HEADER    MEMBRANE PROTEIN                        18-JUN-20   6ZFZ              
TITLE     STRUCTURE OF M1-STAR-T4L IN COMPLEX WITH 77-LH-28-1 AT 2.17A          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MUSCARINIC ACETYLCHOLINE RECEPTOR M1,ENDOLYSIN,MUSCARINIC  
COMPND   3 ACETYLCHOLINE RECEPTOR M1;                                           
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: LYSIS PROTEIN,LYSOZYME,MURAMIDASE;                          
COMPND   6 EC: 3.2.1.17;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4;          
SOURCE   3 ORGANISM_COMMON: HUMAN, BACTERIOPHAGE T4;                            
SOURCE   4 ORGANISM_TAXID: 9606, 10665;                                         
SOURCE   5 GENE: CHRM1;                                                         
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    GPCR, 7TM, MEMBRANE PROTEIN                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.RUCKTOOA,R.M.COOKE                                                  
REVDAT   3   08-DEC-21 6ZFZ    1       JRNL                                     
REVDAT   2   01-DEC-21 6ZFZ    1       JRNL   REMARK                            
REVDAT   1   06-OCT-21 6ZFZ    0                                                
JRNL        AUTH   A.J.H.BROWN,S.J.BRADLEY,F.H.MARSHALL,G.A.BROWN,K.A.BENNETT,  
JRNL        AUTH 2 J.BROWN,J.E.CANSFIELD,D.M.CROSS,C.DE GRAAF,B.D.HUDSON,       
JRNL        AUTH 3 L.DWOMOH,J.M.DIAS,J.C.ERREY,E.HURRELL,J.LIPTROT,G.MATTEDI,   
JRNL        AUTH 4 C.MOLLOY,P.J.NATHAN,K.OKRASA,G.OSBORNE,J.C.PATEL,            
JRNL        AUTH 5 M.PICKWORTH,N.ROBERTSON,S.SHAHABI,C.BUNDGAARD,K.PHILLIPS,    
JRNL        AUTH 6 L.M.BROAD,A.V.GOONAWARDENA,S.R.MORAIRTY,M.BROWNING,F.PERINI, 
JRNL        AUTH 7 G.R.DAWSON,J.F.W.DEAKIN,R.T.SMITH,P.M.SEXTON,J.WARNECK,      
JRNL        AUTH 8 M.VINSON,T.TASKER,B.G.TEHAN,B.TEOBALD,A.CHRISTOPOULOS,       
JRNL        AUTH 9 C.J.LANGMEAD,A.JAZAYERI,R.M.COOKE,P.RUCKTOOA,M.S.CONGREVE,   
JRNL        AUTH10 M.WEIR,A.B.TOBIN                                             
JRNL        TITL   FROM STRUCTURE TO CLINIC: DESIGN OF A MUSCARINIC M1 RECEPTOR 
JRNL        TITL 2 AGONIST WITH POTENTIAL TO TREATMENT OF ALZHEIMER'S DISEASE.  
JRNL        REF    CELL                          V. 184  5886 2021              
JRNL        REFN                   ISSN 1097-4172                               
JRNL        PMID   34822784                                                     
JRNL        DOI    10.1016/J.CELL.2021.11.001                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.17 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.7                                        
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) : 2.17                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.30                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 72.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 25204                          
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)  : 0.215                          
REMARK   3   R VALUE            (WORKING SET)  : 0.214                          
REMARK   3   FREE R VALUE                      : 0.242                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.740                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1194                           
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               : 50                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.17                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.31                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 8.72                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 505                      
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2346                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 493                      
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2318                   
REMARK   3   BIN FREE R VALUE                        : 0.3710                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 2.38                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 12                       
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3556                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 249                                     
REMARK   3   SOLVENT ATOMS            : 33                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.75                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.85270                                             
REMARK   3    B22 (A**2) : 5.50730                                              
REMARK   3    B33 (A**2) : -1.65460                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.350               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.317               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.224               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.324               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.228               
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      : 0.919                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.903                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3896   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 5232   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1436   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : NULL   ; NULL   ; NULL                
REMARK   3    GENERAL PLANES            : 614    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3896   ; 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   : 491    ; 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   : 4330   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.90                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.22                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 17.80                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|20 - A|219 A|354 - A|439 }                         
REMARK   3    ORIGIN FOR THE GROUP (A):   20.8746   17.9193    6.0000           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1087 T22:   -0.0055                                    
REMARK   3     T33:   -0.1069 T12:   -0.0095                                    
REMARK   3     T13:   -0.0283 T23:   -0.0058                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.7828 L22:    0.6279                                    
REMARK   3     L33:    2.1592 L12:   -0.0483                                    
REMARK   3     L13:   -0.2085 L23:   -0.1600                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0063 S12:   -0.2301 S13:   -0.0384                     
REMARK   3     S21:    0.0708 S22:   -0.0072 S23:    0.0113                     
REMARK   3     S31:   -0.0064 S32:   -0.0201 S33:    0.0135                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { A|1002 - A|1161 }                                    
REMARK   3    ORIGIN FOR THE GROUP (A):   13.2308   -3.0518   41.8884           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1504 T22:   -0.1255                                    
REMARK   3     T33:   -0.3040 T12:    0.0777                                    
REMARK   3     T13:    0.0434 T23:    0.1079                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    5.6083 L22:    3.5569                                    
REMARK   3     L33:    3.3624 L12:    1.3782                                    
REMARK   3     L13:   -0.8420 L23:   -1.3789                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1832 S12:    0.2866 S13:   -0.1318                     
REMARK   3     S21:   -0.0311 S22:   -0.1173 S23:   -0.2697                     
REMARK   3     S31:    0.2305 S32:    0.1743 S33:    0.3004                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6ZFZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-JUN-20.                  
REMARK 100 THE DEPOSITION ID IS D_1292109482.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-MAY-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.4-7.8                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I24                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.96861                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25204                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.170                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.1                               
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.17                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.34                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: 2Y00                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NAHEPES PH 7.4-7.8, 0.1M DI         
REMARK 280  -AMMONIUM HYDROGENPHOSPHATE, 30-38% PEG300, LIPIDIC CUBIC PHASE,    
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-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   SMTRY1   2 -1.000000  0.000000  0.000000       31.17050            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       78.29800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.81550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       78.29800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.17050            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       32.81550            
REMARK 290   SMTRY3   4  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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4830 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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     HIS A   440                                                      
REMARK 465     HIS A   441                                                      
REMARK 465     HIS A   442                                                      
REMARK 465     HIS A   443                                                      
REMARK 465     HIS A   444                                                      
REMARK 465     HIS A   445                                                      
REMARK 465     HIS A   446                                                      
REMARK 465     HIS A   447                                                      
REMARK 465     HIS A   448                                                      
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    PHE A  77      -69.86    -94.78                                   
REMARK 500    LEU A 131      -60.33   -100.53                                   
REMARK 500    SER A 184      -75.60    -69.54                                   
REMARK 500    PHE A 197      -64.27   -131.18                                   
REMARK 500    PHE A1114       53.45    -90.55                                   
REMARK 500    LYS A 392      -70.18    -30.66                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  6ZFZ A   27   219  UNP    P11229   ACM1_HUMAN      27    219             
DBREF  6ZFZ A 1002  1161  UNP    P00720   ENLYS_BPT4       2    161             
DBREF  6ZFZ A  354   438  UNP    P11229   ACM1_HUMAN     354    438             
SEQADV 6ZFZ MET A   20  UNP  P11229              INITIATING METHIONINE          
SEQADV 6ZFZ GLU A   21  UNP  P11229              EXPRESSION TAG                 
SEQADV 6ZFZ THR A   22  UNP  P11229              EXPRESSION TAG                 
SEQADV 6ZFZ VAL A   23  UNP  P11229              EXPRESSION TAG                 
SEQADV 6ZFZ GLU A   24  UNP  P11229              EXPRESSION TAG                 
SEQADV 6ZFZ MET A   25  UNP  P11229              EXPRESSION TAG                 
SEQADV 6ZFZ VAL A   26  UNP  P11229              EXPRESSION TAG                 
SEQADV 6ZFZ ALA A   27  UNP  P11229    PHE    27 ENGINEERED MUTATION            
SEQADV 6ZFZ ALA A   29  UNP  P11229    GLY    29 CONFLICT                       
SEQADV 6ZFZ THR A   30  UNP  P11229    ILE    30 CONFLICT                       
SEQADV 6ZFZ VAL A   31  UNP  P11229    THR    31 CONFLICT                       
SEQADV 6ZFZ ALA A   32  UNP  P11229    THR    32 ENGINEERED MUTATION            
SEQADV 6ZFZ ILE A   44  UNP  P11229    LEU    44 ENGINEERED MUTATION            
SEQADV 6ZFZ LEU A   46  UNP  P11229    VAL    46 ENGINEERED MUTATION            
SEQADV 6ZFZ MET A   47  UNP  P11229    LEU    47 CONFLICT                       
SEQADV 6ZFZ LEU A   48  UNP  P11229    ILE    48 CONFLICT                       
SEQADV 6ZFZ ILE A   50  UNP  P11229    PHE    50 CONFLICT                       
SEQADV 6ZFZ ARG A   54  UNP  P11229    THR    54 CONFLICT                       
SEQADV 6ZFZ GLN A   55  UNP  P11229    GLU    55 CONFLICT                       
SEQADV 6ZFZ GLN A   57  UNP  P11229    LYS    57 CONFLICT                       
SEQADV 6ZFZ ALA A   64  UNP  P11229    LEU    64 ENGINEERED MUTATION            
SEQADV 6ZFZ PHE A   65  UNP  P11229    LEU    65 CONFLICT                       
SEQADV 6ZFZ ALA A   76  UNP  P11229    THR    76 ENGINEERED MUTATION            
SEQADV 6ZFZ VAL A   84  UNP  P11229    THR    84 ENGINEERED MUTATION            
SEQADV 6ZFZ ILE A   86  UNP  P11229    LEU    86 CONFLICT                       
SEQADV 6ZFZ ILE A   87  UNP  P11229    LEU    87 CONFLICT                       
SEQADV 6ZFZ ALA A   95  UNP  P11229    THR    95 ENGINEERED MUTATION            
SEQADV 6ZFZ ALA A  101  UNP  P11229    TRP   101 ENGINEERED MUTATION            
SEQADV 6ZFZ ALA A  112  UNP  P11229    SER   112 ENGINEERED MUTATION            
SEQADV 6ZFZ LEU A  143  UNP  P11229    ALA   143 ENGINEERED MUTATION            
SEQADV 6ZFZ THR A  196  UNP  P11229    ALA   196 ENGINEERED MUTATION            
SEQADV 6ZFZ GLY A 1012  UNP  P00720    ARG    12 CONFLICT                       
SEQADV 6ZFZ THR A 1054  UNP  P00720    CYS    54 CONFLICT                       
SEQADV 6ZFZ ALA A 1097  UNP  P00720    CYS    97 CONFLICT                       
SEQADV 6ZFZ ARG A 1137  UNP  P00720    ILE   137 CONFLICT                       
SEQADV 6ZFZ ALA A  362  UNP  P11229    LYS   362 ENGINEERED MUTATION            
SEQADV 6ZFZ LEU A  364  UNP  P11229    ALA   364 ENGINEERED MUTATION            
SEQADV 6ZFZ ALA A  411  UNP  P11229    SER   411 ENGINEERED MUTATION            
SEQADV 6ZFZ ALA A  435  UNP  P11229    CYS   435 CONFLICT                       
SEQADV 6ZFZ HIS A  439  UNP  P11229              EXPRESSION TAG                 
SEQADV 6ZFZ HIS A  440  UNP  P11229              EXPRESSION TAG                 
SEQADV 6ZFZ HIS A  441  UNP  P11229              EXPRESSION TAG                 
SEQADV 6ZFZ HIS A  442  UNP  P11229              EXPRESSION TAG                 
SEQADV 6ZFZ HIS A  443  UNP  P11229              EXPRESSION TAG                 
SEQADV 6ZFZ HIS A  444  UNP  P11229              EXPRESSION TAG                 
SEQADV 6ZFZ HIS A  445  UNP  P11229              EXPRESSION TAG                 
SEQADV 6ZFZ HIS A  446  UNP  P11229              EXPRESSION TAG                 
SEQADV 6ZFZ HIS A  447  UNP  P11229              EXPRESSION TAG                 
SEQADV 6ZFZ HIS A  448  UNP  P11229              EXPRESSION TAG                 
SEQRES   1 A  455  MET GLU THR VAL GLU MET VAL ALA ILE ALA THR VAL ALA          
SEQRES   2 A  455  GLY LEU LEU SER LEU ALA THR VAL THR GLY ASN ILE LEU          
SEQRES   3 A  455  LEU MET LEU SER ILE LYS VAL ASN ARG GLN LEU GLN THR          
SEQRES   4 A  455  VAL ASN ASN TYR PHE ALA PHE SER LEU ALA CYS ALA ASP          
SEQRES   5 A  455  LEU ILE ILE GLY ALA PHE SER MET ASN LEU TYR THR VAL          
SEQRES   6 A  455  TYR ILE ILE MET GLY HIS TRP ALA LEU GLY ALA LEU ALA          
SEQRES   7 A  455  CYS ASP LEU ALA LEU ALA LEU ASP TYR VAL ALA SER ASN          
SEQRES   8 A  455  ALA ALA VAL MET ASN LEU LEU LEU ILE SER PHE ASP ARG          
SEQRES   9 A  455  TYR PHE SER VAL THR ARG PRO LEU SER TYR ARG ALA LYS          
SEQRES  10 A  455  ARG THR PRO ARG ARG ALA LEU LEU MET ILE GLY LEU ALA          
SEQRES  11 A  455  TRP LEU VAL SER PHE VAL LEU TRP ALA PRO ALA ILE LEU          
SEQRES  12 A  455  PHE TRP GLN TYR LEU VAL GLY GLU ARG THR VAL LEU ALA          
SEQRES  13 A  455  GLY GLN CYS TYR ILE GLN PHE LEU SER GLN PRO ILE ILE          
SEQRES  14 A  455  THR PHE GLY THR ALA MET ALA THR PHE TYR LEU PRO VAL          
SEQRES  15 A  455  THR VAL MET CYS THR LEU TYR TRP ARG ILE TYR ARG GLU          
SEQRES  16 A  455  THR GLU ASN ARG ALA ASN ILE PHE GLU MET LEU ARG ILE          
SEQRES  17 A  455  ASP GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP THR GLU          
SEQRES  18 A  455  GLY TYR TYR THR ILE GLY ILE GLY HIS LEU LEU THR LYS          
SEQRES  19 A  455  SER PRO SER LEU ASN ALA ALA LYS SER GLU LEU ASP LYS          
SEQRES  20 A  455  ALA ILE GLY ARG ASN THR ASN GLY VAL ILE THR LYS ASP          
SEQRES  21 A  455  GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP ALA ALA          
SEQRES  22 A  455  VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS PRO VAL          
SEQRES  23 A  455  TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA LEU ILE          
SEQRES  24 A  455  ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL ALA GLY          
SEQRES  25 A  455  PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS ARG TRP          
SEQRES  26 A  455  ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG TRP TYR          
SEQRES  27 A  455  ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE THR THR          
SEQRES  28 A  455  PHE ARG THR GLY THR TRP ASP ALA TYR THR PHE SER LEU          
SEQRES  29 A  455  VAL LYS GLU LYS ALA ALA LEU ARG THR LEU SER ALA ILE          
SEQRES  30 A  455  LEU LEU ALA PHE ILE LEU THR TRP THR PRO TYR ASN ILE          
SEQRES  31 A  455  MET VAL LEU VAL SER THR PHE CYS LYS ASP CYS VAL PRO          
SEQRES  32 A  455  GLU THR LEU TRP GLU LEU GLY TYR TRP LEU CYS TYR VAL          
SEQRES  33 A  455  ASN ALA THR ILE ASN PRO MET CYS TYR ALA LEU CYS ASN          
SEQRES  34 A  455  LYS ALA PHE ARG ASP THR PHE ARG LEU LEU LEU LEU ALA          
SEQRES  35 A  455  ARG TRP ASP HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS          
HET    QJT  A1201      24                                                       
HET    OLA  A1202      20                                                       
HET    OLA  A1203      20                                                       
HET    OLA  A1204      20                                                       
HET    OLA  A1205      20                                                       
HET    PO4  A1206       5                                                       
HET    OLA  A1207      20                                                       
HET    OLA  A1208      20                                                       
HET    OLA  A1209      20                                                       
HET    OLA  A1210      20                                                       
HET    OLC  A1211      25                                                       
HET    EPE  A1212      15                                                       
HET    PGE  A1213      10                                                       
HET    PGE  A1214      10                                                       
HETNAM     QJT 1-[3-(4-BUTYLPIPERIDIN-1-YL)PROPYL]-3,4-                         
HETNAM   2 QJT  DIHYDROQUINOLIN-2-ONE                                           
HETNAM     OLA OLEIC ACID                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE                   
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID              
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETSYN     OLC 1-OLEOYL-R-GLYCEROL                                              
HETSYN     EPE HEPES                                                            
FORMUL   2  QJT    C21 H32 N2 O                                                 
FORMUL   3  OLA    8(C18 H34 O2)                                                
FORMUL   7  PO4    O4 P 3-                                                      
FORMUL  12  OLC    C21 H40 O4                                                   
FORMUL  13  EPE    C8 H18 N2 O4 S                                               
FORMUL  14  PGE    2(C6 H14 O4)                                                 
FORMUL  16  HOH   *33(H2 O)                                                     
HELIX    1 AA1 GLU A   21  ASN A   53  1                                  33    
HELIX    2 AA2 ARG A   54  GLN A   57  5                                   4    
HELIX    3 AA3 THR A   58  PHE A   77  1                                  20    
HELIX    4 AA4 PHE A   77  GLY A   89  1                                  13    
HELIX    5 AA5 GLY A   94  ARG A  129  1                                  36    
HELIX    6 AA6 SER A  132  LYS A  136  5                                   5    
HELIX    7 AA7 THR A  138  GLY A  169  1                                  32    
HELIX    8 AA8 GLN A  185  PHE A  197  1                                  13    
HELIX    9 AA9 PHE A  197  GLU A 1011  1                                  33    
HELIX   10 AB1 SER A 1038  GLY A 1051  1                                  14    
HELIX   11 AB2 THR A 1059  ASN A 1081  1                                  23    
HELIX   12 AB3 LEU A 1084  LEU A 1091  1                                   8    
HELIX   13 AB4 ASP A 1092  GLY A 1113  1                                  22    
HELIX   14 AB5 PHE A 1114  GLN A 1123  1                                  10    
HELIX   15 AB6 ARG A 1125  LYS A 1135  1                                  11    
HELIX   16 AB7 SER A 1136  THR A 1142  1                                   7    
HELIX   17 AB8 THR A 1142  GLY A 1156  1                                  15    
HELIX   18 AB9 LYS A  361  CYS A  391  1                                  31    
HELIX   19 AC1 PRO A  396  VAL A  409  1                                  14    
HELIX   20 AC2 VAL A  409  ASN A  422  1                                  14    
HELIX   21 AC3 ASN A  422  ASP A  438  1                                  17    
SHEET    1 AA1 3 ARG A1014  LYS A1019  0                                        
SHEET    2 AA1 3 TYR A1025  GLY A1028 -1  O  THR A1026   N  TYR A1018           
SHEET    3 AA1 3 HIS A1031  THR A1034 -1  O  LEU A1033   N  TYR A1025           
SSBOND   1 CYS A   98    CYS A  178                          1555   1555  2.05  
SSBOND   2 CYS A  391    CYS A  394                          1555   1555  2.04  
CISPEP   1 ASP A  438    HIS A  439          0         2.13                     
CRYST1   62.341   65.631  156.596  90.00  90.00  90.00 P 21 21 21    4          
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      0.016041  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015237  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006386        0.00000                         
ATOM      1  N   MET A  20      15.568  37.109 -18.140  1.00 75.80           N  
ANISOU    1  N   MET A  20     9803   9921   9075    975   -226   1573       N  
ATOM      2  CA  MET A  20      14.989  37.499 -16.855  1.00 75.51           C  
ANISOU    2  CA  MET A  20     9817   9729   9145   1041   -216   1489       C  
ATOM      3  C   MET A  20      15.019  39.021 -16.702  1.00 79.38           C  
ANISOU    3  C   MET A  20    10460   9969   9731   1119   -169   1605       C  
ATOM      4  O   MET A  20      16.078  39.633 -16.871  1.00 78.77           O  
ANISOU    4  O   MET A  20    10484   9745   9701   1015   -131   1664       O  
ATOM      5  CB  MET A  20      15.736  36.810 -15.694  1.00 77.72           C  
ANISOU    5  CB  MET A  20    10097   9946   9487    897   -208   1309       C  
ATOM      6  CG  MET A  20      14.996  36.872 -14.369  1.00 81.15           C  
ANISOU    6  CG  MET A  20    10540  10302   9993    964   -207   1194       C  
ATOM      7  SD  MET A  20      15.807  35.961 -13.028  1.00 85.05           S  
ANISOU    7  SD  MET A  20    11025  10752  10540    803   -203    998       S  
ATOM      8  CE  MET A  20      15.255  34.303 -13.379  1.00 81.57           C  
ANISOU    8  CE  MET A  20    10417  10582   9995    776   -254    919       C  
ATOM      9  N   GLU A  21      13.856  39.627 -16.388  1.00 76.11           N  
ANISOU    9  N   GLU A  21    10065   9508   9347   1302   -171   1638       N  
ATOM     10  CA  GLU A  21      13.738  41.079 -16.201  1.00 76.01           C  
ANISOU   10  CA  GLU A  21    10209   9240   9432   1407   -124   1741       C  
ATOM     11  C   GLU A  21      14.401  41.547 -14.895  1.00 79.21           C  
ANISOU   11  C   GLU A  21    10739   9388   9970   1315    -82   1612       C  
ATOM     12  O   GLU A  21      14.601  40.738 -13.982  1.00 78.93           O  
ANISOU   12  O   GLU A  21    10647   9399   9943   1222    -96   1441       O  
ATOM     13  CB  GLU A  21      12.279  41.565 -16.335  1.00 77.52           C  
ANISOU   13  CB  GLU A  21    10370   9478   9604   1654   -137   1822       C  
ATOM     14  CG  GLU A  21      11.318  41.048 -15.277  1.00 89.48           C  
ANISOU   14  CG  GLU A  21    11796  11078  11125   1734   -157   1669       C  
ATOM     15  CD  GLU A  21       9.854  41.361 -15.520  1.00114.82           C  
ANISOU   15  CD  GLU A  21    14932  14406  14290   1975   -176   1750       C  
ATOM     16  OE1 GLU A  21       9.513  42.557 -15.677  1.00112.02           O  
ANISOU   16  OE1 GLU A  21    14687  13887  13990   2137   -142   1876       O  
ATOM     17  OE2 GLU A  21       9.043  40.408 -15.538  1.00110.23           O  
ANISOU   17  OE2 GLU A  21    14182  14079  13620   2002   -224   1688       O  
ATOM     18  N   THR A  22      14.756  42.849 -14.826  1.00 74.69           N  
ANISOU   18  N   THR A  22    10339   8543   9496   1337    -32   1698       N  
ATOM     19  CA  THR A  22      15.448  43.473 -13.694  1.00 73.85           C  
ANISOU   19  CA  THR A  22    10372   8173   9514   1240      9   1584       C  
ATOM     20  C   THR A  22      14.661  43.372 -12.364  1.00 75.26           C  
ANISOU   20  C   THR A  22    10544   8316   9737   1337      9   1417       C  
ATOM     21  O   THR A  22      15.291  43.171 -11.324  1.00 74.56           O  
ANISOU   21  O   THR A  22    10486   8144   9698   1208     18   1259       O  
ATOM     22  CB  THR A  22      15.881  44.916 -14.030  1.00 83.44           C  
ANISOU   22  CB  THR A  22    11780   9099  10823   1244     63   1723       C  
ATOM     23  OG1 THR A  22      16.680  45.431 -12.965  1.00 83.15           O  
ANISOU   23  OG1 THR A  22    11871   8823  10898   1110     98   1594       O  
ATOM     24  CG2 THR A  22      14.706  45.857 -14.335  1.00 83.27           C  
ANISOU   24  CG2 THR A  22    11831   8982  10827   1501     81   1856       C  
ATOM     25  N   VAL A  23      13.311  43.479 -12.399  1.00 69.95           N  
ANISOU   25  N   VAL A  23     9817   7727   9035   1560     -2   1452       N  
ATOM     26  CA  VAL A  23      12.464  43.387 -11.202  1.00 68.82           C  
ANISOU   26  CA  VAL A  23     9651   7580   8919   1670      3   1306       C  
ATOM     27  C   VAL A  23      12.443  41.934 -10.654  1.00 70.68           C  
ANISOU   27  C   VAL A  23     9722   8050   9084   1562    -40   1153       C  
ATOM     28  O   VAL A  23      12.396  41.746  -9.436  1.00 70.05           O  
ANISOU   28  O   VAL A  23     9649   7927   9039   1538    -28    996       O  
ATOM     29  CB  VAL A  23      11.048  44.012 -11.404  1.00 72.67           C  
ANISOU   29  CB  VAL A  23    10126   8089   9397   1950     10   1399       C  
ATOM     30  CG1 VAL A  23      10.180  43.204 -12.368  1.00 72.53           C  
ANISOU   30  CG1 VAL A  23     9917   8393   9250   2036    -46   1489       C  
ATOM     31  CG2 VAL A  23      10.331  44.238 -10.076  1.00 72.47           C  
ANISOU   31  CG2 VAL A  23    10123   7989   9423   2067     37   1251       C  
ATOM     32  N   GLU A  24      12.535  40.925 -11.551  1.00 65.87           N  
ANISOU   32  N   GLU A  24     8976   7677   8375   1491    -85   1199       N  
ATOM     33  CA  GLU A  24      12.574  39.507 -11.177  1.00 64.93           C  
ANISOU   33  CA  GLU A  24     8713   7765   8192   1382   -124   1071       C  
ATOM     34  C   GLU A  24      13.918  39.145 -10.542  1.00 66.08           C  
ANISOU   34  C   GLU A  24     8906   7823   8380   1169   -114    962       C  
ATOM     35  O   GLU A  24      13.943  38.388  -9.572  1.00 65.39           O  
ANISOU   35  O   GLU A  24     8762   7794   8289   1105   -124    821       O  
ATOM     36  CB  GLU A  24      12.286  38.603 -12.385  1.00 66.45           C  
ANISOU   36  CB  GLU A  24     8762   8217   8268   1374   -173   1148       C  
ATOM     37  CG  GLU A  24      10.806  38.418 -12.676  1.00 79.37           C  
ANISOU   37  CG  GLU A  24    10282  10038   9838   1554   -202   1191       C  
ATOM     38  CD  GLU A  24      10.478  37.484 -13.826  1.00105.37           C  
ANISOU   38  CD  GLU A  24    13428  13602  13007   1533   -256   1244       C  
ATOM     39  OE1 GLU A  24      10.979  37.716 -14.951  1.00101.89           O  
ANISOU   39  OE1 GLU A  24    13009  13182  12521   1506   -262   1364       O  
ATOM     40  OE2 GLU A  24       9.705  36.524 -13.605  1.00101.39           O  
ANISOU   40  OE2 GLU A  24    12787  13293  12445   1538   -292   1164       O  
ATOM     41  N   MET A  25      15.026  39.706 -11.076  1.00 60.83           N  
ANISOU   41  N   MET A  25     8338   7025   7749   1061    -92   1036       N  
ATOM     42  CA  MET A  25      16.394  39.492 -10.591  1.00 59.90           C  
ANISOU   42  CA  MET A  25     8261   6831   7667    857    -82    954       C  
ATOM     43  C   MET A  25      16.595  40.039  -9.168  1.00 61.29           C  
ANISOU   43  C   MET A  25     8534   6820   7931    828    -54    820       C  
ATOM     44  O   MET A  25      17.245  39.383  -8.354  1.00 60.45           O  
ANISOU   44  O   MET A  25     8395   6749   7826    698    -64    694       O  
ATOM     45  CB  MET A  25      17.418  40.114 -11.556  1.00 62.35           C  
ANISOU   45  CB  MET A  25     8647   7051   7991    759    -60   1085       C  
ATOM     46  CG  MET A  25      17.604  39.333 -12.843  1.00 66.22           C  
ANISOU   46  CG  MET A  25     9027   7755   8377    726    -87   1177       C  
ATOM     47  SD  MET A  25      18.776  40.152 -13.954  1.00 70.60           S  
ANISOU   47  SD  MET A  25     9667   8216   8940    608    -51   1338       S  
ATOM     48  CE  MET A  25      18.942  38.916 -15.219  1.00 67.39           C  
ANISOU   48  CE  MET A  25     9103   8114   8388    582    -87   1392       C  
ATOM     49  N   VAL A  26      16.026  41.233  -8.876  1.00 56.11           N  
ANISOU   49  N   VAL A  26     8002   5972   7345    956    -20    845       N  
ATOM     50  CA  VAL A  26      16.095  41.912  -7.572  1.00 54.89           C  
ANISOU   50  CA  VAL A  26     7958   5626   7271    951     11    712       C  
ATOM     51  C   VAL A  26      15.293  41.131  -6.514  1.00 56.51           C  
ANISOU   51  C   VAL A  26     8063   5972   7437   1020     -5    571       C  
ATOM     52  O   VAL A  26      15.806  40.895  -5.417  1.00 56.24           O  
ANISOU   52  O   VAL A  26     8039   5912   7418    916     -3    427       O  
ATOM     53  CB  VAL A  26      15.678  43.411  -7.684  1.00 58.61           C  
ANISOU   53  CB  VAL A  26     8602   5839   7829   1083     59    786       C  
ATOM     54  CG1 VAL A  26      15.455  44.052  -6.313  1.00 58.33           C  
ANISOU   54  CG1 VAL A  26     8673   5627   7863   1122     91    628       C  
ATOM     55  CG2 VAL A  26      16.709  44.206  -8.478  1.00 58.37           C  
ANISOU   55  CG2 VAL A  26     8690   5638   7851    962     82    908       C  
ATOM     56  N   ALA A  27      14.055  40.710  -6.862  1.00 51.09           N  
ANISOU   56  N   ALA A  27     7268   5451   6692   1184    -22    618       N  
ATOM     57  CA  ALA A  27      13.154  39.943  -5.998  1.00 49.87           C  
ANISOU   57  CA  ALA A  27     7001   5457   6492   1256    -36    511       C  
ATOM     58  C   ALA A  27      13.747  38.592  -5.595  1.00 51.48           C  
ANISOU   58  C   ALA A  27     7093   5822   6644   1090    -70    418       C  
ATOM     59  O   ALA A  27      13.637  38.213  -4.430  1.00 51.14           O  
ANISOU   59  O   ALA A  27     7025   5808   6597   1070    -65    290       O  
ATOM     60  CB  ALA A  27      11.809  39.747  -6.679  1.00 50.62           C  
ANISOU   60  CB  ALA A  27     6987   5720   6528   1439    -53    604       C  
ATOM     61  N   ILE A  28      14.387  37.877  -6.543  1.00 46.02           N  
ANISOU   61  N   ILE A  28     6340   5235   5911    978   -100    484       N  
ATOM     62  CA  ILE A  28      15.018  36.585  -6.270  1.00 44.75           C  
ANISOU   62  CA  ILE A  28     6084   5213   5706    831   -129    408       C  
ATOM     63  C   ILE A  28      16.220  36.789  -5.342  1.00 46.54           C  
ANISOU   63  C   ILE A  28     6389   5312   5982    686   -114    312       C  
ATOM     64  O   ILE A  28      16.315  36.098  -4.328  1.00 45.80           O  
ANISOU   64  O   ILE A  28     6248   5281   5871    634   -123    201       O  
ATOM     65  CB  ILE A  28      15.348  35.791  -7.574  1.00 47.85           C  
ANISOU   65  CB  ILE A  28     6394   5750   6038    769   -161    498       C  
ATOM     66  CG1 ILE A  28      14.047  35.339  -8.284  1.00 48.32           C  
ANISOU   66  CG1 ILE A  28     6343   5988   6028    896   -187    557       C  
ATOM     67  CG2 ILE A  28      16.262  34.575  -7.293  1.00 48.33           C  
ANISOU   67  CG2 ILE A  28     6389   5903   6071    611   -181    421       C  
ATOM     68  CD1 ILE A  28      14.187  34.987  -9.780  1.00 54.23           C  
ANISOU   68  CD1 ILE A  28     7041   6852   6712    880   -212    670       C  
ATOM     69  N   ALA A  29      17.095  37.772  -5.660  1.00 41.84           N  
ANISOU   69  N   ALA A  29     5913   4542   5443    620    -92    357       N  
ATOM     70  CA  ALA A  29      18.291  38.110  -4.880  1.00 40.98           C  
ANISOU   70  CA  ALA A  29     5880   4310   5380    467    -80    273       C  
ATOM     71  C   ALA A  29      17.976  38.479  -3.424  1.00 44.33           C  
ANISOU   71  C   ALA A  29     6359   4651   5833    498    -63    132       C  
ATOM     72  O   ALA A  29      18.730  38.091  -2.530  1.00 43.67           O  
ANISOU   72  O   ALA A  29     6264   4584   5743    375    -73     28       O  
ATOM     73  CB  ALA A  29      19.054  39.238  -5.551  1.00 41.64           C  
ANISOU   73  CB  ALA A  29     6086   4212   5523    405    -54    362       C  
ATOM     74  N   THR A  30      16.853  39.202  -3.191  1.00 39.95           N  
ANISOU   74  N   THR A  30     5856   4023   5301    669    -38    130       N  
ATOM     75  CA  THR A  30      16.401  39.630  -1.865  1.00 39.06           C  
ANISOU   75  CA  THR A  30     5797   3837   5206    729    -14     -5       C  
ATOM     76  C   THR A  30      15.932  38.440  -1.021  1.00 42.18           C  
ANISOU   76  C   THR A  30     6058   4439   5529    734    -35    -93       C  
ATOM     77  O   THR A  30      16.456  38.245   0.076  1.00 42.14           O  
ANISOU   77  O   THR A  30     6062   4436   5514    644    -37   -214       O  
ATOM     78  CB  THR A  30      15.354  40.757  -1.982  1.00 45.38           C  
ANISOU   78  CB  THR A  30     6692   4498   6052    928     25     31       C  
ATOM     79  OG1 THR A  30      15.903  41.817  -2.767  1.00 44.35           O  
ANISOU   79  OG1 THR A  30     6693   4165   5991    905     46    129       O  
ATOM     80  CG2 THR A  30      14.926  41.310  -0.626  1.00 43.85           C  
ANISOU   80  CG2 THR A  30     6573   4210   5878    997     59   -121       C  
ATOM     81  N   VAL A  31      14.962  37.650  -1.534  1.00 38.00           N  
ANISOU   81  N   VAL A  31     5404   4088   4947    831    -53    -30       N  
ATOM     82  CA  VAL A  31      14.383  36.477  -0.857  1.00 37.49           C  
ANISOU   82  CA  VAL A  31     5207   4223   4815    838    -70    -91       C  
ATOM     83  C   VAL A  31      15.449  35.400  -0.572  1.00 41.28           C  
ANISOU   83  C   VAL A  31     5629   4790   5266    660   -101   -130       C  
ATOM     84  O   VAL A  31      15.530  34.917   0.559  1.00 41.13           O  
ANISOU   84  O   VAL A  31     5581   4827   5218    618   -101   -227       O  
ATOM     85  CB  VAL A  31      13.138  35.911  -1.603  1.00 41.12           C  
ANISOU   85  CB  VAL A  31     5546   4849   5227    961    -84     -7       C  
ATOM     86  CG1 VAL A  31      12.532  34.720  -0.862  1.00 40.82           C  
ANISOU   86  CG1 VAL A  31     5376   5006   5126    946    -98    -66       C  
ATOM     87  CG2 VAL A  31      12.077  36.990  -1.801  1.00 41.03           C  
ANISOU   87  CG2 VAL A  31     5581   4768   5241   1158    -53     32       C  
ATOM     88  N   ALA A  32      16.275  35.054  -1.580  1.00 37.36           N  
ANISOU   88  N   ALA A  32     5118   4307   4772    565   -124    -52       N  
ATOM     89  CA  ALA A  32      17.340  34.053  -1.448  1.00 36.84           C  
ANISOU   89  CA  ALA A  32     4996   4321   4680    414   -150    -77       C  
ATOM     90  C   ALA A  32      18.478  34.535  -0.547  1.00 40.50           C  
ANISOU   90  C   ALA A  32     5535   4682   5172    297   -144   -160       C  
ATOM     91  O   ALA A  32      19.063  33.727   0.178  1.00 40.08           O  
ANISOU   91  O   ALA A  32     5428   4714   5087    209   -161   -218       O  
ATOM     92  CB  ALA A  32      17.873  33.662  -2.814  1.00 37.47           C  
ANISOU   92  CB  ALA A  32     5042   4445   4751    363   -168     25       C  
ATOM     93  N   GLY A  33      18.764  35.838  -0.595  1.00 36.93           N  
ANISOU   93  N   GLY A  33     5205   4049   4776    298   -119   -163       N  
ATOM     94  CA  GLY A  33      19.788  36.485   0.220  1.00 36.34           C  
ANISOU   94  CA  GLY A  33     5214   3861   4731    178   -113   -250       C  
ATOM     95  C   GLY A  33      19.420  36.476   1.689  1.00 39.83           C  
ANISOU   95  C   GLY A  33     5663   4323   5147    203   -106   -385       C  
ATOM     96  O   GLY A  33      20.256  36.145   2.533  1.00 38.88           O  
ANISOU   96  O   GLY A  33     5524   4249   5001     88   -124   -465       O  
ATOM     97  N   LEU A  34      18.143  36.807   1.994  1.00 36.52           N  
ANISOU   97  N   LEU A  34     5259   3892   4724    362    -81   -407       N  
ATOM     98  CA  LEU A  34      17.586  36.797   3.349  1.00 36.22           C  
ANISOU   98  CA  LEU A  34     5217   3895   4648    415    -66   -531       C  
ATOM     99  C   LEU A  34      17.517  35.361   3.863  1.00 38.80           C  
ANISOU   99  C   LEU A  34     5404   4438   4899    379    -93   -541       C  
ATOM    100  O   LEU A  34      17.741  35.130   5.055  1.00 37.48           O  
ANISOU  100  O   LEU A  34     5225   4327   4687    336    -94   -640       O  
ATOM    101  CB  LEU A  34      16.189  37.439   3.383  1.00 36.50           C  
ANISOU  101  CB  LEU A  34     5285   3888   4696    611    -27   -532       C  
ATOM    102  CG  LEU A  34      16.132  38.971   3.352  1.00 41.81           C  
ANISOU  102  CG  LEU A  34     6122   4321   5441    674     12   -566       C  
ATOM    103  CD1 LEU A  34      14.797  39.454   2.819  1.00 41.99           C  
ANISOU  103  CD1 LEU A  34     6153   4318   5484    885     43   -497       C  
ATOM    104  CD2 LEU A  34      16.381  39.566   4.729  1.00 44.86           C  
ANISOU  104  CD2 LEU A  34     6592   4634   5817    644     33   -736       C  
ATOM    105  N   LEU A  35      17.237  34.395   2.951  1.00 34.74           N  
ANISOU  105  N   LEU A  35     4791   4041   4369    391   -113   -438       N  
ATOM    106  CA  LEU A  35      17.178  32.969   3.279  1.00 34.34           C  
ANISOU  106  CA  LEU A  35     4618   4170   4258    352   -137   -431       C  
ATOM    107  C   LEU A  35      18.561  32.465   3.677  1.00 37.21           C  
ANISOU  107  C   LEU A  35     4970   4559   4608    201   -164   -459       C  
ATOM    108  O   LEU A  35      18.676  31.759   4.676  1.00 36.51           O  
ANISOU  108  O   LEU A  35     4830   4574   4469    168   -173   -509       O  
ATOM    109  CB  LEU A  35      16.573  32.131   2.133  1.00 34.60           C  
ANISOU  109  CB  LEU A  35     4563   4299   4283    392   -153   -326       C  
ATOM    110  CG  LEU A  35      16.302  30.644   2.439  1.00 39.76           C  
ANISOU  110  CG  LEU A  35     5102   5121   4885    361   -171   -318       C  
ATOM    111  CD1 LEU A  35      15.114  30.462   3.401  1.00 39.88           C  
ANISOU  111  CD1 LEU A  35     5067   5227   4859    447   -150   -360       C  
ATOM    112  CD2 LEU A  35      16.105  29.843   1.158  1.00 42.35           C  
ANISOU  112  CD2 LEU A  35     5366   5515   5211    355   -193   -228       C  
ATOM    113  N   SER A  36      19.607  32.876   2.934  1.00 33.82           N  
ANISOU  113  N   SER A  36     4586   4045   4219    114   -175   -422       N  
ATOM    114  CA  SER A  36      20.998  32.522   3.214  1.00 33.82           C  
ANISOU  114  CA  SER A  36     4567   4074   4207    -27   -200   -442       C  
ATOM    115  C   SER A  36      21.427  33.103   4.566  1.00 38.91           C  
ANISOU  115  C   SER A  36     5263   4688   4833    -82   -198   -561       C  
ATOM    116  O   SER A  36      22.042  32.394   5.366  1.00 38.41           O  
ANISOU  116  O   SER A  36     5140   4734   4719   -151   -222   -598       O  
ATOM    117  CB  SER A  36      21.912  33.027   2.103  1.00 37.18           C  
ANISOU  117  CB  SER A  36     5031   4416   4679   -102   -202   -375       C  
ATOM    118  OG  SER A  36      23.278  32.777   2.396  1.00 45.74           O  
ANISOU  118  OG  SER A  36     6088   5541   5749   -238   -224   -396       O  
ATOM    119  N   LEU A  37      21.063  34.379   4.827  1.00 36.38           N  
ANISOU  119  N   LEU A  37     5052   4221   4548    -44   -171   -622       N  
ATOM    120  CA  LEU A  37      21.360  35.092   6.069  1.00 36.55           C  
ANISOU  120  CA  LEU A  37     5141   4195   4551    -90   -166   -756       C  
ATOM    121  C   LEU A  37      20.737  34.380   7.272  1.00 39.69           C  
ANISOU  121  C   LEU A  37     5473   4740   4868    -34   -165   -823       C  
ATOM    122  O   LEU A  37      21.417  34.222   8.277  1.00 39.79           O  
ANISOU  122  O   LEU A  37     5470   4821   4826   -119   -185   -904       O  
ATOM    123  CB  LEU A  37      20.895  36.560   5.991  1.00 37.01           C  
ANISOU  123  CB  LEU A  37     5344   4045   4672    -33   -128   -805       C  
ATOM    124  CG  LEU A  37      21.482  37.511   7.049  1.00 42.71           C  
ANISOU  124  CG  LEU A  37     6165   4669   5392   -122   -123   -953       C  
ATOM    125  CD1 LEU A  37      22.840  38.065   6.609  1.00 43.21           C  
ANISOU  125  CD1 LEU A  37     6285   4627   5507   -294   -141   -942       C  
ATOM    126  CD2 LEU A  37      20.522  38.653   7.355  1.00 44.95           C  
ANISOU  126  CD2 LEU A  37     6573   4796   5709      6    -76  -1033       C  
ATOM    127  N   ALA A  38      19.476  33.905   7.147  1.00 35.13           N  
ANISOU  127  N   ALA A  38     4845   4228   4274    100   -145   -782       N  
ATOM    128  CA  ALA A  38      18.755  33.173   8.197  1.00 34.23           C  
ANISOU  128  CA  ALA A  38     4658   4266   4081    156   -138   -823       C  
ATOM    129  C   ALA A  38      19.371  31.790   8.436  1.00 36.90           C  
ANISOU  129  C   ALA A  38     4888   4764   4367     75   -173   -774       C  
ATOM    130  O   ALA A  38      19.361  31.297   9.570  1.00 36.25           O  
ANISOU  130  O   ALA A  38     4763   4799   4210     61   -177   -824       O  
ATOM    131  CB  ALA A  38      17.286  33.035   7.826  1.00 34.77           C  
ANISOU  131  CB  ALA A  38     4690   4369   4152    306   -107   -776       C  
ATOM    132  N   THR A  39      19.917  31.178   7.366  1.00 32.33           N  
ANISOU  132  N   THR A  39     4269   4191   3825     27   -197   -675       N  
ATOM    133  CA  THR A  39      20.562  29.866   7.409  1.00 31.61           C  
ANISOU  133  CA  THR A  39     4087   4224   3699    -37   -227   -619       C  
ATOM    134  C   THR A  39      21.944  29.956   8.057  1.00 36.67           C  
ANISOU  134  C   THR A  39     4731   4891   4312   -153   -256   -667       C  
ATOM    135  O   THR A  39      22.280  29.094   8.868  1.00 36.43           O  
ANISOU  135  O   THR A  39     4635   4986   4219   -180   -274   -668       O  
ATOM    136  CB  THR A  39      20.604  29.230   6.009  1.00 31.04           C  
ANISOU  136  CB  THR A  39     3977   4145   3671    -33   -236   -512       C  
ATOM    137  OG1 THR A  39      19.297  29.273   5.449  1.00 27.69           O  
ANISOU  137  OG1 THR A  39     3546   3711   3264     69   -214   -477       O  
ATOM    138  CG2 THR A  39      21.078  27.788   6.036  1.00 26.52           C  
ANISOU  138  CG2 THR A  39     3319   3690   3069    -73   -259   -457       C  
ATOM    139  N   VAL A  40      22.748  30.977   7.693  1.00 34.14           N  
ANISOU  139  N   VAL A  40     4479   4458   4036   -226   -261   -698       N  
ATOM    140  CA  VAL A  40      24.088  31.138   8.257  1.00 34.48           C  
ANISOU  140  CA  VAL A  40     4514   4537   4050   -353   -292   -747       C  
ATOM    141  C   VAL A  40      24.001  31.562   9.730  1.00 38.60           C  
ANISOU  141  C   VAL A  40     5061   5102   4503   -367   -294   -870       C  
ATOM    142  O   VAL A  40      24.742  31.018  10.546  1.00 38.64           O  
ANISOU  142  O   VAL A  40     5005   5238   4439   -432   -326   -891       O  
ATOM    143  CB  VAL A  40      25.062  32.019   7.419  1.00 38.76           C  
ANISOU  143  CB  VAL A  40     5109   4963   4655   -453   -298   -737       C  
ATOM    144  CG1 VAL A  40      25.247  31.456   6.013  1.00 38.25           C  
ANISOU  144  CG1 VAL A  40     5001   4900   4635   -442   -298   -614       C  
ATOM    145  CG2 VAL A  40      24.627  33.479   7.365  1.00 38.95           C  
ANISOU  145  CG2 VAL A  40     5263   4803   4733   -442   -268   -803       C  
ATOM    146  N   THR A  41      23.051  32.465  10.073  1.00 34.86           N  
ANISOU  146  N   THR A  41     4671   4534   4039   -294   -259   -948       N  
ATOM    147  CA  THR A  41      22.817  32.955  11.437  1.00 34.26           C  
ANISOU  147  CA  THR A  41     4632   4494   3893   -291   -252  -1081       C  
ATOM    148  C   THR A  41      22.392  31.819  12.380  1.00 37.25           C  
ANISOU  148  C   THR A  41     4912   5069   4173   -243   -257  -1064       C  
ATOM    149  O   THR A  41      22.993  31.667  13.445  1.00 37.10           O  
ANISOU  149  O   THR A  41     4864   5165   4068   -306   -282  -1128       O  
ATOM    150  CB  THR A  41      21.829  34.139  11.430  1.00 41.58           C  
ANISOU  150  CB  THR A  41     5675   5262   4862   -200   -205  -1160       C  
ATOM    151  OG1 THR A  41      22.376  35.183  10.628  1.00 41.25           O  
ANISOU  151  OG1 THR A  41     5731   5031   4912   -262   -202  -1164       O  
ATOM    152  CG2 THR A  41      21.522  34.678  12.831  1.00 39.63           C  
ANISOU  152  CG2 THR A  41     5474   5048   4537   -186   -190  -1317       C  
ATOM    153  N   GLY A  42      21.375  31.050  11.977  1.00 31.98           N  
ANISOU  153  N   GLY A  42     4193   4442   3515   -139   -234   -975       N  
ATOM    154  CA  GLY A  42      20.848  29.941  12.764  1.00 31.27           C  
ANISOU  154  CA  GLY A  42     4015   4524   3344    -95   -230   -938       C  
ATOM    155  C   GLY A  42      21.856  28.846  13.059  1.00 34.19           C  
ANISOU  155  C   GLY A  42     4301   5023   3666   -173   -273   -874       C  
ATOM    156  O   GLY A  42      21.886  28.314  14.170  1.00 32.94           O  
ANISOU  156  O   GLY A  42     4096   5007   3414   -177   -280   -889       O  
ATOM    157  N   ASN A  43      22.687  28.500  12.069  1.00 30.60           N  
ANISOU  157  N   ASN A  43     3827   4526   3272   -226   -299   -797       N  
ATOM    158  CA  ASN A  43      23.684  27.447  12.231  1.00 30.42           C  
ANISOU  158  CA  ASN A  43     3725   4619   3214   -281   -336   -728       C  
ATOM    159  C   ASN A  43      24.919  27.925  13.017  1.00 35.41           C  
ANISOU  159  C   ASN A  43     4352   5314   3788   -382   -374   -803       C  
ATOM    160  O   ASN A  43      25.485  27.126  13.761  1.00 34.76           O  
ANISOU  160  O   ASN A  43     4198   5379   3630   -401   -402   -771       O  
ATOM    161  CB  ASN A  43      24.025  26.806  10.890  1.00 28.29           C  
ANISOU  161  CB  ASN A  43     3429   4300   3022   -284   -343   -623       C  
ATOM    162  CG  ASN A  43      22.897  25.914  10.428  1.00 39.11           C  
ANISOU  162  CG  ASN A  43     4772   5672   4415   -200   -317   -544       C  
ATOM    163  OD1 ASN A  43      22.715  24.805  10.932  1.00 29.74           O  
ANISOU  163  OD1 ASN A  43     3531   4584   3187   -179   -318   -488       O  
ATOM    164  ND2 ASN A  43      22.087  26.383   9.490  1.00 27.20           N  
ANISOU  164  ND2 ASN A  43     3303   4060   2972   -156   -294   -535       N  
ATOM    165  N   ILE A  44      25.278  29.230  12.928  1.00 32.84           N  
ANISOU  165  N   ILE A  44     4104   4882   3493   -446   -376   -903       N  
ATOM    166  CA  ILE A  44      26.367  29.826  13.719  1.00 32.95           C  
ANISOU  166  CA  ILE A  44     4119   4954   3448   -560   -413   -997       C  
ATOM    167  C   ILE A  44      25.891  29.928  15.184  1.00 37.55           C  
ANISOU  167  C   ILE A  44     4703   5648   3918   -536   -411  -1093       C  
ATOM    168  O   ILE A  44      26.649  29.582  16.092  1.00 36.81           O  
ANISOU  168  O   ILE A  44     4546   5713   3727   -594   -451  -1114       O  
ATOM    169  CB  ILE A  44      26.882  31.166  13.106  1.00 36.20           C  
ANISOU  169  CB  ILE A  44     4621   5199   3936   -652   -412  -1071       C  
ATOM    170  CG1 ILE A  44      27.767  30.883  11.868  1.00 37.08           C  
ANISOU  170  CG1 ILE A  44     4690   5280   4117   -710   -428   -968       C  
ATOM    171  CG2 ILE A  44      27.647  32.022  14.124  1.00 36.75           C  
ANISOU  171  CG2 ILE A  44     4723   5302   3940   -769   -441  -1217       C  
ATOM    172  CD1 ILE A  44      27.960  32.079  10.886  1.00 46.59           C  
ANISOU  172  CD1 ILE A  44     5990   6290   5422   -771   -409   -987       C  
ATOM    173  N   LEU A  45      24.606  30.310  15.397  1.00 35.18           N  
ANISOU  173  N   LEU A  45     4460   5286   3619   -439   -363  -1140       N  
ATOM    174  CA  LEU A  45      23.979  30.365  16.720  1.00 35.62           C  
ANISOU  174  CA  LEU A  45     4515   5456   3562   -395   -348  -1226       C  
ATOM    175  C   LEU A  45      23.990  28.984  17.381  1.00 40.58           C  
ANISOU  175  C   LEU A  45     5031   6288   4098   -367   -364  -1124       C  
ATOM    176  O   LEU A  45      24.224  28.894  18.582  1.00 40.50           O  
ANISOU  176  O   LEU A  45     4990   6432   3966   -391   -381  -1179       O  
ATOM    177  CB  LEU A  45      22.534  30.894  16.651  1.00 35.68           C  
ANISOU  177  CB  LEU A  45     4588   5371   3599   -275   -286  -1269       C  
ATOM    178  CG  LEU A  45      22.336  32.415  16.610  1.00 40.34           C  
ANISOU  178  CG  LEU A  45     5307   5787   4233   -276   -260  -1416       C  
ATOM    179  CD1 LEU A  45      20.946  32.755  16.122  1.00 40.69           C  
ANISOU  179  CD1 LEU A  45     5399   5720   4343   -136   -201  -1401       C  
ATOM    180  CD2 LEU A  45      22.556  33.052  17.970  1.00 42.25           C  
ANISOU  180  CD2 LEU A  45     5584   6108   4359   -310   -263  -1582       C  
ATOM    181  N   LEU A  46      23.766  27.916  16.596  1.00 37.77           N  
ANISOU  181  N   LEU A  46     4622   5931   3800   -321   -358   -974       N  
ATOM    182  CA  LEU A  46      23.784  26.538  17.083  1.00 38.06           C  
ANISOU  182  CA  LEU A  46     4566   6123   3773   -293   -368   -856       C  
ATOM    183  C   LEU A  46      25.207  26.130  17.527  1.00 41.79           C  
ANISOU  183  C   LEU A  46     4974   6718   4185   -371   -426   -829       C  
ATOM    184  O   LEU A  46      25.367  25.584  18.621  1.00 41.41           O  
ANISOU  184  O   LEU A  46     4870   6842   4024   -366   -443   -807       O  
ATOM    185  CB  LEU A  46      23.234  25.587  15.998  1.00 38.38           C  
ANISOU  185  CB  LEU A  46     4583   6093   3905   -236   -346   -721       C  
ATOM    186  CG  LEU A  46      22.774  24.186  16.438  1.00 43.95           C  
ANISOU  186  CG  LEU A  46     5219   6914   4565   -189   -336   -599       C  
ATOM    187  CD1 LEU A  46      21.542  24.249  17.329  1.00 44.37           C  
ANISOU  187  CD1 LEU A  46     5270   7043   4546   -132   -292   -629       C  
ATOM    188  CD2 LEU A  46      22.425  23.340  15.237  1.00 47.81           C  
ANISOU  188  CD2 LEU A  46     5697   7312   5156   -161   -323   -488       C  
ATOM    189  N   MET A  47      26.230  26.439  16.698  1.00 38.06           N  
ANISOU  189  N   MET A  47     4505   6173   3782   -441   -457   -827       N  
ATOM    190  CA  MET A  47      27.647  26.143  16.952  1.00 37.67           C  
ANISOU  190  CA  MET A  47     4383   6244   3686   -516   -513   -801       C  
ATOM    191  C   MET A  47      28.206  26.907  18.153  1.00 41.63           C  
ANISOU  191  C   MET A  47     4881   6867   4071   -596   -548   -930       C  
ATOM    192  O   MET A  47      28.943  26.325  18.950  1.00 40.89           O  
ANISOU  192  O   MET A  47     4702   6960   3874   -615   -590   -894       O  
ATOM    193  CB  MET A  47      28.502  26.438  15.710  1.00 39.75           C  
ANISOU  193  CB  MET A  47     4651   6401   4053   -575   -527   -778       C  
ATOM    194  CG  MET A  47      28.390  25.393  14.638  1.00 43.30           C  
ANISOU  194  CG  MET A  47     5068   6801   4583   -508   -511   -638       C  
ATOM    195  SD  MET A  47      29.302  25.897  13.168  1.00 47.46           S  
ANISOU  195  SD  MET A  47     5602   7214   5216   -575   -518   -622       S  
ATOM    196  CE  MET A  47      28.001  26.091  12.058  1.00 44.07           C  
ANISOU  196  CE  MET A  47     5263   6589   4892   -509   -464   -612       C  
ATOM    197  N   LEU A  48      27.876  28.208  18.266  1.00 38.82           N  
ANISOU  197  N   LEU A  48     4618   6403   3728   -641   -532  -1081       N  
ATOM    198  CA  LEU A  48      28.345  29.054  19.358  1.00 39.29           C  
ANISOU  198  CA  LEU A  48     4693   6552   3682   -729   -562  -1235       C  
ATOM    199  C   LEU A  48      27.679  28.724  20.684  1.00 42.10           C  
ANISOU  199  C   LEU A  48     5026   7073   3896   -667   -552  -1267       C  
ATOM    200  O   LEU A  48      28.332  28.849  21.716  1.00 41.90           O  
ANISOU  200  O   LEU A  48     4959   7220   3743   -733   -596  -1338       O  
ATOM    201  CB  LEU A  48      28.227  30.551  19.027  1.00 39.97           C  
ANISOU  201  CB  LEU A  48     4905   6445   3837   -795   -543  -1390       C  
ATOM    202  CG  LEU A  48      29.107  31.095  17.880  1.00 45.44           C  
ANISOU  202  CG  LEU A  48     5621   7002   4643   -901   -561  -1382       C  
ATOM    203  CD1 LEU A  48      28.818  32.562  17.639  1.00 46.05           C  
ANISOU  203  CD1 LEU A  48     5842   6864   4793   -950   -531  -1523       C  
ATOM    204  CD2 LEU A  48      30.605  30.918  18.164  1.00 47.94           C  
ANISOU  204  CD2 LEU A  48     5841   7482   4891  -1036   -630  -1388       C  
ATOM    205  N   SER A  49      26.402  28.270  20.657  1.00 37.81           N  
ANISOU  205  N   SER A  49     4500   6497   3367   -547   -496  -1210       N  
ATOM    206  CA  SER A  49      25.640  27.863  21.846  1.00 37.16           C  
ANISOU  206  CA  SER A  49     4389   6576   3153   -479   -474  -1217       C  
ATOM    207  C   SER A  49      26.299  26.672  22.535  1.00 40.00           C  
ANISOU  207  C   SER A  49     4635   7158   3404   -480   -516  -1092       C  
ATOM    208  O   SER A  49      26.375  26.641  23.765  1.00 39.14           O  
ANISOU  208  O   SER A  49     4491   7239   3142   -487   -531  -1139       O  
ATOM    209  CB  SER A  49      24.199  27.515  21.482  1.00 40.07           C  
ANISOU  209  CB  SER A  49     4782   6866   3577   -361   -405  -1154       C  
ATOM    210  OG  SER A  49      23.448  28.680  21.188  1.00 47.76           O  
ANISOU  210  OG  SER A  49     5857   7681   4609   -333   -362  -1284       O  
ATOM    211  N   ILE A  50      26.790  25.704  21.733  1.00 36.46           N  
ANISOU  211  N   ILE A  50     4132   6688   3034   -467   -534   -933       N  
ATOM    212  CA  ILE A  50      27.495  24.514  22.216  1.00 36.43           C  
ANISOU  212  CA  ILE A  50     4025   6864   2952   -451   -572   -791       C  
ATOM    213  C   ILE A  50      28.868  24.940  22.787  1.00 41.22           C  
ANISOU  213  C   ILE A  50     4577   7620   3467   -550   -645   -861       C  
ATOM    214  O   ILE A  50      29.256  24.475  23.862  1.00 40.49           O  
ANISOU  214  O   ILE A  50     4410   7747   3229   -546   -679   -826       O  
ATOM    215  CB  ILE A  50      27.565  23.414  21.111  1.00 39.13           C  
ANISOU  215  CB  ILE A  50     4342   7110   3417   -396   -561   -618       C  
ATOM    216  CG1 ILE A  50      26.141  22.905  20.754  1.00 39.03           C  
ANISOU  216  CG1 ILE A  50     4371   6988   3471   -312   -494   -555       C  
ATOM    217  CG2 ILE A  50      28.479  22.245  21.522  1.00 39.90           C  
ANISOU  217  CG2 ILE A  50     4340   7372   3447   -369   -602   -471       C  
ATOM    218  CD1 ILE A  50      25.971  22.309  19.323  1.00 41.15           C  
ANISOU  218  CD1 ILE A  50     4656   7086   3894   -280   -474   -454       C  
ATOM    219  N   LYS A  51      29.542  25.891  22.103  1.00 38.28           N  
ANISOU  219  N   LYS A  51     4240   7134   3170   -645   -666   -964       N  
ATOM    220  CA  LYS A  51      30.838  26.453  22.483  1.00 38.31           C  
ANISOU  220  CA  LYS A  51     4192   7258   3104   -768   -734  -1048       C  
ATOM    221  C   LYS A  51      30.825  27.230  23.818  1.00 43.89           C  
ANISOU  221  C   LYS A  51     4912   8111   3653   -831   -758  -1214       C  
ATOM    222  O   LYS A  51      31.709  27.001  24.644  1.00 43.75           O  
ANISOU  222  O   LYS A  51     4800   8322   3501   -880   -820  -1213       O  
ATOM    223  CB  LYS A  51      31.397  27.336  21.345  1.00 40.15           C  
ANISOU  223  CB  LYS A  51     4476   7307   3473   -864   -738  -1113       C  
ATOM    224  CG  LYS A  51      32.808  27.881  21.591  1.00 44.95           C  
ANISOU  224  CG  LYS A  51     5018   8037   4025  -1011   -808  -1187       C  
ATOM    225  CD  LYS A  51      33.076  29.167  20.825  1.00 50.10           C  
ANISOU  225  CD  LYS A  51     5760   8492   4786  -1134   -801  -1311       C  
ATOM    226  CE  LYS A  51      34.384  29.804  21.233  1.00 55.07           C  
ANISOU  226  CE  LYS A  51     6326   9252   5344  -1307   -869  -1410       C  
ATOM    227  NZ  LYS A  51      34.574  31.136  20.601  1.00 62.25           N  
ANISOU  227  NZ  LYS A  51     7340   9955   6359  -1443   -857  -1535       N  
ATOM    228  N   VAL A  52      29.854  28.150  24.021  1.00 41.72           N  
ANISOU  228  N   VAL A  52     4750   7713   3387   -825   -710  -1359       N  
ATOM    229  CA  VAL A  52      29.800  29.017  25.213  1.00 42.07           C  
ANISOU  229  CA  VAL A  52     4828   7869   3289   -885   -724  -1549       C  
ATOM    230  C   VAL A  52      29.107  28.380  26.450  1.00 48.08           C  
ANISOU  230  C   VAL A  52     5543   8842   3882   -792   -708  -1515       C  
ATOM    231  O   VAL A  52      29.465  28.742  27.569  1.00 48.82           O  
ANISOU  231  O   VAL A  52     5607   9132   3810   -850   -747  -1624       O  
ATOM    232  CB  VAL A  52      29.216  30.434  24.919  1.00 45.44           C  
ANISOU  232  CB  VAL A  52     5405   8066   3794   -923   -681  -1745       C  
ATOM    233  CG1 VAL A  52      29.992  31.139  23.810  1.00 45.10           C  
ANISOU  233  CG1 VAL A  52     5407   7837   3892  -1040   -702  -1783       C  
ATOM    234  CG2 VAL A  52      27.723  30.397  24.601  1.00 45.05           C  
ANISOU  234  CG2 VAL A  52     5434   7863   3822   -781   -595  -1716       C  
ATOM    235  N   ASN A  53      28.119  27.480  26.259  1.00 45.62           N  
ANISOU  235  N   ASN A  53     5226   8499   3608   -661   -651  -1370       N  
ATOM    236  CA  ASN A  53      27.362  26.845  27.349  1.00 45.67           C  
ANISOU  236  CA  ASN A  53     5190   8694   3467   -575   -623  -1316       C  
ATOM    237  C   ASN A  53      27.802  25.392  27.591  1.00 50.93           C  
ANISOU  237  C   ASN A  53     5741   9534   4078   -528   -654  -1092       C  
ATOM    238  O   ASN A  53      27.574  24.523  26.746  1.00 50.77           O  
ANISOU  238  O   ASN A  53     5707   9402   4181   -469   -633   -928       O  
ATOM    239  CB  ASN A  53      25.845  26.949  27.066  1.00 45.33           C  
ANISOU  239  CB  ASN A  53     5219   8511   3493   -471   -533  -1315       C  
ATOM    240  CG  ASN A  53      24.892  26.430  28.125  1.00 64.16           C  
ANISOU  240  CG  ASN A  53     7572  11077   5728   -391   -489  -1289       C  
ATOM    241  OD1 ASN A  53      25.266  25.804  29.123  1.00 59.14           O  
ANISOU  241  OD1 ASN A  53     6856  10685   4928   -394   -520  -1231       O  
ATOM    242  ND2 ASN A  53      23.612  26.682  27.913  1.00 54.45           N  
ANISOU  242  ND2 ASN A  53     6398   9742   4546   -311   -412  -1324       N  
ATOM    243  N   ARG A  54      28.402  25.137  28.770  1.00 48.98           N  
ANISOU  243  N   ARG A  54     5413   9558   3639   -549   -702  -1089       N  
ATOM    244  CA  ARG A  54      28.904  23.825  29.204  1.00 49.43           C  
ANISOU  244  CA  ARG A  54     5359   9808   3614   -497   -736   -878       C  
ATOM    245  C   ARG A  54      27.822  22.738  29.282  1.00 53.19           C  
ANISOU  245  C   ARG A  54     5833  10275   4102   -380   -669   -699       C  
ATOM    246  O   ARG A  54      28.111  21.581  28.972  1.00 52.68           O  
ANISOU  246  O   ARG A  54     5717  10222   4079   -324   -677   -494       O  
ATOM    247  CB  ARG A  54      29.654  23.930  30.543  1.00 51.31           C  
ANISOU  247  CB  ARG A  54     5514  10358   3623   -545   -802   -930       C  
ATOM    248  CG  ARG A  54      31.023  24.601  30.433  1.00 67.05           C  
ANISOU  248  CG  ARG A  54     7466  12410   5601   -670   -887  -1042       C  
ATOM    249  CD  ARG A  54      31.074  25.934  31.169  1.00 82.62           C  
ANISOU  249  CD  ARG A  54     9486  14448   7458   -780   -908  -1309       C  
ATOM    250  NE  ARG A  54      30.279  26.970  30.500  1.00 92.02           N  
ANISOU  250  NE  ARG A  54    10818  15358   8788   -802   -846  -1472       N  
ATOM    251  CZ  ARG A  54      29.928  28.127  31.056  1.00105.47           C  
ANISOU  251  CZ  ARG A  54    12606  17047  10423   -862   -832  -1708       C  
ATOM    252  NH1 ARG A  54      30.295  28.414  32.300  1.00 91.78           N  
ANISOU  252  NH1 ARG A  54    10826  15571   8474   -917   -877  -1824       N  
ATOM    253  NH2 ARG A  54      29.201  29.002  30.374  1.00 90.92           N  
ANISOU  253  NH2 ARG A  54    10893  14931   8722   -859   -772  -1831       N  
ATOM    254  N   GLN A  55      26.583  23.109  29.681  1.00 49.54           N  
ANISOU  254  N   GLN A  55     5428   9790   3605   -343   -600   -775       N  
ATOM    255  CA  GLN A  55      25.442  22.187  29.788  1.00 49.49           C  
ANISOU  255  CA  GLN A  55     5417   9782   3605   -251   -529   -622       C  
ATOM    256  C   GLN A  55      25.044  21.586  28.426  1.00 52.97           C  
ANISOU  256  C   GLN A  55     5892   9972   4261   -214   -494   -500       C  
ATOM    257  O   GLN A  55      24.436  20.513  28.390  1.00 53.07           O  
ANISOU  257  O   GLN A  55     5884   9984   4297   -156   -455   -323       O  
ATOM    258  CB  GLN A  55      24.234  22.874  30.452  1.00 51.09           C  
ANISOU  258  CB  GLN A  55     5664  10026   3723   -224   -462   -756       C  
ATOM    259  CG  GLN A  55      24.380  23.109  31.958  1.00 70.03           C  
ANISOU  259  CG  GLN A  55     8016  12717   5874   -235   -480   -829       C  
ATOM    260  CD  GLN A  55      24.120  21.860  32.768  1.00 92.69           C  
ANISOU  260  CD  GLN A  55    10806  15792   8621   -176   -462   -612       C  
ATOM    261  OE1 GLN A  55      25.043  21.127  33.141  1.00 88.87           O  
ANISOU  261  OE1 GLN A  55    10251  15452   8064   -181   -521   -474       O  
ATOM    262  NE2 GLN A  55      22.853  21.593  33.059  1.00 84.84           N  
ANISOU  262  NE2 GLN A  55     9819  14817   7599   -118   -379   -569       N  
ATOM    263  N   LEU A  56      25.393  22.273  27.318  1.00 48.17           N  
ANISOU  263  N   LEU A  56     5339   9158   3806   -256   -508   -594       N  
ATOM    264  CA  LEU A  56      25.116  21.824  25.955  1.00 47.42           C  
ANISOU  264  CA  LEU A  56     5277   8832   3907   -230   -482   -503       C  
ATOM    265  C   LEU A  56      26.279  21.008  25.361  1.00 50.60           C  
ANISOU  265  C   LEU A  56     5631   9219   4375   -237   -534   -370       C  
ATOM    266  O   LEU A  56      26.185  20.568  24.218  1.00 50.33           O  
ANISOU  266  O   LEU A  56     5621   9006   4494   -217   -517   -297       O  
ATOM    267  CB  LEU A  56      24.774  23.018  25.040  1.00 47.33           C  
ANISOU  267  CB  LEU A  56     5353   8611   4021   -259   -461   -665       C  
ATOM    268  CG  LEU A  56      23.477  23.789  25.315  1.00 51.78           C  
ANISOU  268  CG  LEU A  56     5973   9137   4564   -221   -396   -783       C  
ATOM    269  CD1 LEU A  56      23.396  25.024  24.435  1.00 52.01           C  
ANISOU  269  CD1 LEU A  56     6091   8962   4706   -249   -388   -942       C  
ATOM    270  CD2 LEU A  56      22.246  22.919  25.099  1.00 53.48           C  
ANISOU  270  CD2 LEU A  56     6176   9317   4827   -146   -331   -651       C  
ATOM    271  N   GLN A  57      27.358  20.788  26.139  1.00 46.74           N  
ANISOU  271  N   GLN A  57     5068   8929   3761   -258   -596   -339       N  
ATOM    272  CA  GLN A  57      28.538  20.036  25.697  1.00 46.16           C  
ANISOU  272  CA  GLN A  57     4933   8878   3729   -249   -647   -213       C  
ATOM    273  C   GLN A  57      28.423  18.526  25.982  1.00 49.21           C  
ANISOU  273  C   GLN A  57     5278   9322   4097   -156   -631     16       C  
ATOM    274  O   GLN A  57      29.300  17.922  26.607  1.00 48.99           O  
ANISOU  274  O   GLN A  57     5172   9470   3970   -128   -677    122       O  
ATOM    275  CB  GLN A  57      29.825  20.645  26.274  1.00 47.28           C  
ANISOU  275  CB  GLN A  57     5006   9204   3754   -321   -726   -300       C  
ATOM    276  CG  GLN A  57      30.348  21.805  25.443  1.00 55.21           C  
ANISOU  276  CG  GLN A  57     6046  10078   4853   -418   -749   -463       C  
ATOM    277  CD  GLN A  57      31.227  22.751  26.221  1.00 64.81           C  
ANISOU  277  CD  GLN A  57     7217  11470   5936   -524   -816   -613       C  
ATOM    278  OE1 GLN A  57      32.096  22.345  27.001  1.00 59.12           O  
ANISOU  278  OE1 GLN A  57     6395  10982   5087   -529   -876   -552       O  
ATOM    279  NE2 GLN A  57      31.030  24.042  26.006  1.00 52.15           N  
ANISOU  279  NE2 GLN A  57     5693   9758   4363   -614   -807   -813       N  
ATOM    280  N   THR A  58      27.330  17.928  25.489  1.00 44.78           N  
ANISOU  280  N   THR A  58     4771   8607   3636   -111   -565     95       N  
ATOM    281  CA  THR A  58      27.017  16.502  25.606  1.00 43.79           C  
ANISOU  281  CA  THR A  58     4634   8478   3526    -37   -535    308       C  
ATOM    282  C   THR A  58      27.392  15.794  24.298  1.00 45.87           C  
ANISOU  282  C   THR A  58     4920   8543   3964     -6   -533    397       C  
ATOM    283  O   THR A  58      27.387  16.429  23.243  1.00 45.26           O  
ANISOU  283  O   THR A  58     4883   8308   4006    -41   -530    292       O  
ATOM    284  CB  THR A  58      25.527  16.313  25.900  1.00 47.47           C  
ANISOU  284  CB  THR A  58     5141   8912   3984    -27   -462    330       C  
ATOM    285  OG1 THR A  58      24.779  17.047  24.932  1.00 48.41           O  
ANISOU  285  OG1 THR A  58     5322   8840   4230    -55   -426    208       O  
ATOM    286  CG2 THR A  58      25.143  16.752  27.301  1.00 44.61           C  
ANISOU  286  CG2 THR A  58     4746   8776   3428    -37   -456    276       C  
ATOM    287  N   VAL A  59      27.675  14.473  24.375  1.00 40.96           N  
ANISOU  287  N   VAL A  59     4280   7927   3355     66   -529    591       N  
ATOM    288  CA  VAL A  59      28.055  13.593  23.261  1.00 40.11           C  
ANISOU  288  CA  VAL A  59     4198   7645   3399    115   -522    692       C  
ATOM    289  C   VAL A  59      27.097  13.712  22.052  1.00 42.44           C  
ANISOU  289  C   VAL A  59     4572   7700   3853     86   -471    632       C  
ATOM    290  O   VAL A  59      27.578  13.799  20.920  1.00 42.11           O  
ANISOU  290  O   VAL A  59     4547   7525   3926     87   -480    595       O  
ATOM    291  CB  VAL A  59      28.233  12.118  23.736  1.00 43.90           C  
ANISOU  291  CB  VAL A  59     4666   8158   3856    203   -512    916       C  
ATOM    292  CG1 VAL A  59      28.549  11.174  22.573  1.00 43.69           C  
ANISOU  292  CG1 VAL A  59     4680   7929   3990    262   -496   1005       C  
ATOM    293  CG2 VAL A  59      29.315  12.015  24.804  1.00 43.72           C  
ANISOU  293  CG2 VAL A  59     4553   8385   3674    244   -571    982       C  
ATOM    294  N   ASN A  60      25.764  13.741  22.286  1.00 37.47           N  
ANISOU  294  N   ASN A  60     3980   7037   3219     61   -418    622       N  
ATOM    295  CA  ASN A  60      24.780  13.840  21.199  1.00 36.60           C  
ANISOU  295  CA  ASN A  60     3930   6730   3244     34   -373    570       C  
ATOM    296  C   ASN A  60      24.789  15.211  20.518  1.00 38.24           C  
ANISOU  296  C   ASN A  60     4155   6879   3494    -12   -387    384       C  
ATOM    297  O   ASN A  60      24.468  15.286  19.330  1.00 37.97           O  
ANISOU  297  O   ASN A  60     4162   6677   3586    -22   -370    349       O  
ATOM    298  CB  ASN A  60      23.365  13.431  21.633  1.00 37.56           C  
ANISOU  298  CB  ASN A  60     4070   6855   3346     19   -314    623       C  
ATOM    299  CG  ASN A  60      22.465  13.073  20.456  1.00 60.35           C  
ANISOU  299  CG  ASN A  60     7007   9545   6379     -1   -272    624       C  
ATOM    300  OD1 ASN A  60      21.866  13.939  19.807  1.00 51.56           O  
ANISOU  300  OD1 ASN A  60     5911   8366   5314    -30   -260    499       O  
ATOM    301  ND2 ASN A  60      22.347  11.790  20.146  1.00 51.18           N  
ANISOU  301  ND2 ASN A  60     5874   8284   5289     13   -251    764       N  
ATOM    302  N   ASN A  61      25.212  16.276  21.236  1.00 32.89           N  
ANISOU  302  N   ASN A  61     3450   6335   2711    -42   -418    269       N  
ATOM    303  CA  ASN A  61      25.307  17.624  20.664  1.00 31.74           C  
ANISOU  303  CA  ASN A  61     3332   6124   2604    -91   -431     95       C  
ATOM    304  C   ASN A  61      26.548  17.819  19.783  1.00 34.43           C  
ANISOU  304  C   ASN A  61     3662   6404   3017   -109   -475     73       C  
ATOM    305  O   ASN A  61      26.621  18.809  19.048  1.00 33.39           O  
ANISOU  305  O   ASN A  61     3563   6177   2948   -152   -479    -45       O  
ATOM    306  CB  ASN A  61      25.195  18.705  21.728  1.00 30.91           C  
ANISOU  306  CB  ASN A  61     3217   6159   2367   -125   -441    -35       C  
ATOM    307  CG  ASN A  61      23.780  18.950  22.195  1.00 40.82           C  
ANISOU  307  CG  ASN A  61     4498   7425   3585   -111   -384    -74       C  
ATOM    308  OD1 ASN A  61      22.800  18.627  21.517  1.00 30.13           O  
ANISOU  308  OD1 ASN A  61     3174   5950   2325    -92   -338    -38       O  
ATOM    309  ND2 ASN A  61      23.643  19.539  23.369  1.00 31.35           N  
ANISOU  309  ND2 ASN A  61     3282   6388   2242   -121   -385   -153       N  
ATOM    310  N   TYR A  62      27.502  16.859  19.828  1.00 30.99           N  
ANISOU  310  N   TYR A  62     3179   6022   2575    -68   -503    196       N  
ATOM    311  CA  TYR A  62      28.692  16.843  18.968  1.00 30.61           C  
ANISOU  311  CA  TYR A  62     3104   5934   2592    -70   -538    198       C  
ATOM    312  C   TYR A  62      28.195  16.590  17.540  1.00 31.89           C  
ANISOU  312  C   TYR A  62     3325   5883   2908    -57   -500    203       C  
ATOM    313  O   TYR A  62      28.654  17.244  16.605  1.00 30.96           O  
ANISOU  313  O   TYR A  62     3215   5689   2857    -92   -511    129       O  
ATOM    314  CB  TYR A  62      29.679  15.744  19.407  1.00 32.74           C  
ANISOU  314  CB  TYR A  62     3307   6319   2815     -1   -568    343       C  
ATOM    315  CG  TYR A  62      30.646  16.157  20.502  1.00 36.34           C  
ANISOU  315  CG  TYR A  62     3679   7006   3124    -23   -627    321       C  
ATOM    316  CD1 TYR A  62      30.202  16.399  21.799  1.00 38.56           C  
ANISOU  316  CD1 TYR A  62     3944   7442   3264    -37   -632    309       C  
ATOM    317  CD2 TYR A  62      32.014  16.237  20.257  1.00 37.96           C  
ANISOU  317  CD2 TYR A  62     3809   7295   3319    -28   -677    319       C  
ATOM    318  CE1 TYR A  62      31.087  16.764  22.814  1.00 39.54           C  
ANISOU  318  CE1 TYR A  62     3987   7797   3240    -62   -692    282       C  
ATOM    319  CE2 TYR A  62      32.912  16.589  21.267  1.00 39.47           C  
ANISOU  319  CE2 TYR A  62     3909   7721   3366    -57   -737    299       C  
ATOM    320  CZ  TYR A  62      32.442  16.857  22.544  1.00 47.10           C  
ANISOU  320  CZ  TYR A  62     4867   8836   4191    -76   -747    277       C  
ATOM    321  OH  TYR A  62      33.316  17.215  23.542  1.00 49.21           O  
ANISOU  321  OH  TYR A  62     5042   9351   4305   -111   -811    248       O  
ATOM    322  N   PHE A  63      27.195  15.690  17.398  1.00 27.71           N  
ANISOU  322  N   PHE A  63     2836   5266   2426    -18   -456    288       N  
ATOM    323  CA  PHE A  63      26.541  15.352  16.132  1.00 26.93           C  
ANISOU  323  CA  PHE A  63     2793   4981   2458    -12   -420    293       C  
ATOM    324  C   PHE A  63      25.684  16.530  15.641  1.00 30.06           C  
ANISOU  324  C   PHE A  63     3229   5304   2889    -63   -402    163       C  
ATOM    325  O   PHE A  63      25.587  16.743  14.432  1.00 29.30           O  
ANISOU  325  O   PHE A  63     3164   5082   2888    -71   -393    127       O  
ATOM    326  CB  PHE A  63      25.696  14.072  16.266  1.00 28.53           C  
ANISOU  326  CB  PHE A  63     3023   5128   2688     23   -380    414       C  
ATOM    327  CG  PHE A  63      26.394  12.869  16.862  1.00 30.37           C  
ANISOU  327  CG  PHE A  63     3233   5419   2889     86   -389    561       C  
ATOM    328  CD1 PHE A  63      27.476  12.278  16.216  1.00 33.80           C  
ANISOU  328  CD1 PHE A  63     3657   5807   3378    141   -407    612       C  
ATOM    329  CD2 PHE A  63      25.937  12.292  18.042  1.00 32.65           C  
ANISOU  329  CD2 PHE A  63     3510   5806   3091    100   -376    656       C  
ATOM    330  CE1 PHE A  63      28.122  11.163  16.769  1.00 34.77           C  
ANISOU  330  CE1 PHE A  63     3761   5976   3473    220   -413    755       C  
ATOM    331  CE2 PHE A  63      26.569  11.167  18.584  1.00 35.39           C  
ANISOU  331  CE2 PHE A  63     3841   6196   3408    168   -383    809       C  
ATOM    332  CZ  PHE A  63      27.660  10.612  17.946  1.00 33.57           C  
ANISOU  332  CZ  PHE A  63     3605   5912   3238    233   -402    858       C  
ATOM    333  N   ALA A  64      25.078  17.299  16.577  1.00 26.78           N  
ANISOU  333  N   ALA A  64     2812   4973   2389    -87   -395     94       N  
ATOM    334  CA  ALA A  64      24.277  18.487  16.258  1.00 26.57           C  
ANISOU  334  CA  ALA A  64     2825   4885   2384   -116   -376    -30       C  
ATOM    335  C   ALA A  64      25.197  19.562  15.670  1.00 30.60           C  
ANISOU  335  C   ALA A  64     3348   5355   2925   -159   -408   -130       C  
ATOM    336  O   ALA A  64      24.850  20.165  14.654  1.00 30.23           O  
ANISOU  336  O   ALA A  64     3343   5183   2960   -170   -393   -186       O  
ATOM    337  CB  ALA A  64      23.579  19.012  17.505  1.00 27.10           C  
ANISOU  337  CB  ALA A  64     2886   5069   2342   -119   -360    -83       C  
ATOM    338  N   PHE A  65      26.399  19.743  16.277  1.00 27.51           N  
ANISOU  338  N   PHE A  65     2912   5077   2465   -186   -452   -142       N  
ATOM    339  CA  PHE A  65      27.447  20.673  15.835  1.00 27.25           C  
ANISOU  339  CA  PHE A  65     2874   5031   2449   -248   -487   -225       C  
ATOM    340  C   PHE A  65      27.920  20.281  14.426  1.00 30.83           C  
ANISOU  340  C   PHE A  65     3329   5370   3013   -237   -483   -173       C  
ATOM    341  O   PHE A  65      28.079  21.161  13.581  1.00 30.85           O  
ANISOU  341  O   PHE A  65     3364   5281   3077   -281   -482   -242       O  
ATOM    342  CB  PHE A  65      28.637  20.660  16.819  1.00 28.94           C  
ANISOU  342  CB  PHE A  65     3016   5426   2555   -278   -538   -224       C  
ATOM    343  CG  PHE A  65      29.672  21.745  16.614  1.00 30.66           C  
ANISOU  343  CG  PHE A  65     3220   5660   2768   -369   -576   -327       C  
ATOM    344  CD1 PHE A  65      30.599  21.662  15.578  1.00 33.88           C  
ANISOU  344  CD1 PHE A  65     3599   6028   3248   -390   -591   -295       C  
ATOM    345  CD2 PHE A  65      29.772  22.809  17.502  1.00 33.28           C  
ANISOU  345  CD2 PHE A  65     3567   6062   3017   -441   -596   -456       C  
ATOM    346  CE1 PHE A  65      31.555  22.662  15.388  1.00 34.86           C  
ANISOU  346  CE1 PHE A  65     3704   6175   3367   -491   -624   -382       C  
ATOM    347  CE2 PHE A  65      30.749  23.796  17.331  1.00 36.18           C  
ANISOU  347  CE2 PHE A  65     3924   6439   3382   -547   -632   -553       C  
ATOM    348  CZ  PHE A  65      31.630  23.717  16.272  1.00 34.28           C  
ANISOU  348  CZ  PHE A  65     3649   6156   3218   -576   -645   -510       C  
ATOM    349  N   SER A  66      28.132  18.965  14.182  1.00 26.62           N  
ANISOU  349  N   SER A  66     2767   4842   2505   -175   -478    -53       N  
ATOM    350  CA  SER A  66      28.563  18.424  12.891  1.00 26.69           C  
ANISOU  350  CA  SER A  66     2777   4754   2608   -149   -470     -4       C  
ATOM    351  C   SER A  66      27.509  18.669  11.808  1.00 30.61           C  
ANISOU  351  C   SER A  66     3341   5096   3195   -150   -433    -36       C  
ATOM    352  O   SER A  66      27.864  18.972  10.666  1.00 31.00           O  
ANISOU  352  O   SER A  66     3402   5068   3310   -164   -430    -56       O  
ATOM    353  CB  SER A  66      28.869  16.935  13.008  1.00 29.99           C  
ANISOU  353  CB  SER A  66     3167   5198   3029    -72   -467    123       C  
ATOM    354  OG  SER A  66      29.240  16.394  11.749  1.00 35.49           O  
ANISOU  354  OG  SER A  66     3871   5801   3812    -39   -454    155       O  
ATOM    355  N   LEU A  67      26.220  18.554  12.177  1.00 25.92           N  
ANISOU  355  N   LEU A  67     2780   4474   2593   -135   -405    -37       N  
ATOM    356  CA  LEU A  67      25.086  18.806  11.296  1.00 25.12           C  
ANISOU  356  CA  LEU A  67     2728   4257   2561   -132   -373    -65       C  
