HEADER    MEMBRANE PROTEIN                        18-JUN-20   6ZG9              
TITLE     STRUCTURE OF M1-STAR-T4L IN COMPLEX WITH GSK1034702 AT 2.5A           
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;                                              
SOURCE   4 ORGANISM_TAXID: 9606, 10665;                                         
SOURCE   5 GENE: CHRM1;                                                         
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    GPCR, 7TM, MEMBRANE PROTEIN                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.RUCKTOOA,R.M.COOKE                                                  
REVDAT   3   08-DEC-21 6ZG9    1       JRNL                                     
REVDAT   2   01-DEC-21 6ZG9    1       JRNL   REMARK                            
REVDAT   1   06-OCT-21 6ZG9    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.    2.50 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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.97                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 61.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 14053                          
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)  : 0.205                          
REMARK   3   R VALUE            (WORKING SET)  : 0.203                          
REMARK   3   FREE R VALUE                      : 0.242                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.210                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 732                            
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               : 36                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.50                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.60                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 16.06                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 391                      
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2455                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 375                      
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2453                   
REMARK   3   BIN FREE R VALUE                        : 0.2527                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.09                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 16                       
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          : 159                                     
REMARK   3   SOLVENT ATOMS            : 23                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.08                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -8.73310                                             
REMARK   3    B22 (A**2) : 18.05690                                             
REMARK   3    B33 (A**2) : -9.32380                                             
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) : 0.390               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.360               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.882                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.853                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3794   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 5124   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1362   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : NULL   ; NULL   ; NULL                
REMARK   3    GENERAL PLANES            : 605    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3794   ; 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   : 489    ; 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   : 4298   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.009                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.95                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.17                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 19.90                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|20 - 219 }                                         
REMARK   3    ORIGIN FOR THE GROUP (A):   -7.1925   16.2917   -4.5396           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2492 T22:    0.0619                                    
REMARK   3     T33:   -0.2687 T12:    0.0354                                    
REMARK   3     T13:    0.0320 T23:   -0.0184                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.4837 L22:    0.4508                                    
REMARK   3     L33:    4.8838 L12:    0.3790                                    
REMARK   3     L13:    0.4027 L23:   -0.5158                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0425 S12:    0.1073 S13:    0.0543                     
REMARK   3     S21:   -0.0040 S22:    0.0172 S23:   -0.0080                     
REMARK   3     S31:   -0.1217 S32:   -0.1997 S33:    0.0253                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { A|354 - 439 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A):  -17.4759   12.1790   -8.6403           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2889 T22:    0.2088                                    
REMARK   3     T33:   -0.1948 T12:   -0.0630                                    
REMARK   3     T13:   -0.0098 T23:    0.0395                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.2676 L22:    1.7647                                    
REMARK   3     L33:    4.1200 L12:   -0.0737                                    
REMARK   3     L13:   -0.5405 L23:   -0.9807                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1000 S12:    0.2555 S13:   -0.2939                     
REMARK   3     S21:   -0.3907 S22:    0.1207 S23:    0.0416                     
REMARK   3     S31:    0.0497 S32:    0.1026 S33:   -0.0207                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { A|1002 - 1161 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -17.3730   36.8145  -41.1458           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1939 T22:    0.2022                                    
REMARK   3     T33:   -0.4368 T12:   -0.1022                                    
REMARK   3     T13:   -0.0497 T23:    0.1685                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    6.5854 L22:    5.4411                                    
REMARK   3     L33:    5.3098 L12:   -2.7239                                    
REMARK   3     L13:    1.5510 L23:   -2.9598                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.3161 S12:   -0.2087 S13:   -0.0821                     
REMARK   3     S21:   -0.0107 S22:   -0.0707 S23:   -0.2831                     
REMARK   3     S31:   -0.1486 S32:    0.3016 S33:    0.3869                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6ZG9 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_1292109491.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-JUL-12                          
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) : 0.96860                            
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 : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14062                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 76.551                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.2                               
REMARK 200  DATA REDUNDANCY                : 8.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.63                     
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   (%): 61.08                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 NAHEPES PH 7.4-7.8, 0.1M DI          
REMARK 280  -AMMONIUM HYDROGENOHOSPHATE, 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       31.18150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       76.55100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.28550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       76.55100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.18150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.28550            
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: 4450 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22740 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      -75.93    -92.71                                   
REMARK 500    PHE A 197      -65.87   -132.82                                   
REMARK 500    ILE A1029       79.37   -105.36                                   
REMARK 500    ARG A1125       76.12   -102.60                                   
REMARK 500    TRP A1158       52.04    -94.36                                   
REMARK 500    THR A 354       86.23     64.86                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     OLA A 1205                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue QK2 A 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE A 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1203                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1204                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1205                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1206                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1207                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1208                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 1209                
DBREF  6ZG9 A   27   219  UNP    P11229   ACM1_HUMAN      27    219             
DBREF  6ZG9 A 1002  1161  UNP    P00720   ENLYS_BPT4       2    161             
DBREF  6ZG9 A  354   438  UNP    P11229   ACM1_HUMAN     354    438             
SEQADV 6ZG9 MET A   20  UNP  P11229              INITIATING METHIONINE          
SEQADV 6ZG9 GLU A   21  UNP  P11229              EXPRESSION TAG                 
SEQADV 6ZG9 THR A   22  UNP  P11229              EXPRESSION TAG                 
SEQADV 6ZG9 VAL A   23  UNP  P11229              EXPRESSION TAG                 
SEQADV 6ZG9 GLU A   24  UNP  P11229              EXPRESSION TAG                 
SEQADV 6ZG9 MET A   25  UNP  P11229              EXPRESSION TAG                 
SEQADV 6ZG9 VAL A   26  UNP  P11229              EXPRESSION TAG                 
