  -7.693  27.105  1.00 77.82           C  
HETATM 6778  C17 ITD B1500     -21.681  -6.964  25.965  1.00 75.95           C  
HETATM 6779  C18 ITD B1500     -21.296  -7.816  24.738  1.00 76.07           C  
HETATM 6780  C19 ITD B1500     -21.310  -9.349  24.854  1.00 77.16           C  
HETATM 6781  C20 ITD B1500     -22.373  -9.848  25.824  1.00 75.62           C  
HETATM 6782  C21 ITD B1500     -22.138  -9.200  27.177  1.00 75.27           C  
CONECT    6 3146                                                                
CONECT  637 1259                                                                
CONECT 1259  637                                                                
CONECT 1596 1604                                                                
CONECT 1604 1596                                                                
CONECT 3146    6                                                                
CONECT 3958 4581                                                                
CONECT 4581 3958                                                                
CONECT 4918 4926                                                                
CONECT 4926 4918                                                                
CONECT 6729 6732                                                                
CONECT 6730 6732 6737                                                           
CONECT 6731 6737 6739                                                           
CONECT 6732 6729 6730 6735 6740                                                 
CONECT 6733 6737 6740 6741                                                      
CONECT 6734 6742 6743                                                           
CONECT 6735 6732                                                                
CONECT 6736 6743 6744                                                           
CONECT 6737 6730 6731 6733                                                      
CONECT 6738 6743 6750                                                           
CONECT 6739 6731 6741                                                           
CONECT 6740 6732 6733                                                           
CONECT 6741 6733 6739 6742                                                      
CONECT 6742 6734 6741                                                           
CONECT 6743 6734 6736 6738                                                      
CONECT 6744 6736 6745 6749                                                      
CONECT 6745 6744 6746                                                           
CONECT 6746 6745 6747                                                           
CONECT 6747 6746 6748                                                           
CONECT 6748 6747 6749                                                           
CONECT 6749 6744 6748                                                           
CONECT 6750 6738 6751 6755                                                      
CONECT 6751 6750 6752                                                           
CONECT 6752 6751 6753                                                           
CONECT 6753 6752 6754                                                           
CONECT 6754 6753 6755                                                           
CONECT 6755 6750 6754                                                           
CONECT 6756 6759                                                                
CONECT 6757 6759 6764                                                           
CONECT 6758 6764 6766                                                           
CONECT 6759 6756 6757 6762 6767                                                 
CONECT 6760 6764 6767 6768                                                      
CONECT 6761 6769 6770                                                           
CONECT 6762 6759                                                                
CONECT 6763 6770 6771                                                           
CONECT 6764 6757 6758 6760                                                      
CONECT 6765 6770 6777                                                           
CONECT 6766 6758 6768                                                           
CONECT 6767 6759 6760                                                           
CONECT 6768 6760 6766 6769                                                      
CONECT 6769 6761 6768                                                           
CONECT 6770 6761 6763 6765                                                      
CONECT 6771 6763 6772 6776                                                      
CONECT 6772 6771 6773                                                           
CONECT 6773 6772 6774                                                           
CONECT 6774 6773 6775                                                           
CONECT 6775 6774 6776                                                           
CONECT 6776 6771 6775                                                           
CONECT 6777 6765 6778 6782                                                      
CONECT 6778 6777 6779                                                           
CONECT 6779 6778 6780                                                           
CONECT 6780 6779 6781                                                           
CONECT 6781 6780 6782                                                           
CONECT 6782 6777 6781                                                           
MASTER      617    0    2   44   10    0    6    6 6780    2   64   78          
END