ATOM    357  C   LEU A  67      25.003  20.310  10.969  1.00 29.48           C  
ANISOU  357  C   LEU A  67     3313   4762   3125   -171   -375   -171       C  
ATOM    358  O   LEU A  67      24.740  20.669   9.818  1.00 29.18           O  
ANISOU  358  O   LEU A  67     3306   4625   3156   -172   -363   -187       O  
ATOM    359  CB  LEU A  67      23.785  18.280  11.945  1.00 24.64           C  
ANISOU  359  CB  LEU A  67     2674   4216   2473   -110   -343    -33       C  
ATOM    360  CG  LEU A  67      22.472  18.463  11.182  1.00 28.48           C  
ANISOU  360  CG  LEU A  67     3190   4617   3015   -103   -311    -54       C  
ATOM    361  CD1 LEU A  67      22.472  17.704   9.874  1.00 28.25           C  
ANISOU  361  CD1 LEU A  67     3173   4491   3069    -96   -306    -10       C  
ATOM    362  CD2 LEU A  67      21.297  18.022  12.021  1.00 30.44           C  
ANISOU  362  CD2 LEU A  67     3423   4923   3218    -93   -282    -23       C  
ATOM    363  N   ALA A  68      25.280  21.175  11.972  1.00 26.84           N  
ANISOU  363  N   ALA A  68     2977   4500   2722   -204   -391   -242       N  
ATOM    364  CA  ALA A  68      25.295  22.638  11.836  1.00 26.77           C  
ANISOU  364  CA  ALA A  68     3013   4435   2722   -247   -392   -349       C  
ATOM    365  C   ALA A  68      26.354  23.089  10.826  1.00 30.92           C  
ANISOU  365  C   ALA A  68     3541   4905   3304   -296   -411   -356       C  
ATOM    366  O   ALA A  68      26.116  24.052  10.101  1.00 30.41           O  
ANISOU  366  O   ALA A  68     3528   4735   3290   -317   -399   -406       O  
ATOM    367  CB  ALA A  68      25.552  23.290  13.185  1.00 27.27           C  
ANISOU  367  CB  ALA A  68     3072   4598   2690   -281   -409   -428       C  
ATOM    368  N   CYS A  69      27.510  22.376  10.780  1.00 27.87           N  
ANISOU  368  N   CYS A  69     3092   4593   2903   -307   -437   -298       N  
ATOM    369  CA  CYS A  69      28.646  22.603   9.874  1.00 27.82           C  
ANISOU  369  CA  CYS A  69     3062   4572   2936   -351   -452   -288       C  
ATOM    370  C   CYS A  69      28.246  22.344   8.428  1.00 29.77           C  
ANISOU  370  C   CYS A  69     3338   4707   3268   -317   -424   -247       C  
ATOM    371  O   CYS A  69      28.585  23.140   7.554  1.00 28.96           O  
ANISOU  371  O   CYS A  69     3257   4540   3208   -361   -420   -270       O  
ATOM    372  CB  CYS A  69      29.849  21.748  10.274  1.00 28.50           C  
ANISOU  372  CB  CYS A  69     3062   4791   2975   -346   -483   -228       C  
ATOM    373  SG  CYS A  69      30.722  22.329  11.750  1.00 32.64           S  
ANISOU  373  SG  CYS A  69     3533   5479   3388   -417   -530   -289       S  
ATOM    374  N   ALA A  70      27.537  21.218   8.181  1.00 25.70           N  
ANISOU  374  N   ALA A  70     2822   4171   2771   -246   -406   -184       N  
ATOM    375  CA  ALA A  70      27.037  20.813   6.864  1.00 25.24           C  
ANISOU  375  CA  ALA A  70     2788   4021   2780   -213   -382   -152       C  
ATOM    376  C   ALA A  70      25.984  21.806   6.377  1.00 28.92           C  
ANISOU  376  C   ALA A  70     3313   4397   3278   -219   -363   -200       C  
ATOM    377  O   ALA A  70      25.962  22.154   5.200  1.00 28.24           O  
ANISOU  377  O   ALA A  70     3248   4244   3237   -223   -353   -197       O  
ATOM    378  CB  ALA A  70      26.437  19.416   6.943  1.00 26.04           C  
ANISOU  378  CB  ALA A  70     2883   4123   2889   -154   -368    -89       C  
ATOM    379  N   ASP A  71      25.138  22.285   7.303  1.00 25.99           N  
ANISOU  379  N   ASP A  71     2966   4034   2877   -213   -357   -243       N  
ATOM    380  CA  ASP A  71      24.081  23.247   7.026  1.00 25.61           C  
ANISOU  380  CA  ASP A  71     2970   3910   2851   -197   -337   -289       C  
ATOM    381  C   ASP A  71      24.624  24.656   6.788  1.00 30.11           C  
ANISOU  381  C   ASP A  71     3584   4416   3440   -247   -342   -347       C  
ATOM    382  O   ASP A  71      24.053  25.382   5.971  1.00 29.90           O  
ANISOU  382  O   ASP A  71     3604   4298   3457   -228   -325   -355       O  
ATOM    383  CB  ASP A  71      23.009  23.191   8.122  1.00 27.12           C  
ANISOU  383  CB  ASP A  71     3162   4146   2996   -163   -322   -315       C  
ATOM    384  CG  ASP A  71      22.122  21.953   8.034  1.00 34.22           C  
ANISOU  384  CG  ASP A  71     4030   5075   3896   -122   -307   -251       C  
ATOM    385  OD1 ASP A  71      21.998  21.389   6.930  1.00 33.98           O  
ANISOU  385  OD1 ASP A  71     3995   5000   3914   -112   -304   -207       O  
ATOM    386  OD2 ASP A  71      21.523  21.577   9.060  1.00 39.84           O  
ANISOU  386  OD2 ASP A  71     4723   5858   4558   -107   -297   -247       O  
ATOM    387  N   LEU A  72      25.756  25.020   7.442  1.00 27.09           N  
ANISOU  387  N   LEU A  72     3186   4082   3024   -314   -366   -381       N  
ATOM    388  CA  LEU A  72      26.444  26.301   7.238  1.00 27.22           C  
ANISOU  388  CA  LEU A  72     3244   4037   3060   -389   -372   -436       C  
ATOM    389  C   LEU A  72      27.019  26.358   5.806  1.00 30.24           C  
ANISOU  389  C   LEU A  72     3625   4365   3500   -412   -366   -380       C  
ATOM    390  O   LEU A  72      26.907  27.393   5.157  1.00 29.35           O  
ANISOU  390  O   LEU A  72     3574   4148   3431   -436   -352   -396       O  
ATOM    391  CB  LEU A  72      27.544  26.519   8.300  1.00 27.85           C  
ANISOU  391  CB  LEU A  72     3289   4213   3080   -470   -405   -485       C  
ATOM    392  CG  LEU A  72      28.392  27.801   8.212  1.00 33.56           C  
ANISOU  392  CG  LEU A  72     4051   4881   3819   -579   -416   -552       C  
ATOM    393  CD1 LEU A  72      27.565  29.057   8.497  1.00 34.20           C  
ANISOU  393  CD1 LEU A  72     4236   4843   3917   -578   -395   -645       C  
ATOM    394  CD2 LEU A  72      29.570  27.737   9.159  1.00 36.68           C  
ANISOU  394  CD2 LEU A  72     4378   5412   4146   -665   -457   -584       C  
ATOM    395  N   ILE A  73      27.582  25.231   5.301  1.00 27.28           N  
ANISOU  395  N   ILE A  73     3184   4059   3123   -394   -373   -312       N  
ATOM    396  CA  ILE A  73      28.117  25.111   3.931  1.00 26.98           C  
ANISOU  396  CA  ILE A  73     3131   3996   3123   -403   -364   -258       C  
ATOM    397  C   ILE A  73      26.968  25.310   2.934  1.00 31.57           C  
ANISOU  397  C   ILE A  73     3765   4484   3746   -347   -338   -237       C  
ATOM    398  O   ILE A  73      27.123  26.050   1.960  1.00 31.75           O  
ANISOU  398  O   ILE A  73     3819   4444   3801   -372   -326   -219       O  
ATOM    399  CB  ILE A  73      28.879  23.768   3.698  1.00 29.99           C  
ANISOU  399  CB  ILE A  73     3435   4475   3487   -373   -371   -201       C  
ATOM    400  CG1 ILE A  73      30.163  23.682   4.563  1.00 30.53           C  
ANISOU  400  CG1 ILE A  73     3435   4656   3508   -425   -399   -210       C  
ATOM    401  CG2 ILE A  73      29.204  23.556   2.207  1.00 30.36           C  
ANISOU  401  CG2 ILE A  73     3470   4501   3565   -363   -353   -154       C  
ATOM    402  CD1 ILE A  73      30.748  22.258   4.729  1.00 36.03           C  
ANISOU  402  CD1 ILE A  73     4059   5453   4179   -361   -408   -154       C  
ATOM    403  N   ILE A  74      25.811  24.682   3.204  1.00 27.59           N  
ANISOU  403  N   ILE A  74     3266   3980   3236   -277   -331   -235       N  
ATOM    404  CA  ILE A  74      24.613  24.810   2.379  1.00 27.67           C  
ANISOU  404  CA  ILE A  74     3310   3931   3274   -220   -313   -217       C  
ATOM    405  C   ILE A  74      24.147  26.287   2.330  1.00 33.23           C  
ANISOU  405  C   ILE A  74     4083   4541   4001   -221   -301   -250       C  
ATOM    406  O   ILE A  74      23.905  26.816   1.244  1.00 33.19           O  
ANISOU  406  O   ILE A  74     4108   4477   4025   -205   -290   -216       O  
ATOM    407  CB  ILE A  74      23.516  23.812   2.861  1.00 30.47           C  
ANISOU  407  CB  ILE A  74     3641   4327   3611   -162   -310   -211       C  
ATOM    408  CG1 ILE A  74      23.905  22.358   2.504  1.00 30.89           C  
ANISOU  408  CG1 ILE A  74     3646   4429   3661   -154   -315   -167       C  
ATOM    409  CG2 ILE A  74      22.133  24.168   2.306  1.00 30.83           C  
ANISOU  409  CG2 ILE A  74     3709   4332   3673   -107   -295   -207       C  
ATOM    410  CD1 ILE A  74      23.251  21.246   3.388  1.00 41.24           C  
ANISOU  410  CD1 ILE A  74     4934   5785   4951   -128   -313   -154       C  
ATOM    411  N   GLY A  75      24.084  26.932   3.496  1.00 30.51           N  
ANISOU  411  N   GLY A  75     3767   4184   3639   -238   -303   -314       N  
ATOM    412  CA  GLY A  75      23.666  28.323   3.635  1.00 30.33           C  
ANISOU  412  CA  GLY A  75     3825   4056   3641   -233   -288   -361       C  
ATOM    413  C   GLY A  75      24.592  29.344   3.008  1.00 34.26           C  
ANISOU  413  C   GLY A  75     4373   4469   4177   -310   -286   -356       C  
ATOM    414  O   GLY A  75      24.136  30.209   2.257  1.00 34.00           O  
ANISOU  414  O   GLY A  75     4403   4331   4186   -282   -267   -333       O  
ATOM    415  N   ALA A  76      25.891  29.266   3.323  1.00 30.93           N  
ANISOU  415  N   ALA A  76     3918   4097   3739   -408   -306   -369       N  
ATOM    416  CA  ALA A  76      26.889  30.207   2.812  1.00 31.07           C  
ANISOU  416  CA  ALA A  76     3968   4049   3787   -510   -304   -363       C  
ATOM    417  C   ALA A  76      27.313  29.963   1.359  1.00 35.24           C  
ANISOU  417  C   ALA A  76     4468   4584   4338   -518   -294   -269       C  
ATOM    418  O   ALA A  76      27.432  30.928   0.607  1.00 35.14           O  
ANISOU  418  O   ALA A  76     4516   4472   4366   -554   -277   -239       O  
ATOM    419  CB  ALA A  76      28.109  30.241   3.727  1.00 31.57           C  
ANISOU  419  CB  ALA A  76     3990   4190   3814   -620   -332   -417       C  
ATOM    420  N   PHE A  77      27.551  28.696   0.965  1.00 31.76           N  
ANISOU  420  N   PHE A  77     3943   4256   3870   -484   -302   -224       N  
ATOM    421  CA  PHE A  77      28.017  28.360  -0.381  1.00 31.58           C  
ANISOU  421  CA  PHE A  77     3885   4261   3852   -487   -291   -147       C  
ATOM    422  C   PHE A  77      26.902  27.988  -1.360  1.00 34.25           C  
ANISOU  422  C   PHE A  77     4238   4578   4198   -389   -277   -101       C  
ATOM    423  O   PHE A  77      26.678  28.726  -2.319  1.00 33.97           O  
ANISOU  423  O   PHE A  77     4246   4477   4183   -385   -260    -54       O  
ATOM    424  CB  PHE A  77      29.093  27.257  -0.326  1.00 33.80           C  
ANISOU  424  CB  PHE A  77     4068   4677   4099   -509   -304   -132       C  
ATOM    425  CG  PHE A  77      29.708  26.874  -1.652  1.00 36.09           C  
ANISOU  425  CG  PHE A  77     4313   5017   4383   -510   -287    -66       C  
ATOM    426  CD1 PHE A  77      30.835  27.534  -2.130  1.00 39.86           C  
ANISOU  426  CD1 PHE A  77     4768   5515   4862   -604   -278    -38       C  
ATOM    427  CD2 PHE A  77      29.189  25.822  -2.402  1.00 39.00           C  
ANISOU  427  CD2 PHE A  77     4658   5420   4739   -423   -279    -38       C  
ATOM    428  CE1 PHE A  77      31.410  27.173  -3.355  1.00 41.20           C  
ANISOU  428  CE1 PHE A  77     4889   5750   5015   -600   -256     23       C  
ATOM    429  CE2 PHE A  77      29.761  25.463  -3.627  1.00 42.08           C  
ANISOU  429  CE2 PHE A  77     5009   5865   5113   -418   -260     10       C  
ATOM    430  CZ  PHE A  77      30.879  26.130  -4.087  1.00 40.35           C  
ANISOU  430  CZ  PHE A  77     4763   5679   4890   -501   -247     43       C  
ATOM    431  N   SER A  78      26.262  26.817  -1.161  1.00 29.92           N  
ANISOU  431  N   SER A  78     3648   4091   3627   -318   -285   -108       N  
ATOM    432  CA  SER A  78      25.233  26.257  -2.047  1.00 29.43           C  
ANISOU  432  CA  SER A  78     3582   4036   3562   -240   -279    -75       C  
ATOM    433  C   SER A  78      24.091  27.219  -2.368  1.00 32.57           C  
ANISOU  433  C   SER A  78     4041   4355   3981   -189   -269    -63       C  
ATOM    434  O   SER A  78      23.783  27.404  -3.543  1.00 32.22           O  
ANISOU  434  O   SER A  78     4003   4304   3934   -161   -261    -10       O  
ATOM    435  CB  SER A  78      24.695  24.940  -1.496  1.00 32.04           C  
ANISOU  435  CB  SER A  78     3871   4430   3873   -195   -289    -96       C  
ATOM    436  OG  SER A  78      25.735  23.986  -1.350  1.00 37.47           O  
ANISOU  436  OG  SER A  78     4507   5187   4545   -219   -295    -93       O  
ATOM    437  N   MET A  79      23.505  27.864  -1.342  1.00 27.70           N  
ANISOU  437  N   MET A  79     3466   3682   3376   -172   -267   -111       N  
ATOM    438  CA  MET A  79      22.410  28.816  -1.528  1.00 26.58           C  
ANISOU  438  CA  MET A  79     3382   3461   3255   -102   -254   -103       C  
ATOM    439  C   MET A  79      22.806  30.015  -2.387  1.00 31.06           C  
ANISOU  439  C   MET A  79     4016   3930   3856   -125   -238    -53       C  
ATOM    440  O   MET A  79      22.085  30.346  -3.329  1.00 31.07           O  
ANISOU  440  O   MET A  79     4033   3911   3860    -58   -231      7       O  
ATOM    441  CB  MET A  79      21.850  29.287  -0.181  1.00 28.08           C  
ANISOU  441  CB  MET A  79     3605   3615   3448    -76   -249   -177       C  
ATOM    442  CG  MET A  79      20.874  28.324   0.434  1.00 30.79           C  
ANISOU  442  CG  MET A  79     3892   4047   3759    -17   -253   -199       C  
ATOM    443  SD  MET A  79      20.158  29.044   1.917  1.00 33.91           S  
ANISOU  443  SD  MET A  79     4328   4410   4145     27   -238   -283       S  
ATOM    444  CE  MET A  79      19.082  27.768   2.405  1.00 30.66           C  
ANISOU  444  CE  MET A  79     3832   4127   3692     79   -239   -280       C  
ATOM    445  N   ASN A  80      23.961  30.636  -2.090  1.00 27.45           N  
ANISOU  445  N   ASN A  80     3591   3420   3418   -223   -235    -70       N  
ATOM    446  CA  ASN A  80      24.425  31.828  -2.798  1.00 27.34           C  
ANISOU  446  CA  ASN A  80     3650   3297   3442   -269   -216    -19       C  
ATOM    447  C   ASN A  80      24.918  31.552  -4.229  1.00 31.41           C  
ANISOU  447  C   ASN A  80     4128   3865   3940   -288   -210     77       C  
ATOM    448  O   ASN A  80      24.581  32.331  -5.124  1.00 30.81           O  
ANISOU  448  O   ASN A  80     4106   3719   3882   -258   -193    151       O  
ATOM    449  CB  ASN A  80      25.455  32.589  -1.971  1.00 27.84           C  
ANISOU  449  CB  ASN A  80     3757   3292   3530   -388   -215    -77       C  
ATOM    450  CG  ASN A  80      24.872  33.174  -0.695  1.00 46.94           C  
ANISOU  450  CG  ASN A  80     6239   5633   5964   -362   -215   -175       C  
ATOM    451  OD1 ASN A  80      25.434  33.032   0.392  1.00 42.26           O  
ANISOU  451  OD1 ASN A  80     5624   5084   5349   -425   -231   -256       O  
ATOM    452  ND2 ASN A  80      23.723  33.835  -0.786  1.00 36.78           N  
ANISOU  452  ND2 ASN A  80     5027   4242   4706   -260   -195   -169       N  
ATOM    453  N   LEU A  81      25.657  30.447  -4.467  1.00 28.15           N  
ANISOU  453  N   LEU A  81     3627   3579   3488   -325   -221     78       N  
ATOM    454  CA  LEU A  81      26.102  30.116  -5.826  1.00 28.26           C  
ANISOU  454  CA  LEU A  81     3601   3662   3473   -334   -211    157       C  
ATOM    455  C   LEU A  81      24.919  29.701  -6.714  1.00 32.36           C  
ANISOU  455  C   LEU A  81     4110   4222   3965   -226   -214    197       C  
ATOM    456  O   LEU A  81      24.926  29.972  -7.916  1.00 31.26           O  
ANISOU  456  O   LEU A  81     3973   4102   3804   -215   -202    276       O  
ATOM    457  CB  LEU A  81      27.199  29.039  -5.842  1.00 28.69           C  
ANISOU  457  CB  LEU A  81     3565   3842   3493   -384   -216    140       C  
ATOM    458  CG  LEU A  81      28.594  29.473  -6.319  1.00 34.61           C  
ANISOU  458  CG  LEU A  81     4293   4619   4239   -489   -199    185       C  
ATOM    459  CD1 LEU A  81      29.502  28.290  -6.420  1.00 35.63           C  
ANISOU  459  CD1 LEU A  81     4323   4886   4328   -504   -202    167       C  
ATOM    460  CD2 LEU A  81      28.559  30.132  -7.705  1.00 37.73           C  
ANISOU  460  CD2 LEU A  81     4713   5003   4621   -486   -173    283       C  
ATOM    461  N   TYR A  82      23.891  29.077  -6.107  1.00 29.69           N  
ANISOU  461  N   TYR A  82     3754   3906   3620   -153   -231    146       N  
ATOM    462  CA  TYR A  82      22.685  28.671  -6.815  1.00 29.62           C  
ANISOU  462  CA  TYR A  82     3723   3948   3582    -62   -240    173       C  
ATOM    463  C   TYR A  82      21.852  29.893  -7.201  1.00 34.29           C  
ANISOU  463  C   TYR A  82     4379   4457   4194      4   -230    231       C  
ATOM    464  O   TYR A  82      21.254  29.896  -8.273  1.00 33.51           O  
ANISOU  464  O   TYR A  82     4265   4407   4061     61   -233    294       O  
ATOM    465  CB  TYR A  82      21.856  27.683  -5.985  1.00 30.62           C  
ANISOU  465  CB  TYR A  82     3808   4128   3700    -22   -257    106       C  
ATOM    466  CG  TYR A  82      20.777  26.984  -6.779  1.00 32.12           C  
ANISOU  466  CG  TYR A  82     3951   4402   3850     42   -271    122       C  
ATOM    467  CD1 TYR A  82      21.045  26.450  -8.036  1.00 33.96           C  
ANISOU  467  CD1 TYR A  82     4151   4711   4040     33   -275    156       C  
ATOM    468  CD2 TYR A  82      19.498  26.816  -6.258  1.00 32.82           C  
ANISOU  468  CD2 TYR A  82     4022   4510   3937    103   -281     97       C  
ATOM    469  CE1 TYR A  82      20.064  25.783  -8.762  1.00 34.70           C  
ANISOU  469  CE1 TYR A  82     4201   4893   4089     77   -293    158       C  
ATOM    470  CE2 TYR A  82      18.510  26.140  -6.970  1.00 33.78           C  
ANISOU  470  CE2 TYR A  82     4090   4726   4019    144   -299    107       C  
ATOM    471  CZ  TYR A  82      18.801  25.623  -8.222  1.00 41.61           C  
ANISOU  471  CZ  TYR A  82     5054   5787   4967    127   -307    134       C  
ATOM    472  OH  TYR A  82      17.850  24.954  -8.944  1.00 43.80           O  
ANISOU  472  OH  TYR A  82     5279   6166   5198    153   -329    132       O  
ATOM    473  N   THR A  83      21.836  30.935  -6.340  1.00 31.70           N  
ANISOU  473  N   THR A  83     4126   4003   3918     -1   -217    208       N  
ATOM    474  CA  THR A  83      21.136  32.205  -6.588  1.00 31.83           C  
ANISOU  474  CA  THR A  83     4222   3904   3966     71   -200    261       C  
ATOM    475  C   THR A  83      21.736  32.895  -7.832  1.00 35.54           C  
ANISOU  475  C   THR A  83     4729   4340   4435     39   -183    372       C  
ATOM    476  O   THR A  83      20.985  33.408  -8.664  1.00 35.41           O  
ANISOU  476  O   THR A  83     4734   4311   4407    127   -179    457       O  
ATOM    477  CB  THR A  83      21.175  33.083  -5.318  1.00 39.87           C  
ANISOU  477  CB  THR A  83     5322   4787   5041     58   -186    190       C  
ATOM    478  OG1 THR A  83      20.562  32.364  -4.251  1.00 39.63           O  
ANISOU  478  OG1 THR A  83     5245   4819   4994     92   -199     99       O  
ATOM    479  CG2 THR A  83      20.468  34.423  -5.490  1.00 36.70           C  
ANISOU  479  CG2 THR A  83     5020   4241   4684    147   -163    235       C  
ATOM    480  N   VAL A  84      23.083  32.870  -7.963  1.00 32.01           N  
ANISOU  480  N   VAL A  84     4276   3894   3990    -84   -174    377       N  
ATOM    481  CA  VAL A  84      23.824  33.444  -9.098  1.00 31.85           C  
ANISOU  481  CA  VAL A  84     4278   3861   3962   -140   -153    484       C  
ATOM    482  C   VAL A  84      23.433  32.690 -10.392  1.00 34.47           C  
ANISOU  482  C   VAL A  84     4538   4343   4216    -79   -162    550       C  
ATOM    483  O   VAL A  84      23.109  33.327 -11.391  1.00 33.78           O  
ANISOU  483  O   VAL A  84     4482   4244   4110    -36   -150    658       O  
ATOM    484  CB  VAL A  84      25.365  33.473  -8.848  1.00 35.64           C  
ANISOU  484  CB  VAL A  84     4743   4344   4453   -292   -141    464       C  
ATOM    485  CG1 VAL A  84      26.129  33.976 -10.073  1.00 35.28           C  
ANISOU  485  CG1 VAL A  84     4704   4312   4389   -356   -114    582       C  
ATOM    486  CG2 VAL A  84      25.714  34.317  -7.625  1.00 35.42           C  
ANISOU  486  CG2 VAL A  84     4791   4174   4495   -363   -136    393       C  
ATOM    487  N   TYR A  85      23.414  31.346 -10.335  1.00 30.81           N  
ANISOU  487  N   TYR A  85     3984   4016   3706    -73   -184    482       N  
ATOM    488  CA  TYR A  85      23.042  30.452 -11.433  1.00 30.92           C  
ANISOU  488  CA  TYR A  85     3929   4179   3642    -27   -197    507       C  
ATOM    489  C   TYR A  85      21.612  30.722 -11.940  1.00 35.49           C  
ANISOU  489  C   TYR A  85     4512   4777   4195     90   -214    554       C  
ATOM    490  O   TYR A  85      21.405  30.763 -13.156  1.00 35.00           O  
ANISOU  490  O   TYR A  85     4428   4800   4069    124   -216    632       O  
ATOM    491  CB  TYR A  85      23.226  28.983 -11.002  1.00 32.11           C  
ANISOU  491  CB  TYR A  85     4004   4428   3769    -45   -215    406       C  
ATOM    492  CG  TYR A  85      22.747  27.953 -12.005  1.00 34.25           C  
ANISOU  492  CG  TYR A  85     4211   4840   3963     -4   -231    402       C  
ATOM    493  CD1 TYR A  85      23.503  27.645 -13.133  1.00 36.13           C  
ANISOU  493  CD1 TYR A  85     4416   5171   4140    -34   -216    438       C  
ATOM    494  CD2 TYR A  85      21.565  27.247 -11.798  1.00 35.32           C  
ANISOU  494  CD2 TYR A  85     4315   5024   4083     56   -259    352       C  
ATOM    495  CE1 TYR A  85      23.075  26.687 -14.051  1.00 37.04           C  
ANISOU  495  CE1 TYR A  85     4480   5417   4178      0   -230    416       C  
ATOM    496  CE2 TYR A  85      21.129  26.283 -12.707  1.00 36.42           C  
ANISOU  496  CE2 TYR A  85     4398   5289   4150     76   -277    333       C  
ATOM    497  CZ  TYR A  85      21.889  26.006 -13.832  1.00 46.12           C  
ANISOU  497  CZ  TYR A  85     5605   6600   5316     50   -263    359       C  
ATOM    498  OH  TYR A  85      21.469  25.053 -14.728  1.00 50.84           O  
ANISOU  498  OH  TYR A  85     6156   7323   5838     66   -280    323       O  
ATOM    499  N   ILE A  86      20.643  30.927 -11.011  1.00 32.19           N  
ANISOU  499  N   ILE A  86     4116   4297   3819    155   -225    509       N  
ATOM    500  CA  ILE A  86      19.240  31.220 -11.335  1.00 32.42           C  
ANISOU  500  CA  ILE A  86     4136   4354   3827    277   -240    550       C  
ATOM    501  C   ILE A  86      19.117  32.578 -12.040  1.00 38.52           C  
ANISOU  501  C   ILE A  86     4984   5039   4613    332   -220    677       C  
ATOM    502  O   ILE A  86      18.600  32.636 -13.154  1.00 37.89           O  
ANISOU  502  O   ILE A  86     4875   5052   4470    397   -232    764       O  
ATOM    503  CB  ILE A  86      18.303  31.107 -10.083  1.00 35.24           C  
ANISOU  503  CB  ILE A  86     4487   4681   4222    333   -250    467       C  
ATOM    504  CG1 ILE A  86      18.206  29.650  -9.532  1.00 35.17           C  
ANISOU  504  CG1 ILE A  86     4397   4777   4189    288   -271    365       C  
ATOM    505  CG2 ILE A  86      16.903  31.714 -10.333  1.00 35.46           C  
ANISOU  505  CG2 ILE A  86     4510   4727   4238    472   -258    521       C  
ATOM    506  CD1 ILE A  86      17.862  28.533 -10.532  1.00 40.52           C  
ANISOU  506  CD1 ILE A  86     4991   5616   4791    285   -298    365       C  
ATOM    507  N   ILE A  87      19.603  33.654 -11.384  1.00 37.11           N  
ANISOU  507  N   ILE A  87     4906   4681   4514    303   -191    687       N  
ATOM    508  CA  ILE A  87      19.572  35.044 -11.851  1.00 37.43           C  
ANISOU  508  CA  ILE A  87     5047   4584   4591    346   -164    805       C  
ATOM    509  C   ILE A  87      20.231  35.203 -13.237  1.00 41.71           C  
ANISOU  509  C   ILE A  87     5582   5188   5079    302   -152    930       C  
ATOM    510  O   ILE A  87      19.603  35.764 -14.137  1.00 41.49           O  
ANISOU  510  O   ILE A  87     5570   5175   5017    396   -151   1052       O  
ATOM    511  CB  ILE A  87      20.168  35.986 -10.757  1.00 40.78           C  
ANISOU  511  CB  ILE A  87     5583   4797   5115    284   -134    757       C  
ATOM    512  CG1 ILE A  87      19.171  36.135  -9.582  1.00 41.47           C  
ANISOU  512  CG1 ILE A  87     5690   4824   5243    381   -139    662       C  
ATOM    513  CG2 ILE A  87      20.585  37.360 -11.317  1.00 41.84           C  
ANISOU  513  CG2 ILE A  87     5837   4763   5298    273    -98    881       C  
ATOM    514  CD1 ILE A  87      19.734  36.734  -8.310  1.00 49.70           C  
ANISOU  514  CD1 ILE A  87     6819   5705   6362    307   -119    562       C  
ATOM    515  N   MET A  88      21.467  34.684 -13.411  1.00 38.08           N  
ANISOU  515  N   MET A  88     5088   4780   4599    168   -143    906       N  
ATOM    516  CA  MET A  88      22.211  34.764 -14.675  1.00 37.56           C  
ANISOU  516  CA  MET A  88     5004   4794   4471    115   -126   1016       C  
ATOM    517  C   MET A  88      21.629  33.880 -15.787  1.00 40.15           C  
ANISOU  517  C   MET A  88     5237   5333   4685    184   -152   1043       C  
ATOM    518  O   MET A  88      21.891  34.133 -16.963  1.00 39.79           O  
ANISOU  518  O   MET A  88     5185   5362   4572    184   -139   1159       O  
ATOM    519  CB  MET A  88      23.701  34.462 -14.462  1.00 40.11           C  
ANISOU  519  CB  MET A  88     5306   5129   4805    -40   -105    973       C  
ATOM    520  CG  MET A  88      24.446  35.565 -13.744  1.00 44.17           C  
ANISOU  520  CG  MET A  88     5918   5450   5415   -137    -74    983       C  
ATOM    521  SD  MET A  88      26.221  35.234 -13.627  1.00 49.09           S  
ANISOU  521  SD  MET A  88     6490   6128   6035   -323    -52    950       S  
ATOM    522  CE  MET A  88      26.785  35.904 -15.191  1.00 45.90           C  
ANISOU  522  CE  MET A  88     6094   5771   5573   -366    -12   1135       C  
ATOM    523  N   GLY A  89      20.862  32.860 -15.404  1.00 35.72           N  
ANISOU  523  N   GLY A  89     4604   4869   4097    232   -189    936       N  
ATOM    524  CA  GLY A  89      20.217  31.931 -16.329  1.00 35.19           C  
ANISOU  524  CA  GLY A  89     4446   5000   3924    283   -221    931       C  
ATOM    525  C   GLY A  89      21.128  30.878 -16.931  1.00 38.66           C  
ANISOU  525  C   GLY A  89     4820   5576   4295    201   -217    882       C  
ATOM    526  O   GLY A  89      20.705  30.152 -17.832  1.00 37.32           O  
ANISOU  526  O   GLY A  89     4583   5569   4027    232   -240    873       O  
ATOM    527  N   HIS A  90      22.386  30.788 -16.439  1.00 36.10           N  
ANISOU  527  N   HIS A  90     4511   5191   4014     98   -187    845       N  
ATOM    528  CA  HIS A  90      23.419  29.841 -16.887  1.00 36.31           C  
ANISOU  528  CA  HIS A  90     4477   5334   3987     26   -174    796       C  
ATOM    529  C   HIS A  90      24.618  29.840 -15.925  1.00 39.69           C  
ANISOU  529  C   HIS A  90     4917   5674   4488    -72   -150    743       C  
ATOM    530  O   HIS A  90      24.729  30.736 -15.083  1.00 39.76           O  
ANISOU  530  O   HIS A  90     4991   5534   4581   -101   -140    761       O  
ATOM    531  CB  HIS A  90      23.889  30.171 -18.329  1.00 37.42           C  
ANISOU  531  CB  HIS A  90     4602   5585   4033     17   -149    910       C  
ATOM    532  CG  HIS A  90      24.656  31.456 -18.449  1.00 40.97           C  
ANISOU  532  CG  HIS A  90     5116   5929   4523    -41   -108   1037       C  
ATOM    533  ND1 HIS A  90      24.015  32.682 -18.464  1.00 42.67           N  
ANISOU  533  ND1 HIS A  90     5411   6023   4778      9   -106   1149       N  
ATOM    534  CD2 HIS A  90      25.990  31.660 -18.562  1.00 42.68           C  
ANISOU  534  CD2 HIS A  90     5327   6144   4746   -147    -67   1067       C  
ATOM    535  CE1 HIS A  90      24.974  33.586 -18.572  1.00 42.03           C  
ANISOU  535  CE1 HIS A  90     5382   5854   4734    -78    -63   1242       C  
ATOM    536  NE2 HIS A  90      26.178  33.018 -18.638  1.00 42.36           N  
ANISOU  536  NE2 HIS A  90     5368   5973   4754   -180    -39   1197       N  
ATOM    537  N   TRP A  91      25.515  28.839 -16.063  1.00 35.45           N  
ANISOU  537  N   TRP A  91     4317   5238   3915   -118   -139    676       N  
ATOM    538  CA  TRP A  91      26.749  28.714 -15.285  1.00 34.75           C  
ANISOU  538  CA  TRP A  91     4214   5114   3875   -205   -119    633       C  
ATOM    539  C   TRP A  91      27.848  29.472 -16.047  1.00 38.42           C  
ANISOU  539  C   TRP A  91     4675   5611   4312   -281    -76    737       C  
ATOM    540  O   TRP A  91      28.103  29.167 -17.214  1.00 37.22           O  
ANISOU  540  O   TRP A  91     4480   5594   4069   -267    -57    780       O  
ATOM    541  CB  TRP A  91      27.123  27.238 -15.084  1.00 33.27           C  
ANISOU  541  CB  TRP A  91     3958   5024   3661   -196   -126    520       C  
ATOM    542  CG  TRP A  91      28.300  27.046 -14.174  1.00 34.17           C  
ANISOU  542  CG  TRP A  91     4046   5117   3822   -266   -113    475       C  
ATOM    543  CD1 TRP A  91      29.589  26.801 -14.543  1.00 37.08           C  
ANISOU  543  CD1 TRP A  91     4355   5577   4157   -316    -81    486       C  
ATOM    544  CD2 TRP A  91      28.306  27.167 -12.745  1.00 33.83           C  
ANISOU  544  CD2 TRP A  91     4026   4971   3858   -291   -132    417       C  
ATOM    545  NE1 TRP A  91      30.392  26.719 -13.430  1.00 36.63           N  
ANISOU  545  NE1 TRP A  91     4276   5486   4154   -370    -83    441       N  
ATOM    546  CE2 TRP A  91      29.630  26.938 -12.311  1.00 37.93           C  
ANISOU  546  CE2 TRP A  91     4494   5532   4386   -358   -115    397       C  
ATOM    547  CE3 TRP A  91      27.313  27.423 -11.783  1.00 34.98           C  
ANISOU  547  CE3 TRP A  91     4222   5010   4060   -259   -160    380       C  
ATOM    548  CZ2 TRP A  91      29.991  26.965 -10.956  1.00 37.22           C  
ANISOU  548  CZ2 TRP A  91     4404   5383   4354   -397   -131    341       C  
ATOM    549  CZ3 TRP A  91      27.671  27.446 -10.443  1.00 36.49           C  
ANISOU  549  CZ3 TRP A  91     4419   5139   4308   -298   -170    321       C  
ATOM    550  CH2 TRP A  91      28.995  27.221 -10.040  1.00 37.12           C  
ANISOU  550  CH2 TRP A  91     4450   5264   4390   -368   -159    303       C  
ATOM    551  N   ALA A  92      28.472  30.476 -15.398  1.00 35.55           N  
ANISOU  551  N   ALA A  92     4356   5129   4020   -368    -58    776       N  
ATOM    552  CA  ALA A  92      29.475  31.351 -16.021  1.00 35.66           C  
ANISOU  552  CA  ALA A  92     4373   5154   4020   -463    -14    886       C  
ATOM    553  C   ALA A  92      30.920  31.233 -15.482  1.00 39.91           C  
ANISOU  553  C   ALA A  92     4857   5724   4584   -582      7    850       C  
ATOM    554  O   ALA A  92      31.819  31.931 -15.974  1.00 39.99           O  
ANISOU  554  O   ALA A  92     4859   5750   4586   -682     45    940       O  
ATOM    555  CB  ALA A  92      29.003  32.794 -15.911  1.00 36.46           C  
ANISOU  555  CB  ALA A  92     4584   5086   4183   -479     -6    988       C  
ATOM    556  N   LEU A  93      31.145  30.329 -14.517  1.00 36.08           N  
ANISOU  556  N   LEU A  93     4326   5261   4123   -571    -18    728       N  
ATOM    557  CA  LEU A  93      32.409  30.168 -13.794  1.00 35.64           C  
ANISOU  557  CA  LEU A  93     4209   5243   4091   -666    -10    683       C  
ATOM    558  C   LEU A  93      33.370  29.081 -14.341  1.00 38.42           C  
ANISOU  558  C   LEU A  93     4442   5789   4366   -655     14    661       C  
ATOM    559  O   LEU A  93      34.478  28.933 -13.809  1.00 38.12           O  
ANISOU  559  O   LEU A  93     4335   5812   4337   -728     23    637       O  
ATOM    560  CB  LEU A  93      32.102  29.922 -12.302  1.00 35.75           C  
ANISOU  560  CB  LEU A  93     4245   5168   4172   -654    -50    574       C  
ATOM    561  CG  LEU A  93      31.221  30.967 -11.584  1.00 40.63           C  
ANISOU  561  CG  LEU A  93     4975   5596   4866   -662    -68    573       C  
ATOM    562  CD1 LEU A  93      29.737  30.641 -11.718  1.00 40.98           C  
ANISOU  562  CD1 LEU A  93     5066   5598   4907   -531    -92    554       C  
ATOM    563  CD2 LEU A  93      31.530  31.000 -10.119  1.00 43.47           C  
ANISOU  563  CD2 LEU A  93     5337   5899   5280   -720    -92    483       C  
ATOM    564  N   GLY A  94      32.962  28.369 -15.394  1.00 33.27           N  
ANISOU  564  N   GLY A  94     3766   5241   3636   -563     23    665       N  
ATOM    565  CA  GLY A  94      33.772  27.325 -16.020  1.00 32.22           C  
ANISOU  565  CA  GLY A  94     3532   5285   3424   -530     51    634       C  
ATOM    566  C   GLY A  94      33.425  25.906 -15.608  1.00 35.11           C  
ANISOU  566  C   GLY A  94     3874   5682   3785   -426     27    512       C  
ATOM    567  O   GLY A  94      32.654  25.698 -14.668  1.00 34.63           O  
ANISOU  567  O   GLY A  94     3862   5511   3785   -395    -14    452       O  
ATOM    568  N   ALA A  95      34.012  24.919 -16.312  1.00 31.01           N  
ANISOU  568  N   ALA A  95     3281   5310   3190   -371     56    477       N  
ATOM    569  CA  ALA A  95      33.796  23.486 -16.092  1.00 30.26           C  
ANISOU  569  CA  ALA A  95     3170   5241   3086   -270     43    364       C  
ATOM    570  C   ALA A  95      34.399  22.969 -14.791  1.00 34.26           C  
ANISOU  570  C   ALA A  95     3644   5717   3658   -270     28    307       C  
ATOM    571  O   ALA A  95      33.783  22.120 -14.133  1.00 33.84           O  
ANISOU  571  O   ALA A  95     3622   5594   3642   -208     -2    230       O  
ATOM    572  CB  ALA A  95      34.308  22.682 -17.277  1.00 30.74           C  
ANISOU  572  CB  ALA A  95     3170   5462   3045   -209     87    341       C  
ATOM    573  N   LEU A  96      35.595  23.469 -14.419  1.00 30.76           N  
ANISOU  573  N   LEU A  96     3131   5332   3224   -345     47    349       N  
ATOM    574  CA  LEU A  96      36.257  23.061 -13.179  1.00 30.83           C  
ANISOU  574  CA  LEU A  96     3092   5340   3281   -348     29    307       C  
ATOM    575  C   LEU A  96      35.477  23.546 -11.963  1.00 32.34           C  
ANISOU  575  C   LEU A  96     3358   5376   3552   -388    -21    288       C  
ATOM    576  O   LEU A  96      35.181  22.740 -11.085  1.00 32.01           O  
ANISOU  576  O   LEU A  96     3325   5294   3543   -330    -49    225       O  
ATOM    577  CB  LEU A  96      37.716  23.514 -13.131  1.00 31.37           C  
ANISOU  577  CB  LEU A  96     3054   5538   3328   -429     59    357       C  
ATOM    578  CG  LEU A  96      38.684  22.388 -12.825  1.00 36.86           C  
ANISOU  578  CG  LEU A  96     3646   6357   4001   -350     72    311       C  
ATOM    579  CD1 LEU A  96      39.644  22.173 -13.960  1.00 36.92           C  
ANISOU  579  CD1 LEU A  96     3553   6549   3925   -329    133    343       C  
ATOM    580  CD2 LEU A  96      39.417  22.640 -11.540  1.00 40.63           C  
ANISOU  580  CD2 LEU A  96     4071   6844   4524   -415     41    311       C  
ATOM    581  N   ALA A  97      35.066  24.834 -11.958  1.00 27.46           N  
ANISOU  581  N   ALA A  97     2803   4668   2964   -476    -29    343       N  
ATOM    582  CA  ALA A  97      34.259  25.429 -10.890  1.00 26.92           C  
ANISOU  582  CA  ALA A  97     2813   4449   2965   -508    -70    321       C  
ATOM    583  C   ALA A  97      32.901  24.720 -10.760  1.00 30.60           C  
ANISOU  583  C   ALA A  97     3344   4839   3445   -408    -97    268       C  
ATOM    584  O   ALA A  97      32.391  24.605  -9.648  1.00 29.71           O  
ANISOU  584  O   ALA A  97     3264   4646   3379   -399   -129    221       O  
ATOM    585  CB  ALA A  97      34.059  26.915 -11.137  1.00 27.42           C  
ANISOU  585  CB  ALA A  97     2941   4423   3055   -604    -62    394       C  
ATOM    586  N   CYS A  98      32.343  24.210 -11.883  1.00 27.45           N  
ANISOU  586  N   CYS A  98     2955   4478   2997   -339    -83    271       N  
ATOM    587  CA  CYS A  98      31.078  23.474 -11.884  1.00 27.68           C  
ANISOU  587  CA  CYS A  98     3031   4456   3030   -258   -109    218       C  
ATOM    588  C   CYS A  98      31.217  22.150 -11.122  1.00 31.20           C  
ANISOU  588  C   CYS A  98     3452   4911   3493   -202   -120    139       C  
ATOM    589  O   CYS A  98      30.454  21.910 -10.190  1.00 30.80           O  
ANISOU  589  O   CYS A  98     3437   4779   3486   -186   -150    103       O  
ATOM    590  CB  CYS A  98      30.557  23.253 -13.304  1.00 28.35           C  
ANISOU  590  CB  CYS A  98     3122   4603   3045   -213    -94    234       C  
ATOM    591  SG  CYS A  98      29.143  22.120 -13.397  1.00 32.54           S  
ANISOU  591  SG  CYS A  98     3688   5107   3568   -130   -125    151       S  
ATOM    592  N   ASP A  99      32.203  21.310 -11.509  1.00 27.87           N  
ANISOU  592  N   ASP A  99     2967   4590   3035   -167    -93    120       N  
ATOM    593  CA  ASP A  99      32.479  20.015 -10.880  1.00 27.60           C  
ANISOU  593  CA  ASP A  99     2909   4561   3015    -99    -97     59       C  
ATOM    594  C   ASP A  99      32.835  20.145  -9.393  1.00 28.69           C  
ANISOU  594  C   ASP A  99     3033   4661   3205   -127   -122     59       C  
ATOM    595  O   ASP A  99      32.382  19.328  -8.593  1.00 27.67           O  
ANISOU  595  O   ASP A  99     2927   4478   3107    -81   -142     20       O  
ATOM    596  CB  ASP A  99      33.575  19.251 -11.652  1.00 30.02           C  
ANISOU  596  CB  ASP A  99     3147   4989   3268    -44    -55     46       C  
ATOM    597  CG  ASP A  99      33.195  18.850 -13.075  1.00 45.99           C  
ANISOU  597  CG  ASP A  99     5186   7062   5226      0    -29     21       C  
ATOM    598  OD1 ASP A  99      32.000  18.546 -13.314  1.00 46.24           O  
ANISOU  598  OD1 ASP A  99     5283   7027   5260     16    -51    -15       O  
ATOM    599  OD2 ASP A  99      34.096  18.825 -13.947  1.00 55.35           O  
ANISOU  599  OD2 ASP A  99     6312   8369   6351     16     13     35       O  
ATOM    600  N   LEU A 100      33.612  21.183  -9.029  1.00 24.46           N  
ANISOU  600  N   LEU A 100     2462   4156   2676   -212   -122    104       N  
ATOM    601  CA  LEU A 100      34.011  21.459  -7.644  1.00 24.43           C  
ANISOU  601  CA  LEU A 100     2439   4137   2707   -257   -150    100       C  
ATOM    602  C   LEU A 100      32.837  21.958  -6.781  1.00 27.81           C  
ANISOU  602  C   LEU A 100     2948   4439   3178   -279   -184     80       C  
ATOM    603  O   LEU A 100      32.728  21.547  -5.627  1.00 26.77           O  
ANISOU  603  O   LEU A 100     2817   4288   3067   -263   -208     52       O  
ATOM    604  CB  LEU A 100      35.210  22.427  -7.574  1.00 24.62           C  
ANISOU  604  CB  LEU A 100     2397   4238   2719   -359   -141    143       C  
ATOM    605  CG  LEU A 100      36.532  21.960  -8.223  1.00 29.40           C  
ANISOU  605  CG  LEU A 100     2893   5002   3276   -340   -106    166       C  
ATOM    606  CD1 LEU A 100      37.566  23.070  -8.202  1.00 29.52           C  
ANISOU  606  CD1 LEU A 100     2846   5092   3280   -470    -97    215       C  
ATOM    607  CD2 LEU A 100      37.090  20.693  -7.557  1.00 31.11           C  
ANISOU  607  CD2 LEU A 100     3047   5286   3487   -245   -113    136       C  
ATOM    608  N   ALA A 101      31.944  22.809  -7.351  1.00 24.73           N  
ANISOU  608  N   ALA A 101     2624   3975   2797   -305   -182     99       N  
ATOM    609  CA  ALA A 101      30.742  23.317  -6.675  1.00 24.09           C  
ANISOU  609  CA  ALA A 101     2617   3784   2753   -308   -207     80       C  
ATOM    610  C   ALA A 101      29.715  22.186  -6.470  1.00 28.15           C  
ANISOU  610  C   ALA A 101     3152   4272   3271   -226   -220     39       C  
ATOM    611  O   ALA A 101      29.087  22.134  -5.412  1.00 28.41           O  
ANISOU  611  O   ALA A 101     3211   4255   3330   -221   -241     12       O  
ATOM    612  CB  ALA A 101      30.116  24.453  -7.472  1.00 24.54           C  
ANISOU  612  CB  ALA A 101     2731   3781   2814   -334   -198    123       C  
ATOM    613  N   LEU A 102      29.547  21.286  -7.470  1.00 23.83           N  
ANISOU  613  N   LEU A 102     2595   3763   2695   -171   -206     30       N  
ATOM    614  CA  LEU A 102      28.628  20.146  -7.364  1.00 23.83           C  
ANISOU  614  CA  LEU A 102     2617   3735   2702   -112   -216    -13       C  
ATOM    615  C   LEU A 102      29.132  19.150  -6.327  1.00 27.70           C  
ANISOU  615  C   LEU A 102     3085   4229   3212    -84   -221    -35       C  
ATOM    616  O   LEU A 102      28.329  18.639  -5.543  1.00 26.99           O  
ANISOU  616  O   LEU A 102     3021   4088   3145    -68   -237    -55       O  
ATOM    617  CB  LEU A 102      28.423  19.422  -8.707  1.00 23.86           C  
ANISOU  617  CB  LEU A 102     2620   3780   2666    -71   -199    -32       C  
ATOM    618  CG  LEU A 102      27.606  20.130  -9.784  1.00 28.43           C  
ANISOU  618  CG  LEU A 102     3222   4367   3213    -80   -201     -9       C  
ATOM    619  CD1 LEU A 102      27.855  19.483 -11.138  1.00 28.24           C  
ANISOU  619  CD1 LEU A 102     3180   4420   3128    -48   -180    -30       C  
ATOM    620  CD2 LEU A 102      26.106  20.158  -9.443  1.00 29.22           C  
ANISOU  620  CD2 LEU A 102     3360   4410   3331    -71   -229    -26       C  
ATOM    621  N   ALA A 103      30.462  18.874  -6.323  1.00 23.84           N  
ANISOU  621  N   ALA A 103     2539   3811   2708    -74   -206    -23       N  
ATOM    622  CA  ALA A 103      31.078  17.964  -5.355  1.00 23.18           C  
ANISOU  622  CA  ALA A 103     2425   3746   2636    -33   -211    -28       C  
ATOM    623  C   ALA A 103      30.831  18.489  -3.938  1.00 27.29           C  
ANISOU  623  C   ALA A 103     2953   4239   3176    -75   -241    -21       C  
ATOM    624  O   ALA A 103      30.366  17.723  -3.101  1.00 27.07           O  
ANISOU  624  O   ALA A 103     2944   4177   3164    -40   -252    -28       O  
ATOM    625  CB  ALA A 103      32.573  17.819  -5.621  1.00 23.60           C  
ANISOU  625  CB  ALA A 103     2400   3906   2663    -15   -190     -8       C  
ATOM    626  N   LEU A 104      31.046  19.805  -3.700  1.00 23.57           N  
ANISOU  626  N   LEU A 104     2477   3776   2703   -152   -251     -9       N  
ATOM    627  CA  LEU A 104      30.826  20.435  -2.394  1.00 23.57           C  
ANISOU  627  CA  LEU A 104     2490   3753   2713   -197   -277    -19       C  
ATOM    628  C   LEU A 104      29.348  20.403  -1.968  1.00 26.95           C  
ANISOU  628  C   LEU A 104     2983   4097   3161   -179   -287    -41       C  
ATOM    629  O   LEU A 104      29.062  20.089  -0.819  1.00 26.83           O  
ANISOU  629  O   LEU A 104     2970   4079   3144   -169   -302    -51       O  
ATOM    630  CB  LEU A 104      31.410  21.864  -2.353  1.00 23.58           C  
ANISOU  630  CB  LEU A 104     2485   3763   2712   -292   -281    -14       C  
ATOM    631  CG  LEU A 104      31.297  22.666  -1.039  1.00 28.50           C  
ANISOU  631  CG  LEU A 104     3126   4364   3338   -352   -307    -44       C  
ATOM    632  CD1 LEU A 104      31.803  21.870   0.177  1.00 28.60           C  
ANISOU  632  CD1 LEU A 104     3087   4455   3325   -327   -330    -51       C  
ATOM    633  CD2 LEU A 104      32.075  23.959  -1.132  1.00 31.19           C  
ANISOU  633  CD2 LEU A 104     3460   4711   3680   -458   -308    -43       C  
ATOM    634  N   ASP A 105      28.426  20.676  -2.897  1.00 22.84           N  
ANISOU  634  N   ASP A 105     2505   3526   2649   -170   -277    -43       N  
ATOM    635  CA  ASP A 105      26.986  20.664  -2.646  1.00 22.39           C  
ANISOU  635  CA  ASP A 105     2492   3411   2605   -150   -284    -59       C  
ATOM    636  C   ASP A 105      26.455  19.272  -2.263  1.00 25.70           C  
ANISOU  636  C   ASP A 105     2909   3826   3029   -105   -286    -69       C  
ATOM    637  O   ASP A 105      25.712  19.156  -1.291  1.00 25.36           O  
ANISOU  637  O   ASP A 105     2879   3765   2991   -104   -295    -77       O  
ATOM    638  CB  ASP A 105      26.223  21.215  -3.866  1.00 23.93           C  
ANISOU  638  CB  ASP A 105     2716   3579   2799   -143   -276    -49       C  
ATOM    639  CG  ASP A 105      24.721  21.202  -3.671  1.00 29.73           C  
ANISOU  639  CG  ASP A 105     3478   4279   3541   -117   -285    -63       C  
ATOM    640  OD1 ASP A 105      24.228  21.992  -2.850  1.00 30.59           O  
ANISOU  640  OD1 ASP A 105     3608   4355   3660   -123   -290    -71       O  
ATOM    641  OD2 ASP A 105      24.048  20.377  -4.317  1.00 33.31           O  
ANISOU  641  OD2 ASP A 105     3927   4744   3985    -92   -285    -71       O  
ATOM    642  N   TYR A 106      26.828  18.234  -3.034  1.00 21.57           N  
ANISOU  642  N   TYR A 106     2375   3318   2504    -72   -273    -70       N  
ATOM    643  CA  TYR A 106      26.408  16.849  -2.813  1.00 20.80           C  
ANISOU  643  CA  TYR A 106     2291   3194   2420    -35   -270    -79       C  
ATOM    644  C   TYR A 106      27.069  16.211  -1.590  1.00 23.57           C  
ANISOU  644  C   TYR A 106     2623   3558   2775    -14   -274    -55       C  
ATOM    645  O   TYR A 106      26.411  15.440  -0.891  1.00 22.99           O  
ANISOU  645  O   TYR A 106     2570   3449   2715     -4   -276    -48       O  
ATOM    646  CB  TYR A 106      26.642  16.005  -4.072  1.00 21.53           C  
ANISOU  646  CB  TYR A 106     2389   3285   2507     -3   -252   -100       C  
ATOM    647  CG  TYR A 106      25.555  16.150  -5.116  1.00 22.88           C  
ANISOU  647  CG  TYR A 106     2585   3443   2667    -19   -254   -127       C  
ATOM    648  CD1 TYR A 106      25.481  17.284  -5.924  1.00 24.66           C  
ANISOU  648  CD1 TYR A 106     2802   3700   2866    -39   -256   -116       C  
ATOM    649  CD2 TYR A 106      24.625  15.137  -5.327  1.00 23.55           C  
ANISOU  649  CD2 TYR A 106     2697   3488   2763    -19   -256   -159       C  
ATOM    650  CE1 TYR A 106      24.483  17.422  -6.887  1.00 25.66           C  
ANISOU  650  CE1 TYR A 106     2942   3836   2973    -44   -263   -131       C  
ATOM    651  CE2 TYR A 106      23.636  15.253  -6.304  1.00 24.49           C  
ANISOU  651  CE2 TYR A 106     2825   3620   2861    -39   -264   -188       C  
ATOM    652  CZ  TYR A 106      23.577  16.392  -7.090  1.00 32.23           C  
ANISOU  652  CZ  TYR A 106     3790   4650   3808    -45   -269   -171       C  
ATOM    653  OH  TYR A 106      22.600  16.513  -8.048  1.00 34.17           O  
ANISOU  653  OH  TYR A 106     4035   4928   4022    -56   -282   -189       O  
ATOM    654  N   VAL A 107      28.359  16.525  -1.329  1.00 19.46           N  
ANISOU  654  N   VAL A 107     2057   3098   2238    -11   -276    -37       N  
ATOM    655  CA  VAL A 107      29.099  16.013  -0.163  1.00 19.10           C  
ANISOU  655  CA  VAL A 107     1980   3095   2184     16   -286     -6       C  
ATOM    656  C   VAL A 107      28.483  16.558   1.142  1.00 23.36           C  
ANISOU  656  C   VAL A 107     2527   3637   2711    -22   -306     -4       C  
ATOM    657  O   VAL A 107      28.250  15.772   2.063  1.00 22.88           O  
ANISOU  657  O   VAL A 107     2472   3575   2648      5   -310     24       O  
ATOM    658  CB  VAL A 107      30.638  16.247  -0.269  1.00 22.72           C  
ANISOU  658  CB  VAL A 107     2368   3646   2618     26   -286     12       C  
ATOM    659  CG1 VAL A 107      31.345  16.040   1.067  1.00 22.25           C  
ANISOU  659  CG1 VAL A 107     2261   3659   2533     40   -307     46       C  
ATOM    660  CG2 VAL A 107      31.256  15.350  -1.338  1.00 22.52           C  
ANISOU  660  CG2 VAL A 107     2331   3628   2599     95   -257     13       C  
ATOM    661  N   ALA A 108      28.192  17.887   1.197  1.00 20.13           N  
ANISOU  661  N   ALA A 108     2126   3229   2293    -81   -316    -31       N  
ATOM    662  CA  ALA A 108      27.576  18.573   2.352  1.00 19.98           C  
ANISOU  662  CA  ALA A 108     2121   3213   2256   -113   -331    -48       C  
ATOM    663  C   ALA A 108      26.153  18.064   2.642  1.00 22.82           C  
ANISOU  663  C   ALA A 108     2517   3526   2627    -94   -322    -48       C  
ATOM    664  O   ALA A 108      25.842  17.788   3.800  1.00 22.26           O  
ANISOU  664  O   ALA A 108     2442   3483   2534    -91   -328    -37       O  
ATOM    665  CB  ALA A 108      27.565  20.080   2.139  1.00 20.56           C  
ANISOU  665  CB  ALA A 108     2213   3270   2330   -169   -335    -84       C  
ATOM    666  N   SER A 109      25.313  17.913   1.589  1.00 18.93           N  
ANISOU  666  N   SER A 109     2051   2981   2162    -87   -309    -58       N  
ATOM    667  CA  SER A 109      23.942  17.390   1.670  1.00 18.35           C  
ANISOU  667  CA  SER A 109     1997   2876   2098    -81   -302    -59       C  
ATOM    668  C   SER A 109      23.938  15.943   2.177  1.00 22.90           C  
ANISOU  668  C   SER A 109     2575   3443   2683    -62   -295    -23       C  
ATOM    669  O   SER A 109      23.116  15.602   3.027  1.00 23.47           O  
ANISOU  669  O   SER A 109     2650   3519   2747    -71   -291     -7       O  
ATOM    670  CB  SER A 109      23.258  17.461   0.308  1.00 20.64           C  
ANISOU  670  CB  SER A 109     2303   3134   2406    -81   -296    -77       C  
ATOM    671  OG  SER A 109      23.119  18.800  -0.127  1.00 27.87           O  
ANISOU  671  OG  SER A 109     3226   4048   3316    -91   -300    -93       O  
ATOM    672  N   ASN A 110      24.864  15.101   1.668  1.00 19.13           N  
ANISOU  672  N   ASN A 110     2097   2951   2221    -31   -290     -7       N  
ATOM    673  CA  ASN A 110      25.013  13.704   2.093  1.00 18.63           C  
ANISOU  673  CA  ASN A 110     2047   2856   2174      1   -279     33       C  
ATOM    674  C   ASN A 110      25.504  13.614   3.541  1.00 21.59           C  
ANISOU  674  C   ASN A 110     2398   3286   2518     16   -289     83       C  
ATOM    675  O   ASN A 110      25.048  12.741   4.281  1.00 21.61           O  
ANISOU  675  O   ASN A 110     2419   3268   2526     23   -280    129       O  
ATOM    676  CB  ASN A 110      25.953  12.944   1.163  1.00 18.21           C  
ANISOU  676  CB  ASN A 110     2002   2775   2143     50   -267     30       C  
ATOM    677  CG  ASN A 110      25.879  11.456   1.343  1.00 34.83           C  
ANISOU  677  CG  ASN A 110     4147   4806   4281     86   -249     62       C  
ATOM    678  OD1 ASN A 110      25.048  10.781   0.735  1.00 29.52           O  
ANISOU  678  OD1 ASN A 110     3520   4057   3640     64   -237     36       O  
ATOM    679  ND2 ASN A 110      26.738  10.911   2.192  1.00 24.42           N  
ANISOU  679  ND2 ASN A 110     2815   3507   2957    141   -249    122       N  
ATOM    680  N   ALA A 111      26.424  14.517   3.944  1.00 17.60           N  
ANISOU  680  N   ALA A 111     1852   2859   1977     14   -307     77       N  
ATOM    681  CA  ALA A 111      26.961  14.571   5.307  1.00 17.63           C  
ANISOU  681  CA  ALA A 111     1821   2944   1933     22   -324    114       C  
ATOM    682  C   ALA A 111      25.853  14.918   6.311  1.00 23.07           C  
ANISOU  682  C   ALA A 111     2522   3651   2594    -13   -324    110       C  
ATOM    683  O   ALA A 111      25.871  14.389   7.423  1.00 22.56           O  
ANISOU  683  O   ALA A 111     2446   3634   2493      3   -327    162       O  
ATOM    684  CB  ALA A 111      28.099  15.579   5.396  1.00 18.11           C  
ANISOU  684  CB  ALA A 111     1833   3088   1961      1   -346     87       C  
ATOM    685  N   ALA A 112      24.879  15.775   5.905  1.00 20.72           N  
ANISOU  685  N   ALA A 112     2245   3323   2305    -50   -318     55       N  
ATOM    686  CA  ALA A 112      23.735  16.169   6.733  1.00 21.38           C  
ANISOU  686  CA  ALA A 112     2334   3430   2361    -71   -311     43       C  
ATOM    687  C   ALA A 112      22.864  14.945   7.058  1.00 27.65           C  
ANISOU  687  C   ALA A 112     3140   4201   3167    -68   -290     99       C  
ATOM    688  O   ALA A 112      22.476  14.766   8.212  1.00 27.92           O  
ANISOU  688  O   ALA A 112     3161   4292   3157    -72   -285    132       O  
ATOM    689  CB  ALA A 112      22.911  17.249   6.038  1.00 21.86           C  
ANISOU  689  CB  ALA A 112     2411   3458   2438    -90   -305    -19       C  
ATOM    690  N   VAL A 113      22.629  14.074   6.058  1.00 24.58           N  
ANISOU  690  N   VAL A 113     2776   3730   2833    -66   -279    111       N  
ATOM    691  CA  VAL A 113      21.860  12.833   6.197  1.00 24.60           C  
ANISOU  691  CA  VAL A 113     2800   3685   2861    -81   -259    161       C  
ATOM    692  C   VAL A 113      22.582  11.870   7.150  1.00 29.89           C  
ANISOU  692  C   VAL A 113     3475   4364   3518    -47   -255    246       C  
ATOM    693  O   VAL A 113      21.935  11.248   7.988  1.00 29.73           O  
ANISOU  693  O   VAL A 113     3459   4354   3483    -66   -240    305       O  
ATOM    694  CB  VAL A 113      21.568  12.160   4.817  1.00 27.73           C  
ANISOU  694  CB  VAL A 113     3231   3987   3318    -94   -250    135       C  
ATOM    695  CG1 VAL A 113      20.682  10.925   4.970  1.00 27.21           C  
ANISOU  695  CG1 VAL A 113     3195   3861   3283   -133   -229    176       C  
ATOM    696  CG2 VAL A 113      20.937  13.143   3.840  1.00 27.44           C  
ANISOU  696  CG2 VAL A 113     3182   3960   3283   -116   -258     65       C  
ATOM    697  N   MET A 114      23.910  11.742   7.009  1.00 28.26           N  
ANISOU  697  N   MET A 114     3262   4163   3313      6   -268    259       N  
ATOM    698  CA  MET A 114      24.713  10.830   7.829  1.00 29.49           C  
ANISOU  698  CA  MET A 114     3416   4335   3453     60   -268    348       C  
ATOM    699  C   MET A 114      24.782  11.256   9.288  1.00 30.88           C  
ANISOU  699  C   MET A 114     3551   4635   3548     57   -282    388       C  
ATOM    700  O   MET A 114      24.811  10.389  10.159  1.00 30.20           O  
ANISOU  700  O   MET A 114     3471   4563   3442     82   -273    482       O  
ATOM    701  CB  MET A 114      26.102  10.603   7.227  1.00 32.90           C  
ANISOU  701  CB  MET A 114     3835   4763   3902    128   -278    349       C  
ATOM    702  CG  MET A 114      26.043   9.907   5.891  1.00 38.13           C  
ANISOU  702  CG  MET A 114     4547   5305   4637    143   -258    316       C  
ATOM    703  SD  MET A 114      27.661   9.386   5.321  1.00 44.48           S  
ANISOU  703  SD  MET A 114     5333   6112   5456    247   -256    333       S  
ATOM    704  CE  MET A 114      27.644   7.720   5.882  1.00 41.42           C  
ANISOU  704  CE  MET A 114     5008   5622   5108    316   -231    435       C  
ATOM    705  N   ASN A 115      24.741  12.576   9.553  1.00 26.15           N  
ANISOU  705  N   ASN A 115     2916   4120   2900     25   -301    317       N  
ATOM    706  CA  ASN A 115      24.696  13.126  10.906  1.00 25.51           C  
ANISOU  706  CA  ASN A 115     2799   4163   2729     13   -313    325       C  
ATOM    707  C   ASN A 115      23.325  12.860  11.534  1.00 29.29           C  
ANISOU  707  C   ASN A 115     3292   4649   3190    -19   -285    353       C  
ATOM    708  O   ASN A 115      23.256  12.531  12.717  1.00 29.24           O  
ANISOU  708  O   ASN A 115     3265   4729   3115    -11   -282    417       O  
ATOM    709  CB  ASN A 115      25.053  14.609  10.922  1.00 24.42           C  
ANISOU  709  CB  ASN A 115     2636   4087   2556    -17   -337    225       C  
ATOM    710  CG  ASN A 115      26.527  14.861  10.724  1.00 42.34           C  
ANISOU  710  CG  ASN A 115     4869   6406   4813     -1   -368    217       C  
ATOM    711  OD1 ASN A 115      26.942  15.555   9.792  1.00 41.10           O  
ANISOU  711  OD1 ASN A 115     4713   6215   4690    -22   -375    153       O  
ATOM    712  ND2 ASN A 115      27.356  14.301  11.592  1.00 30.43           N  
ANISOU  712  ND2 ASN A 115     3321   4990   3251     38   -386    288       N  
ATOM    713  N   LEU A 116      22.247  12.929  10.725  1.00 25.39           N  
ANISOU  713  N   LEU A 116     2822   4077   2749    -55   -263    313       N  
ATOM    714  CA  LEU A 116      20.885  12.608  11.164  1.00 25.25           C  
ANISOU  714  CA  LEU A 116     2804   4072   2720    -93   -233    340       C  
ATOM    715  C   LEU A 116      20.804  11.120  11.549  1.00 28.57           C  
ANISOU  715  C   LEU A 116     3248   4448   3159    -94   -213    458       C  
ATOM    716  O   LEU A 116      20.146  10.778  12.532  1.00 27.51           O  
ANISOU  716  O   LEU A 116     3099   4378   2977   -116   -191    522       O  
ATOM    717  CB  LEU A 116      19.834  12.968  10.087  1.00 25.24           C  
ANISOU  717  CB  LEU A 116     2811   4010   2771   -128   -221    274       C  
ATOM    718  CG  LEU A 116      19.597  14.468   9.846  1.00 30.22           C  
ANISOU  718  CG  LEU A 116     3423   4678   3379   -122   -231    174       C  
ATOM    719  CD1 LEU A 116      18.770  14.697   8.595  1.00 30.82           C  
ANISOU  719  CD1 LEU A 116     3507   4689   3513   -139   -227    126       C  
ATOM    720  CD2 LEU A 116      18.939  15.138  11.046  1.00 32.79           C  
ANISOU  720  CD2 LEU A 116     3717   5115   3627   -122   -216    157       C  
ATOM    721  N   LEU A 117      21.521  10.251  10.804  1.00 25.54           N  
ANISOU  721  N   LEU A 117     2905   3956   2844    -66   -216    489       N  
ATOM    722  CA  LEU A 117      21.608   8.820  11.108  1.00 25.70           C  
ANISOU  722  CA  LEU A 117     2967   3902   2897    -54   -195    602       C  
ATOM    723  C   LEU A 117      22.415   8.602  12.393  1.00 30.47           C  
ANISOU  723  C   LEU A 117     3546   4605   3426      2   -205    698       C  
ATOM    724  O   LEU A 117      22.040   7.755  13.205  1.00 31.01           O  
ANISOU  724  O   LEU A 117     3631   4673   3477     -5   -182    809       O  
ATOM    725  CB  LEU A 117      22.228   8.028   9.951  1.00 25.53           C  
ANISOU  725  CB  LEU A 117     3000   3735   2965    -20   -194    592       C  
ATOM    726  CG  LEU A 117      21.328   7.771   8.750  1.00 30.15           C  
ANISOU  726  CG  LEU A 117     3622   4210   3623    -85   -179    524       C  
ATOM    727  CD1 LEU A 117      22.159   7.517   7.503  1.00 30.39           C  
ANISOU  727  CD1 LEU A 117     3688   4148   3713    -39   -187    467       C  
ATOM    728  CD2 LEU A 117      20.351   6.620   9.013  1.00 31.61           C  
ANISOU  728  CD2 LEU A 117     3854   4310   3848   -151   -145    596       C  
ATOM    729  N   LEU A 118      23.492   9.390  12.591  1.00 26.53           N  
ANISOU  729  N   LEU A 118     3004   4201   2876     51   -241    659       N  
ATOM    730  CA  LEU A 118      24.337   9.337  13.787  1.00 26.53           C  
ANISOU  730  CA  LEU A 118     2963   4331   2787    103   -261    736       C  
ATOM    731  C   LEU A 118      23.575   9.754  15.049  1.00 30.01           C  
ANISOU  731  C   LEU A 118     3370   4907   3126     64   -253    756       C  
ATOM    732  O   LEU A 118      23.767   9.138  16.090  1.00 29.42           O  
ANISOU  732  O   LEU A 118     3282   4909   2987     94   -251    869       O  
ATOM    733  CB  LEU A 118      25.603  10.191  13.613  1.00 26.85           C  
ANISOU  733  CB  LEU A 118     2953   4454   2795    140   -304    670       C  
ATOM    734  CG  LEU A 118      26.717   9.599  12.735  1.00 31.93           C  
ANISOU  734  CG  LEU A 118     3606   5022   3503    211   -312    690       C  
ATOM    735  CD1 LEU A 118      27.777  10.638  12.436  1.00 32.01           C  
ANISOU  735  CD1 LEU A 118     3556   5124   3483    216   -350    607       C  
ATOM    736  CD2 LEU A 118      27.358   8.378  13.388  1.00 34.60           C  
ANISOU  736  CD2 LEU A 118     3949   5367   3829    299   -309    836       C  
ATOM    737  N   ILE A 119      22.693  10.774  14.947  1.00 27.06           N  
ANISOU  737  N   ILE A 119     2980   4565   2734      6   -246    651       N  
ATOM    738  CA  ILE A 119      21.849  11.256  16.050  1.00 26.48           C  
ANISOU  738  CA  ILE A 119     2874   4622   2564    -26   -230    648       C  
ATOM    739  C   ILE A 119      20.869  10.137  16.452  1.00 31.42           C  
ANISOU  739  C   ILE A 119     3519   5217   3201    -57   -185    766       C  
ATOM    740  O   ILE A 119      20.790   9.789  17.636  1.00 31.58           O  
ANISOU  740  O   ILE A 119     3517   5349   3132    -50   -173    859       O  
ATOM    741  CB  ILE A 119      21.118  12.588  15.677  1.00 28.70           C  
ANISOU  741  CB  ILE A 119     3142   4921   2841    -62   -227    502       C  
ATOM    742  CG1 ILE A 119      22.118  13.761  15.561  1.00 28.65           C  
ANISOU  742  CG1 ILE A 119     3120   4957   2807    -46   -269    396       C  
ATOM    743  CG2 ILE A 119      20.000  12.928  16.687  1.00 28.38           C  
ANISOU  743  CG2 ILE A 119     3070   5001   2712    -86   -195    499       C  
ATOM    744  CD1 ILE A 119      21.663  14.955  14.670  1.00 34.91           C  
ANISOU  744  CD1 ILE A 119     3929   5686   3649    -68   -269    264       C  
ATOM    745  N   SER A 120      20.153   9.570  15.452  1.00 27.32           N  
ANISOU  745  N   SER A 120     3041   4551   2788    -98   -161    764       N  
ATOM    746  CA  SER A 120      19.167   8.498  15.602  1.00 26.71           C  
ANISOU  746  CA  SER A 120     2988   4416   2743   -155   -117    863       C  
ATOM    747  C   SER A 120      19.748   7.252  16.254  1.00 31.96           C  
ANISOU  747  C   SER A 120     3690   5046   3407   -122   -107   1024       C  
ATOM    748  O   SER A 120      19.179   6.780  17.236  1.00 31.92           O  
ANISOU  748  O   SER A 120     3674   5110   3345   -152    -77   1131       O  
ATOM    749  CB  SER A 120      18.542   8.147  14.256  1.00 28.88           C  
ANISOU  749  CB  SER A 120     3302   4535   3134   -208   -106    809       C  
ATOM    750  OG  SER A 120      17.943   9.286  13.662  1.00 37.44           O  
ANISOU  750  OG  SER A 120     4350   5659   4215   -228   -115    679       O  
ATOM    751  N   PHE A 121      20.881   6.733  15.732  1.00 29.64           N  
ANISOU  751  N   PHE A 121     3437   4653   3170    -52   -130   1047       N  
ATOM    752  CA  PHE A 121      21.544   5.541  16.269  1.00 30.06           C  
ANISOU  752  CA  PHE A 121     3532   4658   3232      7   -122   1204       C  
ATOM    753  C   PHE A 121      22.073   5.728  17.696  1.00 34.78           C  
ANISOU  753  C   PHE A 121     4074   5447   3694     59   -138   1295       C  
ATOM    754  O   PHE A 121      21.910   4.824  18.521  1.00 34.09           O  
ANISOU  754  O   PHE A 121     4008   5366   3579     66   -112   1452       O  
ATOM    755  CB  PHE A 121      22.652   5.039  15.334  1.00 31.88           C  
ANISOU  755  CB  PHE A 121     3810   4752   3551     88   -140   1193       C  
ATOM    756  CG  PHE A 121      22.181   4.087  14.258  1.00 33.71           C  
ANISOU  756  CG  PHE A 121     4131   4763   3916     49   -109   1188       C  
ATOM    757  CD1 PHE A 121      21.880   2.764  14.560  1.00 36.61           C  
ANISOU  757  CD1 PHE A 121     4574   5001   4334     41    -71   1326       C  
ATOM    758  CD2 PHE A 121      22.068   4.506  12.936  1.00 36.08           C  
ANISOU  758  CD2 PHE A 121     4444   4980   4285     20   -117   1046       C  
ATOM    759  CE1 PHE A 121      21.448   1.883  13.562  1.00 37.63           C  
ANISOU  759  CE1 PHE A 121     4796   4915   4586     -7    -43   1305       C  
ATOM    760  CE2 PHE A 121      21.634   3.626  11.940  1.00 38.90           C  
ANISOU  760  CE2 PHE A 121     4883   5144   4753    -22    -92   1027       C  
ATOM    761  CZ  PHE A 121      21.331   2.320  12.259  1.00 36.93           C  
ANISOU  761  CZ  PHE A 121     4714   4762   4558    -39    -55   1149       C  
ATOM    762  N   ASP A 122      22.672   6.904  17.993  1.00 31.78           N  
ANISOU  762  N   ASP A 122     3626   5223   3227     88   -180   1199       N  
ATOM    763  CA  ASP A 122      23.203   7.215  19.323  1.00 32.09           C  
ANISOU  763  CA  ASP A 122     3603   5470   3120    129   -203   1257       C  
ATOM    764  C   ASP A 122      22.099   7.219  20.382  1.00 38.33           C  
ANISOU  764  C   ASP A 122     4371   6377   3818     70   -166   1312       C  
ATOM    765  O   ASP A 122      22.273   6.621  21.442  1.00 38.12           O  
ANISOU  765  O   ASP A 122     4329   6451   3702    101   -159   1456       O  
ATOM    766  CB  ASP A 122      23.957   8.553  19.333  1.00 33.26           C  
ANISOU  766  CB  ASP A 122     3688   5747   3202    144   -254   1114       C  
ATOM    767  CG  ASP A 122      24.487   8.913  20.705  1.00 38.67           C  
ANISOU  767  CG  ASP A 122     4306   6663   3725    173   -284   1153       C  
ATOM    768  OD1 ASP A 122      25.446   8.248  21.167  1.00 38.79           O  
ANISOU  768  OD1 ASP A 122     4302   6735   3702    249   -310   1267       O  
ATOM    769  OD2 ASP A 122      23.940   9.845  21.321  1.00 41.01           O  
ANISOU  769  OD2 ASP A 122     4568   7088   3928    125   -281   1067       O  
ATOM    770  N   ARG A 123      20.970   7.882  20.076  1.00 36.31           N  
ANISOU  770  N   ARG A 123     4105   6114   3575     -7   -140   1206       N  
ATOM    771  CA  ARG A 123      19.800   7.984  20.939  1.00 36.80           C  
ANISOU  771  CA  ARG A 123     4134   6293   3553    -66    -97   1238       C  
ATOM    772  C   ARG A 123      19.115   6.615  21.090  1.00 42.63           C  
ANISOU  772  C   ARG A 123     4917   6938   4342   -111    -46   1408       C  
ATOM    773  O   ARG A 123      18.542   6.337  22.140  1.00 42.59           O  
ANISOU  773  O   ARG A 123     4883   7058   4241   -138    -11   1510       O  
ATOM    774  CB  ARG A 123      18.834   9.060  20.396  1.00 37.57           C  
ANISOU  774  CB  ARG A 123     4207   6402   3666   -118    -84   1073       C  
ATOM    775  CG  ARG A 123      17.939   9.710  21.451  1.00 52.11           C  
ANISOU  775  CG  ARG A 123     5987   8437   5375   -143    -52   1050       C  
ATOM    776  CD  ARG A 123      18.714  10.473  22.523  1.00 64.93           C  
ANISOU  776  CD  ARG A 123     7568  10253   6850    -91    -85   1010       C  
ATOM    777  NE  ARG A 123      19.003  11.855  22.140  1.00 72.33           N  
ANISOU  777  NE  ARG A 123     8495  11207   7781    -76   -117    818       N  
ATOM    778  CZ  ARG A 123      19.823  12.665  22.807  1.00 86.12           C  
ANISOU  778  CZ  ARG A 123    10216  13085   9422    -45   -158    741       C  
ATOM    779  NH1 ARG A 123      20.449  12.239  23.898  1.00 71.90           N  
ANISOU  779  NH1 ARG A 123     8385  11432   7501    -17   -175    840       N  
ATOM    780  NH2 ARG A 123      20.008  13.913  22.399  1.00 73.49           N  
ANISOU  780  NH2 ARG A 123     8620  11470   7832    -45   -181    567       N  
ATOM    781  N   TYR A 124      19.224   5.751  20.062  1.00 40.37           N  
ANISOU  781  N   TYR A 124     4705   6433   4202   -120    -40   1438       N  
ATOM    782  CA  TYR A 124      18.672   4.397  20.044  1.00 40.74           C  
ANISOU  782  CA  TYR A 124     4814   6341   4322   -173      7   1589       C  
ATOM    783  C   TYR A 124      19.427   3.490  21.019  1.00 45.78           C  
ANISOU  783  C   TYR A 124     5478   7009   4907   -103     10   1783       C  
ATOM    784  O   TYR A 124      18.797   2.828  21.842  1.00 45.27           O  
ANISOU  784  O   TYR A 124     5417   6987   4797   -151     53   1929       O  
ATOM    785  CB  TYR A 124      18.659   3.832  18.601  1.00 42.09           C  
ANISOU  785  CB  TYR A 124     5065   6267   4662   -199      8   1534       C  
ATOM    786  CG  TYR A 124      18.310   2.364  18.484  1.00 44.40           C  
ANISOU  786  CG  TYR A 124     5447   6375   5048   -249     51   1679       C  
ATOM    787  CD1 TYR A 124      16.987   1.935  18.531  1.00 46.58           C  
ANISOU  787  CD1 TYR A 124     5726   6624   5348   -383    100   1718       C  
ATOM    788  CD2 TYR A 124      19.299   1.408  18.271  1.00 45.44           C  
ANISOU  788  CD2 TYR A 124     5663   6351   5251   -164     45   1770       C  
ATOM    789  CE1 TYR A 124      16.660   0.584  18.419  1.00 47.63           C  
ANISOU  789  CE1 TYR A 124     5952   6572   5575   -449    141   1847       C  
ATOM    790  CE2 TYR A 124      18.984   0.055  18.152  1.00 46.54           C  
ANISOU  790  CE2 TYR A 124     5904   6292   5487   -209     88   1898       C  
ATOM    791  CZ  TYR A 124      17.663  -0.353  18.230  1.00 54.95           C  
ANISOU  791  CZ  TYR A 124     6979   7323   6578   -360    136   1936       C  
ATOM    792  OH  TYR A 124      17.355  -1.687  18.113  1.00 57.50           O  
ANISOU  792  OH  TYR A 124     7410   7435   7002   -423    180   2060       O  
ATOM    793  N   PHE A 125      20.766   3.477  20.944  1.00 43.12           N  
ANISOU  793  N   PHE A 125     5149   6663   4569     12    -35   1794       N  
ATOM    794  CA  PHE A 125      21.577   2.646  21.827  1.00 43.25           C  
ANISOU  794  CA  PHE A 125     5182   6718   4532    103    -40   1983       C  
ATOM    795  C   PHE A 125      21.636   3.173  23.262  1.00 48.72           C  
ANISOU  795  C   PHE A 125     5788   7690   5034    122    -51   2042       C  
ATOM    796  O   PHE A 125      21.760   2.364  24.182  1.00 48.98           O  
ANISOU  796  O   PHE A 125     5832   7773   5004    158    -33   2235       O  
ATOM    797  CB  PHE A 125      22.977   2.408  21.251  1.00 44.77           C  
ANISOU  797  CB  PHE A 125     5399   6828   4783    228    -82   1979       C  
ATOM    798  CG  PHE A 125      23.017   1.635  19.953  1.00 46.17           C  
ANISOU  798  CG  PHE A 125     5676   6729   5138    231    -63   1953       C  
ATOM    799  CD1 PHE A 125      22.584   0.315  19.896  1.00 49.03           C  
ANISOU  799  CD1 PHE A 125     6140   6894   5593    210    -13   2097       C  
ATOM    800  CD2 PHE A 125      23.542   2.208  18.800  1.00 48.04           C  
ANISOU  800  CD2 PHE A 125     5907   6899   5445    255    -94   1787       C  
ATOM    801  CE1 PHE A 125      22.627  -0.400  18.695  1.00 49.99           C  
ANISOU  801  CE1 PHE A 125     6363   6757   5876    210      5   2054       C  
ATOM    802  CE2 PHE A 125      23.584   1.493  17.601  1.00 50.88           C  
ANISOU  802  CE2 PHE A 125     6358   7018   5955    260    -75   1754       C  
ATOM    803  CZ  PHE A 125      23.129   0.193  17.557  1.00 48.95           C  
ANISOU  803  CZ  PHE A 125     6219   6580   5801    239    -27   1879       C  
ATOM    804  N   SER A 126      21.513   4.503  23.465  1.00 45.87           N  
ANISOU  804  N   SER A 126     5347   7506   4578     99    -78   1878       N  
ATOM    805  CA  SER A 126      21.533   5.096  24.807  1.00 46.29           C  
ANISOU  805  CA  SER A 126     5318   7833   4438    111    -90   1900       C  
ATOM    806  C   SER A 126      20.223   4.880  25.588  1.00 52.09           C  
ANISOU  806  C   SER A 126     6036   8656   5099     27    -26   1980       C  
ATOM    807  O   SER A 126      20.246   4.860  26.820  1.00 52.00           O  
ANISOU  807  O   SER A 126     5976   8852   4929     47    -21   2078       O  
ATOM    808  CB  SER A 126      21.923   6.571  24.758  1.00 49.66           C  
ANISOU  808  CB  SER A 126     5679   8397   4793    116   -138   1688       C  
ATOM    809  OG  SER A 126      20.936   7.369  24.128  1.00 58.61           O  
ANISOU  809  OG  SER A 126     6812   9480   5978     37   -113   1528       O  
ATOM    810  N   VAL A 127      19.094   4.706  24.876  1.00 49.78           N  
ANISOU  810  N   VAL A 127     5775   8225   4913    -69     22   1941       N  
ATOM    811  CA  VAL A 127      17.782   4.460  25.479  1.00 50.07           C  
ANISOU  811  CA  VAL A 127     5787   8341   4897   -163     88   2015       C  
ATOM    812  C   VAL A 127      17.561   2.944  25.664  1.00 55.35           C  
ANISOU  812  C   VAL A 127     6527   8874   5630   -197    134   2248       C  
ATOM    813  O   VAL A 127      17.108   2.529  26.737  1.00 55.55           O  
ANISOU  813  O   VAL A 127     6525   9035   5544   -223    175   2403       O  
ATOM    814  CB  VAL A 127      16.627   5.177  24.712  1.00 54.18           C  
ANISOU  814  CB  VAL A 127     6281   8828   5477   -251    114   1847       C  
ATOM    815  CG1 VAL A 127      15.249   4.752  25.223  1.00 54.00           C  
ANISOU  815  CG1 VAL A 127     6225   8876   5417   -356    188   1941       C  
ATOM    816  CG2 VAL A 127      16.773   6.696  24.797  1.00 53.95           C  
ANISOU  816  CG2 VAL A 127     6186   8952   5360   -211     79   1642       C  
ATOM    817  N   THR A 128      17.911   2.123  24.647  1.00 52.64           N  
ANISOU  817  N   THR A 128     6279   8263   5459   -193    130   2275       N  
ATOM    818  CA  THR A 128      17.758   0.660  24.714  1.00 53.21           C  
ANISOU  818  CA  THR A 128     6444   8157   5618   -224    174   2484       C  
ATOM    819  C   THR A 128      18.802  -0.011  25.604  1.00 59.23           C  
ANISOU  819  C   THR A 128     7229   8968   6307   -104    159   2681       C  
ATOM    820  O   THR A 128      18.458  -0.941  26.335  1.00 58.60           O  
ANISOU  820  O   THR A 128     7184   8881   6201   -133    206   2892       O  
ATOM    821  CB  THR A 128      17.712   0.008  23.324  1.00 61.53           C  
ANISOU  821  CB  THR A 128     7599   8903   6876   -262    179   2429       C  
ATOM    822  OG1 THR A 128      18.951   0.225  22.645  1.00 60.71           O  
ANISOU  822  OG1 THR A 128     7519   8723   6825   -139    121   2338       O  
ATOM    823  CG2 THR A 128      16.529   0.482  22.481  1.00 60.69           C  
ANISOU  823  CG2 THR A 128     7468   8756   6837   -396    200   2272       C  
ATOM    824  N   ARG A 129      20.074   0.447  25.534  1.00 57.69           N  
ANISOU  824  N   ARG A 129     7011   8831   6079     30     93   2620       N  
ATOM    825  CA  ARG A 129      21.190  -0.102  26.322  1.00 58.27           C  
ANISOU  825  CA  ARG A 129     7088   8979   6075    166     66   2795       C  
ATOM    826  C   ARG A 129      21.906   1.020  27.140  1.00 63.57           C  
ANISOU  826  C   ARG A 129     7638   9961   6555    237      5   2713       C  
ATOM    827  O   ARG A 129      23.063   1.334  26.843  1.00 62.80           O  
ANISOU  827  O   ARG A 129     7518   9884   6460    339    -56   2646       O  
ATOM    828  CB  ARG A 129      22.185  -0.842  25.395  1.00 58.82           C  
ANISOU  828  CB  ARG A 129     7246   8805   6297    271     44   2822       C  
ATOM    829  CG  ARG A 129      21.585  -2.020  24.622  1.00 69.28           C  
ANISOU  829  CG  ARG A 129     8706   9810   7808    206    103   2901       C  
ATOM    830  CD  ARG A 129      22.549  -2.607  23.606  1.00 80.76           C  
ANISOU  830  CD  ARG A 129    10246  11027   9412    315     83   2874       C  
ATOM    831  NE  ARG A 129      23.658  -3.334  24.233  1.00 93.51           N  
ANISOU  831  NE  ARG A 129    11885  12653  10993    484     67   3067       N  
ATOM    832  CZ  ARG A 129      23.649  -4.635  24.515  1.00109.75           C  
ANISOU  832  CZ  ARG A 129    14052  14528  13118    522    114   3286       C  
ATOM    833  NH1 ARG A 129      22.575  -5.372  24.252  1.00 98.54           N  
ANISOU  833  NH1 ARG A 129    12734  12900  11807    383    179   3336       N  
ATOM    834  NH2 ARG A 129      24.707  -5.205  25.077  1.00 95.70           N  
ANISOU  834  NH2 ARG A 129    12284  12779  11300    698     95   3459       N  
ATOM    835  N   PRO A 130      21.262   1.621  28.183  1.00 61.46           N  
ANISOU  835  N   PRO A 130     7291   9946   6116    184     20   2714       N  
ATOM    836  CA  PRO A 130      21.925   2.712  28.930  1.00 61.82           C  
ANISOU  836  CA  PRO A 130     7230  10278   5979    239    -39   2611       C  
ATOM    837  C   PRO A 130      23.124   2.329  29.812  1.00 67.54           C  
ANISOU  837  C   PRO A 130     7920  11164   6579    367    -87   2769       C  
ATOM    838  O   PRO A 130      23.743   3.227  30.387  1.00 67.59           O  
ANISOU  838  O   PRO A 130     7835  11414   6430    403   -142   2675       O  
ATOM    839  CB  PRO A 130      20.787   3.300  29.774  1.00 63.43           C  
ANISOU  839  CB  PRO A 130     7373  10685   6043    146      5   2573       C  
ATOM    840  CG  PRO A 130      19.848   2.175  29.964  1.00 67.66           C  
ANISOU  840  CG  PRO A 130     7964  11114   6628     77     83   2774       C  
ATOM    841  CD  PRO A 130      19.882   1.412  28.673  1.00 63.05           C  
ANISOU  841  CD  PRO A 130     7487  10191   6278     63     94   2785       C  
ATOM    842  N   LEU A 131      23.450   1.027  29.938  1.00 64.62           N  
ANISOU  842  N   LEU A 131     7620  10662   6270    437    -66   3006       N  
ATOM    843  CA  LEU A 131      24.573   0.581  30.762  1.00 64.45           C  
ANISOU  843  CA  LEU A 131     7562  10792   6132    577   -111   3182       C  
ATOM    844  C   LEU A 131      25.822   0.263  29.921  1.00 69.39           C  
ANISOU  844  C   LEU A 131     8216  11269   6879    704   -160   3175       C  
ATOM    845  O   LEU A 131      26.855   0.906  30.116  1.00 69.36           O  
ANISOU  845  O   LEU A 131     8123  11453   6779    783   -233   3105       O  
ATOM    846  CB  LEU A 131      24.162  -0.606  31.661  1.00 64.28           C  
ANISOU  846  CB  LEU A 131     7590  10773   6062    590    -53   3481       C  
ATOM    847  CG  LEU A 131      25.107  -1.006  32.806  1.00 68.51           C  
ANISOU  847  CG  LEU A 131     8070  11538   6423    728    -93   3693       C  
ATOM    848  CD1 LEU A 131      24.990  -0.053  33.989  1.00 68.56           C  
ANISOU  848  CD1 LEU A 131     7947  11932   6169    697   -122   3634       C  
ATOM    849  CD2 LEU A 131      24.801  -2.406  33.283  1.00 70.08           C  
ANISOU  849  CD2 LEU A 131     8360  11611   6654    759    -30   4008       C  
ATOM    850  N   SER A 132      25.721  -0.705  28.986  1.00 66.28           N  
ANISOU  850  N   SER A 132     7943  10550   6692    718   -119   3238       N  
ATOM    851  CA  SER A 132      26.832  -1.144  28.135  1.00 66.50           C  
ANISOU  851  CA  SER A 132     8008  10412   6845    849   -150   3240       C  
ATOM    852  C   SER A 132      27.298  -0.097  27.121  1.00 71.28           C  
ANISOU  852  C   SER A 132     8566  11010   7509    833   -199   2972       C  
ATOM    853  O   SER A 132      28.504   0.046  26.912  1.00 71.14           O  
ANISOU  853  O   SER A 132     8496  11053   7480    951   -254   2951       O  
ATOM    854  CB  SER A 132      26.485  -2.449  27.426  1.00 70.26           C  
ANISOU  854  CB  SER A 132     8640  10535   7522    857    -85   3364       C  