SEQADV 6ZG9 ALA A   27  UNP  P11229    PHE    27 ENGINEERED MUTATION            
SEQADV 6ZG9 ALA A   29  UNP  P11229    GLY    29 CONFLICT                       
SEQADV 6ZG9 THR A   30  UNP  P11229    ILE    30 CONFLICT                       
SEQADV 6ZG9 VAL A   31  UNP  P11229    THR    31 CONFLICT                       
SEQADV 6ZG9 ALA A   32  UNP  P11229    THR    32 ENGINEERED MUTATION            
SEQADV 6ZG9 ILE A   44  UNP  P11229    LEU    44 ENGINEERED MUTATION            
SEQADV 6ZG9 LEU A   46  UNP  P11229    VAL    46 ENGINEERED MUTATION            
SEQADV 6ZG9 MET A   47  UNP  P11229    LEU    47 CONFLICT                       
SEQADV 6ZG9 LEU A   48  UNP  P11229    ILE    48 CONFLICT                       
SEQADV 6ZG9 ILE A   50  UNP  P11229    PHE    50 CONFLICT                       
SEQADV 6ZG9 ARG A   54  UNP  P11229    THR    54 CONFLICT                       
SEQADV 6ZG9 GLN A   55  UNP  P11229    GLU    55 CONFLICT                       
SEQADV 6ZG9 GLN A   57  UNP  P11229    LYS    57 CONFLICT                       
SEQADV 6ZG9 ALA A   64  UNP  P11229    LEU    64 ENGINEERED MUTATION            
SEQADV 6ZG9 PHE A   65  UNP  P11229    LEU    65 CONFLICT                       
SEQADV 6ZG9 ALA A   76  UNP  P11229    THR    76 ENGINEERED MUTATION            
SEQADV 6ZG9 VAL A   84  UNP  P11229    THR    84 ENGINEERED MUTATION            
SEQADV 6ZG9 ILE A   86  UNP  P11229    LEU    86 CONFLICT                       
SEQADV 6ZG9 ILE A   87  UNP  P11229    LEU    87 CONFLICT                       
SEQADV 6ZG9 ALA A   95  UNP  P11229    THR    95 ENGINEERED MUTATION            
SEQADV 6ZG9 ALA A  101  UNP  P11229    TRP   101 ENGINEERED MUTATION            
SEQADV 6ZG9 ALA A  112  UNP  P11229    SER   112 ENGINEERED MUTATION            
SEQADV 6ZG9 LEU A  143  UNP  P11229    ALA   143 ENGINEERED MUTATION            
SEQADV 6ZG9 THR A  196  UNP  P11229    ALA   196 ENGINEERED MUTATION            
SEQADV 6ZG9 GLY A 1012  UNP  P00720    ARG    12 CONFLICT                       
SEQADV 6ZG9 THR A 1054  UNP  P00720    CYS    54 CONFLICT                       
SEQADV 6ZG9 ALA A 1097  UNP  P00720    CYS    97 CONFLICT                       
SEQADV 6ZG9 ARG A 1137  UNP  P00720    ILE   137 CONFLICT                       
SEQADV 6ZG9 ALA A  362  UNP  P11229    LYS   362 ENGINEERED MUTATION            
SEQADV 6ZG9 LEU A  364  UNP  P11229    ALA   364 ENGINEERED MUTATION            
SEQADV 6ZG9 ALA A  411  UNP  P11229    SER   411 ENGINEERED MUTATION            
SEQADV 6ZG9 ALA A  435  UNP  P11229    CYS   435 CONFLICT                       
SEQADV 6ZG9 HIS A  439  UNP  P11229              EXPRESSION TAG                 
SEQADV 6ZG9 HIS A  440  UNP  P11229              EXPRESSION TAG                 
SEQADV 6ZG9 HIS A  441  UNP  P11229              EXPRESSION TAG                 
SEQADV 6ZG9 HIS A  442  UNP  P11229              EXPRESSION TAG                 
SEQADV 6ZG9 HIS A  443  UNP  P11229              EXPRESSION TAG                 
SEQADV 6ZG9 HIS A  444  UNP  P11229              EXPRESSION TAG                 
SEQADV 6ZG9 HIS A  445  UNP  P11229              EXPRESSION TAG                 
SEQADV 6ZG9 HIS A  446  UNP  P11229              EXPRESSION TAG                 
SEQADV 6ZG9 HIS A  447  UNP  P11229              EXPRESSION TAG                 
SEQADV 6ZG9 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    QK2  A1201      24                                                       
HET    EPE  A1202      15                                                       
HET    OLA  A1203      20                                                       
HET    OLA  A1204      20                                                       
HET    OLA  A1205      15                                                       
HET    OLA  A1206      20                                                       
HET    OLA  A1207      20                                                       
HET    OLA  A1208      20                                                       
HET    PO4  A1209       5                                                       
HETNAM     QK2 7-FLUORANYL-5-METHYL-3-[1-(OXAN-4-YL)PIPERIDIN-4-YL]-            
HETNAM   2 QK2  1~{H}-BENZIMIDAZOL-2-ONE                                        
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID              
HETNAM     OLA OLEIC ACID                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
HETSYN     EPE HEPES                                                            
FORMUL   2  QK2    C18 H24 F N3 O2                                              
FORMUL   3  EPE    C8 H18 N2 O4 S                                               
FORMUL   4  OLA    6(C18 H34 O2)                                                
FORMUL  10  PO4    O4 P 3-                                                      
FORMUL  11  HOH   *23(H2 O)                                                     
HELIX    1 AA1 GLU A   21  ASN A   53  1                                  33    
HELIX    2 AA2 THR A   58  PHE A   77  1                                  20    
HELIX    3 AA3 PHE A   77  GLY A   89  1                                  13    
HELIX    4 AA4 GLY A   94  ARG A  129  1                                  36    
HELIX    5 AA5 SER A  132  ARG A  137  1                                   6    
HELIX    6 AA6 THR A  138  GLY A  169  1                                  32    
HELIX    7 AA7 GLN A  185  PHE A  197  1                                  13    
HELIX    8 AA8 PHE A  197  ALA A  219  1                                  23    
HELIX    9 AA9 ILE A 1003  GLU A 1011  1                                   9    
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  MET A 1106  1                                  15    
HELIX   14 AB5 GLY A 1107  GLY A 1113  1                                   7    
HELIX   15 AB6 PHE A 1114  GLN A 1122  1                                   9    
HELIX   16 AB7 ARG A 1125  LYS A 1135  1                                  11    
HELIX   17 AB8 SER A 1136  THR A 1142  1                                   7    
HELIX   18 AB9 THR A 1142  GLY A 1156  1                                  15    
HELIX   19 AC1 LYS A  361  CYS A  391  1                                  31    
HELIX   20 AC2 PRO A  396  ASN A  422  1                                  27    
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  2.06  
SSBOND   2 CYS A  391    CYS A  394                          1555   1555  2.03  
SITE     1 AC1 11 TYR A  82  TYR A  85  TRP A  91  LEU A 102                    
SITE     2 AC1 11 ASP A 105  SER A 109  CYS A 178  TRP A 378                    
SITE     3 AC1 11 TYR A 404  TYR A 408  HOH A1313                               
SITE     1 AC2  9 TYR A 179  LEU A 183  PRO A 186  THR A 189                    
SITE     2 AC2  9 SER A 388  GLU A 397  TYR A 404  HOH A1304                    
SITE     3 AC2  9 HOH A1307                                                     
SITE     1 AC3  7 GLN A  57  PHE A  65  ILE A  73  LEU A 143                    
SITE     2 AC3  7 ILE A 146  TRP A 150  OLA A1204                               
SITE     1 AC4  9 LEU A 104  VAL A 107  LEU A 143  ILE A 146                    
SITE     2 AC4  9 GLY A 147  PHE A 154  CYS A 394  OLA A1203                    
SITE     3 AC4  9 OLA A1207                                                     
SITE     1 AC5  4 GLU A  24  GLU A 401  TRP A 405  OLA A1208                    
SITE     1 AC6 11 LEU A  93  GLY A  94  ALA A  95  LEU A  96                    
SITE     2 AC6 11 ALA A  97  ALA A 175  CYS A 205  TYR A 208                    
SITE     3 AC6 11 TRP A 209  TYR A 212  OLA A1207                               
SITE     1 AC7  8 HIS A  90  TRP A  91  ALA A  92  LEU A  93                    
SITE     2 AC7  8 ALA A  97  LEU A 100  OLA A1204  OLA A1206                    
SITE     1 AC8  3 LEU A 144  THR A 398  OLA A1205                               
SITE     1 AC9  4 ARG A 129  LEU A 131  SER A 132  ASP A1072                    
CRYST1   62.363   66.571  153.102  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      0.016035  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015022  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006532        0.00000                         
ATOM      1  N   MET A  20     -16.008  -3.409  17.951  1.00103.27           N  
ANISOU    1  N   MET A  20    11496  17221  10521  -3316   -470   4028       N  
ATOM      2  CA  MET A  20     -17.259  -3.625  17.219  1.00103.00           C  
ANISOU    2  CA  MET A  20    11464  17234  10436  -3622   -482   3974       C  
ATOM      3  C   MET A  20     -17.525  -5.117  16.917  1.00106.20           C  
ANISOU    3  C   MET A  20    12188  17175  10990  -3988   -599   4257       C  
ATOM      4  O   MET A  20     -16.605  -5.939  17.018  1.00105.62           O  
ANISOU    4  O   MET A  20    12395  16607  11128  -3911   -661   4429       O  
ATOM      5  CB  MET A  20     -17.338  -2.748  15.948  1.00105.32           C  
ANISOU    5  CB  MET A  20    11774  17417  10825  -3396   -403   3550       C  
ATOM      6  CG  MET A  20     -16.301  -3.081  14.889  1.00108.87           C  
ANISOU    6  CG  MET A  20    12572  17192  11602  -3179   -415   3399       C  
ATOM      7  SD  MET A  20     -16.678  -2.399  13.257  1.00112.86           S  
ANISOU    7  SD  MET A  20    13130  17551  12201  -3069   -353   2986       S  
ATOM      8  CE  MET A  20     -16.000  -0.764  13.432  1.00109.59           C  
ANISOU    8  CE  MET A  20    12493  17415  11733  -2610   -242   2694       C  
ATOM      9  N   GLU A  21     -18.788  -5.456  16.561  1.00102.29           N  
ANISOU    9  N   GLU A  21    11648  16844  10376  -4386   -631   4304       N  
ATOM     10  CA  GLU A  21     -19.198  -6.834  16.273  1.00101.91           C  
ANISOU   10  CA  GLU A  21    11901  16382  10437  -4810   -750   4561       C  
ATOM     11  C   GLU A  21     -18.509  -7.410  15.022  1.00105.13           C  
ANISOU   11  C   GLU A  21    12741  16013  11190  -4682   -777   4370       C  
ATOM     12  O   GLU A  21     -18.162  -6.669  14.095  1.00104.42           O  
ANISOU   12  O   GLU A  21    12654  15826  11195  -4374   -698   4000       O  
ATOM     13  CB  GLU A  21     -20.738  -7.013  16.230  1.00103.28           C  