ATOM    855  OG  SER A 132      25.404  -2.277  26.525  1.00 79.86           O  
ANISOU  855  OG  SER A 132     9917  11562   8865    700    -40   3215       O  
ATOM    856  N   TYR A 133      26.353   0.614  26.480  1.00 68.07           N  
ANISOU  856  N   TYR A 133     8171  10531   7160    690   -176   2777       N  
ATOM    857  CA  TYR A 133      26.662   1.632  25.476  1.00 67.93           C  
ANISOU  857  CA  TYR A 133     8118  10489   7202    660   -214   2531       C  
ATOM    858  C   TYR A 133      27.239   2.916  26.079  1.00 73.08           C  
ANISOU  858  C   TYR A 133     8643  11438   7688    659   -281   2400       C  
ATOM    859  O   TYR A 133      28.089   3.538  25.445  1.00 72.66           O  
ANISOU  859  O   TYR A 133     8546  11400   7661    691   -329   2266       O  
ATOM    860  CB  TYR A 133      25.442   1.920  24.581  1.00 68.60           C  
ANISOU  860  CB  TYR A 133     8262  10396   7407    519   -168   2384       C  
ATOM    861  CG  TYR A 133      25.717   2.857  23.423  1.00 69.58           C  
ANISOU  861  CG  TYR A 133     8367  10460   7609    494   -200   2152       C  
ATOM    862  CD1 TYR A 133      26.410   2.423  22.297  1.00 71.41           C  
ANISOU  862  CD1 TYR A 133     8649  10501   7981    562   -207   2122       C  
ATOM    863  CD2 TYR A 133      25.250   4.168  23.436  1.00 70.17           C  
ANISOU  863  CD2 TYR A 133     8380  10663   7619    405   -217   1966       C  
ATOM    864  CE1 TYR A 133      26.649   3.277  21.220  1.00 72.03           C  
ANISOU  864  CE1 TYR A 133     8710  10535   8125    535   -232   1921       C  
ATOM    865  CE2 TYR A 133      25.475   5.028  22.363  1.00 70.95           C  
ANISOU  865  CE2 TYR A 133     8469  10697   7792    380   -242   1769       C  
ATOM    866  CZ  TYR A 133      26.180   4.581  21.259  1.00 77.95           C  
ANISOU  866  CZ  TYR A 133     9399  11408   8809    440   -250   1752       C  
ATOM    867  OH  TYR A 133      26.404   5.435  20.205  1.00 78.37           O  
ANISOU  867  OH  TYR A 133     9440  11411   8927    413   -273   1570       O  
ATOM    868  N   ARG A 134      26.815   3.295  27.304  1.00 70.69           N  
ANISOU  868  N   ARG A 134     8279  11370   7208    617   -282   2438       N  
ATOM    869  CA  ARG A 134      27.301   4.508  27.979  1.00 70.90           C  
ANISOU  869  CA  ARG A 134     8192  11683   7063    602   -343   2305       C  
ATOM    870  C   ARG A 134      28.777   4.420  28.433  1.00 73.87           C  
ANISOU  870  C   ARG A 134     8486  12238   7343    725   -416   2376       C  
ATOM    871  O   ARG A 134      29.356   5.434  28.832  1.00 73.76           O  
ANISOU  871  O   ARG A 134     8378  12438   7209    705   -478   2239       O  
ATOM    872  CB  ARG A 134      26.378   4.917  29.133  1.00 73.10           C  
ANISOU  872  CB  ARG A 134     8434  12165   7174    528   -317   2315       C  
ATOM    873  CG  ARG A 134      25.125   5.636  28.646  1.00 88.88           C  
ANISOU  873  CG  ARG A 134    10463  14076   9232    402   -270   2144       C  
ATOM    874  CD  ARG A 134      24.527   6.514  29.728  1.00105.66           C  
ANISOU  874  CD  ARG A 134    12521  16461  11166    344   -265   2064       C  
ATOM    875  NE  ARG A 134      24.404   7.902  29.279  1.00119.01           N  
ANISOU  875  NE  ARG A 134    14186  18172  12860    283   -288   1798       N  
ATOM    876  CZ  ARG A 134      25.346   8.829  29.428  1.00135.85           C  
ANISOU  876  CZ  ARG A 134    16260  20443  14913    297   -358   1658       C  
ATOM    877  NH1 ARG A 134      26.488   8.535  30.037  1.00124.80           N  
ANISOU  877  NH1 ARG A 134    14803  19204  13410    372   -416   1755       N  
ATOM    878  NH2 ARG A 134      25.147  10.061  28.981  1.00123.05           N  
ANISOU  878  NH2 ARG A 134    14636  18805  13313    235   -369   1425       N  
ATOM    879  N   ALA A 135      29.384   3.224  28.336  1.00 69.04           N  
ANISOU  879  N   ALA A 135     7910  11534   6788    850   -410   2583       N  
ATOM    880  CA  ALA A 135      30.793   2.994  28.642  1.00 68.25           C  
ANISOU  880  CA  ALA A 135     7728  11589   6615    990   -476   2673       C  
ATOM    881  C   ALA A 135      31.611   3.278  27.381  1.00 70.21           C  
ANISOU  881  C   ALA A 135     7969  11704   7002   1026   -503   2536       C  
ATOM    882  O   ALA A 135      32.804   3.574  27.469  1.00 70.04           O  
ANISOU  882  O   ALA A 135     7846  11854   6913   1101   -569   2519       O  
ATOM    883  CB  ALA A 135      30.999   1.553  29.079  1.00 69.06           C  
ANISOU  883  CB  ALA A 135     7881  11628   6729   1125   -448   2964       C  
ATOM    884  N   LYS A 136      30.946   3.193  26.209  1.00 64.92           N  
ANISOU  884  N   LYS A 136     7401  10747   6519    965   -452   2439       N  
ATOM    885  CA  LYS A 136      31.497   3.403  24.869  1.00 63.71           C  
ANISOU  885  CA  LYS A 136     7262  10434   6512    984   -461   2305       C  
ATOM    886  C   LYS A 136      31.153   4.802  24.319  1.00 64.85           C  
ANISOU  886  C   LYS A 136     7376  10605   6661    844   -479   2047       C  
ATOM    887  O   LYS A 136      31.857   5.299  23.436  1.00 64.72           O  
ANISOU  887  O   LYS A 136     7326  10559   6706    851   -507   1923       O  
ATOM    888  CB  LYS A 136      30.949   2.323  23.921  1.00 66.36           C  
ANISOU  888  CB  LYS A 136     7738  10432   7043   1009   -392   2370       C  
ATOM    889  CG  LYS A 136      31.917   1.908  22.822  1.00 83.51           C  
ANISOU  889  CG  LYS A 136     9925  12462   9342   1119   -398   2345       C  
ATOM    890  CD  LYS A 136      31.218   1.122  21.709  1.00 95.06           C  
ANISOU  890  CD  LYS A 136    11534  13585  11000   1101   -330   2334       C  
ATOM    891  CE  LYS A 136      31.310  -0.378  21.878  1.00105.32           C  
ANISOU  891  CE  LYS A 136    12933  14714  12369   1224   -286   2554       C  
ATOM    892  NZ  LYS A 136      30.676  -1.098  20.743  1.00112.26           N  
ANISOU  892  NZ  LYS A 136    13958  15260  13437   1191   -224   2515       N  
ATOM    893  N   ARG A 137      30.072   5.422  24.837  1.00 58.72           N  
ANISOU  893  N   ARG A 137     6610   9881   5820    723   -458   1975       N  
ATOM    894  CA  ARG A 137      29.568   6.741  24.437  1.00 57.10           C  
ANISOU  894  CA  ARG A 137     6391   9690   5615    597   -465   1744       C  
ATOM    895  C   ARG A 137      30.428   7.879  25.037  1.00 58.54           C  
ANISOU  895  C   ARG A 137     6458  10137   5646    576   -538   1631       C  
ATOM    896  O   ARG A 137      30.054   8.489  26.042  1.00 58.51           O  
ANISOU  896  O   ARG A 137     6411  10327   5491    525   -551   1599       O  
ATOM    897  CB  ARG A 137      28.082   6.869  24.832  1.00 55.69           C  
ANISOU  897  CB  ARG A 137     6261   9480   5417    498   -410   1727       C  
ATOM    898  CG  ARG A 137      27.284   7.857  24.002  1.00 61.08           C  
ANISOU  898  CG  ARG A 137     6974  10054   6179    392   -391   1520       C  
ATOM    899  CD  ARG A 137      25.844   7.948  24.475  1.00 63.66           C  
ANISOU  899  CD  ARG A 137     7331  10384   6474    311   -336   1515       C  
ATOM    900  NE  ARG A 137      25.646   9.047  25.419  1.00 71.76           N  
ANISOU  900  NE  ARG A 137     8292  11636   7337    264   -355   1406       N  
ATOM    901  CZ  ARG A 137      25.267  10.275  25.076  1.00 85.85           C  
ANISOU  901  CZ  ARG A 137    10072  13423   9126    197   -360   1203       C  
ATOM    902  NH1 ARG A 137      25.036  10.575  23.804  1.00 67.10           N  
ANISOU  902  NH1 ARG A 137     7743  10848   6902    167   -348   1099       N  
ATOM    903  NH2 ARG A 137      25.116  11.212  26.002  1.00 77.38           N  
ANISOU  903  NH2 ARG A 137     8950  12549   7901    164   -374   1104       N  
ATOM    904  N   THR A 138      31.587   8.147  24.412  1.00 52.72           N  
ANISOU  904  N   THR A 138     5670   9413   4949    612   -584   1567       N  
ATOM    905  CA  THR A 138      32.542   9.185  24.826  1.00 51.51           C  
ANISOU  905  CA  THR A 138     5403   9495   4672    579   -657   1455       C  
ATOM    906  C   THR A 138      32.680  10.273  23.735  1.00 53.95           C  
ANISOU  906  C   THR A 138     5718   9705   5074    488   -667   1244       C  
ATOM    907  O   THR A 138      32.381   9.982  22.570  1.00 53.26           O  
ANISOU  907  O   THR A 138     5704   9383   5148    493   -625   1223       O  
ATOM    908  CB  THR A 138      33.927   8.554  25.126  1.00 56.17           C  
ANISOU  908  CB  THR A 138     5900  10238   5205    707   -709   1595       C  
ATOM    909  OG1 THR A 138      34.393   7.842  23.980  1.00 56.11           O  
ANISOU  909  OG1 THR A 138     5931  10032   5358    796   -684   1648       O  
ATOM    910  CG2 THR A 138      33.921   7.648  26.347  1.00 52.98           C  
ANISOU  910  CG2 THR A 138     5473   9985   4672    797   -712   1805       C  
ATOM    911  N   PRO A 139      33.179  11.505  24.051  1.00 49.24           N  
ANISOU  911  N   PRO A 139     5048   9278   4382    401   -721   1089       N  
ATOM    912  CA  PRO A 139      33.377  12.510  22.984  1.00 48.12           C  
ANISOU  912  CA  PRO A 139     4919   9029   4336    313   -727    908       C  
ATOM    913  C   PRO A 139      34.352  12.027  21.902  1.00 49.69           C  
ANISOU  913  C   PRO A 139     5089   9147   4645    382   -734    951       C  
ATOM    914  O   PRO A 139      34.174  12.360  20.732  1.00 49.17           O  
ANISOU  914  O   PRO A 139     5073   8902   4707    342   -708    860       O  
ATOM    915  CB  PRO A 139      33.941  13.728  23.732  1.00 49.85           C  
ANISOU  915  CB  PRO A 139     5058   9472   4412    215   -789    766       C  
ATOM    916  CG  PRO A 139      33.570  13.518  25.160  1.00 54.68           C  
ANISOU  916  CG  PRO A 139     5644  10278   4856    232   -800    835       C  
ATOM    917  CD  PRO A 139      33.603  12.037  25.364  1.00 50.45           C  
ANISOU  917  CD  PRO A 139     5109   9725   4335    371   -779   1068       C  
ATOM    918  N   ARG A 140      35.353  11.211  22.299  1.00 44.70           N  
ANISOU  918  N   ARG A 140     4374   8652   3957    496   -767   1097       N  
ATOM    919  CA  ARG A 140      36.385  10.620  21.439  1.00 43.88           C  
ANISOU  919  CA  ARG A 140     4225   8513   3935    594   -773   1161       C  
ATOM    920  C   ARG A 140      35.781   9.733  20.344  1.00 46.14           C  
ANISOU  920  C   ARG A 140     4629   8507   4396    661   -702   1212       C  
ATOM    921  O   ARG A 140      36.163   9.867  19.180  1.00 45.90           O  
ANISOU  921  O   ARG A 140     4604   8367   4471    662   -688   1147       O  
ATOM    922  CB  ARG A 140      37.389   9.819  22.289  1.00 44.51           C  
ANISOU  922  CB  ARG A 140     4198   8809   3904    728   -817   1331       C  
ATOM    923  CG  ARG A 140      38.768   9.677  21.658  1.00 55.57           C  
ANISOU  923  CG  ARG A 140     5492  10292   5330    807   -847   1354       C  
ATOM    924  CD  ARG A 140      39.635   8.656  22.380  1.00 70.00           C  
ANISOU  924  CD  ARG A 140     7229  12295   7072    980   -877   1554       C  
ATOM    925  NE  ARG A 140      40.004   9.077  23.735  1.00 82.05           N  
ANISOU  925  NE  ARG A 140     8644  14132   8399    944   -948   1574       N  
ATOM    926  CZ  ARG A 140      41.105   9.758  24.042  1.00 98.34           C  
ANISOU  926  CZ  ARG A 140    10550  16468  10348    901  -1023   1515       C  
ATOM    927  NH1 ARG A 140      41.961  10.113  23.091  1.00 85.36           N  
ANISOU  927  NH1 ARG A 140     8834  14826   8772    886  -1034   1439       N  
ATOM    928  NH2 ARG A 140      41.356  10.092  25.301  1.00 87.21           N  
ANISOU  928  NH2 ARG A 140     9046  15341   8748    864  -1088   1528       N  
ATOM    929  N   ARG A 141      34.842   8.837  20.712  1.00 41.14           N  
ANISOU  929  N   ARG A 141     4087   7756   3788    707   -655   1327       N  
ATOM    930  CA  ARG A 141      34.177   7.948  19.760  1.00 40.26           C  
ANISOU  930  CA  ARG A 141     4095   7366   3835    753   -589   1372       C  
ATOM    931  C   ARG A 141      33.184   8.723  18.883  1.00 41.72           C  
ANISOU  931  C   ARG A 141     4357   7384   4110    625   -556   1208       C  
ATOM    932  O   ARG A 141      32.985   8.356  17.727  1.00 40.98           O  
ANISOU  932  O   ARG A 141     4330   7093   4150    641   -519   1180       O  
ATOM    933  CB  ARG A 141      33.488   6.773  20.475  1.00 41.66           C  
ANISOU  933  CB  ARG A 141     4345   7475   4008    819   -551   1548       C  
ATOM    934  CG  ARG A 141      33.181   5.609  19.536  1.00 54.42           C  
ANISOU  934  CG  ARG A 141     6073   8818   5784    895   -491   1623       C  
ATOM    935  CD  ARG A 141      32.305   4.556  20.172  1.00 66.09           C  
ANISOU  935  CD  ARG A 141     7642  10194   7274    919   -445   1780       C  
ATOM    936  NE  ARG A 141      31.882   3.554  19.194  1.00 77.30           N  
ANISOU  936  NE  ARG A 141     9186  11328   8859    956   -385   1815       N  
ATOM    937  CZ  ARG A 141      30.732   3.591  18.527  1.00 95.91           C  
ANISOU  937  CZ  ARG A 141    11633  13498  11310    848   -342   1731       C  
ATOM    938  NH1 ARG A 141      29.874   4.586  18.722  1.00 85.08           N  
ANISOU  938  NH1 ARG A 141    10242  12193   9890    711   -346   1615       N  
ATOM    939  NH2 ARG A 141      30.433   2.637  17.655  1.00 85.02           N  
ANISOU  939  NH2 ARG A 141    10363  11869  10072    878   -293   1757       N  
ATOM    940  N   ALA A 142      32.574   9.794  19.432  1.00 36.60           N  
ANISOU  940  N   ALA A 142     3699   6823   3386    507   -570   1098       N  
ATOM    941  CA  ALA A 142      31.641  10.654  18.706  1.00 35.36           C  
ANISOU  941  CA  ALA A 142     3604   6534   3298    396   -543    946       C  
ATOM    942  C   ALA A 142      32.404  11.409  17.617  1.00 38.10           C  
ANISOU  942  C   ALA A 142     3920   6848   3707    363   -562    826       C  
ATOM    943  O   ALA A 142      31.952  11.429  16.472  1.00 37.77           O  
ANISOU  943  O   ALA A 142     3944   6625   3782    344   -527    771       O  
ATOM    944  CB  ALA A 142      30.969  11.633  19.657  1.00 35.93           C  
ANISOU  944  CB  ALA A 142     3663   6729   3259    302   -556    859       C  
ATOM    945  N   LEU A 143      33.591  11.972  17.964  1.00 33.54           N  
ANISOU  945  N   LEU A 143     3240   6458   3048    357   -618    796       N  
ATOM    946  CA  LEU A 143      34.465  12.695  17.034  1.00 32.95           C  
ANISOU  946  CA  LEU A 143     3117   6387   3016    317   -638    699       C  
ATOM    947  C   LEU A 143      34.931  11.795  15.883  1.00 36.22           C  
ANISOU  947  C   LEU A 143     3546   6673   3543    417   -607    763       C  
ATOM    948  O   LEU A 143      35.045  12.262  14.748  1.00 35.19           O  
ANISOU  948  O   LEU A 143     3432   6446   3493    377   -592    677       O  
ATOM    949  CB  LEU A 143      35.670  13.314  17.767  1.00 32.89           C  
ANISOU  949  CB  LEU A 143     2980   6630   2885    286   -705    674       C  
ATOM    950  CG  LEU A 143      35.394  14.552  18.637  1.00 37.35           C  
ANISOU  950  CG  LEU A 143     3532   7317   3345    156   -740    550       C  
ATOM    951  CD1 LEU A 143      36.546  14.823  19.567  1.00 36.90           C  
ANISOU  951  CD1 LEU A 143     3343   7535   3142    146   -809    565       C  
ATOM    952  CD2 LEU A 143      35.098  15.787  17.797  1.00 39.29           C  
ANISOU  952  CD2 LEU A 143     3821   7451   3657     30   -730    384       C  
ATOM    953  N   LEU A 144      35.141  10.498  16.174  1.00 33.15           N  
ANISOU  953  N   LEU A 144     3161   6276   3159    550   -594    914       N  
ATOM    954  CA  LEU A 144      35.541   9.471  15.210  1.00 33.31           C  
ANISOU  954  CA  LEU A 144     3210   6165   3282    668   -559    982       C  
ATOM    955  C   LEU A 144      34.409   9.180  14.216  1.00 37.06           C  
ANISOU  955  C   LEU A 144     3815   6383   3882    637   -501    935       C  
ATOM    956  O   LEU A 144      34.661   9.137  13.012  1.00 37.22           O  
ANISOU  956  O   LEU A 144     3855   6300   3989    655   -477    883       O  
ATOM    957  CB  LEU A 144      35.962   8.184  15.956  1.00 33.55           C  
ANISOU  957  CB  LEU A 144     3227   6242   3281    821   -559   1162       C  
ATOM    958  CG  LEU A 144      36.325   6.954  15.108  1.00 38.60           C  
ANISOU  958  CG  LEU A 144     3918   6720   4029    968   -514   1244       C  
ATOM    959  CD1 LEU A 144      37.639   7.154  14.354  1.00 38.54           C  
ANISOU  959  CD1 LEU A 144     3807   6809   4026   1038   -530   1216       C  
ATOM    960  CD2 LEU A 144      36.411   5.718  15.975  1.00 41.30           C  
ANISOU  960  CD2 LEU A 144     4288   7054   4350   1103   -503   1430       C  
ATOM    961  N   MET A 145      33.173   8.982  14.717  1.00 33.24           N  
ANISOU  961  N   MET A 145     3412   5816   3401    589   -477    954       N  
ATOM    962  CA  MET A 145      31.995   8.698  13.892  1.00 33.14           C  
ANISOU  962  CA  MET A 145     3511   5585   3495    546   -427    914       C  
ATOM    963  C   MET A 145      31.621   9.891  13.016  1.00 34.50           C  
ANISOU  963  C   MET A 145     3691   5717   3700    437   -428    757       C  
ATOM    964  O   MET A 145      31.155   9.694  11.895  1.00 33.09           O  
ANISOU  964  O   MET A 145     3576   5380   3616    426   -395    710       O  
ATOM    965  CB  MET A 145      30.800   8.235  14.744  1.00 36.19           C  
ANISOU  965  CB  MET A 145     3959   5929   3862    515   -403    984       C  
ATOM    966  CG  MET A 145      31.024   6.903  15.461  1.00 41.16           C  
ANISOU  966  CG  MET A 145     4610   6546   4482    623   -390   1160       C  
ATOM    967  SD  MET A 145      31.460   5.524  14.368  1.00 46.86           S  
ANISOU  967  SD  MET A 145     5414   7047   5343    742   -347   1223       S  
ATOM    968  CE  MET A 145      32.452   4.544  15.476  1.00 43.83           C  
ANISOU  968  CE  MET A 145     4990   6767   4894    902   -361   1421       C  
ATOM    969  N   ILE A 146      31.849  11.123  13.524  1.00 30.60           N  
ANISOU  969  N   ILE A 146     3135   5367   3126    358   -466    677       N  
ATOM    970  CA  ILE A 146      31.604  12.380  12.809  1.00 30.16           C  
ANISOU  970  CA  ILE A 146     3085   5280   3094    258   -469    537       C  
ATOM    971  C   ILE A 146      32.560  12.469  11.609  1.00 33.72           C  
ANISOU  971  C   ILE A 146     3506   5705   3602    282   -469    504       C  
ATOM    972  O   ILE A 146      32.112  12.710  10.487  1.00 33.91           O  
ANISOU  972  O   ILE A 146     3581   5602   3702    251   -442    441       O  
ATOM    973  CB  ILE A 146      31.691  13.605  13.776  1.00 32.87           C  
ANISOU  973  CB  ILE A 146     3379   5775   3334    172   -508    463       C  
ATOM    974  CG1 ILE A 146      30.380  13.744  14.583  1.00 32.97           C  
ANISOU  974  CG1 ILE A 146     3444   5771   3312    132   -490    452       C  
ATOM    975  CG2 ILE A 146      32.022  14.919  13.034  1.00 33.06           C  
ANISOU  975  CG2 ILE A 146     3389   5794   3379     83   -522    335       C  
ATOM    976  CD1 ILE A 146      30.512  14.438  15.904  1.00 37.69           C  
ANISOU  976  CD1 ILE A 146     3993   6547   3781     92   -524    425       C  
ATOM    977  N   GLY A 147      33.844  12.216  11.861  1.00 29.64           N  
ANISOU  977  N   GLY A 147     2900   5321   3040    343   -496    555       N  
ATOM    978  CA  GLY A 147      34.894  12.236  10.852  1.00 29.36           C  
ANISOU  978  CA  GLY A 147     2811   5303   3039    377   -494    537       C  
ATOM    979  C   GLY A 147      34.711  11.196   9.766  1.00 32.79           C  
ANISOU  979  C   GLY A 147     3311   5576   3571    468   -446    568       C  
ATOM    980  O   GLY A 147      34.955  11.485   8.591  1.00 31.81           O  
ANISOU  980  O   GLY A 147     3188   5403   3496    454   -428    507       O  
ATOM    981  N   LEU A 148      34.265   9.981  10.152  1.00 29.59           N  
ANISOU  981  N   LEU A 148     2966   5084   3192    555   -423    661       N  
ATOM    982  CA  LEU A 148      33.996   8.896   9.204  1.00 29.27           C  
ANISOU  982  CA  LEU A 148     3009   4867   3247    635   -375    683       C  
ATOM    983  C   LEU A 148      32.783   9.211   8.328  1.00 32.63           C  
ANISOU  983  C   LEU A 148     3525   5134   3739    543   -347    591       C  
ATOM    984  O   LEU A 148      32.827   8.937   7.130  1.00 32.47           O  
ANISOU  984  O   LEU A 148     3541   5016   3782    567   -319    545       O  
ATOM    985  CB  LEU A 148      33.859   7.528   9.898  1.00 29.38           C  
ANISOU  985  CB  LEU A 148     3072   4816   3275    743   -358    812       C  
ATOM    986  CG  LEU A 148      35.148   6.927  10.497  1.00 34.16           C  
ANISOU  986  CG  LEU A 148     3595   5551   3833    885   -375    922       C  
ATOM    987  CD1 LEU A 148      34.843   5.687  11.329  1.00 34.13           C  
ANISOU  987  CD1 LEU A 148     3649   5487   3832    974   -361   1065       C  
ATOM    988  CD2 LEU A 148      36.187   6.600   9.418  1.00 35.91           C  
ANISOU  988  CD2 LEU A 148     3791   5748   4105    993   -351    903       C  
ATOM    989  N   ALA A 149      31.734   9.851   8.903  1.00 28.71           N  
ANISOU  989  N   ALA A 149     3057   4633   3219    442   -357    561       N  
ATOM    990  CA  ALA A 149      30.527  10.270   8.168  1.00 28.14           C  
ANISOU  990  CA  ALA A 149     3054   4443   3197    355   -336    479       C  
ATOM    991  C   ALA A 149      30.862  11.304   7.081  1.00 31.56           C  
ANISOU  991  C   ALA A 149     3461   4890   3642    305   -341    379       C  
ATOM    992  O   ALA A 149      30.279  11.259   5.998  1.00 31.95           O  
ANISOU  992  O   ALA A 149     3561   4831   3746    284   -318    327       O  
ATOM    993  CB  ALA A 149      29.494  10.842   9.125  1.00 28.64           C  
ANISOU  993  CB  ALA A 149     3129   4537   3216    275   -346    471       C  
ATOM    994  N   TRP A 150      31.809  12.216   7.367  1.00 27.35           N  
ANISOU  994  N   TRP A 150     2845   4495   3053    281   -372    358       N  
ATOM    995  CA  TRP A 150      32.267  13.246   6.435  1.00 27.10           C  
ANISOU  995  CA  TRP A 150     2782   4488   3027    225   -376    282       C  
ATOM    996  C   TRP A 150      33.146  12.654   5.337  1.00 30.53           C  
ANISOU  996  C   TRP A 150     3193   4911   3495    299   -354    290       C  
ATOM    997  O   TRP A 150      33.007  13.033   4.177  1.00 29.55           O  
ANISOU  997  O   TRP A 150     3090   4735   3404    269   -335    234       O  
ATOM    998  CB  TRP A 150      33.006  14.361   7.181  1.00 25.91           C  
ANISOU  998  CB  TRP A 150     2553   4486   2806    158   -416    257       C  
ATOM    999  CG  TRP A 150      32.080  15.385   7.766  1.00 26.88           C  
ANISOU  999  CG  TRP A 150     2714   4594   2907     63   -429    197       C  
ATOM   1000  CD1 TRP A 150      31.608  15.433   9.044  1.00 29.61           C  
ANISOU 1000  CD1 TRP A 150     3063   4991   3197     49   -446    210       C  
ATOM   1001  CD2 TRP A 150      31.486  16.490   7.074  1.00 26.68           C  
ANISOU 1001  CD2 TRP A 150     2730   4498   2910    -17   -420    116       C  
ATOM   1002  NE1 TRP A 150      30.751  16.497   9.193  1.00 29.12           N  
ANISOU 1002  NE1 TRP A 150     3041   4892   3129    -31   -446    132       N  
ATOM   1003  CE2 TRP A 150      30.664  17.171   8.002  1.00 30.61           C  
ANISOU 1003  CE2 TRP A 150     3257   5000   3373    -69   -431     77       C  
ATOM   1004  CE3 TRP A 150      31.569  16.976   5.756  1.00 27.90           C  
ANISOU 1004  CE3 TRP A 150     2900   4590   3112    -43   -402     78       C  
ATOM   1005  CZ2 TRP A 150      29.933  18.315   7.657  1.00 29.85           C  
ANISOU 1005  CZ2 TRP A 150     3209   4836   3297   -135   -424      2       C  
ATOM   1006  CZ3 TRP A 150      30.840  18.104   5.413  1.00 29.39           C  
ANISOU 1006  CZ3 TRP A 150     3137   4714   3318   -115   -398     16       C  
ATOM   1007  CH2 TRP A 150      30.033  18.760   6.355  1.00 30.09           C  
ANISOU 1007  CH2 TRP A 150     3258   4796   3380   -155   -409    -22       C  
ATOM   1008  N   LEU A 151      34.020  11.703   5.703  1.00 27.80           N  
ANISOU 1008  N   LEU A 151     2806   4619   3137    407   -353    364       N  
ATOM   1009  CA  LEU A 151      34.928  11.022   4.785  1.00 27.96           C  
ANISOU 1009  CA  LEU A 151     2799   4642   3183    506   -326    376       C  
ATOM   1010  C   LEU A 151      34.196  10.088   3.824  1.00 30.34           C  
ANISOU 1010  C   LEU A 151     3204   4766   3559    553   -282    354       C  
ATOM   1011  O   LEU A 151      34.500  10.101   2.631  1.00 29.93           O  
ANISOU 1011  O   LEU A 151     3151   4694   3528    569   -257    303       O  
ATOM   1012  CB  LEU A 151      36.038  10.292   5.559  1.00 28.51           C  
ANISOU 1012  CB  LEU A 151     2791   4827   3215    624   -339    468       C  
ATOM   1013  CG  LEU A 151      37.386  10.147   4.842  1.00 34.57           C  
ANISOU 1013  CG  LEU A 151     3466   5698   3972    709   -325    474       C  
ATOM   1014  CD1 LEU A 151      37.959  11.509   4.433  1.00 35.14           C  
ANISOU 1014  CD1 LEU A 151     3442   5913   3999    596   -348    418       C  
ATOM   1015  CD2 LEU A 151      38.386   9.429   5.724  1.00 38.04           C  
ANISOU 1015  CD2 LEU A 151     3831   6247   4375    847   -338    578       C  
ATOM   1016  N   VAL A 152      33.210   9.316   4.327  1.00 26.25           N  
ANISOU 1016  N   VAL A 152     2772   4128   3074    562   -273    387       N  
ATOM   1017  CA  VAL A 152      32.384   8.403   3.519  1.00 25.54           C  
ANISOU 1017  CA  VAL A 152     2788   3861   3054    580   -235    359       C  
ATOM   1018  C   VAL A 152      31.603   9.218   2.475  1.00 28.26           C  
ANISOU 1018  C   VAL A 152     3161   4165   3412    478   -231    261       C  
ATOM   1019  O   VAL A 152      31.578   8.829   1.310  1.00 28.37           O  
ANISOU 1019  O   VAL A 152     3211   4110   3457    502   -204    208       O  
ATOM   1020  CB  VAL A 152      31.477   7.473   4.393  1.00 29.53           C  
ANISOU 1020  CB  VAL A 152     3373   4258   3589    585   -228    426       C  
ATOM   1021  CG1 VAL A 152      30.425   6.740   3.556  1.00 29.43           C  
ANISOU 1021  CG1 VAL A 152     3469   4066   3647    554   -195    377       C  
ATOM   1022  CG2 VAL A 152      32.317   6.467   5.180  1.00 29.14           C  
ANISOU 1022  CG2 VAL A 152     3312   4225   3536    715   -223    535       C  
ATOM   1023  N   SER A 153      31.035  10.374   2.882  1.00 23.42           N  
ANISOU 1023  N   SER A 153     2526   3605   2767    374   -258    237       N  
ATOM   1024  CA  SER A 153      30.280  11.284   2.008  1.00 22.92           C  
ANISOU 1024  CA  SER A 153     2482   3515   2709    286   -258    161       C  
ATOM   1025  C   SER A 153      31.140  11.818   0.864  1.00 26.44           C  
ANISOU 1025  C   SER A 153     2885   4016   3144    294   -249    119       C  
ATOM   1026  O   SER A 153      30.649  11.954  -0.257  1.00 25.63           O  
ANISOU 1026  O   SER A 153     2817   3865   3058    269   -234     65       O  
ATOM   1027  CB  SER A 153      29.712  12.453   2.812  1.00 25.48           C  
ANISOU 1027  CB  SER A 153     2788   3894   3000    198   -286    151       C  
ATOM   1028  OG  SER A 153      28.784  12.009   3.787  1.00 31.06           O  
ANISOU 1028  OG  SER A 153     3532   4562   3709    184   -288    185       O  
ATOM   1029  N   PHE A 154      32.425  12.107   1.158  1.00 23.28           N  
ANISOU 1029  N   PHE A 154     2402   3735   2709    328   -258    149       N  
ATOM   1030  CA  PHE A 154      33.417  12.619   0.212  1.00 23.00           C  
ANISOU 1030  CA  PHE A 154     2303   3782   2653    333   -247    125       C  
ATOM   1031  C   PHE A 154      33.791  11.554  -0.824  1.00 28.03           C  
ANISOU 1031  C   PHE A 154     2960   4377   3313    434   -206    110       C  
ATOM   1032  O   PHE A 154      33.766  11.838  -2.013  1.00 27.58           O  
ANISOU 1032  O   PHE A 154     2908   4318   3252    417   -185     62       O  
ATOM   1033  CB  PHE A 154      34.671  13.136   0.964  1.00 24.51           C  
ANISOU 1033  CB  PHE A 154     2386   4130   2795    330   -271    165       C  
ATOM   1034  CG  PHE A 154      35.694  13.806   0.075  1.00 25.58           C  
ANISOU 1034  CG  PHE A 154     2443   4371   2905    308   -259    148       C  
ATOM   1035  CD1 PHE A 154      35.521  15.120  -0.348  1.00 28.40           C  
ANISOU 1035  CD1 PHE A 154     2795   4743   3251    188   -268    113       C  
ATOM   1036  CD2 PHE A 154      36.813  13.113  -0.370  1.00 27.11           C  
ANISOU 1036  CD2 PHE A 154     2569   4647   3085    410   -235    171       C  
ATOM   1037  CE1 PHE A 154      36.456  15.734  -1.182  1.00 28.89           C  
ANISOU 1037  CE1 PHE A 154     2785   4901   3288    155   -252    109       C  
ATOM   1038  CE2 PHE A 154      37.734  13.720  -1.229  1.00 29.65           C  
ANISOU 1038  CE2 PHE A 154     2809   5081   3377    384   -217    160       C  
ATOM   1039  CZ  PHE A 154      37.559  15.032  -1.613  1.00 27.75           C  
ANISOU 1039  CZ  PHE A 154     2563   4856   3124    248   -227    133       C  
ATOM   1040  N   VAL A 155      34.132  10.338  -0.367  1.00 25.71           N  
ANISOU 1040  N   VAL A 155     2682   4048   3040    544   -193    153       N  
ATOM   1041  CA  VAL A 155      34.530   9.203  -1.202  1.00 26.04           C  
ANISOU 1041  CA  VAL A 155     2755   4032   3108    661   -151    134       C  
ATOM   1042  C   VAL A 155      33.357   8.688  -2.066  1.00 31.84           C  
ANISOU 1042  C   VAL A 155     3603   4611   3884    631   -129     64       C  
ATOM   1043  O   VAL A 155      33.593   8.188  -3.168  1.00 31.70           O  
ANISOU 1043  O   VAL A 155     3609   4564   3872    686    -94      8       O  
ATOM   1044  CB  VAL A 155      35.193   8.091  -0.338  1.00 29.92           C  
ANISOU 1044  CB  VAL A 155     3238   4517   3613    795   -143    211       C  
ATOM   1045  CG1 VAL A 155      35.551   6.861  -1.168  1.00 29.75           C  
ANISOU 1045  CG1 VAL A 155     3267   4409   3627    930    -93    184       C  
ATOM   1046  CG2 VAL A 155      36.436   8.623   0.376  1.00 29.68           C  
ANISOU 1046  CG2 VAL A 155     3074   4678   3525    824   -169    274       C  
ATOM   1047  N   LEU A 156      32.104   8.829  -1.585  1.00 29.46           N  
ANISOU 1047  N   LEU A 156     3363   4227   3605    540   -150     62       N  
ATOM   1048  CA  LEU A 156      30.925   8.383  -2.329  1.00 29.57           C  
ANISOU 1048  CA  LEU A 156     3468   4114   3652    493   -138     -3       C  
ATOM   1049  C   LEU A 156      30.612   9.262  -3.527  1.00 32.63           C  
ANISOU 1049  C   LEU A 156     3842   4547   4009    426   -138    -73       C  
ATOM   1050  O   LEU A 156      30.305   8.733  -4.593  1.00 32.78           O  
ANISOU 1050  O   LEU A 156     3909   4510   4034    437   -116   -141       O  
ATOM   1051  CB  LEU A 156      29.670   8.289  -1.430  1.00 29.88           C  
ANISOU 1051  CB  LEU A 156     3558   4078   3717    415   -159     24       C  
ATOM   1052  CG  LEU A 156      29.513   7.059  -0.520  1.00 35.03           C  
ANISOU 1052  CG  LEU A 156     4270   4625   4414    465   -147     85       C  
ATOM   1053  CD1 LEU A 156      28.302   7.223   0.401  1.00 34.85           C  
ANISOU 1053  CD1 LEU A 156     4271   4573   4398    371   -167    120       C  
ATOM   1054  CD2 LEU A 156      29.389   5.764  -1.325  1.00 37.82           C  
ANISOU 1054  CD2 LEU A 156     4717   4833   4820    514   -110     36       C  
ATOM   1055  N   TRP A 157      30.668  10.596  -3.349  1.00 28.30           N  
ANISOU 1055  N   TRP A 157     3233   4095   3425    355   -163    -57       N  
ATOM   1056  CA  TRP A 157      30.297  11.573  -4.370  1.00 27.73           C  
ANISOU 1056  CA  TRP A 157     3150   4062   3323    288   -166   -100       C  
ATOM   1057  C   TRP A 157      31.440  12.203  -5.169  1.00 29.30           C  
ANISOU 1057  C   TRP A 157     3280   4375   3479    307   -150   -101       C  
ATOM   1058  O   TRP A 157      31.392  12.147  -6.395  1.00 28.80           O  
ANISOU 1058  O   TRP A 157     3228   4322   3393    316   -128   -148       O  
ATOM   1059  CB  TRP A 157      29.441  12.687  -3.749  1.00 26.91           C  
ANISOU 1059  CB  TRP A 157     3044   3966   3215    195   -199    -82       C  
ATOM   1060  CG  TRP A 157      28.058  12.248  -3.384  1.00 28.33           C  
ANISOU 1060  CG  TRP A 157     3284   4056   3424    158   -210    -95       C  
ATOM   1061  CD1 TRP A 157      27.585  11.993  -2.133  1.00 31.43           C  
ANISOU 1061  CD1 TRP A 157     3690   4416   3836    145   -223    -56       C  
ATOM   1062  CD2 TRP A 157      26.968  12.004  -4.285  1.00 28.20           C  
ANISOU 1062  CD2 TRP A 157     3313   3990   3412    123   -208   -147       C  
ATOM   1063  NE1 TRP A 157      26.263  11.614  -2.194  1.00 31.15           N  
ANISOU 1063  NE1 TRP A 157     3702   4312   3821    100   -225    -78       N  
ATOM   1064  CE2 TRP A 157      25.861  11.603  -3.505  1.00 32.31           C  
ANISOU 1064  CE2 TRP A 157     3867   4448   3960     84   -219   -137       C  
ATOM   1065  CE3 TRP A 157      26.819  12.079  -5.683  1.00 29.30           C  
ANISOU 1065  CE3 TRP A 157     3461   4147   3526    118   -198   -201       C  
ATOM   1066  CZ2 TRP A 157      24.620  11.282  -4.071  1.00 31.52           C  
ANISOU 1066  CZ2 TRP A 157     3802   4306   3867     33   -224   -180       C  
ATOM   1067  CZ3 TRP A 157      25.589  11.764  -6.241  1.00 30.64           C  
ANISOU 1067  CZ3 TRP A 157     3668   4276   3696     73   -207   -247       C  
ATOM   1068  CH2 TRP A 157      24.505  11.379  -5.440  1.00 31.32           C  
ANISOU 1068  CH2 TRP A 157     3780   4304   3815     28   -221   -238       C  
ATOM   1069  N   ALA A 158      32.409  12.861  -4.501  1.00 24.95           N  
ANISOU 1069  N   ALA A 158     2652   3920   2909    301   -161    -52       N  
ATOM   1070  CA  ALA A 158      33.498  13.603  -5.156  1.00 24.59           C  
ANISOU 1070  CA  ALA A 158     2526   3997   2820    292   -146    -42       C  
ATOM   1071  C   ALA A 158      34.256  12.827  -6.277  1.00 28.12           C  
ANISOU 1071  C   ALA A 158     2952   4487   3244    385   -101    -72       C  
ATOM   1072  O   ALA A 158      34.356  13.402  -7.362  1.00 27.28           O  
ANISOU 1072  O   ALA A 158     2829   4437   3101    353    -82    -91       O  
ATOM   1073  CB  ALA A 158      34.474  14.168  -4.132  1.00 25.15           C  
ANISOU 1073  CB  ALA A 158     2513   4167   2876    272   -167     11       C  
ATOM   1074  N   PRO A 159      34.730  11.555  -6.117  1.00 23.82           N  
ANISOU 1074  N   PRO A 159     2417   3916   2718    504    -78    -78       N  
ATOM   1075  CA  PRO A 159      35.423  10.898  -7.242  1.00 23.14           C  
ANISOU 1075  CA  PRO A 159     2314   3872   2604    599    -29   -120       C  
ATOM   1076  C   PRO A 159      34.566  10.727  -8.496  1.00 27.35           C  
ANISOU 1076  C   PRO A 159     2922   4345   3124    577    -11   -200       C  
ATOM   1077  O   PRO A 159      35.040  11.057  -9.586  1.00 26.75           O  
ANISOU 1077  O   PRO A 159     2807   4365   2994    586     19   -225       O  
ATOM   1078  CB  PRO A 159      35.886   9.561  -6.650  1.00 24.75           C  
ANISOU 1078  CB  PRO A 159     2538   4022   2846    736    -12   -108       C  
ATOM   1079  CG  PRO A 159      35.905   9.783  -5.156  1.00 28.85           C  
ANISOU 1079  CG  PRO A 159     3033   4541   3388    708    -54    -32       C  
ATOM   1080  CD  PRO A 159      34.734  10.683  -4.922  1.00 24.71           C  
ANISOU 1080  CD  PRO A 159     2553   3963   2871    567    -91    -40       C  
ATOM   1081  N   ALA A 160      33.301  10.266  -8.337  1.00 24.13           N  
ANISOU 1081  N   ALA A 160     2613   3798   2757    539    -31   -235       N  
ATOM   1082  CA  ALA A 160      32.345  10.044  -9.432  1.00 24.15           C  
ANISOU 1082  CA  ALA A 160     2685   3748   2743    505    -24   -315       C  
ATOM   1083  C   ALA A 160      32.004  11.326 -10.189  1.00 28.60           C  
ANISOU 1083  C   ALA A 160     3215   4400   3253    413    -38   -307       C  
ATOM   1084  O   ALA A 160      31.956  11.308 -11.419  1.00 28.38           O  
ANISOU 1084  O   ALA A 160     3193   4420   3172    419    -17   -360       O  
ATOM   1085  CB  ALA A 160      31.076   9.396  -8.903  1.00 24.95           C  
ANISOU 1085  CB  ALA A 160     2879   3701   2901    465    -48   -340       C  
ATOM   1086  N   ILE A 161      31.779  12.434  -9.455  1.00 24.64           N  
ANISOU 1086  N   ILE A 161     2681   3920   2761    333    -71   -240       N  
ATOM   1087  CA  ILE A 161      31.455  13.749 -10.018  1.00 23.84           C  
ANISOU 1087  CA  ILE A 161     2558   3880   2621    249    -84   -214       C  
ATOM   1088  C   ILE A 161      32.616  14.295 -10.875  1.00 28.12           C  
ANISOU 1088  C   ILE A 161     3025   4557   3103    261    -50   -191       C  
ATOM   1089  O   ILE A 161      32.387  14.771 -11.987  1.00 28.12           O  
ANISOU 1089  O   ILE A 161     3026   4609   3048    237    -38   -202       O  
ATOM   1090  CB  ILE A 161      31.008  14.746  -8.893  1.00 25.91           C  
ANISOU 1090  CB  ILE A 161     2816   4110   2918    173   -123   -157       C  
ATOM   1091  CG1 ILE A 161      29.668  14.301  -8.264  1.00 26.02           C  
ANISOU 1091  CG1 ILE A 161     2898   4013   2975    153   -151   -179       C  
ATOM   1092  CG2 ILE A 161      30.914  16.194  -9.405  1.00 24.92           C  
ANISOU 1092  CG2 ILE A 161     2670   4036   2761     97   -129   -116       C  
ATOM   1093  CD1 ILE A 161      29.332  14.882  -6.841  1.00 28.88           C  
ANISOU 1093  CD1 ILE A 161     3258   4340   3375    109   -182   -135       C  
ATOM   1094  N   LEU A 162      33.845  14.225 -10.358  1.00 24.73           N  
ANISOU 1094  N   LEU A 162     2524   4197   2675    298    -34   -155       N  
ATOM   1095  CA  LEU A 162      35.020  14.770 -11.038  1.00 24.57           C  
ANISOU 1095  CA  LEU A 162     2415   4324   2598    298      0   -123       C  
ATOM   1096  C   LEU A 162      35.572  13.921 -12.185  1.00 29.45           C  
ANISOU 1096  C   LEU A 162     3015   5013   3162    396     52   -178       C  
ATOM   1097  O   LEU A 162      36.122  14.488 -13.131  1.00 28.69           O  
ANISOU 1097  O   LEU A 162     2863   5038   2999    378     84   -160       O  
ATOM   1098  CB  LEU A 162      36.173  15.060 -10.037  1.00 24.26           C  
ANISOU 1098  CB  LEU A 162     2284   4363   2572    292     -5    -64       C  
ATOM   1099  CG  LEU A 162      35.923  15.838  -8.726  1.00 28.04           C  
ANISOU 1099  CG  LEU A 162     2767   4792   3096    207    -54    -21       C  
ATOM   1100  CD1 LEU A 162      37.241  16.113  -8.017  1.00 28.26           C  
ANISOU 1100  CD1 LEU A 162     2686   4939   3114    202    -56     25       C  
ATOM   1101  CD2 LEU A 162      35.208  17.145  -8.955  1.00 30.17           C  
ANISOU 1101  CD2 LEU A 162     3071   5028   3365     88    -73      3       C  
ATOM   1102  N   PHE A 163      35.493  12.577 -12.079  1.00 26.98           N  
ANISOU 1102  N   PHE A 163     2750   4625   2875    501     66   -242       N  
ATOM   1103  CA  PHE A 163      36.150  11.693 -13.037  1.00 27.12           C  
ANISOU 1103  CA  PHE A 163     2754   4703   2845    614    121   -306       C  
ATOM   1104  C   PHE A 163      35.263  10.865 -13.971  1.00 33.79           C  
ANISOU 1104  C   PHE A 163     3699   5467   3673    644    133   -414       C  
ATOM   1105  O   PHE A 163      35.824  10.109 -14.777  1.00 32.87           O  
ANISOU 1105  O   PHE A 163     3580   5397   3515    744    183   -482       O  
ATOM   1106  CB  PHE A 163      37.119  10.761 -12.296  1.00 28.00           C  
ANISOU 1106  CB  PHE A 163     2830   4818   2993    739    143   -298       C  
ATOM   1107  CG  PHE A 163      38.374  11.496 -11.909  1.00 28.97           C  
ANISOU 1107  CG  PHE A 163     2815   5105   3088    733    151   -214       C  
ATOM   1108  CD1 PHE A 163      39.416  11.652 -12.819  1.00 31.31           C  
ANISOU 1108  CD1 PHE A 163     3013   5573   3308    781    205   -214       C  
ATOM   1109  CD2 PHE A 163      38.506  12.064 -10.645  1.00 30.32           C  
ANISOU 1109  CD2 PHE A 163     2948   5274   3300    668    106   -139       C  
ATOM   1110  CE1 PHE A 163      40.560  12.371 -12.476  1.00 31.75           C  
ANISOU 1110  CE1 PHE A 163     2930   5796   3336    755    211   -134       C  
ATOM   1111  CE2 PHE A 163      39.655  12.773 -10.301  1.00 32.60           C  
ANISOU 1111  CE2 PHE A 163     3104   5725   3558    641    108    -69       C  
ATOM   1112  CZ  PHE A 163      40.675  12.919 -11.217  1.00 30.69           C  
ANISOU 1112  CZ  PHE A 163     2761   5653   3248    680    160    -65       C  
ATOM   1113  N   TRP A 164      33.922  11.017 -13.918  1.00 32.90           N  
ANISOU 1113  N   TRP A 164     3666   5250   3584    558     91   -435       N  
ATOM   1114  CA  TRP A 164      33.045  10.262 -14.826  1.00 33.77           C  
ANISOU 1114  CA  TRP A 164     3861   5301   3669    566     95   -543       C  
ATOM   1115  C   TRP A 164      33.326  10.598 -16.292  1.00 35.02           C  
ANISOU 1115  C   TRP A 164     3984   5606   3717    573    129   -581       C  
ATOM   1116  O   TRP A 164      33.406   9.688 -17.119  1.00 33.84           O  
ANISOU 1116  O   TRP A 164     3873   5458   3526    642    163   -687       O  
ATOM   1117  CB  TRP A 164      31.557  10.440 -14.497  1.00 33.72           C  
ANISOU 1117  CB  TRP A 164     3924   5189   3701    466     41   -550       C  
ATOM   1118  CG  TRP A 164      30.678   9.618 -15.387  1.00 35.85           C  
ANISOU 1118  CG  TRP A 164     4271   5409   3942    459     40   -667       C  
ATOM   1119  CD1 TRP A 164      29.944  10.059 -16.450  1.00 38.84           C  
ANISOU 1119  CD1 TRP A 164     4652   5863   4242    400     24   -703       C  
ATOM   1120  CD2 TRP A 164      30.537   8.192 -15.364  1.00 36.31           C  
ANISOU 1120  CD2 TRP A 164     4414   5341   4042    516     58   -768       C  
ATOM   1121  NE1 TRP A 164      29.320   9.000 -17.065  1.00 38.60           N  
ANISOU 1121  NE1 TRP A 164     4698   5773   4197    404     26   -830       N  
ATOM   1122  CE2 TRP A 164      29.671   7.840 -16.424  1.00 40.40           C  
ANISOU 1122  CE2 TRP A 164     4984   5864   4503    471     49   -876       C  
ATOM   1123  CE3 TRP A 164      31.043   7.175 -14.535  1.00 38.08           C  
ANISOU 1123  CE3 TRP A 164     4680   5443   4345    600     81   -775       C  
ATOM   1124  CZ2 TRP A 164      29.307   6.512 -16.684  1.00 40.05           C  
ANISOU 1124  CZ2 TRP A 164     5038   5695   4485    493     63  -1002       C  
ATOM   1125  CZ3 TRP A 164      30.686   5.860 -14.796  1.00 39.93           C  
ANISOU 1125  CZ3 TRP A 164     5019   5541   4612    634     98   -886       C  
ATOM   1126  CH2 TRP A 164      29.824   5.539 -15.856  1.00 40.59           C  
ANISOU 1126  CH2 TRP A 164     5158   5620   4643    574     90  -1005       C  
ATOM   1127  N   GLN A 165      33.526  11.898 -16.593  1.00 30.65           N  
ANISOU 1127  N   GLN A 165     3359   5173   3113    503    124   -493       N  
ATOM   1128  CA  GLN A 165      33.856  12.403 -17.930  1.00 30.02           C  
ANISOU 1128  CA  GLN A 165     3233   5254   2920    499    157   -495       C  
ATOM   1129  C   GLN A 165      35.101  11.706 -18.521  1.00 32.71           C  
ANISOU 1129  C   GLN A 165     3521   5703   3204    615    227   -544       C  
ATOM   1130  O   GLN A 165      35.106  11.389 -19.705  1.00 32.85           O  
ANISOU 1130  O   GLN A 165     3545   5808   3127    651    260   -618       O  
ATOM   1131  CB  GLN A 165      33.989  13.947 -17.936  1.00 31.22           C  
ANISOU 1131  CB  GLN A 165     3322   5491   3049    401    143   -366       C  
ATOM   1132  CG  GLN A 165      35.149  14.495 -17.109  1.00 40.38           C  
ANISOU 1132  CG  GLN A 165     4402   6687   4254    389    154   -275       C  
ATOM   1133  CD  GLN A 165      35.155  15.993 -16.977  1.00 58.78           C  
ANISOU 1133  CD  GLN A 165     6694   9059   6579    276    137   -159       C  
ATOM   1134  OE1 GLN A 165      35.470  16.730 -17.916  1.00 51.17           O  
ANISOU 1134  OE1 GLN A 165     5689   8218   5537    241    165   -110       O  
ATOM   1135  NE2 GLN A 165      34.837  16.473 -15.784  1.00 56.36           N  
ANISOU 1135  NE2 GLN A 165     6407   8650   6357    215     93   -112       N  
ATOM   1136  N   TYR A 166      36.110  11.409 -17.681  1.00 28.43           N  
ANISOU 1136  N   TYR A 166     2925   5162   2713    682    247   -508       N  
ATOM   1137  CA  TYR A 166      37.348  10.736 -18.083  1.00 28.00           C  
ANISOU 1137  CA  TYR A 166     2808   5217   2616    812    315   -544       C  
ATOM   1138  C   TYR A 166      37.146   9.246 -18.311  1.00 31.04           C  
ANISOU 1138  C   TYR A 166     3284   5491   3017    935    341   -682       C  
ATOM   1139  O   TYR A 166      37.799   8.678 -19.184  1.00 29.75           O  
ANISOU 1139  O   TYR A 166     3099   5423   2782   1041    402   -756       O  
ATOM   1140  CB  TYR A 166      38.502  11.026 -17.100  1.00 29.05           C  
ANISOU 1140  CB  TYR A 166     2835   5412   2791    839    322   -448       C  
ATOM   1141  CG  TYR A 166      38.712  12.509 -16.895  1.00 30.78           C  
ANISOU 1141  CG  TYR A 166     2974   5725   2995    701    298   -325       C  
ATOM   1142  CD1 TYR A 166      39.326  13.288 -17.872  1.00 32.61           C  
ANISOU 1142  CD1 TYR A 166     3117   6142   3131    662    339   -279       C  
ATOM   1143  CD2 TYR A 166      38.238  13.148 -15.755  1.00 31.63           C  
ANISOU 1143  CD2 TYR A 166     3103   5731   3185    604    237   -258       C  
ATOM   1144  CE1 TYR A 166      39.465  14.666 -17.718  1.00 33.25           C  
ANISOU 1144  CE1 TYR A 166     3142   6284   3208    523    320   -164       C  
ATOM   1145  CE2 TYR A 166      38.380  14.525 -15.585  1.00 32.64           C  
ANISOU 1145  CE2 TYR A 166     3176   5919   3305    473    217   -158       C  
ATOM   1146  CZ  TYR A 166      38.978  15.283 -16.578  1.00 40.07           C  
ANISOU 1146  CZ  TYR A 166     4040   7024   4161    429    258   -110       C  
ATOM   1147  OH  TYR A 166      39.117  16.638 -16.418  1.00 40.64           O  
ANISOU 1147  OH  TYR A 166     4072   7135   4235    292    242     -8       O  
ATOM   1148  N   LEU A 167      36.223   8.619 -17.555  1.00 28.41           N  
ANISOU 1148  N   LEU A 167     3059   4957   2778    917    297   -718       N  
ATOM   1149  CA  LEU A 167      35.913   7.194 -17.712  1.00 28.25           C  
ANISOU 1149  CA  LEU A 167     3150   4792   2792   1010    318   -848       C  
ATOM   1150  C   LEU A 167      35.120   6.959 -18.987  1.00 33.02           C  
ANISOU 1150  C   LEU A 167     3822   5408   3315    973    322   -972       C  
ATOM   1151  O   LEU A 167      35.464   6.061 -19.759  1.00 32.89           O  
ANISOU 1151  O   LEU A 167     3846   5397   3256   1076    374  -1093       O  
ATOM   1152  CB  LEU A 167      35.148   6.630 -16.496  1.00 28.08           C  
ANISOU 1152  CB  LEU A 167     3219   4556   2895    982    271   -832       C  
ATOM   1153  CG  LEU A 167      35.883   6.592 -15.150  1.00 32.34           C  
ANISOU 1153  CG  LEU A 167     3708   5066   3513   1041    267   -726       C  
ATOM   1154  CD1 LEU A 167      34.929   6.242 -14.034  1.00 32.39           C  
ANISOU 1154  CD1 LEU A 167     3796   4890   3620    975    214   -694       C  
ATOM   1155  CD2 LEU A 167      37.048   5.608 -15.171  1.00 34.34           C  
ANISOU 1155  CD2 LEU A 167     3955   5318   3776   1228    329   -764       C  
ATOM   1156  N   VAL A 168      34.084   7.789 -19.221  1.00 30.16           N  
ANISOU 1156  N   VAL A 168     3470   5062   2928    833    269   -943       N  
ATOM   1157  CA  VAL A 168      33.206   7.693 -20.386  1.00 30.41           C  
ANISOU 1157  CA  VAL A 168     3554   5130   2872    779    258  -1047       C  
ATOM   1158  C   VAL A 168      33.941   8.148 -21.680  1.00 34.13           C  
ANISOU 1158  C   VAL A 168     3946   5825   3197    819    309  -1061       C  
ATOM   1159  O   VAL A 168      33.730   7.541 -22.732  1.00 34.43           O  
ANISOU 1159  O   VAL A 168     4028   5904   3149    852    334  -1195       O  
ATOM   1160  CB  VAL A 168      31.828   8.380 -20.148  1.00 34.95           C  
ANISOU 1160  CB  VAL A 168     4155   5657   3467    633    183  -1003       C  
ATOM   1161  CG1 VAL A 168      31.927   9.899 -20.133  1.00 35.08           C  
ANISOU 1161  CG1 VAL A 168     4080   5802   3448    560    162   -855       C  
ATOM   1162  CG2 VAL A 168      30.783   7.910 -21.150  1.00 34.89           C  
ANISOU 1162  CG2 VAL A 168     4214   5655   3387    582    162  -1132       C  
ATOM   1163  N   GLY A 169      34.836   9.133 -21.575  1.00 29.33           N  
ANISOU 1163  N   GLY A 169     3225   5360   2561    815    329   -931       N  
ATOM   1164  CA  GLY A 169      35.621   9.597 -22.714  1.00 28.61           C  
ANISOU 1164  CA  GLY A 169     3047   5492   2333    846    384   -919       C  
ATOM   1165  C   GLY A 169      35.283  10.967 -23.273  1.00 31.79           C  
ANISOU 1165  C   GLY A 169     3390   6031   2657    731    361   -804       C  
ATOM   1166  O   GLY A 169      36.010  11.466 -24.136  1.00 31.88           O  
ANISOU 1166  O   GLY A 169     3319   6237   2557    746    410   -765       O  
ATOM   1167  N   GLU A 170      34.209  11.605 -22.769  1.00 27.51           N  
ANISOU 1167  N   GLU A 170     2889   5393   2172    619    290   -741       N  
ATOM   1168  CA  GLU A 170      33.755  12.943 -23.177  1.00 26.71           C  
ANISOU 1168  CA  GLU A 170     2750   5384   2016    516    262   -620       C  
ATOM   1169  C   GLU A 170      33.034  13.634 -22.022  1.00 29.64           C  
ANISOU 1169  C   GLU A 170     3148   5610   2504    429    197   -528       C  
ATOM   1170  O   GLU A 170      32.370  12.958 -21.238  1.00 28.96           O  
ANISOU 1170  O   GLU A 170     3130   5365   2509    429    160   -588       O  
ATOM   1171  CB  GLU A 170      32.761  12.871 -24.366  1.00 28.13           C  
ANISOU 1171  CB  GLU A 170     2969   5641   2079    488    241   -689       C  
ATOM   1172  CG  GLU A 170      33.337  12.467 -25.718  1.00 39.30           C  
ANISOU 1172  CG  GLU A 170     4350   7243   3338    555    303   -768       C  
ATOM   1173  CD  GLU A 170      34.212  13.459 -26.459  1.00 60.35           C  
ANISOU 1173  CD  GLU A 170     6916  10118   5898    544    352   -643       C  
ATOM   1174  OE1 GLU A 170      34.057  14.684 -26.248  1.00 58.82           O  
ANISOU 1174  OE1 GLU A 170     6691   9936   5723    457    326   -486       O  
ATOM   1175  OE2 GLU A 170      35.031  13.002 -27.287  1.00 53.27           O  
ANISOU 1175  OE2 GLU A 170     5974   9373   4894    622    421   -705       O  
ATOM   1176  N   ARG A 171      33.119  14.977 -21.947  1.00 25.72           N  
ANISOU 1176  N   ARG A 171     2604   5165   2002    352    186   -384       N  
ATOM   1177  CA  ARG A 171      32.336  15.778 -21.009  1.00 25.25           C  
ANISOU 1177  CA  ARG A 171     2577   4982   2037    272    128   -301       C  
ATOM   1178  C   ARG A 171      31.116  16.193 -21.833  1.00 30.71           C  
ANISOU 1178  C   ARG A 171     3303   5705   2659    230     89   -295       C  
ATOM   1179  O   ARG A 171      31.242  16.950 -22.807  1.00 30.85           O  
ANISOU 1179  O   ARG A 171     3287   5857   2579    209    107   -222       O  
ATOM   1180  CB  ARG A 171      33.094  17.003 -20.480  1.00 23.66           C  
ANISOU 1180  CB  ARG A 171     2316   4802   1871    212    138   -159       C  
ATOM   1181  CG  ARG A 171      32.208  17.930 -19.665  1.00 25.52           C  
ANISOU 1181  CG  ARG A 171     2595   4912   2190    135     82    -84       C  
ATOM   1182  CD  ARG A 171      32.948  19.144 -19.164  1.00 28.26           C  
ANISOU 1182  CD  ARG A 171     2898   5265   2573     63     93     41       C  
ATOM   1183  NE  ARG A 171      32.115  19.939 -18.260  1.00 32.05           N  
ANISOU 1183  NE  ARG A 171     3431   5608   3139      4     43     93       N  
ATOM   1184  CZ  ARG A 171      31.992  19.720 -16.954  1.00 41.56           C  
ANISOU 1184  CZ  ARG A 171     4657   6693   4442     -1     14     66       C  
ATOM   1185  NH1 ARG A 171      32.644  18.718 -16.377  1.00 28.06           N  
ANISOU 1185  NH1 ARG A 171     2923   4977   2762     49     26      0       N  
ATOM   1186  NH2 ARG A 171      31.216  20.500 -16.217  1.00 27.04           N  
ANISOU 1186  NH2 ARG A 171     2864   4743   2667    -49    -25    108       N  
ATOM   1187  N   THR A 172      29.953  15.634 -21.493  1.00 27.25           N  
ANISOU 1187  N   THR A 172     2929   5162   2264    221     40   -371       N  
ATOM   1188  CA  THR A 172      28.738  15.866 -22.268  1.00 27.00           C  
ANISOU 1188  CA  THR A 172     2919   5178   2160    189     -2   -381       C  
ATOM   1189  C   THR A 172      27.878  16.990 -21.673  1.00 32.16           C  
ANISOU 1189  C   THR A 172     3581   5765   2872    132    -51   -265       C  
ATOM   1190  O   THR A 172      26.856  17.361 -22.260  1.00 31.79           O  
ANISOU 1190  O   THR A 172     3541   5770   2769    112    -89   -246       O  
ATOM   1191  CB  THR A 172      27.997  14.549 -22.477  1.00 29.79           C  
ANISOU 1191  CB  THR A 172     3326   5488   2505    204    -24   -541       C  
ATOM   1192  OG1 THR A 172      27.605  14.028 -21.208  1.00 25.81           O  
ANISOU 1192  OG1 THR A 172     2865   4809   2134    190    -51   -570       O  
ATOM   1193  CG2 THR A 172      28.839  13.516 -23.249  1.00 23.34           C  
ANISOU 1193  CG2 THR A 172     2510   4741   1616    273     31   -664       C  
ATOM   1194  N   VAL A 173      28.316  17.554 -20.530  1.00 29.18           N  
ANISOU 1194  N   VAL A 173     3200   5288   2600    111    -48   -188       N  
ATOM   1195  CA  VAL A 173      27.675  18.701 -19.887  1.00 29.11           C  
ANISOU 1195  CA  VAL A 173     3204   5204   2651     66    -83    -82       C  
ATOM   1196  C   VAL A 173      28.125  19.906 -20.738  1.00 35.35           C  
ANISOU 1196  C   VAL A 173     3964   6096   3369     46    -57     45       C  
ATOM   1197  O   VAL A 173      29.330  20.145 -20.878  1.00 34.52           O  
ANISOU 1197  O   VAL A 173     3821   6041   3253     37    -10     88       O  
ATOM   1198  CB  VAL A 173      28.081  18.847 -18.390  1.00 32.30           C  
ANISOU 1198  CB  VAL A 173     3619   5472   3182     47    -86    -62       C  
ATOM   1199  CG1 VAL A 173      27.486  20.109 -17.774  1.00 31.90           C  
ANISOU 1199  CG1 VAL A 173     3589   5346   3187      6   -114     38       C  
ATOM   1200  CG2 VAL A 173      27.677  17.618 -17.578  1.00 31.99           C  
ANISOU 1200  CG2 VAL A 173     3612   5336   3208     69   -106   -170       C  
ATOM   1201  N   LEU A 174      27.165  20.617 -21.353  1.00 33.60           N  
ANISOU 1201  N   LEU A 174     3755   5918   3095     41    -87    108       N  
ATOM   1202  CA  LEU A 174      27.474  21.760 -22.216  1.00 34.23           C  
ANISOU 1202  CA  LEU A 174     3817   6088   3102     25    -64    244       C  
ATOM   1203  C   LEU A 174      27.930  22.985 -21.427  1.00 39.81           C  
ANISOU 1203  C   LEU A 174     4541   6684   3902    -23    -52    366       C  
ATOM   1204  O   LEU A 174      27.641  23.083 -20.231  1.00 39.73           O  
ANISOU 1204  O   LEU A 174     4561   6531   4003    -37    -77    347       O  
ATOM   1205  CB  LEU A 174      26.285  22.102 -23.136  1.00 34.31           C  
ANISOU 1205  CB  LEU A 174     3833   6183   3021     48   -102    283       C  
ATOM   1206  CG  LEU A 174      25.863  21.024 -24.146  1.00 39.20           C  
ANISOU 1206  CG  LEU A 174     4431   6947   3518     79   -114    166       C  
ATOM   1207  CD1 LEU A 174      24.498  21.331 -24.727  1.00 39.62           C  
ANISOU 1207  CD1 LEU A 174     4484   7065   3507     95   -171    189       C  
ATOM   1208  CD2 LEU A 174      26.897  20.844 -25.258  1.00 40.99           C  
ANISOU 1208  CD2 LEU A 174     4616   7339   3618     90    -58    177       C  
ATOM   1209  N   ALA A 175      28.669  23.903 -22.088  1.00 37.16           N  
ANISOU 1209  N   ALA A 175     4185   6416   3516    -56    -12    488       N  
ATOM   1210  CA  ALA A 175      29.142  25.147 -21.471  1.00 37.34           C  
ANISOU 1210  CA  ALA A 175     4233   6332   3621   -120      3    607       C  
ATOM   1211  C   ALA A 175      27.927  26.040 -21.162  1.00 40.94           C  
ANISOU 1211  C   ALA A 175     4755   6672   4128   -105    -39    675       C  
ATOM   1212  O   ALA A 175      27.108  26.308 -22.047  1.00 41.05           O  
ANISOU 1212  O   ALA A 175     4777   6757   4065    -62    -56    732       O  
ATOM   1213  CB  ALA A 175      30.112  25.866 -22.400  1.00 38.09           C  
ANISOU 1213  CB  ALA A 175     4294   6539   3641   -166     59    728       C  
ATOM   1214  N   GLY A 176      27.800  26.434 -19.900  1.00 36.05           N  
ANISOU 1214  N   GLY A 176     4176   5890   3631   -130    -57    662       N  
ATOM   1215  CA  GLY A 176      26.665  27.217 -19.425  1.00 35.14           C  
ANISOU 1215  CA  GLY A 176     4123   5652   3576   -102    -92    707       C  
ATOM   1216  C   GLY A 176      25.713  26.376 -18.597  1.00 36.75           C  
ANISOU 1216  C   GLY A 176     4331   5807   3826    -57   -137    588       C  
ATOM   1217  O   GLY A 176      24.822  26.907 -17.931  1.00 36.44           O  
ANISOU 1217  O   GLY A 176     4334   5662   3850    -32   -164    603       O  
ATOM   1218  N   GLN A 177      25.893  25.049 -18.644  1.00 31.68           N  
ANISOU 1218  N   GLN A 177     3646   5240   3152    -46   -142    471       N  
ATOM   1219  CA  GLN A 177      25.105  24.088 -17.877  1.00 30.77           C  
ANISOU 1219  CA  GLN A 177     3531   5082   3077    -19   -178    357       C  
ATOM   1220  C   GLN A 177      25.967  23.561 -16.739  1.00 33.21           C  
ANISOU 1220  C   GLN A 177     3837   5316   3466    -52   -165    289       C  
ATOM   1221  O   GLN A 177      27.193  23.522 -16.859  1.00 32.52           O  
ANISOU 1221  O   GLN A 177     3723   5265   3369    -82   -129    299       O  
ATOM   1222  CB  GLN A 177      24.654  22.904 -18.750  1.00 31.84           C  
ANISOU 1222  CB  GLN A 177     3633   5340   3122     13   -193    269       C  
ATOM   1223  CG  GLN A 177      23.763  23.270 -19.929  1.00 40.66           C  
ANISOU 1223  CG  GLN A 177     4739   6570   4139     47   -215    324       C  
ATOM   1224  CD  GLN A 177      23.138  22.059 -20.581  1.00 55.66           C  
ANISOU 1224  CD  GLN A 177     6610   8578   5960     63   -242    210       C  
ATOM   1225  OE1 GLN A 177      21.947  22.052 -20.895  1.00 51.39           O  
ANISOU 1225  OE1 GLN A 177     6057   8082   5385     84   -286    204       O  
ATOM   1226  NE2 GLN A 177      23.915  21.005 -20.802  1.00 46.50           N  
ANISOU 1226  NE2 GLN A 177     5437   7462   4769     54   -216    113       N  
ATOM   1227  N   CYS A 178      25.326  23.160 -15.636  1.00 28.80           N  
ANISOU 1227  N   CYS A 178     3297   4669   2979    -44   -193    228       N  
ATOM   1228  CA  CYS A 178      26.015  22.584 -14.492  1.00 28.13           C  
ANISOU 1228  CA  CYS A 178     3207   4521   2960    -65   -186    168       C  
ATOM   1229  C   CYS A 178      25.160  21.520 -13.823  1.00 30.31           C  
ANISOU 1229  C   CYS A 178     3488   4760   3266    -41   -215     79       C  
ATOM   1230  O   CYS A 178      24.181  21.836 -13.144  1.00 29.77           O  
ANISOU 1230  O   CYS A 178     3442   4631   3238    -35   -240     82       O  
ATOM   1231  CB  CYS A 178      26.489  23.649 -13.503  1.00 28.59           C  
ANISOU 1231  CB  CYS A 178     3289   4485   3091   -109   -180    220       C  
ATOM   1232  SG  CYS A 178      27.679  23.032 -12.282  1.00 32.66           S  
ANISOU 1232  SG  CYS A 178     3775   4974   3659   -141   -170    166       S  
ATOM   1233  N   TYR A 179      25.517  20.249 -14.062  1.00 25.63           N  
ANISOU 1233  N   TYR A 179     2879   4207   2652    -26   -205      2       N  
ATOM   1234  CA  TYR A 179      24.842  19.066 -13.519  1.00 24.48           C  
ANISOU 1234  CA  TYR A 179     2746   4021   2536    -15   -225    -83       C  
ATOM   1235  C   TYR A 179      25.810  17.881 -13.484  1.00 26.62           C  
ANISOU 1235  C   TYR A 179     3009   4295   2809      6   -199   -147       C  
ATOM   1236  O   TYR A 179      26.877  17.941 -14.098  1.00 25.45           O  
ANISOU 1236  O   TYR A 179     2836   4213   2623     19   -167   -135       O  
ATOM   1237  CB  TYR A 179      23.550  18.732 -14.309  1.00 25.05           C  
ANISOU 1237  CB  TYR A 179     2819   4143   2556     -9   -254   -117       C  
ATOM   1238  CG  TYR A 179      23.767  18.275 -15.736  1.00 26.78           C  
ANISOU 1238  CG  TYR A 179     3023   4470   2681      4   -242   -152       C  
ATOM   1239  CD1 TYR A 179      23.871  19.196 -16.777  1.00 28.75           C  
ANISOU 1239  CD1 TYR A 179     3255   4813   2857     12   -236    -80       C  
ATOM   1240  CD2 TYR A 179      23.811  16.920 -16.057  1.00 27.42           C  
ANISOU 1240  CD2 TYR A 179     3114   4560   2743     10   -237   -259       C  
ATOM   1241  CE1 TYR A 179      24.043  18.779 -18.098  1.00 29.48           C  
ANISOU 1241  CE1 TYR A 179     3329   5026   2846     26   -224   -114       C  
ATOM   1242  CE2 TYR A 179      23.983  16.492 -17.373  1.00 28.40           C  
ANISOU 1242  CE2 TYR A 179     3228   4791   2771     24   -225   -308       C  
ATOM   1243  CZ  TYR A 179      24.094  17.425 -18.390  1.00 35.48           C  
ANISOU 1243  CZ  TYR A 179     4098   5802   3583     32   -220   -237       C  
ATOM   1244  OH  TYR A 179      24.268  16.999 -19.682  1.00 37.39           O  
ANISOU 1244  OH  TYR A 179     4325   6167   3715     47   -207   -287       O  
ATOM   1245  N   ILE A 180      25.445  16.818 -12.760  1.00 22.83           N  
ANISOU 1245  N   ILE A 180     2550   3748   2376     12   -209   -209       N  
ATOM   1246  CA  ILE A 180      26.271  15.624 -12.645  1.00 23.02           C  
ANISOU 1246  CA  ILE A 180     2581   3753   2414     48   -184   -267       C  
ATOM   1247  C   ILE A 180      26.064  14.733 -13.854  1.00 27.31           C  
ANISOU 1247  C   ILE A 180     3139   4342   2896     67   -173   -349       C  
ATOM   1248  O   ILE A 180      24.944  14.295 -14.114  1.00 27.75           O  
ANISOU 1248  O   ILE A 180     3219   4385   2942     40   -200   -398       O  
ATOM   1249  CB  ILE A 180      26.031  14.883 -11.306  1.00 26.23           C  
ANISOU 1249  CB  ILE A 180     3013   4056   2898     48   -194   -283       C  
ATOM   1250  CG1 ILE A 180      26.483  15.743 -10.110  1.00 26.69           C  
ANISOU 1250  CG1 ILE A 180     3050   4092   2999     35   -199   -213       C  
ATOM   1251  CG2 ILE A 180      26.718  13.515 -11.294  1.00 26.63           C  
ANISOU 1251  CG2 ILE A 180     3085   4067   2964     99   -168   -344       C  
ATOM   1252  CD1 ILE A 180      26.186  15.105  -8.810  1.00 35.52           C  
ANISOU 1252  CD1 ILE A 180     4189   5131   4177     34   -211   -216       C  
ATOM   1253  N   GLN A 181      27.153  14.438 -14.563  1.00 23.77           N  
ANISOU 1253  N   GLN A 181     2671   3956   2404    112   -135   -370       N  
ATOM   1254  CA  GLN A 181      27.139  13.617 -15.765  1.00 23.68           C  
ANISOU 1254  CA  GLN A 181     2674   4000   2322    140   -117   -461       C  
ATOM   1255  C   GLN A 181      26.832  12.129 -15.532  1.00 30.40           C  
ANISOU 1255  C   GLN A 181     3585   4750   3214    159   -114   -567       C  
ATOM   1256  O   GLN A 181      26.204  11.513 -16.402  1.00 30.41           O  
ANISOU 1256  O   GLN A 181     3617   4771   3166    144   -122   -657       O  
ATOM   1257  CB  GLN A 181      28.455  13.779 -16.517  1.00 24.46           C  
ANISOU 1257  CB  GLN A 181     2729   4206   2360    191    -68   -448       C  
ATOM   1258  CG  GLN A 181      28.329  13.517 -18.005  1.00 27.41           C  
ANISOU 1258  CG  GLN A 181     3101   4692   2622    205    -52   -513       C  
ATOM   1259  CD  GLN A 181      29.650  13.644 -18.694  1.00 35.18           C  
ANISOU 1259  CD  GLN A 181     4032   5795   3540    258      3   -497       C  
ATOM   1260  OE1 GLN A 181      30.337  14.665 -18.593  1.00 27.25           O  
ANISOU 1260  OE1 GLN A 181     2972   4852   2529    239     17   -392       O  
ATOM   1261  NE2 GLN A 181      30.030  12.604 -19.412  1.00 26.53           N  
ANISOU 1261  NE2 GLN A 181     2952   4735   2393    322     39   -605       N  
ATOM   1262  N   PHE A 182      27.280  11.541 -14.392  1.00 28.25           N  
ANISOU 1262  N   PHE A 182     3333   4373   3027    190   -104   -557       N  
ATOM   1263  CA  PHE A 182      27.068  10.112 -14.133  1.00 28.72           C  
ANISOU 1263  CA  PHE A 182     3463   4314   3137    212    -95   -643       C  
ATOM   1264  C   PHE A 182      25.589   9.777 -13.887  1.00 34.32           C  
ANISOU 1264  C   PHE A 182     4216   4950   3875    127   -136   -678       C  
ATOM   1265  O   PHE A 182      25.210   8.614 -14.004  1.00 34.35           O  
ANISOU 1265  O   PHE A 182     4285   4864   3904    118   -131   -766       O  
ATOM   1266  CB  PHE A 182      28.007   9.555 -13.029  1.00 30.68           C  
ANISOU 1266  CB  PHE A 182     3718   4480   3461    281    -70   -605       C  
ATOM   1267  CG  PHE A 182      27.536   9.554 -11.593  1.00 32.27           C  
ANISOU 1267  CG  PHE A 182     3933   4586   3743    246    -97   -540       C  
ATOM   1268  CD1 PHE A 182      26.706   8.544 -11.115  1.00 35.77           C  
ANISOU 1268  CD1 PHE A 182     4447   4900   4243    217   -107   -580       C  
ATOM   1269  CD2 PHE A 182      28.004  10.500 -10.693  1.00 34.05           C  
ANISOU 1269  CD2 PHE A 182     4101   4851   3985    242   -108   -442       C  
ATOM   1270  CE1 PHE A 182      26.280   8.539  -9.784  1.00 36.75           C  
ANISOU 1270  CE1 PHE A 182     4579   4953   4432    186   -127   -512       C  
ATOM   1271  CE2 PHE A 182      27.577  10.496  -9.363  1.00 36.90           C  
ANISOU 1271  CE2 PHE A 182     4473   5141   4406    214   -131   -389       C  
ATOM   1272  CZ  PHE A 182      26.723   9.512  -8.916  1.00 35.21           C  
ANISOU 1272  CZ  PHE A 182     4324   4814   4242    190   -139   -419       C  
ATOM   1273  N   LEU A 183      24.756  10.789 -13.595  1.00 32.35           N  
ANISOU 1273  N   LEU A 183     3930   4742   3620     65   -175   -612       N  
ATOM   1274  CA  LEU A 183      23.320  10.608 -13.393  1.00 33.25           C  
ANISOU 1274  CA  LEU A 183     4060   4823   3750    -15   -214   -634       C  
ATOM   1275  C   LEU A 183      22.585  10.794 -14.728  1.00 40.80           C  
ANISOU 1275  C   LEU A 183     4999   5890   4613    -53   -237   -690       C  
ATOM   1276  O   LEU A 183      21.777  11.716 -14.874  1.00 40.52           O  
ANISOU 1276  O   LEU A 183     4919   5932   4546    -88   -270   -640       O  
ATOM   1277  CB  LEU A 183      22.772  11.568 -12.311  1.00 33.11           C  
ANISOU 1277  CB  LEU A 183     4007   4799   3773    -45   -240   -535       C  
ATOM   1278  CG  LEU A 183      23.354  11.468 -10.903  1.00 37.17           C  
ANISOU 1278  CG  LEU A 183     4531   5228   4365    -19   -226   -477       C  
ATOM   1279  CD1 LEU A 183      22.889  12.629 -10.054  1.00 37.12           C  
ANISOU 1279  CD1 LEU A 183     4486   5246   4373    -41   -247   -392       C  
ATOM   1280  CD2 LEU A 183      22.975  10.157 -10.232  1.00 39.50           C  
ANISOU 1280  CD2 LEU A 183     4882   5404   4723    -41   -222   -514       C  
ATOM   1281  N   SER A 184      22.895   9.928 -15.718  1.00 40.29           N  
ANISOU 1281  N   SER A 184     4968   5840   4499    -36   -217   -797       N  
ATOM   1282  CA  SER A 184      22.269   9.985 -17.043  1.00 41.53           C  
ANISOU 1282  CA  SER A 184     5109   6121   4551    -71   -239   -865       C  
ATOM   1283  C   SER A 184      20.798   9.571 -16.963  1.00 46.77           C  
ANISOU 1283  C   SER A 184     5779   6772   5220   -170   -287   -916       C  
ATOM   1284  O   SER A 184      19.928  10.448 -16.947  1.00 47.55           O  
ANISOU 1284  O   SER A 184     5819   6963   5285   -206   -327   -855       O  
ATOM   1285  CB  SER A 184      23.049   9.169 -18.080  1.00 45.79           C  
ANISOU 1285  CB  SER A 184     5685   6686   5029    -22   -201   -977       C  
ATOM   1286  OG  SER A 184      23.581   7.953 -17.575  1.00 55.55           O  
ANISOU 1286  OG  SER A 184     6999   7766   6340      0   -170  -1058       O  
ATOM   1287  N   GLN A 185      20.527   8.260 -16.827  1.00 42.27           N  
ANISOU 1287  N   GLN A 185     5278   6085   4697   -214   -281  -1021       N  
ATOM   1288  CA  GLN A 185      19.169   7.731 -16.719  1.00 41.60           C  
ANISOU 1288  CA  GLN A 185     5199   5983   4624   -329   -322  -1077       C  
ATOM   1289  C   GLN A 185      18.552   8.102 -15.360  1.00 44.33           C  
ANISOU 1289  C   GLN A 185     5517   6270   5055   -364   -339   -972       C  
ATOM   1290  O   GLN A 185      19.259   8.053 -14.349  1.00 43.82           O  
ANISOU 1290  O   GLN A 185     5479   6100   5071   -312   -308   -905       O  
ATOM   1291  CB  GLN A 185      19.148   6.198 -16.914  1.00 42.73           C  
ANISOU 1291  CB  GLN A 185     5441   5992   4804   -374   -304  -1220       C  
ATOM   1292  CG  GLN A 185      19.721   5.690 -18.246  1.00 53.04           C  
ANISOU 1292  CG  GLN A 185     6784   7349   6019   -340   -283  -1353       C  
ATOM   1293  CD  GLN A 185      18.907   6.047 -19.473  1.00 73.00           C  
ANISOU 1293  CD  GLN A 185     9257  10066   8415   -407   -331  -1420       C  
ATOM   1294  OE1 GLN A 185      17.684   6.242 -19.426  1.00 68.83           O  
ANISOU 1294  OE1 GLN A 185     8679   9603   7871   -508   -384  -1411       O  
ATOM   1295  NE2 GLN A 185      19.577   6.122 -20.614  1.00 64.91           N  
ANISOU 1295  NE2 GLN A 185     8231   9149   7284   -348   -312  -1487       N  
ATOM   1296  N   PRO A 186      17.237   8.445 -15.305  1.00 40.17           N  
ANISOU 1296  N   PRO A 186     4933   5823   4507   -449   -386   -958       N  
ATOM   1297  CA  PRO A 186      16.605   8.764 -14.007  1.00 39.21           C  
ANISOU 1297  CA  PRO A 186     4781   5659   4459   -478   -395   -864       C  
ATOM   1298  C   PRO A 186      16.620   7.602 -13.006  1.00 41.17           C  
ANISOU 1298  C   PRO A 186     5102   5732   4811   -524   -370   -882       C  
ATOM   1299  O   PRO A 186      16.496   7.843 -11.802  1.00 40.32           O  
ANISOU 1299  O   PRO A 186     4980   5575   4765   -519   -362   -792       O  
ATOM   1300  CB  PRO A 186      15.173   9.150 -14.396  1.00 41.11           C  
ANISOU 1300  CB  PRO A 186     4939   6043   4639   -557   -447   -869       C  
ATOM   1301  CG  PRO A 186      15.237   9.494 -15.849  1.00 45.64           C  
ANISOU 1301  CG  PRO A 186     5485   6759   5096   -539   -469   -923       C  
ATOM   1302  CD  PRO A 186      16.257   8.555 -16.406  1.00 41.53           C  
ANISOU 1302  CD  PRO A 186     5055   6148   4578   -518   -432  -1024       C  
ATOM   1303  N   ILE A 187      16.795   6.348 -13.501  1.00 36.27           N  
ANISOU 1303  N   ILE A 187     4564   5013   4206   -566   -355   -997       N  
ATOM   1304  CA  ILE A 187      16.888   5.136 -12.684  1.00 35.35           C  
ANISOU 1304  CA  ILE A 187     4536   4705   4190   -606   -325  -1016       C  
ATOM   1305  C   ILE A 187      18.187   5.135 -11.844  1.00 38.56           C  
ANISOU 1305  C   ILE A 187     4986   5004   4661   -483   -279   -937       C  
ATOM   1306  O   ILE A 187      18.192   4.595 -10.732  1.00 38.22           O  
ANISOU 1306  O   ILE A 187     4983   4838   4702   -495   -260   -880       O  
ATOM   1307  CB  ILE A 187      16.681   3.840 -13.526  1.00 38.18           C  
ANISOU 1307  CB  ILE A 187     4982   4979   4546   -685   -321  -1172       C  
ATOM   1308  CG1 ILE A 187      16.318   2.621 -12.642  1.00 38.84           C  
ANISOU 1308  CG1 ILE A 187     5155   4865   4740   -772   -300  -1180       C  
ATOM   1309  CG2 ILE A 187      17.859   3.532 -14.464  1.00 38.00           C  
ANISOU 1309  CG2 ILE A 187     5020   4931   4486   -581   -288  -1259       C  
ATOM   1310  CD1 ILE A 187      14.892   2.618 -12.049  1.00 46.94           C  
ANISOU 1310  CD1 ILE A 187     6122   5933   5780   -926   -335  -1149       C  
ATOM   1311  N   ILE A 188      19.270   5.765 -12.369  1.00 34.12           N  
ANISOU 1311  N   ILE A 188     4407   4506   4053   -369   -262   -927       N  
ATOM   1312  CA  ILE A 188      20.554   5.906 -11.670  1.00 33.16           C  
ANISOU 1312  CA  ILE A 188     4299   4325   3974   -252   -225   -851       C  
ATOM   1313  C   ILE A 188      20.356   6.933 -10.548  1.00 35.71           C  
ANISOU 1313  C   ILE A 188     4554   4698   4317   -248   -241   -722       C  
ATOM   1314  O   ILE A 188      20.843   6.729  -9.428  1.00 34.66           O  
ANISOU 1314  O   ILE A 188     4440   4484   4247   -210   -221   -650       O  
ATOM   1315  CB  ILE A 188      21.721   6.257 -12.642  1.00 36.03           C  
ANISOU 1315  CB  ILE A 188     4649   4767   4273   -150   -201   -883       C  
ATOM   1316  CG1 ILE A 188      21.930   5.118 -13.677  1.00 36.36           C  
ANISOU 1316  CG1 ILE A 188     4770   4752   4294   -144   -178  -1028       C  
ATOM   1317  CG2 ILE A 188      23.035   6.550 -11.876  1.00 36.09           C  
ANISOU 1317  CG2 ILE A 188     4644   4753   4317    -38   -168   -794       C  
ATOM   1318  CD1 ILE A 188      22.624   5.524 -14.999  1.00 43.47           C  
ANISOU 1318  CD1 ILE A 188     5638   5789   5087    -84   -166  -1088       C  
ATOM   1319  N   THR A 189      19.582   8.006 -10.847  1.00 31.39           N  
ANISOU 1319  N   THR A 189     3930   4284   3713   -285   -276   -695       N  
ATOM   1320  CA  THR A 189      19.240   9.060  -9.889  1.00 30.74           C  
ANISOU 1320  CA  THR A 189     3786   4252   3641   -282   -291   -591       C  
ATOM   1321  C   THR A 189      18.337   8.475  -8.787  1.00 33.68           C  
ANISOU 1321  C   THR A 189     4169   4556   4073   -356   -296   -563       C  
ATOM   1322  O   THR A 189      18.514   8.818  -7.618  1.00 32.80           O  
ANISOU 1322  O   THR A 189     4043   4422   3996   -331   -287   -481       O  
ATOM   1323  CB  THR A 189      18.633  10.275 -10.605  1.00 36.80           C  
ANISOU 1323  CB  THR A 189     4481   5166   4334   -288   -323   -574       C  
ATOM   1324  OG1 THR A 189      19.408  10.565 -11.773  1.00 36.55           O  
ANISOU 1324  OG1 THR A 189     4450   5197   4240   -239   -315   -609       O  
ATOM   1325  CG2 THR A 189      18.567  11.510  -9.705  1.00 33.93           C  
ANISOU 1325  CG2 THR A 189     4069   4840   3981   -254   -328   -473       C  
ATOM   1326  N   PHE A 190      17.419   7.549  -9.161  1.00 30.15           N  
ANISOU 1326  N   PHE A 190     3747   4077   3632   -453   -307   -634       N  
ATOM   1327  CA  PHE A 190      16.519   6.867  -8.228  1.00 29.87           C  
ANISOU 1327  CA  PHE A 190     3721   3977   3651   -544   -307   -609       C  
ATOM   1328  C   PHE A 190      17.284   6.002  -7.226  1.00 33.63           C  
ANISOU 1328  C   PHE A 190     4275   4296   4206   -509   -268   -565       C  
ATOM   1329  O   PHE A 190      16.899   5.953  -6.058  1.00 33.79           O  
ANISOU 1329  O   PHE A 190     4283   4292   4263   -537   -261   -486       O  
ATOM   1330  CB  PHE A 190      15.426   6.066  -8.956  1.00 31.63           C  
ANISOU 1330  CB  PHE A 190     3951   4206   3860   -673   -328   -702       C  
ATOM   1331  CG  PHE A 190      14.417   5.432  -8.025  1.00 33.42           C  
ANISOU 1331  CG  PHE A 190     4174   4385   4137   -787   -327   -669       C  
ATOM   1332  CD1 PHE A 190      13.576   6.219  -7.242  1.00 36.22           C  
ANISOU 1332  CD1 PHE A 190     4435   4849   4476   -809   -341   -588       C  
ATOM   1333  CD2 PHE A 190      14.329   4.048  -7.906  1.00 35.88           C  
ANISOU 1333  CD2 PHE A 190     4579   4539   4514   -869   -306   -715       C  
ATOM   1334  CE1 PHE A 190      12.669   5.633  -6.354  1.00 37.43           C  
ANISOU 1334  CE1 PHE A 190     4576   4976   4669   -916   -334   -549       C  
ATOM   1335  CE2 PHE A 190      13.418   3.462  -7.021  1.00 38.80           C  
ANISOU 1335  CE2 PHE A 190     4945   4865   4931   -987   -300   -670       C  
ATOM   1336  CZ  PHE A 190      12.592   4.258  -6.253  1.00 36.98           C  
ANISOU 1336  CZ  PHE A 190     4609   4767   4675  -1012   -313   -585       C  
ATOM   1337  N   GLY A 191      18.375   5.378  -7.681  1.00 29.02           N  
ANISOU 1337  N   GLY A 191     3764   3624   3641   -438   -242   -609       N  
ATOM   1338  CA  GLY A 191      19.264   4.581  -6.844  1.00 27.97           C  
ANISOU 1338  CA  GLY A 191     3702   3348   3576   -373   -205   -561       C  
ATOM   1339  C   GLY A 191      19.883   5.430  -5.750  1.00 30.38           C  
ANISOU 1339  C   GLY A 191     3956   3706   3882   -295   -201   -446       C  
ATOM   1340  O   GLY A 191      19.916   5.013  -4.589  1.00 29.10           O  
ANISOU 1340  O   GLY A 191     3816   3476   3766   -293   -187   -367       O  
ATOM   1341  N   THR A 192      20.332   6.657  -6.112  1.00 26.70           N  
ANISOU 1341  N   THR A 192     3420   3366   3358   -240   -216   -435       N  
ATOM   1342  CA  THR A 192      20.923   7.626  -5.177  1.00 26.55           C  
ANISOU 1342  CA  THR A 192     3348   3409   3329   -180   -218   -344       C  
ATOM   1343  C   THR A 192      19.850   8.194  -4.229  1.00 30.17           C  
ANISOU 1343  C   THR A 192     3759   3918   3785   -244   -236   -287       C  
ATOM   1344  O   THR A 192      20.170   8.516  -3.086  1.00 30.01           O  
ANISOU 1344  O   THR A 192     3721   3908   3774   -214   -231   -213       O  
ATOM   1345  CB  THR A 192      21.723   8.740  -5.902  1.00 32.99           C  
ANISOU 1345  CB  THR A 192     4115   4328   4092   -118   -225   -352       C  
ATOM   1346  OG1 THR A 192      20.834   9.690  -6.502  1.00 31.18           O  
ANISOU 1346  OG1 THR A 192     3837   4195   3815   -166   -252   -371       O  
ATOM   1347  CG2 THR A 192      22.725   8.196  -6.926  1.00 30.27           C  
ANISOU 1347  CG2 THR A 192     3803   3961   3737    -52   -201   -411       C  
ATOM   1348  N   ALA A 193      18.591   8.319  -4.706  1.00 25.76           N  
ANISOU 1348  N   ALA A 193     3173   3408   3206   -328   -257   -326       N  
ATOM   1349  CA  ALA A 193      17.466   8.797  -3.902  1.00 25.81           C  
ANISOU 1349  CA  ALA A 193     3125   3479   3204   -385   -269   -280       C  
ATOM   1350  C   ALA A 193      17.102   7.737  -2.848  1.00 30.72           C  
ANISOU 1350  C   ALA A 193     3782   4013   3875   -440   -249   -234       C  
ATOM   1351  O   ALA A 193      16.779   8.091  -1.711  1.00 29.94           O  
ANISOU 1351  O   ALA A 193     3648   3955   3772   -444   -244   -164       O  
ATOM   1352  CB  ALA A 193      16.274   9.097  -4.791  1.00 26.43           C  
ANISOU 1352  CB  ALA A 193     3156   3645   3243   -454   -296   -333       C  
ATOM   1353  N   MET A 194      17.190   6.437  -3.226  1.00 28.51           N  
ANISOU 1353  N   MET A 194     3580   3611   3641   -478   -233   -272       N  
ATOM   1354  CA  MET A 194      16.953   5.294  -2.343  1.00 28.83           C  
ANISOU 1354  CA  MET A 194     3677   3538   3739   -531   -208   -221       C  
ATOM   1355  C   MET A 194      18.045   5.271  -1.263  1.00 32.34           C  
ANISOU 1355  C   MET A 194     4143   3943   4201   -431   -187   -128       C  
ATOM   1356  O   MET A 194      17.745   5.056  -0.089  1.00 31.86           O  
ANISOU 1356  O   MET A 194     4075   3878   4151   -454   -175    -41       O  
ATOM   1357  CB  MET A 194      16.988   3.968  -3.131  1.00 31.52           C  
ANISOU 1357  CB  MET A 194     4115   3732   4131   -580   -194   -295       C  
ATOM   1358  CG  MET A 194      15.731   3.674  -3.939  1.00 35.87           C  
ANISOU 1358  CG  MET A 194     4650   4312   4669   -720   -215   -379       C  
ATOM   1359  SD  MET A 194      14.199   3.395  -3.002  1.00 41.02           S  
ANISOU 1359  SD  MET A 194     5254   4994   5336   -876   -214   -315       S  
ATOM   1360  CE  MET A 194      14.610   1.888  -2.106  1.00 37.63           C  
ANISOU 1360  CE  MET A 194     4959   4335   5005   -902   -167   -254       C  
ATOM   1361  N   ALA A 195      19.304   5.524  -1.667  1.00 28.20           N  
ANISOU 1361  N   ALA A 195     3633   3413   3670   -321   -185   -144       N  
ATOM   1362  CA  ALA A 195      20.471   5.535  -0.786  1.00 27.74           C  
ANISOU 1362  CA  ALA A 195     3581   3342   3618   -217   -171    -65       C  
ATOM   1363  C   ALA A 195      20.551   6.743   0.160  1.00 30.97           C  
ANISOU 1363  C   ALA A 195     3909   3882   3977   -194   -188     -4       C  
ATOM   1364  O   ALA A 195      21.021   6.581   1.287  1.00 30.91           O  
ANISOU 1364  O   ALA A 195     3900   3876   3969   -152   -179     79       O  
ATOM   1365  CB  ALA A 195      21.747   5.434  -1.608  1.00 28.30           C  
ANISOU 1365  CB  ALA A 195     3676   3388   3690   -115   -162   -109       C  
ATOM   1366  N   THR A 196      20.120   7.943  -0.289  1.00 26.17           N  
ANISOU 1366  N   THR A 196     3238   3382   3323   -215   -210    -46       N  
ATOM   1367  CA  THR A 196      20.220   9.173   0.511  1.00 25.29           C  
ANISOU 1367  CA  THR A 196     3063   3379   3167   -190   -224    -10       C  
ATOM   1368  C   THR A 196      18.907   9.630   1.189  1.00 27.94           C  
ANISOU 1368  C   THR A 196     3355   3781   3479   -255   -228     10       C  
ATOM   1369  O   THR A 196      18.970  10.460   2.101  1.00 26.93           O  
ANISOU 1369  O   THR A 196     3188   3728   3316   -232   -232     42       O  
ATOM   1370  CB  THR A 196      20.816  10.320  -0.326  1.00 32.55           C  
ANISOU 1370  CB  THR A 196     3950   4362   4054   -149   -240    -56       C  
ATOM   1371  OG1 THR A 196      19.932  10.625  -1.403  1.00 34.48           O  
ANISOU 1371  OG1 THR A 196     4183   4630   4287   -194   -252   -116       O  
ATOM   1372  CG2 THR A 196      22.203  10.002  -0.867  1.00 30.24           C  
ANISOU 1372  CG2 THR A 196     3679   4039   3771    -78   -231    -67       C  
ATOM   1373  N   PHE A 197      17.732   9.124   0.753  1.00 24.12           N  
ANISOU 1373  N   PHE A 197     2871   3283   3009   -337   -227    -16       N  
ATOM   1374  CA  PHE A 197      16.469   9.570   1.351  1.00 23.62           C  
ANISOU 1374  CA  PHE A 197     2749   3307   2919   -393   -228      3       C  
ATOM   1375  C   PHE A 197      15.520   8.430   1.764  1.00 29.11           C  
ANISOU 1375  C   PHE A 197     3456   3962   3641   -490   -209     36       C  
ATOM   1376  O   PHE A 197      15.245   8.298   2.951  1.00 29.27           O  
ANISOU 1376  O   PHE A 197     3460   4011   3650   -504   -191    108       O  
ATOM   1377  CB  PHE A 197      15.759  10.584   0.425  1.00 24.76           C  
ANISOU 1377  CB  PHE A 197     2839   3538   3030   -397   -250    -56       C  
ATOM   1378  CG  PHE A 197      14.429  11.113   0.920  1.00 25.27           C  
ANISOU 1378  CG  PHE A 197     2831   3709   3063   -434   -250    -42       C  
ATOM   1379  CD1 PHE A 197      14.374  12.085   1.912  1.00 26.71           C  
ANISOU 1379  CD1 PHE A 197     2975   3963   3209   -383   -242    -11       C  
ATOM   1380  CD2 PHE A 197      13.233  10.650   0.378  1.00 26.66           C  
ANISOU 1380  CD2 PHE A 197     2970   3922   3238   -519   -256    -66       C  
ATOM   1381  CE1 PHE A 197      13.146  12.571   2.368  1.00 27.20           C  
ANISOU 1381  CE1 PHE A 197     2966   4132   3238   -401   -235     -2       C  
ATOM   1382  CE2 PHE A 197      12.006  11.144   0.827  1.00 29.02           C  
ANISOU 1382  CE2 PHE A 197     3184   4341   3501   -545   -254    -49       C  
ATOM   1383  CZ  PHE A 197      11.972  12.097   1.825  1.00 26.84           C  
ANISOU 1383  CZ  PHE A 197     2873   4134   3192   -477   -240    -16       C  
ATOM   1384  N   TYR A 198      15.014   7.631   0.810  1.00 26.77           N  
ANISOU 1384  N   TYR A 198     3187   3607   3376   -566   -214    -16       N  
ATOM   1385  CA  TYR A 198      14.040   6.563   1.074  1.00 26.97           C  
ANISOU 1385  CA  TYR A 198     3225   3590   3433   -686   -198      6       C  
ATOM   1386  C   TYR A 198      14.494   5.548   2.126  1.00 31.91           C  
ANISOU 1386  C   TYR A 198     3918   4107   4101   -691   -165     96       C  
ATOM   1387  O   TYR A 198      13.735   5.312   3.068  1.00 31.46           O  
ANISOU 1387  O   TYR A 198     3830   4089   4035   -755   -145    168       O  
ATOM   1388  CB  TYR A 198      13.588   5.869  -0.225  1.00 27.66           C  
ANISOU 1388  CB  TYR A 198     3343   3623   3545   -770   -212    -86       C  
ATOM   1389  CG  TYR A 198      12.801   6.792  -1.132  1.00 28.67           C  
ANISOU 1389  CG  TYR A 198     3385   3891   3619   -786   -246   -152       C  
ATOM   1390  CD1 TYR A 198      11.515   7.208  -0.792  1.00 30.57           C  
ANISOU 1390  CD1 TYR A 198     3526   4264   3823   -851   -252   -132       C  
ATOM   1391  CD2 TYR A 198      13.356   7.287  -2.307  1.00 28.87           C  
ANISOU 1391  CD2 TYR A 198     3418   3930   3621   -724   -269   -225       C  
ATOM   1392  CE1 TYR A 198      10.798   8.085  -1.604  1.00 31.19           C  
ANISOU 1392  CE1 TYR A 198     3520   4482   3848   -846   -284   -181       C  
ATOM   1393  CE2 TYR A 198      12.646   8.158  -3.133  1.00 29.55           C  
ANISOU 1393  CE2 TYR A 198     3425   4151   3652   -728   -301   -270       C  
ATOM   1394  CZ  TYR A 198      11.366   8.555  -2.778  1.00 36.40           C  
ANISOU 1394  CZ  TYR A 198     4198   5145   4488   -783   -310   -246       C  
ATOM   1395  OH  TYR A 198      10.651   9.397  -3.595  1.00 34.83           O  
ANISOU 1395  OH  TYR A 198     3917   5086   4232   -771   -342   -279       O  
ATOM   1396  N   LEU A 199      15.716   4.975   1.998  1.00 29.01           N  
ANISOU 1396  N   LEU A 199     3636   3615   3773   -615   -156    103       N  
ATOM   1397  CA  LEU A 199      16.224   4.022   2.995  1.00 29.01           C  
ANISOU 1397  CA  LEU A 199     3701   3510   3810   -596   -125    204       C  
ATOM   1398  C   LEU A 199      16.584   4.719   4.328  1.00 31.26           C  
ANISOU 1398  C   LEU A 199     3933   3903   4041   -527   -122    298       C  
ATOM   1399  O   LEU A 199      16.056   4.267   5.346  1.00 30.20           O  
ANISOU 1399  O   LEU A 199     3796   3777   3902   -578    -98    390       O  
ATOM   1400  CB  LEU A 199      17.364   3.128   2.476  1.00 29.50           C  
ANISOU 1400  CB  LEU A 199     3867   3411   3930   -521   -113    188       C  
ATOM   1401  CG  LEU A 199      16.938   2.057   1.466  1.00 35.19           C  
ANISOU 1401  CG  LEU A 199     4671   3986   4714   -606   -104    107       C  
ATOM   1402  CD1 LEU A 199      18.089   1.660   0.568  1.00 35.59           C  
ANISOU 1402  CD1 LEU A 199     4794   3934   4793   -501   -100     40       C  
ATOM   1403  CD2 LEU A 199      16.342   0.832   2.161  1.00 38.84           C  
ANISOU 1403  CD2 LEU A 199     5206   4315   5238   -704    -71    184       C  
ATOM   1404  N   PRO A 200      17.355   5.851   4.370  1.00 27.04           N  
ANISOU 1404  N   PRO A 200     3352   3466   3458   -428   -143    275       N  
ATOM   1405  CA  PRO A 200      17.604   6.518   5.664  1.00 26.76           C  
ANISOU 1405  CA  PRO A 200     3266   3540   3361   -380   -142    348       C  
ATOM   1406  C   PRO A 200      16.336   6.896   6.444  1.00 31.52           C  
ANISOU 1406  C   PRO A 200     3803   4255   3919   -454   -131    377       C  
ATOM   1407  O   PRO A 200      16.324   6.734   7.665  1.00 30.90           O  
ANISOU 1407  O   PRO A 200     3712   4225   3805   -448   -113    467       O  
ATOM   1408  CB  PRO A 200      18.421   7.756   5.273  1.00 28.26           C  
ANISOU 1408  CB  PRO A 200     3418   3805   3514   -297   -170    285       C  
ATOM   1409  CG  PRO A 200      19.074   7.387   4.009  1.00 32.26           C  
ANISOU 1409  CG  PRO A 200     3972   4217   4067   -269   -177    221       C  
ATOM   1410  CD  PRO A 200      18.080   6.544   3.282  1.00 27.87           C  
ANISOU 1410  CD  PRO A 200     3450   3583   3556   -364   -167    186       C  
ATOM   1411  N   VAL A 201      15.267   7.364   5.747  1.00 29.06           N  
ANISOU 1411  N   VAL A 201     3443   3998   3601   -517   -139    308       N  
ATOM   1412  CA  VAL A 201      13.974   7.729   6.357  1.00 29.36           C  
ANISOU 1412  CA  VAL A 201     3403   4158   3594   -582   -125    328       C  
ATOM   1413  C   VAL A 201      13.310   6.493   6.996  1.00 33.23           C  
ANISOU 1413  C   VAL A 201     3913   4603   4109   -683    -91    417       C  
ATOM   1414  O   VAL A 201      12.889   6.562   8.149  1.00 32.82           O  
ANISOU 1414  O   VAL A 201     3819   4642   4008   -697    -67    493       O  
ATOM   1415  CB  VAL A 201      13.031   8.506   5.378  1.00 33.33           C  
ANISOU 1415  CB  VAL A 201     3841   4739   4083   -611   -145    239       C  
ATOM   1416  CG1 VAL A 201      11.567   8.467   5.823  1.00 32.83           C  
ANISOU 1416  CG1 VAL A 201     3697   4788   3991   -699   -125    265       C  
ATOM   1417  CG2 VAL A 201      13.492   9.948   5.203  1.00 33.10           C  
ANISOU 1417  CG2 VAL A 201     3780   4784   4013   -509   -166    185       C  
ATOM   1418  N   THR A 202      13.262   5.362   6.263  1.00 29.96           N  
ANISOU 1418  N   THR A 202     3569   4045   3768   -756    -87    407       N  
ATOM   1419  CA  THR A 202      12.675   4.100   6.747  1.00 29.65           C  
ANISOU 1419  CA  THR A 202     3571   3925   3770   -870    -53    491       C  
ATOM   1420  C   THR A 202      13.383   3.616   8.021  1.00 33.74           C  
ANISOU 1420  C   THR A 202     4133   4408   4279   -815    -26    622       C  
ATOM   1421  O   THR A 202      12.718   3.200   8.970  1.00 34.12           O  
ANISOU 1421  O   THR A 202     4159   4501   4305   -885      6    721       O  
ATOM   1422  CB  THR A 202      12.650   3.053   5.616  1.00 34.02           C  
ANISOU 1422  CB  THR A 202     4210   4306   4409   -948    -57    431       C  
ATOM   1423  OG1 THR A 202      12.070   3.648   4.454  1.00 34.70           O  
ANISOU 1423  OG1 THR A 202     4241   4461   4481   -982    -89    309       O  
ATOM   1424  CG2 THR A 202      11.863   1.797   5.983  1.00 30.53           C  
ANISOU 1424  CG2 THR A 202     3811   3770   4017  -1098    -22    503       C  
ATOM   1425  N   VAL A 203      14.724   3.710   8.040  1.00 29.91           N  
ANISOU 1425  N   VAL A 203     3700   3865   3800   -687    -40    626       N  
ATOM   1426  CA  VAL A 203      15.593   3.315   9.149  1.00 29.43           C  
ANISOU 1426  CA  VAL A 203     3674   3787   3721   -608    -25    747       C  
ATOM   1427  C   VAL A 203      15.363   4.226  10.364  1.00 32.62           C  
ANISOU 1427  C   VAL A 203     3986   4389   4019   -581    -22    796       C  
ATOM   1428  O   VAL A 203      15.157   3.720  11.469  1.00 32.17           O  
ANISOU 1428  O   VAL A 203     3929   4364   3930   -604      7    919       O  
ATOM   1429  CB  VAL A 203      17.084   3.258   8.696  1.00 33.28           C  
ANISOU 1429  CB  VAL A 203     4219   4191   4236   -476    -46    723       C  
ATOM   1430  CG1 VAL A 203      18.041   3.110   9.883  1.00 33.02           C  
ANISOU 1430  CG1 VAL A 203     4193   4195   4160   -376    -41    845       C  
ATOM   1431  CG2 VAL A 203      17.305   2.132   7.688  1.00 33.05           C  
ANISOU 1431  CG2 VAL A 203     4295   3954   4307   -495    -35    689       C  
ATOM   1432  N   MET A 204      15.367   5.559  10.151  1.00 28.46           N  
ANISOU 1432  N   MET A 204     3387   3990   3437   -534    -49    700       N  
ATOM   1433  CA  MET A 204      15.175   6.542  11.223  1.00 27.82           C  
ANISOU 1433  CA  MET A 204     3226   4091   3254   -500    -47    715       C  
ATOM   1434  C   MET A 204      13.767   6.497  11.835  1.00 34.03           C  
ANISOU 1434  C   MET A 204     3947   4984   3999   -595    -12    755       C  
ATOM   1435  O   MET A 204      13.635   6.739  13.036  1.00 33.96           O  
ANISOU 1435  O   MET A 204     3894   5103   3905   -578      7    819       O  
ATOM   1436  CB  MET A 204      15.561   7.955  10.775  1.00 29.39           C  
ANISOU 1436  CB  MET A 204     3383   4365   3418   -428    -81    597       C  
ATOM   1437  CG  MET A 204      17.055   8.125  10.573  1.00 32.15           C  
ANISOU 1437  CG  MET A 204     3771   4667   3776   -332   -111    582       C  
ATOM   1438  SD  MET A 204      17.560   9.815  10.170  1.00 35.82           S  
ANISOU 1438  SD  MET A 204     4193   5216   4201   -267   -146    457       S  
ATOM   1439  CE  MET A 204      17.175   9.883   8.410  1.00 32.09           C  
ANISOU 1439  CE  MET A 204     3741   4644   3808   -297   -159    362       C  
ATOM   1440  N   CYS A 205      12.734   6.150  11.029  1.00 31.48           N  
ANISOU 1440  N   CYS A 205     3611   4622   3727   -698     -4    718       N  
ATOM   1441  CA  CYS A 205      11.348   5.998  11.493  1.00 31.69           C  
ANISOU 1441  CA  CYS A 205     3564   4758   3721   -803     31    759       C  
ATOM   1442  C   CYS A 205      11.206   4.732  12.341  1.00 35.32           C  
ANISOU 1442  C   CYS A 205     4065   5160   4192   -882     72    907       C  
ATOM   1443  O   CYS A 205      10.498   4.756  13.347  1.00 34.42           O  
ANISOU 1443  O   CYS A 205     3887   5183   4008   -923    108    985       O  
ATOM   1444  CB  CYS A 205      10.365   6.001  10.324  1.00 32.44           C  
ANISOU 1444  CB  CYS A 205     3622   4842   3861   -893     20    672       C  
ATOM   1445  SG  CYS A 205      10.085   7.635   9.593  1.00 36.67           S  
ANISOU 1445  SG  CYS A 205     4074   5506   4352   -806    -15    533       S  
ATOM   1446  N   THR A 206      11.883   3.631  11.937  1.00 32.72           N  
ANISOU 1446  N   THR A 206     3849   4631   3953   -897     71    949       N  
ATOM   1447  CA  THR A 206      11.905   2.347  12.658  1.00 32.92           C  
ANISOU 1447  CA  THR A 206     3944   4556   4010   -959    110   1102       C  
ATOM   1448  C   THR A 206      12.627   2.540  14.000  1.00 37.50           C  
ANISOU 1448  C   THR A 206     4515   5231   4502   -857    120   1214       C  
ATOM   1449  O   THR A 206      12.153   2.051  15.028  1.00 37.73           O  
ANISOU 1449  O   THR A 206     4529   5321   4487   -912    161   1348       O  
ATOM   1450  CB  THR A 206      12.559   1.239  11.792  1.00 40.06           C  
ANISOU 1450  CB  THR A 206     4982   5204   5035   -970    104   1097       C  
ATOM   1451  OG1 THR A 206      11.835   1.095  10.565  1.00 37.19           O  
ANISOU 1451  OG1 THR A 206     4619   4778   4735  -1072     90    978       O  
ATOM   1452  CG2 THR A 206      12.625  -0.110  12.504  1.00 38.74           C  
ANISOU 1452  CG2 THR A 206     4907   4898   4915  -1029    148   1260       C  
ATOM   1453  N   LEU A 207      13.761   3.273  13.979  1.00 34.06           N  
ANISOU 1453  N   LEU A 207     4082   4826   4034   -715     82   1159       N  
ATOM   1454  CA  LEU A 207      14.585   3.592  15.147  1.00 33.44           C  
ANISOU 1454  CA  LEU A 207     3985   4859   3861   -610     78   1239       C  
ATOM   1455  C   LEU A 207      13.781   4.399  16.161  1.00 37.41           C  
ANISOU 1455  C   LEU A 207     4382   5592   4240   -630     99   1249       C  
ATOM   1456  O   LEU A 207      13.694   3.976  17.311  1.00 37.22           O  
ANISOU 1456  O   LEU A 207     4348   5649   4147   -639    130   1383       O  
ATOM   1457  CB  LEU A 207      15.857   4.350  14.718  1.00 33.32           C  
ANISOU 1457  CB  LEU A 207     3979   4840   3840   -479     28   1147       C  
ATOM   1458  CG  LEU A 207      17.198   3.583  14.670  1.00 37.62           C  
ANISOU 1458  CG  LEU A 207     4606   5257   4431   -385     14   1220       C  
ATOM   1459  CD1 LEU A 207      17.064   2.199  14.049  1.00 37.88           C  
ANISOU 1459  CD1 LEU A 207     4744   5060   4589   -436     37   1263       C  
ATOM   1460  CD2 LEU A 207      18.235   4.369  13.900  1.00 38.75           C  
ANISOU 1460  CD2 LEU A 207     4738   5410   4574   -284    -33   1106       C  
ATOM   1461  N   TYR A 208      13.119   5.498  15.716  1.00 33.96           N  
ANISOU 1461  N   TYR A 208     3869   5258   3775   -638     88   1113       N  
ATOM   1462  CA  TYR A 208      12.282   6.358  16.560  1.00 33.88           C  
ANISOU 1462  CA  TYR A 208     3757   5465   3651   -643    112   1096       C  
ATOM   1463  C   TYR A 208      11.148   5.575  17.235  1.00 40.23           C  
ANISOU 1463  C   TYR A 208     4522   6335   4428   -759    170   1218       C  
ATOM   1464  O   TYR A 208      10.859   5.825  18.411  1.00 39.04           O  
ANISOU 1464  O   TYR A 208     4312   6360   4163   -747    201   1281       O  
ATOM   1465  CB  TYR A 208      11.740   7.571  15.778  1.00 34.30           C  
ANISOU 1465  CB  TYR A 208     3749   5579   3703   -622     92    934       C  
ATOM   1466  CG  TYR A 208      10.958   8.536  16.643  1.00 35.60           C  
ANISOU 1466  CG  TYR A 208     3815   5960   3750   -599    120    902       C  
ATOM   1467  CD1 TYR A 208      11.608   9.468  17.448  1.00 38.03           C  
ANISOU 1467  CD1 TYR A 208     4110   6378   3962   -498    107    858       C  
ATOM   1468  CD2 TYR A 208       9.567   8.489  16.692  1.00 35.85           C  
ANISOU 1468  CD2 TYR A 208     3764   6095   3762   -679    161    913       C  
ATOM   1469  CE1 TYR A 208      10.894  10.320  18.291  1.00 39.41           C  
ANISOU 1469  CE1 TYR A 208     4202   6747   4023   -469    139    819       C  
ATOM   1470  CE2 TYR A 208       8.841   9.352  17.511  1.00 36.59           C  
ANISOU 1470  CE2 TYR A 208     3763   6396   3742   -642    194    883       C  
ATOM   1471  CZ  TYR A 208       9.508  10.264  18.313  1.00 45.44           C  
ANISOU 1471  CZ  TYR A 208     4885   7611   4770   -533    184    832       C  
ATOM   1472  OH  TYR A 208       8.794  11.119  19.117  1.00 46.79           O  
ANISOU 1472  OH  TYR A 208     4972   7981   4827   -488    221    786       O  
ATOM   1473  N   TRP A 209      10.528   4.636  16.476  1.00 39.68           N  
ANISOU 1473  N   TRP A 209     4486   6130   4461   -878    184   1246       N  
ATOM   1474  CA ATRP A 209       9.442   3.776  16.944  0.50 40.25           C  
ANISOU 1474  CA ATRP A 209     4526   6236   4529  -1020    239   1363       C  
ATOM   1475  CA BTRP A 209       9.443   3.766  16.939  0.50 40.37           C  
ANISOU 1475  CA BTRP A 209     4543   6250   4547  -1021    239   1363       C  
ATOM   1476  C   TRP A 209       9.909   2.929  18.138  1.00 43.55           C  
ANISOU 1476  C   TRP A 209     4993   6649   4904  -1016    272   1549       C  
ATOM   1477  O   TRP A 209       9.184   2.826  19.132  1.00 42.99           O  
ANISOU 1477  O   TRP A 209     4854   6736   4744  -1072    321   1649       O  
ATOM   1478  CB ATRP A 209       8.947   2.883  15.793  0.50 39.65           C  
ANISOU 1478  CB ATRP A 209     4501   5980   4585  -1152    237   1342       C  
ATOM   1479  CB BTRP A 209       8.944   2.870  15.783  0.50 39.88           C  
ANISOU 1479  CB BTRP A 209     4533   6005   4617  -1152    237   1341       C  
ATOM   1480  CG ATRP A 209       7.633   2.207  16.049  0.50 41.18           C  
ANISOU 1480  CG ATRP A 209     4638   6232   4778  -1325    289   1426       C  
ATOM   1481  CG BTRP A 209       8.089   1.705  16.197  0.50 41.50           C  
ANISOU 1481  CG BTRP A 209     4744   6175   4847  -1319    291   1480       C  
ATOM   1482  CD1ATRP A 209       6.396   2.657  15.691  0.50 44.18           C  
ANISOU 1482  CD1ATRP A 209     4895   6762   5130  -1409    300   1359       C  
ATOM   1483  CD1BTRP A 209       8.486   0.407  16.336  0.50 44.55           C  
ANISOU 1483  CD1BTRP A 209     5250   6365   5311  -1377    311   1609       C  
ATOM   1484  CD2ATRP A 209       7.431   0.938  16.688  0.50 41.31           C  
ANISOU 1484  CD2ATRP A 209     4711   6159   4823  -1441    337   1599       C  
ATOM   1485  CD2BTRP A 209       6.691   1.735  16.521  0.50 41.63           C  
ANISOU 1485  CD2BTRP A 209     4643   6358   4817  -1451    333   1509       C  
ATOM   1486  NE1ATRP A 209       5.434   1.748  16.067  0.50 43.89           N  
ANISOU 1486  NE1ATRP A 209     4827   6749   5101  -1581    352   1474       N  
ATOM   1487  NE1BTRP A 209       7.425  -0.373  16.739  0.50 44.20           N  
ANISOU 1487  NE1BTRP A 209     5178   6343   5274  -1551    365   1720       N  
ATOM   1488  CE2ATRP A 209       6.041   0.686  16.688  0.50 45.50           C  
ANISOU 1488  CE2ATRP A 209     5147   6799   5343  -1610    377   1625       C  
ATOM   1489  CE2BTRP A 209       6.309   0.416  16.854  0.50 45.79           C  
ANISOU 1489  CE2BTRP A 209     5225   6776   5395  -1605    379   1660       C  
ATOM   1490  CE3ATRP A 209       8.292  -0.014  17.265  0.50 42.66           C  
ANISOU 1490  CE3ATRP A 209     5007   6172   5032  -1416    351   1743       C  
ATOM   1491  CE3BTRP A 209       5.722   2.754  16.571  0.50 42.99           C  
ANISOU 1491  CE3BTRP A 209     4665   6763   4905  -1451    341   1425       C  
ATOM   1492  CZ2ATRP A 209       5.490  -0.474  17.250  0.50 45.01           C  
ANISOU 1492  CZ2ATRP A 209     5112   6684   5305  -1770    433   1790       C  
ATOM   1493  CZ2BTRP A 209       4.997   0.087  17.225  0.50 45.25           C  
ANISOU 1493  CZ2BTRP A 209     5058   6837   5296  -1773    430   1730       C  
ATOM   1494  CZ3ATRP A 209       7.747  -1.162  17.816  0.50 44.26           C  
ANISOU 1494  CZ3ATRP A 209     5246   6308   5261  -1560    407   1911       C  
ATOM   1495  CZ3BTRP A 209       4.426   2.428  16.947  0.50 44.60           C  
ANISOU 1495  CZ3BTRP A 209     4764   7106   5075  -1599    391   1492       C  
ATOM   1496  CH2ATRP A 209       6.363  -1.384  17.809  0.50 45.04           C  
ANISOU 1496  CH2ATRP A 209     5253   6510   5350  -1743    448   1933       C  
ATOM   1497  CH2BTRP A 209       4.073   1.109  17.265  0.50 45.28           C  
ANISOU 1497  CH2BTRP A 209     4900   7094   5212  -1767    435   1643       C  
ATOM   1498  N   ARG A 210      11.125   2.341  18.045  1.00 39.26           N  
ANISOU 1498  N   ARG A 210     4561   5939   4416   -941    247   1600       N  
ATOM   1499  CA  ARG A 210      11.716   1.516  19.103  1.00 39.11           C  
ANISOU 1499  CA  ARG A 210     4597   5901   4361   -911    271   1786       C  
ATOM   1500  C   ARG A 210      12.137   2.377  20.292  1.00 41.43           C  
ANISOU 1500  C   ARG A 210     4817   6428   4494   -802    265   1806       C  
ATOM   1501  O   ARG A 210      11.967   1.943  21.426  1.00 41.45           O  
ANISOU 1501  O   ARG A 210     4805   6535   4411   -819    304   1963       O  
ATOM   1502  CB  ARG A 210      12.903   0.682  18.586  1.00 41.51           C  
ANISOU 1502  CB  ARG A 210     5034   5964   4772   -842    245   1825       C  
ATOM   1503  CG  ARG A 210      12.532  -0.341  17.507  1.00 58.48           C  
ANISOU 1503  CG  ARG A 210     7280   7864   7078   -954    258   1816       C  
ATOM   1504  CD  ARG A 210      13.699  -1.252  17.166  1.00 74.27           C  
ANISOU 1504  CD  ARG A 210     9417   9629   9174   -868    245   1874       C  
ATOM   1505  NE  ARG A 210      13.481  -1.989  15.919  1.00 85.87           N  
ANISOU 1505  NE  ARG A 210    10979  10857  10789   -951    246   1798       N  
ATOM   1506  CZ  ARG A 210      14.296  -2.926  15.443  1.00101.41           C  
ANISOU 1506  CZ  ARG A 210    13082  12585  12864   -896    246   1831       C  
ATOM   1507  NH1 ARG A 210      15.394  -3.264  16.110  1.00 89.37           N  
ANISOU 1507  NH1 ARG A 210    11607  11031  11318   -750    244   1953       N  
ATOM   1508  NH2 ARG A 210      14.018  -3.538  14.299  1.00 87.98           N  
ANISOU 1508  NH2 ARG A 210    11464  10678  11286   -981    248   1740       N  
ATOM   1509  N   ILE A 211      12.660   3.597  20.031  1.00 36.74           N  
ANISOU 1509  N   ILE A 211     4182   5921   3857   -699    218   1648       N  
ATOM   1510  CA  ILE A 211      13.082   4.570  21.049  1.00 36.02           C  
ANISOU 1510  CA  ILE A 211     4024   6049   3614   -602    205   1624       C  
ATOM   1511  C   ILE A 211      11.872   4.987  21.900  1.00 40.01           C  
ANISOU 1511  C   ILE A 211     4425   6775   4002   -661    258   1639       C  
ATOM   1512  O   ILE A 211      11.943   4.914  23.127  1.00 39.90           O  
ANISOU 1512  O   ILE A 211     4379   6923   3860   -638    282   1745       O  
ATOM   1513  CB  ILE A 211      13.849   5.791  20.437  1.00 38.63           C  
ANISOU 1513  CB  ILE A 211     4344   6389   3943   -500    145   1439       C  
ATOM   1514  CG1 ILE A 211      15.160   5.340  19.755  1.00 38.33           C  
ANISOU 1514  CG1 ILE A 211     4395   6165   4002   -433     99   1441       C  
ATOM   1515  CG2 ILE A 211      14.156   6.851  21.508  1.00 39.32           C  
ANISOU 1515  CG2 ILE A 211     4366   6702   3870   -420    134   1396       C  
ATOM   1516  CD1 ILE A 211      15.704   6.264  18.660  1.00 38.78           C  
ANISOU 1516  CD1 ILE A 211     4457   6162   4116   -380     50   1261       C  
ATOM   1517  N   TYR A 212      10.763   5.381  21.244  1.00 36.69           N  
ANISOU 1517  N   TYR A 212     3948   6374   3619   -733    276   1542       N  
ATOM   1518  CA  TYR A 212       9.522   5.792  21.903  1.00 36.60           C  
ANISOU 1518  CA  TYR A 212     3824   6576   3505   -785    331   1545       C  
ATOM   1519  C   TYR A 212       8.940   4.660  22.771  1.00 42.24           C  
ANISOU 1519  C   TYR A 212     4528   7338   4182   -892    393   1751       C  
ATOM   1520  O   TYR A 212       8.513   4.918  23.896  1.00 41.40           O  
ANISOU 1520  O   TYR A 212     4344   7453   3932   -886    437   1808       O  
ATOM   1521  CB  TYR A 212       8.490   6.291  20.870  1.00 36.91           C  
ANISOU 1521  CB  TYR A 212     3804   6609   3611   -840    333   1414       C  
ATOM   1522  CG  TYR A 212       7.287   6.969  21.490  1.00 37.92           C  
ANISOU 1522  CG  TYR A 212     3800   6982   3625   -854    384   1384       C  
ATOM   1523  CD1 TYR A 212       6.183   6.230  21.915  1.00 39.69           C  
ANISOU 1523  CD1 TYR A 212     3955   7298   3825   -983    448   1505       C  
ATOM   1524  CD2 TYR A 212       7.253   8.349  21.662  1.00 38.48           C  
ANISOU 1524  CD2 TYR A 212     3815   7192   3614   -738    374   1235       C  
ATOM   1525  CE1 TYR A 212       5.088   6.845  22.519  1.00 40.29           C  
ANISOU 1525  CE1 TYR A 212     3897   7622   3788   -986    501   1481       C  
ATOM   1526  CE2 TYR A 212       6.154   8.978  22.250  1.00 39.40           C  
ANISOU 1526  CE2 TYR A 212     3811   7536   3624   -731    427   1202       C  
ATOM   1527  CZ  TYR A 212       5.072   8.222  22.674  1.00 46.75           C  
ANISOU 1527  CZ  TYR A 212     4661   8577   4523   -850    491   1326       C  
ATOM   1528  OH  TYR A 212       3.984   8.835  23.250  1.00 47.42           O  
ANISOU 1528  OH  TYR A 212     4615   8907   4497   -835    548   1295       O  
ATOM   1529  N   ARG A 213       8.930   3.419  22.239  1.00 40.58           N  
ANISOU 1529  N   ARG A 213     4402   6917   4099   -991    401   1858       N  
ATOM   1530  CA  ARG A 213       8.435   2.212  22.902  1.00 40.90           C  
ANISOU 1530  CA  ARG A 213     4460   6943   4137  -1110    461   2066       C  
ATOM   1531  C   ARG A 213       9.260   1.889  24.153  1.00 45.28           C  
ANISOU 1531  C   ARG A 213     5047   7575   4583  -1028    469   2225       C  
ATOM   1532  O   ARG A 213       8.681   1.588  25.195  1.00 45.19           O  
ANISOU 1532  O   ARG A 213     4980   7726   4463  -1082    527   2366       O  
ATOM   1533  CB  ARG A 213       8.415   1.027  21.913  1.00 42.77           C  
ANISOU 1533  CB  ARG A 213     4807   6891   4553  -1222    458   2114       C  
ATOM   1534  CG  ARG A 213       7.995  -0.312  22.519  1.00 61.03           C  
ANISOU 1534  CG  ARG A 213     7166   9135   6887  -1356    520   2338       C  
ATOM   1535  CD  ARG A 213       7.599  -1.309  21.452  1.00 80.22           C  
ANISOU 1535  CD  ARG A 213     9682  11305   9492  -1505    524   2338       C  
ATOM   1536  NE  ARG A 213       6.170  -1.235  21.146  1.00 94.92           N  
ANISOU 1536  NE  ARG A 213    11436  13273  11356  -1674    559   2295       N  
ATOM   1537  CZ  ARG A 213       5.278  -2.155  21.502  1.00112.70           C  
ANISOU 1537  CZ  ARG A 213    13678  15517  13627  -1859    621   2441       C  
ATOM   1538  NH1 ARG A 213       5.662  -3.241  22.164  1.00101.27           N  
ANISOU 1538  NH1 ARG A 213    12336  13939  12202  -1896    658   2648       N  
ATOM   1539  NH2 ARG A 213       3.998  -2.004  21.187  1.00101.76           N  
ANISOU 1539  NH2 ARG A 213    12172  14256  12234  -2009    647   2389       N  
ATOM   1540  N   GLU A 214      10.602   1.971  24.048  1.00 42.09           N  
ANISOU 1540  N   GLU A 214     4721   7075   4197   -897    412   2203       N  
ATOM   1541  CA  GLU A 214      11.538   1.716  25.145  1.00 41.96           C  
ANISOU 1541  CA  GLU A 214     4730   7140   4075   -799    405   2343       C  
ATOM   1542  C   GLU A 214      11.343   2.752  26.256  1.00 45.59           C  
ANISOU 1542  C   GLU A 214     5074   7915   4332   -739    416   2299       C  
ATOM   1543  O   GLU A 214      11.217   2.368  27.419  1.00 45.46           O  
ANISOU 1543  O   GLU A 214     5030   8052   4189   -745    455   2462       O  
ATOM   1544  CB  GLU A 214      12.989   1.729  24.629  1.00 43.38           C  
ANISOU 1544  CB  GLU A 214     4994   7166   4321   -669    336   2297       C  
ATOM   1545  CG  GLU A 214      13.967   0.948  25.496  1.00 52.89           C  
ANISOU 1545  CG  GLU A 214     6256   8365   5474   -588    331   2496       C  
ATOM   1546  CD  GLU A 214      13.900  -0.564  25.397  1.00 73.45           C  
ANISOU 1546  CD  GLU A 214     8970  10743   8194   -653    370   2698       C  
ATOM   1547  OE1 GLU A 214      13.520  -1.080  24.321  1.00 66.50           O  
ANISOU 1547  OE1 GLU A 214     8161   9628   7479   -734    377   2648       O  
ATOM   1548  OE2 GLU A 214      14.247  -1.236  26.396  1.00 71.34           O  
ANISOU 1548  OE2 GLU A 214     8726  10531   7851   -620    394   2908       O  
ATOM   1549  N   THR A 215      11.273   4.053  25.882  1.00 41.62           N  
ANISOU 1549  N   THR A 215     4510   7505   3799   -685    385   2081       N  
ATOM   1550  CA  THR A 215      11.052   5.197  26.778  1.00 41.28           C  
ANISOU 1550  CA  THR A 215     4367   7740   3576   -623    394   1989       C  
ATOM   1551  C   THR A 215       9.741   5.017  27.569  1.00 45.61           C  
ANISOU 1551  C   THR A 215     4822   8484   4022   -714    477   2079       C  
ATOM   1552  O   THR A 215       9.727   5.230  28.782  1.00 45.60           O  
ANISOU 1552  O   THR A 215     4764   8715   3845   -677    505   2139       O  
ATOM   1553  CB  THR A 215      11.112   6.518  25.971  1.00 46.25           C  
ANISOU 1553  CB  THR A 215     4972   8363   4236   -560    351   1738       C  
ATOM   1554  OG1 THR A 215      12.339   6.569  25.239  1.00 42.04           O  
ANISOU 1554  OG1 THR A 215     4523   7650   3801   -492    280   1678       O  
ATOM   1555  CG2 THR A 215      10.985   7.762  26.847  1.00 44.14           C  
ANISOU 1555  CG2 THR A 215     4626   8351   3794   -482    356   1619       C  
ATOM   1556  N   GLU A 216       8.664   4.602  26.865  1.00 42.28           N  
ANISOU 1556  N   GLU A 216     4380   7979   3707   -837    517   2089       N  
ATOM   1557  CA AGLU A 216       7.336   4.350  27.427  0.50 42.07           C  
ANISOU 1557  CA AGLU A 216     4254   8125   3607   -947    599   2178       C  
ATOM   1558  CA BGLU A 216       7.343   4.361  27.440  0.50 41.97           C  
ANISOU 1558  CA BGLU A 216     4240   8115   3592   -945    598   2177       C  
ATOM   1559  C   GLU A 216       7.418   3.271  28.515  1.00 45.96           C  
ANISOU 1559  C   GLU A 216     4766   8676   4020  -1001    647   2433       C  
ATOM   1560  O   GLU A 216       6.868   3.456  29.605  1.00 46.02           O  
ANISOU 1560  O   GLU A 216     4682   8944   3861  -1008    704   2501       O  
ATOM   1561  CB AGLU A 216       6.356   3.950  26.298  0.50 43.51           C  
ANISOU 1561  CB AGLU A 216     4423   8167   3942  -1082    615   2146       C  
ATOM   1562  CB BGLU A 216       6.347   3.975  26.332  0.50 43.32           C  
ANISOU 1562  CB BGLU A 216     4394   8153   3911  -1080    616   2145       C  
ATOM   1563  CG AGLU A 216       4.960   3.530  26.742  0.50 54.77           C  
ANISOU 1563  CG AGLU A 216     5738   9758   5314  -1224    699   2248       C  
ATOM   1564  CG BGLU A 216       4.908   4.366  26.626  0.50 53.15           C  
ANISOU 1564  CG BGLU A 216     5491   9631   5073  -1154    685   2125       C  
ATOM   1565  CD AGLU A 216       4.712   2.033  26.797  0.50 73.25           C  
ANISOU 1565  CD AGLU A 216     8139  11957   7737  -1389    740   2468       C  
ATOM   1566  CD BGLU A 216       3.895   4.017  25.551  0.50 67.65           C  
ANISOU 1566  CD BGLU A 216     7289  11372   7041  -1293    697   2089       C  
ATOM   1567  OE1AGLU A 216       4.981   1.338  25.790  0.50 65.14           O  
ANISOU 1567  OE1AGLU A 216     7212  10656   6884  -1459    708   2465       O  
ATOM   1568  OE1BGLU A 216       4.196   4.211  24.351  0.50 55.68           O  
ANISOU 1568  OE1BGLU A 216     5827   9674   5657  -1272    638   1955       O  
ATOM   1569  OE2AGLU A 216       4.233   1.554  27.851  0.50 66.70           O  
ANISOU 1569  OE2AGLU A 216     7259  11289   6795  -1453    808   2643       O  
ATOM   1570  OE2BGLU A 216       2.786   3.561  25.913  0.50 59.77           O  
ANISOU 1570  OE2BGLU A 216     6201  10500   6008  -1427    765   2196       O  
ATOM   1571  N   ASN A 217       8.121   2.151  28.224  1.00 41.87           N  
ANISOU 1571  N   ASN A 217     4372   7918   3619  -1030    627   2576       N  
ATOM   1572  CA  ASN A 217       8.277   1.039  29.164  1.00 41.58           C  
ANISOU 1572  CA  ASN A 217     4377   7892   3529  -1074    670   2840       C  
ATOM   1573  C   ASN A 217       9.177   1.369  30.353  1.00 43.87           C  
ANISOU 1573  C   ASN A 217     4654   8376   3637   -935    651   2902       C  
ATOM   1574  O   ASN A 217       8.856   0.982  31.472  1.00 43.38           O  
ANISOU 1574  O   ASN A 217     4548   8499   3434   -965    706   3078       O  
ATOM   1575  CB  ASN A 217       8.742  -0.234  28.452  1.00 44.70           C  
ANISOU 1575  CB  ASN A 217     4920   7951   4114  -1132    657   2965       C  
ATOM   1576  CG  ASN A 217       7.705  -0.864  27.550  1.00 74.51           C  
ANISOU 1576  CG  ASN A 217     8708  11557   8045  -1312    692   2959       C  
ATOM   1577  OD1 ASN A 217       7.960  -1.126  26.372  1.00 70.98           O  
ANISOU 1577  OD1 ASN A 217     8345  10856   7767  -1329    651   2864       O  
ATOM   1578  ND2 ASN A 217       6.514  -1.139  28.080  1.00 67.80           N  
ANISOU 1578  ND2 ASN A 217     7771  10856   7135  -1456    768   3059       N  
ATOM   1579  N   ARG A 218      10.284   2.092  30.113  1.00 39.85           N  
ANISOU 1579  N   ARG A 218     4176   7842   3123   -793    572   2758       N  
ATOM   1580  CA  ARG A 218      11.249   2.489  31.142  1.00 39.47           C  
ANISOU 1580  CA  ARG A 218     4111   7983   2904   -662    537   2786       C  
ATOM   1581  C   ARG A 218      10.700   3.525  32.119  1.00 44.05           C  
ANISOU 1581  C   ARG A 218     4566   8902   3269   -633    567   2693       C  
ATOM   1582  O   ARG A 218      11.047   3.482  33.300  1.00 44.41           O  
ANISOU 1582  O   ARG A 218     4579   9161   3133   -580    576   2800       O  
ATOM   1583  CB  ARG A 218      12.559   2.968  30.505  1.00 39.03           C  
ANISOU 1583  CB  ARG A 218     4116   7798   2916   -539    444   2649       C  
ATOM   1584  CG  ARG A 218      13.391   1.823  29.957  1.00 46.27           C  
ANISOU 1584  CG  ARG A 218     5155   8442   3984   -521    417   2793       C  
ATOM   1585  CD  ARG A 218      14.691   2.297  29.350  1.00 53.61           C  
ANISOU 1585  CD  ARG A 218     6126   9272   4970   -399    331   2663       C  
ATOM   1586  NE  ARG A 218      15.424   1.188  28.740  1.00 62.04           N  
ANISOU 1586  NE  ARG A 218     7310  10069   6193   -373    313   2788       N  
ATOM   1587  CZ  ARG A 218      16.283   0.406  29.387  1.00 75.71           C  
ANISOU 1587  CZ  ARG A 218     9086  11798   7883   -291    301   2985       C  
ATOM   1588  NH1 ARG A 218      16.537   0.608  30.676  1.00 57.41           N  
ANISOU 1588  NH1 ARG A 218     6701   9749   5362   -235    300   3084       N  
ATOM   1589  NH2 ARG A 218      16.897  -0.583  28.752  1.00 64.66           N  
ANISOU 1589  NH2 ARG A 218     7798  10133   6638   -256    291   3084       N  
ATOM   1590  N   ALA A 219       9.843   4.447  31.627  1.00 41.01           N  
ANISOU 1590  N   ALA A 219     4111   8572   2900   -659    585   2494       N  
ATOM   1591  CA  ALA A 219       9.187   5.491  32.422  1.00 40.55           C  
ANISOU 1591  CA  ALA A 219     3937   8817   2654   -624    623   2378       C  
ATOM   1592  C   ALA A 219       8.181   4.853  33.364  1.00 43.35           C  
ANISOU 1592  C   ALA A 219     4214   9368   2887   -716    718   2569       C  
ATOM   1593  O   ALA A 219       8.070   5.282  34.513  1.00 43.75           O  
ANISOU 1593  O   ALA A 219     4190   9708   2727   -668    750   2577       O  
ATOM   1594  CB  ALA A 219       8.486   6.489  31.512  1.00 41.40           C  
ANISOU 1594  CB  ALA A 219     4000   8890   2839   -621    622   2140       C  
ATOM   1595  N   ASN A1002       7.470   3.805  32.884  1.00 38.55           N  
ANISOU 1595  N   ASN A1002     4511   6910   3225    239   -286   2305       N  
ATOM   1596  CA  ASN A1002       6.495   3.046  33.671  1.00 37.75           C  
ANISOU 1596  CA  ASN A1002     4448   6717   3179    261   -271   2085       C  
ATOM   1597  C   ASN A1002       7.165   2.307  34.837  1.00 39.44           C  
ANISOU 1597  C   ASN A1002     4823   6689   3472    332   -130   1804       C  
ATOM   1598  O   ASN A1002       6.637   2.351  35.944  1.00 38.99           O  
ANISOU 1598  O   ASN A1002     4783   6428   3604    415   -111   1716       O  
ATOM   1599  CB  ASN A1002       5.674   2.103  32.784  1.00 38.24           C  
ANISOU 1599  CB  ASN A1002     4497   7083   2950     95   -322   2001       C  
ATOM   1600  CG  ASN A1002       4.655   2.791  31.895  1.00 52.98           C  
ANISOU 1600  CG  ASN A1002     6162   9203   4765     22   -508   2303       C  
ATOM   1601  OD1 ASN A1002       4.381   2.349  30.776  1.00 47.43           O  
ANISOU 1601  OD1 ASN A1002     5436   8847   3739   -161   -584   2324       O  
ATOM   1602  ND2 ASN A1002       4.056   3.879  32.366  1.00 41.07           N  
ANISOU 1602  ND2 ASN A1002     4497   7534   3572    158   -585   2544       N  
ATOM   1603  N   ILE A1003       8.354   1.694  34.608  1.00 34.79           N  
ANISOU 1603  N   ILE A1003     4337   6133   2749    308    -24   1690       N  
ATOM   1604  CA  ILE A1003       9.137   1.028  35.660  1.00 34.35           C  
ANISOU 1604  CA  ILE A1003     4401   5870   2780    384     92   1494       C  
ATOM   1605  C   ILE A1003       9.600   2.099  36.669  1.00 38.22           C  
ANISOU 1605  C   ILE A1003     4869   6130   3523    482     55   1591       C  
ATOM   1606  O   ILE A1003       9.509   1.866  37.872  1.00 36.87           O  
ANISOU 1606  O   ILE A1003     4767   5777   3464    540     84   1462       O  
ATOM   1607  CB  ILE A1003      10.338   0.187  35.116  1.00 37.25           C  
ANISOU 1607  CB  ILE A1003     4835   6325   2992    361    226   1392       C  
ATOM   1608  CG1 ILE A1003       9.884  -0.855  34.066  1.00 37.38           C  
ANISOU 1608  CG1 ILE A1003     4907   6552   2744    238    286   1234       C  
ATOM   1609  CG2 ILE A1003      11.105  -0.499  36.273  1.00 37.86           C  
ANISOU 1609  CG2 ILE A1003     4996   6186   3205    459    323   1254       C  
ATOM   1610  CD1 ILE A1003      11.009  -1.467  33.205  1.00 41.03           C  
ANISOU 1610  CD1 ILE A1003     5412   7158   3021    207    445   1153       C  
ATOM   1611  N   PHE A1004      10.059   3.281  36.169  1.00 35.78           N  
ANISOU 1611  N   PHE A1004     4469   5833   3292    478     -9   1817       N  
ATOM   1612  CA  PHE A1004      10.498   4.398  37.014  1.00 35.58           C  
ANISOU 1612  CA  PHE A1004     4430   5572   3518    531    -48   1896       C  
ATOM   1613  C   PHE A1004       9.395   4.872  37.971  1.00 39.12           C  
ANISOU 1613  C   PHE A1004     4884   5825   4154    601    -74   1835       C  
ATOM   1614  O   PHE A1004       9.657   5.036  39.162  1.00 38.12           O  
ANISOU 1614  O   PHE A1004     4838   5503   4145    637    -48   1702       O  
ATOM   1615  CB  PHE A1004      11.065   5.559  36.177  1.00 37.18           C  
ANISOU 1615  CB  PHE A1004     4524   5810   3792    491   -107   2177       C  
ATOM   1616  CG  PHE A1004      11.500   6.768  36.979  1.00 38.75           C  
ANISOU 1616  CG  PHE A1004     4715   5729   4280    514   -149   2245       C  
ATOM   1617  CD1 PHE A1004      12.615   6.709  37.812  1.00 41.73           C  
ANISOU 1617  CD1 PHE A1004     5151   5992   4713    491   -127   2140       C  
ATOM   1618  CD2 PHE A1004      10.802   7.967  36.895  1.00 40.93           C  
ANISOU 1618  CD2 PHE A1004     4917   5847   4788    548   -212   2419       C  
ATOM   1619  CE1 PHE A1004      13.020   7.829  38.549  1.00 42.68           C  
ANISOU 1619  CE1 PHE A1004     5279   5857   5081    466   -176   2167       C  
ATOM   1620  CE2 PHE A1004      11.215   9.088  37.623  1.00 43.96           C  
ANISOU 1620  CE2 PHE A1004     5317   5926   5459    551   -230   2440       C  
ATOM   1621  CZ  PHE A1004      12.318   9.009  38.450  1.00 42.02           C  
ANISOU 1621  CZ  PHE A1004     5154   5583   5231    492   -216   2294       C  
ATOM   1622  N   GLU A1005       8.164   5.048  37.449  1.00 35.83           N  
ANISOU 1622  N   GLU A1005     4373   5490   3749    612   -121   1931       N  
ATOM   1623  CA  GLU A1005       6.992   5.459  38.220  1.00 35.58           C  
ANISOU 1623  CA  GLU A1005     4304   5303   3913    697   -115   1892       C  
ATOM   1624  C   GLU A1005       6.537   4.408  39.237  1.00 38.86           C  
ANISOU 1624  C   GLU A1005     4820   5688   4255    708    -30   1630       C  
ATOM   1625  O   GLU A1005       6.114   4.777  40.331  1.00 38.56           O  
ANISOU 1625  O   GLU A1005     4812   5467   4371    780     28   1526       O  
ATOM   1626  CB  GLU A1005       5.839   5.877  37.294  1.00 37.00           C  
ANISOU 1626  CB  GLU A1005     4302   5619   4136    706   -201   2122       C  
ATOM   1627  CG  GLU A1005       6.017   7.260  36.677  1.00 49.74           C  
ANISOU 1627  CG  GLU A1005     5795   7154   5948    740   -277   2433       C  
ATOM   1628  CD  GLU A1005       6.336   8.390  37.641  1.00 75.23           C  
ANISOU 1628  CD  GLU A1005     9062  10007   9515    838   -224   2408       C  
ATOM   1629  OE1 GLU A1005       5.593   8.564  38.636  1.00 74.16           O  
ANISOU 1629  OE1 GLU A1005     8942   9681   9556    937   -144   2251       O  
ATOM   1630  OE2 GLU A1005       7.338   9.102  37.401  1.00 68.06           O  
ANISOU 1630  OE2 GLU A1005     8171   8998   8691    800   -249   2531       O  
ATOM   1631  N   MET A1006       6.650   3.108  38.886  1.00 34.75           N  
ANISOU 1631  N   MET A1006     4361   5337   3507    632     -3   1521       N  
ATOM   1632  CA  MET A1006       6.284   1.967  39.732  1.00 34.09           C  
ANISOU 1632  CA  MET A1006     4372   5226   3355    622     78   1312       C  
ATOM   1633  C   MET A1006       7.167   1.911  40.986  1.00 37.09           C  
ANISOU 1633  C   MET A1006     4881   5434   3779    665    137   1194       C  
ATOM   1634  O   MET A1006       6.656   1.742  42.097  1.00 35.79           O  
ANISOU 1634  O   MET A1006     4767   5174   3656    694    195   1083       O  
ATOM   1635  CB  MET A1006       6.415   0.660  38.925  1.00 36.33           C  
ANISOU 1635  CB  MET A1006     4701   5681   3422    521    101   1230       C  
ATOM   1636  CG  MET A1006       5.717  -0.535  39.553  1.00 39.69           C  
ANISOU 1636  CG  MET A1006     5189   6080   3810    483    171   1063       C  
ATOM   1637  SD  MET A1006       6.403  -2.104  38.964  1.00 43.80           S  
ANISOU 1637  SD  MET A1006     5835   6655   4152    391    256    903       S  
ATOM   1638  CE  MET A1006       4.958  -3.161  39.096  1.00 40.19           C  
ANISOU 1638  CE  MET A1006     5375   6218   3678    279    279    782       C  
ATOM   1639  N   LEU A1007       8.489   2.062  40.791  1.00 33.42           N  
ANISOU 1639  N   LEU A1007     4450   4961   3288    654    118   1237       N  
ATOM   1640  CA  LEU A1007       9.500   2.015  41.845  1.00 33.12           C  
ANISOU 1640  CA  LEU A1007     4500   4813   3271    666    131   1169       C  
ATOM   1641  C   LEU A1007       9.556   3.296  42.681  1.00 37.35           C  
ANISOU 1641  C   LEU A1007     5048   5184   3961    681     95   1164       C  
ATOM   1642  O   LEU A1007      10.036   3.259  43.812  1.00 36.64           O  
ANISOU 1642  O   LEU A1007     5045   5020   3856    665     98   1066       O  
ATOM   1643  CB  LEU A1007      10.880   1.658  41.249  1.00 32.99           C  
ANISOU 1643  CB  LEU A1007     4470   4872   3192    646    129   1235       C  
ATOM   1644  CG  LEU A1007      11.295   0.160  41.172  1.00 37.46           C  
ANISOU 1644  CG  LEU A1007     5087   5496   3648    656    215   1157       C  
ATOM   1645  CD1 LEU A1007      11.651  -0.410  42.544  1.00 37.60           C  
ANISOU 1645  CD1 LEU A1007     5184   5419   3683    682    227   1093       C  
ATOM   1646  CD2 LEU A1007      10.278  -0.713  40.419  1.00 38.68           C  
ANISOU 1646  CD2 LEU A1007     5255   5740   3701    624    273   1080       C  
ATOM   1647  N   ARG A1008       9.041   4.415  42.138  1.00 34.77           N  
ANISOU 1647  N   ARG A1008     4635   4795   3780    704     63   1270       N  
ATOM   1648  CA  ARG A1008       8.960   5.713  42.816  1.00 34.92           C  
ANISOU 1648  CA  ARG A1008     4668   4597   4001    725     59   1244       C  
ATOM   1649  C   ARG A1008       7.892   5.641  43.924  1.00 38.90           C  
ANISOU 1649  C   ARG A1008     5232   5013   4536    780    156   1062       C  
ATOM   1650  O   ARG A1008       8.084   6.190  45.011  1.00 38.94           O  
ANISOU 1650  O   ARG A1008     5336   4868   4593    765    193    912       O  
ATOM   1651  CB  ARG A1008       8.601   6.801  41.796  1.00 36.18           C  
ANISOU 1651  CB  ARG A1008     4696   4701   4349    758     14   1457       C  
ATOM   1652  CG  ARG A1008       8.843   8.221  42.275  1.00 48.73           C  
ANISOU 1652  CG  ARG A1008     6303   6011   6201    764     11   1459       C  
ATOM   1653  CD  ARG A1008       8.514   9.199  41.172  1.00 58.97           C  
ANISOU 1653  CD  ARG A1008     7452   7248   7707    804    -38   1738       C  
ATOM   1654  NE  ARG A1008       8.511  10.576  41.657  1.00 70.75           N  
ANISOU 1654  NE  ARG A1008     8959   8397   9524    832    -10   1728       N  
ATOM   1655  CZ  ARG A1008       8.229  11.635  40.906  1.00 87.37           C  
ANISOU 1655  CZ  ARG A1008    10941  10354  11904    883    -38   1987       C  
ATOM   1656  NH1 ARG A1008       7.920  11.484  39.623  1.00 76.07           N  
ANISOU 1656  NH1 ARG A1008     9350   9142  10411    898   -118   2296       N  
ATOM   1657  NH2 ARG A1008       8.249  12.852  41.432  1.00 74.66           N  
ANISOU 1657  NH2 ARG A1008     9368   8371  10629    908     13   1942       N  
ATOM   1658  N   ILE A1009       6.779   4.943  43.634  1.00 35.03           N  
ANISOU 1658  N   ILE A1009     4677   4635   3996    821    204   1068       N  
ATOM   1659  CA  ILE A1009       5.655   4.719  44.541  1.00 34.61           C  
ANISOU 1659  CA  ILE A1009     4639   4547   3963    871    320    929       C  
ATOM   1660  C   ILE A1009       6.045   3.659  45.597  1.00 39.19           C  
ANISOU 1660  C   ILE A1009     5364   5190   4335    811    366    777       C  
ATOM   1661  O   ILE A1009       5.905   3.902  46.799  1.00 38.65           O  
ANISOU 1661  O   ILE A1009     5391   5047   4246    811    448    625       O  
ATOM   1662  CB  ILE A1009       4.396   4.306  43.709  1.00 37.32           C  
ANISOU 1662  CB  ILE A1009     4819   5021   4341    907    326   1038       C  
ATOM   1663  CG1 ILE A1009       3.890   5.482  42.831  1.00 37.26           C  
ANISOU 1663  CG1 ILE A1009     4640   4956   4563    982    269   1242       C  
ATOM   1664  CG2 ILE A1009       3.274   3.743  44.601  1.00 37.76           C  
ANISOU 1664  CG2 ILE A1009     4863   5088   4395    939    460    911       C  
ATOM   1665  CD1 ILE A1009       3.016   5.100  41.603  1.00 40.79           C  
ANISOU 1665  CD1 ILE A1009     4897   5621   4982    964    186   1435       C  
ATOM   1666  N   ASP A1010       6.552   2.502  45.131  1.00 36.24           N  
ANISOU 1666  N   ASP A1010     5008   4952   3810    758    323    827       N  
ATOM   1667  CA  ASP A1010       6.912   1.338  45.938  1.00 36.11           C  
ANISOU 1667  CA  ASP A1010     5099   4988   3632    713    357    758       C  
ATOM   1668  C   ASP A1010       8.174   1.486  46.786  1.00 41.96           C  
ANISOU 1668  C   ASP A1010     5943   5697   4303    674    305    731       C  
ATOM   1669  O   ASP A1010       8.162   1.056  47.942  1.00 41.22           O  
ANISOU 1669  O   ASP A1010     5942   5620   4099    643    344    655       O  
ATOM   1670  CB  ASP A1010       7.012   0.086  45.049  1.00 37.52           C  
ANISOU 1670  CB  ASP A1010     5255   5268   3733    683    349    815       C  
ATOM   1671  CG  ASP A1010       5.678  -0.448  44.543  1.00 44.57           C  
ANISOU 1671  CG  ASP A1010     6069   6229   4635    663    394    808       C  
ATOM   1672  OD1 ASP A1010       4.620   0.006  45.043  1.00 45.08           O  
ANISOU 1672  OD1 ASP A1010     6082   6276   4770    690    450    776       O  
ATOM   1673  OD2 ASP A1010       5.689  -1.328  43.662  1.00 47.65           O  
ANISOU 1673  OD2 ASP A1010     6445   6695   4965    611    382    822       O  
ATOM   1674  N   GLU A1011       9.263   2.041  46.228  1.00 40.24           N  
ANISOU 1674  N   GLU A1011     5694   5465   4131    656    210    813       N  
ATOM   1675  CA  GLU A1011      10.512   2.176  46.982  1.00 41.27           C  
ANISOU 1675  CA  GLU A1011     5881   5597   4205    594    130    815       C  
ATOM   1676  C   GLU A1011      10.706   3.573  47.568  1.00 47.57           C  
ANISOU 1676  C   GLU A1011     6721   6273   5079    540     90    725       C  
ATOM   1677  O   GLU A1011      11.073   3.693  48.735  1.00 47.98           O  
ANISOU 1677  O   GLU A1011     6874   6334   5025    463     68    619       O  
ATOM   1678  CB  GLU A1011      11.727   1.752  46.131  1.00 42.79           C  
ANISOU 1678  CB  GLU A1011     5994   5857   4405    593     65    962       C  
ATOM   1679  CG  GLU A1011      12.971   1.403  46.932  1.00 55.47           C  
ANISOU 1679  CG  GLU A1011     7613   7518   5946    543    -17   1015       C  
ATOM   1680  CD  GLU A1011      13.055  -0.051  47.351  1.00 84.37           C  
ANISOU 1680  CD  GLU A1011    11299  11244   9514    583     26   1060       C  
ATOM   1681  OE1 GLU A1011      13.393  -0.898  46.491  1.00 82.27           O  
ANISOU 1681  OE1 GLU A1011    10972  10998   9289    650     79   1138       O  
ATOM   1682  OE2 GLU A1011      12.773  -0.348  48.536  1.00 79.99           O  
ANISOU 1682  OE2 GLU A1011    10831  10713   8849    545     20   1016       O  
ATOM   1683  N   GLY A1012      10.479   4.600  46.754  1.00 45.25           N  
ANISOU 1683  N   GLY A1012     6357   5870   4966    565     81    771       N  
ATOM   1684  CA  GLY A1012      10.658   5.993  47.147  1.00 45.51           C  
ANISOU 1684  CA  GLY A1012     6428   5720   5143    515     59    687       C  
ATOM   1685  C   GLY A1012      11.835   6.639  46.444  1.00 50.12           C  
ANISOU 1685  C   GLY A1012     6940   6266   5837    442    -57    832       C  
ATOM   1686  O   GLY A1012      12.850   5.982  46.188  1.00 49.51           O  
ANISOU 1686  O   GLY A1012     6814   6333   5664    398   -132    944       O  
ATOM   1687  N   LEU A1013      11.701   7.934  46.120  1.00 47.23           N  
ANISOU 1687  N   LEU A1013     6550   5692   5701    435    -57    848       N  
ATOM   1688  CA  LEU A1013      12.738   8.705  45.437  1.00 47.11           C  
ANISOU 1688  CA  LEU A1013     6459   5611   5832    347   -155   1008       C  
ATOM   1689  C   LEU A1013      13.313   9.779  46.360  1.00 51.76           C  
ANISOU 1689  C   LEU A1013     7149   5992   6526    198   -204    845       C  
ATOM   1690  O   LEU A1013      12.567  10.612  46.877  1.00 51.64           O  
ANISOU 1690  O   LEU A1013     7225   5745   6651    219   -117    665       O  
ATOM   1691  CB  LEU A1013      12.177   9.322  44.135  1.00 47.00           C  
ANISOU 1691  CB  LEU A1013     6320   5518   6021    436   -130   1222       C  
ATOM   1692  CG  LEU A1013      13.119  10.192  43.290  1.00 51.37           C  
ANISOU 1692  CG  LEU A1013     6774   6008   6739    347   -213   1450       C  
ATOM   1693  CD1 LEU A1013      14.199   9.360  42.634  1.00 51.53           C  
ANISOU 1693  CD1 LEU A1013     6697   6305   6577    306   -262   1616       C  
ATOM   1694  CD2 LEU A1013      12.350  10.932  42.221  1.00 53.07           C  
ANISOU 1694  CD2 LEU A1013     6886   6101   7179    436   -187   1662       C  
ATOM   1695  N   ARG A1014      14.639   9.748  46.565  1.00 48.73           N  
ANISOU 1695  N   ARG A1014     6739   5693   6083     40   -335    897       N  
ATOM   1696  CA  ARG A1014      15.353  10.707  47.411  1.00 48.79           C  
ANISOU 1696  CA  ARG A1014     6834   5543   6163   -165   -421    743       C  
ATOM   1697  C   ARG A1014      16.339  11.496  46.552  1.00 53.06           C  
ANISOU 1697  C   ARG A1014     7241   6001   6917   -278   -517    965       C  
ATOM   1698  O   ARG A1014      17.219  10.905  45.919  1.00 52.40           O  
ANISOU 1698  O   ARG A1014     7009   6138   6761   -296   -587   1187       O  
ATOM   1699  CB  ARG A1014      16.072  10.001  48.585  1.00 49.20           C  
ANISOU 1699  CB  ARG A1014     6954   5809   5930   -300   -525    618       C  
ATOM   1700  CG  ARG A1014      15.149   9.358  49.626  1.00 59.39           C  
ANISOU 1700  CG  ARG A1014     8397   7176   6993   -236   -429    395       C  
ATOM   1701  CD  ARG A1014      14.943   7.877  49.353  1.00 73.15           C  
ANISOU 1701  CD  ARG A1014    10068   9170   8555    -87   -398    547       C  
ATOM   1702  NE  ARG A1014      14.156   7.214  50.393  1.00 82.82           N  
ANISOU 1702  NE  ARG A1014    11425  10487   9556    -57   -316    377       N  
ATOM   1703  CZ  ARG A1014      13.755   5.947  50.338  1.00 97.42           C  
ANISOU 1703  CZ  ARG A1014    13247  12502  11267     60   -261    471       C  
ATOM   1704  NH1 ARG A1014      14.050   5.193  49.285  1.00 84.59           N  
ANISOU 1704  NH1 ARG A1014    11484  10958   9700    164   -269    690       N  
ATOM   1705  NH2 ARG A1014      13.044   5.427  51.329  1.00 85.57           N  
ANISOU 1705  NH2 ARG A1014    11862  11080   9570     64   -182    336       N  
ATOM   1706  N   LEU A1015      16.174  12.826  46.507  1.00 50.21           N  
ANISOU 1706  N   LEU A1015     6924   5307   6845   -348   -496    914       N  
ATOM   1707  CA  LEU A1015      17.019  13.703  45.695  1.00 50.30           C  
ANISOU 1707  CA  LEU A1015     6813   5195   7105   -473   -574   1147       C  
ATOM   1708  C   LEU A1015      18.314  14.148  46.400  1.00 55.85           C  
ANISOU 1708  C   LEU A1015     7523   5893   7803   -767   -735   1068       C  
ATOM   1709  O   LEU A1015      19.176  14.764  45.765  1.00 55.51           O  
ANISOU 1709  O   LEU A1015     7347   5800   7946   -903   -812   1288       O  
ATOM   1710  CB  LEU A1015      16.219  14.912  45.166  1.00 50.19           C  
ANISOU 1710  CB  LEU A1015     6816   4793   7460   -405   -478   1197       C  
ATOM   1711  CG  LEU A1015      15.059  14.625  44.188  1.00 54.31           C  
ANISOU 1711  CG  LEU A1015     7252   5350   8034   -141   -364   1393       C  
ATOM   1712  CD1 LEU A1015      14.423  15.914  43.722  1.00 54.24           C  
ANISOU 1712  CD1 LEU A1015     7235   4935   8439    -78   -289   1482       C  
ATOM   1713  CD2 LEU A1015      15.520  13.823  42.968  1.00 56.32           C  
ANISOU 1713  CD2 LEU A1015     7321   5936   8144    -96   -411   1742       C  
ATOM   1714  N   LYS A1016      18.463  13.806  47.692  1.00 53.57           N  
ANISOU 1714  N   LYS A1016     7375   5694   7287   -882   -794    780       N  
ATOM   1715  CA  LYS A1016      19.651  14.116  48.490  1.00 54.03           C  
ANISOU 1715  CA  LYS A1016     7436   5814   7277  -1191   -982    690       C  
ATOM   1716  C   LYS A1016      20.252  12.825  49.073  1.00 58.75           C  
ANISOU 1716  C   LYS A1016     7966   6834   7522  -1202  -1096    739       C  
ATOM   1717  O   LYS A1016      19.511  11.868  49.327  1.00 58.39           O  
ANISOU 1717  O   LYS A1016     7977   6939   7268  -1006  -1004    693       O  
ATOM   1718  CB  LYS A1016      19.323  15.135  49.595  1.00 56.88           C  
ANISOU 1718  CB  LYS A1016     8042   5874   7696  -1385   -971    284       C  
ATOM   1719  CG  LYS A1016      20.541  15.914  50.081  1.00 76.08           C  
ANISOU 1719  CG  LYS A1016    10461   8229  10216  -1761  -1167    222       C  
ATOM   1720  CD  LYS A1016      20.165  17.070  50.993  1.00 88.59           C  
ANISOU 1720  CD  LYS A1016    12313   9438  11907  -1960  -1116   -219       C  
ATOM   1721  CE  LYS A1016      21.370  17.908  51.350  1.00100.95           C  
ANISOU 1721  CE  LYS A1016    13865  10905  13588  -2374  -1322   -283       C  
ATOM   1722  NZ  LYS A1016      21.001  19.094  52.168  1.00110.50           N  
ANISOU 1722  NZ  LYS A1016    15361  11695  14929  -2586  -1247   -760       N  
ATOM   1723  N   ILE A1017      21.597  12.799  49.268  1.00 55.58           N  
ANISOU 1723  N   ILE A1017     7419   6614   7084  -1431  -1298    864       N  
ATOM   1724  CA  ILE A1017      22.352  11.655  49.806  1.00 55.19           C  
ANISOU 1724  CA  ILE A1017     7251   6957   6762  -1452  -1434    981       C  
ATOM   1725  C   ILE A1017      21.802  11.204  51.173  1.00 58.58           C  
ANISOU 1725  C   ILE A1017     7893   7495   6869  -1493  -1461    700       C  
ATOM   1726  O   ILE A1017      21.632  12.026  52.077  1.00 58.72           O  
ANISOU 1726  O   ILE A1017     8105   7376   6830  -1719  -1512    391       O  
ATOM   1727  CB  ILE A1017      23.894  11.926  49.827  1.00 58.17           C  
ANISOU 1727  CB  ILE A1017     7396   7493   7212  -1717  -1660   1183       C  
ATOM   1728  CG1 ILE A1017      24.474  11.948  48.388  1.00 58.68           C  
ANISOU 1728  CG1 ILE A1017     7199   7570   7526  -1611  -1589   1539       C  
ATOM   1729  CG2 ILE A1017      24.641  10.904  50.699  1.00 58.65           C  
ANISOU 1729  CG2 ILE A1017     7346   7942   6999  -1778  -1839   1278       C  
ATOM   1730  CD1 ILE A1017      26.001  12.248  48.234  1.00 65.76           C  
ANISOU 1730  CD1 ILE A1017     7814   8615   8556  -1863  -1775   1783       C  
ATOM   1731  N   TYR A1018      21.508   9.898  51.293  1.00 54.04           N  
ANISOU 1731  N   TYR A1018     7289   7156   6086  -1282  -1408    804       N  
ATOM   1732  CA  TYR A1018      20.990   9.258  52.505  1.00 53.43           C  
ANISOU 1732  CA  TYR A1018     7382   7237   5681  -1294  -1417    623       C  
ATOM   1733  C   TYR A1018      21.711   7.922  52.788  1.00 56.96           C  
ANISOU 1733  C   TYR A1018     7659   8043   5941  -1235  -1538    900       C  
ATOM   1734  O   TYR A1018      22.508   7.466  51.967  1.00 55.83           O  
ANISOU 1734  O   TYR A1018     7269   7994   5950  -1139  -1567   1202       O  
ATOM   1735  CB  TYR A1018      19.459   9.064  52.404  1.00 54.18           C  
ANISOU 1735  CB  TYR A1018     7658   7169   5761  -1057  -1162    446       C  
ATOM   1736  CG  TYR A1018      19.015   8.008  51.411  1.00 55.22           C  
ANISOU 1736  CG  TYR A1018     7667   7359   5954   -753  -1024    679       C  
ATOM   1737  CD1 TYR A1018      18.960   8.282  50.047  1.00 56.94           C  
ANISOU 1737  CD1 TYR A1018     7761   7440   6434   -620   -936    838       C  
ATOM   1738  CD2 TYR A1018      18.617   6.744  51.839  1.00 55.76           C  
ANISOU 1738  CD2 TYR A1018     7759   7619   5809   -619   -976    733       C  
ATOM   1739  CE1 TYR A1018      18.555   7.314  49.131  1.00 57.37           C  
ANISOU 1739  CE1 TYR A1018     7725   7568   6504   -379   -810   1007       C  
ATOM   1740  CE2 TYR A1018      18.205   5.769  50.932  1.00 56.52           C  
ANISOU 1740  CE2 TYR A1018     7764   7740   5971   -372   -843    904       C  
ATOM   1741  CZ  TYR A1018      18.167   6.063  49.579  1.00 63.82           C  
ANISOU 1741  CZ  TYR A1018     8578   8544   7127   -260   -761   1018       C  
ATOM   1742  OH  TYR A1018      17.748   5.118  48.675  1.00 65.79           O  
ANISOU 1742  OH  TYR A1018     8759   8835   7404    -52   -632   1143       O  
ATOM   1743  N   LYS A1019      21.426   7.300  53.943  1.00 54.11           N  
ANISOU 1743  N   LYS A1019     7421   7877   5262  -1286  -1590    813       N  
ATOM   1744  CA  LYS A1019      22.016   6.015  54.313  1.00 54.01           C  
ANISOU 1744  CA  LYS A1019     7252   8177   5090  -1217  -1702   1106       C  
ATOM   1745  C   LYS A1019      20.968   4.907  54.221  1.00 58.86           C  
ANISOU 1745  C   LYS A1019     7950   8783   5630   -937  -1494   1134       C  
ATOM   1746  O   LYS A1019      19.848   5.079  54.715  1.00 58.63           O  
ANISOU 1746  O   LYS A1019     8150   8662   5463   -925  -1357    875       O  
ATOM   1747  CB  LYS A1019      22.619   6.066  55.725  1.00 55.90           C  
ANISOU 1747  CB  LYS A1019     7533   8701   5005  -1518  -1961   1071       C  
ATOM   1748  CG  LYS A1019      23.922   6.846  55.827  1.00 65.60           C  
ANISOU 1748  CG  LYS A1019     8593  10028   6305  -1816  -2228   1146       C  
ATOM   1749  CD  LYS A1019      24.435   6.836  57.259  1.00 75.21           C  
ANISOU 1749  CD  LYS A1019     9857  11577   7141  -2140  -2507   1108       C  
ATOM   1750  CE  LYS A1019      25.679   7.667  57.443  1.00 84.93           C  
ANISOU 1750  CE  LYS A1019    10920  12926   8426  -2491  -2802   1162       C  
ATOM   1751  NZ  LYS A1019      26.188   7.594  58.838  1.00 93.37           N  
ANISOU 1751  NZ  LYS A1019    12027  14375   9074  -2837  -3105   1137       N  
ATOM   1752  N   ASP A1020      21.333   3.768  53.597  1.00 55.76           N  
ANISOU 1752  N   ASP A1020     7364   8474   5347   -719  -1456   1441       N  
ATOM   1753  CA  ASP A1020      20.448   2.604  53.470  1.00 55.82           C  
ANISOU 1753  CA  ASP A1020     7432   8459   5319   -476  -1270   1493       C  
ATOM   1754  C   ASP A1020      20.403   1.779  54.780  1.00 60.02           C  
ANISOU 1754  C   ASP A1020     8026   9221   5559   -535  -1366   1585       C  
ATOM   1755  O   ASP A1020      21.002   2.194  55.778  1.00 59.18           O  
ANISOU 1755  O   ASP A1020     7939   9312   5236   -781  -1579   1570       O  
ATOM   1756  CB  ASP A1020      20.827   1.743  52.239  1.00 57.58           C  
ANISOU 1756  CB  ASP A1020     7453   8631   5795   -229  -1155   1735       C  
ATOM   1757  CG  ASP A1020      22.181   1.039  52.249  1.00 67.14           C  
ANISOU 1757  CG  ASP A1020     8391  10023   7096   -199  -1291   2074       C  
ATOM   1758  OD1 ASP A1020      22.764   0.870  53.344  1.00 67.68           O  
ANISOU 1758  OD1 ASP A1020     8408  10306   7002   -353  -1507   2198       O  
ATOM   1759  OD2 ASP A1020      22.646   0.637  51.161  1.00 73.36           O  
ANISOU 1759  OD2 ASP A1020     9008  10755   8112    -19  -1174   2223       O  
ATOM   1760  N   THR A1021      19.712   0.612  54.771  1.00 57.16           N  
ANISOU 1760  N   THR A1021     7691   8842   5184   -335  -1218   1693       N  
ATOM   1761  CA  THR A1021      19.596  -0.280  55.941  1.00 57.25           C  
ANISOU 1761  CA  THR A1021     7750   9059   4945   -368  -1284   1846       C  
ATOM   1762  C   THR A1021      20.962  -0.784  56.442  1.00 60.94           C  
ANISOU 1762  C   THR A1021     7989   9776   5390   -433  -1538   2210       C  
ATOM   1763  O   THR A1021      21.133  -0.970  57.646  1.00 60.67           O  
ANISOU 1763  O   THR A1021     7995   9997   5061   -595  -1705   2313       O  
ATOM   1764  CB  THR A1021      18.609  -1.432  55.686  1.00 65.24           C  
ANISOU 1764  CB  THR A1021     8818   9947   6021   -144  -1059   1907       C  
ATOM   1765  OG1 THR A1021      18.899  -2.054  54.432  1.00 65.50           O  
ANISOU 1765  OG1 THR A1021     8693   9815   6381     77   -948   2043       O  
ATOM   1766  CG2 THR A1021      17.157  -0.978  55.726  1.00 63.28           C  
ANISOU 1766  CG2 THR A1021     8794   9564   5685   -145   -857   1580       C  
ATOM   1767  N   GLU A1022      21.933  -0.966  55.524  1.00 57.46           N  
ANISOU 1767  N   GLU A1022     7295   9286   5250   -314  -1566   2415       N  
ATOM   1768  CA  GLU A1022      23.298  -1.410  55.829  1.00 57.16           C  
ANISOU 1768  CA  GLU A1022     6969   9470   5278   -337  -1790   2796       C  
ATOM   1769  C   GLU A1022      24.218  -0.239  56.233  1.00 59.83           C  
ANISOU 1769  C   GLU A1022     7222   9999   5513   -645  -2066   2753       C  
ATOM   1770  O   GLU A1022      25.374  -0.465  56.592  1.00 59.47           O  
ANISOU 1770  O   GLU A1022     6916  10192   5489   -719  -2301   3074       O  
ATOM   1771  CB  GLU A1022      23.898  -2.174  54.637  1.00 58.73           C  
ANISOU 1771  CB  GLU A1022     6920   9526   5870    -48  -1643   3026       C  
ATOM   1772  CG  GLU A1022      23.374  -3.589  54.462  1.00 70.52           C  
ANISOU 1772  CG  GLU A1022     8433  10882   7480    222  -1441   3176       C  
ATOM   1773  CD  GLU A1022      24.042  -4.358  53.338  1.00 94.88           C  
ANISOU 1773  CD  GLU A1022    11279  13822  10948    499  -1276   3372       C  
ATOM   1774  OE1 GLU A1022      23.847  -3.983  52.160  1.00 92.41           O  
ANISOU 1774  OE1 GLU A1022    10986  13337  10789    584  -1088   3171       O  
ATOM   1775  OE2 GLU A1022      24.763  -5.337  53.636  1.00 91.59           O  
ANISOU 1775  OE2 GLU A1022    10653  13468  10678    636  -1324   3735       O  
ATOM   1776  N   GLY A1023      23.695   0.986  56.166  1.00 55.55           N  
ANISOU 1776  N   GLY A1023     6884   9336   4886   -823  -2035   2370       N  
ATOM   1777  CA  GLY A1023      24.413   2.204  56.523  1.00 54.88           C  
ANISOU 1777  CA  GLY A1023     6773   9359   4721  -1151  -2268   2248       C  
ATOM   1778  C   GLY A1023      25.237   2.834  55.414  1.00 58.15           C  
ANISOU 1778  C   GLY A1023     6968   9654   5472  -1144  -2273   2311       C  
ATOM   1779  O   GLY A1023      25.945   3.814  55.666  1.00 57.94           O  
ANISOU 1779  O   GLY A1023     6886   9704   5425  -1435  -2477   2244       O  
ATOM   1780  N   TYR A1024      25.162   2.289  54.177  1.00 53.51           N  
ANISOU 1780  N   TYR A1024     6259   8888   5185   -837  -2043   2433       N  
ATOM   1781  CA  TYR A1024      25.931   2.807  53.038  1.00 52.66           C  
ANISOU 1781  CA  TYR A1024     5932   8693   5382   -809  -2004   2523       C  
ATOM   1782  C   TYR A1024      25.249   3.999  52.370  1.00 54.85           C  
ANISOU 1782  C   TYR A1024     6403   8701   5736   -883  -1875   2206       C  
ATOM   1783  O   TYR A1024      24.021   4.017  52.260  1.00 54.45           O  
ANISOU 1783  O   TYR A1024     6607   8469   5612   -784  -1697   1965       O  
ATOM   1784  CB  TYR A1024      26.202   1.714  51.986  1.00 53.88           C  
ANISOU 1784  CB  TYR A1024     5881   8799   5792   -464  -1792   2772       C  
ATOM   1785  CG  TYR A1024      26.834   0.431  52.490  1.00 55.87           C  
ANISOU 1785  CG  TYR A1024     5923   9239   6068   -316  -1861   3121       C  
ATOM   1786  CD1 TYR A1024      28.018   0.452  53.225  1.00 58.01           C  
ANISOU 1786  CD1 TYR A1024     5929   9792   6319   -482  -2152   3403       C  
ATOM   1787  CD2 TYR A1024      26.302  -0.809  52.150  1.00 56.68           C  
ANISOU 1787  CD2 TYR A1024     6059   9224   6255    -10  -1634   3195       C  
ATOM   1788  CE1 TYR A1024      28.625  -0.727  53.656  1.00 58.98           C  
ANISOU 1788  CE1 TYR A1024     5819  10080   6513   -319  -2219   3785       C  
ATOM   1789  CE2 TYR A1024      26.901  -1.995  52.574  1.00 57.74           C  
ANISOU 1789  CE2 TYR A1024     5987   9475   6478    150  -1677   3545       C  
ATOM   1790  CZ  TYR A1024      28.061  -1.949  53.328  1.00 65.13           C  
ANISOU 1790  CZ  TYR A1024     6648  10693   7404     10  -1969   3859       C  
ATOM   1791  OH  TYR A1024      28.655  -3.118  53.735  1.00 66.54           O  
ANISOU 1791  OH  TYR A1024     6592  10980   7709    191  -2015   4257       O  
ATOM   1792  N   TYR A1025      26.050   4.975  51.890  1.00 50.38           N  
ANISOU 1792  N   TYR A1025     5689   8106   5349  -1050  -1961   2241       N  
ATOM   1793  CA  TYR A1025      25.548   6.165  51.192  1.00 49.72           C  
ANISOU 1793  CA  TYR A1025     5746   7748   5400  -1125  -1854   2014       C  
ATOM   1794  C   TYR A1025      24.897   5.815  49.857  1.00 51.24           C  
ANISOU 1794  C   TYR A1025     5945   7769   5755   -827  -1567   2042       C  
ATOM   1795  O   TYR A1025      25.497   5.145  49.013  1.00 50.04           O  
ANISOU 1795  O   TYR A1025     5565   7703   5745   -656  -1475   2286       O  
ATOM   1796  CB  TYR A1025      26.624   7.249  51.051  1.00 51.20           C  
ANISOU 1796  CB  TYR A1025     5760   7948   5747  -1412  -2033   2084       C  
ATOM   1797  CG  TYR A1025      27.075   7.815  52.380  1.00 53.37           C  
ANISOU 1797  CG  TYR A1025     6097   8358   5824  -1778  -2325   1956       C  
ATOM   1798  CD1 TYR A1025      26.327   8.788  53.036  1.00 55.34           C  
ANISOU 1798  CD1 TYR A1025     6665   8410   5951  -1987  -2339   1565       C  
ATOM   1799  CD2 TYR A1025      28.243   7.369  52.989  1.00 54.58           C  
ANISOU 1799  CD2 TYR A1025     5984   8847   5909  -1921  -2584   2221       C  
ATOM   1800  CE1 TYR A1025      26.729   9.302  54.268  1.00 56.76           C  
ANISOU 1800  CE1 TYR A1025     6932   8730   5905  -2358  -2596   1396       C  
ATOM   1801  CE2 TYR A1025      28.655   7.874  54.223  1.00 55.67           C  
ANISOU 1801  CE2 TYR A1025     6180   9160   5814  -2301  -2882   2101       C  
ATOM   1802  CZ  TYR A1025      27.896   8.845  54.856  1.00 63.79           C  
ANISOU 1802  CZ  TYR A1025     7563   9994   6682  -2532  -2884   1664       C  
ATOM   1803  OH  TYR A1025      28.294   9.356  56.066  1.00 66.64           O  
ANISOU 1803  OH  TYR A1025     8010  10539   6772  -2938  -3167   1495       O  
ATOM   1804  N   THR A1026      23.633   6.239  49.716  1.00 46.92           N  
ANISOU 1804  N   THR A1026     5658   6997   5171   -769  -1422   1783       N  
ATOM   1805  CA  THR A1026      22.724   5.962  48.605  1.00 45.93           C  
ANISOU 1805  CA  THR A1026     5589   6726   5134   -524  -1177   1763       C  
ATOM   1806  C   THR A1026      22.062   7.280  48.105  1.00 48.68           C  
ANISOU 1806  C   THR A1026     6063   6810   5622   -598  -1115   1604       C  
ATOM   1807  O   THR A1026      22.146   8.306  48.782  1.00 47.81           O  
ANISOU 1807  O   THR A1026     6056   6583   5529   -820  -1228   1441       O  
ATOM   1808  CB  THR A1026      21.686   4.913  49.114  1.00 52.18           C  
ANISOU 1808  CB  THR A1026     6548   7536   5743   -353  -1070   1654       C  
ATOM   1809  OG1 THR A1026      22.351   3.891  49.860  1.00 50.09           O  
ANISOU 1809  OG1 THR A1026     6190   7485   5356   -343  -1177   1806       O  
ATOM   1810  CG2 THR A1026      20.904   4.257  48.008  1.00 50.67           C  
ANISOU 1810  CG2 THR A1026     6363   7277   5614   -105   -847   1682       C  
ATOM   1811  N   ILE A1027      21.423   7.237  46.910  1.00 45.00           N  
ANISOU 1811  N   ILE A1027     5586   6251   5262   -419   -936   1660       N  
ATOM   1812  CA  ILE A1027      20.694   8.340  46.263  1.00 44.63           C  
ANISOU 1812  CA  ILE A1027     5621   5962   5375   -432   -860   1594       C  
ATOM   1813  C   ILE A1027      19.641   7.773  45.280  1.00 48.09           C  
ANISOU 1813  C   ILE A1027     6088   6390   5794   -197   -675   1622       C  
ATOM   1814  O   ILE A1027      19.751   6.611  44.887  1.00 47.81           O  
ANISOU 1814  O   ILE A1027     5978   6530   5658    -57   -600   1715       O  
ATOM   1815  CB  ILE A1027      21.665   9.378  45.611  1.00 47.82           C  
ANISOU 1815  CB  ILE A1027     5866   6305   5997   -599   -934   1772       C  
ATOM   1816  CG1 ILE A1027      20.983  10.748  45.405  1.00 47.92           C  
ANISOU 1816  CG1 ILE A1027     5996   5995   6216   -674   -906   1680       C  
ATOM   1817  CG2 ILE A1027      22.314   8.850  44.319  1.00 49.06           C  
ANISOU 1817  CG2 ILE A1027     5796   6647   6197   -489   -845   2060       C  
ATOM   1818  CD1 ILE A1027      21.770  11.914  45.849  1.00 52.37           C  
ANISOU 1818  CD1 ILE A1027     6544   6400   6953   -956  -1049   1653       C  
ATOM   1819  N   GLY A1028      18.644   8.589  44.915  1.00 44.28           N  
ANISOU 1819  N   GLY A1028     5706   5699   5418   -165   -607   1541       N  
ATOM   1820  CA  GLY A1028      17.576   8.237  43.981  1.00 43.60           C  
ANISOU 1820  CA  GLY A1028     5631   5616   5319     16   -471   1582       C  
ATOM   1821  C   GLY A1028      16.690   7.115  44.475  1.00 46.56           C  
ANISOU 1821  C   GLY A1028     6106   6077   5508    146   -395   1437       C  
ATOM   1822  O   GLY A1028      16.153   7.193  45.581  1.00 46.29           O  
ANISOU 1822  O   GLY A1028     6209   5961   5418    124   -400   1237       O  
ATOM   1823  N   ILE A1029      16.545   6.058  43.658  1.00 42.72           N  
ANISOU 1823  N   ILE A1029     5556   5755   4920    267   -310   1528       N  
ATOM   1824  CA  ILE A1029      15.790   4.851  44.010  1.00 42.27           C  
ANISOU 1824  CA  ILE A1029     5578   5773   4710    375   -231   1419       C  
ATOM   1825  C   ILE A1029      16.808   3.723  44.290  1.00 45.95           C  
ANISOU 1825  C   ILE A1029     5983   6388   5089    397   -237   1483       C  
ATOM   1826  O   ILE A1029      17.154   2.953  43.389  1.00 45.42           O  
ANISOU 1826  O   ILE A1029     5831   6427   5001    475   -151   1574       O  
ATOM   1827  CB  ILE A1029      14.693   4.451  42.960  1.00 45.11           C  
ANISOU 1827  CB  ILE A1029     5932   6170   5037    477   -126   1433       C  
ATOM   1828  CG1 ILE A1029      13.745   5.631  42.632  1.00 45.26           C  
ANISOU 1828  CG1 ILE A1029     5957   6046   5194    476   -134   1444       C  
ATOM   1829  CG2 ILE A1029      13.895   3.219  43.434  1.00 45.35           C  
ANISOU 1829  CG2 ILE A1029     6048   6247   4937    551    -49   1306       C  
ATOM   1830  CD1 ILE A1029      12.896   5.464  41.379  1.00 49.89           C  
ANISOU 1830  CD1 ILE A1029     6474   6726   5755    535    -87   1554       C  
ATOM   1831  N   GLY A1030      17.308   3.690  45.526  1.00 42.57           N  
ANISOU 1831  N   GLY A1030     5590   5969   4617    322   -337   1441       N  
ATOM   1832  CA  GLY A1030      18.254   2.690  46.018  1.00 42.68           C  
ANISOU 1832  CA  GLY A1030     5524   6114   4577    345   -374   1545       C  
ATOM   1833  C   GLY A1030      19.548   2.510  45.242  1.00 47.22           C  
ANISOU 1833  C   GLY A1030     5894   6795   5252    364   -373   1745       C  
ATOM   1834  O   GLY A1030      20.037   1.382  45.123  1.00 46.78           O  
ANISOU 1834  O   GLY A1030     5753   6822   5200    478   -304   1839       O  
ATOM   1835  N   HIS A1031      20.120   3.615  44.720  1.00 44.19           N  
ANISOU 1835  N   HIS A1031     5418   6395   4976    257   -430   1821       N  
ATOM   1836  CA  HIS A1031      21.373   3.581  43.961  1.00 44.10           C  
ANISOU 1836  CA  HIS A1031     5183   6504   5067    255   -414   2028       C  
ATOM   1837  C   HIS A1031      22.588   3.746  44.886  1.00 49.38           C  
ANISOU 1837  C   HIS A1031     5713   7263   5786    126   -593   2144       C  
ATOM   1838  O   HIS A1031      22.877   4.863  45.323  1.00 49.48           O  
ANISOU 1838  O   HIS A1031     5733   7220   5848    -72   -745   2123       O  
ATOM   1839  CB  HIS A1031      21.371   4.631  42.831  1.00 44.58           C  
ANISOU 1839  CB  HIS A1031     5192   6529   5218    194   -373   2103       C  
ATOM   1840  CG  HIS A1031      22.599   4.591  41.977  1.00 47.89           C  
ANISOU 1840  CG  HIS A1031     5374   7097   5724    188   -318   2321       C  
ATOM   1841  ND1 HIS A1031      22.686   3.757  40.876  1.00 49.59           N  
ANISOU 1841  ND1 HIS A1031     5516   7439   5888    335   -116   2374       N  
ATOM   1842  CD2 HIS A1031      23.763   5.270  42.105  1.00 49.55           C  
ANISOU 1842  CD2 HIS A1031     5403   7357   6065     39   -428   2484       C  
ATOM   1843  CE1 HIS A1031      23.891   3.957  40.370  1.00 49.00           C  
ANISOU 1843  CE1 HIS A1031     5212   7492   5912    295    -86   2573       C  
ATOM   1844  NE2 HIS A1031      24.575   4.861  41.074  1.00 49.30           N  
ANISOU 1844  NE2 HIS A1031     5165   7494   6074    114   -279   2663       N  
ATOM   1845  N   LEU A1032      23.293   2.631  45.183  1.00 46.26           N  
ANISOU 1845  N   LEU A1032     5184   6998   5394    232   -580   2272       N  
ATOM   1846  CA  LEU A1032      24.487   2.619  46.035  1.00 46.36           C  
ANISOU 1846  CA  LEU A1032     5012   7151   5453    127   -767   2443       C  
ATOM   1847  C   LEU A1032      25.611   3.440  45.392  1.00 51.01           C  
ANISOU 1847  C   LEU A1032     5359   7819   6203      6   -812   2619       C  
ATOM   1848  O   LEU A1032      25.939   3.234  44.218  1.00 50.44           O  
ANISOU 1848  O   LEU A1032     5153   7787   6225    123   -628   2722       O  
ATOM   1849  CB  LEU A1032      24.957   1.176  46.295  1.00 46.47           C  
ANISOU 1849  CB  LEU A1032     4898   7263   5494    323   -703   2597       C  
ATOM   1850  CG  LEU A1032      26.037   1.003  47.368  1.00 51.40           C  
ANISOU 1850  CG  LEU A1032     5329   8062   6140    233   -931   2812       C  