ANISOU   13  CB  GLU A  21    11882  17003  10358  -5304   -779   4660       C  
ATOM     14  CG  GLU A  21     -21.516  -6.100  15.290  1.00114.84           C  
ANISOU   14  CG  GLU A  21    13156  18755  11724  -5251   -699   4297       C  
ATOM     15  CD  GLU A  21     -23.030  -6.265  15.273  1.00138.17           C  
ANISOU   15  CD  GLU A  21    15865  22242  14391  -5722   -726   4406       C  
ATOM     16  OE1 GLU A  21     -23.514  -7.418  15.187  1.00133.25           O  
ANISOU   16  OE1 GLU A  21    15435  21412  13783  -6208   -838   4663       O  
ATOM     17  OE2 GLU A  21     -23.735  -5.232  15.326  1.00131.52           O  
ANISOU   17  OE2 GLU A  21    14640  22025  13306  -5602   -638   4231       O  
ATOM     18  N   THR A  22     -18.278  -8.742  15.044  1.00101.14           N  
ANISOU   18  N   THR A  22    12608  14955  10865  -4912   -892   4634       N  
ATOM     19  CA  THR A  22     -17.632  -9.525  13.983  1.00100.30           C  
ANISOU   19  CA  THR A  22    12959  14067  11083  -4818   -935   4495       C  
ATOM     20  C   THR A  22     -18.418  -9.438  12.672  1.00101.70           C  
ANISOU   20  C   THR A  22    13196  14182  11265  -5002   -919   4183       C  
ATOM     21  O   THR A  22     -17.803  -9.430  11.608  1.00101.24           O  
ANISOU   21  O   THR A  22    13364  13687  11417  -4748   -889   3886       O  
ATOM     22  CB  THR A  22     -17.396 -10.988  14.428  1.00110.70           C  
ANISOU   22  CB  THR A  22    14663  14836  12564  -5064  -1072   4878       C  
ATOM     23  OG1 THR A  22     -17.178 -11.059  15.843  1.00111.55           O  
ANISOU   23  OG1 THR A  22    14598  15251  12536  -5096  -1105   5272       O  
ATOM     24  CG2 THR A  22     -16.235 -11.642  13.690  1.00109.14           C  
ANISOU   24  CG2 THR A  22    14903  13849  12715  -4723  -1093   4752       C  
ATOM     25  N   VAL A  23     -19.768  -9.356  12.753  1.00 96.38           N  
ANISOU   25  N   VAL A  23    12292  13991  10338  -5437   -936   4253       N  
ATOM     26  CA  VAL A  23     -20.676  -9.227  11.602  1.00 95.26           C  
ANISOU   26  CA  VAL A  23    12134  13923  10138  -5660   -926   3992       C  
ATOM     27  C   VAL A  23     -20.503  -7.831  10.954  1.00 96.45           C  
ANISOU   27  C   VAL A  23    12019  14387  10239  -5229   -792   3600       C  
ATOM     28  O   VAL A  23     -20.507  -7.724   9.725  1.00 95.90           O  
ANISOU   28  O   VAL A  23    12078  14088  10272  -5161   -769   3299       O  
ATOM     29  CB  VAL A  23     -22.157  -9.528  11.980  1.00 99.26           C  
ANISOU   29  CB  VAL A  23    12424  14936  10353  -6251   -986   4218       C  
ATOM     30  CG1 VAL A  23     -23.054  -9.563  10.742  1.00 99.00           C  
ANISOU   30  CG1 VAL A  23    12413  14933  10268  -6521   -994   3971       C  
ATOM     31  CG2 VAL A  23     -22.281 -10.836  12.765  1.00 99.09           C  
ANISOU   31  CG2 VAL A  23    12651  14634  10366  -6688  -1123   4658       C  
ATOM     32  N   GLU A  24     -20.329  -6.777  11.785  1.00 91.08           N  
ANISOU   32  N   GLU A  24    10987  14213   9404  -4943   -709   3606       N  
ATOM     33  CA  GLU A  24     -20.111  -5.403  11.326  1.00 89.83           C  
ANISOU   33  CA  GLU A  24    10592  14336   9203  -4523   -588   3268       C  
ATOM     34  C   GLU A  24     -18.740  -5.264  10.660  1.00 91.33           C  
ANISOU   34  C   GLU A  24    11039  13984   9679  -4087   -552   3044       C  
ATOM     35  O   GLU A  24     -18.632  -4.531   9.677  1.00 91.05           O  
ANISOU   35  O   GLU A  24    10970  13940   9686  -3863   -485   2729       O  
ATOM     36  CB  GLU A  24     -20.247  -4.389  12.479  1.00 91.21           C  
ANISOU   36  CB  GLU A  24    10369  15145   9140  -4349   -519   3334       C  
ATOM     37  CG  GLU A  24     -20.631  -2.982  12.023  1.00100.06           C  
ANISOU   37  CG  GLU A  24    11186  16714  10119  -4087   -412   3024       C  
ATOM     38  CD  GLU A  24     -20.566  -1.843  13.032  1.00112.58           C  
ANISOU   38  CD  GLU A  24    12432  18834  11508  -3818   -331   2996       C  
ATOM     39  OE1 GLU A  24     -20.720  -2.098  14.249  1.00122.87           O  
ANISOU   39  OE1 GLU A  24    13596  20436  12652  -3961   -357   3260       O  
ATOM     40  OE2 GLU A  24     -20.376  -0.684  12.595  1.00 85.25           O  
ANISOU   40  OE2 GLU A  24     8851  15496   8043  -3470   -245   2707       O  
ATOM     41  N   MET A  25     -17.701  -5.960  11.187  1.00 85.87           N  
ANISOU   41  N   MET A  25    10587  12871   9169  -3964   -597   3221       N  
ATOM     42  CA  MET A  25     -16.339  -5.920  10.641  1.00 84.83           C  
ANISOU   42  CA  MET A  25    10681  12260   9291  -3546   -567   3043       C  
ATOM     43  C   MET A  25     -16.277  -6.466   9.217  1.00 84.61           C  
ANISOU   43  C   MET A  25    10962  11737   9449  -3578   -585   2809       C  
ATOM     44  O   MET A  25     -15.633  -5.854   8.372  1.00 83.97           O  
ANISOU   44  O   MET A  25    10899  11541   9465  -3250   -516   2518       O  
ATOM     45  CB  MET A  25     -15.337  -6.650  11.545  1.00 87.64           C  
ANISOU   45  CB  MET A  25    11208  12316   9775  -3422   -620   3320       C  
ATOM     46  CG  MET A  25     -14.945  -5.853  12.768  1.00 92.22           C  
ANISOU   46  CG  MET A  25    11478  13364  10196  -3231   -576   3446       C  
ATOM     47  SD  MET A  25     -13.424  -6.460  13.548  1.00 97.16           S  
ANISOU   47  SD  MET A  25    12274  13648  10994  -2919   -613   3675       S  
ATOM     48  CE  MET A  25     -13.454  -5.515  15.080  1.00 93.87           C  
ANISOU   48  CE  MET A  25    11427  13953  10285  -2881   -574   3843       C  
ATOM     49  N   VAL A  26     -16.970  -7.591   8.952  1.00 78.00           N  
ANISOU   49  N   VAL A  26    10361  10634   8643  -3996   -679   2932       N  
ATOM     50  CA  VAL A  26     -17.043  -8.259   7.647  1.00 76.13           C  
ANISOU   50  CA  VAL A  26    10443   9924   8557  -4107   -712   2714       C  
ATOM     51  C   VAL A  26     -17.806  -7.395   6.635  1.00 76.31           C  
ANISOU   51  C   VAL A  26    10250  10304   8442  -4146   -647   2410       C  
ATOM     52  O   VAL A  26     -17.312  -7.194   5.526  1.00 76.10           O  
ANISOU   52  O   VAL A  26    10344  10038   8533  -3919   -605   2111       O  
ATOM     53  CB  VAL A  26     -17.623  -9.702   7.771  1.00 79.85           C  
ANISOU   53  CB  VAL A  26    11238  10020   9083  -4595   -844   2951       C  
ATOM     54  CG1 VAL A  26     -17.841 -10.359   6.404  1.00 79.52           C  
ANISOU   54  CG1 VAL A  26    11517   9537   9160  -4764   -880   2687       C  
ATOM     55  CG2 VAL A  26     -16.732 -10.578   8.650  1.00 79.58           C  
ANISOU   55  CG2 VAL A  26    11466   9545   9226  -4485   -910   3248       C  
ATOM     56  N   ALA A  27     -18.985  -6.873   7.025  1.00 69.96           N  
ANISOU   56  N   ALA A  27     9110  10099   7373  -4411   -639   2496       N  
ATOM     57  CA  ALA A  27     -19.833  -6.031   6.179  1.00 68.65           C  
ANISOU   57  CA  ALA A  27     8695  10347   7041  -4452   -584   2260       C  
ATOM     58  C   ALA A  27     -19.158  -4.722   5.721  1.00 70.66           C  
ANISOU   58  C   ALA A  27     8777  10749   7323  -3949   -471   1990       C  
ATOM     59  O   ALA A  27     -19.220  -4.408   4.532  1.00 71.28           O  
ANISOU   59  O   ALA A  27     8880  10777   7425  -3874   -439   1727       O  
ATOM     60  CB  ALA A  27     -21.150  -5.741   6.876  1.00 69.25           C  
ANISOU   60  CB  ALA A  27     8420  11076   6818  -4780   -595   2446       C  
ATOM     61  N   ILE A  28     -18.494  -3.985   6.642  1.00 64.51           N  
ANISOU   61  N   ILE A  28     7834  10143   6534  -3627   -416   2058       N  
ATOM     62  CA  ILE A  28     -17.802  -2.724   6.342  1.00 62.89           C  
ANISOU   62  CA  ILE A  28     7481  10063   6353  -3178   -318   1830       C  
ATOM     63  C   ILE A  28     -16.574  -2.968   5.454  1.00 63.98           C  
ANISOU   63  C   ILE A  28     7901   9669   6737  -2903   -304   1642       C  
ATOM     64  O   ILE A  28     -16.387  -2.241   4.480  1.00 63.93           O  
ANISOU   64  O   ILE A  28     7851   9690   6750  -2706   -247   1391       O  
ATOM     65  CB  ILE A  28     -17.481  -1.905   7.638  1.00 66.04           C  
ANISOU   65  CB  ILE A  28     7634  10811   6648  -2965   -273   1951       C  
ATOM     66  CG1 ILE A  28     -18.766  -1.485   8.423  1.00 66.10           C  
ANISOU   66  CG1 ILE A  28     7307  11438   6369  -3188   -267   2084       C  
ATOM     67  CG2 ILE A  28     -16.572  -0.693   7.367  1.00 67.24           C  
ANISOU   67  CG2 ILE A  28     7699  10993   6858  -2521   -186   1724       C  
ATOM     68  CD1 ILE A  28     -19.919  -0.705   7.649  1.00 72.83           C  
ANISOU   68  CD1 ILE A  28     7925  12704   7043  -3255   -228   1914       C  
ATOM     69  N   ALA A  29     -15.768  -4.009   5.770  1.00 58.52           N  
ANISOU   69  N   ALA A  29     7496   8515   6224  -2889   -358   1774       N  
ATOM     70  CA  ALA A  29     -14.560  -4.401   5.023  1.00 57.43           C  
ANISOU   70  CA  ALA A  29     7634   7873   6314  -2611   -348   1617       C  
ATOM     71  C   ALA A  29     -14.840  -4.773   3.565  1.00 58.58           C  
ANISOU   71  C   ALA A  29     7961   7780   6516  -2715   -355   1363       C  
ATOM     72  O   ALA A  29     -14.014  -4.487   2.697  1.00 58.28           O  
ANISOU   72  O   ALA A  29     7998   7565   6582  -2424   -305   1133       O  
ATOM     73  CB  ALA A  29     -13.861  -5.557   5.720  1.00 58.22           C  
ANISOU   73  CB  ALA A  29     8006   7545   6571  -2608   -418   1846       C  
ATOM     74  N   THR A  30     -15.997  -5.415   3.310  1.00 52.54           N  
ANISOU   74  N   THR A  30     7254   7043   5665  -3146   -419   1408       N  
ATOM     75  CA  THR A  30     -16.448  -5.830   1.986  1.00 51.11           C  
ANISOU   75  CA  THR A  30     7232   6690   5496  -3330   -438   1176       C  
ATOM     76  C   THR A  30     -16.841  -4.606   1.154  1.00 52.37           C  
ANISOU   76  C   THR A  30     7108   7275   5516  -3209   -361    950       C  
ATOM     77  O   THR A  30     -16.348  -4.462   0.038  1.00 51.15           O  