ATOM   1851  CD1 LEU A1032      25.454   0.424  48.631  1.00 51.71           C  
ANISOU 1851  CD1 LEU A1032     5539   8113   5996    217  -1042   2757       C  
ATOM   1852  CD2 LEU A1032      27.163   0.116  46.875  1.00 53.79           C  
ANISOU 1852  CD2 LEU A1032     5315   8475   6648    424   -827   3089       C  
ATOM   1853  N   LEU A1033      26.178   4.383  46.157  1.00 48.42           N  
ANISOU 1853  N   LEU A1033     4984   7519   5893   -252  -1049   2640       N  
ATOM   1854  CA  LEU A1033      27.259   5.246  45.674  1.00 48.76           C  
ANISOU 1854  CA  LEU A1033     4790   7630   6108   -423  -1124   2817       C  
ATOM   1855  C   LEU A1033      28.633   4.713  46.083  1.00 54.79           C  
ANISOU 1855  C   LEU A1033     5221   8636   6961   -442  -1244   3090       C  
ATOM   1856  O   LEU A1033      29.544   4.669  45.251  1.00 54.64           O  
ANISOU 1856  O   LEU A1033     4921   8729   7112   -387  -1142   3312       O  
ATOM   1857  CB  LEU A1033      27.069   6.705  46.140  1.00 48.54           C  
ANISOU 1857  CB  LEU A1033     4900   7449   6093   -727  -1304   2668       C  
ATOM   1858  CG  LEU A1033      25.828   7.442  45.618  1.00 52.66           C  
ANISOU 1858  CG  LEU A1033     5680   7707   6621   -708  -1180   2466       C  
ATOM   1859  CD1 LEU A1033      25.517   8.651  46.475  1.00 52.58           C  
ANISOU 1859  CD1 LEU A1033     5859   7503   6618   -971  -1346   2249       C  
ATOM   1860  CD2 LEU A1033      25.989   7.846  44.153  1.00 54.52           C  
ANISOU 1860  CD2 LEU A1033     5783   7918   7012   -661  -1023   2640       C  
ATOM   1861  N   THR A1034      28.775   4.305  47.363  1.00 52.50           N  
ANISOU 1861  N   THR A1034     4947   8449   6551   -519  -1456   3095       N  
ATOM   1862  CA  THR A1034      30.005   3.765  47.949  1.00 52.92           C  
ANISOU 1862  CA  THR A1034     4672   8758   6677   -544  -1624   3391       C  
ATOM   1863  C   THR A1034      29.708   2.973  49.226  1.00 58.71           C  
ANISOU 1863  C   THR A1034     5510   9585   7213   -526  -1781   3387       C  
ATOM   1864  O   THR A1034      28.697   3.223  49.888  1.00 58.40           O  
ANISOU 1864  O   THR A1034     5797   9440   6951   -620  -1831   3120       O  
ATOM   1865  CB  THR A1034      31.061   4.884  48.175  1.00 60.78           C  
ANISOU 1865  CB  THR A1034     5440   9875   7777   -884  -1869   3517       C  
ATOM   1866  OG1 THR A1034      32.330   4.297  48.466  1.00 59.75           O  
ANISOU 1866  OG1 THR A1034     4911  10023   7770   -865  -1999   3868       O  
ATOM   1867  CG2 THR A1034      30.670   5.883  49.273  1.00 59.17           C  
ANISOU 1867  CG2 THR A1034     5484   9609   7388  -1243  -2137   3266       C  
ATOM   1868  N   LYS A1035      30.595   2.026  49.568  1.00 56.52           N  
ANISOU 1868  N   LYS A1035     4937   9511   7028   -401  -1846   3707       N  
ATOM   1869  CA  LYS A1035      30.501   1.246  50.799  1.00 56.83           C  
ANISOU 1869  CA  LYS A1035     5009   9687   6896   -394  -2025   3810       C  
ATOM   1870  C   LYS A1035      31.449   1.843  51.854  1.00 62.58           C  
ANISOU 1870  C   LYS A1035     5549  10702   7526   -743  -2424   3971       C  
ATOM   1871  O   LYS A1035      31.468   1.398  53.004  1.00 62.61           O  
ANISOU 1871  O   LYS A1035     5578  10888   7321   -829  -2644   4071       O  
ATOM   1872  CB  LYS A1035      30.775  -0.244  50.544  1.00 58.96           C  
ANISOU 1872  CB  LYS A1035     5081   9971   7352    -23  -1846   4088       C  
ATOM   1873  CG  LYS A1035      29.568  -0.988  49.987  1.00 68.61           C  
ANISOU 1873  CG  LYS A1035     6589  10925   8556    250  -1523   3870       C  
ATOM   1874  CD  LYS A1035      29.874  -2.456  49.762  1.00 75.63           C  
ANISOU 1874  CD  LYS A1035     7297  11774   9666    598  -1336   4120       C  
ATOM   1875  CE  LYS A1035      28.697  -3.199  49.190  1.00 81.63           C  
ANISOU 1875  CE  LYS A1035     8344  12261  10412    824  -1026   3881       C  
ATOM   1876  NZ  LYS A1035      29.056  -4.598  48.844  1.00 89.57           N  
ANISOU 1876  NZ  LYS A1035     9180  13168  11685   1159   -810   4094       N  
ATOM   1877  N   SER A1036      32.201   2.886  51.455  1.00 60.19           N  
ANISOU 1877  N   SER A1036     5065  10448   7356   -974  -2524   3996       N  
ATOM   1878  CA  SER A1036      33.146   3.629  52.287  1.00 60.73           C  
ANISOU 1878  CA  SER A1036     4941  10775   7357  -1368  -2908   4114       C  
ATOM   1879  C   SER A1036      32.383   4.526  53.284  1.00 67.07           C  
ANISOU 1879  C   SER A1036     6142  11527   7815  -1720  -3102   3728       C  
ATOM   1880  O   SER A1036      31.420   5.187  52.881  1.00 66.78           O  
ANISOU 1880  O   SER A1036     6440  11192   7743  -1722  -2918   3370       O  
ATOM   1881  CB  SER A1036      34.066   4.471  51.404  1.00 63.63           C  
ANISOU 1881  CB  SER A1036     5020  11150   8007  -1505  -2899   4229       C  
ATOM   1882  OG  SER A1036      34.957   5.277  52.156  1.00 71.53           O  
ANISOU 1882  OG  SER A1036     5827  12389   8962  -1931  -3280   4326       O  
ATOM   1883  N   PRO A1037      32.793   4.583  54.577  1.00 65.55           N  
ANISOU 1883  N   PRO A1037     5917  11628   7361  -2021  -3463   3790       N  
ATOM   1884  CA  PRO A1037      32.066   5.431  55.539  1.00 65.97           C  
ANISOU 1884  CA  PRO A1037     6372  11637   7058  -2363  -3607   3370       C  
ATOM   1885  C   PRO A1037      32.466   6.914  55.495  1.00 71.58           C  
ANISOU 1885  C   PRO A1037     7113  12262   7824  -2786  -3763   3141       C  
ATOM   1886  O   PRO A1037      32.848   7.496  56.515  1.00 71.53           O  
ANISOU 1886  O   PRO A1037     7125  12473   7582  -3207  -4095   3055       O  
ATOM   1887  CB  PRO A1037      32.361   4.760  56.882  1.00 67.63           C  
ANISOU 1887  CB  PRO A1037     6529  12237   6931  -2495  -3909   3560       C  
ATOM   1888  CG  PRO A1037      33.716   4.156  56.704  1.00 71.90           C  
ANISOU 1888  CG  PRO A1037     6532  13073   7713  -2418  -4080   4106       C  
ATOM   1889  CD  PRO A1037      33.908   3.867  55.232  1.00 67.24           C  
ANISOU 1889  CD  PRO A1037     5723  12244   7579  -2067  -3751   4248       C  
ATOM   1890  N   SER A1038      32.361   7.528  54.303  1.00 69.25           N  
ANISOU 1890  N   SER A1038     6832  11646   7836  -2692  -3522   3044       N  
ATOM   1891  CA  SER A1038      32.680   8.935  54.062  1.00 69.48           C  
ANISOU 1891  CA  SER A1038     6890  11501   8008  -3050  -3609   2856       C  
ATOM   1892  C   SER A1038      31.642   9.582  53.142  1.00 74.08           C  
ANISOU 1892  C   SER A1038     7764  11627   8757  -2895  -3279   2569       C  
ATOM   1893  O   SER A1038      31.161   8.939  52.205  1.00 73.50           O  
ANISOU 1893  O   SER A1038     7668  11438   8821  -2502  -2987   2680       O  
ATOM   1894  CB  SER A1038      34.074   9.069  53.457  1.00 73.18           C  
ANISOU 1894  CB  SER A1038     6866  12155   8783  -3149  -3732   3254       C  
ATOM   1895  OG  SER A1038      34.450  10.427  53.291  1.00 82.66           O  
ANISOU 1895  OG  SER A1038     8079  13191  10137  -3541  -3841   3102       O  
ATOM   1896  N   LEU A1039      31.303  10.857  53.417  1.00 71.25           N  
ANISOU 1896  N   LEU A1039     7673  11008   8390  -3214  -3330   2205       N  
ATOM   1897  CA  LEU A1039      30.345  11.643  52.635  1.00 71.13           C  
ANISOU 1897  CA  LEU A1039     7918  10541   8567  -3107  -3054   1955       C  
ATOM   1898  C   LEU A1039      31.035  12.259  51.411  1.00 75.14           C  
ANISOU 1898  C   LEU A1039     8160  10922   9466  -3129  -2982   2207       C  
ATOM   1899  O   LEU A1039      30.408  12.371  50.355  1.00 74.63           O  
ANISOU 1899  O   LEU A1039     8158  10612   9584  -2871  -2707   2230       O  
ATOM   1900  CB  LEU A1039      29.689  12.728  53.515  1.00 71.15           C  
ANISOU 1900  CB  LEU A1039     8309  10285   8442  -3426  -3116   1464       C  
ATOM   1901  CG  LEU A1039      28.530  13.531  52.906  1.00 75.81           C  
ANISOU 1901  CG  LEU A1039     9201  10382   9222  -3281  -2823   1181       C  
ATOM   1902  CD1 LEU A1039      27.235  12.729  52.884  1.00 75.77           C  
ANISOU 1902  CD1 LEU A1039     9423  10334   9031  -2903  -2582   1048       C  
ATOM   1903  CD2 LEU A1039      28.318  14.824  53.660  1.00 78.40           C  
ANISOU 1903  CD2 LEU A1039     9805  10411   9572  -3671  -2904    755       C  
ATOM   1904  N   ASN A1040      32.326  12.639  51.551  1.00 71.81           N  
ANISOU 1904  N   ASN A1040     7425  10701   9160  -3451  -3235   2420       N  
ATOM   1905  CA  ASN A1040      33.140  13.208  50.468  1.00 71.64           C  
ANISOU 1905  CA  ASN A1040     7098  10620   9502  -3523  -3186   2707       C  
ATOM   1906  C   ASN A1040      33.378  12.167  49.372  1.00 75.07           C  
ANISOU 1906  C   ASN A1040     7245  11228  10052  -3094  -2947   3084       C  
ATOM   1907  O   ASN A1040      33.335  12.510  48.189  1.00 74.78           O  
ANISOU 1907  O   ASN A1040     7132  11032  10251  -2977  -2727   3219       O  
ATOM   1908  CB  ASN A1040      34.468  13.749  50.999  1.00 72.96           C  
ANISOU 1908  CB  ASN A1040     6968  11014   9741  -3986  -3533   2854       C  
ATOM   1909  CG  ASN A1040      34.306  14.865  51.998  1.00103.18           C  
ANISOU 1909  CG  ASN A1040    11086  14646  13471  -4467  -3760   2444       C  
ATOM   1910  OD1 ASN A1040      33.868  15.973  51.666  1.00 99.27           O  
ANISOU 1910  OD1 ASN A1040    10813  13722  13182  -4615  -3656   2215       O  
ATOM   1911  ND2 ASN A1040      34.659  14.595  53.246  1.00 97.13           N  
ANISOU 1911  ND2 ASN A1040    10326  14189  12391  -4727  -4070   2345       N  
ATOM   1912  N   ALA A1041      33.596  10.892  49.772  1.00 71.22           N  
ANISOU 1912  N   ALA A1041     6611  11055   9393  -2864  -2977   3247       N  
ATOM   1913  CA  ALA A1041      33.778   9.754  48.868  1.00 70.81           C  
ANISOU 1913  CA  ALA A1041     6318  11151   9435  -2438  -2728   3547       C  
ATOM   1914  C   ALA A1041      32.466   9.479  48.109  1.00 74.16           C  
ANISOU 1914  C   ALA A1041     7058  11307   9814  -2094  -2392   3355       C  
ATOM   1915  O   ALA A1041      32.504   9.144  46.923  1.00 73.85           O  
ANISOU 1915  O   ALA A1041     6885  11260   9915  -1839  -2128   3524       O  
ATOM   1916  CB  ALA A1041      34.203   8.524  49.656  1.00 71.53           C  
ANISOU 1916  CB  ALA A1041     6227  11573   9378  -2297  -2858   3734       C  
ATOM   1917  N   ALA A1042      31.314   9.663  48.792  1.00 69.93           N  
ANISOU 1917  N   ALA A1042     6929  10572   9071  -2109  -2400   2997       N  
ATOM   1918  CA  ALA A1042      29.975   9.498  48.224  1.00 69.47           C  
ANISOU 1918  CA  ALA A1042     7171  10263   8960  -1829  -2126   2797       C  
ATOM   1919  C   ALA A1042      29.675  10.606  47.208  1.00 72.51           C  
ANISOU 1919  C   ALA A1042     7620  10364   9565  -1889  -1986   2768       C  
ATOM   1920  O   ALA A1042      29.100  10.324  46.155  1.00 72.28           O  
ANISOU 1920  O   ALA A1042     7625  10255   9581  -1624  -1735   2822       O  
ATOM   1921  CB  ALA A1042      28.937   9.508  49.332  1.00 70.19           C  
ANISOU 1921  CB  ALA A1042     7629  10244   8795  -1871  -2187   2444       C  
ATOM   1922  N   LYS A1043      30.080  11.858  47.519  1.00 68.11           N  
ANISOU 1922  N   LYS A1043     7077   9658   9145  -2254  -2157   2696       N  
ATOM   1923  CA  LYS A1043      29.900  13.022  46.648  1.00 67.45           C  
ANISOU 1923  CA  LYS A1043     7035   9273   9320  -2356  -2056   2716       C  
ATOM   1924  C   LYS A1043      30.775  12.903  45.394  1.00 70.99           C  
ANISOU 1924  C   LYS A1043     7128   9884   9960  -2284  -1936   3117       C  
ATOM   1925  O   LYS A1043      30.338  13.292  44.311  1.00 70.32           O  
ANISOU 1925  O   LYS A1043     7075   9643  10001  -2172  -1739   3212       O  
ATOM   1926  CB  LYS A1043      30.201  14.327  47.400  1.00 69.39           C  
ANISOU 1926  CB  LYS A1043     7384   9294   9687  -2793  -2275   2524       C  
ATOM   1927  CG  LYS A1043      29.093  14.769  48.348  1.00 80.41           C  
ANISOU 1927  CG  LYS A1043     9194  10408  10948  -2848  -2286   2073       C  
ATOM   1928  CD  LYS A1043      29.507  16.006  49.126  1.00 90.82           C  
ANISOU 1928  CD  LYS A1043    10621  11505  12381  -3309  -2492   1841       C  
ATOM   1929  CE  LYS A1043      28.456  16.455  50.108  1.00101.51           C  
ANISOU 1929  CE  LYS A1043    12388  12590  13590  -3366  -2467   1352       C  
ATOM   1930  NZ  LYS A1043      28.900  17.651  50.871  1.00110.01           N  
ANISOU 1930  NZ  LYS A1043    13592  13440  14766  -3842  -2655   1072       N  
ATOM   1931  N   SER A1044      31.995  12.340  45.543  1.00 67.55           N  
ANISOU 1931  N   SER A1044     6340   9787   9538  -2341  -2047   3368       N  
ATOM   1932  CA  SER A1044      32.949  12.121  44.452  1.00 67.37           C  
ANISOU 1932  CA  SER A1044     5935   9976   9688  -2267  -1911   3750       C  
ATOM   1933  C   SER A1044      32.421  11.094  43.447  1.00 71.44           C  
ANISOU 1933  C   SER A1044     6454  10583  10105  -1837  -1588   3825       C  
ATOM   1934  O   SER A1044      32.534  11.313  42.240  1.00 70.65           O  
ANISOU 1934  O   SER A1044     6235  10500  10108  -1762  -1379   4017       O  
ATOM   1935  CB  SER A1044      34.301  11.683  45.003  1.00 70.76           C  
ANISOU 1935  CB  SER A1044     5974  10749  10165  -2405  -2110   3984       C  
ATOM   1936  OG  SER A1044      34.854  12.687  45.839  1.00 79.89           O  
ANISOU 1936  OG  SER A1044     7104  11846  11405  -2860  -2422   3921       O  
ATOM   1937  N   GLU A1045      31.823   9.992  43.946  1.00 68.56           N  
ANISOU 1937  N   GLU A1045     6240  10280   9530  -1580  -1547   3666       N  
ATOM   1938  CA  GLU A1045      31.231   8.932  43.122  1.00 68.51           C  
ANISOU 1938  CA  GLU A1045     6285  10332   9415  -1197  -1254   3669       C  
ATOM   1939  C   GLU A1045      29.976   9.433  42.401  1.00 72.14           C  
ANISOU 1939  C   GLU A1045     7046  10544   9819  -1118  -1096   3507       C  
ATOM   1940  O   GLU A1045      29.728   9.031  41.264  1.00 71.66           O  
ANISOU 1940  O   GLU A1045     6959  10548   9721   -912   -848   3591       O  
ATOM   1941  CB  GLU A1045      30.911   7.687  43.968  1.00 69.96           C  
ANISOU 1941  CB  GLU A1045     6552  10606   9425   -990  -1281   3553       C  
ATOM   1942  CG  GLU A1045      32.133   6.884  44.386  1.00 82.05           C  
ANISOU 1942  CG  GLU A1045     7722  12421  11032   -950  -1363   3806       C  
ATOM   1943  CD  GLU A1045      32.716   5.979  43.317  1.00107.19           C  
ANISOU 1943  CD  GLU A1045    10635  15769  14325   -658  -1067   4024       C  
ATOM   1944  OE1 GLU A1045      33.491   6.478  42.469  1.00102.45           O  
ANISOU 1944  OE1 GLU A1045     9777  15267  13884   -732   -969   4231       O  
ATOM   1945  OE2 GLU A1045      32.407   4.766  43.335  1.00103.98           O  
ANISOU 1945  OE2 GLU A1045    10273  15385  13849   -363   -917   3982       O  
ATOM   1946  N   LEU A1046      29.201  10.323  43.060  1.00 68.57           N  
ANISOU 1946  N   LEU A1046     6870   9818   9364  -1287  -1237   3277       N  
ATOM   1947  CA  LEU A1046      27.983  10.930  42.517  1.00 68.27           C  
ANISOU 1947  CA  LEU A1046     7095   9517   9328  -1223  -1122   3146       C  
ATOM   1948  C   LEU A1046      28.317  11.940  41.407  1.00 72.50           C  
ANISOU 1948  C   LEU A1046     7503   9978  10066  -1345  -1049   3391       C  
ATOM   1949  O   LEU A1046      27.649  11.936  40.374  1.00 72.09           O  
ANISOU 1949  O   LEU A1046     7511   9905   9977  -1188   -869   3465       O  
ATOM   1950  CB  LEU A1046      27.138  11.574  43.643  1.00 68.17           C  
ANISOU 1950  CB  LEU A1046     7385   9223   9292  -1355  -1270   2824       C  
ATOM   1951  CG  LEU A1046      25.800  12.246  43.264  1.00 72.38           C  
ANISOU 1951  CG  LEU A1046     8179   9449   9872  -1270  -1160   2677       C  
ATOM   1952  CD1 LEU A1046      24.787  11.238  42.746  1.00 72.45           C  
ANISOU 1952  CD1 LEU A1046     8290   9548   9689   -950   -976   2624       C  
ATOM   1953  CD2 LEU A1046      25.212  12.980  44.446  1.00 74.29           C  
ANISOU 1953  CD2 LEU A1046     8677   9413  10137  -1429  -1283   2353       C  
ATOM   1954  N   ASP A1047      29.354  12.781  41.613  1.00 69.33           N  
ANISOU 1954  N   ASP A1047     6914   9559   9870  -1643  -1198   3539       N  
ATOM   1955  CA  ASP A1047      29.812  13.777  40.635  1.00 69.32           C  
ANISOU 1955  CA  ASP A1047     6759   9488  10092  -1805  -1143   3820       C  
ATOM   1956  C   ASP A1047      30.395  13.115  39.381  1.00 73.13           C  
ANISOU 1956  C   ASP A1047     6972  10302  10513  -1637   -916   4126       C  
ATOM   1957  O   ASP A1047      30.251  13.657  38.284  1.00 73.06           O  
ANISOU 1957  O   ASP A1047     6920  10270  10567  -1649   -780   4342       O  
ATOM   1958  CB  ASP A1047      30.844  14.735  41.264  1.00 71.34           C  
ANISOU 1958  CB  ASP A1047     6864   9658  10584  -2197  -1371   3888       C  
ATOM   1959  CG  ASP A1047      30.291  15.744  42.259  1.00 82.56           C  
ANISOU 1959  CG  ASP A1047     8570  10679  12121  -2433  -1552   3589       C  
ATOM   1960  OD1 ASP A1047      29.153  15.541  42.748  1.00 82.97           O  
ANISOU 1960  OD1 ASP A1047     8927  10565  12035  -2273  -1524   3289       O  
ATOM   1961  OD2 ASP A1047      31.002  16.728  42.563  1.00 89.14           O  
ANISOU 1961  OD2 ASP A1047     9318  11361  13189  -2786  -1709   3642       O  
ATOM   1962  N   LYS A1048      31.041  11.943  39.550  1.00 69.37           N  
ANISOU 1962  N   LYS A1048     6314  10128   9915  -1479   -862   4147       N  
ATOM   1963  CA  LYS A1048      31.648  11.147  38.481  1.00 69.18           C  
ANISOU 1963  CA  LYS A1048     6037  10423   9826  -1289   -604   4372       C  
ATOM   1964  C   LYS A1048      30.562  10.516  37.595  1.00 73.16           C  
ANISOU 1964  C   LYS A1048     6753  10947  10096  -1008   -366   4263       C  
ATOM   1965  O   LYS A1048      30.696  10.523  36.369  1.00 72.94           O  
ANISOU 1965  O   LYS A1048     6622  11084  10009   -950   -146   4451       O  
ATOM   1966  CB  LYS A1048      32.555  10.057  39.087  1.00 71.67           C  
ANISOU 1966  CB  LYS A1048     6109  10988  10134  -1179   -622   4401       C  
ATOM   1967  CG  LYS A1048      33.517   9.400  38.098  1.00 86.19           C  
ANISOU 1967  CG  LYS A1048     7596  13146  12005  -1034   -353   4663       C  
ATOM   1968  CD  LYS A1048      34.175   8.143  38.676  1.00 96.72           C  
ANISOU 1968  CD  LYS A1048     8722  14676  13352   -829   -326   4672       C  
ATOM   1969  CE  LYS A1048      35.462   8.422  39.418  1.00110.37           C  
ANISOU 1969  CE  LYS A1048    10087  16543  15304  -1045   -555   4896       C  
ATOM   1970  NZ  LYS A1048      36.038   7.185  40.009  1.00121.00           N  
ANISOU 1970  NZ  LYS A1048    11219  18071  16686   -819   -545   4949       N  
ATOM   1971  N   ALA A1049      29.491   9.983  38.221  1.00 69.45           N  
ANISOU 1971  N   ALA A1049     6574  10335   9480   -860   -413   3965       N  
ATOM   1972  CA  ALA A1049      28.365   9.334  37.544  1.00 69.24           C  
ANISOU 1972  CA  ALA A1049     6760  10318   9231   -624   -232   3824       C  
ATOM   1973  C   ALA A1049      27.437  10.317  36.817  1.00 73.41           C  
ANISOU 1973  C   ALA A1049     7445  10688   9759   -692   -219   3885       C  
ATOM   1974  O   ALA A1049      26.800   9.932  35.835  1.00 72.54           O  
ANISOU 1974  O   ALA A1049     7399  10701   9462   -554    -46   3906       O  
ATOM   1975  CB  ALA A1049      27.570   8.503  38.537  1.00 69.92           C  
ANISOU 1975  CB  ALA A1049     7072  10297   9197   -482   -305   3520       C  
ATOM   1976  N   ILE A1050      27.350  11.570  37.303  1.00 70.71           N  
ANISOU 1976  N   ILE A1050     7164  10071   9632   -908   -404   3915       N  
ATOM   1977  CA  ILE A1050      26.491  12.604  36.720  1.00 70.86           C  
ANISOU 1977  CA  ILE A1050     7310   9878   9735   -966   -409   4014       C  
ATOM   1978  C   ILE A1050      27.261  13.456  35.695  1.00 76.45           C  
ANISOU 1978  C   ILE A1050     7796  10669  10581  -1137   -350   4404       C  
ATOM   1979  O   ILE A1050      26.861  13.513  34.532  1.00 76.60           O  
ANISOU 1979  O   ILE A1050     7800  10830  10474  -1068   -207   4600       O  
ATOM   1980  CB  ILE A1050      25.775  13.453  37.821  1.00 73.72           C  
ANISOU 1980  CB  ILE A1050     7898   9832  10281  -1067   -595   3794       C  
ATOM   1981  CG1 ILE A1050      24.880  12.586  38.763  1.00 73.92           C  
ANISOU 1981  CG1 ILE A1050     8147   9812  10129   -890   -619   3429       C  
ATOM   1982  CG2 ILE A1050      24.995  14.636  37.229  1.00 74.48           C  
ANISOU 1982  CG2 ILE A1050     8082   9655  10561  -1118   -593   3950       C  
ATOM   1983  CD1 ILE A1050      23.708  11.732  38.131  1.00 81.68           C  
ANISOU 1983  CD1 ILE A1050     9255  10910  10871   -628   -471   3352       C  
ATOM   1984  N   GLY A1051      28.335  14.105  36.136  1.00 73.70           N  
ANISOU 1984  N   GLY A1051     7276  10254  10473  -1378   -467   4522       N  
ATOM   1985  CA  GLY A1051      29.163  14.951  35.281  1.00 73.96           C  
ANISOU 1985  CA  GLY A1051     7074  10350  10678  -1581   -421   4910       C  
ATOM   1986  C   GLY A1051      29.162  16.423  35.649  1.00 78.85           C  
ANISOU 1986  C   GLY A1051     7744  10562  11655  -1860   -594   5000       C  
ATOM   1987  O   GLY A1051      29.549  17.263  34.830  1.00 78.49           O  
ANISOU 1987  O   GLY A1051     7553  10496  11775  -2022   -549   5357       O  
ATOM   1988  N   ARG A1052      28.731  16.743  36.890  1.00 75.96           N  
ANISOU 1988  N   ARG A1052     7590   9860  11411  -1927   -777   4672       N  
ATOM   1989  CA  ARG A1052      28.669  18.105  37.438  1.00 75.92           C  
ANISOU 1989  CA  ARG A1052     7687   9395  11765  -2195   -932   4645       C  
ATOM   1990  C   ARG A1052      28.809  18.106  38.970  1.00 80.64           C  
ANISOU 1990  C   ARG A1052     8421   9818  12402  -2336  -1132   4245       C  
ATOM   1991  O   ARG A1052      28.578  17.072  39.605  1.00 80.41           O  
ANISOU 1991  O   ARG A1052     8469   9976  12107  -2165  -1146   3987       O  
ATOM   1992  CB  ARG A1052      27.376  18.829  36.999  1.00 75.29           C  
ANISOU 1992  CB  ARG A1052     7826   8974  11807  -2080   -877   4678       C  
ATOM   1993  CG  ARG A1052      26.090  18.231  37.564  1.00 83.74           C  
ANISOU 1993  CG  ARG A1052     9167   9956  12693  -1814   -860   4315       C  
ATOM   1994  CD  ARG A1052      24.909  19.162  37.402  1.00 90.94           C  
ANISOU 1994  CD  ARG A1052    10264  10448  13841  -1746   -840   4331       C  
ATOM   1995  NE  ARG A1052      23.747  18.701  38.165  1.00 96.63           N  
ANISOU 1995  NE  ARG A1052    11227  11052  14437  -1533   -832   3948       N  
ATOM   1996  CZ  ARG A1052      23.475  19.065  39.415  1.00108.28           C  
ANISOU 1996  CZ  ARG A1052    12899  12205  16039  -1611   -912   3565       C  
ATOM   1997  NH1 ARG A1052      24.290  19.884  40.069  1.00 95.76           N  
ANISOU 1997  NH1 ARG A1052    11312  10370  14702  -1916  -1028   3486       N  
ATOM   1998  NH2 ARG A1052      22.398  18.595  40.029  1.00 92.40           N  
ANISOU 1998  NH2 ARG A1052    11085  10135  13889  -1406   -871   3249       N  
ATOM   1999  N   ASN A1053      29.172  19.270  39.559  1.00 77.32           N  
ANISOU 1999  N   ASN A1053     8037   9040  12302  -2666  -1286   4194       N  
ATOM   2000  CA  ASN A1053      29.304  19.428  41.010  1.00 77.18           C  
ANISOU 2000  CA  ASN A1053     8171   8854  12299  -2866  -1486   3795       C  
ATOM   2001  C   ASN A1053      27.908  19.487  41.656  1.00 80.86           C  
ANISOU 2001  C   ASN A1053     9005   9011  12706  -2683  -1449   3406       C  
ATOM   2002  O   ASN A1053      27.333  20.565  41.838  1.00 80.60           O  
ANISOU 2002  O   ASN A1053     9163   8504  12957  -2783  -1447   3288       O  
ATOM   2003  CB  ASN A1053      30.166  20.648  41.365  1.00 78.58           C  
ANISOU 2003  CB  ASN A1053     8275   8751  12832  -3313  -1650   3842       C  
ATOM   2004  CG  ASN A1053      31.616  20.516  40.964  1.00105.84           C  
ANISOU 2004  CG  ASN A1053    11331  12549  16335  -3526  -1712   4194       C  
ATOM   2005  OD1 ASN A1053      32.084  21.154  40.013  1.00101.38           O  
ANISOU 2005  OD1 ASN A1053    10572  11953  15996  -3633  -1629   4584       O  
ATOM   2006  ND2 ASN A1053      32.364  19.693  41.688  1.00 98.23           N  
ANISOU 2006  ND2 ASN A1053    10217  11934  15173  -3595  -1856   4095       N  
ATOM   2007  N   THR A1054      27.356  18.301  41.953  1.00 76.98           N  
ANISOU 2007  N   THR A1054     8597   8784  11869  -2401  -1396   3226       N  
ATOM   2008  CA  THR A1054      26.025  18.111  42.537  1.00 76.71           C  
ANISOU 2008  CA  THR A1054     8867   8558  11720  -2191  -1334   2881       C  
ATOM   2009  C   THR A1054      25.972  18.486  44.019  1.00 80.12           C  
ANISOU 2009  C   THR A1054     9519   8775  12148  -2404  -1479   2445       C  
ATOM   2010  O   THR A1054      24.970  19.049  44.465  1.00 79.84           O  
ANISOU 2010  O   THR A1054     9743   8375  12218  -2355  -1414   2172       O  
ATOM   2011  CB  THR A1054      25.538  16.667  42.314  1.00 84.48           C  
ANISOU 2011  CB  THR A1054     9842   9914  12344  -1854  -1227   2867       C  
ATOM   2012  OG1 THR A1054      26.441  15.761  42.950  1.00 84.00           O  
ANISOU 2012  OG1 THR A1054     9650  10198  12070  -1912  -1335   2826       O  
ATOM   2013  CG2 THR A1054      25.391  16.310  40.836  1.00 82.76           C  
ANISOU 2013  CG2 THR A1054     9470   9890  12085  -1644  -1058   3221       C  
ATOM   2014  N   ASN A1055      27.049  18.155  44.772  1.00 75.95           N  
ANISOU 2014  N   ASN A1055     8873   8497  11486  -2642  -1669   2387       N  
ATOM   2015  CA  ASN A1055      27.229  18.373  46.215  1.00 75.32           C  
ANISOU 2015  CA  ASN A1055     8967   8347  11305  -2909  -1851   1995       C  
ATOM   2016  C   ASN A1055      26.114  17.702  47.048  1.00 77.11           C  
ANISOU 2016  C   ASN A1055     9471   8589  11237  -2688  -1779   1631       C  
ATOM   2017  O   ASN A1055      25.545  18.306  47.963  1.00 76.98           O  
ANISOU 2017  O   ASN A1055     9729   8289  11230  -2815  -1790   1239       O  
ATOM   2018  CB  ASN A1055      27.422  19.864  46.563  1.00 78.09           C  
ANISOU 2018  CB  ASN A1055     9439   8228  12003  -3274  -1929   1834       C  
ATOM   2019  CG  ASN A1055      28.041  20.106  47.926  1.00108.34           C  
ANISOU 2019  CG  ASN A1055    13365  12091  15708  -3670  -2169   1493       C  
ATOM   2020  OD1 ASN A1055      29.101  19.568  48.271  1.00104.28           O  
ANISOU 2020  OD1 ASN A1055    12622  11971  15030  -3859  -2376   1624       O  
ATOM   2021  ND2 ASN A1055      27.387  20.926  48.733  1.00101.58           N  
ANISOU 2021  ND2 ASN A1055    12840  10831  14926  -3809  -2145   1048       N  
ATOM   2022  N   GLY A1056      25.821  16.450  46.704  1.00 71.63           N  
ANISOU 2022  N   GLY A1056     8701   8224  10293  -2367  -1687   1760       N  
ATOM   2023  CA  GLY A1056      24.824  15.638  47.390  1.00 70.44           C  
ANISOU 2023  CA  GLY A1056     8762   8145   9855  -2147  -1611   1491       C  
ATOM   2024  C   GLY A1056      23.390  15.769  46.920  1.00 71.93           C  
ANISOU 2024  C   GLY A1056     9122   8087  10120  -1853  -1384   1413       C  
ATOM   2025  O   GLY A1056      22.565  14.925  47.270  1.00 71.60           O  
ANISOU 2025  O   GLY A1056     9185   8176   9843  -1624  -1294   1289       O  
ATOM   2026  N   VAL A1057      23.071  16.823  46.142  1.00 66.70           N  
ANISOU 2026  N   VAL A1057     8474   7068   9802  -1861  -1295   1512       N  
ATOM   2027  CA  VAL A1057      21.714  17.076  45.636  1.00 65.53           C  
ANISOU 2027  CA  VAL A1057     8445   6672   9783  -1589  -1098   1494       C  
ATOM   2028  C   VAL A1057      21.648  16.877  44.116  1.00 66.73           C  
ANISOU 2028  C   VAL A1057     8390   6950  10014  -1399  -1009   1925       C  
ATOM   2029  O   VAL A1057      22.421  17.494  43.380  1.00 66.51           O  
ANISOU 2029  O   VAL A1057     8197   6883  10192  -1543  -1051   2214       O  
ATOM   2030  CB  VAL A1057      21.170  18.472  46.071  1.00 69.60           C  
ANISOU 2030  CB  VAL A1057     9158   6644  10643  -1704  -1043   1257       C  
ATOM   2031  CG1 VAL A1057      19.735  18.691  45.592  1.00 69.40           C  
ANISOU 2031  CG1 VAL A1057     9215   6378  10776  -1391   -839   1268       C  
ATOM   2032  CG2 VAL A1057      21.256  18.660  47.584  1.00 69.40           C  
ANISOU 2032  CG2 VAL A1057     9361   6529  10478  -1926  -1115    780       C  
ATOM   2033  N   ILE A1058      20.717  16.020  43.656  1.00 61.16           N  
ANISOU 2033  N   ILE A1058     7696   6414   9127  -1101   -886   1965       N  
ATOM   2034  CA  ILE A1058      20.481  15.723  42.233  1.00 59.82           C  
ANISOU 2034  CA  ILE A1058     7366   6414   8948   -921   -795   2323       C  
ATOM   2035  C   ILE A1058      19.018  15.992  41.836  1.00 61.62           C  
ANISOU 2035  C   ILE A1058     7684   6452   9277   -694   -673   2325       C  
ATOM   2036  O   ILE A1058      18.169  16.191  42.709  1.00 61.03           O  
ANISOU 2036  O   ILE A1058     7785   6157   9245   -631   -628   2026       O  
ATOM   2037  CB  ILE A1058      20.937  14.287  41.828  1.00 62.62           C  
ANISOU 2037  CB  ILE A1058     7591   7237   8966   -809   -776   2424       C  
ATOM   2038  CG1 ILE A1058      20.188  13.196  42.626  1.00 62.93           C  
ANISOU 2038  CG1 ILE A1058     7774   7400   8736   -645   -739   2140       C  
ATOM   2039  CG2 ILE A1058      22.456  14.129  41.911  1.00 63.02           C  
ANISOU 2039  CG2 ILE A1058     7462   7487   8994  -1005   -880   2548       C  
ATOM   2040  CD1 ILE A1058      19.967  11.915  41.880  1.00 69.44           C  
ANISOU 2040  CD1 ILE A1058     8521   8551   9313   -442   -643   2248       C  
ATOM   2041  N   THR A1059      18.728  15.982  40.520  1.00 56.82           N  
ANISOU 2041  N   THR A1059     6938   5963   8688   -577   -616   2672       N  
ATOM   2042  CA  THR A1059      17.376  16.188  39.975  1.00 55.65           C  
ANISOU 2042  CA  THR A1059     6810   5707   8627   -367   -531   2765       C  
ATOM   2043  C   THR A1059      16.697  14.842  39.667  1.00 57.48           C  
ANISOU 2043  C   THR A1059     7035   6304   8501   -175   -475   2718       C  
ATOM   2044  O   THR A1059      17.375  13.810  39.621  1.00 56.53           O  
ANISOU 2044  O   THR A1059     6876   6505   8098   -194   -483   2680       O  
ATOM   2045  CB  THR A1059      17.413  17.105  38.740  1.00 60.24           C  
ANISOU 2045  CB  THR A1059     7244   6192   9452   -391   -532   3208       C  
ATOM   2046  OG1 THR A1059      18.254  16.524  37.743  1.00 56.32           O  
ANISOU 2046  OG1 THR A1059     6583   6092   8723   -452   -542   3485       O  
ATOM   2047  CG2 THR A1059      17.868  18.525  39.069  1.00 59.07           C  
ANISOU 2047  CG2 THR A1059     7123   5577   9742   -570   -568   3247       C  
ATOM   2048  N   LYS A1060      15.359  14.864  39.454  1.00 53.04           N  
ANISOU 2048  N   LYS A1060     6496   5674   7982      8   -416   2727       N  
ATOM   2049  CA  LYS A1060      14.533  13.694  39.126  1.00 52.64           C  
ANISOU 2049  CA  LYS A1060     6437   5928   7635    167   -370   2683       C  
ATOM   2050  C   LYS A1060      15.009  13.011  37.831  1.00 56.39           C  
ANISOU 2050  C   LYS A1060     6778   6799   7850    148   -375   2949       C  
ATOM   2051  O   LYS A1060      15.008  11.780  37.757  1.00 56.02           O  
ANISOU 2051  O   LYS A1060     6751   7038   7497    195   -338   2823       O  
ATOM   2052  CB  LYS A1060      13.056  14.106  39.008  1.00 55.22           C  
ANISOU 2052  CB  LYS A1060     6755   6093   8132    335   -326   2723       C  
ATOM   2053  CG  LYS A1060      12.068  12.944  39.000  1.00 69.58           C  
ANISOU 2053  CG  LYS A1060     8591   8161   9686    470   -282   2583       C  
ATOM   2054  CD  LYS A1060      10.656  13.411  38.673  1.00 79.19           C  
ANISOU 2054  CD  LYS A1060     9723   9276  11090    627   -257   2718       C  
ATOM   2055  CE  LYS A1060      10.201  12.981  37.298  1.00 91.94           C  
ANISOU 2055  CE  LYS A1060    11184  11239  12510    653   -316   3030       C  
ATOM   2056  NZ  LYS A1060      10.898  13.724  36.211  1.00101.42           N  
ANISOU 2056  NZ  LYS A1060    12268  12485  13781    561   -385   3422       N  
ATOM   2057  N   ASP A1061      15.424  13.816  36.827  1.00 52.64           N  
ANISOU 2057  N   ASP A1061     6173   6329   7499     73   -403   3312       N  
ATOM   2058  CA  ASP A1061      15.934  13.343  35.537  1.00 52.51           C  
ANISOU 2058  CA  ASP A1061     6028   6698   7226     29   -384   3582       C  
ATOM   2059  C   ASP A1061      17.285  12.634  35.691  1.00 55.00           C  
ANISOU 2059  C   ASP A1061     6318   7213   7365    -66   -347   3484       C  
ATOM   2060  O   ASP A1061      17.517  11.610  35.040  1.00 54.53           O  
ANISOU 2060  O   ASP A1061     6222   7502   6996    -35   -273   3480       O  
ATOM   2061  CB  ASP A1061      16.031  14.504  34.531  1.00 54.70           C  
ANISOU 2061  CB  ASP A1061     6170   6910   7702    -44   -421   4028       C  
ATOM   2062  CG  ASP A1061      14.697  15.075  34.064  1.00 68.12           C  
ANISOU 2062  CG  ASP A1061     7829   8501   9553     74   -460   4240       C  
ATOM   2063  OD1 ASP A1061      13.636  14.576  34.522  1.00 68.35           O  
ANISOU 2063  OD1 ASP A1061     7926   8505   9540    214   -452   4021       O  
ATOM   2064  OD2 ASP A1061      14.712  16.022  33.240  1.00 75.29           O  
ANISOU 2064  OD2 ASP A1061     8615   9355  10635     26   -500   4657       O  
ATOM   2065  N   GLU A1062      18.162  13.169  36.567  1.00 50.18           N  
ANISOU 2065  N   GLU A1062     5724   6381   6963   -185   -396   3395       N  
ATOM   2066  CA  GLU A1062      19.470  12.584  36.873  1.00 49.17           C  
ANISOU 2066  CA  GLU A1062     5532   6420   6731   -277   -388   3327       C  
ATOM   2067  C   GLU A1062      19.291  11.276  37.644  1.00 50.34           C  
ANISOU 2067  C   GLU A1062     5779   6694   6653   -165   -357   3005       C  
ATOM   2068  O   GLU A1062      20.058  10.338  37.433  1.00 49.99           O  
ANISOU 2068  O   GLU A1062     5658   6906   6432   -147   -295   2997       O  
ATOM   2069  CB  GLU A1062      20.351  13.572  37.651  1.00 50.54           C  
ANISOU 2069  CB  GLU A1062     5687   6323   7195   -471   -487   3323       C  
ATOM   2070  CG  GLU A1062      20.940  14.661  36.766  1.00 58.51           C  
ANISOU 2070  CG  GLU A1062     6548   7264   8419   -621   -500   3698       C  
ATOM   2071  CD  GLU A1062      21.604  15.835  37.460  1.00 76.42           C  
ANISOU 2071  CD  GLU A1062     8817   9182  11039   -843   -605   3696       C  
ATOM   2072  OE1 GLU A1062      21.477  15.961  38.700  1.00 66.25           O  
ANISOU 2072  OE1 GLU A1062     7677   7663   9833   -886   -676   3367       O  
ATOM   2073  OE2 GLU A1062      22.252  16.639  36.751  1.00 71.52           O  
ANISOU 2073  OE2 GLU A1062     8053   8522  10601   -995   -612   4024       O  
ATOM   2074  N   ALA A1063      18.252  11.211  38.502  1.00 44.94           N  
ANISOU 2074  N   ALA A1063     5255   5826   5995    -80   -380   2760       N  
ATOM   2075  CA  ALA A1063      17.877  10.026  39.281  1.00 43.87           C  
ANISOU 2075  CA  ALA A1063     5228   5780   5662     23   -351   2481       C  
ATOM   2076  C   ALA A1063      17.282   8.949  38.369  1.00 45.81           C  
ANISOU 2076  C   ALA A1063     5460   6287   5658    152   -249   2501       C  
ATOM   2077  O   ALA A1063      17.499   7.763  38.616  1.00 45.44           O  
ANISOU 2077  O   ALA A1063     5439   6390   5436    213   -194   2360       O  
ATOM   2078  CB  ALA A1063      16.884  10.403  40.366  1.00 44.46           C  
ANISOU 2078  CB  ALA A1063     5463   5592   5840     60   -378   2243       C  
ATOM   2079  N   GLU A1064      16.550   9.366  37.309  1.00 41.04           N  
ANISOU 2079  N   GLU A1064     4812   5736   5046    180   -232   2685       N  
ATOM   2080  CA  GLU A1064      15.957   8.477  36.304  1.00 40.34           C  
ANISOU 2080  CA  GLU A1064     4710   5923   4695    248   -157   2711       C  
ATOM   2081  C   GLU A1064      17.054   7.832  35.443  1.00 43.32           C  
ANISOU 2081  C   GLU A1064     4993   6584   4881    209    -58   2802       C  
ATOM   2082  O   GLU A1064      16.934   6.660  35.084  1.00 42.53           O  
ANISOU 2082  O   GLU A1064     4929   6683   4548    265     42   2667       O  
ATOM   2083  CB  GLU A1064      14.953   9.238  35.426  1.00 41.68           C  
ANISOU 2083  CB  GLU A1064     4827   6101   4906    257   -203   2936       C  
ATOM   2084  CG  GLU A1064      13.993   8.324  34.683  1.00 51.82           C  
ANISOU 2084  CG  GLU A1064     6127   7643   5919    307   -171   2890       C  
ATOM   2085  CD  GLU A1064      12.796   8.973  34.014  1.00 71.78           C  
ANISOU 2085  CD  GLU A1064     8583  10202   8490    324   -253   3114       C  
ATOM   2086  OE1 GLU A1064      12.700  10.223  34.015  1.00 67.08           O  
ANISOU 2086  OE1 GLU A1064     7918   9398   8172    322   -320   3348       O  
ATOM   2087  OE2 GLU A1064      11.945   8.220  33.487  1.00 62.07           O  
ANISOU 2087  OE2 GLU A1064     7355   9198   7029    333   -255   3065       O  
ATOM   2088  N   LYS A1065      18.126   8.597  35.140  1.00 39.86           N  
ANISOU 2088  N   LYS A1065     4434   6149   4563    108    -68   3020       N  
ATOM   2089  CA  LYS A1065      19.294   8.146  34.381  1.00 39.99           C  
ANISOU 2089  CA  LYS A1065     4322   6426   4446     69     51   3134       C  
ATOM   2090  C   LYS A1065      20.045   7.054  35.170  1.00 43.82           C  
ANISOU 2090  C   LYS A1065     4813   6938   4900    138    119   2913       C  
ATOM   2091  O   LYS A1065      20.417   6.034  34.584  1.00 43.78           O  
ANISOU 2091  O   LYS A1065     4775   7152   4707    203    279   2854       O  
ATOM   2092  CB  LYS A1065      20.216   9.340  34.062  1.00 43.00           C  
ANISOU 2092  CB  LYS A1065     4553   6759   5026    -75      8   3436       C  
ATOM   2093  CG  LYS A1065      21.457   8.993  33.240  1.00 63.08           C  
ANISOU 2093  CG  LYS A1065     6925   9598   7444   -123    157   3601       C  
ATOM   2094  CD  LYS A1065      22.373  10.199  33.071  1.00 75.36           C  
ANISOU 2094  CD  LYS A1065     8318  11079   9238   -290    101   3906       C  
ATOM   2095  CE  LYS A1065      23.727   9.814  32.530  1.00 87.88           C  
ANISOU 2095  CE  LYS A1065     9700  12948  10742   -332    263   4045       C  
ATOM   2096  NZ  LYS A1065      24.649  10.978  32.481  1.00 98.16           N  
ANISOU 2096  NZ  LYS A1065    10823  14171  12301   -523    199   4351       N  
ATOM   2097  N   LEU A1066      20.250   7.263  36.494  1.00 39.71           N  
ANISOU 2097  N   LEU A1066     4335   6192   4561    123      2   2793       N  
ATOM   2098  CA  LEU A1066      20.909   6.287  37.372  1.00 39.11           C  
ANISOU 2098  CA  LEU A1066     4250   6135   4475    185     22   2639       C  
ATOM   2099  C   LEU A1066      20.022   5.052  37.532  1.00 42.27           C  
ANISOU 2099  C   LEU A1066     4794   6559   4707    327    102   2409       C  
ATOM   2100  O   LEU A1066      20.540   3.938  37.574  1.00 42.59           O  
ANISOU 2100  O   LEU A1066     4802   6692   4688    418    209   2335       O  
ATOM   2101  CB  LEU A1066      21.239   6.873  38.762  1.00 39.23           C  
ANISOU 2101  CB  LEU A1066     4289   5945   4671     92   -152   2578       C  
ATOM   2102  CG  LEU A1066      22.150   8.111  38.852  1.00 43.84           C  
ANISOU 2102  CG  LEU A1066     4740   6456   5462    -94   -260   2766       C  
ATOM   2103  CD1 LEU A1066      22.183   8.644  40.276  1.00 43.73           C  
ANISOU 2103  CD1 LEU A1066     4823   6217   5576   -213   -437   2618       C  
ATOM   2104  CD2 LEU A1066      23.579   7.820  38.360  1.00 45.75           C  
ANISOU 2104  CD2 LEU A1066     4742   6915   5725   -124   -196   2949       C  
ATOM   2105  N   PHE A1067      18.688   5.252  37.602  1.00 37.84           N  
ANISOU 2105  N   PHE A1067     4373   5902   4102    345     58   2312       N  
ATOM   2106  CA  PHE A1067      17.698   4.181  37.722  1.00 37.64           C  
ANISOU 2106  CA  PHE A1067     4478   5890   3933    442    120   2107       C  
ATOM   2107  C   PHE A1067      17.721   3.237  36.517  1.00 41.79           C  
ANISOU 2107  C   PHE A1067     4987   6638   4253    483    285   2084       C  
ATOM   2108  O   PHE A1067      17.699   2.022  36.711  1.00 41.37           O  
ANISOU 2108  O   PHE A1067     4994   6597   4127    564    388   1915       O  
ATOM   2109  CB  PHE A1067      16.277   4.747  37.943  1.00 39.31           C  
ANISOU 2109  CB  PHE A1067     4792   5971   4174    439     37   2051       C  
ATOM   2110  CG  PHE A1067      15.212   3.685  38.110  1.00 40.47           C  
ANISOU 2110  CG  PHE A1067     5050   6136   4191    510     89   1856       C  
ATOM   2111  CD1 PHE A1067      15.089   2.982  39.304  1.00 43.20           C  
ANISOU 2111  CD1 PHE A1067     5486   6371   4557    557     89   1687       C  
ATOM   2112  CD2 PHE A1067      14.342   3.379  37.069  1.00 42.05           C  
ANISOU 2112  CD2 PHE A1067     5257   6483   4239    504    130   1860       C  
ATOM   2113  CE1 PHE A1067      14.113   1.991  39.454  1.00 44.02           C  
ANISOU 2113  CE1 PHE A1067     5683   6480   4563    602    145   1530       C  
ATOM   2114  CE2 PHE A1067      13.366   2.389  37.220  1.00 44.88           C  
ANISOU 2114  CE2 PHE A1067     5705   6853   4492    534    170   1678       C  
ATOM   2115  CZ  PHE A1067      13.259   1.701  38.410  1.00 43.05           C  
ANISOU 2115  CZ  PHE A1067     5562   6481   4316    586    186   1517       C  
ATOM   2116  N   ASN A1068      17.755   3.794  35.285  1.00 38.61           N  
ANISOU 2116  N   ASN A1068     4512   6406   3753    417    318   2251       N  
ATOM   2117  CA  ASN A1068      17.786   3.026  34.036  1.00 38.64           C  
ANISOU 2117  CA  ASN A1068     4511   6666   3504    416    483   2215       C  
ATOM   2118  C   ASN A1068      19.048   2.194  33.879  1.00 43.15           C  
ANISOU 2118  C   ASN A1068     5005   7325   4064    482    673   2164       C  
ATOM   2119  O   ASN A1068      19.011   1.145  33.232  1.00 42.99           O  
ANISOU 2119  O   ASN A1068     5041   7427   3868    524    854   1995       O  
ATOM   2120  CB  ASN A1068      17.550   3.920  32.824  1.00 39.01           C  
ANISOU 2120  CB  ASN A1068     4489   6910   3424    308    455   2451       C  
ATOM   2121  CG  ASN A1068      16.095   4.251  32.611  1.00 54.05           C  
ANISOU 2121  CG  ASN A1068     6460   8809   5267    272    321   2473       C  
ATOM   2122  OD1 ASN A1068      15.236   3.368  32.524  1.00 45.68           O  
ANISOU 2122  OD1 ASN A1068     5500   7803   4052    286    342   2274       O  
ATOM   2123  ND2 ASN A1068      15.787   5.532  32.512  1.00 46.00           N  
ANISOU 2123  ND2 ASN A1068     5369   7712   4396    224    182   2732       N  
ATOM   2124  N   GLN A1069      20.156   2.649  34.488  1.00 40.14           N  
ANISOU 2124  N   GLN A1069     4489   6872   3890    488    638   2302       N  
ATOM   2125  CA  GLN A1069      21.427   1.925  34.502  1.00 39.87           C  
ANISOU 2125  CA  GLN A1069     4324   6904   3922    574    803   2305       C  
ATOM   2126  C   GLN A1069      21.266   0.723  35.437  1.00 43.45           C  
ANISOU 2126  C   GLN A1069     4866   7198   4444    708    834   2096       C  
ATOM   2127  O   GLN A1069      21.711  -0.373  35.092  1.00 43.31           O  
ANISOU 2127  O   GLN A1069     4825   7224   4407    824   1046   1990       O  
ATOM   2128  CB  GLN A1069      22.577   2.840  34.951  1.00 41.12           C  
ANISOU 2128  CB  GLN A1069     4284   7043   4297    507    704   2545       C  
ATOM   2129  CG  GLN A1069      22.971   3.875  33.895  1.00 56.08           C  
ANISOU 2129  CG  GLN A1069     6050   9110   6148    379    733   2794       C  
ATOM   2130  CD  GLN A1069      23.938   4.932  34.386  1.00 79.87           C  
ANISOU 2130  CD  GLN A1069     8882  12059   9405    261    597   3031       C  
ATOM   2131  OE1 GLN A1069      24.537   4.840  35.469  1.00 76.78           O  
ANISOU 2131  OE1 GLN A1069     8423  11552   9196    271    493   3015       O  
ATOM   2132  NE2 GLN A1069      24.115   5.973  33.587  1.00 72.89           N  
ANISOU 2132  NE2 GLN A1069     7910  11262   8523    124    583   3276       N  
ATOM   2133  N   ASP A1070      20.563   0.922  36.583  1.00 39.42           N  
ANISOU 2133  N   ASP A1070     4465   6496   4016    693    642   2036       N  
ATOM   2134  CA  ASP A1070      20.249  -0.118  37.570  1.00 39.00           C  
ANISOU 2134  CA  ASP A1070     4510   6292   4016    793    641   1881       C  
ATOM   2135  C   ASP A1070      19.269  -1.149  36.999  1.00 41.68           C  
ANISOU 2135  C   ASP A1070     5010   6627   4201    839    781   1659       C  
ATOM   2136  O   ASP A1070      19.386  -2.330  37.319  1.00 41.47           O  
ANISOU 2136  O   ASP A1070     5022   6507   4227    948    897   1545       O  
ATOM   2137  CB  ASP A1070      19.699   0.488  38.883  1.00 41.00           C  
ANISOU 2137  CB  ASP A1070     4843   6388   4347    734    416   1877       C  
ATOM   2138  CG  ASP A1070      20.668   1.335  39.705  1.00 52.44           C  
ANISOU 2138  CG  ASP A1070     6163   7817   5946    657    258   2038       C  
ATOM   2139  OD1 ASP A1070      21.870   1.393  39.348  1.00 53.60           O  
ANISOU 2139  OD1 ASP A1070     6120   8071   6176    667    311   2189       O  
ATOM   2140  OD2 ASP A1070      20.226   1.934  40.706  1.00 57.46           O  
ANISOU 2140  OD2 ASP A1070     6881   8336   6614    576     90   2001       O  
ATOM   2141  N   VAL A1071      18.322  -0.713  36.140  1.00 37.76           N  
ANISOU 2141  N   VAL A1071     4592   6228   3529    745    764   1617       N  
ATOM   2142  CA  VAL A1071      17.357  -1.604  35.475  1.00 37.21           C  
ANISOU 2142  CA  VAL A1071     4662   6197   3278    730    867   1405       C  
ATOM   2143  C   VAL A1071      18.102  -2.580  34.556  1.00 41.48           C  
ANISOU 2143  C   VAL A1071     5188   6841   3733    787   1133   1287       C  
ATOM   2144  O   VAL A1071      17.869  -3.784  34.645  1.00 40.83           O  
ANISOU 2144  O   VAL A1071     5208   6645   3659    848   1268   1077       O  
ATOM   2145  CB  VAL A1071      16.208  -0.838  34.757  1.00 40.43           C  
ANISOU 2145  CB  VAL A1071     5112   6733   3515    599    749   1441       C  
ATOM   2146  CG1 VAL A1071      15.378  -1.761  33.867  1.00 40.08           C  
ANISOU 2146  CG1 VAL A1071     5183   6810   3237    534    852   1232       C  
ATOM   2147  CG2 VAL A1071      15.308  -0.146  35.768  1.00 40.02           C  
ANISOU 2147  CG2 VAL A1071     5096   6520   3589    585    550   1484       C  
ATOM   2148  N   ASP A1072      19.032  -2.066  33.724  1.00 39.14           N  
ANISOU 2148  N   ASP A1072     4757   6736   3380    771   1228   1423       N  
ATOM   2149  CA  ASP A1072      19.843  -2.877  32.816  1.00 39.35           C  
ANISOU 2149  CA  ASP A1072     4746   6883   3323    834   1525   1311       C  
ATOM   2150  C   ASP A1072      20.720  -3.883  33.558  1.00 43.01           C  
ANISOU 2150  C   ASP A1072     5145   7147   4050   1027   1675   1260       C  
ATOM   2151  O   ASP A1072      20.822  -5.028  33.115  1.00 42.87           O  
ANISOU 2151  O   ASP A1072     5198   7077   4014   1111   1929   1035       O  
ATOM   2152  CB  ASP A1072      20.666  -2.000  31.866  1.00 41.54           C  
ANISOU 2152  CB  ASP A1072     4864   7428   3493    769   1593   1517       C  
ATOM   2153  CG  ASP A1072      19.904  -1.585  30.621  1.00 57.17           C  
ANISOU 2153  CG  ASP A1072     6926   9677   5119    598   1589   1501       C  
ATOM   2154  OD1 ASP A1072      18.807  -1.003  30.762  1.00 58.23           O  
ANISOU 2154  OD1 ASP A1072     7138   9797   5192    495   1356   1554       O  
ATOM   2155  OD2 ASP A1072      20.406  -1.837  29.505  1.00 65.35           O  
ANISOU 2155  OD2 ASP A1072     7936  10957   5936    566   1822   1448       O  
ATOM   2156  N   ALA A1073      21.318  -3.473  34.697  1.00 38.97           N  
ANISOU 2156  N   ALA A1073     4503   6516   3788   1089   1512   1466       N  
ATOM   2157  CA  ALA A1073      22.140  -4.347  35.542  1.00 38.67           C  
ANISOU 2157  CA  ALA A1073     4366   6308   4021   1269   1592   1503       C  
ATOM   2158  C   ALA A1073      21.277  -5.461  36.156  1.00 42.91           C  
ANISOU 2158  C   ALA A1073     5092   6605   4606   1330   1609   1305       C  
ATOM   2159  O   ALA A1073      21.732  -6.599  36.236  1.00 43.66           O  
ANISOU 2159  O   ALA A1073     5168   6553   4867   1492   1813   1230       O  
ATOM   2160  CB  ALA A1073      22.826  -3.540  36.634  1.00 39.23           C  
ANISOU 2160  CB  ALA A1073     4268   6361   4277   1254   1351   1776       C  
ATOM   2161  N   ALA A1074      20.021  -5.142  36.534  1.00 39.02           N  
ANISOU 2161  N   ALA A1074     4769   6066   3990   1205   1417   1231       N  
ATOM   2162  CA  ALA A1074      19.055  -6.093  37.092  1.00 38.73           C  
ANISOU 2162  CA  ALA A1074     4910   5825   3979   1218   1417   1061       C  
ATOM   2163  C   ALA A1074      18.587  -7.089  36.024  1.00 43.40           C  
ANISOU 2163  C   ALA A1074     5646   6398   4448   1200   1659    770       C  
ATOM   2164  O   ALA A1074      18.576  -8.294  36.287  1.00 42.94           O  
ANISOU 2164  O   ALA A1074     5661   6116   4537   1297   1811    639       O  
ATOM   2165  CB  ALA A1074      17.867  -5.353  37.688  1.00 39.20           C  
ANISOU 2165  CB  ALA A1074     5072   5882   3941   1083   1167   1075       C  
ATOM   2166  N   VAL A1075      18.244  -6.585  34.813  1.00 40.90           N  
ANISOU 2166  N   VAL A1075     5366   6315   3861   1064   1694    677       N  
ATOM   2167  CA  VAL A1075      17.811  -7.377  33.648  1.00 41.33           C  
ANISOU 2167  CA  VAL A1075     5565   6429   3711    986   1907    375       C  
ATOM   2168  C   VAL A1075      18.955  -8.308  33.185  1.00 48.30           C  
ANISOU 2168  C   VAL A1075     6400   7230   4721   1152   2254    252       C  
ATOM   2169  O   VAL A1075      18.692  -9.454  32.816  1.00 47.89           O  
ANISOU 2169  O   VAL A1075     6497   7019   4680   1164   2469    -41       O  
ATOM   2170  CB  VAL A1075      17.246  -6.467  32.516  1.00 44.58           C  
ANISOU 2170  CB  VAL A1075     5996   7177   3767    785   1821    377       C  
ATOM   2171  CG1 VAL A1075      17.108  -7.209  31.185  1.00 44.13           C  
ANISOU 2171  CG1 VAL A1075     6066   7266   3435    682   2064     68       C  
ATOM   2172  CG2 VAL A1075      15.912  -5.855  32.927  1.00 44.20           C  
ANISOU 2172  CG2 VAL A1075     6005   7148   3642    646   1529    444       C  
ATOM   2173  N   ARG A1076      20.218  -7.830  33.269  1.00 47.06           N  
ANISOU 2173  N   ARG A1076     6025   7156   4701   1284   2313    479       N  
ATOM   2174  CA  ARG A1076      21.411  -8.611  32.933  1.00 48.14           C  
ANISOU 2174  CA  ARG A1076     6048   7221   5022   1483   2652    424       C  
ATOM   2175  C   ARG A1076      21.551  -9.799  33.900  1.00 53.77           C  
ANISOU 2175  C   ARG A1076     6778   7553   6097   1677   2735    394       C  
ATOM   2176  O   ARG A1076      21.882 -10.904  33.466  1.00 53.59           O  
ANISOU 2176  O   ARG A1076     6800   7353   6207   1809   3064    176       O  
ATOM   2177  CB  ARG A1076      22.674  -7.732  32.953  1.00 49.48           C  
ANISOU 2177  CB  ARG A1076     5931   7580   5291   1561   2641    741       C  
ATOM   2178  CG  ARG A1076      23.817  -8.278  32.107  1.00 62.66           C  
ANISOU 2178  CG  ARG A1076     7459   9310   7037   1722   3040    666       C  
ATOM   2179  CD  ARG A1076      25.052  -7.401  32.185  1.00 78.95           C  
ANISOU 2179  CD  ARG A1076     9202  11569   9226   1780   3009   1016       C  
ATOM   2180  NE  ARG A1076      24.954  -6.236  31.304  1.00 94.79           N  
ANISOU 2180  NE  ARG A1076    11188  13922  10906   1571   2934   1107       N  
ATOM   2181  CZ  ARG A1076      25.847  -5.252  31.252  1.00114.23           C  
ANISOU 2181  CZ  ARG A1076    13394  16584  13423   1542   2870   1420       C  
ATOM   2182  NH1 ARG A1076      26.921  -5.278  32.031  1.00105.00           N  
ANISOU 2182  NH1 ARG A1076    11954  15336  12607   1697   2855   1663       N  
ATOM   2183  NH2 ARG A1076      25.671  -4.233  30.422  1.00101.62           N  
ANISOU 2183  NH2 ARG A1076    11797  15277  11538   1345   2809   1520       N  
ATOM   2184  N   GLY A1077      21.254  -9.563  35.179  1.00 51.49           N  
ANISOU 2184  N   GLY A1077     6467   7140   5959   1683   2448    609       N  
ATOM   2185  CA  GLY A1077      21.284 -10.585  36.219  1.00 51.82           C  
ANISOU 2185  CA  GLY A1077     6522   6850   6319   1837   2465    660       C  
ATOM   2186  C   GLY A1077      20.256 -11.673  35.975  1.00 56.44           C  
ANISOU 2186  C   GLY A1077     7369   7197   6879   1772   2590    339       C  
ATOM   2187  O   GLY A1077      20.609 -12.857  35.928  1.00 56.03           O  
ANISOU 2187  O   GLY A1077     7347   6853   7089   1931   2846    227       O  
ATOM   2188  N   ILE A1078      18.978 -11.261  35.790  1.00 53.18           N  
ANISOU 2188  N   ILE A1078     7132   6899   6176   1533   2410    201       N  
ATOM   2189  CA  ILE A1078      17.810 -12.114  35.518  1.00 53.10           C  
ANISOU 2189  CA  ILE A1078     7363   6726   6088   1392   2467   -102       C  
ATOM   2190  C   ILE A1078      18.062 -13.090  34.346  1.00 58.93           C  
ANISOU 2190  C   ILE A1078     8219   7367   6804   1405   2837   -470       C  
ATOM   2191  O   ILE A1078      17.805 -14.288  34.486  1.00 58.65           O  
ANISOU 2191  O   ILE A1078     8320   6995   6968   1439   3008   -666       O  
ATOM   2192  CB  ILE A1078      16.532 -11.243  35.321  1.00 55.79           C  
ANISOU 2192  CB  ILE A1078     7794   7304   6099   1132   2198   -136       C  
ATOM   2193  CG1 ILE A1078      16.115 -10.555  36.639  1.00 55.68           C  
ANISOU 2193  CG1 ILE A1078     7712   7285   6160   1130   1892    152       C  
ATOM   2194  CG2 ILE A1078      15.368 -12.056  34.746  1.00 56.67           C  
ANISOU 2194  CG2 ILE A1078     8124   7330   6078    937   2261   -470       C  
ATOM   2195  CD1 ILE A1078      15.311  -9.261  36.467  1.00 60.61           C  
ANISOU 2195  CD1 ILE A1078     8322   8184   6524    956   1639    227       C  
ATOM   2196  N   LEU A1079      18.589 -12.580  33.215  1.00 57.02           N  
ANISOU 2196  N   LEU A1079     7927   7411   6327   1375   2975   -562       N  
ATOM   2197  CA  LEU A1079      18.893 -13.386  32.024  1.00 57.32           C  
ANISOU 2197  CA  LEU A1079     8080   7424   6274   1371   3355   -942       C  
ATOM   2198  C   LEU A1079      20.066 -14.349  32.244  1.00 62.27           C  
ANISOU 2198  C   LEU A1079     8609   7722   7327   1683   3705   -956       C  
ATOM   2199  O   LEU A1079      20.142 -15.378  31.568  1.00 61.85           O  
ANISOU 2199  O   LEU A1079     8706   7465   7329   1708   4053  -1329       O  
ATOM   2200  CB  LEU A1079      19.117 -12.506  30.775  1.00 57.37           C  
ANISOU 2200  CB  LEU A1079     8049   7885   5863   1235   3400   -996       C  
ATOM   2201  CG  LEU A1079      17.948 -11.602  30.338  1.00 61.89           C  
ANISOU 2201  CG  LEU A1079     8716   8794   6006    923   3095   -998       C  
ATOM   2202  CD1 LEU A1079      18.418 -10.541  29.362  1.00 61.68           C  
ANISOU 2202  CD1 LEU A1079     8566   9211   5660    848   3076   -848       C  
ATOM   2203  CD2 LEU A1079      16.785 -12.407  29.755  1.00 64.34           C  
ANISOU 2203  CD2 LEU A1079     9292   9073   6081    680   3162  -1420       C  
ATOM   2204  N   ARG A1080      20.965 -14.025  33.197  1.00 59.73           N  
ANISOU 2204  N   ARG A1080     8031   7345   7317   1914   3611   -552       N  
ATOM   2205  CA  ARG A1080      22.105 -14.873  33.558  1.00 59.93           C  
ANISOU 2205  CA  ARG A1080     7893   7070   7807   2242   3894   -456       C  
ATOM   2206  C   ARG A1080      21.703 -15.911  34.625  1.00 64.59           C  
ANISOU 2206  C   ARG A1080     8561   7205   8773   2343   3858   -392       C  
ATOM   2207  O   ARG A1080      22.410 -16.905  34.814  1.00 64.98           O  
ANISOU 2207  O   ARG A1080     8542   6907   9240   2602   4144   -391       O  
ATOM   2208  CB  ARG A1080      23.322 -14.033  34.000  1.00 60.32           C  
ANISOU 2208  CB  ARG A1080     7591   7329   8000   2416   3799    -26       C  
ATOM   2209  CG  ARG A1080      24.036 -13.343  32.837  1.00 72.03           C  
ANISOU 2209  CG  ARG A1080     8955   9168   9244   2396   3997    -95       C  
ATOM   2210  CD  ARG A1080      25.468 -12.962  33.166  1.00 85.83           C  
ANISOU 2210  CD  ARG A1080    10322  11023  11266   2623   4034    286       C  
ATOM   2211  NE  ARG A1080      26.153 -12.375  32.009  1.00 98.02           N  
ANISOU 2211  NE  ARG A1080    11746  12914  12584   2593   4259    227       N  
ATOM   2212  CZ  ARG A1080      27.474 -12.338  31.849  1.00112.79           C  
ANISOU 2212  CZ  ARG A1080    13292  14867  14695   2811   4485    422       C  
ATOM   2213  NH1 ARG A1080      28.277 -12.874  32.761  1.00100.36           N  
ANISOU 2213  NH1 ARG A1080    11467  13054  13611   3087   4504    701       N  
ATOM   2214  NH2 ARG A1080      28.001 -11.782  30.766  1.00 98.79           N  
ANISOU 2214  NH2 ARG A1080    11426  13437  12675   2752   4698    366       N  
ATOM   2215  N   ASN A1081      20.547 -15.693  35.287  1.00 60.80           N  
ANISOU 2215  N   ASN A1081     8218   6724   8160   2143   3526   -329       N  
ATOM   2216  CA  ASN A1081      19.986 -16.576  36.314  1.00 60.26           C  
ANISOU 2216  CA  ASN A1081     8240   6277   8380   2179   3456   -241       C  
ATOM   2217  C   ASN A1081      19.127 -17.660  35.643  1.00 63.43           C  
ANISOU 2217  C   ASN A1081     8935   6389   8776   2038   3687   -699       C  
ATOM   2218  O   ASN A1081      18.169 -17.334  34.938  1.00 62.70           O  
ANISOU 2218  O   ASN A1081     9022   6500   8300   1752   3605   -980       O  
ATOM   2219  CB  ASN A1081      19.157 -15.762  37.322  1.00 59.31           C  
ANISOU 2219  CB  ASN A1081     8120   6330   8086   2012   3025     20       C  
ATOM   2220  CG  ASN A1081      18.917 -16.455  38.639  1.00 75.13           C  
ANISOU 2220  CG  ASN A1081    10130   8028  10387   2087   2919    263       C  
ATOM   2221  OD1 ASN A1081      18.181 -17.443  38.729  1.00 70.39           O  
ANISOU 2221  OD1 ASN A1081     9718   7120   9906   2014   3017     87       O  
ATOM   2222  ND2 ASN A1081      19.521 -15.937  39.697  1.00 63.61           N  
ANISOU 2222  ND2 ASN A1081     8465   6667   9036   2206   2703    684       N  
ATOM   2223  N   ALA A1082      19.484 -18.943  35.852  1.00 59.70           N  
ANISOU 2223  N   ALA A1082     8499   5436   8747   2232   3971   -763       N  
ATOM   2224  CA  ALA A1082      18.785 -20.097  35.268  1.00 59.19           C  
ANISOU 2224  CA  ALA A1082     8719   5005   8765   2107   4231  -1216       C  
ATOM   2225  C   ALA A1082      17.324 -20.248  35.720  1.00 62.17           C  
ANISOU 2225  C   ALA A1082     9297   5326   8998   1801   3973  -1279       C  
ATOM   2226  O   ALA A1082      16.509 -20.772  34.960  1.00 61.63           O  
ANISOU 2226  O   ALA A1082     9473   5165   8778   1554   4087  -1715       O  
ATOM   2227  CB  ALA A1082      19.557 -21.376  35.544  1.00 59.80           C  
ANISOU 2227  CB  ALA A1082     8757   4527   9437   2419   4583  -1191       C  
ATOM   2228  N   LYS A1083      17.000 -19.790  36.945  1.00 57.91           N  
ANISOU 2228  N   LYS A1083     8648   4864   8491   1800   3633   -857       N  
ATOM   2229  CA  LYS A1083      15.653 -19.861  37.521  1.00 57.25           C  
ANISOU 2229  CA  LYS A1083     8704   4757   8294   1536   3391   -848       C  
ATOM   2230  C   LYS A1083      14.738 -18.721  37.057  1.00 59.69           C  
ANISOU 2230  C   LYS A1083     9049   5547   8085   1247   3118   -952       C  
ATOM   2231  O   LYS A1083      13.520 -18.907  36.995  1.00 58.86           O  
ANISOU 2231  O   LYS A1083     9089   5439   7835    976   3010  -1119       O  
ATOM   2232  CB  LYS A1083      15.724 -19.852  39.059  1.00 60.08           C  
ANISOU 2232  CB  LYS A1083     8927   5013   8889   1664   3177   -349       C  
ATOM   2233  CG  LYS A1083      16.271 -21.128  39.690  1.00 75.29           C  
ANISOU 2233  CG  LYS A1083    10834   6416  11357   1898   3393   -181       C  
ATOM   2234  CD  LYS A1083      17.677 -20.917  40.239  1.00 86.31           C  
ANISOU 2234  CD  LYS A1083    11953   7845  12998   2243   3403    226       C  
ATOM   2235  CE  LYS A1083      18.125 -22.042  41.140  1.00 98.77           C  
ANISOU 2235  CE  LYS A1083    13459   8957  15113   2478   3520    549       C  
ATOM   2236  NZ  LYS A1083      17.508 -21.954  42.491  1.00109.15           N  
ANISOU 2236  NZ  LYS A1083    14757  10311  16402   2380   3215    943       N  
ATOM   2237  N   LEU A1084      15.323 -17.540  36.761  1.00 55.64           N  
ANISOU 2237  N   LEU A1084     8380   5434   7326   1305   3003   -820       N  
ATOM   2238  CA  LEU A1084      14.599 -16.318  36.386  1.00 55.02           C  
ANISOU 2238  CA  LEU A1084     8291   5804   6811   1082   2736   -829       C  
ATOM   2239  C   LEU A1084      14.505 -16.035  34.877  1.00 59.22           C  
ANISOU 2239  C   LEU A1084     8908   6604   6991    918   2850  -1176       C  
ATOM   2240  O   LEU A1084      13.585 -15.326  34.460  1.00 58.39           O  
ANISOU 2240  O   LEU A1084     8830   6814   6542    682   2637  -1223       O  
ATOM   2241  CB  LEU A1084      15.200 -15.094  37.108  1.00 54.81           C  
ANISOU 2241  CB  LEU A1084     8046   6040   6738   1211   2499   -428       C  
ATOM   2242  CG  LEU A1084      15.328 -15.162  38.639  1.00 59.21           C  
ANISOU 2242  CG  LEU A1084     8511   6444   7544   1338   2340    -60       C  
ATOM   2243  CD1 LEU A1084      16.214 -14.047  39.157  1.00 59.32           C  
ANISOU 2243  CD1 LEU A1084     8311   6696   7530   1471   2172    267       C  
ATOM   2244  CD2 LEU A1084      13.965 -15.122  39.326  1.00 61.13           C  
ANISOU 2244  CD2 LEU A1084     8849   6695   7683   1136   2132    -36       C  
ATOM   2245  N   LYS A1085      15.454 -16.548  34.069  1.00 56.46           N  
ANISOU 2245  N   LYS A1085     8584   6151   6717   1043   3186  -1398       N  
ATOM   2246  CA  LYS A1085      15.476 -16.331  32.616  1.00 56.63           C  
ANISOU 2246  CA  LYS A1085     8695   6456   6365    884   3334  -1738       C  
ATOM   2247  C   LYS A1085      14.230 -16.894  31.871  1.00 61.05           C  
ANISOU 2247  C   LYS A1085     9502   7028   6667    532   3328  -2150       C  
ATOM   2248  O   LYS A1085      13.664 -16.135  31.078  1.00 60.27           O  
ANISOU 2248  O   LYS A1085     9420   7353   6128    295   3167  -2223       O  
ATOM   2249  CB  LYS A1085      16.783 -16.853  31.989  1.00 59.35           C  
ANISOU 2249  CB  LYS A1085     9006   6672   6872   1118   3747  -1897       C  
ATOM   2250  CG  LYS A1085      17.007 -16.429  30.541  1.00 72.95           C  
ANISOU 2250  CG  LYS A1085    10775   8787   8156    980   3903  -2169       C  
ATOM   2251  CD  LYS A1085      17.982 -17.361  29.831  1.00 83.68           C  
ANISOU 2251  CD  LYS A1085    12187   9926   9680   1157   4404  -2494       C  
ATOM   2252  CE  LYS A1085      18.216 -16.968  28.392  1.00 96.49           C  
ANISOU 2252  CE  LYS A1085    13867  11975  10818   1004   4588  -2775       C  
ATOM   2253  NZ  LYS A1085      17.051 -17.285  27.521  1.00105.99           N  
ANISOU 2253  NZ  LYS A1085    15354  13326  11591    606   4548  -3212       N  
ATOM   2254  N   PRO A1086      13.779 -18.170  32.071  1.00 58.22           N  
ANISOU 2254  N   PRO A1086     9324   6234   6562    467   3483  -2407       N  
ATOM   2255  CA  PRO A1086      12.611 -18.656  31.308  1.00 58.08           C  
ANISOU 2255  CA  PRO A1086     9529   6267   6273     83   3456  -2814       C  
ATOM   2256  C   PRO A1086      11.290 -17.957  31.628  1.00 61.02           C  
ANISOU 2256  C   PRO A1086     9854   6929   6401   -183   3042  -2639       C  
ATOM   2257  O   PRO A1086      10.458 -17.822  30.729  1.00 61.09           O  
ANISOU 2257  O   PRO A1086     9957   7230   6025   -512   2939  -2885       O  
ATOM   2258  CB  PRO A1086      12.561 -20.156  31.629  1.00 59.98           C  
ANISOU 2258  CB  PRO A1086     9945   5901   6941    108   3722  -3065       C  
ATOM   2259  CG  PRO A1086      13.889 -20.480  32.232  1.00 64.41           C  
ANISOU 2259  CG  PRO A1086    10380   6133   7959    537   3965  -2843       C  
ATOM   2260  CD  PRO A1086      14.299 -19.238  32.948  1.00 59.85           C  
ANISOU 2260  CD  PRO A1086     9536   5884   7318    717   3685  -2328       C  
ATOM   2261  N   VAL A1087      11.102 -17.497  32.884  1.00 56.09           N  
ANISOU 2261  N   VAL A1087     9074   6250   5986    -46   2812  -2214       N  
ATOM   2262  CA  VAL A1087       9.880 -16.789  33.277  1.00 55.37           C  
ANISOU 2262  CA  VAL A1087     8909   6413   5717   -248   2457  -2025       C  
ATOM   2263  C   VAL A1087       9.877 -15.364  32.668  1.00 58.75           C  
ANISOU 2263  C   VAL A1087     9196   7369   5756   -291   2247  -1864       C  
ATOM   2264  O   VAL A1087       8.874 -14.984  32.064  1.00 58.13           O  
ANISOU 2264  O   VAL A1087     9120   7594   5373   -566   2052  -1935       O  
ATOM   2265  CB  VAL A1087       9.566 -16.838  34.810  1.00 58.82           C  
ANISOU 2265  CB  VAL A1087     9253   6613   6481   -117   2319  -1675       C  
ATOM   2266  CG1 VAL A1087      10.686 -16.250  35.663  1.00 58.62           C  
ANISOU 2266  CG1 VAL A1087     9066   6573   6634    222   2308  -1308       C  
ATOM   2267  CG2 VAL A1087       8.224 -16.189  35.142  1.00 58.46           C  
ANISOU 2267  CG2 VAL A1087     9134   6809   6268   -335   2012  -1539       C  
ATOM   2268  N   TYR A1088      11.011 -14.629  32.753  1.00 55.24           N  
ANISOU 2268  N   TYR A1088     8622   7031   5337    -37   2293  -1645       N  
ATOM   2269  CA  TYR A1088      11.168 -13.271  32.213  1.00 55.17           C  
ANISOU 2269  CA  TYR A1088     8473   7466   5022    -54   2121  -1451       C  
ATOM   2270  C   TYR A1088      10.888 -13.191  30.709  1.00 59.59           C  
ANISOU 2270  C   TYR A1088     9120   8373   5146   -308   2160  -1724       C  
ATOM   2271  O   TYR A1088      10.196 -12.268  30.276  1.00 59.40           O  
ANISOU 2271  O   TYR A1088     9015   8721   4833   -476   1910  -1587       O  
ATOM   2272  CB  TYR A1088      12.562 -12.708  32.537  1.00 56.37           C  
ANISOU 2272  CB  TYR A1088     8479   7613   5327    245   2209  -1200       C  
ATOM   2273  CG  TYR A1088      12.754 -11.253  32.160  1.00 58.09           C  
ANISOU 2273  CG  TYR A1088     8540   8226   5305    234   2023   -943       C  
ATOM   2274  CD1 TYR A1088      12.295 -10.230  32.987  1.00 59.92           C  
ANISOU 2274  CD1 TYR A1088     8645   8535   5588    256   1736   -624       C  
ATOM   2275  CD2 TYR A1088      13.433 -10.897  30.997  1.00 58.77           C  
ANISOU 2275  CD2 TYR A1088     8608   8591   5133    207   2157  -1015       C  
ATOM   2276  CE1 TYR A1088      12.480  -8.888  32.652  1.00 60.29           C  
ANISOU 2276  CE1 TYR A1088     8554   8884   5471    248   1578   -382       C  
ATOM   2277  CE2 TYR A1088      13.619  -9.558  30.648  1.00 59.69           C  
ANISOU 2277  CE2 TYR A1088     8576   9047   5057    187   1988   -739       C  
ATOM   2278  CZ  TYR A1088      13.144  -8.557  31.481  1.00 67.17           C  
ANISOU 2278  CZ  TYR A1088     9401  10019   6102    211   1695   -419       C  
ATOM   2279  OH  TYR A1088      13.323  -7.237  31.140  1.00 67.91           O  
ANISOU 2279  OH  TYR A1088     9354  10390   6059    192   1541   -144       O  
ATOM   2280  N   ASP A1089      11.419 -14.154  29.922  1.00 56.22           N  
ANISOU 2280  N   ASP A1089     8856   7829   4674   -338   2479  -2104       N  
ATOM   2281  CA  ASP A1089      11.228 -14.229  28.470  1.00 56.17           C  
ANISOU 2281  CA  ASP A1089     8971   8161   4210   -604   2562  -2428       C  
ATOM   2282  C   ASP A1089       9.757 -14.459  28.095  1.00 59.94           C  
ANISOU 2282  C   ASP A1089     9542   8797   4435   -988   2335  -2603       C  
ATOM   2283  O   ASP A1089       9.298 -13.921  27.087  1.00 59.79           O  
ANISOU 2283  O   ASP A1089     9517   9239   3961  -1239   2194  -2644       O  
ATOM   2284  CB  ASP A1089      12.106 -15.341  27.854  1.00 58.10           C  
ANISOU 2284  CB  ASP A1089     9391   8169   4515   -536   3007  -2852       C  
ATOM   2285  CG  ASP A1089      13.616 -15.129  27.903  1.00 67.70           C  
ANISOU 2285  CG  ASP A1089    10485   9315   5925   -183   3270  -2708       C  
ATOM   2286  OD1 ASP A1089      14.053 -13.999  28.223  1.00 68.38           O  
ANISOU 2286  OD1 ASP A1089    10357   9634   5990    -46   3095  -2297       O  
ATOM   2287  OD2 ASP A1089      14.359 -16.092  27.611  1.00 72.09           O  
ANISOU 2287  OD2 ASP A1089    11146   9573   6672    -47   3659  -3007       O  
ATOM   2288  N   SER A1090       9.027 -15.251  28.908  1.00 55.95           N  
ANISOU 2288  N   SER A1090     9102   7932   4226  -1042   2291  -2673       N  
ATOM   2289  CA  SER A1090       7.621 -15.595  28.685  1.00 55.61           C  
ANISOU 2289  CA  SER A1090     9120   7991   4020  -1412   2082  -2830       C  
ATOM   2290  C   SER A1090       6.623 -14.515  29.140  1.00 58.67           C  
ANISOU 2290  C   SER A1090     9284   8678   4332  -1477   1683  -2424       C  
ATOM   2291  O   SER A1090       5.451 -14.575  28.756  1.00 58.96           O  
ANISOU 2291  O   SER A1090     9307   8950   4147  -1802   1470  -2497       O  
ATOM   2292  CB  SER A1090       7.293 -16.936  29.337  1.00 59.47           C  
ANISOU 2292  CB  SER A1090     9762   7951   4884  -1456   2231  -3064       C  
ATOM   2293  OG  SER A1090       7.393 -16.869  30.750  1.00 68.73           O  
ANISOU 2293  OG  SER A1090    10818   8804   6493  -1177   2189  -2716       O  
ATOM   2294  N   LEU A1091       7.077 -13.544  29.956  1.00 53.48           N  
ANISOU 2294  N   LEU A1091     8445   8005   3871  -1178   1589  -2007       N  
ATOM   2295  CA  LEU A1091       6.223 -12.469  30.471  1.00 52.48           C  
ANISOU 2295  CA  LEU A1091     8106   8099   3736  -1185   1263  -1630       C  
ATOM   2296  C   LEU A1091       6.152 -11.249  29.548  1.00 55.70           C  
ANISOU 2296  C   LEU A1091     8378   9005   3782  -1257   1076  -1431       C  
ATOM   2297  O   LEU A1091       7.098 -10.967  28.809  1.00 54.97           O  
ANISOU 2297  O   LEU A1091     8317   9066   3503  -1192   1209  -1463       O  
ATOM   2298  CB  LEU A1091       6.665 -12.022  31.883  1.00 52.17           C  
ANISOU 2298  CB  LEU A1091     7956   7791   4074   -861   1250  -1308       C  
ATOM   2299  CG  LEU A1091       6.529 -13.013  33.047  1.00 56.21           C  
ANISOU 2299  CG  LEU A1091     8541   7860   4955   -788   1352  -1354       C  
ATOM   2300  CD1 LEU A1091       7.297 -12.523  34.265  1.00 56.07           C  
ANISOU 2300  CD1 LEU A1091     8434   7651   5219   -465   1369  -1052       C  
ATOM   2301  CD2 LEU A1091       5.071 -13.292  33.401  1.00 58.00           C  
ANISOU 2301  CD2 LEU A1091     8724   8107   5205  -1018   1175  -1346       C  
ATOM   2302  N   ASP A1092       5.023 -10.514  29.629  1.00 51.86           N  
ANISOU 2302  N   ASP A1092     7719   8762   3224  -1380    777  -1189       N  
ATOM   2303  CA  ASP A1092       4.757  -9.265  28.909  1.00 51.09           C  
ANISOU 2303  CA  ASP A1092     7445   9109   2856  -1437    551   -899       C  
ATOM   2304  C   ASP A1092       5.478  -8.115  29.639  1.00 52.19           C  
ANISOU 2304  C   ASP A1092     7445   9162   3224  -1110    528   -530       C  
ATOM   2305  O   ASP A1092       5.919  -8.302  30.769  1.00 51.30           O  
ANISOU 2305  O   ASP A1092     7352   8691   3447   -887    632   -498       O  
ATOM   2306  CB  ASP A1092       3.239  -8.997  28.848  1.00 53.27           C  
ANISOU 2306  CB  ASP A1092     7559   9623   3060  -1665    252   -762       C  
ATOM   2307  CG  ASP A1092       2.559  -9.000  30.210  1.00 65.11           C  
ANISOU 2307  CG  ASP A1092     8949  10836   4953  -1536    188   -612       C  
ATOM   2308  OD1 ASP A1092       2.379 -10.097  30.780  1.00 65.81           O  
ANISOU 2308  OD1 ASP A1092     9162  10625   5218  -1592    310   -849       O  
ATOM   2309  OD2 ASP A1092       2.208  -7.904  30.703  1.00 70.39           O  
ANISOU 2309  OD2 ASP A1092     9413  11573   5760  -1382     34   -259       O  
ATOM   2310  N   ALA A1093       5.580  -6.933  29.001  1.00 47.64           N  
ANISOU 2310  N   ALA A1093     6726   8914   2462  -1105    383   -242       N  
ATOM   2311  CA  ALA A1093       6.252  -5.742  29.540  1.00 46.71           C  
ANISOU 2311  CA  ALA A1093     6475   8731   2541   -846    347    104       C  
ATOM   2312  C   ALA A1093       5.781  -5.309  30.930  1.00 48.85           C  
ANISOU 2312  C   ALA A1093     6646   8720   3197   -663    260    284       C  
ATOM   2313  O   ALA A1093       6.615  -4.895  31.740  1.00 48.58           O  
ANISOU 2313  O   ALA A1093     6607   8457   3394   -437    340    387       O  
ATOM   2314  CB  ALA A1093       6.142  -4.584  28.561  1.00 47.40           C  
ANISOU 2314  CB  ALA A1093     6412   9219   2380   -928    169    411       C  
ATOM   2315  N   VAL A1094       4.461  -5.417  31.210  1.00 43.93           N  
ANISOU 2315  N   VAL A1094     5934   8130   2627   -775    104    313       N  
ATOM   2316  CA  VAL A1094       3.858  -5.044  32.503  1.00 42.66           C  
ANISOU 2316  CA  VAL A1094     5673   7738   2797   -623     48    457       C  
ATOM   2317  C   VAL A1094       4.270  -6.029  33.620  1.00 44.81           C  
ANISOU 2317  C   VAL A1094     6099   7640   3288   -520    235    252       C  
ATOM   2318  O   VAL A1094       4.691  -5.590  34.694  1.00 44.88           O  
ANISOU 2318  O   VAL A1094     6094   7432   3527   -313    276    366       O  
ATOM   2319  CB  VAL A1094       2.319  -4.835  32.417  1.00 45.96           C  
ANISOU 2319  CB  VAL A1094     5909   8336   3219   -767   -153    577       C  
ATOM   2320  CG1 VAL A1094       1.737  -4.436  33.771  1.00 45.69           C  
ANISOU 2320  CG1 VAL A1094     5767   8069   3523   -591   -159    711       C  
ATOM   2321  CG2 VAL A1094       1.963  -3.788  31.365  1.00 45.48           C  
ANISOU 2321  CG2 VAL A1094     5666   8647   2966   -849   -358    855       C  
ATOM   2322  N   ARG A1095       4.176  -7.347  33.355  1.00 39.10           N  
ANISOU 2322  N   ARG A1095     5525   6842   2490   -676    346    -43       N  
ATOM   2323  CA  ARG A1095       4.560  -8.390  34.310  1.00 37.81           C  
ANISOU 2323  CA  ARG A1095     5505   6317   2546   -592    526   -208       C  
ATOM   2324  C   ARG A1095       6.083  -8.509  34.478  1.00 40.65           C  
ANISOU 2324  C   ARG A1095     5963   6498   2982   -386    709   -236       C  
ATOM   2325  O   ARG A1095       6.538  -8.999  35.518  1.00 40.60           O  
ANISOU 2325  O   ARG A1095     6012   6203   3211   -239    815   -230       O  
ATOM   2326  CB  ARG A1095       3.910  -9.734  33.963  1.00 36.42           C  
ANISOU 2326  CB  ARG A1095     5450   6073   2316   -835    590   -503       C  
ATOM   2327  CG  ARG A1095       2.402  -9.726  34.171  1.00 42.82           C  
ANISOU 2327  CG  ARG A1095     6129   6992   3150  -1019    420   -441       C  
ATOM   2328  CD  ARG A1095       1.783 -11.078  33.926  1.00 45.70           C  
ANISOU 2328  CD  ARG A1095     6615   7244   3503  -1284    483   -734       C  
ATOM   2329  NE  ARG A1095       0.334 -11.043  34.116  1.00 46.68           N  
ANISOU 2329  NE  ARG A1095     6573   7504   3659  -1479    311   -648       N  
ATOM   2330  CZ  ARG A1095      -0.554 -10.985  33.130  1.00 59.08           C  
ANISOU 2330  CZ  ARG A1095     8042   9411   4996  -1764    127   -687       C  
ATOM   2331  NH1 ARG A1095      -0.152 -10.951  31.866  1.00 47.68           N  
ANISOU 2331  NH1 ARG A1095     6673   8219   3225  -1905     93   -826       N  
ATOM   2332  NH2 ARG A1095      -1.852 -10.961  33.400  1.00 44.58           N  
ANISOU 2332  NH2 ARG A1095     6012   7691   3236  -1923    -25   -575       N  
ATOM   2333  N   ARG A1096       6.869  -8.041  33.470  1.00 35.68           N  
ANISOU 2333  N   ARG A1096     5333   6069   2156   -380    743   -233       N  
ATOM   2334  CA  ARG A1096       8.338  -8.013  33.519  1.00 34.70           C  
ANISOU 2334  CA  ARG A1096     5247   5834   2104   -187    913   -220       C  
ATOM   2335  C   ARG A1096       8.806  -6.964  34.539  1.00 37.18           C  
ANISOU 2335  C   ARG A1096     5443   6065   2619     18    822     72       C  
ATOM   2336  O   ARG A1096       9.770  -7.198  35.267  1.00 36.09           O  
ANISOU 2336  O   ARG A1096     5324   5721   2668    189    929    104       O  
ATOM   2337  CB  ARG A1096       8.935  -7.705  32.137  1.00 33.59           C  
ANISOU 2337  CB  ARG A1096     5109   5982   1672   -262    972   -267       C  
ATOM   2338  CG  ARG A1096       9.102  -8.936  31.267  1.00 40.52           C  
ANISOU 2338  CG  ARG A1096     6159   6853   2385   -401   1183   -638       C  
ATOM   2339  CD  ARG A1096       9.860  -8.621  29.998  1.00 44.24           C  
ANISOU 2339  CD  ARG A1096     6636   7622   2550   -451   1290   -683       C  
ATOM   2340  NE  ARG A1096       9.873  -9.764  29.087  1.00 50.03           N  
ANISOU 2340  NE  ARG A1096     7556   8379   3076   -621   1501  -1095       N  
ATOM   2341  CZ  ARG A1096      10.633  -9.851  28.001  1.00 65.10           C  
ANISOU 2341  CZ  ARG A1096     9523  10498   4714   -665   1698  -1249       C  
ATOM   2342  NH1 ARG A1096      11.459  -8.863  27.679  1.00 52.18           N  
ANISOU 2342  NH1 ARG A1096     7754   9077   2995   -550   1702   -986       N  
ATOM   2343  NH2 ARG A1096      10.579 -10.929  27.232  1.00 53.71           N  
ANISOU 2343  NH2 ARG A1096     8275   9046   3086   -834   1909  -1679       N  
ATOM   2344  N   ALA A1097       8.096  -5.820  34.593  1.00 33.43           N  
ANISOU 2344  N   ALA A1097     4839   5748   2116     -8    623    283       N  
ATOM   2345  CA  ALA A1097       8.349  -4.709  35.506  1.00 33.11           C  
ANISOU 2345  CA  ALA A1097     4699   5626   2255    146    529    521       C  
ATOM   2346  C   ALA A1097       8.101  -5.140  36.946  1.00 36.84           C  
ANISOU 2346  C   ALA A1097     5213   5843   2942    232    550    500       C  
ATOM   2347  O   ALA A1097       8.851  -4.739  37.840  1.00 36.82           O  
ANISOU 2347  O   ALA A1097     5198   5711   3080    369    554    603       O  
ATOM   2348  CB  ALA A1097       7.453  -3.534  35.149  1.00 33.76           C  
ANISOU 2348  CB  ALA A1097     4641   5896   2290     91    343    719       C  
ATOM   2349  N   ALA A1098       7.057  -5.976  37.161  1.00 32.81           N  
ANISOU 2349  N   ALA A1098     4746   5280   2439    127    558    373       N  
ATOM   2350  CA  ALA A1098       6.672  -6.537  38.458  1.00 31.97           C  
ANISOU 2350  CA  ALA A1098     4683   4963   2503    172    595    361       C  
ATOM   2351  C   ALA A1098       7.786  -7.437  39.008  1.00 35.68           C  
ANISOU 2351  C   ALA A1098     5259   5214   3085    281    742    310       C  
ATOM   2352  O   ALA A1098       8.059  -7.408  40.208  1.00 35.36           O  
ANISOU 2352  O   ALA A1098     5225   5038   3172    384    744    411       O  
ATOM   2353  CB  ALA A1098       5.374  -7.322  38.319  1.00 32.57           C  
ANISOU 2353  CB  ALA A1098     4767   5055   2554     -3    585    243       C  
ATOM   2354  N   LEU A1099       8.442  -8.207  38.116  1.00 32.44           N  
ANISOU 2354  N   LEU A1099     4921   4783   2621    259    870    162       N  
ATOM   2355  CA  LEU A1099       9.555  -9.100  38.432  1.00 32.32           C  
ANISOU 2355  CA  LEU A1099     4976   4552   2752    388   1037    124       C  
ATOM   2356  C   LEU A1099      10.803  -8.287  38.810  1.00 36.18           C  
ANISOU 2356  C   LEU A1099     5374   5071   3301    560   1011    317       C  
ATOM   2357  O   LEU A1099      11.462  -8.625  39.790  1.00 36.15           O  
ANISOU 2357  O   LEU A1099     5364   4907   3464    686   1041    426       O  
ATOM   2358  CB  LEU A1099       9.837 -10.038  37.239  1.00 32.39           C  
ANISOU 2358  CB  LEU A1099     5081   4540   2685    315   1214   -126       C  
ATOM   2359  CG  LEU A1099      10.706 -11.274  37.513  1.00 37.32           C  
ANISOU 2359  CG  LEU A1099     5789   4862   3527    440   1437   -215       C  
ATOM   2360  CD1 LEU A1099       9.947 -12.324  38.329  1.00 37.95           C  
ANISOU 2360  CD1 LEU A1099     5962   4675   3783    379   1471   -264       C  
ATOM   2361  CD2 LEU A1099      11.188 -11.896  36.216  1.00 39.02           C  
ANISOU 2361  CD2 LEU A1099     6087   5094   3646    399   1644   -481       C  
ATOM   2362  N   ILE A1100      11.103  -7.208  38.049  1.00 32.57           N  
ANISOU 2362  N   ILE A1100     4834   4831   2711    545    940    385       N  
ATOM   2363  CA  ILE A1100      12.228  -6.285  38.279  1.00 32.27           C  
ANISOU 2363  CA  ILE A1100     4690   4846   2724    660    895    572       C  
ATOM   2364  C   ILE A1100      12.058  -5.603  39.649  1.00 36.65           C  
ANISOU 2364  C   ILE A1100     5212   5330   3385    704    748    726       C  
ATOM   2365  O   ILE A1100      13.023  -5.515  40.419  1.00 36.43           O  
ANISOU 2365  O   ILE A1100     5139   5235   3466    802    735    845       O  
ATOM   2366  CB  ILE A1100      12.367  -5.271  37.103  1.00 34.98           C  
ANISOU 2366  CB  ILE A1100     4957   5435   2898    595    849    627       C  
ATOM   2367  CG1 ILE A1100      12.876  -5.975  35.818  1.00 35.00           C  
ANISOU 2367  CG1 ILE A1100     4999   5536   2762    561   1037    466       C  
ATOM   2368  CG2 ILE A1100      13.270  -4.084  37.472  1.00 35.54           C  
ANISOU 2368  CG2 ILE A1100     4909   5545   3049    668    758    848       C  
ATOM   2369  CD1 ILE A1100      12.495  -5.270  34.496  1.00 35.93           C  
ANISOU 2369  CD1 ILE A1100     5087   5952   2612    416    986    474       C  
ATOM   2370  N   ASN A1101      10.813  -5.168  39.954  1.00 32.84           N  
ANISOU 2370  N   ASN A1101     4744   4873   2862    624    648    712       N  
ATOM   2371  CA  ASN A1101      10.409  -4.567  41.226  1.00 32.69           C  
ANISOU 2371  CA  ASN A1101     4718   4794   2910    647    550    795       C  
ATOM   2372  C   ASN A1101      10.799  -5.517  42.373  1.00 37.25           C  
ANISOU 2372  C   ASN A1101     5358   5220   3576    706    604    815       C  
ATOM   2373  O   ASN A1101      11.442  -5.081  43.331  1.00 36.89           O  
ANISOU 2373  O   ASN A1101     5294   5156   3568    755    537    923       O  
ATOM   2374  CB  ASN A1101       8.892  -4.328  41.221  1.00 32.39           C  
ANISOU 2374  CB  ASN A1101     4673   4801   2834    562    502    747       C  
ATOM   2375  CG  ASN A1101       8.363  -3.459  42.333  1.00 42.91           C  
ANISOU 2375  CG  ASN A1101     5984   6097   4222    589    435    804       C  
ATOM   2376  OD1 ASN A1101       8.642  -3.656  43.516  1.00 31.71           O  
ANISOU 2376  OD1 ASN A1101     4620   4592   2835    623    451    816       O  
ATOM   2377  ND2 ASN A1101       7.554  -2.487  41.968  1.00 35.55           N  
ANISOU 2377  ND2 ASN A1101     4970   5236   3301    572    367    843       N  
ATOM   2378  N   MET A1102      10.452  -6.821  42.238  1.00 34.58           N  
ANISOU 2378  N   MET A1102     5091   4776   3273    687    719    722       N  
ATOM   2379  CA  MET A1102      10.778  -7.880  43.198  1.00 35.09           C  
ANISOU 2379  CA  MET A1102     5207   4673   3451    745    784    782       C  
ATOM   2380  C   MET A1102      12.292  -8.055  43.345  1.00 40.38           C  
ANISOU 2380  C   MET A1102     5819   5301   4222    879    810    909       C  
ATOM   2381  O   MET A1102      12.763  -8.284  44.457  1.00 40.34           O  
ANISOU 2381  O   MET A1102     5801   5243   4283    937    767   1066       O  
ATOM   2382  CB  MET A1102      10.129  -9.215  42.799  1.00 37.36           C  
ANISOU 2382  CB  MET A1102     5584   4814   3799    682    918    646       C  
ATOM   2383  CG  MET A1102       8.658  -9.311  43.143  1.00 40.99           C  
ANISOU 2383  CG  MET A1102     6074   5289   4210    546    888    588       C  
ATOM   2384  SD  MET A1102       8.027 -10.991  42.894  1.00 45.05           S  
ANISOU 2384  SD  MET A1102     6696   5580   4842    439   1039    450       S  
ATOM   2385  CE  MET A1102       8.559 -11.771  44.437  1.00 41.67           C  
ANISOU 2385  CE  MET A1102     6300   4950   4582    549   1083    679       C  
ATOM   2386  N   VAL A1103      13.046  -7.951  42.226  1.00 37.60           N  
ANISOU 2386  N   VAL A1103     5415   4999   3871    921    881    858       N  
ATOM   2387  CA  VAL A1103      14.510  -8.069  42.193  1.00 37.51           C  
ANISOU 2387  CA  VAL A1103     5301   4974   3976   1055    930    984       C  
ATOM   2388  C   VAL A1103      15.148  -6.883  42.941  1.00 42.15           C  
ANISOU 2388  C   VAL A1103     5785   5691   4539   1058    747   1167       C  
ATOM   2389  O   VAL A1103      16.070  -7.088  43.725  1.00 41.35           O  
ANISOU 2389  O   VAL A1103     5602   5567   4542   1138    705   1343       O  
ATOM   2390  CB  VAL A1103      15.053  -8.253  40.737  1.00 40.92           C  
ANISOU 2390  CB  VAL A1103     5704   5457   4387   1082   1093    856       C  
ATOM   2391  CG1 VAL A1103      16.572  -8.104  40.666  1.00 40.49           C  
ANISOU 2391  CG1 VAL A1103     5490   5440   4453   1220   1142   1011       C  
ATOM   2392  CG2 VAL A1103      14.629  -9.602  40.159  1.00 40.53           C  
ANISOU 2392  CG2 VAL A1103     5775   5233   4391   1076   1296    644       C  
ATOM   2393  N   PHE A1104      14.626  -5.659  42.726  1.00 39.85           N  
ANISOU 2393  N   PHE A1104     5494   5525   4121    959    632   1132       N  
ATOM   2394  CA  PHE A1104      15.111  -4.430  43.369  1.00 40.14           C  
ANISOU 2394  CA  PHE A1104     5463   5647   4141    923    467   1251       C  
ATOM   2395  C   PHE A1104      14.970  -4.470  44.894  1.00 43.82           C  
ANISOU 2395  C   PHE A1104     5976   6080   4594    901    361   1319       C  
ATOM   2396  O   PHE A1104      15.816  -3.915  45.599  1.00 43.15           O  
ANISOU 2396  O   PHE A1104     5825   6056   4515    880    236   1437       O  
ATOM   2397  CB  PHE A1104      14.370  -3.202  42.809  1.00 42.24           C  
ANISOU 2397  CB  PHE A1104     5738   5988   4323    833    398   1189       C  
ATOM   2398  CG  PHE A1104      15.097  -2.437  41.729  1.00 44.31           C  
ANISOU 2398  CG  PHE A1104     5896   6354   4588    822    399   1255       C  
ATOM   2399  CD1 PHE A1104      15.062  -2.864  40.406  1.00 47.39           C  
ANISOU 2399  CD1 PHE A1104     6274   6818   4913    827    524   1194       C  
ATOM   2400  CD2 PHE A1104      15.769  -1.256  42.023  1.00 47.34           C  
ANISOU 2400  CD2 PHE A1104     6198   6770   5020    779    278   1372       C  
ATOM   2401  CE1 PHE A1104      15.718  -2.142  39.401  1.00 48.46           C  
ANISOU 2401  CE1 PHE A1104     6310   7086   5017    804    538   1281       C  
ATOM   2402  CE2 PHE A1104      16.425  -0.533  41.015  1.00 50.16           C  
ANISOU 2402  CE2 PHE A1104     6447   7222   5390    753    285   1467       C  
ATOM   2403  CZ  PHE A1104      16.396  -0.984  39.712  1.00 47.88           C  
ANISOU 2403  CZ  PHE A1104     6139   7033   5020    772    420   1437       C  
ATOM   2404  N   GLN A1105      13.910  -5.135  45.392  1.00 40.52           N  
ANISOU 2404  N   GLN A1105     5667   5590   4140    881    408   1248       N  
ATOM   2405  CA  GLN A1105      13.602  -5.244  46.815  1.00 40.44           C  
ANISOU 2405  CA  GLN A1105     5718   5580   4066    843    338   1307       C  
ATOM   2406  C   GLN A1105      14.385  -6.327  47.557  1.00 46.07           C  
ANISOU 2406  C   GLN A1105     6403   6250   4854    913    342   1493       C  
ATOM   2407  O   GLN A1105      14.989  -6.014  48.582  1.00 45.95           O  
ANISOU 2407  O   GLN A1105     6353   6328   4778    884    209   1632       O  
ATOM   2408  CB  GLN A1105      12.087  -5.424  47.035  1.00 41.33           C  
ANISOU 2408  CB  GLN A1105     5933   5659   4111    780    399   1179       C  
ATOM   2409  CG  GLN A1105      11.660  -5.358  48.508  1.00 45.94           C  
ANISOU 2409  CG  GLN A1105     6587   6288   4581    721    351   1217       C  
ATOM   2410  CD  GLN A1105      10.166  -5.297  48.725  1.00 54.41           C  
ANISOU 2410  CD  GLN A1105     7722   7355   5597    662    429   1094       C  
ATOM   2411  OE1 GLN A1105       9.356  -5.570  47.834  1.00 48.35           O  
ANISOU 2411  OE1 GLN A1105     6942   6540   4889    655    507   1005       O  
ATOM   2412  NE2 GLN A1105       9.766  -4.937  49.932  1.00 44.19           N  
ANISOU 2412  NE2 GLN A1105     6484   6132   4173    605    413   1084       N  
ATOM   2413  N   MET A1106      14.345  -7.592  47.080  1.00 43.94           N  
ANISOU 2413  N   MET A1106     6147   5833   4716    994    490   1500       N  
ATOM   2414  CA  MET A1106      14.962  -8.732  47.776  1.00 44.15           C  
ANISOU 2414  CA  MET A1106     6139   5761   4874   1085    518   1710       C  
ATOM   2415  C   MET A1106      16.162  -9.393  47.074  1.00 48.61           C  
ANISOU 2415  C   MET A1106     6577   6230   5662   1245    618   1806       C  
ATOM   2416  O   MET A1106      16.729 -10.346  47.621  1.00 48.14           O  
ANISOU 2416  O   MET A1106     6460   6060   5769   1352    650   2016       O  
ATOM   2417  CB  MET A1106      13.914  -9.813  48.127  1.00 46.61           C  
ANISOU 2417  CB  MET A1106     6571   5916   5221   1056    627   1688       C  
ATOM   2418  CG  MET A1106      12.574  -9.659  47.430  1.00 50.42           C  
ANISOU 2418  CG  MET A1106     7153   6369   5636    955    712   1428       C  
ATOM   2419  SD  MET A1106      11.770 -11.231  47.048  1.00 54.72           S  
ANISOU 2419  SD  MET A1106     7794   6647   6351    937    904   1353       S  
ATOM   2420  CE  MET A1106      11.190 -11.692  48.655  1.00 51.71           C  
ANISOU 2420  CE  MET A1106     7462   6267   5919    875    857   1571       C  
ATOM   2421  N   GLY A1107      16.550  -8.886  45.906  1.00 45.97           N  
ANISOU 2421  N   GLY A1107     6184   5944   5340   1268    675   1680       N  
ATOM   2422  CA  GLY A1107      17.680  -9.419  45.152  1.00 46.04           C  
ANISOU 2422  CA  GLY A1107     6059   5886   5549   1425    813   1739       C  
ATOM   2423  C   GLY A1107      17.350 -10.618  44.286  1.00 51.52           C  
ANISOU 2423  C   GLY A1107     6838   6352   6384   1500   1070   1564       C  
ATOM   2424  O   GLY A1107      16.225 -11.125  44.310  1.00 51.29           O  
ANISOU 2424  O   GLY A1107     6970   6212   6305   1411   1120   1411       O  
ATOM   2425  N   GLU A1108      18.355 -11.090  43.532  1.00 49.26           N  
ANISOU 2425  N   GLU A1108     6438   5994   6285   1657   1248   1576       N  
ATOM   2426  CA  GLU A1108      18.278 -12.223  42.603  1.00 49.45           C  
ANISOU 2426  CA  GLU A1108     6541   5783   6463   1741   1538   1365       C  
ATOM   2427  C   GLU A1108      17.934 -13.546  43.284  1.00 52.82           C  
ANISOU 2427  C   GLU A1108     7054   5896   7121   1808   1632   1428       C  
ATOM   2428  O   GLU A1108      17.003 -14.223  42.849  1.00 52.38           O  
ANISOU 2428  O   GLU A1108     7178   5664   7061   1719   1763   1182       O  
ATOM   2429  CB  GLU A1108      19.594 -12.365  41.825  1.00 51.06           C  
ANISOU 2429  CB  GLU A1108     6570   5993   6837   1922   1729   1393       C  
ATOM   2430  CG  GLU A1108      19.922 -11.179  40.939  1.00 63.41           C  
ANISOU 2430  CG  GLU A1108     8062   7847   8184   1841   1696   1310       C  
ATOM   2431  CD  GLU A1108      19.809 -11.468  39.458  1.00 87.04           C  
ANISOU 2431  CD  GLU A1108    11141  10836  11096   1829   1966    993       C  
ATOM   2432  OE1 GLU A1108      20.451 -12.438  38.991  1.00 75.43           O  
ANISOU 2432  OE1 GLU A1108     9628   9184   9849   2002   2250    922       O  
ATOM   2433  OE2 GLU A1108      19.083 -10.721  38.763  1.00 84.64           O  
ANISOU 2433  OE2 GLU A1108    10941  10716  10501   1645   1901    820       O  
ATOM   2434  N   THR A1109      18.690 -13.918  44.336  1.00 49.35           N  
ANISOU 2434  N   THR A1109     6474   5392   6885   1947   1556   1778       N  
ATOM   2435  CA  THR A1109      18.498 -15.167  45.088  1.00 49.41           C  
ANISOU 2435  CA  THR A1109     6528   5096   7152   2030   1630   1941       C  
ATOM   2436  C   THR A1109      17.121 -15.243  45.759  1.00 51.63           C  
ANISOU 2436  C   THR A1109     6999   5359   7257   1826   1518   1894       C  
ATOM   2437  O   THR A1109      16.510 -16.314  45.769  1.00 50.92           O  
ANISOU 2437  O   THR A1109     7033   4971   7343   1817   1664   1838       O  
ATOM   2438  CB  THR A1109      19.650 -15.407  46.082  1.00 63.39           C  
ANISOU 2438  CB  THR A1109     8064   6875   9145   2214   1527   2397       C  
ATOM   2439  OG1 THR A1109      19.859 -14.228  46.864  1.00 68.05           O  
ANISOU 2439  OG1 THR A1109     8560   7832   9465   2099   1219   2578       O  
ATOM   2440  CG2 THR A1109      20.945 -15.810  45.390  1.00 62.16           C  
ANISOU 2440  CG2 THR A1109     7703   6602   9313   2472   1740   2460       C  
ATOM   2441  N   GLY A1110      16.651 -14.106  46.281  1.00 47.22           N  
ANISOU 2441  N   GLY A1110     6458   5106   6379   1665   1284   1907       N  
ATOM   2442  CA  GLY A1110      15.352 -13.966  46.930  1.00 46.51           C  
ANISOU 2442  CA  GLY A1110     6515   5063   6094   1475   1186   1860       C  
ATOM   2443  C   GLY A1110      14.198 -14.341  46.024  1.00 49.54           C  
ANISOU 2443  C   GLY A1110     7062   5315   6446   1345   1330   1521       C  
ATOM   2444  O   GLY A1110      13.433 -15.253  46.351  1.00 49.19           O  
ANISOU 2444  O   GLY A1110     7122   5071   6498   1277   1403   1522       O  
ATOM   2445  N   VAL A1111      14.099 -13.673  44.854  1.00 45.60           N  
ANISOU 2445  N   VAL A1111     6576   4938   5812   1295   1366   1249       N  
ATOM   2446  CA  VAL A1111      13.055 -13.915  43.842  1.00 45.44           C  
ANISOU 2446  CA  VAL A1111     6690   4867   5710   1141   1470    918       C  
ATOM   2447  C   VAL A1111      13.118 -15.360  43.313  1.00 50.28           C  
ANISOU 2447  C   VAL A1111     7395   5122   6588   1184   1718    779       C  
ATOM   2448  O   VAL A1111      12.077 -16.001  43.162  1.00 49.90           O  
ANISOU 2448  O   VAL A1111     7476   4932   6552   1025   1777    612       O  
ATOM   2449  CB  VAL A1111      13.082 -12.867  42.696  1.00 48.91           C  
ANISOU 2449  CB  VAL A1111     7100   5557   5925   1081   1436    721       C  
ATOM   2450  CG1 VAL A1111      11.893 -13.035  41.748  1.00 48.57           C  
ANISOU 2450  CG1 VAL A1111     7175   5540   5740    880   1477    426       C  
ATOM   2451  CG2 VAL A1111      13.111 -11.453  43.255  1.00 48.61           C  
ANISOU 2451  CG2 VAL A1111     6970   5797   5703   1059   1213    871       C  
ATOM   2452  N   ALA A1112      14.343 -15.880  43.087  1.00 47.69           N  
ANISOU 2452  N   ALA A1112     6987   4631   6500   1399   1870    856       N  
ATOM   2453  CA  ALA A1112      14.595 -17.243  42.607  1.00 47.58           C  
ANISOU 2453  CA  ALA A1112     7051   4221   6807   1491   2150    726       C  
ATOM   2454  C   ALA A1112      14.096 -18.327  43.580  1.00 51.21           C  
ANISOU 2454  C   ALA A1112     7580   4358   7520   1478   2176    907       C  
ATOM   2455  O   ALA A1112      13.856 -19.458  43.159  1.00 51.58           O  
ANISOU 2455  O   ALA A1112     7749   4034   7814   1464   2397    729       O  
ATOM   2456  CB  ALA A1112      16.076 -17.426  42.317  1.00 48.39           C  
ANISOU 2456  CB  ALA A1112     6998   4246   7143   1765   2302    838       C  
ATOM   2457  N   GLY A1113      13.912 -17.955  44.849  1.00 47.04           N  
ANISOU 2457  N   GLY A1113     6984   3976   6912   1460   1958   1245       N  
ATOM   2458  CA  GLY A1113      13.409 -18.828  45.906  1.00 46.46           C  
ANISOU 2458  CA  GLY A1113     6957   3680   7015   1425   1949   1491       C  
ATOM   2459  C   GLY A1113      11.926 -19.143  45.814  1.00 49.46           C  
ANISOU 2459  C   GLY A1113     7502   3985   7306   1159   1968   1276       C  
ATOM   2460  O   GLY A1113      11.451 -20.047  46.503  1.00 48.72           O  
ANISOU 2460  O   GLY A1113     7467   3628   7417   1109   2025   1433       O  
ATOM   2461  N   PHE A1114      11.183 -18.400  44.967  1.00 46.00           N  
ANISOU 2461  N   PHE A1114     7117   3785   6576    978   1914    950       N  
ATOM   2462  CA  PHE A1114       9.748 -18.587  44.719  1.00 45.88           C  
ANISOU 2462  CA  PHE A1114     7214   3762   6456    705   1909    731       C  
ATOM   2463  C   PHE A1114       9.545 -19.566  43.543  1.00 51.23           C  
ANISOU 2463  C   PHE A1114     8031   4131   7301    610   2129    361       C  
ATOM   2464  O   PHE A1114       8.825 -19.247  42.595  1.00 50.85           O  
ANISOU 2464  O   PHE A1114     8041   4240   7039    411   2108     39       O  
ATOM   2465  CB  PHE A1114       9.081 -17.232  44.403  1.00 47.33           C  
ANISOU 2465  CB  PHE A1114     7350   4375   6260    570   1724    608       C  
ATOM   2466  CG  PHE A1114       8.816 -16.331  45.584  1.00 48.49           C  
ANISOU 2466  CG  PHE A1114     7406   4789   6228    580   1536    878       C  
ATOM   2467  CD1 PHE A1114       7.644 -16.454  46.324  1.00 51.10           C  
ANISOU 2467  CD1 PHE A1114     7753   5160   6503    418   1491    958       C  
ATOM   2468  CD2 PHE A1114       9.704 -15.316  45.918  1.00 50.31           C  
ANISOU 2468  CD2 PHE A1114     7537   5245   6335    730   1415   1026       C  
ATOM   2469  CE1 PHE A1114       7.384 -15.599  47.400  1.00 51.81           C  
ANISOU 2469  CE1 PHE A1114     7775   5508   6402    424   1356   1160       C  
ATOM   2470  CE2 PHE A1114       9.446 -14.465  46.995  1.00 52.93           C  
ANISOU 2470  CE2 PHE A1114     7815   5816   6482    713   1257   1216       C  
ATOM   2471  CZ  PHE A1114       8.284 -14.607  47.723  1.00 50.96           C  
ANISOU 2471  CZ  PHE A1114     7597   5604   6162    567   1241   1268       C  
ATOM   2472  N   THR A1115      10.167 -20.765  43.631  1.00 48.67           N  
ANISOU 2472  N   THR A1115     7759   3365   7367    746   2339    415       N  
ATOM   2473  CA  THR A1115      10.180 -21.830  42.618  1.00 49.10           C  
ANISOU 2473  CA  THR A1115     7967   3034   7654    693   2603     52       C  
ATOM   2474  C   THR A1115       8.793 -22.134  42.007  1.00 54.08           C  
ANISOU 2474  C   THR A1115     8744   3647   8157    325   2596   -293       C  
ATOM   2475  O   THR A1115       8.663 -22.093  40.780  1.00 54.39           O  
ANISOU 2475  O   THR A1115     8879   3739   8047    192   2680   -709       O  
ATOM   2476  CB  THR A1115      10.857 -23.103  43.175  1.00 58.26           C  
ANISOU 2476  CB  THR A1115     9144   3663   9328    897   2813    265       C  
ATOM   2477  OG1 THR A1115      12.053 -22.745  43.876  1.00 59.94           O  
ANISOU 2477  OG1 THR A1115     9171   3969   9633   1211   2753    668       O  
ATOM   2478  CG2 THR A1115      11.188 -24.121  42.086  1.00 54.53           C  
ANISOU 2478  CG2 THR A1115     8822   2760   9139    923   3143   -137       C  
ATOM   2479  N   ASN A1116       7.780 -22.433  42.846  1.00 50.51           N  
ANISOU 2479  N   ASN A1116     8294   3152   7746    147   2496   -112       N  
ATOM   2480  CA  ASN A1116       6.419 -22.757  42.395  1.00 50.22           C  
ANISOU 2480  CA  ASN A1116     8349   3110   7620   -222   2466   -377       C  
ATOM   2481  C   ASN A1116       5.681 -21.571  41.774  1.00 53.12           C  
ANISOU 2481  C   ASN A1116     8644   4002   7537   -401   2256   -546       C  
ATOM   2482  O   ASN A1116       4.988 -21.753  40.771  1.00 52.50           O  
ANISOU 2482  O   ASN A1116     8645   3972   7331   -673   2259   -902       O  
ATOM   2483  CB  ASN A1116       5.599 -23.391  43.523  1.00 52.19           C  
ANISOU 2483  CB  ASN A1116     8585   3180   8063   -348   2436    -81       C  
ATOM   2484  CG  ASN A1116       5.856 -24.864  43.731  1.00 76.24           C  
ANISOU 2484  CG  ASN A1116    11760   5612  11595   -341   2670    -57       C  
ATOM   2485  OD1 ASN A1116       6.973 -25.375  43.560  1.00 71.18           O  
ANISOU 2485  OD1 ASN A1116    11157   4650  11239    -79   2850    -29       O  
ATOM   2486  ND2 ASN A1116       4.818 -25.583  44.117  1.00 69.27           N  
ANISOU 2486  ND2 ASN A1116    10930   4539  10852   -624   2682    -46       N  
ATOM   2487  N   SER A1117       5.836 -20.365  42.362  1.00 49.16           N  
ANISOU 2487  N   SER A1117     7988   3885   6805   -257   2072   -285       N  
ATOM   2488  CA  SER A1117       5.230 -19.119  41.879  1.00 48.53           C  
ANISOU 2488  CA  SER A1117     7809   4281   6350   -365   1873   -367       C  
ATOM   2489  C   SER A1117       5.750 -18.778  40.480  1.00 51.74           C  
ANISOU 2489  C   SER A1117     8259   4832   6567   -371   1907   -683       C  
ATOM   2490  O   SER A1117       4.953 -18.442  39.603  1.00 51.11           O  
ANISOU 2490  O   SER A1117     8174   4997   6249   -606   1810   -900       O  
ATOM   2491  CB  SER A1117       5.536 -17.967  42.832  1.00 51.81           C  
ANISOU 2491  CB  SER A1117     8078   4979   6628   -173   1718    -36       C  
ATOM   2492  OG  SER A1117       5.166 -18.261  44.169  1.00 59.26           O  
ANISOU 2492  OG  SER A1117     8989   5839   7690   -168   1701    260       O  
ATOM   2493  N   LEU A1118       7.084 -18.896  40.272  1.00 48.04           N  
ANISOU 2493  N   LEU A1118     7818   4233   6204   -119   2049   -686       N  
ATOM   2494  CA  LEU A1118       7.764 -18.619  39.000  1.00 47.65           C  
ANISOU 2494  CA  LEU A1118     7806   4317   5980    -92   2133   -961       C  
ATOM   2495  C   LEU A1118       7.285 -19.558  37.889  1.00 52.88           C  
ANISOU 2495  C   LEU A1118     8648   4814   6629   -348   2286  -1405       C  
ATOM   2496  O   LEU A1118       7.070 -19.104  36.764  1.00 52.59           O  
ANISOU 2496  O   LEU A1118     8637   5072   6274   -507   2243  -1659       O  
ATOM   2497  CB  LEU A1118       9.301 -18.684  39.150  1.00 47.22           C  
ANISOU 2497  CB  LEU A1118     7711   4122   6107    245   2288   -836       C  
ATOM   2498  CG  LEU A1118       9.967 -17.646  40.069  1.00 51.10           C  
ANISOU 2498  CG  LEU A1118     8023   4829   6563    472   2124   -441       C  
ATOM   2499  CD1 LEU A1118      11.328 -18.119  40.527  1.00 51.08           C  
ANISOU 2499  CD1 LEU A1118     7964   4576   6868    775   2277   -246       C  
ATOM   2500  CD2 LEU A1118      10.065 -16.282  39.417  1.00 52.88           C  
ANISOU 2500  CD2 LEU A1118     8154   5491   6447    455   1974   -462       C  
ATOM   2501  N   ARG A1119       7.086 -20.852  38.216  1.00 50.36           N  
ANISOU 2501  N   ARG A1119     8457   4030   6646   -409   2457  -1490       N  
ATOM   2502  CA  ARG A1119       6.599 -21.853  37.268  1.00 50.78           C  
ANISOU 2502  CA  ARG A1119     8710   3853   6733   -686   2618  -1944       C  
ATOM   2503  C   ARG A1119       5.150 -21.607  36.840  1.00 55.89           C  
ANISOU 2503  C   ARG A1119     9351   4790   7096  -1094   2401  -2099       C  
ATOM   2504  O   ARG A1119       4.825 -21.805  35.668  1.00 55.98           O  
ANISOU 2504  O   ARG A1119     9478   4914   6879  -1355   2430  -2501       O  
ATOM   2505  CB  ARG A1119       6.799 -23.282  37.797  1.00 51.95           C  
ANISOU 2505  CB  ARG A1119     8988   3368   7381   -633   2865  -1959       C  
ATOM   2506  CG  ARG A1119       7.912 -24.020  37.055  1.00 66.13           C  
ANISOU 2506  CG  ARG A1119    10927   4817   9384   -459   3209  -2261       C  
ATOM   2507  CD  ARG A1119       7.845 -25.521  37.245  1.00 79.70           C  
ANISOU 2507  CD  ARG A1119    12822   5872  11590   -512   3471  -2413       C  
ATOM   2508  NE  ARG A1119       8.975 -26.039  38.019  1.00 91.07           N  
ANISOU 2508  NE  ARG A1119    14202   6895  13505   -103   3673  -2102       N  
ATOM   2509  CZ  ARG A1119       8.982 -26.180  39.342  1.00106.17           C  
ANISOU 2509  CZ  ARG A1119    15989   8664  15687     53   3571  -1587       C  
ATOM   2510  NH1 ARG A1119       7.918 -25.838  40.060  1.00 91.93           N  
ANISOU 2510  NH1 ARG A1119    14117   7089  13723   -157   3302  -1350       N  
ATOM   2511  NH2 ARG A1119      10.050 -26.669  39.957  1.00 94.77           N  
ANISOU 2511  NH2 ARG A1119    14473   6867  14669    419   3743  -1290       N  
ATOM   2512  N   MET A1120       4.292 -21.150  37.775  1.00 52.88           N  
ANISOU 2512  N   MET A1120     8820   4562   6711  -1153   2185  -1776       N  
ATOM   2513  CA  MET A1120       2.884 -20.849  37.493  1.00 52.94           C  
ANISOU 2513  CA  MET A1120     8753   4870   6494  -1508   1966  -1842       C  
ATOM   2514  C   MET A1120       2.728 -19.580  36.656  1.00 56.37           C  
ANISOU 2514  C   MET A1120     9064   5860   6494  -1552   1761  -1870       C  
ATOM   2515  O   MET A1120       1.796 -19.492  35.852  1.00 55.80           O  
ANISOU 2515  O   MET A1120     8971   6047   6184  -1879   1620  -2061       O  
ATOM   2516  CB  MET A1120       2.044 -20.807  38.777  1.00 55.50           C  
ANISOU 2516  CB  MET A1120     8938   5171   6978  -1530   1852  -1483       C  
ATOM   2517  CG  MET A1120       1.876 -22.181  39.413  1.00 59.53           C  
ANISOU 2517  CG  MET A1120     9570   5156   7892  -1614   2028  -1472       C  
ATOM   2518  SD  MET A1120       0.829 -22.227  40.886  1.00 64.16           S  
ANISOU 2518  SD  MET A1120     9997   5752   8631  -1698   1923  -1057       S  
ATOM   2519  CE  MET A1120       1.862 -21.335  42.059  1.00 60.71           C  
ANISOU 2519  CE  MET A1120     9451   5427   8188  -1244   1902   -610       C  
ATOM   2520  N   LEU A1121       3.666 -18.619  36.813  1.00 52.80           N  
ANISOU 2520  N   LEU A1121     8525   5587   5949  -1236   1739  -1664       N  
ATOM   2521  CA  LEU A1121       3.703 -17.377  36.035  1.00 52.49           C  
ANISOU 2521  CA  LEU A1121     8371   6030   5542  -1234   1569  -1641       C  
ATOM   2522  C   LEU A1121       4.104 -17.690  34.589  1.00 56.48           C  
ANISOU 2522  C   LEU A1121     9024   6624   5812  -1381   1679  -2032       C  
ATOM   2523  O   LEU A1121       3.571 -17.075  33.665  1.00 56.26           O  
ANISOU 2523  O   LEU A1121     8937   7009   5431  -1581   1511  -2111       O  
ATOM   2524  CB  LEU A1121       4.677 -16.353  36.649  1.00 52.38           C  
ANISOU 2524  CB  LEU A1121     8241   6117   5545   -875   1541  -1324       C  
ATOM   2525  CG  LEU A1121       4.246 -15.645  37.935  1.00 56.32           C  
ANISOU 2525  CG  LEU A1121     8580   6677   6143   -751   1393   -955       C  
ATOM   2526  CD1 LEU A1121       5.418 -14.946  38.578  1.00 56.18           C  
ANISOU 2526  CD1 LEU A1121     8508   6644   6194   -421   1417   -713       C  
ATOM   2527  CD2 LEU A1121       3.123 -14.652  37.684  1.00 58.15           C  
ANISOU 2527  CD2 LEU A1121     8642   7298   6152   -902   1155   -862       C  
ATOM   2528  N   GLN A1122       5.017 -18.672  34.402  1.00 53.23           N  
ANISOU 2528  N   GLN A1122     8800   5829   5598  -1283   1972  -2269       N  
ATOM   2529  CA  GLN A1122       5.482 -19.147  33.095  1.00 53.31           C  
ANISOU 2529  CA  GLN A1122     8988   5853   5413  -1409   2161  -2705       C  
ATOM   2530  C   GLN A1122       4.368 -19.966  32.404  1.00 57.76           C  
ANISOU 2530  C   GLN A1122     9690   6402   5853  -1864   2125  -3084       C  
ATOM   2531  O   GLN A1122       4.314 -20.010  31.173  1.00 57.54           O  
ANISOU 2531  O   GLN A1122     9769   6621   5472  -2101   2146  -3431       O  
ATOM   2532  CB  GLN A1122       6.759 -19.994  33.258  1.00 54.60           C  
ANISOU 2532  CB  GLN A1122     9283   5549   5913  -1126   2521  -2822       C  
ATOM   2533  CG  GLN A1122       7.565 -20.175  31.967  1.00 66.32           C  
ANISOU 2533  CG  GLN A1122    10904   7120   7174  -1130   2762  -3205       C  
ATOM   2534  CD  GLN A1122       8.711 -21.157  32.088  1.00 84.26           C  
ANISOU 2534  CD  GLN A1122    13295   8880   9839   -854   3159  -3356       C  
ATOM   2535  OE1 GLN A1122       9.240 -21.425  33.173  1.00 80.09           O  
ANISOU 2535  OE1 GLN A1122    12680   8022   9728   -548   3224  -3041       O  
ATOM   2536  NE2 GLN A1122       9.135 -21.710  30.959  1.00 76.28           N  
ANISOU 2536  NE2 GLN A1122    12477   7808   8699   -955   3443  -3838       N  
ATOM   2537  N   GLN A1123       3.485 -20.606  33.205  1.00 54.18           N  
ANISOU 2537  N   GLN A1123     9230   5682   5674  -2008   2067  -3010       N  
ATOM   2538  CA  GLN A1123       2.349 -21.405  32.728  1.00 53.81           C  
ANISOU 2538  CA  GLN A1123     9281   5589   5573  -2468   2005  -3321       C  
ATOM   2539  C   GLN A1123       1.111 -20.532  32.442  1.00 57.83           C  
ANISOU 2539  C   GLN A1123     9576   6653   5745  -2746   1633  -3166       C  
ATOM   2540  O   GLN A1123       0.106 -21.044  31.939  1.00 57.47           O  
ANISOU 2540  O   GLN A1123     9559   6680   5596  -3168   1520  -3393       O  
ATOM   2541  CB  GLN A1123       2.002 -22.507  33.744  1.00 54.99           C  
ANISOU 2541  CB  GLN A1123     9499   5183   6214  -2494   2127  -3265       C  
ATOM   2542  CG  GLN A1123       2.920 -23.725  33.675  1.00 68.98           C  
ANISOU 2542  CG  GLN A1123    11524   6346   8341  -2367   2508  -3550       C  
ATOM   2543  CD  GLN A1123       2.602 -24.782  34.709  1.00 90.87           C  
ANISOU 2543  CD  GLN A1123    14347   8551  11627  -2381   2622  -3421       C  
ATOM   2544  OE1 GLN A1123       1.890 -24.553  35.697  1.00 86.89           O  
ANISOU 2544  OE1 GLN A1123    13674   8104  11235  -2399   2442  -3042       O  
ATOM   2545  NE2 GLN A1123       3.136 -25.976  34.506  1.00 84.85           N  
ANISOU 2545  NE2 GLN A1123    13818   7215  11205  -2365   2946  -3726       N  
ATOM   2546  N   LYS A1124       1.198 -19.215  32.765  1.00 54.28           N  
ANISOU 2546  N   LYS A1124     8899   6577   5150  -2509   1445  -2774       N  
ATOM   2547  CA  LYS A1124       0.169 -18.174  32.614  1.00 54.00           C  
ANISOU 2547  CA  LYS A1124     8605   7054   4858  -2652   1109  -2525       C  
ATOM   2548  C   LYS A1124      -1.012 -18.366  33.595  1.00 57.79           C  
ANISOU 2548  C   LYS A1124     8921   7454   5583  -2773    978  -2300       C  
ATOM   2549  O   LYS A1124      -2.113 -17.855  33.363  1.00 57.76           O  
ANISOU 2549  O   LYS A1124     8709   7821   5417  -2998    722  -2182       O  
ATOM   2550  CB  LYS A1124      -0.294 -18.004  31.150  1.00 56.59           C  
ANISOU 2550  CB  LYS A1124     8948   7833   4719  -3017    951  -2788       C  
ATOM   2551  CG  LYS A1124       0.804 -17.478  30.230  1.00 70.88           C  
ANISOU 2551  CG  LYS A1124    10849   9860   6222  -2870   1046  -2893       C  
ATOM   2552  CD  LYS A1124       0.286 -17.141  28.836  1.00 81.58           C  
ANISOU 2552  CD  LYS A1124    12180  11764   7053  -3234    841  -3056       C  
ATOM   2553  CE  LYS A1124       1.382 -16.683  27.897  1.00 93.39           C  
ANISOU 2553  CE  LYS A1124    13769  13498   8216  -3110    960  -3152       C  
ATOM   2554  NZ  LYS A1124       1.933 -15.350  28.271  1.00102.96           N  
ANISOU 2554  NZ  LYS A1124    14769  14903   9449  -2742    865  -2679       N  
ATOM   2555  N   ARG A1125      -0.751 -19.060  34.718  1.00 53.61           N  
ANISOU 2555  N   ARG A1125     8461   6459   5449  -2604   1160  -2199       N  
ATOM   2556  CA  ARG A1125      -1.708 -19.305  35.799  1.00 52.98           C  
ANISOU 2556  CA  ARG A1125     8241   6264   5625  -2677   1099  -1957       C  
ATOM   2557  C   ARG A1125      -1.430 -18.226  36.853  1.00 56.90           C  
ANISOU 2557  C   ARG A1125     8556   6881   6181  -2299   1049  -1527       C  
ATOM   2558  O   ARG A1125      -0.733 -18.468  37.842  1.00 56.58           O  
ANISOU 2558  O   ARG A1125     8580   6532   6384  -2032   1204  -1364       O  
ATOM   2559  CB  ARG A1125      -1.524 -20.726  36.363  1.00 51.65           C  
ANISOU 2559  CB  ARG A1125     8273   5516   5835  -2733   1338  -2087       C  
ATOM   2560  CG  ARG A1125      -1.933 -21.837  35.396  1.00 55.80           C  
ANISOU 2560  CG  ARG A1125     8989   5870   6341  -3157   1396  -2549       C  
ATOM   2561  CD  ARG A1125      -1.389 -23.191  35.809  1.00 56.51           C  
ANISOU 2561  CD  ARG A1125     9326   5303   6843  -3126   1694  -2709       C  
ATOM   2562  NE  ARG A1125      -1.936 -23.642  37.089  1.00 61.38           N  
ANISOU 2562  NE  ARG A1125     9852   5651   7818  -3116   1717  -2384       N  
ATOM   2563  CZ  ARG A1125      -1.428 -24.634  37.812  1.00 74.69           C  
ANISOU 2563  CZ  ARG A1125    11687   6772   9921  -2989   1956  -2324       C  
ATOM   2564  NH1 ARG A1125      -0.361 -25.297  37.385  1.00 60.73           N  
ANISOU 2564  NH1 ARG A1125    10153   4612   8308  -2838   2206  -2581       N  
ATOM   2565  NH2 ARG A1125      -1.983 -24.972  38.967  1.00 63.14           N  
ANISOU 2565  NH2 ARG A1125    10123   5135   8732  -3004   1958  -1985       N  
ATOM   2566  N   TRP A1126      -1.932 -17.011  36.591  1.00 53.65           N  
ANISOU 2566  N   TRP A1126     7921   6924   5539  -2280    830  -1349       N  
ATOM   2567  CA  TRP A1126      -1.687 -15.822  37.403  1.00 53.83           C  
ANISOU 2567  CA  TRP A1126     7781   7094   5579  -1948    775  -1001       C  
ATOM   2568  C   TRP A1126      -2.459 -15.763  38.722  1.00 56.16           C  
ANISOU 2568  C   TRP A1126     7923   7326   6088  -1900    777   -730       C  
ATOM   2569  O   TRP A1126      -1.904 -15.258  39.700  1.00 55.43           O  
ANISOU 2569  O   TRP A1126     7816   7158   6085  -1605    843   -513       O  
ATOM   2570  CB  TRP A1126      -1.914 -14.552  36.579  1.00 53.15           C  
ANISOU 2570  CB  TRP A1126     7518   7466   5210  -1938    564   -911       C  
ATOM   2571  CG  TRP A1126      -1.022 -14.471  35.373  1.00 54.60           C  
ANISOU 2571  CG  TRP A1126     7847   7756   5145  -1949    583  -1126       C  
ATOM   2572  CD1 TRP A1126       0.340 -14.384  35.360  1.00 57.62           C  
ANISOU 2572  CD1 TRP A1126     8379   7979   5536  -1690    742  -1165       C  
ATOM   2573  CD2 TRP A1126      -1.436 -14.498  34.003  1.00 54.71           C  
ANISOU 2573  CD2 TRP A1126     7857   8086   4845  -2252    447  -1326       C  
ATOM   2574  NE1 TRP A1126       0.802 -14.351  34.067  1.00 57.45           N  
ANISOU 2574  NE1 TRP A1126     8450   8147   5230  -1799    743  -1385       N  
ATOM   2575  CE2 TRP A1126      -0.268 -14.406  33.210  1.00 59.02           C  
ANISOU 2575  CE2 TRP A1126     8570   8651   5202  -2151    558  -1491       C  
ATOM   2576  CE3 TRP A1126      -2.683 -14.565  33.364  1.00 56.23           C  
ANISOU 2576  CE3 TRP A1126     7902   8584   4879  -2613    231  -1364       C  
ATOM   2577  CZ2 TRP A1126      -0.312 -14.374  31.814  1.00 58.64           C  
ANISOU 2577  CZ2 TRP A1126     8572   8929   4779  -2401    475  -1705       C  
ATOM   2578  CZ3 TRP A1126      -2.725 -14.559  31.979  1.00 58.34           C  
ANISOU 2578  CZ3 TRP A1126     8216   9178   4774  -2877    117  -1570       C  
ATOM   2579  CH2 TRP A1126      -1.550 -14.476  31.217  1.00 59.14           C  
ANISOU 2579  CH2 TRP A1126     8512   9299   4658  -2774    246  -1748       C  
ATOM   2580  N   ASP A1127      -3.713 -16.267  38.764  1.00 51.79           N  
ANISOU 2580  N   ASP A1127     7253   6824   5602  -2202    711   -743       N  
ATOM   2581  CA  ASP A1127      -4.524 -16.297  39.991  1.00 51.27           C  
ANISOU 2581  CA  ASP A1127     7029   6718   5733  -2189    746   -492       C  
ATOM   2582  C   ASP A1127      -3.901 -17.248  41.020  1.00 52.52           C  
ANISOU 2582  C   ASP A1127     7378   6442   6136  -2085    964   -443       C  
ATOM   2583  O   ASP A1127      -3.914 -16.953  42.214  1.00 51.90           O  
ANISOU 2583  O   ASP A1127     7232   6335   6151  -1900   1033   -185       O  
ATOM   2584  CB  ASP A1127      -5.978 -16.725  39.695  1.00 53.85           C  
ANISOU 2584  CB  ASP A1127     7164   7206   6088  -2573    628   -519       C  
ATOM   2585  CG  ASP A1127      -6.901 -15.635  39.167  1.00 68.90           C  
ANISOU 2585  CG  ASP A1127     8758   9588   7834  -2624    402   -387       C  
ATOM   2586  OD1 ASP A1127      -6.803 -14.479  39.653  1.00 70.09           O  
ANISOU 2586  OD1 ASP A1127     8757   9895   7979  -2330    390   -150       O  
ATOM   2587  OD2 ASP A1127      -7.744 -15.943  38.292  1.00 74.98           O  
ANISOU 2587  OD2 ASP A1127     9424  10566   8499  -2968    236   -512       O  
ATOM   2588  N   GLU A1128      -3.346 -18.376  40.544  1.00 47.76           N  
ANISOU 2588  N   GLU A1128     7013   5503   5631  -2200   1080   -687       N  
ATOM   2589  CA  GLU A1128      -2.699 -19.408  41.356  1.00 47.05           C  
ANISOU 2589  CA  GLU A1128     7107   4951   5818  -2106   1288   -632       C  
ATOM   2590  C   GLU A1128      -1.327 -18.951  41.857  1.00 48.56           C  
ANISOU 2590  C   GLU A1128     7384   5057   6010  -1703   1370   -487       C  
ATOM   2591  O   GLU A1128      -0.969 -19.254  42.997  1.00 48.10           O  
ANISOU 2591  O   GLU A1128     7350   4805   6121  -1543   1470   -239       O  
ATOM   2592  CB  GLU A1128      -2.591 -20.731  40.583  1.00 48.64           C  
ANISOU 2592  CB  GLU A1128     7527   4791   6164  -2357   1401   -968       C  
ATOM   2593  CG  GLU A1128      -3.932 -21.322  40.171  1.00 62.41           C  
ANISOU 2593  CG  GLU A1128     9199   6572   7944  -2808   1320  -1112       C  
ATOM   2594  CD  GLU A1128      -4.401 -20.934  38.780  1.00 88.68           C  
ANISOU 2594  CD  GLU A1128    12470  10261  10965  -3073   1131  -1397       C  
ATOM   2595  OE1 GLU A1128      -4.782 -19.757  38.580  1.00 80.42           O  
ANISOU 2595  OE1 GLU A1128    11197   9676   9684  -3010    940  -1245       O  
ATOM   2596  OE2 GLU A1128      -4.390 -21.813  37.889  1.00 86.63           O  
ANISOU 2596  OE2 GLU A1128    12394   9821  10700  -3353   1176  -1770       O  
ATOM   2597  N   ALA A1129      -0.568 -18.210  41.013  1.00 43.11           N  
ANISOU 2597  N   ALA A1129     6723   4539   5117  -1561   1316   -619       N  
ATOM   2598  CA  ALA A1129       0.746 -17.657  41.358  1.00 41.94           C  
ANISOU 2598  CA  ALA A1129     6620   4363   4951  -1206   1366   -491       C  
ATOM   2599  C   ALA A1129       0.615 -16.605  42.478  1.00 44.27           C  
ANISOU 2599  C   ALA A1129     6759   4878   5185  -1015   1282   -170       C  
ATOM   2600  O   ALA A1129       1.465 -16.544  43.368  1.00 43.39           O  
ANISOU 2600  O   ALA A1129     6686   4651   5149   -780   1343     20       O  
ATOM   2601  CB  ALA A1129       1.388 -17.040  40.130  1.00 42.51           C  
ANISOU 2601  CB  ALA A1129     6723   4628   4800  -1156   1318   -694       C  
ATOM   2602  N   ALA A1130      -0.483 -15.817  42.443  1.00 39.92           N  
ANISOU 2602  N   ALA A1130     6024   4640   4504  -1128   1147   -117       N  
ATOM   2603  CA  ALA A1130      -0.851 -14.781  43.411  1.00 38.98           C  
ANISOU 2603  CA  ALA A1130     5748   4736   4328   -983   1093    125       C  
ATOM   2604  C   ALA A1130      -1.011 -15.347  44.837  1.00 42.34           C  
ANISOU 2604  C   ALA A1130     6193   4995   4898   -949   1211    340       C  
ATOM   2605  O   ALA A1130      -0.639 -14.678  45.802  1.00 42.15           O  
ANISOU 2605  O   ALA A1130     6144   5055   4818   -755   1222    520       O  
ATOM   2606  CB  ALA A1130      -2.142 -14.109  42.970  1.00 39.44           C  
ANISOU 2606  CB  ALA A1130     5587   5104   4295  -1141    963    122       C  
ATOM   2607  N   VAL A1131      -1.546 -16.580  44.955  1.00 37.85           N  
ANISOU 2607  N   VAL A1131     5679   4195   4505  -1159   1300    320       N  
ATOM   2608  CA  VAL A1131      -1.765 -17.291  46.221  1.00 37.24           C  
ANISOU 2608  CA  VAL A1131     5624   3949   4577  -1175   1421    554       C  
ATOM   2609  C   VAL A1131      -0.423 -17.573  46.916  1.00 40.92           C  
ANISOU 2609  C   VAL A1131     6237   4203   5106   -930   1496    712       C  
ATOM   2610  O   VAL A1131      -0.262 -17.222  48.084  1.00 40.97           O  
ANISOU 2610  O   VAL A1131     6214   4307   5047   -803   1515    957       O  
ATOM   2611  CB  VAL A1131      -2.597 -18.597  46.026  1.00 40.74           C  
ANISOU 2611  CB  VAL A1131     6094   4154   5234  -1487   1495    494       C  
ATOM   2612  CG1 VAL A1131      -2.825 -19.321  47.351  1.00 40.40           C  
ANISOU 2612  CG1 VAL A1131     6051   3963   5338  -1513   1621    794       C  
ATOM   2613  CG2 VAL A1131      -3.927 -18.315  45.334  1.00 40.44           C  
ANISOU 2613  CG2 VAL A1131     5875   4364   5127  -1756   1386    353       C  
ATOM   2614  N   ASN A1132       0.525 -18.204  46.195  1.00 36.80           N  
ANISOU 2614  N   ASN A1132     5863   3413   4708   -871   1543    571       N  
ATOM   2615  CA  ASN A1132       1.846 -18.572  46.707  1.00 36.41           C  
ANISOU 2615  CA  ASN A1132     5917   3144   4775   -632   1613    734       C  
ATOM   2616  C   ASN A1132       2.725 -17.384  47.068  1.00 39.46           C  
ANISOU 2616  C   ASN A1132     6252   3783   4960   -381   1516    841       C  
ATOM   2617  O   ASN A1132       3.462 -17.460  48.051  1.00 39.03           O  
ANISOU 2617  O   ASN A1132     6211   3686   4932   -222   1527   1101       O  
ATOM   2618  CB  ASN A1132       2.570 -19.500  45.731  1.00 36.18           C  
ANISOU 2618  CB  ASN A1132     6030   2762   4953   -623   1722    520       C  
ATOM   2619  CG  ASN A1132       2.084 -20.916  45.783  1.00 55.21           C  
ANISOU 2619  CG  ASN A1132     8537   4784   7658   -827   1858    485       C  
ATOM   2620  OD1 ASN A1132       0.899 -21.197  45.620  1.00 47.94           O  
ANISOU 2620  OD1 ASN A1132     7580   3906   6730  -1110   1837    378       O  
ATOM   2621  ND2 ASN A1132       2.993 -21.841  46.018  1.00 49.61           N  
ANISOU 2621  ND2 ASN A1132     7935   3672   7243   -692   2002    592       N  
ATOM   2622  N   LEU A1133       2.653 -16.299  46.274  1.00 35.16           N  
ANISOU 2622  N   LEU A1133     5640   3500   4217   -363   1410    659       N  
ATOM   2623  CA  LEU A1133       3.439 -15.081  46.491  1.00 34.31           C  
ANISOU 2623  CA  LEU A1133     5481   3618   3935   -160   1313    729       C  
ATOM   2624  C   LEU A1133       2.988 -14.292  47.730  1.00 37.37           C  
ANISOU 2624  C   LEU A1133     5789   4226   4181   -128   1265    921       C  
ATOM   2625  O   LEU A1133       3.821 -13.656  48.376  1.00 36.73           O  
ANISOU 2625  O   LEU A1133     5710   4242   4004     31   1213   1044       O  
ATOM   2626  CB  LEU A1133       3.401 -14.184  45.246  1.00 34.05           C  
ANISOU 2626  CB  LEU A1133     5398   3782   3758   -175   1223    508       C  
ATOM   2627  CG  LEU A1133       4.221 -14.617  44.020  1.00 38.37           C  
ANISOU 2627  CG  LEU A1133     6030   4201   4349   -148   1273    309       C  
ATOM   2628  CD1 LEU A1133       3.653 -14.014  42.746  1.00 38.36           C  
ANISOU 2628  CD1 LEU A1133     5977   4422   4177   -281   1187     94       C  
ATOM   2629  CD2 LEU A1133       5.681 -14.217  44.152  1.00 39.79           C  
ANISOU 2629  CD2 LEU A1133     6218   4371   4532     95   1273    410       C  
ATOM   2630  N   ALA A1134       1.678 -14.336  48.057  1.00 33.40           N  
ANISOU 2630  N   ALA A1134     5213   3813   3664   -291   1294    932       N  
ATOM   2631  CA  ALA A1134       1.090 -13.633  49.206  1.00 32.82           C  
ANISOU 2631  CA  ALA A1134     5062   3955   3454   -276   1303   1073       C  
ATOM   2632  C   ALA A1134       1.351 -14.329  50.550  1.00 36.90           C  
ANISOU 2632  C   ALA A1134     5647   4393   3981   -263   1383   1336       C  
ATOM   2633  O   ALA A1134       1.226 -13.694  51.602  1.00 36.47           O  
ANISOU 2633  O   ALA A1134     5570   4536   3750   -216   1391   1450       O  
ATOM   2634  CB  ALA A1134      -0.401 -13.442  48.996  1.00 33.34           C  
ANISOU 2634  CB  ALA A1134     4984   4159   3523   -445   1327   1003       C  
ATOM   2635  N   LYS A1135       1.696 -15.630  50.519  1.00 33.51           N  
ANISOU 2635  N   LYS A1135     5304   3674   3755   -311   1449   1433       N  
ATOM   2636  CA  LYS A1135       1.979 -16.409  51.723  1.00 33.31           C  
ANISOU 2636  CA  LYS A1135     5333   3553   3771   -302   1513   1746       C  
ATOM   2637  C   LYS A1135       3.495 -16.492  51.902  1.00 36.77           C  
ANISOU 2637  C   LYS A1135     5838   3894   4241    -98   1451   1881       C  
ATOM   2638  O   LYS A1135       4.090 -17.572  51.841  1.00 36.67           O  
ANISOU 2638  O   LYS A1135     5883   3576   4472    -58   1506   2009       O  
ATOM   2639  CB  LYS A1135       1.301 -17.792  51.663  1.00 35.98           C  
ANISOU 2639  CB  LYS A1135     5699   3606   4366   -487   1633   1823       C  
ATOM   2640  CG  LYS A1135      -0.209 -17.743  51.861  1.00 52.81           C  
ANISOU 2640  CG  LYS A1135     7724   5890   6452   -704   1696   1798       C  
ATOM   2641  CD  LYS A1135      -0.793 -19.145  52.034  1.00 64.61           C  
ANISOU 2641  CD  LYS A1135     9247   7093   8211   -910   1814   1934       C  
ATOM   2642  CE  LYS A1135      -2.240 -19.153  52.474  1.00 75.02           C  
ANISOU 2642  CE  LYS A1135    10427   8587   9491  -1135   1890   1980       C  
ATOM   2643  NZ  LYS A1135      -3.169 -18.792  51.370  1.00 85.84           N  
ANISOU 2643  NZ  LYS A1135    11681  10053  10883  -1280   1835   1674       N  
ATOM   2644  N   SER A1136       4.116 -15.315  52.108  1.00 32.53           N  
ANISOU 2644  N   SER A1136     5273   3605   3480     30   1339   1853       N  
ATOM   2645  CA  SER A1136       5.563 -15.146  52.247  1.00 31.66           C  
ANISOU 2645  CA  SER A1136     5180   3480   3368    210   1247   1974       C  
ATOM   2646  C   SER A1136       5.937 -14.083  53.292  1.00 34.75           C  
ANISOU 2646  C   SER A1136     5554   4194   3457    253   1136   2074       C  
ATOM   2647  O   SER A1136       5.142 -13.184  53.566  1.00 33.46           O  
ANISOU 2647  O   SER A1136     5370   4248   3094    184   1141   1936       O  
ATOM   2648  CB  SER A1136       6.158 -14.748  50.896  1.00 33.71           C  
ANISOU 2648  CB  SER A1136     5427   3666   3715    302   1214   1722       C  
ATOM   2649  OG  SER A1136       5.609 -13.524  50.429  1.00 36.70           O  
ANISOU 2649  OG  SER A1136     5758   4270   3914    267   1154   1493       O  
ATOM   2650  N   ARG A1137       7.183 -14.148  53.809  1.00 31.95           N  
ANISOU 2650  N   ARG A1137     5195   3863   3083    366   1037   2298       N  
ATOM   2651  CA  ARG A1137       7.751 -13.167  54.742  1.00 32.12           C  
ANISOU 2651  CA  ARG A1137     5208   4186   2809    380    900   2378       C  
ATOM   2652  C   ARG A1137       7.725 -11.773  54.104  1.00 35.68           C  
ANISOU 2652  C   ARG A1137     5639   4776   3141    400    840   2064       C  
ATOM   2653  O   ARG A1137       7.441 -10.798  54.796  1.00 35.93           O  
ANISOU 2653  O   ARG A1137     5692   5042   2916    342    801   1988       O  
ATOM   2654  CB  ARG A1137       9.187 -13.555  55.137  1.00 33.65           C  
ANISOU 2654  CB  ARG A1137     5358   4363   3065    496    776   2675       C  
ATOM   2655  CG  ARG A1137       9.263 -14.466  56.366  1.00 48.85           C  
ANISOU 2655  CG  ARG A1137     7294   6322   4946    453    767   3084       C  
ATOM   2656  CD  ARG A1137      10.614 -15.151  56.531  1.00 63.88           C  
ANISOU 2656  CD  ARG A1137     9108   8120   7044    600    666   3432       C  
ATOM   2657  NE  ARG A1137      11.736 -14.207  56.508  1.00 78.85           N  
ANISOU 2657  NE  ARG A1137    10925  10230   8804    664    478   3416       N  
ATOM   2658  CZ  ARG A1137      13.014 -14.549  56.640  1.00 96.08           C  
ANISOU 2658  CZ  ARG A1137    12979  12391  11135    796    359   3709       C  
ATOM   2659  NH1 ARG A1137      13.354 -15.821  56.822  1.00 83.89           N  
ANISOU 2659  NH1 ARG A1137    11376  10599   9900    908    418   4053       N  
ATOM   2660  NH2 ARG A1137      13.963 -13.623  56.595  1.00 83.59           N  
ANISOU 2660  NH2 ARG A1137    11311  11026   9425    817    182   3676       N  
ATOM   2661  N   TRP A1138       7.961 -11.706  52.772  1.00 31.89           N  
ANISOU 2661  N   TRP A1138     5125   4139   2852    471    851   1879       N  
ATOM   2662  CA  TRP A1138       7.923 -10.510  51.920  1.00 31.55           C  
ANISOU 2662  CA  TRP A1138     5049   4182   2757    494    802   1621       C  
ATOM   2663  C   TRP A1138       6.607  -9.746  52.070  1.00 35.46           C  
ANISOU 2663  C   TRP A1138     5543   4806   3123    401    857   1447       C  
ATOM   2664  O   TRP A1138       6.639  -8.534  52.283  1.00 35.59           O  
ANISOU 2664  O   TRP A1138     5551   4970   3001    409    800   1338       O  
ATOM   2665  CB  TRP A1138       8.149 -10.907  50.450  1.00 30.15           C  
ANISOU 2665  CB  TRP A1138     4844   3820   2790    550    845   1485       C  
ATOM   2666  CG  TRP A1138       7.865  -9.835  49.436  1.00 31.08           C  
ANISOU 2666  CG  TRP A1138     4921   4026   2862    545    810   1255       C  
ATOM   2667  CD1 TRP A1138       8.377  -8.570  49.410  1.00 34.05           C  
ANISOU 2667  CD1 TRP A1138     5261   4543   3136    586    705   1209       C  
ATOM   2668  CD2 TRP A1138       7.051  -9.963  48.262  1.00 30.82           C  
ANISOU 2668  CD2 TRP A1138     4871   3942   2896    484    868   1068       C  
ATOM   2669  NE1 TRP A1138       7.911  -7.892  48.305  1.00 33.52           N  
ANISOU 2669  NE1 TRP A1138     5149   4504   3083    573    702   1038       N  
ATOM   2670  CE2 TRP A1138       7.107  -8.728  47.575  1.00 34.99           C  
ANISOU 2670  CE2 TRP A1138     5341   4601   3351    508    790    954       C  
ATOM   2671  CE3 TRP A1138       6.292 -11.010  47.710  1.00 31.87           C  
ANISOU 2671  CE3 TRP A1138     5030   3936   3143    389    967    992       C  
ATOM   2672  CZ2 TRP A1138       6.414  -8.503  46.378  1.00 34.22           C  
ANISOU 2672  CZ2 TRP A1138     5199   4538   3264    448    794    803       C  
ATOM   2673  CZ3 TRP A1138       5.610 -10.789  46.525  1.00 33.24           C  
ANISOU 2673  CZ3 TRP A1138     5168   4153   3310    307    965    801       C  
ATOM   2674  CH2 TRP A1138       5.677  -9.549  45.869  1.00 33.96           C  
ANISOU 2674  CH2 TRP A1138     5188   4413   3301    342    873    725       C  
ATOM   2675  N   TYR A1139       5.461 -10.448  51.957  1.00 32.20           N  
ANISOU 2675  N   TYR A1139     5125   4324   2784    311    976   1425       N  
ATOM   2676  CA  TYR A1139       4.136  -9.848  52.125  1.00 32.54           C  
ANISOU 2676  CA  TYR A1139     5122   4494   2748    233   1052   1298       C  
ATOM   2677  C   TYR A1139       3.948  -9.337  53.554  1.00 36.41           C  
ANISOU 2677  C   TYR A1139     5651   5179   3005    204   1087   1366       C  
ATOM   2678  O   TYR A1139       3.354  -8.288  53.738  1.00 35.92           O  
ANISOU 2678  O   TYR A1139     5557   5244   2847    208   1124   1214       O  
ATOM   2679  CB  TYR A1139       3.012 -10.839  51.758  1.00 34.51           C  
ANISOU 2679  CB  TYR A1139     5332   4638   3140    114   1163   1295       C  
ATOM   2680  CG  TYR A1139       1.629 -10.217  51.762  1.00 37.57           C  
ANISOU 2680  CG  TYR A1139     5613   5168   3494     45   1237   1181       C  
ATOM   2681  CD1 TYR A1139       1.088  -9.662  50.606  1.00 39.72           C  
ANISOU 2681  CD1 TYR A1139     5781   5460   3852     42   1195   1016       C  
ATOM   2682  CD2 TYR A1139       0.864 -10.175  52.926  1.00 38.72           C  
ANISOU 2682  CD2 TYR A1139     5742   5450   3521    -15   1357   1260       C  
ATOM   2683  CE1 TYR A1139      -0.176  -9.069  50.612  1.00 40.92           C  
ANISOU 2683  CE1 TYR A1139     5789   5746   4013      2   1259    954       C  
ATOM   2684  CE2 TYR A1139      -0.378  -9.545  52.953  1.00 39.92           C  
ANISOU 2684  CE2 TYR A1139     5761   5735   3671    -47   1454   1162       C  
ATOM   2685  CZ  TYR A1139      -0.909  -9.023  51.787  1.00 48.09           C  
ANISOU 2685  CZ  TYR A1139     6667   6766   4839    -32   1400   1021       C  
ATOM   2686  OH  TYR A1139      -2.156  -8.448  51.815  1.00 52.06           O  
ANISOU 2686  OH  TYR A1139     6996   7398   5385    -48   1493    969       O  
ATOM   2687  N   ASN A1140       4.428 -10.076  54.558  1.00 33.68           N  
ANISOU 2687  N   ASN A1140     5372   4858   2567    172   1084   1597       N  
ATOM   2688  CA  ASN A1140       4.283  -9.675  55.958  1.00 33.82           C  
ANISOU 2688  CA  ASN A1140     5446   5107   2297    111   1117   1669       C  
ATOM   2689  C   ASN A1140       5.084  -8.413  56.316  1.00 38.52           C  
ANISOU 2689  C   ASN A1140     6086   5854   2696    150   1000   1546       C  
ATOM   2690  O   ASN A1140       4.643  -7.642  57.169  1.00 39.37           O  
ANISOU 2690  O   ASN A1140     6240   6149   2570     94   1068   1434       O  
ATOM   2691  CB  ASN A1140       4.640 -10.828  56.891  1.00 33.77           C  
ANISOU 2691  CB  ASN A1140     5488   5112   2231     53   1117   2002       C  
ATOM   2692  CG  ASN A1140       4.242 -10.590  58.323  1.00 51.75           C  
ANISOU 2692  CG  ASN A1140     7824   7669   4169    -56   1187   2092       C  
ATOM   2693  OD1 ASN A1140       3.069 -10.368  58.648  1.00 45.91           O  
ANISOU 2693  OD1 ASN A1140     7066   7034   3346   -126   1360   1982       O  
ATOM   2694  ND2 ASN A1140       5.216 -10.638  59.210  1.00 43.36           N  
ANISOU 2694  ND2 ASN A1140     6822   6760   2893    -78   1059   2302       N  
ATOM   2695  N   GLN A1141       6.247  -8.211  55.673  1.00 33.93           N  
ANISOU 2695  N   GLN A1141     5490   5186   2216    233    842   1553       N  
ATOM   2696  CA  GLN A1141       7.119  -7.060  55.908  1.00 33.67           C  
ANISOU 2696  CA  GLN A1141     5484   5266   2042    244    708   1451       C  
ATOM   2697  C   GLN A1141       6.578  -5.810  55.224  1.00 37.26           C  
ANISOU 2697  C   GLN A1141     5912   5684   2560    280    751   1158       C  
ATOM   2698  O   GLN A1141       6.479  -4.764  55.867  1.00 37.30           O  
ANISOU 2698  O   GLN A1141     5974   5802   2396    238    765    998       O  
ATOM   2699  CB  GLN A1141       8.555  -7.359  55.442  1.00 35.34           C  
ANISOU 2699  CB  GLN A1141     5649   5403   2374    317    537   1606       C  
ATOM   2700  CG  GLN A1141       9.295  -8.341  56.356  1.00 59.28           C  
ANISOU 2700  CG  GLN A1141     8689   8513   5322    292    454   1939       C  
ATOM   2701  CD  GLN A1141      10.615  -8.816  55.793  1.00 81.42           C  
ANISOU 2701  CD  GLN A1141    11398  11210   8328    402    327   2122       C  
ATOM   2702  OE1 GLN A1141      11.399  -8.049  55.214  1.00 77.16           O  
ANISOU 2702  OE1 GLN A1141    10806  10692   7820    438    216   2031       O  
ATOM   2703  NE2 GLN A1141      10.899 -10.099  55.972  1.00 74.15           N  
ANISOU 2703  NE2 GLN A1141    10441  10160   7571    462    357   2398       N  
ATOM   2704  N   THR A1142       6.227  -5.916  53.919  1.00 32.77           N  
ANISOU 2704  N   THR A1142     5258   4957   2235    351    774   1091       N  
ATOM   2705  CA  THR A1142       5.695  -4.808  53.117  1.00 31.45           C  
ANISOU 2705  CA  THR A1142     5031   4748   2170    398    798    885       C  
ATOM   2706  C   THR A1142       4.338  -5.193  52.471  1.00 33.34           C  
ANISOU 2706  C   THR A1142     5179   4940   2550    395    924    842       C  
ATOM   2707  O   THR A1142       4.292  -5.384  51.255  1.00 32.62           O  
ANISOU 2707  O   THR A1142     5016   4760   2617    421    883    833       O  
ATOM   2708  CB  THR A1142       6.762  -4.326  52.104  1.00 35.96           C  
ANISOU 2708  CB  THR A1142     5564   5241   2859    462    656    874       C  
ATOM   2709  OG1 THR A1142       7.150  -5.416  51.259  1.00 33.65           O  
ANISOU 2709  OG1 THR A1142     5234   4853   2697    493    635    988       O  
ATOM   2710  CG2 THR A1142       7.988  -3.708  52.782  1.00 31.32           C  
ANISOU 2710  CG2 THR A1142     5032   4723   2143    436    524    895       C  
ATOM   2711  N   PRO A1143       3.221  -5.296  53.243  1.00 29.69           N  
ANISOU 2711  N   PRO A1143     4704   4562   2017    346   1077    816       N  
ATOM   2712  CA  PRO A1143       1.947  -5.737  52.629  1.00 29.62           C  
ANISOU 2712  CA  PRO A1143     4569   4529   2156    318   1177    808       C  
ATOM   2713  C   PRO A1143       1.382  -4.855  51.514  1.00 34.42           C  
ANISOU 2713  C   PRO A1143     5039   5107   2932    383   1151    697       C  
ATOM   2714  O   PRO A1143       0.840  -5.403  50.556  1.00 34.15           O  
ANISOU 2714  O   PRO A1143     4905   5043   3026    341   1129    724       O  
ATOM   2715  CB  PRO A1143       0.976  -5.847  53.813  1.00 31.19           C  
ANISOU 2715  CB  PRO A1143     4765   4856   2231    260   1362    815       C  
ATOM   2716  CG  PRO A1143       1.617  -5.123  54.937  1.00 35.22           C  
ANISOU 2716  CG  PRO A1143     5402   5465   2514    274   1370    745       C  
ATOM   2717  CD  PRO A1143       3.090  -5.146  54.712  1.00 30.90           C  
ANISOU 2717  CD  PRO A1143     4947   4862   1931    291   1170    809       C  
ATOM   2718  N   ASN A1144       1.513  -3.519  51.615  1.00 31.05           N  
ANISOU 2718  N   ASN A1144     4605   4684   2510    471   1147    584       N  
ATOM   2719  CA  ASN A1144       0.993  -2.600  50.597  1.00 30.57           C  
ANISOU 2719  CA  ASN A1144     4395   4585   2633    549   1116    536       C  
ATOM   2720  C   ASN A1144       1.759  -2.683  49.287  1.00 34.42           C  
ANISOU 2720  C   ASN A1144     4868   5018   3192    555    942    590       C  
ATOM   2721  O   ASN A1144       1.136  -2.739  48.228  1.00 34.53           O  
ANISOU 2721  O   ASN A1144     4744   5055   3320    547    899    625       O  
ATOM   2722  CB  ASN A1144       0.920  -1.163  51.112  1.00 30.93           C  
ANISOU 2722  CB  ASN A1144     4446   4594   2712    646   1188    407       C  
ATOM   2723  CG  ASN A1144       0.046  -0.992  52.326  1.00 52.66           C  
ANISOU 2723  CG  ASN A1144     7187   7415   5407    654   1411    315       C  
ATOM   2724  OD1 ASN A1144       0.525  -0.669  53.412  1.00 50.77           O  
ANISOU 2724  OD1 ASN A1144     7093   7193   5006    644   1489    192       O  
ATOM   2725  ND2 ASN A1144      -1.254  -1.206  52.176  1.00 43.77           N  
ANISOU 2725  ND2 ASN A1144     5882   6352   4396    657   1526    366       N  
ATOM   2726  N   ARG A1145       3.102  -2.716  49.353  1.00 30.40           N  
ANISOU 2726  N   ARG A1145     4483   4465   2600    557    845    608       N  
ATOM   2727  CA  ARG A1145       3.956  -2.842  48.170  1.00 29.77           C  
ANISOU 2727  CA  ARG A1145     4393   4350   2568    566    716    657       C  
ATOM   2728  C   ARG A1145       3.768  -4.225  47.518  1.00 33.59           C  
ANISOU 2728  C   ARG A1145     4870   4831   3063    491    724    696       C  
ATOM   2729  O   ARG A1145       3.636  -4.300  46.293  1.00 33.45           O  
ANISOU 2729  O   ARG A1145     4782   4833   3093    468    669    691       O  
ATOM   2730  CB  ARG A1145       5.429  -2.594  48.528  1.00 29.07           C  
ANISOU 2730  CB  ARG A1145     4406   4229   2409    587    631    681       C  
ATOM   2731  CG  ARG A1145       6.361  -2.666  47.330  1.00 36.53           C  
ANISOU 2731  CG  ARG A1145     5321   5154   3406    606    534    735       C  
ATOM   2732  CD  ARG A1145       7.812  -2.557  47.719  1.00 40.36           C  
ANISOU 2732  CD  ARG A1145     5863   5626   3846    621    455    791       C  
ATOM   2733  NE  ARG A1145       8.671  -2.619  46.539  1.00 43.13           N  
ANISOU 2733  NE  ARG A1145     6161   5973   4253    648    401    844       N  
ATOM   2734  CZ  ARG A1145       9.977  -2.377  46.549  1.00 54.64           C  
ANISOU 2734  CZ  ARG A1145     7610   7435   5716    667    328    915       C  
ATOM   2735  NH1 ARG A1145      10.593  -2.068  47.683  1.00 42.48           N  
ANISOU 2735  NH1 ARG A1145     6113   5909   4119    643    267    944       N  
ATOM   2736  NH2 ARG A1145      10.678  -2.449  45.425  1.00 40.34           N  
ANISOU 2736  NH2 ARG A1145     5737   5640   3952    693    318    961       N  
ATOM   2737  N   ALA A1146       3.724  -5.301  48.335  1.00 30.00           N  
ANISOU 2737  N   ALA A1146     4492   4347   2559    438    795    737       N  
ATOM   2738  CA  ALA A1146       3.534  -6.674  47.859  1.00 30.35           C  
ANISOU 2738  CA  ALA A1146     4553   4324   2654    355    828    759       C  
ATOM   2739  C   ALA A1146       2.188  -6.890  47.161  1.00 35.13           C  
ANISOU 2739  C   ALA A1146     5040   4982   3325    256    854    707       C  
ATOM   2740  O   ALA A1146       2.185  -7.428  46.058  1.00 34.39           O  
ANISOU 2740  O   ALA A1146     4934   4868   3265    187    813    656       O  
ATOM   2741  CB  ALA A1146       3.720  -7.671  48.990  1.00 31.11           C  
ANISOU 2741  CB  ALA A1146     4742   4360   2717    322    902    861       C  
ATOM   2742  N   LYS A1147       1.062  -6.425  47.756  1.00 33.13           N  
ANISOU 2742  N   LYS A1147     4686   4815   3084    243    923    713       N  
ATOM   2743  CA  LYS A1147      -0.262  -6.571  47.130  1.00 33.45           C  
ANISOU 2743  CA  LYS A1147     4561   4941   3208    144    931    700       C  
ATOM   2744  C   LYS A1147      -0.339  -5.862  45.759  1.00 37.60           C  
ANISOU 2744  C   LYS A1147     4973   5548   3765    155    798    679       C  
ATOM   2745  O   LYS A1147      -0.928  -6.427  44.834  1.00 38.44           O  
ANISOU 2745  O   LYS A1147     4998   5718   3888     18    742    661       O  
ATOM   2746  CB  LYS A1147      -1.433  -6.179  48.065  1.00 35.77           C  
ANISOU 2746  CB  LYS A1147     4731   5323   3535    154   1059    731       C  
ATOM   2747  CG  LYS A1147      -1.486  -4.721  48.533  1.00 54.12           C  
ANISOU 2747  CG  LYS A1147     7007   7686   5871    315   1097    701       C  
ATOM   2748  CD  LYS A1147      -2.410  -3.831  47.694  1.00 62.20           C  
ANISOU 2748  CD  LYS A1147     7793   8794   7047    364   1063    725       C  
ATOM   2749  CE  LYS A1147      -2.649  -2.483  48.335  1.00 66.90           C  
ANISOU 2749  CE  LYS A1147     8335   9369   7716    533   1168    686       C  
ATOM   2750  NZ  LYS A1147      -1.446  -1.614  48.295  1.00 71.38           N  
ANISOU 2750  NZ  LYS A1147     9040   9829   8253    632   1084    636       N  
ATOM   2751  N   ARG A1148       0.299  -4.672  45.618  1.00 32.58           N  
ANISOU 2751  N   ARG A1148     4339   4915   3125    293    740    690       N  
ATOM   2752  CA  ARG A1148       0.349  -3.916  44.356  1.00 31.69           C  
ANISOU 2752  CA  ARG A1148     4122   4884   3033    312    611    725       C  
ATOM   2753  C   ARG A1148       1.124  -4.683  43.284  1.00 34.97           C  
ANISOU 2753  C   ARG A1148     4628   5307   3352    220    537    680       C  
ATOM   2754  O   ARG A1148       0.685  -4.719  42.138  1.00 34.80           O  
ANISOU 2754  O   ARG A1148     4512   5417   3293    124    445    688       O  
ATOM   2755  CB  ARG A1148       0.964  -2.522  44.551  1.00 30.44           C  
ANISOU 2755  CB  ARG A1148     3966   4678   2921    468    584    760       C  
ATOM   2756  CG  ARG A1148       0.022  -1.504  45.169  1.00 33.41           C  
ANISOU 2756  CG  ARG A1148     4209   5049   3435    570    661    784       C  
ATOM   2757  CD  ARG A1148       0.554  -0.089  45.039  1.00 33.98           C  
ANISOU 2757  CD  ARG A1148     4268   5037   3605    700    620    819       C  
ATOM   2758  NE  ARG A1148       1.817   0.113  45.756  1.00 35.19           N  
ANISOU 2758  NE  ARG A1148     4617   5077   3677    728    631    739       N  
ATOM   2759  CZ  ARG A1148       1.916   0.596  46.993  1.00 49.26           C  
ANISOU 2759  CZ  ARG A1148     6489   6772   5456    779    736    637       C  
ATOM   2760  NH1 ARG A1148       0.826   0.930  47.673  1.00 38.85           N  
ANISOU 2760  NH1 ARG A1148     5091   5450   4221    832    881    584       N  
ATOM   2761  NH2 ARG A1148       3.106   0.751  47.557  1.00 33.92           N  
ANISOU 2761  NH2 ARG A1148     4707   4767   3415    765    702    581       N  
ATOM   2762  N   VAL A1149       2.267  -5.301  43.663  1.00 31.23           N  
ANISOU 2762  N   VAL A1149     4327   4705   2832    249    584    635       N  
ATOM   2763  CA  VAL A1149       3.107  -6.122  42.782  1.00 30.75           C  
ANISOU 2763  CA  VAL A1149     4365   4608   2709    194    576    566       C  
ATOM   2764  C   VAL A1149       2.313  -7.382  42.362  1.00 36.44           C  
ANISOU 2764  C   VAL A1149     5100   5316   3430     14    615    468       C  
ATOM   2765  O   VAL A1149       2.276  -7.705  41.174  1.00 36.20           O  
ANISOU 2765  O   VAL A1149     5072   5362   3320    -99    573    377       O  
ATOM   2766  CB  VAL A1149       4.480  -6.474  43.434  1.00 33.85           C  
ANISOU 2766  CB  VAL A1149     4896   4854   3113    299    632    583       C  
ATOM   2767  CG1 VAL A1149       5.268  -7.484  42.595  1.00 33.71           C  
ANISOU 2767  CG1 VAL A1149     4967   4758   3082    266    683    498       C  
ATOM   2768  CG2 VAL A1149       5.316  -5.222  43.684  1.00 33.39           C  
ANISOU 2768  CG2 VAL A1149     4816   4823   3045    424    568    659       C  
ATOM   2769  N   ILE A1150       1.660  -8.062  43.338  1.00 33.66           N  
ANISOU 2769  N   ILE A1150     4757   4880   3153    -37    696    485       N  
ATOM   2770  CA  ILE A1150       0.860  -9.274  43.121  1.00 33.88           C  
ANISOU 2770  CA  ILE A1150     4793   4857   3222   -233    741    406       C  
ATOM   2771  C   ILE A1150      -0.303  -9.011  42.153  1.00 38.49           C  
ANISOU 2771  C   ILE A1150     5209   5652   3765   -395    632    375       C  
ATOM   2772  O   ILE A1150      -0.469  -9.782  41.207  1.00 37.99           O  
ANISOU 2772  O   ILE A1150     5183   5602   3648   -580    603    241       O  
ATOM   2773  CB  ILE A1150       0.409  -9.937  44.469  1.00 37.03           C  
ANISOU 2773  CB  ILE A1150     5217   5139   3715   -252    856    488       C  
ATOM   2774  CG1 ILE A1150       1.608 -10.450  45.305  1.00 37.55           C  
ANISOU 2774  CG1 ILE A1150     5447   5013   3809   -129    937    553       C  
ATOM   2775  CG2 ILE A1150      -0.617 -11.059  44.274  1.00 37.13           C  
ANISOU 2775  CG2 ILE A1150     5199   5105   3804   -486    895    433       C  
ATOM   2776  CD1 ILE A1150       2.765 -10.992  44.511  1.00 44.76           C  
ANISOU 2776  CD1 ILE A1150     6482   5781   4743    -89    948    471       C  
ATOM   2777  N   THR A1151      -1.071  -7.915  42.366  1.00 35.51           N  
ANISOU 2777  N   THR A1151     4640   5438   3413   -327    573    497       N  
ATOM   2778  CA  THR A1151      -2.189  -7.517  41.500  1.00 35.53           C  
ANISOU 2778  CA  THR A1151     4423   5673   3403   -449    445    543       C  
ATOM   2779  C   THR A1151      -1.693  -7.325  40.057  1.00 40.44           C  
ANISOU 2779  C   THR A1151     5068   6433   3866   -517    311    492       C  
ATOM   2780  O   THR A1151      -2.359  -7.778  39.128  1.00 40.74           O  
ANISOU 2780  O   THR A1151     5030   6634   3815   -739    208    438       O  
ATOM   2781  CB  THR A1151      -2.905  -6.272  42.056  1.00 43.53           C  
ANISOU 2781  CB  THR A1151     5225   6783   4530   -293    443    707       C  
ATOM   2782  OG1 THR A1151      -3.258  -6.499  43.422  1.00 43.21           O  
ANISOU 2782  OG1 THR A1151     5200   6634   4585   -239    605    721       O  
ATOM   2783  CG2 THR A1151      -4.159  -5.908  41.263  1.00 42.18           C  
ANISOU 2783  CG2 THR A1151     4770   6859   4399   -404    309    816       C  
ATOM   2784  N   THR A1152      -0.509  -6.692  39.887  1.00 36.94           N  
ANISOU 2784  N   THR A1152     4729   5938   3368   -351    315    507       N  
ATOM   2785  CA  THR A1152       0.141  -6.458  38.592  1.00 36.94           C  
ANISOU 2785  CA  THR A1152     4766   6074   3196   -394    226    476       C  
ATOM   2786  C   THR A1152       0.420  -7.791  37.879  1.00 42.16           C  
ANISOU 2786  C   THR A1152     5591   6695   3733   -591    278    243       C  
ATOM   2787  O   THR A1152       0.157  -7.897  36.679  1.00 41.97           O  
ANISOU 2787  O   THR A1152     5539   6884   3523   -772    179    176       O  
ATOM   2788  CB  THR A1152       1.378  -5.557  38.760  1.00 39.63           C  
ANISOU 2788  CB  THR A1152     5173   6337   3547   -178    251    555       C  
ATOM   2789  OG1 THR A1152       0.997  -4.378  39.470  1.00 37.98           O  
ANISOU 2789  OG1 THR A1152     4829   6122   3479    -24    221    724       O  
ATOM   2790  CG2 THR A1152       2.015  -5.168  37.435  1.00 35.67           C  
ANISOU 2790  CG2 THR A1152     4681   6006   2865   -217    176    567       C  
ATOM   2791  N   PHE A1153       0.894  -8.814  38.628  1.00 39.26           N  
ANISOU 2791  N   PHE A1153     5392   6055   3470   -568    435    125       N  
ATOM   2792  CA  PHE A1153       1.144 -10.158  38.094  1.00 39.60           C  
ANISOU 2792  CA  PHE A1153     5606   5965   3474   -733    532   -115       C  
ATOM   2793  C   PHE A1153      -0.172 -10.846  37.721  1.00 46.02           C  
ANISOU 2793  C   PHE A1153     6352   6868   4266  -1029    464   -215       C  
ATOM   2794  O   PHE A1153      -0.207 -11.644  36.787  1.00 46.13           O  
ANISOU 2794  O   PHE A1153     6469   6900   4160  -1246    474   -443       O  
ATOM   2795  CB  PHE A1153       1.893 -11.033  39.115  1.00 40.95           C  
ANISOU 2795  CB  PHE A1153     5937   5792   3832   -609    711   -142       C  
ATOM   2796  CG  PHE A1153       3.399 -10.905  39.141  1.00 41.99           C  
ANISOU 2796  CG  PHE A1153     6176   5805   3974   -397    804   -137       C  
ATOM   2797  CD1 PHE A1153       4.157 -11.170  38.006  1.00 44.68           C  
ANISOU 2797  CD1 PHE A1153     6607   6176   4194   -430    862   -309       C  
ATOM   2798  CD2 PHE A1153       4.065 -10.594  40.319  1.00 43.52           C  
ANISOU 2798  CD2 PHE A1153     6375   5868   4292   -184    843     35       C  
ATOM   2799  CE1 PHE A1153       5.550 -11.081  38.040  1.00 45.46           C  
ANISOU 2799  CE1 PHE A1153     6767   6174   4332   -228    967   -285       C  
ATOM   2800  CE2 PHE A1153       5.458 -10.502  40.350  1.00 46.09           C  
ANISOU 2800  CE2 PHE A1153     6761   6105   4646     -5    911     65       C  
ATOM   2801  CZ  PHE A1153       6.192 -10.753  39.214  1.00 44.18           C  
ANISOU 2801  CZ  PHE A1153     6578   5886   4321    -18    979    -85       C  
ATOM   2802  N   ARG A1154      -1.245 -10.531  38.452  1.00 43.99           N  
ANISOU 2802  N   ARG A1154     5916   6674   4124  -1048    407    -55       N  
ATOM   2803  CA  ARG A1154      -2.569 -11.111  38.263  1.00 44.54           C  
ANISOU 2803  CA  ARG A1154     5863   6845   4217  -1328    334    -95       C  
ATOM   2804  C   ARG A1154      -3.338 -10.528  37.066  1.00 49.77           C  
ANISOU 2804  C   ARG A1154     6330   7889   4691  -1510    112    -57       C  
ATOM   2805  O   ARG A1154      -3.984 -11.287  36.347  1.00 49.05           O  
ANISOU 2805  O   ARG A1154     6228   7901   4507  -1826     34   -209       O  
ATOM   2806  CB  ARG A1154      -3.381 -10.970  39.563  1.00 44.29           C  
ANISOU 2806  CB  ARG A1154     5686   6751   4390  -1255    391     88       C  
ATOM   2807  CG  ARG A1154      -4.351 -12.115  39.819  1.00 57.30           C  
ANISOU 2807  CG  ARG A1154     7300   8324   6148  -1532    425     20       C  
ATOM   2808  CD  ARG A1154      -4.895 -12.115  41.243  1.00 72.72           C  
ANISOU 2808  CD  ARG A1154     9159  10179   8291  -1437    548    197       C  
ATOM   2809  NE  ARG A1154      -5.694 -10.924  41.548  1.00 87.62           N  
ANISOU 2809  NE  ARG A1154    10769  12314  10210  -1312    485    402       N  
ATOM   2810  CZ  ARG A1154      -6.999 -10.808  41.317  1.00106.66           C  
ANISOU 2810  CZ  ARG A1154    12897  14949  12678  -1477    395    495       C  
ATOM   2811  NH1 ARG A1154      -7.677 -11.813  40.774  1.00 95.23           N  
ANISOU 2811  NH1 ARG A1154    11415  13532  11236  -1815    330    393       N  
ATOM   2812  NH2 ARG A1154      -7.635  -9.685  41.623  1.00 96.00           N  
ANISOU 2812  NH2 ARG A1154    11288  13784  11402  -1308    373    689       N  
ATOM   2813  N   THR A1155      -3.274  -9.193  36.859  1.00 47.84           N  
ANISOU 2813  N   THR A1155     5926   7851   4398  -1329      2    158       N  
ATOM   2814  CA  THR A1155      -4.020  -8.488  35.806  1.00 48.34           C  
ANISOU 2814  CA  THR A1155     5759   8297   4310  -1461   -229    295       C  
ATOM   2815  C   THR A1155      -3.219  -8.172  34.534  1.00 54.14           C  
ANISOU 2815  C   THR A1155     6591   9224   4755  -1508   -314    238       C  
ATOM   2816  O   THR A1155      -3.804  -8.136  33.449  1.00 53.85           O  
ANISOU 2816  O   THR A1155     6446   9519   4497  -1755   -503    247       O  
ATOM   2817  CB  THR A1155      -4.667  -7.200  36.351  1.00 54.76           C  
ANISOU 2817  CB  THR A1155     6288   9213   5306  -1240   -294    618       C  
ATOM   2818  OG1 THR A1155      -3.651  -6.253  36.696  1.00 54.25           O  
ANISOU 2818  OG1 THR A1155     6313   9008   5293   -936   -213    705       O  
ATOM   2819  CG2 THR A1155      -5.605  -7.454  37.533  1.00 52.08           C  
ANISOU 2819  CG2 THR A1155     5806   8765   5217  -1221   -201    682       C  
ATOM   2820  N   GLY A1156      -1.923  -7.896  34.683  1.00 51.93           N  
ANISOU 2820  N   GLY A1156     6491   8774   4466  -1284   -185    207       N  
ATOM   2821  CA  GLY A1156      -1.048  -7.535  33.571  1.00 52.27           C  
ANISOU 2821  CA  GLY A1156     6621   8991   4247  -1295   -220    177       C  
ATOM   2822  C   GLY A1156      -1.289  -6.125  33.073  1.00 57.91           C  
ANISOU 2822  C   GLY A1156     7106   9988   4909  -1206   -407    510       C  
ATOM   2823  O   GLY A1156      -0.982  -5.806  31.920  1.00 57.77           O  
ANISOU 2823  O   GLY A1156     7087  10245   4616  -1310   -506    548       O  
ATOM   2824  N   THR A1157      -1.853  -5.274  33.952  1.00 55.63           N  
ANISOU 2824  N   THR A1157     6620   9624   4892  -1010   -439    758       N  
ATOM   2825  CA  THR A1157      -2.174  -3.864  33.705  1.00 55.81           C  
ANISOU 2825  CA  THR A1157     6400   9817   4989   -871   -588   1109       C  
ATOM   2826  C   THR A1157      -1.690  -3.022  34.888  1.00 60.01           C  
ANISOU 2826  C   THR A1157     6938  10043   5820   -546   -455   1215       C  
ATOM   2827  O   THR A1157      -1.376  -3.570  35.946  1.00 59.36           O  
ANISOU 2827  O   THR A1157     6996   9690   5868   -464   -286   1048       O  
ATOM   2828  CB  THR A1157      -3.698  -3.667  33.508  1.00 64.51           C  
ANISOU 2828  CB  THR A1157     7187  11171   6155  -1002   -775   1305       C  
ATOM   2829  OG1 THR A1157      -4.405  -4.161  34.651  1.00 64.89           O  
ANISOU 2829  OG1 THR A1157     7188  11027   6442   -979   -665   1221       O  
ATOM   2830  CG2 THR A1157      -4.228  -4.302  32.223  1.00 62.57           C  
ANISOU 2830  CG2 THR A1157     6897  11309   5568  -1362   -971   1247       C  
ATOM   2831  N   TRP A1158      -1.658  -1.693  34.714  1.00 57.42           N  
ANISOU 2831  N   TRP A1158     6458   9760   5599   -380   -535   1497       N  
ATOM   2832  CA  TRP A1158      -1.267  -0.749  35.759  1.00 57.75           C  
ANISOU 2832  CA  TRP A1158     6502   9517   5924   -101   -421   1582       C  
ATOM   2833  C   TRP A1158      -2.528  -0.271  36.505  1.00 62.01           C  
ANISOU 2833  C   TRP A1158     6800  10013   6748      4   -415   1718       C  
ATOM   2834  O   TRP A1158      -2.894   0.903  36.422  1.00 62.71           O  
ANISOU 2834  O   TRP A1158     6685  10109   7032    152   -478   1981       O  
ATOM   2835  CB  TRP A1158      -0.502   0.444  35.155  1.00 56.67           C  
ANISOU 2835  CB  TRP A1158     6340   9397   5796     15   -486   1803       C  
ATOM   2836  CG  TRP A1158       0.696   0.084  34.329  1.00 57.69           C  
ANISOU 2836  CG  TRP A1158     6656   9620   5645    -85   -478   1709       C  
ATOM   2837  CD1 TRP A1158       0.859   0.289  32.991  1.00 60.59           C  
ANISOU 2837  CD1 TRP A1158     6971  10292   5758   -223   -611   1854       C  
ATOM   2838  CD2 TRP A1158       1.919  -0.498  34.797  1.00 57.57           C  
ANISOU 2838  CD2 TRP A1158     6889   9409   5576    -46   -316   1472       C  
ATOM   2839  NE1 TRP A1158       2.107  -0.129  32.595  1.00 59.95           N  
ANISOU 2839  NE1 TRP A1158     7096  10211   5470   -266   -510   1693       N  
ATOM   2840  CE2 TRP A1158       2.781  -0.615  33.684  1.00 61.41           C  
ANISOU 2840  CE2 TRP A1158     7454  10081   5798   -148   -332   1467       C  
ATOM   2841  CE3 TRP A1158       2.375  -0.931  36.055  1.00 58.87           C  
ANISOU 2841  CE3 TRP A1158     7200   9282   5885     64   -158   1286       C  
ATOM   2842  CZ2 TRP A1158       4.069  -1.151  33.787  1.00 60.78           C  
ANISOU 2842  CZ2 TRP A1158     7573   9881   5640   -119   -179   1280       C  
ATOM   2843  CZ3 TRP A1158       3.654  -1.457  36.157  1.00 60.31           C  
ANISOU 2843  CZ3 TRP A1158     7574   9356   5984     84    -44   1133       C  
ATOM   2844  CH2 TRP A1158       4.484  -1.567  35.033  1.00 60.92           C  
ANISOU 2844  CH2 TRP A1158     7705   9599   5843      5    -46   1128       C  
ATOM   2845  N   ASP A1159      -3.221  -1.194  37.187  1.00 57.66           N  
ANISOU 2845  N   ASP A1159     6254   9417   6236    -74   -328   1557       N  
ATOM   2846  CA  ASP A1159      -4.443  -0.866  37.926  1.00 57.18           C  