ANISOU   77  O   THR A  30     7049   6952   5432  -3032   -326    696       O  
ATOM     78  CB  THR A  30     -17.572  -6.872   2.116  1.00 57.79           C  
ANISOU   78  CB  THR A  30     8211   7477   6271  -3871   -541   1327       C  
ATOM     79  OG1 THR A  30     -17.108  -7.950   2.932  1.00 57.02           O  
ANISOU   79  OG1 THR A  30     8398   6945   6323  -3946   -615   1564       O  
ATOM     80  CG2 THR A  30     -18.037  -7.414   0.771  1.00 55.83           C  
ANISOU   80  CG2 THR A  30     8154   7035   6024  -4110   -573   1079       C  
ATOM     81  N   VAL A  31     -17.707  -3.723   1.706  1.00 47.99           N  
ANISOU   81  N   VAL A  31     6204   7276   4756  -3284   -335   1050       N  
ATOM     82  CA  VAL A  31     -18.186  -2.498   1.047  1.00 47.43           C  
ANISOU   82  CA  VAL A  31     5847   7635   4540  -3155   -267    880       C  
ATOM     83  C   VAL A  31     -17.026  -1.535   0.757  1.00 50.19           C  
ANISOU   83  C   VAL A  31     6160   7915   4993  -2682   -186    725       C  
ATOM     84  O   VAL A  31     -16.892  -1.081  -0.378  1.00 50.35           O  
ANISOU   84  O   VAL A  31     6174   7937   5020  -2560   -150    510       O  
ATOM     85  CB  VAL A  31     -19.366  -1.810   1.792  1.00 51.61           C  
ANISOU   85  CB  VAL A  31     6016   8768   4823  -3300   -257   1027       C  
ATOM     86  CG1 VAL A  31     -19.824  -0.550   1.060  1.00 51.42           C  
ANISOU   86  CG1 VAL A  31     5728   9141   4668  -3124   -192    855       C  
ATOM     87  CG2 VAL A  31     -20.544  -2.765   1.962  1.00 51.58           C  
ANISOU   87  CG2 VAL A  31     6026   8883   4690  -3811   -342   1187       C  
ATOM     88  N   ALA A  32     -16.177  -1.252   1.760  1.00 45.63           N  
ANISOU   88  N   ALA A  32     5560   7289   4487  -2441   -162    840       N  
ATOM     89  CA  ALA A  32     -15.016  -0.371   1.588  1.00 44.94           C  
ANISOU   89  CA  ALA A  32     5438   7146   4489  -2032    -94    716       C  
ATOM     90  C   ALA A  32     -13.981  -0.976   0.631  1.00 48.00           C  
ANISOU   90  C   ALA A  32     6093   7088   5056  -1882    -92    554       C  
ATOM     91  O   ALA A  32     -13.378  -0.237  -0.149  1.00 47.93           O  
ANISOU   91  O   ALA A  32     6038   7103   5072  -1639    -37    377       O  
ATOM     92  CB  ALA A  32     -14.376  -0.066   2.927  1.00 45.17           C  
ANISOU   92  CB  ALA A  32     5389   7241   4533  -1866    -82    886       C  
ATOM     93  N   GLY A  33     -13.822  -2.304   0.687  1.00 43.34           N  
ANISOU   93  N   GLY A  33     5780   6107   4580  -2030   -154    618       N  
ATOM     94  CA  GLY A  33     -12.916  -3.071  -0.162  1.00 42.82           C  
ANISOU   94  CA  GLY A  33     6000   5589   4680  -1889   -157    459       C  
ATOM     95  C   GLY A  33     -13.313  -3.043  -1.625  1.00 46.58           C  
ANISOU   95  C   GLY A  33     6518   6065   5113  -1972   -144    197       C  
ATOM     96  O   GLY A  33     -12.459  -2.855  -2.492  1.00 46.37           O  
ANISOU   96  O   GLY A  33     6554   5912   5154  -1718    -98     -1       O  
ATOM     97  N   LEU A  34     -14.622  -3.208  -1.903  1.00 42.53           N  
ANISOU   97  N   LEU A  34     5947   5748   4465  -2337   -184    201       N  
ATOM     98  CA  LEU A  34     -15.193  -3.167  -3.249  1.00 42.00           C  
ANISOU   98  CA  LEU A  34     5881   5766   4312  -2476   -181    -28       C  
ATOM     99  C   LEU A  34     -15.111  -1.746  -3.831  1.00 43.61           C  
ANISOU   99  C   LEU A  34     5801   6353   4417  -2233   -103   -139       C  
ATOM    100  O   LEU A  34     -14.848  -1.584  -5.025  1.00 43.31           O  
ANISOU  100  O   LEU A  34     5792   6296   4368  -2145    -75   -355       O  
ATOM    101  CB  LEU A  34     -16.652  -3.660  -3.215  1.00 42.31           C  
ANISOU  101  CB  LEU A  34     5878   5999   4201  -2950   -249     55       C  
ATOM    102  CG  LEU A  34     -16.938  -5.114  -3.625  1.00 47.31           C  
ANISOU  102  CG  LEU A  34     6853   6228   4895  -3301   -336     11       C  
ATOM    103  CD1 LEU A  34     -16.194  -6.131  -2.757  1.00 47.85           C  
ANISOU  103  CD1 LEU A  34     7229   5781   5169  -3233   -378    151       C  
ATOM    104  CD2 LEU A  34     -18.415  -5.403  -3.550  1.00 49.58           C  
ANISOU  104  CD2 LEU A  34     7027   6815   4996  -3793   -404    138       C  
ATOM    105  N   LEU A  35     -15.316  -0.729  -2.979  1.00 38.20           N  
ANISOU  105  N   LEU A  35     4854   6005   3654  -2125    -72     10       N  
ATOM    106  CA  LEU A  35     -15.241   0.682  -3.344  1.00 37.15           C  
ANISOU  106  CA  LEU A  35     4473   6201   3440  -1889     -7    -57       C  
ATOM    107  C   LEU A  35     -13.807   1.035  -3.713  1.00 39.00           C  
ANISOU  107  C   LEU A  35     4786   6227   3805  -1541     44   -168       C  
ATOM    108  O   LEU A  35     -13.598   1.710  -4.716  1.00 38.50           O  
ANISOU  108  O   LEU A  35     4650   6273   3704  -1413     82   -313       O  
ATOM    109  CB  LEU A  35     -15.730   1.536  -2.168  1.00 37.58           C  
ANISOU  109  CB  LEU A  35     4287   6592   3400  -1851      8    122       C  
ATOM    110  CG  LEU A  35     -16.531   2.821  -2.423  1.00 42.59           C  
ANISOU  110  CG  LEU A  35     4635   7672   3874  -1776     45    102       C  
ATOM    111  CD1 LEU A  35     -17.321   2.784  -3.715  1.00 41.97           C  
ANISOU  111  CD1 LEU A  35     4510   7746   3690  -1920     34    -24       C  
ATOM    112  CD2 LEU A  35     -17.492   3.079  -1.257  1.00 46.11           C  
ANISOU  112  CD2 LEU A  35     4881   8458   4181  -1893     33    278       C  
ATOM    113  N   SER A  36     -12.818   0.530  -2.941  1.00 34.84           N  
ANISOU  113  N   SER A  36     4401   5418   3418  -1400     40    -88       N  
ATOM    114  CA  SER A  36     -11.386   0.737  -3.195  1.00 33.73           C  
ANISOU  114  CA  SER A  36     4325   5102   3391  -1076     84   -172       C  
ATOM    115  C   SER A  36     -10.987   0.086  -4.532  1.00 36.55           C  
ANISOU  115  C   SER A  36     4860   5234   3794  -1046     91   -395       C  
ATOM    116  O   SER A  36     -10.282   0.701  -5.332  1.00 36.02           O  
ANISOU  116  O   SER A  36     4730   5237   3719   -838    141   -528       O  
ATOM    117  CB  SER A  36     -10.551   0.164  -2.056  1.00 35.32           C  
ANISOU  117  CB  SER A  36     4631   5078   3709   -960     67    -17       C  
ATOM    118  OG  SER A  36      -9.167   0.286  -2.342  1.00 41.94           O  
ANISOU  118  OG  SER A  36     5515   5783   4638   -652    108    -97       O  
ATOM    119  N   LEU A  37     -11.470  -1.149  -4.768  1.00 31.96           N  
ANISOU  119  N   LEU A  37     4502   4394   3248  -1273     37   -437       N  
ATOM    120  CA  LEU A  37     -11.228  -1.931  -5.970  1.00 31.24           C  
ANISOU  120  CA  LEU A  37     4617   4064   3190  -1283     35   -674       C  
ATOM    121  C   LEU A  37     -11.768  -1.180  -7.199  1.00 34.98           C  
ANISOU  121  C   LEU A  37     4923   4858   3511  -1345     65   -841       C  
ATOM    122  O   LEU A  37     -11.080  -1.129  -8.214  1.00 34.79           O  
ANISOU  122  O   LEU A  37     4934   4799   3486  -1175    106  -1037       O  
ATOM    123  CB  LEU A  37     -11.870  -3.326  -5.818  1.00 31.36           C  
ANISOU  123  CB  LEU A  37     4912   3746   3259  -1585    -43   -663       C  
ATOM    124  CG  LEU A  37     -11.768  -4.277  -7.005  1.00 37.07           C  
ANISOU  124  CG  LEU A  37     5891   4190   4003  -1657    -58   -938       C  
ATOM    125  CD1 LEU A  37     -10.383  -4.933  -7.087  1.00 37.77           C  
ANISOU  125  CD1 LEU A  37     6208   3888   4256  -1305    -30  -1053       C  
ATOM    126  CD2 LEU A  37     -12.872  -5.316  -6.957  1.00 39.73           C  
ANISOU  126  CD2 LEU A  37     6432   4343   4322  -2094   -147   -920       C  
ATOM    127  N   ALA A  38     -12.969  -0.564  -7.088  1.00 30.70           N  
ANISOU  127  N   ALA A  38     4178   4662   2826  -1565     48   -751       N  
ATOM    128  CA  ALA A  38     -13.595   0.226  -8.157  1.00 29.75           C  
ANISOU  128  CA  ALA A  38     3867   4893   2545  -1621     68   -858       C  
ATOM    129  C   ALA A  38     -12.826   1.544  -8.424  1.00 33.31           C  
ANISOU  129  C   ALA A  38     4128   5546   2983  -1301    135   -862       C  
ATOM    130  O   ALA A  38     -12.760   1.994  -9.568  1.00 32.22           O  
ANISOU  130  O   ALA A  38     3918   5564   2762  -1249    162   -997       O  
ATOM    131  CB  ALA A  38     -15.054   0.509  -7.814  1.00 30.12           C  
ANISOU  131  CB  ALA A  38     3731   5271   2441  -1901     30   -728       C  
ATOM    132  N   THR A  39     -12.223   2.137  -7.368  1.00 30.52           N  
ANISOU  132  N   THR A  39     3705   5186   2705  -1107    157   -710       N  
ATOM    133  CA  THR A  39     -11.444   3.383  -7.443  1.00 30.19           C  
ANISOU  133  CA  THR A  39     3511   5297   2663   -838    210   -691       C  
ATOM    134  C   THR A  39     -10.075   3.148  -8.082  1.00 34.55           C  
ANISOU  134  C   THR A  39     4168   5669   3293   -619    247   -823       C  
ATOM    135  O   THR A  39      -9.676   3.911  -8.966  1.00 34.40           O  
ANISOU  135  O   THR A  39     4044   5813   3213   -503    283   -898       O  
ATOM    136  CB  THR A  39     -11.331   4.045  -6.061  1.00 33.47           C  
ANISOU  136  CB  THR A  39     3826   5778   3112   -748    214   -505       C  
ATOM    137  OG1 THR A  39     -12.619   4.079  -5.460  1.00 33.86           O  
ANISOU  137  OG1 THR A  39     3782   6010   3073   -950    181   -397       O  
ATOM    138  CG2 THR A  39     -10.781   5.459  -6.134  1.00 28.08           C  
ANISOU  138  CG2 THR A  39     2989   5273   2407   -536    255   -484       C  
ATOM    139  N   VAL A  40      -9.356   2.106  -7.628  1.00 31.10           N  
ANISOU  139  N   VAL A  40     3923   4914   2978   -554    237   -836       N  
ATOM    140  CA  VAL A  40      -8.042   1.766  -8.172  1.00 30.93           C  
ANISOU  140  CA  VAL A  40     3992   4739   3021   -314    276   -964       C  
ATOM    141  C   VAL A  40      -8.165   1.320  -9.652  1.00 35.76           C  
ANISOU  141  C   VAL A  40     4676   5352   3559   -365    288  -1205       C  
ATOM    142  O   VAL A  40      -7.365   1.772 -10.481  1.00 36.95           O  
ANISOU  142  O   VAL A  40     4749   5628   3662   -189    336  -1312       O  
ATOM    143  CB  VAL A  40      -7.202   0.790  -7.299  1.00 34.59           C  
ANISOU  143  CB  VAL A  40     4633   4878   3632   -172    263   -903       C  
ATOM    144  CG1 VAL A  40      -6.914   1.392  -5.937  1.00 33.87           C  
ANISOU  144  CG1 VAL A  40     4423   4870   3577    -95    260   -679       C  
ATOM    145  CG2 VAL A  40      -7.861  -0.570  -7.141  1.00 34.88           C  
ANISOU  145  CG2 VAL A  40     4920   4598   3736   -368    206   -922       C  
ATOM    146  N   THR A  41      -9.209   0.519  -9.990  1.00 30.33           N  
ANISOU  146  N   THR A  41     4112   4575   2835   -634    242  -1285       N  
ATOM    147  CA  THR A  41      -9.452   0.045 -11.352  1.00 29.74           C  
ANISOU  147  CA  THR A  41     4112   4519   2668   -730    245  -1531       C  
ATOM    148  C   THR A  41      -9.777   1.200 -12.311  1.00 34.27           C  
ANISOU  148  C   THR A  41     4436   5509   3074   -741    275  -1559       C  
ATOM    149  O   THR A  41      -9.124   1.321 -13.349  1.00 36.13           O  
ANISOU  149  O   THR A  41     4644   5836   3247   -608    317  -1721       O  
ATOM    150  CB  THR A  41     -10.508  -1.071 -11.362  1.00 32.13           C  
ANISOU  150  CB  THR A  41     4611   4632   2966  -1060    178  -1592       C  
ATOM    151  OG1 THR A  41     -10.089  -2.098 -10.459  1.00 27.66           O  
ANISOU  151  OG1 THR A  41     4294   3645   2570  -1023    147  -1536       O  
ATOM    152  CG2 THR A  41     -10.729  -1.665 -12.758  1.00 30.08           C  
ANISOU  152  CG2 THR A  41     4456   4372   2602  -1180    177  -1881       C  
ATOM    153  N   GLY A  42     -10.757   2.024 -11.944  1.00 28.54           N  
ANISOU  153  N   GLY A  42     3528   5041   2274   -882    253  -1394       N  
ATOM    154  CA  GLY A  42     -11.217   3.164 -12.732  1.00 27.34           C  
ANISOU  154  CA  GLY A  42     3143   5276   1970   -891    268  -1370       C  
ATOM    155  C   GLY A  42     -10.171   4.213 -13.052  1.00 29.67           C  
ANISOU  155  C   GLY A  42     3310   5700   2263   -629    321  -1337       C  
ATOM    156  O   GLY A  42     -10.140   4.715 -14.176  1.00 29.32           O  
ANISOU  156  O   GLY A  42     3157   5888   2095   -613    340  -1411       O  
ATOM    157  N   ASN A  43      -9.316   4.567 -12.074  1.00 25.66           N  
ANISOU  157  N   ASN A  43     2806   5069   1877   -445    340  -1216       N  
ATOM    158  CA  ASN A  43      -8.277   5.572 -12.291  1.00 25.56           C  
ANISOU  158  CA  ASN A  43     2675   5178   1859   -234    382  -1168       C  
ATOM    159  C   ASN A  43      -7.084   5.017 -13.064  1.00 31.97           C  
ANISOU  159  C   ASN A  43     3554   5922   2671    -79    424  -1337       C  
ATOM    160  O   ASN A  43      -6.450   5.765 -13.810  1.00 31.70           O  
ANISOU  160  O   ASN A  43     3393   6095   2557     21    457  -1344       O  
ATOM    161  CB  ASN A  43      -7.873   6.251 -10.997  1.00 21.15           C  
ANISOU  161  CB  ASN A  43     2073   4567   1397   -129    382   -985       C  
ATOM    162  CG  ASN A  43      -8.968   7.142 -10.472  1.00 27.73           C  
ANISOU  162  CG  ASN A  43     2790   5560   2188   -223    356   -840       C  
ATOM    163  OD1 ASN A  43      -9.242   8.238 -10.994  1.00 14.03           O  
ANISOU  163  OD1 ASN A  43      804   3864    662   -236    172   -700       O  
ATOM    164  ND2 ASN A  43      -9.636   6.686  -9.430  1.00 21.24           N  
ANISOU  164  ND2 ASN A  43     2013   4644   1412   -319    327   -766       N  
ATOM    165  N   ILE A  44      -6.806   3.702 -12.928  1.00 30.48           N  
ANISOU  165  N   ILE A  44     3565   5455   2562    -58    420  -1471       N  
ATOM    166  CA  ILE A  44      -5.760   3.012 -13.701  1.00 30.82           C  
ANISOU  166  CA  ILE A  44     3690   5426   2594    117    463  -1671       C  
ATOM    167  C   ILE A  44      -6.210   2.955 -15.172  1.00 34.29           C  
ANISOU  167  C   ILE A  44     4089   6074   2867      9    474  -1863       C  
ATOM    168  O   ILE A  44      -5.414   3.248 -16.057  1.00 33.14           O  
ANISOU  168  O   ILE A  44     3847   6122   2625    148    521  -1958       O  
ATOM    169  CB  ILE A  44      -5.396   1.621 -13.096  1.00 33.99           C  
ANISOU  169  CB  ILE A  44     4348   5428   3140    194    450  -1755       C  
ATOM    170  CG1 ILE A  44      -4.337   1.775 -11.988  1.00 34.20           C  
ANISOU  170  CG1 ILE A  44     4354   5356   3286    422    465  -1595       C  
ATOM    171  CG2 ILE A  44      -4.963   0.601 -14.174  1.00 34.49           C  
ANISOU  171  CG2 ILE A  44     4564   5377   3162    283    477  -2050       C  
ATOM    172  CD1 ILE A  44      -4.220   0.601 -11.017  1.00 42.29           C  
ANISOU  172  CD1 ILE A  44     5607   5992   4468    464    431  -1561       C  
ATOM    173  N   LEU A  45      -7.501   2.641 -15.412  1.00 31.90           N  
ANISOU  173  N   LEU A  45     3830   5784   2507   -254    428  -1902       N  
ATOM    174  CA  LEU A  45      -8.130   2.600 -16.734  1.00 32.11           C  
ANISOU  174  CA  LEU A  45     3801   6048   2352   -409    425  -2066       C  
ATOM    175  C   LEU A  45      -8.075   3.974 -17.392  1.00 35.95           C  
ANISOU  175  C   LEU A  45     4021   6939   2700   -369    447  -1945       C  
ATOM    176  O   LEU A  45      -7.870   4.058 -18.596  1.00 36.90           O  
ANISOU  176  O   LEU A  45     4063   7292   2666   -362    473  -2083       O  
ATOM    177  CB  LEU A  45      -9.593   2.174 -16.588  1.00 32.53           C  
ANISOU  177  CB  LEU A  45     3910   6083   2369   -724    361  -2059       C  
ATOM    178  CG  LEU A  45      -9.984   0.822 -17.123  1.00 38.04           C  
ANISOU  178  CG  LEU A  45     4838   6572   3043   -896    335  -2320       C  
ATOM    179  CD1 LEU A  45      -9.362  -0.316 -16.316  1.00 38.90           C  
ANISOU  179  CD1 LEU A  45     5232   6195   3353   -806    325  -2369       C  
ATOM    180  CD2 LEU A  45     -11.482   0.695 -17.107  1.00 40.16           C  
ANISOU  180  CD2 LEU A  45     5071   6979   3208  -1249    271  -2284       C  
ATOM    181  N   LEU A  46      -8.260   5.045 -16.607  1.00 31.74           N  
ANISOU  181  N   LEU A  46     3358   6483   2217   -343    434  -1689       N  
ATOM    182  CA  LEU A  46      -8.226   6.422 -17.086  1.00 31.13           C  
ANISOU  182  CA  LEU A  46     3064   6723   2040   -302    443  -1534       C  
ATOM    183  C   LEU A  46      -6.797   6.793 -17.508  1.00 35.87           C  
ANISOU  183  C   LEU A  46     3604   7402   2624   -101    495  -1553       C  
ATOM    184  O   LEU A  46      -6.610   7.377 -18.579  1.00 34.75           O  
ANISOU  184  O   LEU A  46     3322   7552   2331   -100    512  -1557       O  
ATOM    185  CB  LEU A  46      -8.768   7.368 -15.987  1.00 30.80           C  
ANISOU  185  CB  LEU A  46     2954   6668   2080   -307    414  -1285       C  
ATOM    186  CG  LEU A  46      -9.130   8.794 -16.405  1.00 35.21           C  
ANISOU  186  CG  LEU A  46     3327   7506   2547   -296    403  -1107       C  
ATOM    187  CD1 LEU A  46     -10.365   8.824 -17.286  1.00 35.59           C  
ANISOU  187  CD1 LEU A  46     3278   7813   2433   -459    373  -1124       C  
ATOM    188  CD2 LEU A  46      -9.395   9.652 -15.201  1.00 37.39           C  
ANISOU  188  CD2 LEU A  46     3580   7699   2928   -241    385   -907       C  
ATOM    189  N   MET A  47      -5.792   6.407 -16.684  1.00 33.53           N  
ANISOU  189  N   MET A  47     3400   6877   2464     61    519  -1558       N  
ATOM    190  CA  MET A  47      -4.367   6.669 -16.924  1.00 33.19           C  
ANISOU  190  CA  MET A  47     3284   6925   2400    256    568  -1567       C  
ATOM    191  C   MET A  47      -3.836   5.890 -18.128  1.00 38.65           C  
ANISOU  191  C   MET A  47     3989   7730   2966    327    612  -1822       C  
ATOM    192  O   MET A  47      -3.174   6.471 -18.983  1.00 39.16           O  
ANISOU  192  O   MET A  47     3895   8094   2892    384    646  -1820       O  
ATOM    193  CB  MET A  47      -3.546   6.387 -15.667  1.00 34.94           C  
ANISOU  193  CB  MET A  47     3587   6902   2787    406    575  -1498       C  
ATOM    194  CG  MET A  47      -3.518   7.552 -14.717  1.00 38.08           C  
ANISOU  194  CG  MET A  47     3897   7323   3249    389    551  -1251       C  
ATOM    195  SD  MET A  47      -3.057   7.111 -13.020  1.00 41.79           S  
ANISOU  195  SD  MET A  47     4475   7501   3904    493    539  -1158       S  
ATOM    196  CE  MET A  47      -1.305   6.680 -13.238  1.00 38.35           C  
ANISOU  196  CE  MET A  47     3989   7137   3445    744    595  -1235       C  
ATOM    197  N   LEU A  48      -4.164   4.595 -18.214  1.00 35.44           N  
ANISOU  197  N   LEU A  48     3775   7092   2597    309    609  -2042       N  
ATOM    198  CA  LEU A  48      -3.781   3.725 -19.319  1.00 35.55           C  
ANISOU  198  CA  LEU A  48     3846   7166   2494    380    649  -2336       C  
ATOM    199  C   LEU A  48      -4.429   4.138 -20.635  1.00 40.15           C  
ANISOU  199  C   LEU A  48     4291   8108   2855    212    647  -2411       C  
ATOM    200  O   LEU A  48      -3.797   3.964 -21.673  1.00 39.40           O  
ANISOU  200  O   LEU A  48     4126   8239   2604    306    695  -2590       O  
ATOM    201  CB  LEU A  48      -4.151   2.276 -18.985  1.00 35.69           C  
ANISOU  201  CB  LEU A  48     4152   6780   2627    359    628  -2540       C  
ATOM    202  CG  LEU A  48      -3.024   1.309 -18.685  1.00 40.58           C  
ANISOU  202  CG  LEU A  48     4928   7143   3347    645    669  -2692       C  
ATOM    203  CD1 LEU A  48      -2.383   0.822 -19.970  1.00 40.91           C  
ANISOU  203  CD1 LEU A  48     4961   7359   3223    785    728  -2999       C  
ATOM    204  CD2 LEU A  48      -2.005   1.880 -17.677  1.00 42.65           C  