ANISOU 2846  CA  ASP A1159     5952   9338   6434     14   -280   1664       C  
ATOM   2847  C   ASP A1159      -4.179  -0.570  39.408  1.00 59.66           C  
ANISOU 2847  C   ASP A1159     6379   9346   6944    226    -50   1550       C  
ATOM   2848  O   ASP A1159      -4.941   0.182  40.022  1.00 59.37           O  
ANISOU 2848  O   ASP A1159     6150   9248   7159    387     32   1658       O  
ATOM   2849  CB  ASP A1159      -5.521  -1.952  37.742  1.00 59.22           C  
ANISOU 2849  CB  ASP A1159     6091   9787   6624   -234   -335   1604       C  
ATOM   2850  CG  ASP A1159      -6.192  -1.980  36.372  1.00 71.48           C  
ANISOU 2850  CG  ASP A1159     7430  11708   8022   -453   -595   1771       C  
ATOM   2851  OD1 ASP A1159      -6.084  -0.975  35.629  1.00 71.86           O  
ANISOU 2851  OD1 ASP A1159     7338  11888   8077   -368   -736   2025       O  
ATOM   2852  OD2 ASP A1159      -6.840  -3.000  36.050  1.00 78.31           O  
ANISOU 2852  OD2 ASP A1159     8262  12734   8759   -727   -666   1662       O  
ATOM   2853  N   ALA A1160      -3.091  -1.138  39.970  1.00 54.70           N  
ANISOU 2853  N   ALA A1160     6050   8539   6195    228     60   1338       N  
ATOM   2854  CA  ALA A1160      -2.693  -0.931  41.367  1.00 54.10           C  
ANISOU 2854  CA  ALA A1160     6115   8218   6223    384    251   1222       C  
ATOM   2855  C   ALA A1160      -2.088   0.467  41.584  1.00 57.16           C  
ANISOU 2855  C   ALA A1160     6514   8454   6751    590    270   1298       C  
ATOM   2856  O   ALA A1160      -2.092   0.971  42.708  1.00 56.35           O  
ANISOU 2856  O   ALA A1160     6460   8177   6773    726    421   1221       O  
ATOM   2857  CB  ALA A1160      -1.713  -2.011  41.799  1.00 54.76           C  
ANISOU 2857  CB  ALA A1160     6477   8194   6134    303    322   1028       C  
ATOM   2858  N   TYR A1161      -1.575   1.084  40.503  1.00 53.87           N  
ANISOU 2858  N   TYR A1161     6060   8106   6301    591    122   1443       N  
ATOM   2859  CA  TYR A1161      -0.999   2.433  40.490  1.00 53.96           C  
ANISOU 2859  CA  TYR A1161     6067   7965   6470    751    113   1556       C  
ATOM   2860  C   TYR A1161      -1.723   3.234  39.419  1.00 62.83           C  
ANISOU 2860  C   TYR A1161     6923   9234   7716    779    -37   1856       C  
ATOM   2861  O   TYR A1161      -2.099   2.674  38.388  1.00 62.85           O  
ANISOU 2861  O   TYR A1161     6839   9507   7537    619   -191   1957       O  
ATOM   2862  CB  TYR A1161       0.508   2.423  40.135  1.00 53.38           C  
ANISOU 2862  CB  TYR A1161     6206   7841   6234    711     73   1502       C  
ATOM   2863  CG  TYR A1161       1.304   1.255  40.677  1.00 52.65           C  
ANISOU 2863  CG  TYR A1161     6342   7714   5948    626    148   1276       C  
ATOM   2864  CD1 TYR A1161       1.312   0.027  40.018  1.00 53.82           C  
ANISOU 2864  CD1 TYR A1161     6539   8019   5890    466    110   1205       C  
ATOM   2865  CD2 TYR A1161       2.143   1.409  41.776  1.00 52.58           C  
ANISOU 2865  CD2 TYR A1161     6502   7511   5965    698    247   1147       C  
ATOM   2866  CE1 TYR A1161       2.039  -1.052  40.512  1.00 53.05           C  
ANISOU 2866  CE1 TYR A1161     6636   7844   5676    415    194   1028       C  
ATOM   2867  CE2 TYR A1161       2.900   0.344  42.261  1.00 52.78           C  
ANISOU 2867  CE2 TYR A1161     6705   7511   5837    635    299   1004       C  
ATOM   2868  CZ  TYR A1161       2.835  -0.888  41.633  1.00 57.07           C  
ANISOU 2868  CZ  TYR A1161     7279   8171   6233    511    282    956       C  
ATOM   2869  OH  TYR A1161       3.573  -1.943  42.109  1.00 54.68           O  
ANISOU 2869  OH  TYR A1161     7137   7799   5840    475    350    841       O  
ATOM   2870  N   THR A 354      -1.898   4.540  39.636  1.00 62.63           N  
ANISOU 2870  N   THR A 354     5456  14240   4098  -1302   1610   3234       N  
ATOM   2871  CA  THR A 354      -2.513   5.401  38.624  1.00 63.63           C  
ANISOU 2871  CA  THR A 354     5523  14310   4342  -1255   1591   2983       C  
ATOM   2872  C   THR A 354      -1.354   6.030  37.868  1.00 68.85           C  
ANISOU 2872  C   THR A 354     6336  14695   5130  -1117   1468   2780       C  
ATOM   2873  O   THR A 354      -0.635   6.854  38.430  1.00 68.90           O  
ANISOU 2873  O   THR A 354     6370  14804   5003   -952   1437   2635       O  
ATOM   2874  CB  THR A 354      -3.523   6.374  39.252  1.00 75.87           C  
ANISOU 2874  CB  THR A 354     6887  16244   5696  -1164   1681   2849       C  
ATOM   2875  OG1 THR A 354      -2.931   7.010  40.388  1.00 77.46           O  
ANISOU 2875  OG1 THR A 354     7090  16681   5658  -1016   1693   2799       O  
ATOM   2876  CG2 THR A 354      -4.813   5.675  39.670  1.00 74.48           C  
ANISOU 2876  CG2 THR A 354     6542  16296   5460  -1335   1799   3039       C  
ATOM   2877  N   PHE A 355      -1.102   5.565  36.633  1.00 65.90           N  
ANISOU 2877  N   PHE A 355     6065  13971   5005  -1196   1399   2782       N  
ATOM   2878  CA  PHE A 355       0.052   6.023  35.863  1.00 65.96           C  
ANISOU 2878  CA  PHE A 355     6219  13698   5144  -1086   1285   2620       C  
ATOM   2879  C   PHE A 355      -0.212   7.147  34.889  1.00 70.65           C  
ANISOU 2879  C   PHE A 355     6787  14227   5829   -988   1245   2344       C  
ATOM   2880  O   PHE A 355      -1.196   7.125  34.143  1.00 70.70           O  
ANISOU 2880  O   PHE A 355     6706  14232   5926  -1062   1276   2309       O  
ATOM   2881  CB  PHE A 355       0.719   4.855  35.123  1.00 67.72           C  
ANISOU 2881  CB  PHE A 355     6587  13568   5575  -1202   1227   2773       C  
ATOM   2882  CG  PHE A 355       1.769   4.076  35.884  1.00 69.12           C  
ANISOU 2882  CG  PHE A 355     6874  13692   5695  -1193   1205   2970       C  
ATOM   2883  CD1 PHE A 355       2.031   4.346  37.223  1.00 71.75           C  
ANISOU 2883  CD1 PHE A 355     7163  14312   5786  -1108   1237   3026       C  
ATOM   2884  CD2 PHE A 355       2.493   3.070  35.261  1.00 71.33           C  
ANISOU 2884  CD2 PHE A 355     7299  13645   6157  -1263   1153   3099       C  
ATOM   2885  CE1 PHE A 355       2.999   3.624  37.920  1.00 72.65           C  
ANISOU 2885  CE1 PHE A 355     7370  14394   5839  -1092   1213   3220       C  
ATOM   2886  CE2 PHE A 355       3.460   2.350  35.962  1.00 74.07           C  
ANISOU 2886  CE2 PHE A 355     7743  13948   6451  -1236   1133   3292       C  
ATOM   2887  CZ  PHE A 355       3.693   2.620  37.290  1.00 71.97           C  
ANISOU 2887  CZ  PHE A 355     7424  13980   5942  -1152   1162   3360       C  
ATOM   2888  N   SER A 356       0.728   8.101  34.855  1.00 66.92           N  
ANISOU 2888  N   SER A 356     6396  13691   5339   -826   1173   2154       N  
ATOM   2889  CA  SER A 356       0.701   9.241  33.951  1.00 66.47           C  
ANISOU 2889  CA  SER A 356     6347  13539   5371   -714   1126   1893       C  
ATOM   2890  C   SER A 356       1.145   8.805  32.554  1.00 69.65           C  
ANISOU 2890  C   SER A 356     6856  13583   6024   -777   1046   1881       C  
ATOM   2891  O   SER A 356       1.797   7.764  32.414  1.00 69.54           O  
ANISOU 2891  O   SER A 356     6941  13383   6098   -866   1012   2041       O  
ATOM   2892  CB  SER A 356       1.609  10.355  34.472  1.00 70.13           C  
ANISOU 2892  CB  SER A 356     6868  14059   5718   -539   1081   1707       C  
ATOM   2893  OG  SER A 356       2.988  10.115  34.234  1.00 78.61           O  
ANISOU 2893  OG  SER A 356     8085  14924   6857   -526    992   1737       O  
ATOM   2894  N   LEU A 357       0.822   9.616  31.524  1.00 64.84           N  
ANISOU 2894  N   LEU A 357     6232  12880   5525   -719   1016   1690       N  
ATOM   2895  CA  LEU A 357       1.239   9.362  30.143  1.00 63.79           C  
ANISOU 2895  CA  LEU A 357     6195  12428   5614   -762    938   1648       C  
ATOM   2896  C   LEU A 357       2.758   9.544  30.047  1.00 66.89           C  
ANISOU 2896  C   LEU A 357     6741  12628   6047   -678    849   1593       C  
ATOM   2897  O   LEU A 357       3.362  10.154  30.935  1.00 66.47           O  
ANISOU 2897  O   LEU A 357     6704  12701   5852   -570    843   1529       O  
ATOM   2898  CB  LEU A 357       0.534  10.320  29.159  1.00 63.52           C  
ANISOU 2898  CB  LEU A 357     6097  12380   5656   -698    928   1457       C  
ATOM   2899  CG  LEU A 357      -0.987  10.199  28.995  1.00 67.95           C  
ANISOU 2899  CG  LEU A 357     6494  13118   6207   -779   1002   1495       C  
ATOM   2900  CD1 LEU A 357      -1.542  11.394  28.254  1.00 67.78           C  
ANISOU 2900  CD1 LEU A 357     6406  13138   6211   -652    995   1291       C  
ATOM   2901  CD2 LEU A 357      -1.378   8.925  28.262  1.00 70.55           C  
ANISOU 2901  CD2 LEU A 357     6830  13289   6688   -981    993   1645       C  
ATOM   2902  N   VAL A 358       3.377   9.004  28.990  1.00 62.98           N  
ANISOU 2902  N   VAL A 358     6352  11841   5737   -733    783   1616       N  
ATOM   2903  CA  VAL A 358       4.821   9.111  28.794  1.00 62.58           C  
ANISOU 2903  CA  VAL A 358     6435  11607   5736   -660    700   1573       C  
ATOM   2904  C   VAL A 358       5.221  10.580  28.510  1.00 65.21           C  
ANISOU 2904  C   VAL A 358     6784  11943   6051   -512    655   1330       C  
ATOM   2905  O   VAL A 358       4.817  11.163  27.496  1.00 65.15           O  
ANISOU 2905  O   VAL A 358     6767  11839   6150   -489    637   1198       O  
ATOM   2906  CB  VAL A 358       5.387   8.084  27.758  1.00 66.68           C  
ANISOU 2906  CB  VAL A 358     7063  11819   6452   -748    648   1661       C  
ATOM   2907  CG1 VAL A 358       4.657   8.146  26.416  1.00 66.38           C  
ANISOU 2907  CG1 VAL A 358     7006  11645   6571   -806    636   1573       C  
ATOM   2908  CG2 VAL A 358       6.900   8.227  27.575  1.00 66.50           C  
ANISOU 2908  CG2 VAL A 358     7162  11637   6469   -660    566   1619       C  
ATOM   2909  N   LYS A 359       5.974  11.176  29.454  1.00 59.80           N  
ANISOU 2909  N   LYS A 359     6119  11382   5222   -415    642   1274       N  
ATOM   2910  CA  LYS A 359       6.489  12.539  29.340  1.00 58.61           C  
ANISOU 2910  CA  LYS A 359     5998  11227   5042   -287    601   1049       C  
ATOM   2911  C   LYS A 359       7.663  12.482  28.367  1.00 59.53           C  
ANISOU 2911  C   LYS A 359     6232  11075   5311   -279    510   1008       C  
ATOM   2912  O   LYS A 359       8.674  11.840  28.652  1.00 59.52           O  
ANISOU 2912  O   LYS A 359     6294  11022   5299   -290    468   1102       O  
ATOM   2913  CB  LYS A 359       6.912  13.091  30.726  1.00 61.24           C  
ANISOU 2913  CB  LYS A 359     6313  11796   5160   -210    616   1005       C  
ATOM   2914  CG  LYS A 359       7.503  14.511  30.721  1.00 79.12           C  
ANISOU 2914  CG  LYS A 359     8622  14053   7386    -91    574    764       C  
ATOM   2915  CD  LYS A 359       6.461  15.615  30.466  1.00 91.20           C  
ANISOU 2915  CD  LYS A 359    10098  15641   8915    -14    621    587       C  
ATOM   2916  CE  LYS A 359       7.034  17.011  30.558  1.00102.48           C  
ANISOU 2916  CE  LYS A 359    11587  17045  10306     98    586    351       C  
ATOM   2917  NZ  LYS A 359       7.836  17.370  29.357  1.00110.76           N  
ANISOU 2917  NZ  LYS A 359    12736  17815  11534    101    505    271       N  
ATOM   2918  N   GLU A 360       7.498  13.094  27.193  1.00 53.62           N  
ANISOU 2918  N   GLU A 360     5505  10164   4702   -260    482    882       N  
ATOM   2919  CA  GLU A 360       8.528  13.091  26.159  1.00 52.25           C  
ANISOU 2919  CA  GLU A 360     5434   9742   4678   -254    402    836       C  
ATOM   2920  C   GLU A 360       9.592  14.132  26.484  1.00 53.02           C  
ANISOU 2920  C   GLU A 360     5586   9847   4714   -159    352    687       C  
ATOM   2921  O   GLU A 360       9.287  15.315  26.596  1.00 52.11           O  
ANISOU 2921  O   GLU A 360     5453   9798   4550    -83    364    521       O  
ATOM   2922  CB  GLU A 360       7.907  13.277  24.763  1.00 53.74           C  
ANISOU 2922  CB  GLU A 360     5620   9777   5023   -273    393    766       C  
ATOM   2923  CG  GLU A 360       6.931  12.162  24.416  1.00 65.44           C  
ANISOU 2923  CG  GLU A 360     7048  11248   6569   -390    435    907       C  
ATOM   2924  CD  GLU A 360       6.008  12.392  23.237  1.00 86.80           C  
ANISOU 2924  CD  GLU A 360     9711  13883   9384   -411    437    836       C  
ATOM   2925  OE1 GLU A 360       6.513  12.573  22.105  1.00 80.29           O  
ANISOU 2925  OE1 GLU A 360     8955  12864   8686   -399    380    767       O  
ATOM   2926  OE2 GLU A 360       4.773  12.358  23.442  1.00 80.43           O  
ANISOU 2926  OE2 GLU A 360     8796  13233   8532   -441    496    856       O  
ATOM   2927  N   LYS A 361      10.824  13.675  26.732  1.00 47.96           N  
ANISOU 2927  N   LYS A 361     5005   9151   4065   -164    299    752       N  
ATOM   2928  CA  LYS A 361      11.938  14.551  27.091  1.00 47.17           C  
ANISOU 2928  CA  LYS A 361     4949   9070   3901    -97    244    626       C  
ATOM   2929  C   LYS A 361      12.432  15.327  25.869  1.00 49.72           C  
ANISOU 2929  C   LYS A 361     5336   9189   4368    -71    191    480       C  
ATOM   2930  O   LYS A 361      12.161  14.915  24.736  1.00 49.50           O  
ANISOU 2930  O   LYS A 361     5328   8989   4490   -106    184    515       O  
ATOM   2931  CB  LYS A 361      13.083  13.745  27.740  1.00 49.89           C  
ANISOU 2931  CB  LYS A 361     5321   9446   4188   -110    203    760       C  
ATOM   2932  CG  LYS A 361      12.719  13.052  29.059  1.00 58.29           C  
ANISOU 2932  CG  LYS A 361     6327  10732   5087   -128    252    912       C  
ATOM   2933  CD  LYS A 361      12.890  13.957  30.274  1.00 67.20           C  
ANISOU 2933  CD  LYS A 361     7419  12103   6011    -70    257    800       C  
ATOM   2934  CE  LYS A 361      12.557  13.257  31.571  1.00 78.04           C  
ANISOU 2934  CE  LYS A 361     8730  13715   7206    -86    308    958       C  
ATOM   2935  NZ  LYS A 361      13.625  12.308  31.989  1.00 85.41           N  
ANISOU 2935  NZ  LYS A 361     9688  14659   8104    -95    263   1137       N  
ATOM   2936  N   ALA A 362      13.153  16.450  26.102  1.00 44.49           N  
ANISOU 2936  N   ALA A 362     4706   8546   3653    -17    154    318       N  
ATOM   2937  CA  ALA A 362      13.708  17.326  25.063  1.00 43.49           C  
ANISOU 2937  CA  ALA A 362     4642   8239   3642      6    106    176       C  
ATOM   2938  C   ALA A 362      14.443  16.558  23.956  1.00 46.16           C  
ANISOU 2938  C   ALA A 362     5027   8379   4134    -35     57    262       C  
ATOM   2939  O   ALA A 362      14.276  16.883  22.782  1.00 45.50           O  
ANISOU 2939  O   ALA A 362     4973   8134   4180    -33     46    203       O  
ATOM   2940  CB  ALA A 362      14.630  18.365  25.687  1.00 43.98           C  
ANISOU 2940  CB  ALA A 362     4737   8364   3610     40     67     29       C  
ATOM   2941  N   ALA A 363      15.212  15.516  24.338  1.00 42.01           N  
ANISOU 2941  N   ALA A 363     4504   7870   3586    -62     33    407       N  
ATOM   2942  CA  ALA A 363      15.982  14.647  23.446  1.00 41.43           C  
ANISOU 2942  CA  ALA A 363     4475   7625   3643    -87     -7    500       C  
ATOM   2943  C   ALA A 363      15.096  13.914  22.429  1.00 44.15           C  
ANISOU 2943  C   ALA A 363     4825   7828   4122   -130     24    567       C  
ATOM   2944  O   ALA A 363      15.398  13.938  21.234  1.00 44.01           O  
ANISOU 2944  O   ALA A 363     4849   7639   4234   -135     -4    527       O  
ATOM   2945  CB  ALA A 363      16.781  13.644  24.266  1.00 42.15           C  
ANISOU 2945  CB  ALA A 363     4560   7793   3663    -89    -24    659       C  
ATOM   2946  N   LEU A 364      14.007  13.276  22.909  1.00 39.42           N  
ANISOU 2946  N   LEU A 364     4180   7314   3484   -168     82    666       N  
ATOM   2947  CA  LEU A 364      13.036  12.530  22.105  1.00 38.76           C  
ANISOU 2947  CA  LEU A 364     4088   7132   3508   -231    116    733       C  
ATOM   2948  C   LEU A 364      12.253  13.479  21.168  1.00 41.58           C  
ANISOU 2948  C   LEU A 364     4426   7444   3927   -215    123    589       C  
ATOM   2949  O   LEU A 364      12.027  13.159  20.002  1.00 41.13           O  
ANISOU 2949  O   LEU A 364     4389   7244   3996   -250    112    588       O  
ATOM   2950  CB  LEU A 364      12.081  11.766  23.057  1.00 38.81           C  
ANISOU 2950  CB  LEU A 364     4035   7282   3428   -283    180    871       C  
ATOM   2951  CG  LEU A 364      11.077  10.773  22.439  1.00 43.79           C  
ANISOU 2951  CG  LEU A 364     4649   7834   4154   -380    218    969       C  
ATOM   2952  CD1 LEU A 364      11.760   9.515  21.946  1.00 44.00           C  
ANISOU 2952  CD1 LEU A 364     4754   7674   4291   -429    195   1095       C  
ATOM   2953  CD2 LEU A 364      10.025  10.382  23.438  1.00 45.91           C  
ANISOU 2953  CD2 LEU A 364     4839   8290   4316   -430    288   1071       C  
ATOM   2954  N   ARG A 365      11.870  14.651  21.696  1.00 37.31           N  
ANISOU 2954  N   ARG A 365     3852   7030   3295   -154    140    467       N  
ATOM   2955  CA  ARG A 365      11.119  15.710  21.022  1.00 36.27           C  
ANISOU 2955  CA  ARG A 365     3702   6881   3200   -109    152    330       C  
ATOM   2956  C   ARG A 365      11.915  16.309  19.848  1.00 37.42           C  
ANISOU 2956  C   ARG A 365     3918   6841   3460    -84     96    236       C  
ATOM   2957  O   ARG A 365      11.366  16.437  18.751  1.00 37.10           O  
ANISOU 2957  O   ARG A 365     3873   6709   3513    -86     95    205       O  
ATOM   2958  CB  ARG A 365      10.726  16.796  22.045  1.00 38.04           C  
ANISOU 2958  CB  ARG A 365     3890   7278   3286    -36    186    223       C  
ATOM   2959  CG  ARG A 365       9.727  16.328  23.130  1.00 48.72           C  
ANISOU 2959  CG  ARG A 365     5154   8840   4517    -53    255    306       C  
ATOM   2960  CD  ARG A 365       9.297  17.449  24.078  1.00 59.04           C  
ANISOU 2960  CD  ARG A 365     6426  10321   5687     34    296    179       C  
ATOM   2961  NE  ARG A 365       8.113  17.082  24.867  1.00 69.25           N  
ANISOU 2961  NE  ARG A 365     7616  11818   6879     23    373    250       N  
ATOM   2962  CZ  ARG A 365       7.246  17.945  25.397  1.00 79.62           C  
ANISOU 2962  CZ  ARG A 365     8870  13286   8097    103    429    149       C  
ATOM   2963  NH1 ARG A 365       7.403  19.249  25.218  1.00 69.35           N  
ANISOU 2963  NH1 ARG A 365     7615  11936   6799    204    418    -32       N  
ATOM   2964  NH2 ARG A 365       6.214  17.507  26.104  1.00 60.02           N  
ANISOU 2964  NH2 ARG A 365     6283  11004   5518     85    501    230       N  
ATOM   2965  N   THR A 366      13.208  16.648  20.075  1.00 31.83           N  
ANISOU 2965  N   THR A 366     3266   6092   2736    -64     48    197       N  
ATOM   2966  CA  THR A 366      14.128  17.209  19.074  1.00 30.81           C  
ANISOU 2966  CA  THR A 366     3201   5804   2702    -50     -4    118       C  
ATOM   2967  C   THR A 366      14.353  16.207  17.941  1.00 34.62           C  
ANISOU 2967  C   THR A 366     3706   6136   3310    -97    -25    205       C  
ATOM   2968  O   THR A 366      14.409  16.615  16.780  1.00 34.13           O  
ANISOU 2968  O   THR A 366     3673   5954   3343    -90    -44    146       O  
ATOM   2969  CB  THR A 366      15.471  17.630  19.718  1.00 34.66           C  
ANISOU 2969  CB  THR A 366     3723   6319   3128    -36    -47     72       C  
ATOM   2970  OG1 THR A 366      15.226  18.487  20.832  1.00 32.84           O  
ANISOU 2970  OG1 THR A 366     3473   6235   2768     -1    -26    -16       O  
ATOM   2971  CG2 THR A 366      16.393  18.346  18.743  1.00 30.85           C  
ANISOU 2971  CG2 THR A 366     3296   5691   2733    -29    -95    -17       C  
ATOM   2972  N   LEU A 367      14.466  14.901  18.286  1.00 30.93           N  
ANISOU 2972  N   LEU A 367     3234   5677   2841   -144    -17    344       N  
ATOM   2973  CA  LEU A 367      14.669  13.801  17.339  1.00 30.54           C  
ANISOU 2973  CA  LEU A 367     3217   5481   2904   -190    -31    428       C  
ATOM   2974  C   LEU A 367      13.533  13.706  16.310  1.00 33.56           C  
ANISOU 2974  C   LEU A 367     3580   5803   3369   -227    -11    409       C  
ATOM   2975  O   LEU A 367      13.818  13.643  15.116  1.00 33.24           O  
ANISOU 2975  O   LEU A 367     3576   5628   3426   -235    -38    380       O  
ATOM   2976  CB  LEU A 367      14.870  12.457  18.074  1.00 30.50           C  
ANISOU 2976  CB  LEU A 367     3217   5498   2874   -226    -16    587       C  
ATOM   2977  CG  LEU A 367      15.253  11.237  17.210  1.00 34.62           C  
ANISOU 2977  CG  LEU A 367     3792   5850   3512   -265    -27    674       C  
ATOM   2978  CD1 LEU A 367      16.590  11.434  16.510  1.00 34.17           C  
ANISOU 2978  CD1 LEU A 367     3785   5685   3513   -217    -78    629       C  
ATOM   2979  CD2 LEU A 367      15.281   9.973  18.039  1.00 36.20           C  
ANISOU 2979  CD2 LEU A 367     4001   6069   3684   -296     -1    839       C  
ATOM   2980  N   SER A 368      12.265  13.728  16.760  1.00 29.32           N  
ANISOU 2980  N   SER A 368     2977   5382   2782   -248     36    423       N  
ATOM   2981  CA  SER A 368      11.129  13.685  15.841  1.00 29.24           C  
ANISOU 2981  CA  SER A 368     2925   5352   2832   -284     53    404       C  
ATOM   2982  C   SER A 368      11.018  14.974  15.037  1.00 31.86           C  
ANISOU 2982  C   SER A 368     3259   5653   3192   -215     32    273       C  
ATOM   2983  O   SER A 368      10.649  14.901  13.873  1.00 31.87           O  
ANISOU 2983  O   SER A 368     3260   5576   3273   -235     18    252       O  
ATOM   2984  CB  SER A 368       9.823  13.380  16.566  1.00 32.99           C  
ANISOU 2984  CB  SER A 368     3313   5986   3237   -323    110    460       C  
ATOM   2985  OG  SER A 368       9.563  14.344  17.570  1.00 45.39           O  
ANISOU 2985  OG  SER A 368     4842   7710   4695   -248    136    399       O  
ATOM   2986  N   ALA A 369      11.374  16.135  15.632  1.00 27.23           N  
ANISOU 2986  N   ALA A 369     2683   5123   2541   -135     31    185       N  
ATOM   2987  CA  ALA A 369      11.348  17.439  14.958  1.00 26.44           C  
ANISOU 2987  CA  ALA A 369     2602   4976   2469    -61     16     65       C  
ATOM   2988  C   ALA A 369      12.339  17.481  13.782  1.00 29.23           C  
ANISOU 2988  C   ALA A 369     3025   5162   2918    -69    -35     42       C  
ATOM   2989  O   ALA A 369      11.944  17.847  12.675  1.00 27.51           O  
ANISOU 2989  O   ALA A 369     2808   4882   2763    -53    -45      5       O  
ATOM   2990  CB  ALA A 369      11.659  18.560  15.943  1.00 26.90           C  
ANISOU 2990  CB  ALA A 369     2675   5108   2437     10     26    -26       C  
ATOM   2991  N   ILE A 370      13.611  17.086  14.017  1.00 25.68           N  
ANISOU 2991  N   ILE A 370     2626   4659   2473    -89    -65     71       N  
ATOM   2992  CA  ILE A 370      14.650  17.095  12.976  1.00 25.10           C  
ANISOU 2992  CA  ILE A 370     2610   4449   2480    -94   -108     54       C  
ATOM   2993  C   ILE A 370      14.337  16.044  11.882  1.00 27.61           C  
ANISOU 2993  C   ILE A 370     2928   4680   2882   -145   -113    113       C  
ATOM   2994  O   ILE A 370      14.558  16.317  10.704  1.00 26.62           O  
ANISOU 2994  O   ILE A 370     2830   4463   2822   -139   -136     75       O  
ATOM   2995  CB  ILE A 370      16.104  17.011  13.543  1.00 27.94           C  
ANISOU 2995  CB  ILE A 370     3006   4798   2812    -93   -138     64       C  
ATOM   2996  CG1 ILE A 370      16.386  15.682  14.288  1.00 27.71           C  
ANISOU 2996  CG1 ILE A 370     2965   4811   2752   -125   -131    181       C  
ATOM   2997  CG2 ILE A 370      16.411  18.241  14.424  1.00 28.79           C  
ANISOU 2997  CG2 ILE A 370     3120   4976   2843    -54   -141    -30       C  
ATOM   2998  CD1 ILE A 370      17.847  15.454  14.730  1.00 30.68           C  
ANISOU 2998  CD1 ILE A 370     3366   5185   3108   -114   -166    211       C  
ATOM   2999  N   LEU A 371      13.742  14.893  12.271  1.00 23.67           N  
ANISOU 2999  N   LEU A 371     2401   4214   2377   -201    -89    201       N  
ATOM   3000  CA  LEU A 371      13.345  13.828  11.347  1.00 22.74           C  
ANISOU 3000  CA  LEU A 371     2290   4015   2335   -267    -90    248       C  
ATOM   3001  C   LEU A 371      12.156  14.292  10.491  1.00 26.24           C  
ANISOU 3001  C   LEU A 371     2685   4485   2800   -275    -84    198       C  
ATOM   3002  O   LEU A 371      12.196  14.112   9.277  1.00 25.92           O  
ANISOU 3002  O   LEU A 371     2664   4359   2824   -294   -108    173       O  
ATOM   3003  CB  LEU A 371      13.040  12.507  12.103  1.00 22.45           C  
ANISOU 3003  CB  LEU A 371     2246   3999   2286   -336    -61    362       C  
ATOM   3004  CG  LEU A 371      12.434  11.334  11.300  1.00 26.68           C  
ANISOU 3004  CG  LEU A 371     2791   4449   2897   -427    -55    408       C  
ATOM   3005  CD1 LEU A 371      13.343  10.891  10.143  1.00 26.41           C  
ANISOU 3005  CD1 LEU A 371     2830   4257   2947   -423    -88    383       C  
ATOM   3006  CD2 LEU A 371      12.107  10.166  12.208  1.00 29.10           C  
ANISOU 3006  CD2 LEU A 371     3096   4773   3187   -498    -20    528       C  
ATOM   3007  N   LEU A 372      11.131  14.931  11.108  1.00 22.23           N  
ANISOU 3007  N   LEU A 372     2108   4107   2231   -250    -54    179       N  
ATOM   3008  CA  LEU A 372       9.983  15.473  10.371  1.00 21.46           C  
ANISOU 3008  CA  LEU A 372     1949   4063   2143   -235    -49    136       C  
ATOM   3009  C   LEU A 372      10.407  16.634   9.459  1.00 24.93           C  
ANISOU 3009  C   LEU A 372     2424   4435   2612   -155    -79     54       C  
ATOM   3010  O   LEU A 372       9.815  16.802   8.399  1.00 24.03           O  
ANISOU 3010  O   LEU A 372     2284   4313   2532   -154    -93     34       O  
ATOM   3011  CB  LEU A 372       8.836  15.892  11.307  1.00 21.21           C  
ANISOU 3011  CB  LEU A 372     1829   4198   2031   -208     -3    138       C  
ATOM   3012  CG  LEU A 372       8.042  14.752  11.968  1.00 25.28           C  
ANISOU 3012  CG  LEU A 372     2281   4806   2520   -306     33    230       C  
ATOM   3013  CD1 LEU A 372       7.288  15.246  13.187  1.00 24.87           C  
ANISOU 3013  CD1 LEU A 372     2155   4928   2366   -263     84    235       C  
ATOM   3014  CD2 LEU A 372       7.086  14.094  10.990  1.00 27.47           C  
ANISOU 3014  CD2 LEU A 372     2499   5095   2845   -387     28    248       C  
ATOM   3015  N   ALA A 373      11.458  17.401   9.854  1.00 21.58           N  
ANISOU 3015  N   ALA A 373     2061   3965   2174    -98    -90     11       N  
ATOM   3016  CA  ALA A 373      12.011  18.517   9.074  1.00 20.83           C  
ANISOU 3016  CA  ALA A 373     2014   3791   2111    -35   -115    -57       C  
ATOM   3017  C   ALA A 373      12.725  18.002   7.823  1.00 23.89           C  
ANISOU 3017  C   ALA A 373     2444   4065   2569    -74   -151    -44       C  
ATOM   3018  O   ALA A 373      12.602  18.611   6.765  1.00 22.94           O  
ANISOU 3018  O   ALA A 373     2332   3905   2480    -43   -167    -75       O  
ATOM   3019  CB  ALA A 373      12.962  19.345   9.928  1.00 21.25           C  
ANISOU 3019  CB  ALA A 373     2118   3829   2127      5   -117   -105       C  
ATOM   3020  N   PHE A 374      13.449  16.867   7.945  1.00 20.47           N  
ANISOU 3020  N   PHE A 374     2037   3586   2155   -133   -159      6       N  
ATOM   3021  CA  PHE A 374      14.157  16.218   6.845  1.00 19.82           C  
ANISOU 3021  CA  PHE A 374     1996   3401   2133   -165   -185     15       C  
ATOM   3022  C   PHE A 374      13.157  15.702   5.804  1.00 24.56           C  
ANISOU 3022  C   PHE A 374     2563   4005   2764   -208   -189     18       C  
ATOM   3023  O   PHE A 374      13.313  15.992   4.615  1.00 23.62           O  
ANISOU 3023  O   PHE A 374     2459   3840   2674   -197   -211    -14       O  
ATOM   3024  CB  PHE A 374      15.050  15.077   7.370  1.00 21.25           C  
ANISOU 3024  CB  PHE A 374     2212   3538   2324   -201   -186     73       C  
ATOM   3025  CG  PHE A 374      15.786  14.276   6.314  1.00 22.37           C  
ANISOU 3025  CG  PHE A 374     2398   3575   2526   -222   -205     79       C  
ATOM   3026  CD1 PHE A 374      16.725  14.881   5.486  1.00 24.92           C  
ANISOU 3026  CD1 PHE A 374     2751   3847   2870   -185   -227     37       C  
ATOM   3027  CD2 PHE A 374      15.585  12.906   6.192  1.00 23.97           C  
ANISOU 3027  CD2 PHE A 374     2617   3728   2763   -279   -195    127       C  
ATOM   3028  CE1 PHE A 374      17.431  14.133   4.541  1.00 25.75           C  
ANISOU 3028  CE1 PHE A 374     2893   3871   3020   -195   -238     38       C  
ATOM   3029  CE2 PHE A 374      16.301  12.158   5.255  1.00 26.54           C  
ANISOU 3029  CE2 PHE A 374     2992   3950   3141   -287   -208    120       C  
ATOM   3030  CZ  PHE A 374      17.212  12.778   4.431  1.00 24.84           C  
ANISOU 3030  CZ  PHE A 374     2798   3704   2938   -239   -228     74       C  
ATOM   3031  N   ILE A 375      12.123  14.954   6.262  1.00 21.43           N  
ANISOU 3031  N   ILE A 375     2115   3675   2352   -265   -167     57       N  
ATOM   3032  CA  ILE A 375      11.056  14.417   5.418  1.00 21.03           C  
ANISOU 3032  CA  ILE A 375     2016   3654   2320   -327   -171     57       C  
ATOM   3033  C   ILE A 375      10.344  15.576   4.693  1.00 25.00           C  
ANISOU 3033  C   ILE A 375     2470   4223   2806   -263   -183      9       C  
ATOM   3034  O   ILE A 375      10.242  15.539   3.474  1.00 24.66           O  
ANISOU 3034  O   ILE A 375     2428   4155   2786   -274   -210    -15       O  
ATOM   3035  CB  ILE A 375      10.066  13.508   6.228  1.00 23.86           C  
ANISOU 3035  CB  ILE A 375     2319   4088   2659   -411   -140    115       C  
ATOM   3036  CG1 ILE A 375      10.805  12.306   6.869  1.00 24.22           C  
ANISOU 3036  CG1 ILE A 375     2428   4046   2730   -469   -128    178       C  
ATOM   3037  CG2 ILE A 375       8.889  13.029   5.344  1.00 23.18           C  
ANISOU 3037  CG2 ILE A 375     2168   4055   2586   -490   -148    105       C  
ATOM   3038  CD1 ILE A 375      10.111  11.635   8.086  1.00 27.86           C  
ANISOU 3038  CD1 ILE A 375     2847   4586   3154   -529    -88    258       C  
ATOM   3039  N   LEU A 376       9.896  16.609   5.433  1.00 21.43           N  
ANISOU 3039  N   LEU A 376     1981   3853   2309   -186   -162     -4       N  
ATOM   3040  CA  LEU A 376       9.171  17.760   4.879  1.00 21.24           C  
ANISOU 3040  CA  LEU A 376     1914   3889   2268   -101   -167    -38       C  
ATOM   3041  C   LEU A 376       9.887  18.468   3.720  1.00 25.06           C  
ANISOU 3041  C   LEU A 376     2456   4280   2785    -51   -199    -69       C  
ATOM   3042  O   LEU A 376       9.299  18.649   2.660  1.00 24.81           O  
ANISOU 3042  O   LEU A 376     2388   4282   2756    -38   -219    -73       O  
ATOM   3043  CB  LEU A 376       8.828  18.768   5.996  1.00 21.15           C  
ANISOU 3043  CB  LEU A 376     1881   3947   2208    -12   -132    -58       C  
ATOM   3044  CG  LEU A 376       8.104  20.056   5.595  1.00 25.81           C  
ANISOU 3044  CG  LEU A 376     2440   4583   2783    105   -127    -92       C  
ATOM   3045  CD1 LEU A 376       6.668  19.780   5.188  1.00 26.10           C  
ANISOU 3045  CD1 LEU A 376     2359   4763   2797    100   -122    -68       C  
ATOM   3046  CD2 LEU A 376       8.156  21.077   6.719  1.00 27.58           C  
ANISOU 3046  CD2 LEU A 376     2687   4823   2969    197    -93   -133       C  
ATOM   3047  N   THR A 377      11.138  18.864   3.935  1.00 21.40           N  
ANISOU 3047  N   THR A 377     2075   3717   2338    -29   -204    -85       N  
ATOM   3048  CA  THR A 377      11.953  19.621   2.986  1.00 21.17           C  
ANISOU 3048  CA  THR A 377     2104   3602   2337     11   -227   -106       C  
ATOM   3049  C   THR A 377      12.491  18.806   1.800  1.00 24.61           C  
ANISOU 3049  C   THR A 377     2562   3984   2804    -46   -254    -97       C  
ATOM   3050  O   THR A 377      12.551  19.342   0.695  1.00 24.11           O  
ANISOU 3050  O   THR A 377     2508   3904   2748    -16   -272   -105       O  
ATOM   3051  CB  THR A 377      13.095  20.324   3.733  1.00 27.41           C  
ANISOU 3051  CB  THR A 377     2964   4323   3130     39   -221   -128       C  
ATOM   3052  OG1 THR A 377      13.916  19.338   4.361  1.00 25.63           O  
ANISOU 3052  OG1 THR A 377     2758   4076   2906    -23   -221   -109       O  
ATOM   3053  CG2 THR A 377      12.587  21.345   4.764  1.00 24.23           C  
ANISOU 3053  CG2 THR A 377     2554   3960   2692    109   -194   -160       C  
ATOM   3054  N   TRP A 378      12.897  17.541   2.022  1.00 21.70           N  
ANISOU 3054  N   TRP A 378     2207   3586   2451   -122   -254    -81       N  
ATOM   3055  CA  TRP A 378      13.477  16.678   0.980  1.00 22.17           C  
ANISOU 3055  CA  TRP A 378     2298   3585   2540   -170   -273    -87       C  
ATOM   3056  C   TRP A 378      12.458  15.866   0.165  1.00 25.77           C  
ANISOU 3056  C   TRP A 378     2708   4088   2995   -233   -285    -93       C  
ATOM   3057  O   TRP A 378      12.827  15.374  -0.904  1.00 25.73           O  
ANISOU 3057  O   TRP A 378     2729   4044   3004   -261   -303   -116       O  
ATOM   3058  CB  TRP A 378      14.549  15.743   1.567  1.00 21.70           C  
ANISOU 3058  CB  TRP A 378     2289   3451   2504   -203   -265    -68       C  
ATOM   3059  CG  TRP A 378      15.869  16.387   1.886  1.00 23.45           C  
ANISOU 3059  CG  TRP A 378     2555   3626   2727   -157   -267    -71       C  
ATOM   3060  CD1 TRP A 378      16.077  17.519   2.622  1.00 26.46           C  
ANISOU 3060  CD1 TRP A 378     2939   4028   3087   -111   -261    -81       C  
ATOM   3061  CD2 TRP A 378      17.170  15.859   1.585  1.00 23.67           C  
ANISOU 3061  CD2 TRP A 378     2627   3587   2779   -159   -273    -68       C  
ATOM   3062  NE1 TRP A 378      17.425  17.772   2.731  1.00 26.27           N  
ANISOU 3062  NE1 TRP A 378     2954   3959   3071    -99   -268    -85       N  
ATOM   3063  CE2 TRP A 378      18.121  16.752   2.133  1.00 27.76           C  
ANISOU 3063  CE2 TRP A 378     3160   4102   3284   -123   -275    -71       C  
ATOM   3064  CE3 TRP A 378      17.628  14.711   0.909  1.00 25.02           C  
ANISOU 3064  CE3 TRP A 378     2826   3703   2979   -185   -275    -67       C  
ATOM   3065  CZ2 TRP A 378      19.502  16.549   2.002  1.00 27.09           C  
ANISOU 3065  CZ2 TRP A 378     3101   3982   3210   -114   -281    -65       C  
ATOM   3066  CZ3 TRP A 378      18.994  14.511   0.780  1.00 26.54           C  
ANISOU 3066  CZ3 TRP A 378     3049   3850   3183   -158   -276    -63       C  
ATOM   3067  CH2 TRP A 378      19.916  15.430   1.308  1.00 27.21           C  
ANISOU 3067  CH2 TRP A 378     3133   3954   3252   -124   -280    -58       C  
ATOM   3068  N   THR A 379      11.198  15.719   0.650  1.00 21.99           N  
ANISOU 3068  N   THR A 379     2158   3704   2494   -261   -275    -80       N  
ATOM   3069  CA  THR A 379      10.143  14.979  -0.061  1.00 22.39           C  
ANISOU 3069  CA  THR A 379     2149   3822   2538   -339   -290    -89       C  
ATOM   3070  C   THR A 379       9.881  15.533  -1.490  1.00 27.81           C  
ANISOU 3070  C   THR A 379     2812   4552   3203   -306   -323   -119       C  
ATOM   3071  O   THR A 379       9.874  14.707  -2.408  1.00 28.25           O  
ANISOU 3071  O   THR A 379     2876   4593   3264   -377   -345   -149       O  
ATOM   3072  CB  THR A 379       8.843  14.857   0.775  1.00 26.73           C  
ANISOU 3072  CB  THR A 379     2606   4490   3058   -371   -269    -62       C  
ATOM   3073  OG1 THR A 379       9.038  13.858   1.773  1.00 25.07           O  
ANISOU 3073  OG1 THR A 379     2422   4235   2868   -444   -243    -29       O  
ATOM   3074  CG2 THR A 379       7.622  14.476  -0.060  1.00 23.26           C  
ANISOU 3074  CG2 THR A 379     2078   4162   2597   -440   -291    -77       C  
ATOM   3075  N   PRO A 380       9.675  16.865  -1.734  1.00 24.07           N  
ANISOU 3075  N   PRO A 380     2314   4127   2704   -202   -328   -111       N  
ATOM   3076  CA  PRO A 380       9.387  17.315  -3.114  1.00 23.75           C  
ANISOU 3076  CA  PRO A 380     2248   4141   2636   -170   -361   -121       C  
ATOM   3077  C   PRO A 380      10.414  16.908  -4.182  1.00 27.70           C  
ANISOU 3077  C   PRO A 380     2817   4561   3146   -198   -380   -148       C  
ATOM   3078  O   PRO A 380      10.008  16.442  -5.244  1.00 28.08           O  
ANISOU 3078  O   PRO A 380     2835   4668   3167   -243   -408   -173       O  
ATOM   3079  CB  PRO A 380       9.259  18.833  -2.976  1.00 25.30           C  
ANISOU 3079  CB  PRO A 380     2440   4355   2819    -41   -353    -95       C  
ATOM   3080  CG  PRO A 380       8.853  19.043  -1.557  1.00 29.15           C  
ANISOU 3080  CG  PRO A 380     2905   4863   3309    -18   -318    -85       C  
ATOM   3081  CD  PRO A 380       9.614  18.007  -0.792  1.00 24.78           C  
ANISOU 3081  CD  PRO A 380     2402   4229   2785   -106   -303    -93       C  
ATOM   3082  N   TYR A 381      11.719  17.037  -3.900  1.00 23.80           N  
ANISOU 3082  N   TYR A 381     2406   3952   2685   -175   -364   -146       N  
ATOM   3083  CA  TYR A 381      12.778  16.659  -4.846  1.00 23.44           C  
ANISOU 3083  CA  TYR A 381     2420   3841   2646   -190   -374   -170       C  
ATOM   3084  C   TYR A 381      12.822  15.140  -5.107  1.00 28.05           C  
ANISOU 3084  C   TYR A 381     3021   4392   3244   -286   -378   -213       C  
ATOM   3085  O   TYR A 381      12.995  14.723  -6.252  1.00 28.05           O  
ANISOU 3085  O   TYR A 381     3032   4403   3224   -311   -395   -252       O  
ATOM   3086  CB  TYR A 381      14.158  17.204  -4.396  1.00 23.75           C  
ANISOU 3086  CB  TYR A 381     2526   3783   2713   -144   -355   -154       C  
ATOM   3087  CG  TYR A 381      15.342  16.465  -4.980  1.00 24.66           C  
ANISOU 3087  CG  TYR A 381     2695   3832   2842   -168   -352   -179       C  
ATOM   3088  CD1 TYR A 381      15.706  16.632  -6.315  1.00 27.14           C  
ANISOU 3088  CD1 TYR A 381     3018   4168   3127   -155   -365   -194       C  
ATOM   3089  CD2 TYR A 381      16.078  15.568  -4.210  1.00 24.57           C  
ANISOU 3089  CD2 TYR A 381     2723   3746   2867   -195   -335   -182       C  
ATOM   3090  CE1 TYR A 381      16.771  15.921  -6.869  1.00 27.83           C  
ANISOU 3090  CE1 TYR A 381     3148   4207   3220   -168   -357   -223       C  
ATOM   3091  CE2 TYR A 381      17.134  14.840  -4.757  1.00 25.07           C  
ANISOU 3091  CE2 TYR A 381     2831   3753   2943   -200   -329   -206       C  
ATOM   3092  CZ  TYR A 381      17.481  15.027  -6.084  1.00 32.92           C  
ANISOU 3092  CZ  TYR A 381     3830   4773   3907   -185   -338   -231       C  
ATOM   3093  OH  TYR A 381      18.533  14.333  -6.620  1.00 35.97           O  
ANISOU 3093  OH  TYR A 381     4254   5114   4298   -178   -326   -259       O  
ATOM   3094  N   ASN A 382      12.680  14.329  -4.050  1.00 24.51           N  
ANISOU 3094  N   ASN A 382     2582   3901   2831   -338   -358   -204       N  
ATOM   3095  CA  ASN A 382      12.723  12.872  -4.147  1.00 23.91           C  
ANISOU 3095  CA  ASN A 382     2540   3762   2782   -430   -355   -236       C  
ATOM   3096  C   ASN A 382      11.494  12.275  -4.821  1.00 26.32           C  
ANISOU 3096  C   ASN A 382     2790   4148   3064   -522   -378   -275       C  
ATOM   3097  O   ASN A 382      11.609  11.215  -5.429  1.00 26.82           O  
ANISOU 3097  O   ASN A 382     2893   4157   3140   -596   -384   -328       O  
ATOM   3098  CB  ASN A 382      12.996  12.247  -2.796  1.00 23.26           C  
ANISOU 3098  CB  ASN A 382     2489   3606   2742   -453   -325   -197       C  
ATOM   3099  CG  ASN A 382      14.436  12.434  -2.403  1.00 34.37           C  
ANISOU 3099  CG  ASN A 382     3960   4928   4172   -384   -310   -178       C  
ATOM   3100  OD1 ASN A 382      15.302  11.632  -2.758  1.00 25.99           O  
ANISOU 3100  OD1 ASN A 382     2960   3779   3138   -388   -303   -198       O  
ATOM   3101  ND2 ASN A 382      14.731  13.513  -1.691  1.00 22.45           N  
ANISOU 3101  ND2 ASN A 382     2436   3447   2648   -317   -303   -144       N  
ATOM   3102  N   ILE A 383      10.344  12.962  -4.761  1.00 22.05           N  
ANISOU 3102  N   ILE A 383     2155   3740   2483   -514   -392   -254       N  
ATOM   3103  CA  ILE A 383       9.127  12.546  -5.465  1.00 21.61           C  
ANISOU 3103  CA  ILE A 383     2021   3800   2390   -599   -421   -288       C  
ATOM   3104  C   ILE A 383       9.321  12.882  -6.949  1.00 25.21           C  
ANISOU 3104  C   ILE A 383     2475   4307   2796   -570   -457   -332       C  
ATOM   3105  O   ILE A 383       8.942  12.079  -7.797  1.00 25.34           O  
ANISOU 3105  O   ILE A 383     2482   4356   2790   -662   -482   -395       O  
ATOM   3106  CB  ILE A 383       7.821  13.131  -4.831  1.00 24.80           C  
ANISOU 3106  CB  ILE A 383     2309   4351   2764   -592   -420   -244       C  
ATOM   3107  CG1 ILE A 383       7.546  12.552  -3.404  1.00 25.42           C  
ANISOU 3107  CG1 ILE A 383     2385   4395   2880   -649   -382   -205       C  
ATOM   3108  CG2 ILE A 383       6.586  12.981  -5.737  1.00 25.37           C  
ANISOU 3108  CG2 ILE A 383     2274   4587   2779   -658   -461   -274       C  
ATOM   3109  CD1 ILE A 383       7.380  10.972  -3.264  1.00 34.64           C  
ANISOU 3109  CD1 ILE A 383     3588   5485   4088   -809   -374   -229       C  
ATOM   3110  N   MET A 384       9.977  14.031  -7.256  1.00 21.32           N  
ANISOU 3110  N   MET A 384     2002   3814   2286   -451   -456   -300       N  
ATOM   3111  CA  MET A 384      10.297  14.458  -8.630  1.00 20.89           C  
ANISOU 3111  CA  MET A 384     1951   3809   2178   -411   -483   -322       C  
ATOM   3112  C   MET A 384      11.228  13.457  -9.314  1.00 26.18           C  
ANISOU 3112  C   MET A 384     2702   4388   2858   -463   -480   -392       C  
ATOM   3113  O   MET A 384      11.068  13.208 -10.502  1.00 25.55           O  
ANISOU 3113  O   MET A 384     2609   4378   2721   -490   -508   -444       O  
ATOM   3114  CB  MET A 384      10.918  15.860  -8.660  1.00 22.56           C  
ANISOU 3114  CB  MET A 384     2181   4009   2382   -283   -473   -260       C  
ATOM   3115  CG  MET A 384       9.918  16.970  -8.518  1.00 25.03           C  
ANISOU 3115  CG  MET A 384     2415   4432   2665   -209   -484   -203       C  
ATOM   3116  SD  MET A 384      10.775  18.540  -8.273  1.00 28.23           S  
ANISOU 3116  SD  MET A 384     2875   4761   3088    -73   -460   -134       S  
ATOM   3117  CE  MET A 384       9.598  19.378  -7.201  1.00 24.83           C  
ANISOU 3117  CE  MET A 384     2376   4394   2664     -3   -448    -91       C  
ATOM   3118  N   VAL A 385      12.176  12.865  -8.557  1.00 24.43           N  
ANISOU 3118  N   VAL A 385     2560   4020   2702   -469   -445   -394       N  
ATOM   3119  CA  VAL A 385      13.092  11.826  -9.047  1.00 24.67           C  
ANISOU 3119  CA  VAL A 385     2674   3947   2754   -500   -433   -459       C  
ATOM   3120  C   VAL A 385      12.261  10.565  -9.364  1.00 30.81           C  
ANISOU 3120  C   VAL A 385     3450   4723   3532   -628   -448   -535       C  
ATOM   3121  O   VAL A 385      12.470   9.944 -10.406  1.00 30.61           O  
ANISOU 3121  O   VAL A 385     3459   4692   3478   -664   -459   -619       O  
ATOM   3122  CB  VAL A 385      14.254  11.531  -8.051  1.00 27.97           C  
ANISOU 3122  CB  VAL A 385     3165   4222   3240   -460   -393   -427       C  
ATOM   3123  CG1 VAL A 385      15.114  10.362  -8.525  1.00 27.59           C  
ANISOU 3123  CG1 VAL A 385     3200   4066   3216   -477   -376   -493       C  
ATOM   3124  CG2 VAL A 385      15.122  12.765  -7.828  1.00 27.64           C  
ANISOU 3124  CG2 VAL A 385     3123   4188   3192   -356   -382   -366       C  
ATOM   3125  N   LEU A 386      11.306  10.215  -8.474  1.00 29.33           N  
ANISOU 3125  N   LEU A 386     3221   4549   3373   -703   -447   -510       N  
ATOM   3126  CA  LEU A 386      10.408   9.066  -8.633  1.00 30.00           C  
ANISOU 3126  CA  LEU A 386     3297   4636   3466   -848   -460   -571       C  
ATOM   3127  C   LEU A 386       9.547   9.216  -9.903  1.00 34.89           C  
ANISOU 3127  C   LEU A 386     3838   5418   3999   -899   -510   -635       C  
ATOM   3128  O   LEU A 386       9.488   8.276 -10.694  1.00 34.66           O  
ANISOU 3128  O   LEU A 386     3845   5366   3958   -996   -525   -732       O  
ATOM   3129  CB  LEU A 386       9.558   8.862  -7.353  1.00 30.42           C  
ANISOU 3129  CB  LEU A 386     3304   4695   3559   -911   -443   -508       C  
ATOM   3130  CG  LEU A 386       8.486   7.749  -7.329  1.00 35.87           C  
ANISOU 3130  CG  LEU A 386     3969   5399   4263  -1085   -453   -551       C  
ATOM   3131  CD1 LEU A 386       9.096   6.362  -7.522  1.00 36.39           C  
ANISOU 3131  CD1 LEU A 386     4163   5268   4394  -1164   -431   -613       C  
ATOM   3132  CD2 LEU A 386       7.722   7.771  -6.016  1.00 38.55           C  
ANISOU 3132  CD2 LEU A 386     4237   5788   4622  -1125   -432   -467       C  
ATOM   3133  N   VAL A 387       8.950  10.417 -10.125  1.00 31.80           N  
ANISOU 3133  N   VAL A 387     3347   5190   3546   -826   -535   -581       N  
ATOM   3134  CA  VAL A 387       8.139  10.768 -11.305  1.00 31.76           C  
ANISOU 3134  CA  VAL A 387     3251   5373   3444   -844   -587   -615       C  
ATOM   3135  C   VAL A 387       8.955  10.561 -12.601  1.00 37.74           C  
ANISOU 3135  C   VAL A 387     4070   6118   4151   -826   -600   -692       C  
ATOM   3136  O   VAL A 387       8.461   9.947 -13.547  1.00 37.34           O  
ANISOU 3136  O   VAL A 387     3996   6153   4040   -917   -637   -782       O  
ATOM   3137  CB  VAL A 387       7.539  12.207 -11.196  1.00 34.92           C  
ANISOU 3137  CB  VAL A 387     3547   5922   3797   -729   -602   -520       C  
ATOM   3138  CG1 VAL A 387       6.886  12.655 -12.502  1.00 34.22           C  
ANISOU 3138  CG1 VAL A 387     3372   6029   3600   -714   -656   -537       C  
ATOM   3139  CG2 VAL A 387       6.537  12.307 -10.048  1.00 34.78           C  
ANISOU 3139  CG2 VAL A 387     3448   5958   3808   -759   -591   -466       C  
ATOM   3140  N   SER A 388      10.211  11.034 -12.609  1.00 36.23           N  
ANISOU 3140  N   SER A 388     3956   5828   3981   -716   -569   -661       N  
ATOM   3141  CA  SER A 388      11.157  10.943 -13.725  1.00 37.03           C  
ANISOU 3141  CA  SER A 388     4116   5918   4035   -676   -567   -718       C  
ATOM   3142  C   SER A 388      11.417   9.522 -14.232  1.00 44.38           C  
ANISOU 3142  C   SER A 388     5124   6764   4975   -775   -563   -849       C  
ATOM   3143  O   SER A 388      11.681   9.353 -15.421  1.00 44.08           O  
ANISOU 3143  O   SER A 388     5099   6790   4860   -775   -579   -925       O  
ATOM   3144  CB  SER A 388      12.471  11.613 -13.353  1.00 39.32           C  
ANISOU 3144  CB  SER A 388     4468   6108   4365   -556   -526   -651       C  
ATOM   3145  OG  SER A 388      12.226  12.968 -13.022  1.00 47.43           O  
ANISOU 3145  OG  SER A 388     5437   7206   5379   -468   -531   -544       O  
ATOM   3146  N   THR A 389      11.353   8.512 -13.341  1.00 43.79           N  
ANISOU 3146  N   THR A 389     5105   6542   4990   -856   -539   -874       N  
ATOM   3147  CA  THR A 389      11.565   7.104 -13.700  1.00 44.84           C  
ANISOU 3147  CA  THR A 389     5332   6555   5152   -951   -528   -997       C  
ATOM   3148  C   THR A 389      10.387   6.545 -14.514  1.00 52.32           C  
ANISOU 3148  C   THR A 389     6226   7619   6033  -1098   -577  -1100       C  
ATOM   3149  O   THR A 389      10.602   5.708 -15.391  1.00 52.35           O  
ANISOU 3149  O   THR A 389     6294   7589   6008  -1156   -583  -1230       O  
ATOM   3150  CB  THR A 389      11.903   6.237 -12.471  1.00 50.42           C  
ANISOU 3150  CB  THR A 389     6124   7054   5979   -981   -482   -971       C  
ATOM   3151  OG1 THR A 389      10.749   6.095 -11.645  1.00 51.99           O  
ANISOU 3151  OG1 THR A 389     6259   7286   6210  -1079   -494   -920       O  
ATOM   3152  CG2 THR A 389      13.078   6.773 -11.667  1.00 45.47           C  
ANISOU 3152  CG2 THR A 389     5541   6332   5404   -840   -439   -879       C  
ATOM   3153  N   PHE A 390       9.154   7.010 -14.227  1.00 51.33           N  
ANISOU 3153  N   PHE A 390     5980   7641   5880  -1157   -614  -1048       N  
ATOM   3154  CA  PHE A 390       7.944   6.581 -14.929  1.00 52.27           C  
ANISOU 3154  CA  PHE A 390     6019   7911   5929  -1304   -668  -1132       C  
ATOM   3155  C   PHE A 390       7.797   7.281 -16.276  1.00 58.74           C  
ANISOU 3155  C   PHE A 390     6768   8941   6611  -1254   -717  -1166       C  
ATOM   3156  O   PHE A 390       7.536   6.614 -17.280  1.00 58.72           O  
ANISOU 3156  O   PHE A 390     6775   8995   6539  -1350   -749  -1297       O  
ATOM   3157  CB  PHE A 390       6.699   6.765 -14.054  1.00 54.19           C  
ANISOU 3157  CB  PHE A 390     6146   8251   6191  -1380   -684  -1055       C  
ATOM   3158  CG  PHE A 390       6.593   5.760 -12.932  1.00 56.04           C  
ANISOU 3158  CG  PHE A 390     6446   8306   6541  -1489   -644  -1049       C  
ATOM   3159  CD1 PHE A 390       5.922   4.556 -13.115  1.00 59.60           C  
ANISOU 3159  CD1 PHE A 390     6916   8719   7009  -1688   -658  -1150       C  
ATOM   3160  CD2 PHE A 390       7.143   6.028 -11.682  1.00 58.24           C  
ANISOU 3160  CD2 PHE A 390     6767   8454   6906  -1401   -593   -938       C  
ATOM   3161  CE1 PHE A 390       5.808   3.632 -12.069  1.00 60.72           C  
ANISOU 3161  CE1 PHE A 390     7124   8686   7260  -1793   -617  -1128       C  
ATOM   3162  CE2 PHE A 390       7.033   5.103 -10.639  1.00 61.29           C  
ANISOU 3162  CE2 PHE A 390     7212   8685   7389  -1498   -555   -916       C  
ATOM   3163  CZ  PHE A 390       6.365   3.911 -10.838  1.00 59.52           C  
ANISOU 3163  CZ  PHE A 390     7012   8415   7188  -1692   -565  -1004       C  
ATOM   3164  N   CYS A 391       7.979   8.614 -16.308  1.00 57.05           N  
ANISOU 3164  N   CYS A 391     6488   8833   6353  -1104   -721  -1049       N  
ATOM   3165  CA  CYS A 391       7.918   9.375 -17.553  1.00 57.93           C  
ANISOU 3165  CA  CYS A 391     6537   9139   6333  -1035   -762  -1050       C  
ATOM   3166  C   CYS A 391       9.061  10.382 -17.666  1.00 62.58           C  
ANISOU 3166  C   CYS A 391     7176   9680   6922   -864   -726   -963       C  
ATOM   3167  O   CYS A 391       9.199  11.287 -16.840  1.00 62.01           O  
ANISOU 3167  O   CYS A 391     7096   9553   6910   -769   -699   -843       O  
ATOM   3168  CB  CYS A 391       6.550  10.007 -17.784  1.00 58.72           C  
ANISOU 3168  CB  CYS A 391     6476   9484   6351  -1049   -820   -993       C  
ATOM   3169  SG  CYS A 391       5.982  11.096 -16.459  1.00 62.76           S  
ANISOU 3169  SG  CYS A 391     6910  10003   6933   -948   -800   -823       S  
ATOM   3170  N   LYS A 392       9.899  10.160 -18.695  1.00 60.15           N  
ANISOU 3170  N   LYS A 392     6921   9392   6543   -837   -723  -1034       N  
ATOM   3171  CA  LYS A 392      11.148  10.836 -19.058  1.00 60.43           C  
ANISOU 3171  CA  LYS A 392     7011   9387   6563   -703   -685   -980       C  
ATOM   3172  C   LYS A 392      11.271  12.330 -18.688  1.00 63.87           C  
ANISOU 3172  C   LYS A 392     7397   9866   7003   -572   -678   -812       C  
ATOM   3173  O   LYS A 392      12.084  12.653 -17.821  1.00 63.51           O  
ANISOU 3173  O   LYS A 392     7408   9672   7051   -508   -631   -746       O  
ATOM   3174  CB  LYS A 392      11.455  10.642 -20.558  1.00 63.48           C  
ANISOU 3174  CB  LYS A 392     7405   9898   6816   -703   -703  -1072       C  
ATOM   3175  CG  LYS A 392      12.209   9.346 -20.868  1.00 82.23           C  
ANISOU 3175  CG  LYS A 392     9894  12134   9216   -755   -668  -1225       C  
ATOM   3176  CD  LYS A 392      13.696   9.406 -20.458  1.00 94.15           C  
ANISOU 3176  CD  LYS A 392    11496  13467  10810   -650   -597  -1182       C  
ATOM   3177  CE  LYS A 392      14.216   8.097 -19.905  1.00104.87           C  
ANISOU 3177  CE  LYS A 392    12966  14612  12268   -699   -556  -1290       C  
ATOM   3178  NZ  LYS A 392      13.640   7.779 -18.568  1.00112.51           N  
ANISOU 3178  NZ  LYS A 392    13940  15449  13358   -767   -555  -1250       N  
ATOM   3179  N   ASP A 393      10.517  13.228 -19.357  1.00 59.86           N  
ANISOU 3179  N   ASP A 393     6793   9557   6395   -529   -722   -745       N  
ATOM   3180  CA  ASP A 393      10.626  14.674 -19.138  1.00 59.25           C  
ANISOU 3180  CA  ASP A 393     6686   9506   6322   -397   -712   -588       C  
ATOM   3181  C   ASP A 393       9.343  15.322 -18.574  1.00 60.76           C  
ANISOU 3181  C   ASP A 393     6776   9789   6522   -375   -743   -503       C  
ATOM   3182  O   ASP A 393       9.019  16.464 -18.918  1.00 59.97           O  
ANISOU 3182  O   ASP A 393     6622   9793   6371   -271   -759   -391       O  
ATOM   3183  CB  ASP A 393      11.096  15.377 -20.431  1.00 61.56           C  
ANISOU 3183  CB  ASP A 393     6968   9929   6493   -322   -721   -545       C  
ATOM   3184  CG  ASP A 393      12.389  14.833 -21.014  1.00 74.41           C  
ANISOU 3184  CG  ASP A 393     8686  11480   8106   -322   -680   -615       C  
ATOM   3185  OD1 ASP A 393      13.460  15.070 -20.411  1.00 75.02           O  
ANISOU 3185  OD1 ASP A 393     8832  11403   8270   -271   -626   -567       O  
ATOM   3186  OD2 ASP A 393      12.329  14.176 -22.079  1.00 81.76           O  
ANISOU 3186  OD2 ASP A 393     9614  12517   8936   -373   -700   -721       O  
ATOM   3187  N   CYS A 394       8.642  14.607 -17.675  1.00 56.00           N  
ANISOU 3187  N   CYS A 394     6150   9140   5988   -463   -746   -548       N  
ATOM   3188  CA  CYS A 394       7.431  15.108 -17.025  1.00 55.44           C  
ANISOU 3188  CA  CYS A 394     5976   9159   5930   -446   -767   -478       C  
ATOM   3189  C   CYS A 394       7.736  16.249 -16.061  1.00 52.76           C  
ANISOU 3189  C   CYS A 394     5660   8721   5665   -316   -727   -356       C  
ATOM   3190  O   CYS A 394       6.894  17.132 -15.891  1.00 52.67           O  
ANISOU 3190  O   CYS A 394     5565   8816   5631   -235   -743   -270       O  
ATOM   3191  CB  CYS A 394       6.683  13.983 -16.320  1.00 57.32           C  
ANISOU 3191  CB  CYS A 394     6187   9374   6219   -589   -773   -558       C  
ATOM   3192  SG  CYS A 394       5.781  12.873 -17.430  1.00 62.45           S  
ANISOU 3192  SG  CYS A 394     6763  10200   6764   -756   -838   -694       S  
ATOM   3193  N   VAL A 395       8.920  16.221 -15.416  1.00 43.50           N  
ANISOU 3193  N   VAL A 395     4598   7348   4581   -297   -674   -353       N  
ATOM   3194  CA  VAL A 395       9.322  17.249 -14.453  1.00 40.76           C  
ANISOU 3194  CA  VAL A 395     4286   6894   4308   -193   -635   -257       C  
ATOM   3195  C   VAL A 395      10.007  18.428 -15.172  1.00 40.91           C  
ANISOU 3195  C   VAL A 395     4337   6919   4289    -80   -628   -172       C  
ATOM   3196  O   VAL A 395      11.097  18.255 -15.728  1.00 39.69           O  
ANISOU 3196  O   VAL A 395     4250   6707   4123    -86   -610   -194       O  
ATOM   3197  CB  VAL A 395      10.151  16.707 -13.249  1.00 43.34           C  
ANISOU 3197  CB  VAL A 395     4699   7026   4744   -229   -587   -285       C  
ATOM   3198  CG1 VAL A 395      10.308  17.775 -12.169  1.00 42.86           C  
ANISOU 3198  CG1 VAL A 395     4655   6886   4745   -136   -556   -200       C  
ATOM   3199  CG2 VAL A 395       9.528  15.443 -12.661  1.00 42.70           C  
ANISOU 3199  CG2 VAL A 395     4599   6929   4696   -353   -592   -361       C  
ATOM   3200  N   PRO A 396       9.380  19.629 -15.173  1.00 35.41           N  
ANISOU 3200  N   PRO A 396     3591   6292   3571     28   -637    -71       N  
ATOM   3201  CA  PRO A 396      10.004  20.783 -15.839  1.00 34.56           C  
ANISOU 3201  CA  PRO A 396     3524   6173   3434    131   -626     25       C  
ATOM   3202  C   PRO A 396      11.142  21.367 -15.008  1.00 37.38           C  
ANISOU 3202  C   PRO A 396     3983   6333   3887    164   -572     60       C  
ATOM   3203  O   PRO A 396      11.156  21.194 -13.788  1.00 36.89           O  
ANISOU 3203  O   PRO A 396     3942   6168   3908    144   -549     33       O  
ATOM   3204  CB  PRO A 396       8.845  21.787 -15.981  1.00 36.15           C  
ANISOU 3204  CB  PRO A 396     3643   6497   3594    239   -652    121       C  
ATOM   3205  CG  PRO A 396       7.605  21.072 -15.499  1.00 40.33           C  
ANISOU 3205  CG  PRO A 396     4070   7135   4117    183   -681     64       C  
ATOM   3206  CD  PRO A 396       8.085  20.007 -14.578  1.00 36.20           C  
ANISOU 3206  CD  PRO A 396     3599   6481   3674     68   -654    -33       C  
ATOM   3207  N   GLU A 397      12.082  22.074 -15.670  1.00 33.37           N  
ANISOU 3207  N   GLU A 397     3531   5786   3360    207   -554    122       N  
ATOM   3208  CA  GLU A 397      13.247  22.726 -15.056  1.00 33.06           C  
ANISOU 3208  CA  GLU A 397     3583   5579   3401    226   -506    160       C  
ATOM   3209  C   GLU A 397      12.885  23.621 -13.855  1.00 34.24           C  
ANISOU 3209  C   GLU A 397     3752   5626   3630    289   -487    203       C  
ATOM   3210  O   GLU A 397      13.597  23.578 -12.858  1.00 34.23           O  
ANISOU 3210  O   GLU A 397     3804   5495   3706    258   -457    172       O  
ATOM   3211  CB  GLU A 397      14.037  23.525 -16.108  1.00 34.94           C  
ANISOU 3211  CB  GLU A 397     3858   5827   3589    266   -493    245       C  
ATOM   3212  CG  GLU A 397      15.497  23.764 -15.738  1.00 52.80           C  
ANISOU 3212  CG  GLU A 397     6201   7948   5912    235   -447    252       C  
ATOM   3213  CD  GLU A 397      16.257  24.777 -16.581  1.00 92.61           C  
ANISOU 3213  CD  GLU A 397    11283  12983  10923    269   -425    358       C  
ATOM   3214  OE1 GLU A 397      15.883  24.995 -17.758  1.00 94.96           O  
ANISOU 3214  OE1 GLU A 397    11546  13410  11124    305   -446    414       O  
ATOM   3215  OE2 GLU A 397      17.240  25.352 -16.060  1.00 96.08           O  
ANISOU 3215  OE2 GLU A 397    11785  13294  11429    254   -388    389       O  
ATOM   3216  N   THR A 398      11.782  24.400 -13.942  1.00 28.71           N  
ANISOU 3216  N   THR A 398     3004   4996   2906    381   -504    270       N  
ATOM   3217  CA  THR A 398      11.299  25.295 -12.875  1.00 28.22           C  
ANISOU 3217  CA  THR A 398     2959   4854   2911    462   -484    306       C  
ATOM   3218  C   THR A 398      11.007  24.511 -11.588  1.00 31.33           C  
ANISOU 3218  C   THR A 398     3331   5216   3358    405   -475    219       C  
ATOM   3219  O   THR A 398      11.353  24.967 -10.498  1.00 30.97           O  
ANISOU 3219  O   THR A 398     3340   5046   3382    423   -442    211       O  
ATOM   3220  CB  THR A 398      10.065  26.092 -13.355  1.00 35.36           C  
ANISOU 3220  CB  THR A 398     3797   5876   3764    584   -508    389       C  
ATOM   3221  OG1 THR A 398      10.395  26.779 -14.560  1.00 39.38           O  
ANISOU 3221  OG1 THR A 398     4328   6417   4216    633   -516    482       O  
ATOM   3222  CG2 THR A 398       9.556  27.097 -12.320  1.00 30.97           C  
ANISOU 3222  CG2 THR A 398     3265   5230   3273    693   -479    425       C  
ATOM   3223  N   LEU A 399      10.392  23.328 -11.727  1.00 27.37           N  
ANISOU 3223  N   LEU A 399     2754   4827   2818    329   -503    153       N  
ATOM   3224  CA  LEU A 399      10.050  22.480 -10.598  1.00 27.14           C  
ANISOU 3224  CA  LEU A 399     2700   4782   2832    262   -494     83       C  
ATOM   3225  C   LEU A 399      11.254  21.863  -9.924  1.00 30.81           C  
ANISOU 3225  C   LEU A 399     3245   5106   3356    185   -465     31       C  
ATOM   3226  O   LEU A 399      11.263  21.798  -8.693  1.00 30.89           O  
ANISOU 3226  O   LEU A 399     3269   5049   3419    176   -441     11       O  
ATOM   3227  CB  LEU A 399       9.017  21.434 -10.987  1.00 27.24           C  
ANISOU 3227  CB  LEU A 399     2612   4949   2789    190   -531     35       C  
ATOM   3228  CG  LEU A 399       7.632  21.898 -10.613  1.00 31.83           C  
ANISOU 3228  CG  LEU A 399     3093   5651   3350    255   -542     67       C  
ATOM   3229  CD1 LEU A 399       6.760  22.096 -11.831  1.00 31.94           C  
ANISOU 3229  CD1 LEU A 399     3012   5851   3271    296   -589    106       C  
ATOM   3230  CD2 LEU A 399       7.056  21.057  -9.509  1.00 33.45           C  
ANISOU 3230  CD2 LEU A 399     3252   5873   3586    170   -532     11       C  
ATOM   3231  N   TRP A 400      12.294  21.480 -10.704  1.00 27.00           N  
ANISOU 3231  N   TRP A 400     2811   4589   2861    141   -465     15       N  
ATOM   3232  CA  TRP A 400      13.546  20.949 -10.155  1.00 26.89           C  
ANISOU 3232  CA  TRP A 400     2865   4453   2897     85   -438    -24       C  
ATOM   3233  C   TRP A 400      14.202  22.014  -9.292  1.00 29.94           C  
ANISOU 3233  C   TRP A 400     3310   4725   3339    134   -407     17       C  
ATOM   3234  O   TRP A 400      14.722  21.697  -8.232  1.00 30.18           O  
ANISOU 3234  O   TRP A 400     3371   4677   3419    102   -388    -14       O  
ATOM   3235  CB  TRP A 400      14.519  20.530 -11.269  1.00 25.84           C  
ANISOU 3235  CB  TRP A 400     2761   4327   2728     52   -439    -42       C  
ATOM   3236  CG  TRP A 400      14.176  19.244 -11.955  1.00 26.90           C  
ANISOU 3236  CG  TRP A 400     2864   4537   2819    -18   -462   -116       C  
ATOM   3237  CD1 TRP A 400      13.819  19.085 -13.263  1.00 29.83           C  
ANISOU 3237  CD1 TRP A 400     3199   5028   3107    -24   -490   -128       C  
ATOM   3238  CD2 TRP A 400      14.198  17.930 -11.381  1.00 26.74           C  
ANISOU 3238  CD2 TRP A 400     2854   4471   2836    -96   -457   -193       C  
ATOM   3239  NE1 TRP A 400      13.601  17.755 -13.536  1.00 29.44           N  
ANISOU 3239  NE1 TRP A 400     3139   5005   3040   -108   -504   -222       N  
ATOM   3240  CE2 TRP A 400      13.837  17.021 -12.402  1.00 30.88           C  
ANISOU 3240  CE2 TRP A 400     3355   5076   3302   -153   -482   -259       C  
ATOM   3241  CE3 TRP A 400      14.475  17.429 -10.096  1.00 27.93           C  
ANISOU 3241  CE3 TRP A 400     3034   4519   3058   -124   -434   -208       C  
ATOM   3242  CZ2 TRP A 400      13.737  15.641 -12.177  1.00 30.03           C  
ANISOU 3242  CZ2 TRP A 400     3263   4927   3219   -240   -482   -343       C  
ATOM   3243  CZ3 TRP A 400      14.382  16.063  -9.875  1.00 29.27           C  
ANISOU 3243  CZ3 TRP A 400     3215   4657   3250   -202   -433   -274       C  
ATOM   3244  CH2 TRP A 400      14.011  15.185 -10.905  1.00 29.94           C  
ANISOU 3244  CH2 TRP A 400     3288   4801   3289   -261   -455   -342       C  
ATOM   3245  N   GLU A 401      14.149  23.279  -9.746  1.00 26.68           N  
ANISOU 3245  N   GLU A 401     2916   4305   2916    210   -404     87       N  
ATOM   3246  CA  GLU A 401      14.705  24.453  -9.067  1.00 26.84           C  
ANISOU 3246  CA  GLU A 401     3003   4207   2988    254   -376    123       C  
ATOM   3247  C   GLU A 401      14.024  24.714  -7.728  1.00 30.41           C  
ANISOU 3247  C   GLU A 401     3448   4626   3479    286   -363     99       C  
ATOM   3248  O   GLU A 401      14.709  24.999  -6.746  1.00 30.09           O  
ANISOU 3248  O   GLU A 401     3459   4489   3485    268   -341     75       O  
ATOM   3249  CB  GLU A 401      14.629  25.696  -9.965  1.00 28.05           C  
ANISOU 3249  CB  GLU A 401     3181   4354   3121    330   -375    212       C  
ATOM   3250  CG  GLU A 401      15.532  25.602 -11.181  1.00 38.80           C  
ANISOU 3250  CG  GLU A 401     4560   5740   4441    294   -376    245       C  
ATOM   3251  CD  GLU A 401      15.352  26.658 -12.253  1.00 61.54           C  
ANISOU 3251  CD  GLU A 401     7455   8646   7283    365   -379    349       C  
ATOM   3252  OE1 GLU A 401      14.462  27.530 -12.112  1.00 56.60           O  
ANISOU 3252  OE1 GLU A 401     6827   8014   6664    458   -382    402       O  
ATOM   3253  OE2 GLU A 401      16.119  26.611 -13.241  1.00 59.40           O  
ANISOU 3253  OE2 GLU A 401     7196   8404   6970    333   -375    383       O  
ATOM   3254  N   LEU A 402      12.685  24.597  -7.691  1.00 26.21           N  
ANISOU 3254  N   LEU A 402     2844   4194   2919    332   -378    102       N  
ATOM   3255  CA  LEU A 402      11.888  24.782  -6.479  1.00 25.92           C  
ANISOU 3255  CA  LEU A 402     2783   4161   2905    371   -362     79       C  
ATOM   3256  C   LEU A 402      12.103  23.611  -5.511  1.00 28.92           C  
ANISOU 3256  C   LEU A 402     3148   4539   3302    278   -356     16       C  
ATOM   3257  O   LEU A 402      12.183  23.824  -4.301  1.00 28.77           O  
ANISOU 3257  O   LEU A 402     3150   4470   3310    287   -332     -8       O  
ATOM   3258  CB  LEU A 402      10.401  24.992  -6.819  1.00 26.06           C  
ANISOU 3258  CB  LEU A 402     2709   4314   2879    448   -379    108       C  
ATOM   3259  CG  LEU A 402      10.057  26.270  -7.616  1.00 30.92           C  
ANISOU 3259  CG  LEU A 402     3338   4932   3478    572   -382    188       C  
ATOM   3260  CD1 LEU A 402       8.763  26.110  -8.361  1.00 31.10           C  
ANISOU 3260  CD1 LEU A 402     3247   5135   3435    621   -415    221       C  
ATOM   3261  CD2 LEU A 402       9.996  27.499  -6.721  1.00 33.67           C  
ANISOU 3261  CD2 LEU A 402     3747   5171   3874    675   -345    199       C  
ATOM   3262  N   GLY A 403      12.261  22.406  -6.058  1.00 25.15           N  
ANISOU 3262  N   GLY A 403     2644   4107   2806    193   -375    -10       N  
ATOM   3263  CA  GLY A 403      12.561  21.202  -5.290  1.00 25.02           C  
ANISOU 3263  CA  GLY A 403     2627   4071   2810    105   -368    -56       C  
ATOM   3264  C   GLY A 403      13.918  21.286  -4.612  1.00 28.80           C  
ANISOU 3264  C   GLY A 403     3180   4433   3328     84   -347    -67       C  
ATOM   3265  O   GLY A 403      14.074  20.833  -3.474  1.00 27.89           O  
ANISOU 3265  O   GLY A 403     3071   4293   3233     53   -333    -87       O  
ATOM   3266  N   TYR A 404      14.905  21.899  -5.304  1.00 25.54           N  
ANISOU 3266  N   TYR A 404     2818   3965   2920     99   -347    -47       N  
ATOM   3267  CA  TYR A 404      16.263  22.128  -4.801  1.00 25.23           C  
ANISOU 3267  CA  TYR A 404     2838   3835   2912     76   -330    -53       C  
ATOM   3268  C   TYR A 404      16.259  23.178  -3.693  1.00 29.53           C  
ANISOU 3268  C   TYR A 404     3415   4325   3481    114   -312    -54       C  
ATOM   3269  O   TYR A 404      16.991  23.022  -2.714  1.00 28.65           O  
ANISOU 3269  O   TYR A 404     3327   4173   3388     82   -302    -78       O  
ATOM   3270  CB  TYR A 404      17.211  22.565  -5.935  1.00 26.07           C  
ANISOU 3270  CB  TYR A 404     2977   3919   3010     74   -331    -25       C  
ATOM   3271  CG  TYR A 404      17.600  21.481  -6.924  1.00 27.67           C  
ANISOU 3271  CG  TYR A 404     3162   4165   3185     33   -341    -43       C  
ATOM   3272  CD1 TYR A 404      17.568  20.136  -6.567  1.00 29.59           C  
ANISOU 3272  CD1 TYR A 404     3390   4418   3436    -13   -344    -88       C  
ATOM   3273  CD2 TYR A 404      18.093  21.806  -8.183  1.00 28.35           C  
ANISOU 3273  CD2 TYR A 404     3257   4275   3239     40   -343    -14       C  
ATOM   3274  CE1 TYR A 404      17.974  19.142  -7.452  1.00 29.78           C  
ANISOU 3274  CE1 TYR A 404     3412   4463   3439    -44   -348   -117       C  
ATOM   3275  CE2 TYR A 404      18.493  20.820  -9.081  1.00 29.19           C  
ANISOU 3275  CE2 TYR A 404     3351   4426   3313      9   -347    -44       C  
ATOM   3276  CZ  TYR A 404      18.433  19.488  -8.711  1.00 37.48           C  
ANISOU 3276  CZ  TYR A 404     4393   5474   4376    -30   -350   -103       C  
ATOM   3277  OH  TYR A 404      18.846  18.508  -9.582  1.00 40.61           O  
ANISOU 3277  OH  TYR A 404     4789   5897   4743    -54   -350   -145       O  
ATOM   3278  N   TRP A 405      15.453  24.253  -3.857  1.00 27.09           N  
ANISOU 3278  N   TRP A 405     3108   4016   3167    189   -309    -30       N  
ATOM   3279  CA  TRP A 405      15.311  25.326  -2.870  1.00 27.84           C  
ANISOU 3279  CA  TRP A 405     3243   4050   3284    239   -288    -44       C  
ATOM   3280  C   TRP A 405      14.669  24.815  -1.580  1.00 32.48           C  
ANISOU 3280  C   TRP A 405     3793   4684   3862    238   -277    -85       C  
ATOM   3281  O   TRP A 405      15.186  25.101  -0.503  1.00 31.75           O  
ANISOU 3281  O   TRP A 405     3737   4545   3781    226   -262   -120       O  
ATOM   3282  CB  TRP A 405      14.556  26.544  -3.441  1.00 27.08           C  
ANISOU 3282  CB  TRP A 405     3163   3938   3189    338   -282     -2       C  
ATOM   3283  CG  TRP A 405      15.435  27.523  -4.168  1.00 28.38           C  
ANISOU 3283  CG  TRP A 405     3403   4004   3377    340   -277     39       C  
ATOM   3284  CD1 TRP A 405      15.398  27.821  -5.498  1.00 31.47           C  
ANISOU 3284  CD1 TRP A 405     3794   4412   3751    365   -288    106       C  
ATOM   3285  CD2 TRP A 405      16.481  28.329  -3.605  1.00 28.34           C  
ANISOU 3285  CD2 TRP A 405     3480   3876   3411    305   -259     19       C  
ATOM   3286  NE1 TRP A 405      16.362  28.756  -5.801  1.00 31.21           N  
ANISOU 3286  NE1 TRP A 405     3841   4268   3748    347   -273    140       N  
ATOM   3287  CE2 TRP A 405      17.050  29.075  -4.660  1.00 32.54           C  
ANISOU 3287  CE2 TRP A 405     4062   4348   3956    303   -256     83       C  
ATOM   3288  CE3 TRP A 405      17.009  28.479  -2.310  1.00 29.89           C  
ANISOU 3288  CE3 TRP A 405     3711   4019   3627    266   -246    -46       C  
ATOM   3289  CZ2 TRP A 405      18.109  29.970  -4.460  1.00 31.84           C  
ANISOU 3289  CZ2 TRP A 405     4055   4137   3906    253   -240     83       C  
ATOM   3290  CZ3 TRP A 405      18.062  29.361  -2.116  1.00 31.43           C  
ANISOU 3290  CZ3 TRP A 405     3985   4103   3856    218   -235    -57       C  
ATOM   3291  CH2 TRP A 405      18.600  30.092  -3.182  1.00 31.94           C  
ANISOU 3291  CH2 TRP A 405     4096   4098   3940    206   -231      7       C  
ATOM   3292  N   LEU A 406      13.575  24.023  -1.695  1.00 30.22           N  
ANISOU 3292  N   LEU A 406     3430   4502   3550    240   -285    -79       N  
ATOM   3293  CA  LEU A 406      12.863  23.380  -0.580  1.00 30.06           C  
ANISOU 3293  CA  LEU A 406     3360   4549   3514    226   -271   -103       C  
ATOM   3294  C   LEU A 406      13.808  22.453   0.196  1.00 34.42           C  
ANISOU 3294  C   LEU A 406     3932   5071   4074    143   -269   -122       C  
ATOM   3295  O   LEU A 406      13.775  22.419   1.423  1.00 33.89           O  
ANISOU 3295  O   LEU A 406     3863   5017   3997    140   -251   -142       O  
ATOM   3296  CB  LEU A 406      11.682  22.570  -1.135  1.00 30.31           C  
ANISOU 3296  CB  LEU A 406     3300   4698   3517    213   -286    -86       C  
ATOM   3297  CG  LEU A 406      10.242  23.066  -0.902  1.00 35.71           C  
ANISOU 3297  CG  LEU A 406     3910   5485   4173    291   -274    -78       C  
ATOM   3298  CD1 LEU A 406      10.169  24.524  -0.408  1.00 36.32           C  
ANISOU 3298  CD1 LEU A 406     4034   5507   4259    408   -249    -84       C  
ATOM   3299  CD2 LEU A 406       9.397  22.864  -2.146  1.00 37.06           C  
ANISOU 3299  CD2 LEU A 406     4005   5760   4315    299   -302    -49       C  
ATOM   3300  N   CYS A 407      14.664  21.729  -0.531  1.00 32.22           N  
ANISOU 3300  N   CYS A 407     3672   4760   3809     85   -286   -114       N  
ATOM   3301  CA  CYS A 407      15.686  20.822  -0.019  1.00 33.22           C  
ANISOU 3301  CA  CYS A 407     3820   4855   3947     22   -286   -120       C  
ATOM   3302  C   CYS A 407      16.687  21.592   0.875  1.00 35.17           C  
ANISOU 3302  C   CYS A 407     4115   5049   4201     30   -277   -137       C  
ATOM   3303  O   CYS A 407      17.015  21.131   1.972  1.00 34.54           O  
ANISOU 3303  O   CYS A 407     4032   4980   4110      5   -270   -144       O  
ATOM   3304  CB  CYS A 407      16.386  20.154  -1.196  1.00 35.01           C  
ANISOU 3304  CB  CYS A 407     4059   5058   4185    -13   -301   -113       C  
ATOM   3305  SG  CYS A 407      17.397  18.731  -0.751  1.00 39.85           S  
ANISOU 3305  SG  CYS A 407     4688   5639   4814    -70   -299   -114       S  
ATOM   3306  N   TYR A 408      17.121  22.789   0.416  1.00 29.79           N  
ANISOU 3306  N   TYR A 408     3474   4312   3531     60   -277   -141       N  
ATOM   3307  CA  TYR A 408      18.039  23.683   1.128  1.00 28.29           C  
ANISOU 3307  CA  TYR A 408     3334   4066   3348     52   -271   -167       C  
ATOM   3308  C   TYR A 408      17.423  24.268   2.397  1.00 30.07           C  
ANISOU 3308  C   TYR A 408     3565   4305   3554     87   -254   -207       C  
ATOM   3309  O   TYR A 408      18.160  24.625   3.318  1.00 28.76           O  
ANISOU 3309  O   TYR A 408     3427   4120   3379     61   -252   -243       O  
ATOM   3310  CB  TYR A 408      18.492  24.832   0.215  1.00 28.75           C  
ANISOU 3310  CB  TYR A 408     3441   4051   3430     65   -271   -154       C  
ATOM   3311  CG  TYR A 408      19.479  24.457  -0.867  1.00 29.46           C  
ANISOU 3311  CG  TYR A 408     3532   4132   3529     22   -282   -122       C  
ATOM   3312  CD1 TYR A 408      20.409  23.436  -0.670  1.00 31.19           C  
ANISOU 3312  CD1 TYR A 408     3729   4379   3743    -28   -290   -124       C  
ATOM   3313  CD2 TYR A 408      19.533  25.165  -2.063  1.00 30.07           C  
ANISOU 3313  CD2 TYR A 408     3633   4176   3615     39   -282    -85       C  
ATOM   3314  CE1 TYR A 408      21.337  23.105  -1.654  1.00 32.15           C  
ANISOU 3314  CE1 TYR A 408     3845   4502   3867    -56   -294   -101       C  
ATOM   3315  CE2 TYR A 408      20.462  24.848  -3.051  1.00 30.78           C  
ANISOU 3315  CE2 TYR A 408     3718   4274   3702      1   -286    -56       C  
ATOM   3316  CZ  TYR A 408      21.358  23.814  -2.844  1.00 36.18           C  
ANISOU 3316  CZ  TYR A 408     4375   4992   4380    -45   -291    -70       C  
ATOM   3317  OH  TYR A 408      22.271  23.506  -3.813  1.00 35.19           O  
ANISOU 3317  OH  TYR A 408     4238   4885   4246    -71   -289    -47       O  
ATOM   3318  N   VAL A 409      16.074  24.371   2.442  1.00 25.60           N  
ANISOU 3318  N   VAL A 409     2965   3787   2975    146   -241   -205       N  
ATOM   3319  CA  VAL A 409      15.314  24.898   3.585  1.00 24.34           C  
ANISOU 3319  CA  VAL A 409     2800   3660   2788    197   -217   -245       C  
ATOM   3320  C   VAL A 409      15.517  24.016   4.846  1.00 26.83           C  
ANISOU 3320  C   VAL A 409     3087   4043   3066    150   -212   -258       C  
ATOM   3321  O   VAL A 409      15.374  24.535   5.953  1.00 25.85           O  
ANISOU 3321  O   VAL A 409     2974   3939   2908    174   -193   -305       O  
ATOM   3322  CB  VAL A 409      13.824  25.165   3.223  1.00 27.51           C  
ANISOU 3322  CB  VAL A 409     3152   4122   3179    279   -203   -230       C  
ATOM   3323  CG1 VAL A 409      12.962  25.446   4.458  1.00 27.01           C  
ANISOU 3323  CG1 VAL A 409     3063   4124   3077    336   -171   -270       C  
ATOM   3324  CG2 VAL A 409      13.716  26.322   2.229  1.00 27.10           C  
ANISOU 3324  CG2 VAL A 409     3142   3996   3157    348   -205   -213       C  
ATOM   3325  N   ASN A 410      15.936  22.729   4.691  1.00 23.00           N  
ANISOU 3325  N   ASN A 410     2573   3585   2583     86   -226   -218       N  
ATOM   3326  CA  ASN A 410      16.234  21.862   5.844  1.00 23.35           C  
ANISOU 3326  CA  ASN A 410     2596   3684   2593     44   -222   -209       C  
ATOM   3327  C   ASN A 410      17.316  22.498   6.724  1.00 27.66           C  
ANISOU 3327  C   ASN A 410     3183   4211   3116     31   -228   -251       C  
ATOM   3328  O   ASN A 410      17.180  22.495   7.946  1.00 27.77           O  
ANISOU 3328  O   ASN A 410     3184   4289   3078     34   -216   -271       O  
ATOM   3329  CB  ASN A 410      16.669  20.453   5.424  1.00 23.66           C  
ANISOU 3329  CB  ASN A 410     2617   3721   2651    -11   -237   -156       C  
ATOM   3330  CG  ASN A 410      16.694  19.480   6.583  1.00 42.37           C  
ANISOU 3330  CG  ASN A 410     4963   6148   4987    -42   -227   -123       C  
ATOM   3331  OD1 ASN A 410      15.687  19.248   7.257  1.00 35.97           O  
ANISOU 3331  OD1 ASN A 410     4113   5408   4143    -38   -205   -111       O  
ATOM   3332  ND2 ASN A 410      17.848  18.896   6.851  1.00 35.29           N  
ANISOU 3332  ND2 ASN A 410     4084   5232   4092    -69   -241    -99       N  
ATOM   3333  N   ALA A 411      18.348  23.096   6.087  1.00 23.73           N  
ANISOU 3333  N   ALA A 411     2729   3637   2650     12   -246   -266       N  
ATOM   3334  CA  ALA A 411      19.460  23.800   6.732  1.00 23.32           C  
ANISOU 3334  CA  ALA A 411     2713   3566   2583    -20   -257   -311       C  
ATOM   3335  C   ALA A 411      19.002  25.018   7.545  1.00 27.34           C  
ANISOU 3335  C   ALA A 411     3260   4061   3066     14   -239   -389       C  
ATOM   3336  O   ALA A 411      19.643  25.360   8.541  1.00 27.11           O  
ANISOU 3336  O   ALA A 411     3247   4057   2996    -18   -246   -440       O  
ATOM   3337  CB  ALA A 411      20.475  24.225   5.683  1.00 23.92           C  
ANISOU 3337  CB  ALA A 411     2818   3566   2703    -55   -275   -302       C  
ATOM   3338  N   THR A 412      17.902  25.662   7.118  1.00 23.95           N  
ANISOU 3338  N   THR A 412     2845   3599   2656     83   -217   -400       N  
ATOM   3339  CA  THR A 412      17.309  26.845   7.749  1.00 24.08           C  
ANISOU 3339  CA  THR A 412     2905   3587   2657    143   -191   -475       C  
ATOM   3340  C   THR A 412      16.449  26.482   8.963  1.00 29.83           C  
ANISOU 3340  C   THR A 412     3587   4431   3316    181   -166   -501       C  
ATOM   3341  O   THR A 412      16.527  27.172   9.983  1.00 29.58           O  
ANISOU 3341  O   THR A 412     3588   4411   3240    194   -152   -582       O  
ATOM   3342  CB  THR A 412      16.456  27.635   6.722  1.00 30.53           C  
ANISOU 3342  CB  THR A 412     3749   4327   3523    223   -175   -461       C  
ATOM   3343  OG1 THR A 412      17.109  27.666   5.454  1.00 30.08           O  
ANISOU 3343  OG1 THR A 412     3711   4198   3518    186   -197   -406       O  
ATOM   3344  CG2 THR A 412      16.136  29.054   7.178  1.00 29.12           C  