ANISOU  204  CD2 LEU A  48     5081   7411   3713    859    690  -2464       C  
ATOM    205  N   SER A  49      -5.684   4.683 -20.593  1.00 37.57           N  
ANISOU  205  N   SER A  49     3908   7871   2497    -22    592  -2270       N  
ATOM    206  CA  SER A  49      -6.431   5.152 -21.773  1.00 37.61           C  
ANISOU  206  CA  SER A  49     3759   8248   2284   -192    577  -2290       C  
ATOM    207  C   SER A  49      -5.701   6.268 -22.507  1.00 43.82           C  
ANISOU  207  C   SER A  49     4309   9412   2929   -104    610  -2156       C  
ATOM    208  O   SER A  49      -5.551   6.189 -23.728  1.00 44.56           O  
ANISOU  208  O   SER A  49     4302   9814   2815   -128    635  -2297       O  
ATOM    209  CB  SER A  49      -7.838   5.608 -21.402  1.00 39.19           C  
ANISOU  209  CB  SER A  49     3919   8480   2491   -410    512  -2116       C  
ATOM    210  OG  SER A  49      -8.687   4.494 -21.186  1.00 44.85           O  
ANISOU  210  OG  SER A  49     4818   8979   3244   -581    476  -2281       O  
ATOM    211  N   ILE A  50      -5.221   7.286 -21.758  1.00 40.82           N  
ANISOU  211  N   ILE A  50     3848   9011   2652    -18    606  -1888       N  
ATOM    212  CA  ILE A  50      -4.462   8.424 -22.284  1.00 40.59           C  
ANISOU  212  CA  ILE A  50     3617   9291   2515     38    625  -1712       C  
ATOM    213  C   ILE A  50      -3.101   7.929 -22.821  1.00 47.45           C  
ANISOU  213  C   ILE A  50     4446  10284   3297    211    694  -1886       C  
ATOM    214  O   ILE A  50      -2.664   8.380 -23.888  1.00 47.97           O  
ANISOU  214  O   ILE A  50     4335  10729   3161    204    720  -1879       O  
ATOM    215  CB  ILE A  50      -4.351   9.577 -21.246  1.00 42.73           C  
ANISOU  215  CB  ILE A  50     3856   9449   2931     58    594  -1404       C  
ATOM    216  CG1 ILE A  50      -5.745   9.943 -20.678  1.00 43.01           C  
ANISOU  216  CG1 ILE A  50     3932   9368   3041    -69    534  -1270       C  
ATOM    217  CG2 ILE A  50      -3.678  10.811 -21.851  1.00 42.38           C  
ANISOU  217  CG2 ILE A  50     3626   9707   2769     59    598  -1199       C  
ATOM    218  CD1 ILE A  50      -5.724  10.581 -19.292  1.00 49.55           C  
ANISOU  218  CD1 ILE A  50     4818   9950   4061    -20    510  -1074       C  
ATOM    219  N   LYS A  51      -2.492   6.940 -22.126  1.00 44.54           N  
ANISOU  219  N   LYS A  51     4236   9621   3067    370    723  -2046       N  
ATOM    220  CA  LYS A  51      -1.225   6.305 -22.492  1.00 44.61           C  
ANISOU  220  CA  LYS A  51     4225   9711   3012    592    793  -2236       C  
ATOM    221  C   LYS A  51      -1.306   5.493 -23.834  1.00 51.67           C  
ANISOU  221  C   LYS A  51     5118  10814   3698    599    832  -2560       C  
ATOM    222  O   LYS A  51      -0.476   5.701 -24.725  1.00 50.70           O  
ANISOU  222  O   LYS A  51     4820  11062   3382    695    885  -2623       O  
ATOM    223  CB  LYS A  51      -0.749   5.423 -21.324  1.00 45.74           C  
ANISOU  223  CB  LYS A  51     4564   9443   3374    770    800  -2300       C  
ATOM    224  CG  LYS A  51       0.715   5.019 -21.387  1.00 54.69           C  
ANISOU  224  CG  LYS A  51     5639  10670   4471   1055    868  -2405       C  
ATOM    225  CD  LYS A  51       0.975   3.743 -20.587  1.00 59.58           C  
ANISOU  225  CD  LYS A  51     6501  10863   5275   1253    876  -2560       C  
ATOM    226  CE  LYS A  51       2.296   3.089 -20.930  1.00 56.33           C  
ANISOU  226  CE  LYS A  51     6048  10568   4789   1581    951  -2747       C  
ATOM    227  NZ  LYS A  51       2.272   1.619 -20.682  1.00 55.22           N  
ANISOU  227  NZ  LYS A  51     6197  10010   4776   1764    959  -3008       N  
ATOM    228  N   VAL A  52      -2.324   4.607 -23.976  1.00 50.61           N  
ANISOU  228  N   VAL A  52     5172  10470   3588    475    803  -2763       N  
ATOM    229  CA  VAL A  52      -2.532   3.696 -25.119  1.00 51.00           C  
ANISOU  229  CA  VAL A  52     5280  10640   3458    452    829  -3117       C  
ATOM    230  C   VAL A  52      -3.200   4.380 -26.352  1.00 57.23           C  
ANISOU  230  C   VAL A  52     5859  11903   3981    238    814  -3086       C  
ATOM    231  O   VAL A  52      -2.880   4.017 -27.491  1.00 57.12           O  
ANISOU  231  O   VAL A  52     5774  12187   3742    272    859  -3332       O  
ATOM    232  CB  VAL A  52      -3.295   2.416 -24.652  1.00 54.76           C  
ANISOU  232  CB  VAL A  52     6077  10646   4084    377    793  -3340       C  
ATOM    233  CG1 VAL A  52      -3.764   1.555 -25.820  1.00 54.90           C  
ANISOU  233  CG1 VAL A  52     6179  10770   3911    266    801  -3705       C  
ATOM    234  CG2 VAL A  52      -2.436   1.584 -23.705  1.00 54.44           C  
ANISOU  234  CG2 VAL A  52     6240  10187   4257    642    819  -3418       C  
ATOM    235  N   ASN A  53      -4.119   5.335 -26.136  1.00 54.96           N  
ANISOU  235  N   ASN A  53     5473  11700   3709     37    752  -2794       N  
ATOM    236  CA  ASN A  53      -4.801   6.031 -27.231  1.00 55.06           C  
ANISOU  236  CA  ASN A  53     5282  12160   3480   -151    728  -2712       C  
ATOM    237  C   ASN A  53      -4.153   7.384 -27.519  1.00 60.29           C  
ANISOU  237  C   ASN A  53     5691  13164   4051   -109    737  -2400       C  
ATOM    238  O   ASN A  53      -3.996   8.194 -26.602  1.00 60.61           O  
ANISOU  238  O   ASN A  53     5726  13040   4264    -75    712  -2115       O  
ATOM    239  CB  ASN A  53      -6.287   6.208 -26.905  1.00 57.99           C  
ANISOU  239  CB  ASN A  53     5694  12440   3901   -384    649  -2585       C  
ATOM    240  CG  ASN A  53      -7.186   6.504 -28.082  1.00 85.92           C  
ANISOU  240  CG  ASN A  53     9062  16410   7172   -589    618  -2589       C  
ATOM    241  OD1 ASN A  53      -6.830   7.205 -29.036  1.00 84.27           O  
ANISOU  241  OD1 ASN A  53     8635  16631   6754   -583    635  -2496       O  
ATOM    242  ND2 ASN A  53      -8.398   5.984 -28.023  1.00 77.56           N  
ANISOU  242  ND2 ASN A  53     8089  15276   6103   -793    565  -2676       N  
ATOM    243  N   ARG A  54      -3.780   7.627 -28.794  1.00 57.96           N  
ANISOU  243  N   ARG A  54     5197  13350   3477   -128    769  -2454       N  
ATOM    244  CA  ARG A  54      -3.158   8.875 -29.260  1.00 57.98           C  
ANISOU  244  CA  ARG A  54     4951  13728   3350   -130    773  -2153       C  
ATOM    245  C   ARG A  54      -4.184  10.034 -29.355  1.00 60.86           C  
ANISOU  245  C   ARG A  54     5213  14213   3696   -312    694  -1802       C  
ATOM    246  O   ARG A  54      -3.833  11.177 -29.061  1.00 60.41           O  
ANISOU  246  O   ARG A  54     5070  14189   3695   -309    669  -1470       O  
ATOM    247  CB  ARG A  54      -2.411   8.661 -30.592  1.00 59.95           C  
ANISOU  247  CB  ARG A  54     5011  14482   3285    -89    836  -2330       C  
ATOM    248  CG  ARG A  54      -1.375   9.744 -30.906  1.00 75.89           C  
ANISOU  248  CG  ARG A  54     6792  16854   5189    -63    853  -2038       C  
ATOM    249  CD  ARG A  54       0.014   9.176 -31.167  1.00 91.78           C  
ANISOU  249  CD  ARG A  54     8725  19058   7091    142    944  -2247       C  
ATOM    250  NE  ARG A  54       0.235   8.868 -32.584  1.00108.61           N  
ANISOU  250  NE  ARG A  54    10672  21724   8871    128    994  -2460       N  
ATOM    251  CZ  ARG A  54       1.433   8.687 -33.139  1.00122.49           C  
ANISOU  251  CZ  ARG A  54    12261  23850  10429    282   1075  -2592       C  
ATOM    252  NH1 ARG A  54       2.535   8.781 -32.404  1.00111.25           N  
ANISOU  252  NH1 ARG A  54    10820  22327   9122    459   1112  -2519       N  
ATOM    253  NH2 ARG A  54       1.537   8.412 -34.434  1.00100.90           N  
ANISOU  253  NH2 ARG A  54     9353  21628   7356    261   1120  -2796       N  
ATOM    254  N   GLN A  55      -5.448   9.736 -29.731  1.00 56.50           N  
ANISOU  254  N   GLN A  55     4680  13718   3067   -467    650  -1875       N  
ATOM    255  CA  GLN A  55      -6.524  10.737 -29.839  1.00 55.84           C  
ANISOU  255  CA  GLN A  55     4493  13770   2954   -603    575  -1558       C  
ATOM    256  C   GLN A  55      -6.912  11.321 -28.469  1.00 58.59           C  
ANISOU  256  C   GLN A  55     4967  13701   3595   -560    531  -1319       C  
ATOM    257  O   GLN A  55      -7.521  12.393 -28.412  1.00 59.82           O  
ANISOU  257  O   GLN A  55     5039  13930   3760   -600    475  -1006       O  
ATOM    258  CB  GLN A  55      -7.765  10.168 -30.566  1.00 57.27           C  
ANISOU  258  CB  GLN A  55     4635  14174   2950   -782    540  -1713       C  
ATOM    259  CG  GLN A  55      -7.542   9.788 -32.035  1.00 74.19           C  
ANISOU  259  CG  GLN A  55     6618  16816   4754   -852    574  -1919       C  
ATOM    260  CD  GLN A  55      -7.197  10.964 -32.922  1.00 99.06           C  
ANISOU  260  CD  GLN A  55     9510  20424   7704   -860    568  -1615       C  
ATOM    261  OE1 GLN A  55      -8.070  11.751 -33.309  1.00 97.11           O  
ANISOU  261  OE1 GLN A  55     9121  20417   7359   -962    504  -1326       O  
ATOM    262  NE2 GLN A  55      -5.917  11.101 -33.273  1.00 88.41           N  
ANISOU  262  NE2 GLN A  55     8088  19224   6279   -751    631  -1659       N  
ATOM    263  N   LEU A  56      -6.549  10.615 -27.373  1.00 51.17           N  
ANISOU  263  N   LEU A  56     4227  12332   2884   -463    555  -1467       N  
ATOM    264  CA  LEU A  56      -6.790  11.042 -25.999  1.00 48.70           C  
ANISOU  264  CA  LEU A  56     4036  11631   2837   -411    524  -1285       C  
ATOM    265  C   LEU A  56      -5.618  11.834 -25.454  1.00 49.60           C  
ANISOU  265  C   LEU A  56     4133  11650   3061   -289    542  -1096       C  
ATOM    266  O   LEU A  56      -5.740  12.426 -24.390  1.00 48.52           O  
ANISOU  266  O   LEU A  56     4073  11245   3116   -253    512   -914       O  
ATOM    267  CB  LEU A  56      -7.095   9.836 -25.089  1.00 48.22           C  
ANISOU  267  CB  LEU A  56     4192  11183   2948   -401    531  -1520       C  
ATOM    268  CG  LEU A  56      -8.439   9.126 -25.318  1.00 51.63           C  
ANISOU  268  CG  LEU A  56     4668  11635   3312   -576    493  -1660       C  
ATOM    269  CD1 LEU A  56      -8.541   7.900 -24.463  1.00 51.59           C  
ANISOU  269  CD1 LEU A  56     4897  11229   3475   -581    498  -1880       C  
ATOM    270  CD2 LEU A  56      -9.625  10.050 -25.046  1.00 51.63           C  
ANISOU  270  CD2 LEU A  56     4573  11727   3317   -660    429  -1384       C  
ATOM    271  N   GLN A  57      -4.489  11.865 -26.182  1.00 45.51           N  
ANISOU  271  N   GLN A  57     3506  11383   2403   -238    590  -1143       N  
ATOM    272  CA  GLN A  57      -3.281  12.581 -25.768  1.00 45.20           C  
ANISOU  272  CA  GLN A  57     3422  11325   2426   -158    607   -970       C  
ATOM    273  C   GLN A  57      -3.355  14.098 -26.031  1.00 48.82           C  
ANISOU  273  C   GLN A  57     3765  11946   2840   -250    553   -596       C  
ATOM    274  O   GLN A  57      -2.482  14.669 -26.677  1.00 49.09           O  
ANISOU  274  O   GLN A  57     3653  12267   2730   -279    567   -473       O  
ATOM    275  CB  GLN A  57      -2.031  11.949 -26.395  1.00 46.57           C  
ANISOU  275  CB  GLN A  57     3507  11734   2453    -60    682  -1172       C  
ATOM    276  CG  GLN A  57      -1.421  10.842 -25.563  1.00 60.34           C  
ANISOU  276  CG  GLN A  57     5405  13173   4350    109    729  -1421       C  
ATOM    277  CD  GLN A  57      -0.581   9.907 -26.391  1.00 78.17           C  
ANISOU  277  CD  GLN A  57     7598  15673   6431    236    806  -1718       C  
ATOM    278  OE1 GLN A  57       0.247  10.320 -27.219  1.00 73.93           O  
ANISOU  278  OE1 GLN A  57     6856  15548   5685    247    841  -1671       O  
ATOM    279  NE2 GLN A  57      -0.776   8.615 -26.176  1.00 68.51           N  
ANISOU  279  NE2 GLN A  57     6553  14196   5281    337    833  -2032       N  
ATOM    280  N   THR A  58      -4.376  14.749 -25.482  1.00 44.84           N  
ANISOU  280  N   THR A  58     3332  11245   2460   -288    491   -411       N  
ATOM    281  CA  THR A  58      -4.610  16.191 -25.587  1.00 43.70           C  
ANISOU  281  CA  THR A  58     3137  11149   2319   -344    430    -54       C  
ATOM    282  C   THR A  58      -4.117  16.900 -24.304  1.00 45.02           C  
ANISOU  282  C   THR A  58     3437  10950   2718   -295    408     98       C  
ATOM    283  O   THR A  58      -4.121  16.288 -23.230  1.00 43.87           O  
ANISOU  283  O   THR A  58     3423  10502   2744   -220    427    -51       O  
ATOM    284  CB  THR A  58      -6.115  16.447 -25.798  1.00 50.28           C  
ANISOU  284  CB  THR A  58     3960  12017   3127   -378    376     37       C  
ATOM    285  OG1 THR A  58      -6.844  15.940 -24.673  1.00 52.53           O  
ANISOU  285  OG1 THR A  58     4393  11966   3601   -323    370    -80       O  
ATOM    286  CG2 THR A  58      -6.644  15.807 -27.059  1.00 46.99           C  
ANISOU  286  CG2 THR A  58     3400  11997   2457   -459    387   -102       C  
ATOM    287  N   VAL A  59      -3.751  18.200 -24.418  1.00 39.96           N  
ANISOU  287  N   VAL A  59     2771  10335   2075   -354    362    400       N  
ATOM    288  CA  VAL A  59      -3.297  19.081 -23.324  1.00 39.01           C  
ANISOU  288  CA  VAL A  59     2781   9891   2148   -347    329    564       C  
ATOM    289  C   VAL A  59      -4.259  19.042 -22.109  1.00 42.77           C  
ANISOU  289  C   VAL A  59     3423   9991   2837   -251    307    518       C  
ATOM    290  O   VAL A  59      -3.788  18.966 -20.972  1.00 42.62           O  
ANISOU  290  O   VAL A  59     3515   9704   2975   -211    316    461       O  
ATOM    291  CB  VAL A  59      -3.024  20.536 -23.812  1.00 42.48           C  
ANISOU  291  CB  VAL A  59     3197  10405   2540   -455    265    912       C  
ATOM    292  CG1 VAL A  59      -2.501  21.432 -22.694  1.00 42.08           C  
ANISOU  292  CG1 VAL A  59     3305  10003   2680   -476    226   1050       C  
ATOM    293  CG2 VAL A  59      -2.059  20.555 -24.984  1.00 42.26           C  
ANISOU  293  CG2 VAL A  59     2980  10800   2279   -571    288    972       C  
ATOM    294  N   ASN A  60      -5.587  19.065 -22.336  1.00 39.08           N  
ANISOU  294  N   ASN A  60     2951   9547   2352   -217    278    542       N  
ATOM    295  CA  ASN A  60      -6.537  19.008 -21.217  1.00 38.87           C  
ANISOU  295  CA  ASN A  60     3046   9231   2492   -125    262    499       C  
ATOM    296  C   ASN A  60      -6.552  17.635 -20.520  1.00 42.63           C  
ANISOU  296  C   ASN A  60     3573   9590   3034    -98    312    213       C  
ATOM    297  O   ASN A  60      -6.817  17.570 -19.315  1.00 43.31           O  
ANISOU  297  O   ASN A  60     3773   9403   3280    -38    309    177       O  
ATOM    298  CB  ASN A  60      -7.955  19.454 -21.613  1.00 38.51           C  
ANISOU  298  CB  ASN A  60     2952   9287   2391    -85    217    624       C  
ATOM    299  CG  ASN A  60      -8.830  19.798 -20.406  1.00 56.28           C  
ANISOU  299  CG  ASN A  60     5316  11261   4806     32    193    648       C  
ATOM    300  OD1 ASN A  60      -9.424  18.929 -19.754  1.00 43.80           O  
ANISOU  300  OD1 ASN A  60     3755   9618   3270     52    216    473       O  
ATOM    301  ND2 ASN A  60      -8.920  21.076 -20.060  1.00 45.55           N  
ANISOU  301  ND2 ASN A  60     4041   9727   3536    108    146    864       N  
ATOM    302  N   ASN A  61      -6.234  16.549 -21.263  1.00 37.18           N  
ANISOU  302  N   ASN A  61     2810   9097   2218   -139    357     12       N  
ATOM    303  CA  ASN A  61      -6.197  15.194 -20.705  1.00 35.73           C  
ANISOU  303  CA  ASN A  61     2704   8772   2099   -113    399   -254       C  
ATOM    304  C   ASN A  61      -4.934  14.920 -19.869  1.00 37.63           C  
ANISOU  304  C   ASN A  61     3018   8822   2458    -48    433   -318       C  
ATOM    305  O   ASN A  61      -4.877  13.913 -19.154  1.00 37.64           O  
ANISOU  305  O   ASN A  61     3112   8635   2553      0    459   -492       O  
ATOM    306  CB  ASN A  61      -6.418  14.141 -21.774  1.00 33.11           C  
ANISOU  306  CB  ASN A  61     2304   8679   1599   -170    428   -467       C  
ATOM    307  CG  ASN A  61      -7.875  13.915 -22.109  1.00 50.15           C  
ANISOU  307  CG  ASN A  61     4430  10940   3683   -246    395   -488       C  
ATOM    308  OD1 ASN A  61      -8.789  14.445 -21.471  1.00 34.15           O  
ANISOU  308  OD1 ASN A  61     2428   8810   1739   -233    355   -354       O  
ATOM    309  ND2 ASN A  61      -8.132  13.116 -23.124  1.00 50.03           N  
ANISOU  309  ND2 ASN A  61     4353  11161   3496   -329    410   -669       N  
ATOM    310  N   TYR A  62      -3.956  15.842 -19.916  1.00 31.61           N  
ANISOU  310  N   TYR A  62     2213   8110   1687    -56    427   -156       N  
ATOM    311  CA  TYR A  62      -2.763  15.803 -19.076  1.00 30.74           C  
ANISOU  311  CA  TYR A  62     2143   7867   1671    -11    449   -170       C  
ATOM    312  C   TYR A  62      -3.228  16.095 -17.609  1.00 31.36           C  
ANISOU  312  C   TYR A  62     2363   7608   1946     25    419   -121       C  
ATOM    313  O   TYR A  62      -2.754  15.460 -16.665  1.00 31.28           O  
ANISOU  313  O   TYR A  62     2416   7433   2036     86    441   -220       O  
ATOM    314  CB  TYR A  62      -1.760  16.873 -19.545  1.00 32.37           C  
ANISOU  314  CB  TYR A  62     2258   8248   1794    -88    434     26       C  
ATOM    315  CG  TYR A  62      -0.784  16.418 -20.609  1.00 35.05           C  
ANISOU  315  CG  TYR A  62     2441   8932   1945    -97    483    -52       C  
ATOM    316  CD1 TYR A  62      -1.193  16.219 -21.923  1.00 36.12           C  
ANISOU  316  CD1 TYR A  62     2464   9367   1895   -136    494    -85       C  
ATOM    317  CD2 TYR A  62       0.566  16.272 -20.321  1.00 37.20           C  
ANISOU  317  CD2 TYR A  62     2654   9283   2199    -66    517    -79       C  
ATOM    318  CE1 TYR A  62      -0.294  15.815 -22.907  1.00 35.43           C  
ANISOU  318  CE1 TYR A  62     2217   9635   1609   -134    545   -173       C  
ATOM    319  CE2 TYR A  62       1.477  15.879 -21.300  1.00 38.47           C  
ANISOU  319  CE2 TYR A  62     2644   9810   2163    -51    568   -153       C  
ATOM    320  CZ  TYR A  62       1.042  15.643 -22.589  1.00 42.99           C  
ANISOU  320  CZ  TYR A  62     3115  10666   2553    -80    584   -210       C  
ATOM    321  OH  TYR A  62       1.969  15.268 -23.528  1.00 43.93           O  
ANISOU  321  OH  TYR A  62     3052  11179   2458    -54    640   -297       O  
ATOM    322  N   PHE A  63      -4.196  17.022 -17.446  1.00 24.27           N  
ANISOU  322  N   PHE A  63     1503   6630   1087      5    370     29       N  
ATOM    323  CA  PHE A  63      -4.758  17.386 -16.158  1.00 22.93           C  
ANISOU  323  CA  PHE A  63     1449   6192   1071     52    344     65       C  
ATOM    324  C   PHE A  63      -5.651  16.282 -15.658  1.00 27.51           C  
ANISOU  324  C   PHE A  63     2066   6692   1693     89    361    -94       C  
ATOM    325  O   PHE A  63      -5.725  16.078 -14.458  1.00 28.34           O  
ANISOU  325  O   PHE A  63     2253   6598   1915    128    361   -128       O  
ATOM    326  CB  PHE A  63      -5.531  18.701 -16.235  1.00 24.17           C  
ANISOU  326  CB  PHE A  63     1635   6307   1242     58    290    261       C  
ATOM    327  CG  PHE A  63      -4.795  19.859 -16.864  1.00 25.44           C  
ANISOU  327  CG  PHE A  63     1781   6530   1354    -12    257    456       C  
ATOM    328  CD1 PHE A  63      -3.672  20.406 -16.256  1.00 28.57           C  
ANISOU  328  CD1 PHE A  63     2237   6804   1813    -69    247    512       C  
ATOM    329  CD2 PHE A  63      -5.255  20.438 -18.036  1.00 26.56           C  
ANISOU  329  CD2 PHE A  63     1849   6860   1382    -41    229    606       C  
ATOM    330  CE1 PHE A  63      -2.998  21.479 -16.839  1.00 28.83           C  
ANISOU  330  CE1 PHE A  63     2267   6893   1796   -179    208    710       C  
ATOM    331  CE2 PHE A  63      -4.593  21.521 -18.603  1.00 28.89           C  
ANISOU  331  CE2 PHE A  63     2144   7199   1634   -129    189    819       C  