ANISOU 3344  CG2 THR A 412     3649   4063   3351    287   -149   -541       C  
ATOM   3345  N   ILE A 413      15.602  25.439   8.846  1.00 27.53           N  
ANISOU 3345  N   ILE A 413     3219   4229   3010    193   -158   -436       N  
ATOM   3346  CA  ILE A 413      14.671  25.080   9.915  1.00 28.05           C  
ANISOU 3346  CA  ILE A 413     3229   4418   3009    226   -127   -443       C  
ATOM   3347  C   ILE A 413      15.281  24.126  10.962  1.00 33.16           C  
ANISOU 3347  C   ILE A 413     3848   5155   3597    159   -136   -420       C  
ATOM   3348  O   ILE A 413      14.726  24.017  12.057  1.00 32.82           O  
ANISOU 3348  O   ILE A 413     3770   5220   3481    180   -109   -436       O  
ATOM   3349  CB  ILE A 413      13.300  24.576   9.379  1.00 31.07           C  
ANISOU 3349  CB  ILE A 413     3538   4868   3400    268   -108   -388       C  
ATOM   3350  CG1 ILE A 413      13.415  23.264   8.565  1.00 31.13           C  
ANISOU 3350  CG1 ILE A 413     3505   4880   3442    196   -133   -301       C  
ATOM   3351  CG2 ILE A 413      12.581  25.686   8.584  1.00 32.19           C  
ANISOU 3351  CG2 ILE A 413     3701   4952   3578    365    -95   -414       C  
ATOM   3352  CD1 ILE A 413      12.023  22.559   8.269  1.00 34.84           C  
ANISOU 3352  CD1 ILE A 413     3886   5449   3904    203   -116   -250       C  
ATOM   3353  N   ASN A 414      16.406  23.457  10.644  1.00 30.05           N  
ANISOU 3353  N   ASN A 414     3465   4727   3228     89   -171   -377       N  
ATOM   3354  CA  ASN A 414      17.077  22.549  11.578  1.00 30.61           C  
ANISOU 3354  CA  ASN A 414     3509   4877   3245     39   -183   -340       C  
ATOM   3355  C   ASN A 414      17.492  23.249  12.914  1.00 36.39           C  
ANISOU 3355  C   ASN A 414     4257   5676   3892     40   -180   -418       C  
ATOM   3356  O   ASN A 414      17.129  22.720  13.969  1.00 35.70           O  
ANISOU 3356  O   ASN A 414     4129   5708   3727     43   -163   -395       O  
ATOM   3357  CB  ASN A 414      18.250  21.846  10.910  1.00 31.63           C  
ANISOU 3357  CB  ASN A 414     3646   4954   3419    -14   -218   -285       C  
ATOM   3358  CG  ASN A 414      18.544  20.487  11.456  1.00 57.72           C  
ANISOU 3358  CG  ASN A 414     6911   8326   6692    -43   -223   -202       C  
ATOM   3359  OD1 ASN A 414      18.876  20.308  12.635  1.00 50.57           O  
ANISOU 3359  OD1 ASN A 414     5990   7511   5712    -51   -226   -199       O  
ATOM   3360  ND2 ASN A 414      18.447  19.500  10.592  1.00 53.26           N  
ANISOU 3360  ND2 ASN A 414     6335   7717   6183    -58   -225   -131       N  
ATOM   3361  N   PRO A 415      18.159  24.449  12.920  1.00 33.75           N  
ANISOU 3361  N   PRO A 415     3984   5274   3564     35   -194   -512       N  
ATOM   3362  CA  PRO A 415      18.455  25.118  14.206  1.00 33.80           C  
ANISOU 3362  CA  PRO A 415     4009   5352   3482     29   -191   -604       C  
ATOM   3363  C   PRO A 415      17.196  25.614  14.935  1.00 38.33           C  
ANISOU 3363  C   PRO A 415     4577   5989   3998    105   -143   -664       C  
ATOM   3364  O   PRO A 415      17.220  25.753  16.158  1.00 37.09           O  
ANISOU 3364  O   PRO A 415     4410   5941   3740    106   -133   -719       O  
ATOM   3365  CB  PRO A 415      19.346  26.296  13.795  1.00 35.38           C  
ANISOU 3365  CB  PRO A 415     4285   5433   3725     -8   -214   -691       C  
ATOM   3366  CG  PRO A 415      19.814  25.977  12.410  1.00 39.62           C  
ANISOU 3366  CG  PRO A 415     4826   5870   4359    -33   -234   -617       C  
ATOM   3367  CD  PRO A 415      18.675  25.253  11.793  1.00 35.04           C  
ANISOU 3367  CD  PRO A 415     4206   5297   3812     23   -210   -539       C  
ATOM   3368  N   MET A 416      16.100  25.865  14.181  1.00 35.89           N  
ANISOU 3368  N   MET A 416     4264   5628   3743    174   -112   -651       N  
ATOM   3369  CA  MET A 416      14.799  26.294  14.710  1.00 36.25           C  
ANISOU 3369  CA  MET A 416     4288   5743   3743    265    -60   -696       C  
ATOM   3370  C   MET A 416      14.156  25.159  15.521  1.00 39.59           C  
ANISOU 3370  C   MET A 416     4619   6338   4086    257    -37   -621       C  
ATOM   3371  O   MET A 416      13.443  25.436  16.483  1.00 39.49           O  
ANISOU 3371  O   MET A 416     4580   6438   3987    309      4   -670       O  
ATOM   3372  CB  MET A 416      13.843  26.727  13.580  1.00 38.95           C  
ANISOU 3372  CB  MET A 416     4633   6002   4165    342    -40   -678       C  
ATOM   3373  CG  MET A 416      14.297  27.949  12.811  1.00 43.10           C  
ANISOU 3373  CG  MET A 416     5256   6354   4765    365    -52   -742       C  
ATOM   3374  SD  MET A 416      13.172  28.313  11.435  1.00 47.84           S  
ANISOU 3374  SD  MET A 416     5846   6881   5451    461    -36   -688       S  
ATOM   3375  CE  MET A 416      13.959  29.762  10.754  1.00 44.49           C  
ANISOU 3375  CE  MET A 416     5556   6243   5106    468    -49   -752       C  
ATOM   3376  N   CYS A 417      14.398  23.888  15.116  1.00 35.60           N  
ANISOU 3376  N   CYS A 417     4069   5849   3610    193    -59   -501       N  
ATOM   3377  CA  CYS A 417      13.914  22.677  15.790  1.00 35.49           C  
ANISOU 3377  CA  CYS A 417     3978   5970   3536    164    -40   -406       C  
ATOM   3378  C   CYS A 417      14.556  22.549  17.177  1.00 38.45           C  
ANISOU 3378  C   CYS A 417     4350   6462   3799    139    -43   -423       C  
ATOM   3379  O   CYS A 417      13.860  22.216  18.137  1.00 38.43           O  
ANISOU 3379  O   CYS A 417     4293   6604   3704    154     -6   -399       O  
ATOM   3380  CB  CYS A 417      14.178  21.434  14.942  1.00 35.97           C  
ANISOU 3380  CB  CYS A 417     4020   5979   3670     99    -66   -288       C  
ATOM   3381  SG  CYS A 417      13.200  21.343  13.420  1.00 39.75           S  
ANISOU 3381  SG  CYS A 417     4477   6377   4250    117    -60   -257       S  
ATOM   3382  N   TYR A 418      15.878  22.818  17.278  1.00 34.02           N  
ANISOU 3382  N   TYR A 418     3838   5852   3236     99    -89   -460       N  
ATOM   3383  CA  TYR A 418      16.615  22.784  18.545  1.00 33.50           C  
ANISOU 3383  CA  TYR A 418     3767   5907   3057     72   -104   -485       C  
ATOM   3384  C   TYR A 418      16.111  23.881  19.488  1.00 38.11           C  
ANISOU 3384  C   TYR A 418     4368   6567   3546    122    -71   -621       C  
ATOM   3385  O   TYR A 418      15.879  23.603  20.660  1.00 38.49           O  
ANISOU 3385  O   TYR A 418     4377   6779   3471    127    -53   -619       O  
ATOM   3386  CB  TYR A 418      18.136  22.877  18.321  1.00 33.77           C  
ANISOU 3386  CB  TYR A 418     3835   5879   3116     13   -164   -498       C  
ATOM   3387  CG  TYR A 418      18.766  21.554  17.935  1.00 34.06           C  
ANISOU 3387  CG  TYR A 418     3840   5910   3192    -25   -192   -355       C  
ATOM   3388  CD1 TYR A 418      18.855  21.163  16.601  1.00 35.48           C  
ANISOU 3388  CD1 TYR A 418     4034   5953   3494    -34   -202   -301       C  
ATOM   3389  CD2 TYR A 418      19.267  20.689  18.905  1.00 34.37           C  
ANISOU 3389  CD2 TYR A 418     3837   6080   3142    -44   -206   -275       C  
ATOM   3390  CE1 TYR A 418      19.419  19.940  16.242  1.00 35.33           C  
ANISOU 3390  CE1 TYR A 418     3994   5916   3513    -59   -222   -183       C  
ATOM   3391  CE2 TYR A 418      19.831  19.462  18.558  1.00 34.90           C  
ANISOU 3391  CE2 TYR A 418     3884   6126   3252    -63   -227   -142       C  
ATOM   3392  CZ  TYR A 418      19.901  19.090  17.225  1.00 41.15           C  
ANISOU 3392  CZ  TYR A 418     4696   6767   4170    -69   -233   -102       C  
ATOM   3393  OH  TYR A 418      20.454  17.881  16.878  1.00 41.57           O  
ANISOU 3393  OH  TYR A 418     4740   6788   4267    -77   -248     17       O  
ATOM   3394  N   ALA A 419      15.873  25.097  18.959  1.00 34.45           N  
ANISOU 3394  N   ALA A 419     3966   5984   3139    167    -60   -736       N  
ATOM   3395  CA  ALA A 419      15.345  26.233  19.722  1.00 34.12           C  
ANISOU 3395  CA  ALA A 419     3960   5979   3026    232    -23   -883       C  
ATOM   3396  C   ALA A 419      13.930  25.956  20.274  1.00 37.45           C  
ANISOU 3396  C   ALA A 419     4311   6540   3378    311     43   -859       C  
ATOM   3397  O   ALA A 419      13.669  26.270  21.430  1.00 37.16           O  
ANISOU 3397  O   ALA A 419     4263   6639   3217    342     74   -936       O  
ATOM   3398  CB  ALA A 419      15.339  27.486  18.858  1.00 34.74           C  
ANISOU 3398  CB  ALA A 419     4129   5866   3204    271    -21   -984       C  
ATOM   3399  N   LEU A 420      13.045  25.338  19.460  1.00 33.79           N  
ANISOU 3399  N   LEU A 420     3793   6060   2986    335     64   -755       N  
ATOM   3400  CA  LEU A 420      11.663  25.001  19.818  1.00 33.83           C  
ANISOU 3400  CA  LEU A 420     3713   6205   2938    396    126   -715       C  
ATOM   3401  C   LEU A 420      11.513  23.899  20.872  1.00 39.02           C  
ANISOU 3401  C   LEU A 420     4288   7055   3482    347    144   -617       C  
ATOM   3402  O   LEU A 420      10.617  23.985  21.707  1.00 38.55           O  
ANISOU 3402  O   LEU A 420     4170   7155   3321    399    201   -637       O  
ATOM   3403  CB  LEU A 420      10.868  24.592  18.568  1.00 33.86           C  
ANISOU 3403  CB  LEU A 420     3674   6140   3051    412    133   -629       C  
ATOM   3404  CG  LEU A 420      10.280  25.708  17.702  1.00 38.25           C  
ANISOU 3404  CG  LEU A 420     4270   6580   3683    513    148   -709       C  
ATOM   3405  CD1 LEU A 420       9.849  25.163  16.352  1.00 37.82           C  
ANISOU 3405  CD1 LEU A 420     4182   6449   3737    496    128   -611       C  
ATOM   3406  CD2 LEU A 420       9.103  26.400  18.395  1.00 39.31           C  
ANISOU 3406  CD2 LEU A 420     4361   6836   3740    635    217   -782       C  
ATOM   3407  N   CYS A 421      12.345  22.847  20.800  1.00 37.01           N  
ANISOU 3407  N   CYS A 421     4028   6788   3246    254    101   -503       N  
ATOM   3408  CA  CYS A 421      12.273  21.676  21.681  1.00 37.12           C  
ANISOU 3408  CA  CYS A 421     3975   6959   3170    202    114   -378       C  
ATOM   3409  C   CYS A 421      13.172  21.748  22.910  1.00 41.40           C  
ANISOU 3409  C   CYS A 421     4531   7620   3580    184     96   -412       C  
ATOM   3410  O   CYS A 421      12.832  21.149  23.933  1.00 41.21           O  
ANISOU 3410  O   CYS A 421     4447   7778   3434    179    130   -350       O  
ATOM   3411  CB  CYS A 421      12.538  20.396  20.893  1.00 37.37           C  
ANISOU 3411  CB  CYS A 421     3995   6906   3299    126     85   -224       C  
ATOM   3412  SG  CYS A 421      11.482  20.177  19.439  1.00 41.08           S  
ANISOU 3412  SG  CYS A 421     4436   7268   3906    128    102   -180       S  
ATOM   3413  N   ASN A 422      14.338  22.410  22.799  1.00 37.90           N  
ANISOU 3413  N   ASN A 422     4158   7089   3155    164     40   -498       N  
ATOM   3414  CA  ASN A 422      15.325  22.489  23.878  1.00 37.77           C  
ANISOU 3414  CA  ASN A 422     4148   7191   3012    134      8   -536       C  
ATOM   3415  C   ASN A 422      15.407  23.892  24.487  1.00 42.43           C  
ANISOU 3415  C   ASN A 422     4790   7807   3526    174     17   -739       C  
ATOM   3416  O   ASN A 422      15.865  24.823  23.818  1.00 42.05           O  
ANISOU 3416  O   ASN A 422     4816   7597   3566    174     -8   -851       O  
ATOM   3417  CB  ASN A 422      16.688  22.036  23.350  1.00 38.20           C  
ANISOU 3417  CB  ASN A 422     4228   7156   3130     69    -64   -476       C  
ATOM   3418  CG  ASN A 422      17.477  21.176  24.295  1.00 63.50           C  
ANISOU 3418  CG  ASN A 422     7390  10519   6218     33    -93   -381       C  
ATOM   3419  OD1 ASN A 422      18.061  21.655  25.277  1.00 60.96           O  
ANISOU 3419  OD1 ASN A 422     7067  10329   5765     26   -113   -467       O  
ATOM   3420  ND2 ASN A 422      17.531  19.887  23.998  1.00 53.82           N  
ANISOU 3420  ND2 ASN A 422     6132   9281   5037     10    -99   -202       N  
ATOM   3421  N   LYS A 423      14.965  24.038  25.762  1.00 39.84           N  
ANISOU 3421  N   LYS A 423     4426   7680   3033    205     54   -788       N  
ATOM   3422  CA  LYS A 423      14.974  25.313  26.494  1.00 39.94           C  
ANISOU 3422  CA  LYS A 423     4489   7735   2950    246     70   -995       C  
ATOM   3423  C   LYS A 423      16.377  25.927  26.619  1.00 43.93           C  
ANISOU 3423  C   LYS A 423     5061   8186   3444    175     -3  -1104       C  
ATOM   3424  O   LYS A 423      16.518  27.142  26.473  1.00 43.74           O  
ANISOU 3424  O   LYS A 423     5121   8050   3448    190     -4  -1281       O  
ATOM   3425  CB  LYS A 423      14.320  25.172  27.879  1.00 43.12           C  
ANISOU 3425  CB  LYS A 423     4830   8395   3160    287    124  -1012       C  
ATOM   3426  CG  LYS A 423      13.862  26.509  28.451  1.00 61.90           C  
ANISOU 3426  CG  LYS A 423     7261  10799   5460    366    168  -1235       C  
ATOM   3427  CD  LYS A 423      13.183  26.379  29.804  1.00 74.87           C  
ANISOU 3427  CD  LYS A 423     8833  12712   6903    416    232  -1253       C  
ATOM   3428  CE  LYS A 423      12.157  27.472  30.029  1.00 88.31           C  
ANISOU 3428  CE  LYS A 423    10560  14416   8576    539    310  -1421       C  
ATOM   3429  NZ  LYS A 423      12.765  28.831  30.069  1.00 97.86           N  
ANISOU 3429  NZ  LYS A 423    11894  15503   9787    555    289  -1661       N  
ATOM   3430  N   ALA A 424      17.403  25.088  26.870  1.00 40.38           N  
ANISOU 3430  N   ALA A 424     4573   7813   2956    100    -62   -995       N  
ATOM   3431  CA  ALA A 424      18.793  25.526  27.012  1.00 40.09           C  
ANISOU 3431  CA  ALA A 424     4572   7764   2898     21   -137  -1075       C  
ATOM   3432  C   ALA A 424      19.342  26.138  25.716  1.00 44.31           C  
ANISOU 3432  C   ALA A 424     5180   8047   3609    -15   -170  -1126       C  
ATOM   3433  O   ALA A 424      20.132  27.074  25.792  1.00 44.35           O  
ANISOU 3433  O   ALA A 424     5243   8002   3607    -69   -208  -1272       O  
ATOM   3434  CB  ALA A 424      19.668  24.375  27.478  1.00 40.69           C  
ANISOU 3434  CB  ALA A 424     4573   7986   2902    -30   -188   -915       C  
ATOM   3435  N   PHE A 425      18.895  25.646  24.537  1.00 40.17           N  
ANISOU 3435  N   PHE A 425     4654   7372   3238     10   -155  -1011       N  
ATOM   3436  CA  PHE A 425      19.301  26.191  23.235  1.00 39.39           C  
ANISOU 3436  CA  PHE A 425     4620   7043   3303    -15   -178  -1041       C  
ATOM   3437  C   PHE A 425      18.639  27.550  22.980  1.00 43.01           C  
ANISOU 3437  C   PHE A 425     5166   7369   3808     37   -138  -1205       C  
ATOM   3438  O   PHE A 425      19.326  28.503  22.621  1.00 42.25           O  
ANISOU 3438  O   PHE A 425     5147   7139   3766     -9   -166  -1317       O  
ATOM   3439  CB  PHE A 425      19.004  25.207  22.083  1.00 40.78           C  
ANISOU 3439  CB  PHE A 425     4764   7119   3611     -3   -174   -872       C  
ATOM   3440  CG  PHE A 425      20.133  24.252  21.765  1.00 41.76           C  
ANISOU 3440  CG  PHE A 425     4850   7253   3762    -65   -230   -747       C  
ATOM   3441  CD1 PHE A 425      21.288  24.698  21.132  1.00 44.16           C  
ANISOU 3441  CD1 PHE A 425     5188   7461   4132   -128   -282   -787       C  
ATOM   3442  CD2 PHE A 425      20.035  22.904  22.082  1.00 43.57           C  
ANISOU 3442  CD2 PHE A 425     5011   7585   3957    -57   -226   -582       C  
ATOM   3443  CE1 PHE A 425      22.336  23.818  20.851  1.00 44.87           C  
ANISOU 3443  CE1 PHE A 425     5232   7576   4242   -169   -330   -673       C  
ATOM   3444  CE2 PHE A 425      21.073  22.020  21.778  1.00 46.15           C  
ANISOU 3444  CE2 PHE A 425     5309   7912   4316    -94   -274   -467       C  
ATOM   3445  CZ  PHE A 425      22.219  22.484  21.168  1.00 44.07           C  
ANISOU 3445  CZ  PHE A 425     5067   7569   4107   -143   -325   -515       C  
ATOM   3446  N   ARG A 426      17.314  27.636  23.205  1.00 40.00           N  
ANISOU 3446  N   ARG A 426     4770   7029   3399    135    -70  -1217       N  
ATOM   3447  CA  ARG A 426      16.484  28.837  23.041  1.00 40.31           C  
ANISOU 3447  CA  ARG A 426     4881   6961   3472    222    -18  -1358       C  
ATOM   3448  C   ARG A 426      17.034  30.037  23.844  1.00 45.08           C  
ANISOU 3448  C   ARG A 426     5573   7555   4001    199    -27  -1567       C  
ATOM   3449  O   ARG A 426      17.109  31.144  23.305  1.00 45.03           O  
ANISOU 3449  O   ARG A 426     5670   7356   4084    213    -21  -1682       O  
ATOM   3450  CB  ARG A 426      15.046  28.520  23.482  1.00 39.83           C  
ANISOU 3450  CB  ARG A 426     4754   7030   3349    329     56  -1323       C  
ATOM   3451  CG  ARG A 426      13.971  29.419  22.891  1.00 45.51           C  
ANISOU 3451  CG  ARG A 426     5519   7626   4148    448    113  -1394       C  
ATOM   3452  CD  ARG A 426      12.615  29.165  23.533  1.00 52.24           C  
ANISOU 3452  CD  ARG A 426     6288   8651   4909    553    188  -1378       C  
ATOM   3453  NE  ARG A 426      12.232  27.752  23.472  1.00 59.27           N  
ANISOU 3453  NE  ARG A 426     7061   9675   5784    516    191  -1187       N  
ATOM   3454  CZ  ARG A 426      11.902  27.015  24.529  1.00 70.58           C  
ANISOU 3454  CZ  ARG A 426     8409  11333   7077    506    219  -1131       C  
ATOM   3455  NH1 ARG A 426      11.872  27.556  25.741  1.00 54.52           N  
ANISOU 3455  NH1 ARG A 426     6385   9439   4892    539    246  -1257       N  
ATOM   3456  NH2 ARG A 426      11.590  25.735  24.380  1.00 57.36           N  
ANISOU 3456  NH2 ARG A 426     6642   9744   5409    461    221   -949       N  
ATOM   3457  N   ASP A 427      17.429  29.805  25.115  1.00 41.69           N  
ANISOU 3457  N   ASP A 427     5106   7330   3406    159    -42  -1613       N  
ATOM   3458  CA  ASP A 427      17.984  30.838  25.993  1.00 41.64           C  
ANISOU 3458  CA  ASP A 427     5172   7347   3301    119    -56  -1822       C  
ATOM   3459  C   ASP A 427      19.369  31.296  25.533  1.00 45.24           C  
ANISOU 3459  C   ASP A 427     5688   7673   3827    -11   -131  -1874       C  
ATOM   3460  O   ASP A 427      19.633  32.499  25.548  1.00 44.96           O  
ANISOU 3460  O   ASP A 427     5763   7502   3819    -38   -130  -2052       O  
ATOM   3461  CB  ASP A 427      18.005  30.382  27.468  1.00 43.45           C  
ANISOU 3461  CB  ASP A 427     5329   7864   3316    111    -55  -1844       C  
ATOM   3462  CG  ASP A 427      16.644  30.088  28.092  1.00 53.87           C  
ANISOU 3462  CG  ASP A 427     6589   9337   4541    233     28  -1817       C  
ATOM   3463  OD1 ASP A 427      15.612  30.486  27.499  1.00 53.70           O  
ANISOU 3463  OD1 ASP A 427     6597   9200   4607    338     90  -1838       O  
ATOM   3464  OD2 ASP A 427      16.613  29.470  29.182  1.00 60.50           O  
ANISOU 3464  OD2 ASP A 427     7347  10426   5213    225     31  -1770       O  
ATOM   3465  N   THR A 428      20.239  30.351  25.103  1.00 41.48           N  
ANISOU 3465  N   THR A 428     5142   7233   3385    -92   -190  -1718       N  
ATOM   3466  CA  THR A 428      21.585  30.675  24.612  1.00 41.20           C  
ANISOU 3466  CA  THR A 428     5136   7105   3414   -219   -261  -1742       C  
ATOM   3467  C   THR A 428      21.521  31.444  23.285  1.00 45.31           C  
ANISOU 3467  C   THR A 428     5750   7344   4121   -218   -248  -1761       C  
ATOM   3468  O   THR A 428      22.319  32.360  23.088  1.00 44.85           O  
ANISOU 3468  O   THR A 428     5769   7167   4107   -311   -279  -1874       O  
ATOM   3469  CB  THR A 428      22.504  29.442  24.558  1.00 47.28           C  
ANISOU 3469  CB  THR A 428     5796   8009   4158   -281   -320  -1569       C  
ATOM   3470  OG1 THR A 428      22.281  28.630  25.709  1.00 47.70           O  
ANISOU 3470  OG1 THR A 428     5764   8313   4046   -250   -317  -1514       O  
ATOM   3471  CG2 THR A 428      23.974  29.823  24.532  1.00 43.90           C  
ANISOU 3471  CG2 THR A 428     5370   7581   3727   -418   -396  -1624       C  
ATOM   3472  N   PHE A 429      20.557  31.098  22.401  1.00 42.63           N  
ANISOU 3472  N   PHE A 429     5403   6909   3885   -118   -202  -1650       N  
ATOM   3473  CA  PHE A 429      20.328  31.762  21.105  1.00 42.47           C  
ANISOU 3473  CA  PHE A 429     5464   6641   4033    -92   -184  -1643       C  
ATOM   3474  C   PHE A 429      19.973  33.236  21.353  1.00 47.76           C  
ANISOU 3474  C   PHE A 429     6263   7168   4715    -57   -146  -1838       C  
ATOM   3475  O   PHE A 429      20.587  34.127  20.764  1.00 47.12           O  
ANISOU 3475  O   PHE A 429     6278   6897   4728   -123   -163  -1904       O  
ATOM   3476  CB  PHE A 429      19.169  31.078  20.344  1.00 43.85           C  
ANISOU 3476  CB  PHE A 429     5589   6797   4276     22   -139  -1500       C  
ATOM   3477  CG  PHE A 429      19.458  29.858  19.495  1.00 44.90           C  
ANISOU 3477  CG  PHE A 429     5642   6941   4477     -9   -169  -1312       C  
ATOM   3478  CD1 PHE A 429      20.498  28.992  19.815  1.00 47.68           C  
ANISOU 3478  CD1 PHE A 429     5925   7415   4777    -96   -222  -1236       C  
ATOM   3479  CD2 PHE A 429      18.644  29.537  18.416  1.00 46.52           C  
ANISOU 3479  CD2 PHE A 429     5837   7049   4789     59   -143  -1211       C  
ATOM   3480  CE1 PHE A 429      20.735  27.844  19.052  1.00 48.33           C  
ANISOU 3480  CE1 PHE A 429     5944   7497   4923   -110   -243  -1071       C  
ATOM   3481  CE2 PHE A 429      18.888  28.393  17.649  1.00 49.11           C  
ANISOU 3481  CE2 PHE A 429     6100   7385   5174     29   -168  -1055       C  
ATOM   3482  CZ  PHE A 429      19.930  27.554  17.973  1.00 47.11           C  
ANISOU 3482  CZ  PHE A 429     5791   7231   4876    -51   -215   -989       C  
ATOM   3483  N   ARG A 430      19.004  33.472  22.262  1.00 46.00           N  
ANISOU 3483  N   ARG A 430     6044   7040   4392     45    -93  -1930       N  
ATOM   3484  CA  ARG A 430      18.513  34.788  22.673  1.00 46.77           C  
ANISOU 3484  CA  ARG A 430     6264   7024   4481    108    -45  -2127       C  
ATOM   3485  C   ARG A 430      19.613  35.610  23.356  1.00 52.60           C  
ANISOU 3485  C   ARG A 430     7084   7737   5163    -27    -89  -2306       C  
ATOM   3486  O   ARG A 430      19.678  36.819  23.145  1.00 52.44           O  
ANISOU 3486  O   ARG A 430     7202   7507   5214    -34    -71  -2448       O  
ATOM   3487  CB  ARG A 430      17.303  34.630  23.603  1.00 47.60           C  
ANISOU 3487  CB  ARG A 430     6324   7296   4464    247     21  -2171       C  
ATOM   3488  CG  ARG A 430      16.354  35.823  23.587  1.00 61.04           C  
ANISOU 3488  CG  ARG A 430     8138   8849   6207    387     94  -2315       C  
ATOM   3489  CD  ARG A 430      15.258  35.710  24.633  1.00 72.75           C  
ANISOU 3489  CD  ARG A 430     9566  10528   7547    521    163  -2375       C  
ATOM   3490  NE  ARG A 430      14.234  34.726  24.271  1.00 82.37           N  
ANISOU 3490  NE  ARG A 430    10656  11867   8775    617    198  -2192       N  
ATOM   3491  CZ  ARG A 430      14.117  33.521  24.824  1.00 97.13           C  
ANISOU 3491  CZ  ARG A 430    12388  13978  10538    586    189  -2068       C  
ATOM   3492  NH1 ARG A 430      14.959  33.134  25.775  1.00 84.50           N  
ANISOU 3492  NH1 ARG A 430    10757  12539   8809    477    146  -2097       N  
ATOM   3493  NH2 ARG A 430      13.154  32.697  24.435  1.00 84.12           N  
ANISOU 3493  NH2 ARG A 430    10634  12415   8912    660    223  -1911       N  
ATOM   3494  N   LEU A 431      20.481  34.951  24.155  1.00 50.27           N  
ANISOU 3494  N   LEU A 431     6704   7655   4743   -138   -146  -2296       N  
ATOM   3495  CA  LEU A 431      21.603  35.588  24.850  1.00 50.67           C  
ANISOU 3495  CA  LEU A 431     6802   7733   4718   -288   -200  -2457       C  
ATOM   3496  C   LEU A 431      22.657  36.087  23.847  1.00 55.43           C  
ANISOU 3496  C   LEU A 431     7464   8133   5462   -424   -248  -2446       C  
ATOM   3497  O   LEU A 431      23.116  37.221  23.974  1.00 55.48           O  
ANISOU 3497  O   LEU A 431     7588   8002   5490   -513   -257  -2620       O  
ATOM   3498  CB  LEU A 431      22.225  34.622  25.881  1.00 50.78           C  
ANISOU 3498  CB  LEU A 431     6684   8055   4555   -355   -253  -2411       C  
ATOM   3499  CG  LEU A 431      23.270  35.209  26.830  1.00 55.38           C  
ANISOU 3499  CG  LEU A 431     7291   8741   5009   -498   -309  -2595       C  
ATOM   3500  CD1 LEU A 431      22.931  34.909  28.273  1.00 55.37           C  
ANISOU 3500  CD1 LEU A 431     7229   9020   4790   -452   -297  -2663       C  
ATOM   3501  CD2 LEU A 431      24.661  34.703  26.489  1.00 57.97           C  
ANISOU 3501  CD2 LEU A 431     7543   9133   5350   -656   -398  -2507       C  
ATOM   3502  N   LEU A 432      23.024  35.251  22.857  1.00 52.38           N  
ANISOU 3502  N   LEU A 432     7001   7730   5171   -445   -276  -2246       N  
ATOM   3503  CA  LEU A 432      24.012  35.588  21.827  1.00 52.78           C  
ANISOU 3503  CA  LEU A 432     7086   7617   5350   -567   -317  -2206       C  
ATOM   3504  C   LEU A 432      23.530  36.712  20.896  1.00 58.51           C  
ANISOU 3504  C   LEU A 432     7960   8039   6232   -525   -268  -2257       C  
ATOM   3505  O   LEU A 432      24.331  37.568  20.518  1.00 58.18           O  
ANISOU 3505  O   LEU A 432     8005   7839   6263   -651   -291  -2331       O  
ATOM   3506  CB  LEU A 432      24.417  34.342  21.013  1.00 52.77           C  
ANISOU 3506  CB  LEU A 432     6961   7691   5399   -574   -349  -1981       C  
ATOM   3507  CG  LEU A 432      25.273  33.283  21.725  1.00 57.43           C  
ANISOU 3507  CG  LEU A 432     7412   8545   5864   -643   -410  -1908       C  
ATOM   3508  CD1 LEU A 432      25.061  31.916  21.114  1.00 57.57           C  
ANISOU 3508  CD1 LEU A 432     7323   8635   5917   -568   -409  -1689       C  
ATOM   3509  CD2 LEU A 432      26.749  33.635  21.678  1.00 60.02           C  
ANISOU 3509  CD2 LEU A 432     7725   8889   6191   -820   -479  -1953       C  
ATOM   3510  N   LEU A 433      22.225  36.717  20.548  1.00 56.46           N  
ANISOU 3510  N   LEU A 433     7726   7705   6020   -350   -202  -2213       N  
ATOM   3511  CA  LEU A 433      21.606  37.724  19.680  1.00 56.98           C  
ANISOU 3511  CA  LEU A 433     7924   7498   6226   -271   -150  -2240       C  
ATOM   3512  C   LEU A 433      21.477  39.095  20.347  1.00 64.51           C  
ANISOU 3512  C   LEU A 433     9036   8306   7168   -272   -118  -2468       C  
ATOM   3513  O   LEU A 433      21.741  40.106  19.693  1.00 64.19           O  
ANISOU 3513  O   LEU A 433     9129   8012   7248   -315   -107  -2516       O  
ATOM   3514  CB  LEU A 433      20.241  37.246  19.157  1.00 56.74           C  
ANISOU 3514  CB  LEU A 433     7851   7473   6235    -78    -94  -2119       C  
ATOM   3515  CG  LEU A 433      20.263  36.222  18.018  1.00 60.83           C  
ANISOU 3515  CG  LEU A 433     8269   8015   6830    -72   -115  -1900       C  
ATOM   3516  CD1 LEU A 433      18.964  35.453  17.964  1.00 60.84           C  
ANISOU 3516  CD1 LEU A 433     8181   8130   6805     86    -73  -1799       C  
ATOM   3517  CD2 LEU A 433      20.538  36.886  16.675  1.00 62.30           C  
ANISOU 3517  CD2 LEU A 433     8542   7958   7172    -93   -114  -1844       C  
ATOM   3518  N   LEU A 434      21.071  39.134  21.636  1.00 64.01           N  
ANISOU 3518  N   LEU A 434     8964   8398   6958   -227    -99  -2608       N  
ATOM   3519  CA  LEU A 434      20.922  40.379  22.398  1.00 65.40           C  
ANISOU 3519  CA  LEU A 434     9291   8456   7102   -221    -66  -2850       C  
ATOM   3520  C   LEU A 434      22.270  41.046  22.685  1.00 73.33           C  
ANISOU 3520  C   LEU A 434    10368   9397   8099   -446   -126  -2987       C  
ATOM   3521  O   LEU A 434      22.340  42.274  22.748  1.00 72.99           O  
ANISOU 3521  O   LEU A 434    10493   9129   8112   -479   -101  -3159       O  
ATOM   3522  CB  LEU A 434      20.150  40.150  23.708  1.00 65.56           C  
ANISOU 3522  CB  LEU A 434     9266   8697   6949   -111    -29  -2959       C  
ATOM   3523  CG  LEU A 434      18.638  39.913  23.602  1.00 70.50           C  
ANISOU 3523  CG  LEU A 434     9864   9343   7579    125     53  -2900       C  
ATOM   3524  CD1 LEU A 434      18.091  39.342  24.899  1.00 70.64           C  
ANISOU 3524  CD1 LEU A 434     9777   9660   7403    195     76  -2945       C  
ATOM   3525  CD2 LEU A 434      17.888  41.190  23.236  1.00 73.45           C  
ANISOU 3525  CD2 LEU A 434    10413   9443   8051    253    125  -3033       C  
ATOM   3526  N   ALA A 435      23.335  40.233  22.853  1.00 73.12           N  
ANISOU 3526  N   ALA A 435    10212   9566   8004   -601   -203  -2910       N  
ATOM   3527  CA  ALA A 435      24.703  40.692  23.104  1.00 74.41           C  
ANISOU 3527  CA  ALA A 435    10401   9725   8147   -832   -272  -3015       C  
ATOM   3528  C   ALA A 435      25.301  41.323  21.845  1.00 81.90           C  
ANISOU 3528  C   ALA A 435    11436  10403   9279   -935   -280  -2954       C  
ATOM   3529  O   ALA A 435      26.094  42.260  21.953  1.00 81.23           O  
ANISOU 3529  O   ALA A 435    11453  10188   9223  -1105   -304  -3096       O  
ATOM   3530  CB  ALA A 435      25.568  39.530  23.567  1.00 75.13           C  
ANISOU 3530  CB  ALA A 435    10307  10128   8113   -931   -348  -2917       C  
ATOM   3531  N   ARG A 436      24.916  40.811  20.656  1.00 81.67           N  
ANISOU 3531  N   ARG A 436    11365  10296   9369   -841   -259  -2744       N  
ATOM   3532  CA  ARG A 436      25.368  41.314  19.357  1.00 83.14           C  
ANISOU 3532  CA  ARG A 436    11621  10244   9723   -914   -258  -2653       C  
ATOM   3533  C   ARG A 436      24.717  42.654  19.012  1.00 90.87           C  
ANISOU 3533  C   ARG A 436    12808  10899  10822   -845   -192  -2757       C  
ATOM   3534  O   ARG A 436      25.321  43.456  18.298  1.00 90.48           O  
ANISOU 3534  O   ARG A 436    12862  10625  10890   -964   -195  -2758       O  
ATOM   3535  CB  ARG A 436      25.118  40.281  18.247  1.00 83.93           C  
ANISOU 3535  CB  ARG A 436    11605  10394   9891   -825   -258  -2403       C  
ATOM   3536  CG  ARG A 436      26.191  39.196  18.173  1.00 95.76           C  
ANISOU 3536  CG  ARG A 436    12934  12117  11332   -947   -329  -2284       C  
ATOM   3537  CD  ARG A 436      27.195  39.428  17.052  1.00107.23           C  
ANISOU 3537  CD  ARG A 436    14392  13453  12898  -1090   -355  -2191       C  
ATOM   3538  NE  ARG A 436      28.068  40.580  17.300  1.00115.68           N  
ANISOU 3538  NE  ARG A 436    15568  14393  13990  -1281   -375  -2346       N  
ATOM   3539  CZ  ARG A 436      29.242  40.517  17.920  1.00129.53           C  
ANISOU 3539  CZ  ARG A 436    17252  16303  15660  -1470   -440  -2418       C  
ATOM   3540  NH1 ARG A 436      29.701  39.357  18.375  1.00116.70           N  
ANISOU 3540  NH1 ARG A 436    15451  14970  13920  -1476   -491  -2342       N  
ATOM   3541  NH2 ARG A 436      29.964  41.615  18.098  1.00116.33           N  
ANISOU 3541  NH2 ARG A 436    15685  14499  14017  -1655   -455  -2565       N  
ATOM   3542  N   TRP A 437      23.491  42.892  19.519  1.00 90.56           N  
ANISOU 3542  N   TRP A 437    12826  10835  10749   -649   -129  -2837       N  
ATOM   3543  CA  TRP A 437      22.742  44.134  19.316  1.00 91.91           C  
ANISOU 3543  CA  TRP A 437    13193  10709  11019   -538    -58  -2943       C  
ATOM   3544  C   TRP A 437      23.244  45.243  20.258  1.00 98.08           C  
ANISOU 3544  C   TRP A 437    14127  11376  11763   -666    -59  -3209       C  
ATOM   3545  O   TRP A 437      23.214  46.418  19.886  1.00 97.84           O  
ANISOU 3545  O   TRP A 437    14287  11036  11854   -683    -22  -3292       O  
ATOM   3546  CB  TRP A 437      21.230  43.891  19.485  1.00 91.00           C  
ANISOU 3546  CB  TRP A 437    13056  10645  10874   -267     12  -2918       C  
ATOM   3547  CG  TRP A 437      20.373  45.100  19.239  1.00 92.25           C  
ANISOU 3547  CG  TRP A 437    13403  10514  11135   -112     90  -3007       C  
ATOM   3548  CD1 TRP A 437      19.675  45.809  20.171  1.00 95.20           C  
ANISOU 3548  CD1 TRP A 437    13882  10839  11450      7    147  -3210       C  
ATOM   3549  CD2 TRP A 437      20.130  45.743  17.979  1.00 92.24           C  
ANISOU 3549  CD2 TRP A 437    13508  10231  11307    -49    123  -2892       C  
ATOM   3550  NE1 TRP A 437      19.005  46.850  19.571  1.00 94.73           N  
ANISOU 3550  NE1 TRP A 437    13992  10475  11526    151    215  -3228       N  
ATOM   3551  CE2 TRP A 437      19.270  46.836  18.225  1.00 96.14           C  
ANISOU 3551  CE2 TRP A 437    14175  10507  11848    118    199  -3029       C  
ATOM   3552  CE3 TRP A 437      20.561  45.505  16.660  1.00 93.57           C  
ANISOU 3552  CE3 TRP A 437    13644  10318  11592   -109     97  -2684       C  
ATOM   3553  CZ2 TRP A 437      18.831  47.690  17.205  1.00 95.47           C  
ANISOU 3553  CZ2 TRP A 437    14230  10121  11924    229    248  -2952       C  
ATOM   3554  CZ3 TRP A 437      20.126  46.351  15.650  1.00 95.07           C  
ANISOU 3554  CZ3 TRP A 437    13969  10223  11932    -10    144  -2610       C  
ATOM   3555  CH2 TRP A 437      19.271  47.428  15.926  1.00 95.71           C  
ANISOU 3555  CH2 TRP A 437    14221  10086  12059    159    217  -2737       C  
ATOM   3556  N   ASP A 438      23.714  44.864  21.465  1.00 96.19           N  
ANISOU 3556  N   ASP A 438    13808  11385  11354   -761   -103  -3340       N  
ATOM   3557  CA  ASP A 438      24.250  45.787  22.468  1.00 96.83           C  
ANISOU 3557  CA  ASP A 438    14010  11414  11366   -902   -116  -3609       C  
ATOM   3558  C   ASP A 438      25.616  45.271  22.999  1.00102.02           C  
ANISOU 3558  C   ASP A 438    14538  12315  11909  -1152   -214  -3632       C  
ATOM   3559  O   ASP A 438      25.630  44.477  23.943  1.00101.92           O  
ANISOU 3559  O   ASP A 438    14390  12613  11723  -1137   -246  -3656       O  
ATOM   3560  CB  ASP A 438      23.228  46.008  23.604  1.00 98.84           C  
ANISOU 3560  CB  ASP A 438    14311  11748  11497   -726    -58  -3790       C  
ATOM   3561  CG  ASP A 438      23.704  46.952  24.688  1.00110.33           C  
ANISOU 3561  CG  ASP A 438    15900  13154  12868   -858    -67  -4091       C  
ATOM   3562  OD1 ASP A 438      23.600  48.182  24.491  1.00111.45           O  
ANISOU 3562  OD1 ASP A 438    16256  12968  13124   -866    -22  -4233       O  
ATOM   3563  OD2 ASP A 438      24.182  46.462  25.733  1.00116.30           O  
ANISOU 3563  OD2 ASP A 438    16550  14199  13441   -954   -120  -4185       O  
ATOM   3564  N   HIS A 439      26.766  45.671  22.395  1.00 99.00           N  
ANISOU 3564  N   HIS A 439    14185  11815  11616  -1379   -263  -3612       N  
ATOM   3565  CA  HIS A 439      26.930  46.606  21.272  1.00138.49           C  
ANISOU 3565  CA  HIS A 439    19342  16460  16817  -1435   -231  -3568       C  
ATOM   3566  C   HIS A 439      26.633  45.958  19.918  1.00161.33           C  
ANISOU 3566  C   HIS A 439    22153  19316  19828  -1327   -216  -3284       C  
ATOM   3567  O   HIS A 439      26.316  46.658  18.959  1.00120.35           O  
ANISOU 3567  O   HIS A 439    17093  13837  14796  -1275   -167  -3218       O  
ATOM   3568  CB  HIS A 439      28.349  47.207  21.276  1.00139.44           C  
ANISOU 3568  CB  HIS A 439    19499  16521  16959  -1748   -293  -3661       C  
ATOM   3569  CG  HIS A 439      29.446  46.190  21.171  1.00142.93           C  
ANISOU 3569  CG  HIS A 439    19721  17258  17327  -1904   -380  -3525       C  
ATOM   3570  ND1 HIS A 439      29.943  45.787  19.943  1.00144.73           N  
ANISOU 3570  ND1 HIS A 439    19874  17452  17667  -1954   -394  -3300       N  
ATOM   3571  CD2 HIS A 439      30.108  45.527  22.148  1.00144.70           C  
ANISOU 3571  CD2 HIS A 439    19788  17817  17373  -2002   -452  -3584       C  
ATOM   3572  CE1 HIS A 439      30.885  44.897  20.211  1.00144.14           C  
ANISOU 3572  CE1 HIS A 439    19601  17681  17485  -2075   -471  -3235       C  
ATOM   3573  NE2 HIS A 439      31.021  44.708  21.524  1.00144.48           N  
ANISOU 3573  NE2 HIS A 439    19587  17954  17353  -2106   -510  -3394       N  
TER    3574      HIS A 439                                                      
HETATM 3575  N1  QJT A1201      21.201  19.989  -4.867  1.00 28.25           N  
HETATM 3576  C4  QJT A1201      21.054  16.298  -2.444  1.00 28.90           C  
HETATM 3577  C5  QJT A1201      20.642  17.432  -3.421  1.00 29.07           C  
HETATM 3578  C6  QJT A1201      21.563  17.527  -4.663  1.00 28.94           C  
HETATM 3579  C7  QJT A1201      21.182  18.645  -5.647  1.00 28.79           C  
HETATM 3580  C8  QJT A1201      20.234  19.993  -3.638  1.00 27.56           C  
HETATM 3581  C10 QJT A1201      20.899  21.194  -5.787  1.00 28.74           C  
HETATM 3582  C13 QJT A1201      22.617  23.451  -9.536  1.00 37.99           C  
HETATM 3583  C15 QJT A1201      25.124  24.148  -9.886  1.00 37.74           C  
HETATM 3584  C17 QJT A1201      25.166  24.448  -8.392  1.00 37.71           C  
HETATM 3585  C20 QJT A1201      26.393  25.298  -6.468  1.00 37.14           C  
HETATM 3586  C21 QJT A1201      26.320  25.018  -7.831  1.00 37.02           C  
HETATM 3587  C1  QJT A1201      23.180  13.772  -1.520  1.00 28.76           C  
HETATM 3588  O1  QJT A1201      21.611  22.946 -10.059  1.00 39.76           O  
HETATM 3589  C2  QJT A1201      21.721  13.843  -1.997  1.00 28.38           C  
HETATM 3590  N2  QJT A1201      22.878  23.534  -8.174  1.00 35.81           N  
HETATM 3591  C3  QJT A1201      21.424  14.923  -3.049  1.00 27.83           C  
HETATM 3592  C9  QJT A1201      20.570  18.808  -2.698  1.00 27.71           C  
HETATM 3593  C11 QJT A1201      22.061  21.564  -6.725  1.00 31.58           C  
HETATM 3594  C12 QJT A1201      21.815  22.974  -7.293  1.00 34.02           C  
HETATM 3595  C14 QJT A1201      23.692  24.064 -10.468  1.00 37.12           C  
HETATM 3596  C16 QJT A1201      24.050  24.128  -7.567  1.00 36.75           C  
HETATM 3597  C18 QJT A1201      24.160  24.433  -6.185  1.00 35.76           C  
HETATM 3598  C19 QJT A1201      25.310  25.001  -5.643  1.00 36.06           C  
HETATM 3599  C1  OLA A1202      32.611  21.236  22.375  1.00 69.10           C  
HETATM 3600  O1  OLA A1202      32.336  20.232  23.070  1.00 70.45           O  
HETATM 3601  O2  OLA A1202      33.226  22.232  22.812  1.00 69.49           O  
HETATM 3602  C2  OLA A1202      32.170  21.247  20.920  1.00 65.97           C  
HETATM 3603  C3  OLA A1202      32.968  20.359  20.017  1.00 62.94           C  
HETATM 3604  C4  OLA A1202      32.494  20.412  18.578  1.00 60.15           C  
HETATM 3605  C5  OLA A1202      32.486  19.076  17.881  1.00 58.76           C  
HETATM 3606  C6  OLA A1202      33.424  18.994  16.704  1.00 58.03           C  
HETATM 3607  C7  OLA A1202      32.750  18.672  15.376  1.00 56.90           C  
HETATM 3608  C8  OLA A1202      33.704  18.530  14.230  1.00 55.82           C  
HETATM 3609  C9  OLA A1202      33.368  19.392  13.053  1.00 55.36           C  
HETATM 3610  C10 OLA A1202      32.877  18.973  11.914  1.00 55.26           C  
HETATM 3611  C11 OLA A1202      33.651  18.706  10.661  1.00 54.80           C  
HETATM 3612  C12 OLA A1202      33.205  19.539   9.502  1.00 54.45           C  
HETATM 3613  C13 OLA A1202      34.143  19.500   8.309  1.00 55.98           C  
HETATM 3614  C14 OLA A1202      33.780  20.458   7.200  1.00 58.21           C  
HETATM 3615  C15 OLA A1202      34.674  21.673   7.110  1.00 60.23           C  
HETATM 3616  C16 OLA A1202      33.985  22.915   6.596  1.00 61.89           C  
HETATM 3617  C17 OLA A1202      34.887  23.883   5.868  1.00 63.17           C  
HETATM 3618  C18 OLA A1202      34.678  23.938   4.370  1.00 63.21           C  
HETATM 3619  C1  OLA A1203      36.041  15.355  13.453  1.00 59.49           C  
HETATM 3620  O1  OLA A1203      36.561  14.236  13.287  1.00 61.21           O  
HETATM 3621  O2  OLA A1203      35.437  15.680  14.489  1.00 59.16           O  
HETATM 3622  C2  OLA A1203      36.147  16.379  12.336  1.00 58.28           C  
HETATM 3623  C3  OLA A1203      37.306  16.197  11.405  1.00 57.12           C  
HETATM 3624  C4  OLA A1203      36.903  15.520  10.110  1.00 55.56           C  
HETATM 3625  C5  OLA A1203      37.027  16.403   8.897  1.00 54.17           C  
HETATM 3626  C6  OLA A1203      36.398  15.833   7.656  1.00 53.12           C  
HETATM 3627  C7  OLA A1203      37.362  15.068   6.761  1.00 52.07           C  
HETATM 3628  C8  OLA A1203      37.611  15.723   5.444  1.00 51.73           C  
HETATM 3629  C9  OLA A1203      36.849  15.092   4.321  1.00 51.95           C  
HETATM 3630  C10 OLA A1203      35.797  15.596   3.732  1.00 52.18           C  
HETATM 3631  C11 OLA A1203      35.790  16.802   2.845  1.00 52.36           C  
HETATM 3632  C12 OLA A1203      34.426  17.376   2.636  1.00 52.44           C  
HETATM 3633  C13 OLA A1203      34.330  18.871   2.881  1.00 54.39           C  
HETATM 3634  C14 OLA A1203      34.522  19.721   1.648  1.00 57.40           C  
HETATM 3635  C15 OLA A1203      35.204  21.046   1.909  1.00 60.47           C  
HETATM 3636  C16 OLA A1203      35.516  21.862   0.669  1.00 63.17           C  
HETATM 3637  C17 OLA A1203      36.772  21.496  -0.092  1.00 64.45           C  
HETATM 3638  C18 OLA A1203      37.683  22.659  -0.415  1.00 64.62           C  
HETATM 3639  C1  OLA A1204      42.968   2.373  13.314  1.00 78.77           C  
HETATM 3640  O1  OLA A1204      41.758   2.569  13.086  1.00 79.44           O  
HETATM 3641  O2  OLA A1204      43.579   2.876  14.279  1.00 79.89           O  
HETATM 3642  C2  OLA A1204      43.740   1.473  12.364  1.00 76.26           C  
HETATM 3643  C3  OLA A1204      44.543   2.198  11.326  1.00 73.66           C  
HETATM 3644  C4  OLA A1204      43.722   2.586  10.106  1.00 70.54           C  
HETATM 3645  C5  OLA A1204      43.852   1.634   8.942  1.00 67.52           C  
HETATM 3646  C6  OLA A1204      44.640   2.178   7.780  1.00 64.99           C  
HETATM 3647  C7  OLA A1204      44.860   1.172   6.657  1.00 63.03           C  
HETATM 3648  C8  OLA A1204      44.205   1.540   5.363  1.00 60.92           C  
HETATM 3649  C9  OLA A1204      45.132   1.456   4.190  1.00 58.89           C  
HETATM 3650  C10 OLA A1204      44.787   1.162   2.963  1.00 56.65           C  
HETATM 3651  C11 OLA A1204      45.081   1.986   1.748  1.00 54.10           C  
HETATM 3652  C12 OLA A1204      43.855   2.544   1.094  1.00 52.80           C  
HETATM 3653  C13 OLA A1204      43.512   3.965   1.510  1.00 51.47           C  
HETATM 3654  C14 OLA A1204      42.083   4.367   1.236  1.00 50.52           C  
HETATM 3655  C15 OLA A1204      41.374   5.004   2.409  1.00 49.50           C  
HETATM 3656  C16 OLA A1204      39.888   5.184   2.206  1.00 49.26           C  
HETATM 3657  C17 OLA A1204      39.251   6.320   2.968  1.00 48.33           C  
HETATM 3658  C18 OLA A1204      37.765   6.144   3.182  1.00 47.34           C  
HETATM 3659  C1  OLA A1205      35.708  33.480 -12.447  1.00 85.62           C  
HETATM 3660  O1  OLA A1205      35.062  34.255 -13.183  1.00 85.75           O  
HETATM 3661  O2  OLA A1205      36.321  32.477 -12.869  1.00 85.81           O  
HETATM 3662  C2  OLA A1205      35.753  33.774 -10.957  1.00 85.08           C  
HETATM 3663  C3  OLA A1205      34.792  32.975 -10.129  1.00 84.21           C  
HETATM 3664  C4  OLA A1205      35.309  32.706  -8.725  1.00 82.81           C  
HETATM 3665  C5  OLA A1205      34.274  32.150  -7.777  1.00 81.30           C  
HETATM 3666  C6  OLA A1205      34.674  30.859  -7.106  1.00 79.88           C  
HETATM 3667  C7  OLA A1205      34.019  29.614  -7.690  1.00 77.99           C  
HETATM 3668  C8  OLA A1205      33.280  28.779  -6.689  1.00 75.53           C  
HETATM 3669  C9  OLA A1205      33.443  27.304  -6.903  1.00 73.14           C  
HETATM 3670  C10 OLA A1205      34.381  26.536  -6.400  1.00 71.52           C  
HETATM 3671  C11 OLA A1205      34.571  26.187  -4.956  1.00 70.48           C  
HETATM 3672  C12 OLA A1205      34.300  24.749  -4.652  1.00 70.17           C  
HETATM 3673  C13 OLA A1205      35.367  24.082  -3.800  1.00 70.57           C  
HETATM 3674  C14 OLA A1205      34.973  22.728  -3.257  1.00 70.71           C  
HETATM 3675  C15 OLA A1205      35.794  21.576  -3.789  1.00 69.60           C  
HETATM 3676  C16 OLA A1205      35.301  20.215  -3.364  1.00 67.85           C  
HETATM 3677  C17 OLA A1205      36.396  19.194  -3.206  1.00 66.71           C  
HETATM 3678  C18 OLA A1205      36.383  18.111  -4.258  1.00 65.58           C  
HETATM 3679  P   PO4 A1206      22.795  -3.907  28.398  1.00103.29           P  
HETATM 3680  O1  PO4 A1206      21.735  -4.210  27.239  1.00103.16           O  
HETATM 3681  O2  PO4 A1206      24.072  -4.758  28.163  1.00103.65           O  
HETATM 3682  O3  PO4 A1206      22.152  -4.288  29.814  1.00103.28           O  
HETATM 3683  O4  PO4 A1206      23.170  -2.352  28.383  1.00102.88           O  
HETATM 3684  C1  OLA A1207      36.833  18.462  22.406  1.00 79.98           C  
HETATM 3685  O1  OLA A1207      37.768  18.343  23.225  1.00 80.89           O  
HETATM 3686  O2  OLA A1207      35.855  17.689  22.356  1.00 79.79           O  
HETATM 3687  C2  OLA A1207      36.891  19.613  21.416  1.00 78.81           C  
HETATM 3688  C3  OLA A1207      36.239  20.873  21.889  1.00 78.19           C  
HETATM 3689  C4  OLA A1207      36.926  22.122  21.360  1.00 77.85           C  
HETATM 3690  C5  OLA A1207      36.240  23.414  21.738  1.00 77.15           C  
HETATM 3691  C6  OLA A1207      36.466  24.550  20.770  1.00 75.75           C  
HETATM 3692  C7  OLA A1207      35.189  25.236  20.300  1.00 74.16           C  
HETATM 3693  C8  OLA A1207      34.794  24.914  18.892  1.00 72.31           C  
HETATM 3694  C9  OLA A1207      34.785  26.111  17.994  1.00 70.64           C  
HETATM 3695  C10 OLA A1207      33.926  26.336  17.035  1.00 69.34           C  
HETATM 3696  C11 OLA A1207      34.073  27.355  15.948  1.00 68.41           C  
HETATM 3697  C12 OLA A1207      32.975  28.372  15.944  1.00 67.94           C  
HETATM 3698  C13 OLA A1207      31.974  28.206  14.812  1.00 67.66           C  
HETATM 3699  C14 OLA A1207      31.943  29.356  13.836  1.00 67.18           C  
HETATM 3700  C15 OLA A1207      32.527  29.037  12.479  1.00 66.57           C  
HETATM 3701  C16 OLA A1207      31.987  29.890  11.355  1.00 65.62           C  
HETATM 3702  C17 OLA A1207      32.916  30.981  10.888  1.00 65.04           C  
HETATM 3703  C18 OLA A1207      32.758  31.330   9.426  1.00 65.11           C  
HETATM 3704  C1  OLA A1208      25.245  -0.829  14.107  1.00 74.51           C  
HETATM 3705  O1  OLA A1208      24.518  -1.445  14.914  1.00 74.75           O  
HETATM 3706  O2  OLA A1208      24.867  -0.473  12.972  1.00 74.54           O  
HETATM 3707  C2  OLA A1208      26.671  -0.505  14.523  1.00 73.83           C  
HETATM 3708  C3  OLA A1208      26.808   0.591  15.539  1.00 72.39           C  
HETATM 3709  C4  OLA A1208      27.637   1.760  15.028  1.00 70.40           C  
HETATM 3710  C5  OLA A1208      27.181   3.124  15.508  1.00 67.70           C  
HETATM 3711  C6  OLA A1208      26.044   3.728  14.711  1.00 64.91           C  
HETATM 3712  C7  OLA A1208      26.472   4.592  13.532  1.00 62.47           C  
HETATM 3713  C8  OLA A1208      25.802   4.238  12.240  1.00 60.98           C  
HETATM 3714  C9  OLA A1208      25.681   5.390  11.291  1.00 59.64           C  
HETATM 3715  C10 OLA A1208      26.269   5.488  10.124  1.00 58.24           C  
HETATM 3716  C11 OLA A1208      26.661   6.751   9.418  1.00 57.41           C  
HETATM 3717  C12 OLA A1208      28.010   7.279   9.815  1.00 57.58           C  
HETATM 3718  C13 OLA A1208      29.181   6.695   9.041  1.00 58.23           C  
HETATM 3719  C14 OLA A1208      30.165   5.926   9.885  1.00 59.59           C  
HETATM 3720  C15 OLA A1208      30.539   4.574   9.327  1.00 61.59           C  
HETATM 3721  C16 OLA A1208      29.888   3.407  10.036  1.00 63.20           C  
HETATM 3722  C17 OLA A1208      30.785   2.641  10.979  1.00 63.60           C  
HETATM 3723  C18 OLA A1208      30.044   1.743  11.944  1.00 63.59           C  
HETATM 3724  C1  OLA A1209      -5.531  25.237   3.413  1.00 66.24           C  
HETATM 3725  O1  OLA A1209      -6.693  25.682   3.453  1.00 66.60           O  
HETATM 3726  O2  OLA A1209      -4.922  24.997   2.352  1.00 67.09           O  
HETATM 3727  C2  OLA A1209      -4.815  24.979   4.728  1.00 65.16           C  
HETATM 3728  C3  OLA A1209      -3.852  26.048   5.128  1.00 65.15           C  
HETATM 3729  C4  OLA A1209      -3.147  25.735   6.435  1.00 66.30           C  
HETATM 3730  C5  OLA A1209      -2.423  26.910   7.045  1.00 67.04           C  
HETATM 3731  C6  OLA A1209      -0.920  26.758   7.099  1.00 67.41           C  
HETATM 3732  C7  OLA A1209      -0.174  28.027   7.494  1.00 67.82           C  
HETATM 3733  C8  OLA A1209       0.100  28.155   8.965  1.00 67.22           C  
HETATM 3734  C9  OLA A1209       1.537  27.939   9.326  1.00 65.05           C  
HETATM 3735  C10 OLA A1209       2.021  26.900   9.955  1.00 62.34           C  
HETATM 3736  C11 OLA A1209       3.180  26.071   9.499  1.00 59.73           C  
HETATM 3737  C12 OLA A1209       4.469  26.458  10.149  1.00 57.79           C  
HETATM 3738  C13 OLA A1209       5.685  25.727   9.609  1.00 56.48           C  
HETATM 3739  C14 OLA A1209       6.951  25.985  10.389  1.00 54.81           C  
HETATM 3740  C15 OLA A1209       7.878  24.800  10.478  1.00 53.12           C  
HETATM 3741  C16 OLA A1209       8.662  24.731  11.764  1.00 52.24           C  
HETATM 3742  C17 OLA A1209      10.154  24.675  11.577  1.00 51.51           C  
HETATM 3743  C18 OLA A1209      10.913  24.321  12.832  1.00 50.86           C  
HETATM 3744  C1  OLA A1210       9.059  29.181 -16.603  1.00 84.65           C  
HETATM 3745  O1  OLA A1210       8.452  29.256 -17.692  1.00 84.79           O  
HETATM 3746  O2  OLA A1210      10.293  29.027 -16.511  1.00 84.73           O  
HETATM 3747  C2  OLA A1210       8.249  29.270 -15.321  1.00 84.34           C  
HETATM 3748  C3  OLA A1210       7.758  30.640 -14.968  1.00 84.15           C  
HETATM 3749  C4  OLA A1210       6.635  30.609 -13.945  1.00 83.73           C  
HETATM 3750  C5  OLA A1210       7.041  31.064 -12.567  1.00 83.41           C  
HETATM 3751  C6  OLA A1210       7.021  29.974 -11.523  1.00 83.44           C  
HETATM 3752  C7  OLA A1210       7.627  30.374 -10.184  1.00 83.40           C  
HETATM 3753  C8  OLA A1210       6.626  30.818  -9.162  1.00 83.58           C  
HETATM 3754  C9  OLA A1210       6.742  30.084  -7.863  1.00 84.00           C  
HETATM 3755  C10 OLA A1210       7.267  30.565  -6.767  1.00 84.64           C  
HETATM 3756  C11 OLA A1210       7.099  29.994  -5.392  1.00 85.26           C  
HETATM 3757  C12 OLA A1210       7.146  31.024  -4.304  1.00 85.43           C  
HETATM 3758  C13 OLA A1210       8.548  31.366  -3.819  1.00 85.20           C  
HETATM 3759  C14 OLA A1210       8.681  32.730  -3.180  1.00 85.08           C  
HETATM 3760  C15 OLA A1210       8.831  33.876  -4.158  1.00 85.27           C  
HETATM 3761  C16 OLA A1210      10.258  34.273  -4.455  1.00 85.42           C  
HETATM 3762  C17 OLA A1210      10.405  35.630  -5.099  1.00 85.56           C  
HETATM 3763  C18 OLA A1210      10.603  35.594  -6.597  1.00 85.50           C  
HETATM 3764  C18 OLC A1211      19.553  -0.615  -6.096  1.00 68.09           C  
HETATM 3765  C10 OLC A1211      22.385   2.795   2.031  1.00 72.57           C  
HETATM 3766  C9  OLC A1211      21.872   3.216   3.196  1.00 73.82           C  
HETATM 3767  C17 OLC A1211      20.068   0.685  -5.516  1.00 68.45           C  
HETATM 3768  C11 OLC A1211      22.195   1.405   1.456  1.00 71.30           C  
HETATM 3769  C8  OLC A1211      21.021   2.369   4.122  1.00 75.08           C  
HETATM 3770  C24 OLC A1211      24.174   7.959   3.158  1.00 81.78           C  
HETATM 3771  C16 OLC A1211      20.907   0.448  -4.264  1.00 68.40           C  
HETATM 3772  C12 OLC A1211      22.605   1.394  -0.012  1.00 69.93           C  
HETATM 3773  C7  OLC A1211      20.538   3.215   5.296  1.00 76.14           C  
HETATM 3774  C15 OLC A1211      20.197   0.963  -3.013  1.00 68.47           C  
HETATM 3775  C13 OLC A1211      21.524   0.753  -0.875  1.00 69.00           C  
HETATM 3776  C6  OLC A1211      21.126   2.716   6.612  1.00 77.22           C  
HETATM 3777  C14 OLC A1211      21.172   1.647  -2.060  1.00 68.70           C  
HETATM 3778  C5  OLC A1211      22.070   3.758   7.203  1.00 78.17           C  
HETATM 3779  C4  OLC A1211      23.365   3.158   7.753  1.00 78.92           C  
HETATM 3780  C3  OLC A1211      24.487   3.136   6.714  1.00 79.91           C  
HETATM 3781  C2  OLC A1211      25.320   4.416   6.692  1.00 80.56           C  
HETATM 3782  C21 OLC A1211      25.598   5.917   3.249  1.00 82.33           C  
HETATM 3783  C1  OLC A1211      25.985   4.553   5.340  1.00 81.27           C  
HETATM 3784  C22 OLC A1211      24.382   6.558   2.589  1.00 82.36           C  
HETATM 3785  O19 OLC A1211      27.188   4.367   5.230  1.00 81.05           O  
HETATM 3786  O25 OLC A1211      23.094   8.609   2.476  1.00 81.13           O  
HETATM 3787  O23 OLC A1211      24.596   6.637   1.173  1.00 82.44           O  
HETATM 3788  O20 OLC A1211      25.189   4.896   4.164  1.00 81.97           O  
HETATM 3789  N1  EPE A1212      37.327  14.734 -20.765  1.00 85.86           N  
HETATM 3790  C2  EPE A1212      36.699  13.570 -21.407  1.00 84.39           C  
HETATM 3791  C3  EPE A1212      37.589  12.331 -21.367  1.00 83.97           C  
HETATM 3792  N4  EPE A1212      38.839  12.621 -22.064  1.00 84.29           N  
HETATM 3793  C5  EPE A1212      39.552  13.564 -21.195  1.00 85.37           C  
HETATM 3794  C6  EPE A1212      38.769  14.880 -21.043  1.00 85.80           C  
HETATM 3795  C7  EPE A1212      39.596  11.365 -22.200  1.00 84.52           C  
HETATM 3796  C8  EPE A1212      40.204  11.220 -23.596  1.00 85.31           C  
HETATM 3797  O8  EPE A1212      39.261  10.633 -24.504  1.00 85.85           O  
HETATM 3798  C9  EPE A1212      36.538  15.963 -21.028  1.00 88.01           C  
HETATM 3799  C10 EPE A1212      36.971  16.831 -22.221  1.00 90.15           C  
HETATM 3800  S   EPE A1212      35.892  16.797 -23.495  1.00 91.98           S  
HETATM 3801  O1S EPE A1212      36.471  17.527 -24.643  1.00 93.58           O  
HETATM 3802  O2S EPE A1212      35.629  15.407 -23.916  1.00 91.99           O  
HETATM 3803  O3S EPE A1212      34.618  17.459 -23.147  1.00 91.91           O  
HETATM 3804  C1  PGE A1213      19.185  20.874 -14.125  1.00 67.80           C  
HETATM 3805  O1  PGE A1213      19.585  20.850 -15.483  1.00 67.52           O  
HETATM 3806  C2  PGE A1213      19.215  19.515 -13.495  1.00 67.41           C  
HETATM 3807  O2  PGE A1213      17.944  18.886 -13.633  1.00 66.17           O  
HETATM 3808  C3  PGE A1213      17.740  17.838 -12.691  1.00 64.41           C  
HETATM 3809  C4  PGE A1213      17.487  16.550 -13.414  1.00 62.75           C  
HETATM 3810  O4  PGE A1213      16.067  12.377 -13.292  1.00 54.45           O  
HETATM 3811  C6  PGE A1213      16.754  13.288 -12.457  1.00 57.20           C  
HETATM 3812  C5  PGE A1213      17.675  14.195 -13.220  1.00 59.50           C  
HETATM 3813  O3  PGE A1213      17.786  15.452 -12.559  1.00 60.90           O  
HETATM 3814  C1  PGE A1214      29.788  31.505 -20.480  1.00 78.20           C  
HETATM 3815  O1  PGE A1214      28.792  30.684 -21.065  1.00 78.70           O  
HETATM 3816  C2  PGE A1214      30.880  30.708 -19.833  1.00 77.14           C  
HETATM 3817  O2  PGE A1214      30.317  29.673 -19.032  1.00 75.77           O  
HETATM 3818  C3  PGE A1214      31.289  28.787 -18.487  1.00 73.11           C  
HETATM 3819  C4  PGE A1214      31.098  27.412 -19.053  1.00 70.76           C  
HETATM 3820  O4  PGE A1214      29.897  23.130 -17.517  1.00 61.92           O  
HETATM 3821  C6  PGE A1214      30.366  24.390 -17.080  1.00 63.64           C  
HETATM 3822  C5  PGE A1214      30.935  25.208 -18.195  1.00 65.56           C  
HETATM 3823  O3  PGE A1214      30.504  26.561 -18.079  1.00 67.80           O  
HETATM 3824  O   HOH A1301      25.188  14.505 -20.189  1.00 34.59           O  
HETATM 3825  O   HOH A1302      21.364  22.572  11.535  1.00 37.31           O  
HETATM 3826  O   HOH A1303      20.536  14.827  -8.370  1.00 39.25           O  
HETATM 3827  O   HOH A1304       8.550  13.410  20.566  1.00 46.07           O  
HETATM 3828  O   HOH A1305      20.361  19.724   5.596  1.00 23.42           O  
HETATM 3829  O   HOH A1306      24.204  18.473 -21.931  1.00 46.88           O  
HETATM 3830  O   HOH A1307      18.308   3.797  41.058  1.00 32.58           O  
HETATM 3831  O   HOH A1308      16.646  17.634   9.617  1.00 30.13           O  
HETATM 3832  O   HOH A1309      30.888  22.085 -19.808  1.00 47.67           O  
HETATM 3833  O   HOH A1310      32.554   8.349  -6.057  1.00 30.01           O  
HETATM 3834  O   HOH A1311      -1.238  -3.079  38.639  1.00 30.29           O  
HETATM 3835  O   HOH A1312      12.648  19.015  -2.035  1.00 17.85           O  
HETATM 3836  O   HOH A1313      26.371  31.555 -13.064  1.00 38.43           O  
HETATM 3837  O   HOH A1314      19.203  12.144  -5.134  1.00 36.85           O  
HETATM 3838  O   HOH A1315      -2.686 -13.068  46.626  1.00 34.59           O  
HETATM 3839  O   HOH A1316      31.279  15.886 -16.338  1.00 26.13           O  
HETATM 3840  O   HOH A1317      18.273  29.100  10.827  1.00 28.33           O  
HETATM 3841  O   HOH A1318      20.788  19.888   0.801  1.00 29.70           O  
HETATM 3842  O   HOH A1319      -2.956   7.725  32.137  1.00 45.23           O  
HETATM 3843  O   HOH A1320      22.165  -2.060  51.175  1.00 60.01           O  
HETATM 3844  O   HOH A1321      36.536  27.086 -13.918  1.00 38.37           O  
HETATM 3845  O   HOH A1322       8.590  -6.302  45.276  1.00 29.73           O  
HETATM 3846  O   HOH A1323      19.474  -2.204  21.418  1.00 46.01           O  
HETATM 3847  O   HOH A1324      17.983  12.394  -2.614  1.00 22.04           O  
HETATM 3848  O   HOH A1325      18.055   6.563  41.089  1.00 35.37           O  
HETATM 3849  O   HOH A1326      19.471  20.367   3.132  1.00 36.99           O  
HETATM 3850  O   HOH A1327      32.487  14.073 -14.744  1.00 21.91           O  
HETATM 3851  O   HOH A1328      20.824 -12.154  45.019  1.00 45.03           O  
HETATM 3852  O   HOH A1329      18.790  23.528 -11.241  1.00 43.28           O  
HETATM 3853  O   HOH A1330      -3.751  -9.700  49.684  1.00 34.51           O  
HETATM 3854  O   HOH A1331      18.015  14.322  19.923  1.00 38.77           O  
HETATM 3855  O   HOH A1332      29.632  12.863 -13.182  1.00 35.59           O  
HETATM 3856  O   HOH A1333      30.013  15.969 -13.521  1.00 45.10           O  
CONECT  591 1232                                                                
CONECT 1232  591                                                                
CONECT 3169 3192                                                                
CONECT 3192 3169                                                                
CONECT 3575 3579 3580 3581                                                      
CONECT 3576 3577 3591                                                           
CONECT 3577 3576 3578 3592                                                      
CONECT 3578 3577 3579                                                           
CONECT 3579 3575 3578                                                           
CONECT 3580 3575 3592                                                           
CONECT 3581 3575 3593                                                           
CONECT 3582 3588 3590 3595                                                      
CONECT 3583 3584 3595                                                           
CONECT 3584 3583 3586 3596                                                      
CONECT 3585 3586 3598                                                           
CONECT 3586 3584 3585                                                           
CONECT 3587 3589                                                                
CONECT 3588 3582                                                                
CONECT 3589 3587 3591                                                           
CONECT 3590 3582 3594 3596                                                      
CONECT 3591 3576 3589                                                           
CONECT 3592 3577 3580                                                           
CONECT 3593 3581 3594                                                           
CONECT 3594 3590 3593                                                           
CONECT 3595 3582 3583                                                           
CONECT 3596 3584 3590 3597                                                      
CONECT 3597 3596 3598                                                           
CONECT 3598 3585 3597                                                           
CONECT 3599 3600 3601 3602                                                      
CONECT 3600 3599                                                                
CONECT 3601 3599                                                                
CONECT 3602 3599 3603                                                           
CONECT 3603 3602 3604                                                           
CONECT 3604 3603 3605                                                           
CONECT 3605 3604 3606                                                           
CONECT 3606 3605 3607                                                           
CONECT 3607 3606 3608                                                           
CONECT 3608 3607 3609                                                           
CONECT 3609 3608 3610                                                           
CONECT 3610 3609 3611                                                           
CONECT 3611 3610 3612                                                           
CONECT 3612 3611 3613                                                           
CONECT 3613 3612 3614                                                           
CONECT 3614 3613 3615                                                           
CONECT 3615 3614 3616                                                           
CONECT 3616 3615 3617                                                           
CONECT 3617 3616 3618                                                           
CONECT 3618 3617                                                                
CONECT 3619 3620 3621 3622                                                      
CONECT 3620 3619                                                                
CONECT 3621 3619                                                                
CONECT 3622 3619 3623                                                           
CONECT 3623 3622 3624                                                           
CONECT 3624 3623 3625                                                           
CONECT 3625 3624 3626                                                           
CONECT 3626 3625 3627                                                           
CONECT 3627 3626 3628                                                           
CONECT 3628 3627 3629                                                           
CONECT 3629 3628 3630                                                           
CONECT 3630 3629 3631                                                           
CONECT 3631 3630 3632                                                           
CONECT 3632 3631 3633                                                           
CONECT 3633 3632 3634                                                           
CONECT 3634 3633 3635                                                           
CONECT 3635 3634 3636                                                           
CONECT 3636 3635 3637                                                           
CONECT 3637 3636 3638                                                           
CONECT 3638 3637                                                                
CONECT 3639 3640 3641 3642                                                      
CONECT 3640 3639                                                                
CONECT 3641 3639                                                                
CONECT 3642 3639 3643                                                           
CONECT 3643 3642 3644                                                           
CONECT 3644 3643 3645                                                           
CONECT 3645 3644 3646                                                           
CONECT 3646 3645 3647                                                           
CONECT 3647 3646 3648                                                           
CONECT 3648 3647 3649                                                           
CONECT 3649 3648 3650                                                           
CONECT 3650 3649 3651                                                           
CONECT 3651 3650 3652                                                           
CONECT 3652 3651 3653                                                           
CONECT 3653 3652 3654                                                           
CONECT 3654 3653 3655                                                           
CONECT 3655 3654 3656                                                           
CONECT 3656 3655 3657                                                           
CONECT 3657 3656 3658                                                           
CONECT 3658 3657                                                                
CONECT 3659 3660 3661 3662                                                      
CONECT 3660 3659                                                                
CONECT 3661 3659                                                                
CONECT 3662 3659 3663                                                           
CONECT 3663 3662 3664                                                           
CONECT 3664 3663 3665                                                           
CONECT 3665 3664 3666                                                           
CONECT 3666 3665 3667                                                           
CONECT 3667 3666 3668                                                           
CONECT 3668 3667 3669                                                           
CONECT 3669 3668 3670                                                           
CONECT 3670 3669 3671                                                           
CONECT 3671 3670 3672                                                           
CONECT 3672 3671 3673                                                           
CONECT 3673 3672 3674                                                           
CONECT 3674 3673 3675                                                           
CONECT 3675 3674 3676                                                           
CONECT 3676 3675 3677                                                           
CONECT 3677 3676 3678                                                           
CONECT 3678 3677                                                                
CONECT 3679 3680 3681 3682 3683                                                 
CONECT 3680 3679                                                                
CONECT 3681 3679                                                                
CONECT 3682 3679                                                                
CONECT 3683 3679                                                                
CONECT 3684 3685 3686 3687                                                      
CONECT 3685 3684                                                                
CONECT 3686 3684                                                                
CONECT 3687 3684 3688                                                           
CONECT 3688 3687 3689                                                           
CONECT 3689 3688 3690                                                           
CONECT 3690 3689 3691                                                           
CONECT 3691 3690 3692                                                           
CONECT 3692 3691 3693                                                           
CONECT 3693 3692 3694                                                           
CONECT 3694 3693 3695                                                           
CONECT 3695 3694 3696                                                           
CONECT 3696 3695 3697                                                           
CONECT 3697 3696 3698                                                           
CONECT 3698 3697 3699                                                           
CONECT 3699 3698 3700                                                           
CONECT 3700 3699 3701                                                           
CONECT 3701 3700 3702                                                           
CONECT 3702 3701 3703                                                           
CONECT 3703 3702                                                                
CONECT 3704 3705 3706 3707                                                      
CONECT 3705 3704                                                                
CONECT 3706 3704                                                                
CONECT 3707 3704 3708                                                           
CONECT 3708 3707 3709                                                           
CONECT 3709 3708 3710                                                           
CONECT 3710 3709 3711                                                           
CONECT 3711 3710 3712                                                           
CONECT 3712 3711 3713                                                           
CONECT 3713 3712 3714                                                           
CONECT 3714 3713 3715                                                           
CONECT 3715 3714 3716                                                           
CONECT 3716 3715 3717                                                           
CONECT 3717 3716 3718                                                           
CONECT 3718 3717 3719                                                           
CONECT 3719 3718 3720                                                           
CONECT 3720 3719 3721                                                           
CONECT 3721 3720 3722                                                           
CONECT 3722 3721 3723                                                           
CONECT 3723 3722                                                                
CONECT 3724 3725 3726 3727                                                      
CONECT 3725 3724                                                                
CONECT 3726 3724                                                                
CONECT 3727 3724 3728                                                           
CONECT 3728 3727 3729                                                           
CONECT 3729 3728 3730                                                           
CONECT 3730 3729 3731                                                           
CONECT 3731 3730 3732                                                           
CONECT 3732 3731 3733                                                           
CONECT 3733 3732 3734                                                           
CONECT 3734 3733 3735                                                           
CONECT 3735 3734 3736                                                           
CONECT 3736 3735 3737                                                           
CONECT 3737 3736 3738                                                           
CONECT 3738 3737 3739                                                           
CONECT 3739 3738 3740                                                           
CONECT 3740 3739 3741                                                           
CONECT 3741 3740 3742                                                           
CONECT 3742 3741 3743                                                           
CONECT 3743 3742                                                                
CONECT 3744 3745 3746 3747                                                      
CONECT 3745 3744                                                                
CONECT 3746 3744                                                                
CONECT 3747 3744 3748                                                           
CONECT 3748 3747 3749                                                           
CONECT 3749 3748 3750                                                           
CONECT 3750 3749 3751                                                           
CONECT 3751 3750 3752                                                           
CONECT 3752 3751 3753                                                           
CONECT 3753 3752 3754                                                           
CONECT 3754 3753 3755                                                           
CONECT 3755 3754 3756                                                           
CONECT 3756 3755 3757                                                           
CONECT 3757 3756 3758                                                           
CONECT 3758 3757 3759                                                           
CONECT 3759 3758 3760                                                           
CONECT 3760 3759 3761                                                           
CONECT 3761 3760 3762                                                           
CONECT 3762 3761 3763                                                           
CONECT 3763 3762                                                                
CONECT 3764 3767                                                                
CONECT 3765 3766 3768                                                           
CONECT 3766 3765 3769                                                           
CONECT 3767 3764 3771                                                           
CONECT 3768 3765 3772                                                           
CONECT 3769 3766 3773                                                           
CONECT 3770 3784 3786                                                           
CONECT 3771 3767 3774                                                           
CONECT 3772 3768 3775                                                           
CONECT 3773 3769 3776                                                           
CONECT 3774 3771 3777                                                           
CONECT 3775 3772 3777                                                           
CONECT 3776 3773 3778                                                           
CONECT 3777 3774 3775                                                           
CONECT 3778 3776 3779                                                           
CONECT 3779 3778 3780                                                           
CONECT 3780 3779 3781                                                           
CONECT 3781 3780 3783                                                           
CONECT 3782 3784 3788                                                           
CONECT 3783 3781 3785 3788                                                      
CONECT 3784 3770 3782 3787                                                      
CONECT 3785 3783                                                                
CONECT 3786 3770                                                                
CONECT 3787 3784                                                                
CONECT 3788 3782 3783                                                           
CONECT 3789 3790 3794 3798                                                      
CONECT 3790 3789 3791                                                           
CONECT 3791 3790 3792                                                           
CONECT 3792 3791 3793 3795                                                      
CONECT 3793 3792 3794                                                           
CONECT 3794 3789 3793                                                           
CONECT 3795 3792 3796                                                           
CONECT 3796 3795 3797                                                           
CONECT 3797 3796                                                                
CONECT 3798 3789 3799                                                           
CONECT 3799 3798 3800                                                           
CONECT 3800 3799 3801 3802 3803                                                 
CONECT 3801 3800                                                                
CONECT 3802 3800                                                                
CONECT 3803 3800                                                                
CONECT 3804 3805 3806                                                           
CONECT 3805 3804                                                                
CONECT 3806 3804 3807                                                           
CONECT 3807 3806 3808                                                           
CONECT 3808 3807 3809                                                           
CONECT 3809 3808 3813                                                           
CONECT 3810 3811                                                                
CONECT 3811 3810 3812                                                           
CONECT 3812 3811 3813                                                           
CONECT 3813 3809 3812                                                           
CONECT 3814 3815 3816                                                           
CONECT 3815 3814                                                                
CONECT 3816 3814 3817                                                           
CONECT 3817 3816 3818                                                           
CONECT 3818 3817 3819                                                           
CONECT 3819 3818 3823                                                           
CONECT 3820 3821                                                                
CONECT 3821 3820 3822                                                           
CONECT 3822 3821 3823                                                           
CONECT 3823 3819 3822                                                           
MASTER      288    0   14   21    3    0    0    6 3838    1  253   35          
END