ATOM    332  CZ  PHE A  63      -3.468  22.034 -18.003  1.00 26.92           C  
ANISOU  332  CZ  PHE A  63     1966   6812   1450   -209    178    870       C  
ATOM    333  N   ALA A  64      -6.319  15.557 -16.564  1.00 24.25           N  
ANISOU  333  N   ALA A  64     1593   6447   1175     54    371   -188       N  
ATOM    334  CA  ALA A  64      -7.176  14.419 -16.226  1.00 23.72           C  
ANISOU  334  CA  ALA A  64     1565   6320   1127     36    380   -340       C  
ATOM    335  C   ALA A  64      -6.289  13.272 -15.693  1.00 28.88           C  
ANISOU  335  C   ALA A  64     2298   6823   1853     67    418   -504       C  
ATOM    336  O   ALA A  64      -6.684  12.592 -14.748  1.00 29.13           O  
ANISOU  336  O   ALA A  64     2414   6675   1978     69    415   -564       O  
ATOM    337  CB  ALA A  64      -7.933  13.960 -17.455  1.00 24.11           C  
ANISOU  337  CB  ALA A  64     1530   6611   1020    -43    378   -411       C  
ATOM    338  N   PHE A  65      -5.077  13.085 -16.283  1.00 24.75           N  
ANISOU  338  N   PHE A  65     1736   6391   1277    101    452   -559       N  
ATOM    339  CA  PHE A  65      -4.096  12.069 -15.871  1.00 23.94           C  
ANISOU  339  CA  PHE A  65     1691   6174   1229    182    490   -701       C  
ATOM    340  C   PHE A  65      -3.561  12.419 -14.470  1.00 27.67           C  
ANISOU  340  C   PHE A  65     2219   6452   1842    236    480   -604       C  
ATOM    341  O   PHE A  65      -3.400  11.537 -13.629  1.00 26.29           O  
ANISOU  341  O   PHE A  65     2131   6097   1761    291    489   -680       O  
ATOM    342  CB  PHE A  65      -2.938  11.998 -16.884  1.00 24.92           C  
ANISOU  342  CB  PHE A  65     1716   6523   1230    227    530   -758       C  
ATOM    343  CG  PHE A  65      -2.000  10.824 -16.727  1.00 26.14           C  
ANISOU  343  CG  PHE A  65     1915   6610   1409    357    577   -934       C  
ATOM    344  CD1 PHE A  65      -1.049  10.801 -15.711  1.00 29.59           C  
ANISOU  344  CD1 PHE A  65     2367   6932   1942    454    586   -881       C  
ATOM    345  CD2 PHE A  65      -2.016   9.777 -17.635  1.00 28.45           C  
ANISOU  345  CD2 PHE A  65     2226   6972   1612    395    612  -1157       C  
ATOM    346  CE1 PHE A  65      -0.167   9.727 -15.582  1.00 30.53           C  
ANISOU  346  CE1 PHE A  65     2518   7003   2079    615    628  -1026       C  
ATOM    347  CE2 PHE A  65      -1.117   8.711 -17.520  1.00 31.31           C  
ANISOU  347  CE2 PHE A  65     2643   7253   1999    560    656  -1326       C  
ATOM    348  CZ  PHE A  65      -0.199   8.695 -16.496  1.00 29.71           C  
ANISOU  348  CZ  PHE A  65     2450   6938   1902    683    664  -1248       C  
ATOM    349  N   SER A  66      -3.282  13.713 -14.243  1.00 24.94           N  
ANISOU  349  N   SER A  66     1831   6143   1502    210    456   -433       N  
ATOM    350  CA  SER A  66      -2.828  14.279 -12.974  1.00 24.94           C  
ANISOU  350  CA  SER A  66     1877   5992   1608    229    438   -339       C  
ATOM    351  C   SER A  66      -3.899  14.070 -11.872  1.00 30.27           C  
ANISOU  351  C   SER A  66     2642   6476   2384    234    416   -343       C  
ATOM    352  O   SER A  66      -3.557  13.690 -10.755  1.00 30.78           O  
ANISOU  352  O   SER A  66     2756   6407   2531    271    418   -355       O  
ATOM    353  CB  SER A  66      -2.526  15.764 -13.153  1.00 27.52           C  
ANISOU  353  CB  SER A  66     2169   6380   1906    165    406   -169       C  
ATOM    354  OG  SER A  66      -2.121  16.357 -11.933  1.00 34.16           O  
ANISOU  354  OG  SER A  66     3069   7072   2837    161    384   -103       O  
ATOM    355  N   LEU A  67      -5.188  14.297 -12.204  1.00 26.71           N  
ANISOU  355  N   LEU A  67     2188   6055   1904    196    396   -324       N  
ATOM    356  CA  LEU A  67      -6.339  14.105 -11.322  1.00 25.96           C  
ANISOU  356  CA  LEU A  67     2138   5861   1863    190    378   -324       C  
ATOM    357  C   LEU A  67      -6.505  12.605 -10.994  1.00 30.77           C  
ANISOU  357  C   LEU A  67     2804   6383   2505    169    394   -450       C  
ATOM    358  O   LEU A  67      -6.802  12.274  -9.852  1.00 31.16           O  
ANISOU  358  O   LEU A  67     2903   6311   2627    171    386   -438       O  
ATOM    359  CB  LEU A  67      -7.604  14.694 -11.991  1.00 25.66           C  
ANISOU  359  CB  LEU A  67     2044   5955   1750    165    355   -265       C  
ATOM    360  CG  LEU A  67      -8.956  14.503 -11.298  1.00 30.51           C  
ANISOU  360  CG  LEU A  67     2656   6566   2372    155    338   -261       C  
ATOM    361  CD1 LEU A  67      -9.013  15.240  -9.995  1.00 30.77           C  
ANISOU  361  CD1 LEU A  67     2730   6477   2484    228    328   -196       C  
ATOM    362  CD2 LEU A  67     -10.101  14.999 -12.172  1.00 33.53           C  
ANISOU  362  CD2 LEU A  67     2946   7146   2647    144    317   -202       C  
ATOM    363  N   ALA A  68      -6.277  11.709 -11.984  1.00 27.25           N  
ANISOU  363  N   ALA A  68     2359   5992   2003    148    415   -571       N  
ATOM    364  CA  ALA A  68      -6.346  10.247 -11.841  1.00 26.94           C  
ANISOU  364  CA  ALA A  68     2414   5823   2000    127    425   -706       C  
ATOM    365  C   ALA A  68      -5.250   9.718 -10.903  1.00 30.57           C  
ANISOU  365  C   ALA A  68     2941   6112   2562    230    440   -711       C  
ATOM    366  O   ALA A  68      -5.465   8.710 -10.227  1.00 30.72           O  
ANISOU  366  O   ALA A  68     3063   5958   2653    218    432   -748       O  
ATOM    367  CB  ALA A  68      -6.221   9.585 -13.202  1.00 27.90           C  
ANISOU  367  CB  ALA A  68     2530   6047   2024    104    446   -858       C  
ATOM    368  N   CYS A  69      -4.079  10.395 -10.872  1.00 26.83           N  
ANISOU  368  N   CYS A  69     2404   5705   2084    318    457   -655       N  
ATOM    369  CA  CYS A  69      -2.937  10.074 -10.010  1.00 26.82           C  
ANISOU  369  CA  CYS A  69     2422   5619   2151    425    469   -633       C  
ATOM    370  C   CYS A  69      -3.289  10.325  -8.538  1.00 29.32           C  
ANISOU  370  C   CYS A  69     2772   5818   2550    402    441   -527       C  
ATOM    371  O   CYS A  69      -2.983   9.493  -7.677  1.00 27.82           O  
ANISOU  371  O   CYS A  69     2643   5498   2430    455    439   -522       O  
ATOM    372  CB  CYS A  69      -1.708  10.876 -10.428  1.00 27.59           C  
ANISOU  372  CB  CYS A  69     2409   5890   2186    477    488   -586       C  
ATOM    373  SG  CYS A  69      -0.879  10.244 -11.900  1.00 31.79           S  
ANISOU  373  SG  CYS A  69     2879   6593   2608    566    537   -728       S  
ATOM    374  N   ALA A  70      -3.936  11.481  -8.263  1.00 25.76           N  
ANISOU  374  N   ALA A  70     2283   5422   2083    335    418   -440       N  
ATOM    375  CA  ALA A  70      -4.389  11.889  -6.935  1.00 25.31           C  
ANISOU  375  CA  ALA A  70     2244   5299   2073    316    394   -361       C  
ATOM    376  C   ALA A  70      -5.488  10.939  -6.456  1.00 30.87           C  
ANISOU  376  C   ALA A  70     3004   5922   2804    260    383   -382       C  
ATOM    377  O   ALA A  70      -5.510  10.564  -5.276  1.00 30.88           O  
ANISOU  377  O   ALA A  70     3034   5848   2850    260    372   -335       O  
ATOM    378  CB  ALA A  70      -4.919  13.320  -6.979  1.00 25.71           C  
ANISOU  378  CB  ALA A  70     2259   5418   2092    287    376   -296       C  
ATOM    379  N   ASP A  71      -6.384  10.527  -7.386  1.00 27.38           N  
ANISOU  379  N   ASP A  71     2569   5518   2316    190    382   -445       N  
ATOM    380  CA  ASP A  71      -7.502   9.627  -7.091  1.00 26.87           C  
ANISOU  380  CA  ASP A  71     2551   5407   2253     83    363   -461       C  
ATOM    381  C   ASP A  71      -7.036   8.189  -6.851  1.00 28.51           C  
ANISOU  381  C   ASP A  71     2878   5426   2529     80    363   -513       C  
ATOM    382  O   ASP A  71      -7.694   7.457  -6.112  1.00 27.60           O  
ANISOU  382  O   ASP A  71     2821   5224   2443    -12    339   -474       O  
ATOM    383  CB  ASP A  71      -8.589   9.712  -8.181  1.00 28.91           C  
ANISOU  383  CB  ASP A  71     2763   5805   2418    -14    356   -509       C  
ATOM    384  CG  ASP A  71      -9.388  11.013  -8.260  1.00 39.55           C  
ANISOU  384  CG  ASP A  71     4001   7329   3699      0    346   -428       C  
ATOM    385  OD1 ASP A  71      -9.442  11.747  -7.245  1.00 41.32           O  
ANISOU  385  OD1 ASP A  71     4203   7546   3951     60    341   -350       O  
ATOM    386  OD2 ASP A  71      -9.990  11.276  -9.326  1.00 43.05           O  
ANISOU  386  OD2 ASP A  71     4381   7921   4054    -39    341   -447       O  
ATOM    387  N   LEU A  72      -5.889   7.797  -7.452  1.00 24.12           N  
ANISOU  387  N   LEU A  72     2359   4811   1995    190    388   -591       N  
ATOM    388  CA  LEU A  72      -5.277   6.478  -7.285  1.00 23.80           C  
ANISOU  388  CA  LEU A  72     2448   4565   2029    252    391   -647       C  
ATOM    389  C   LEU A  72      -4.716   6.317  -5.859  1.00 29.71           C  
ANISOU  389  C   LEU A  72     3213   5219   2855    324    378   -518       C  
ATOM    390  O   LEU A  72      -4.875   5.244  -5.275  1.00 31.28           O  
ANISOU  390  O   LEU A  72     3532   5228   3123    304    356   -492       O  
ATOM    391  CB  LEU A  72      -4.192   6.254  -8.346  1.00 23.75           C  
ANISOU  391  CB  LEU A  72     2442   4583   1998    394    430   -773       C  
ATOM    392  CG  LEU A  72      -3.532   4.875  -8.400  1.00 28.58           C  
ANISOU  392  CG  LEU A  72     3204   4974   2683    515    438   -867       C  
ATOM    393  CD1 LEU A  72      -4.534   3.777  -8.729  1.00 29.44           C  
ANISOU  393  CD1 LEU A  72     3482   4892   2812    371    412   -975       C  
ATOM    394  CD2 LEU A  72      -2.433   4.855  -9.426  1.00 28.63           C  
ANISOU  394  CD2 LEU A  72     3159   5085   2635    694    486   -987       C  
ATOM    395  N   ILE A  73      -4.100   7.391  -5.288  1.00 24.44           N  
ANISOU  395  N   ILE A  73     2430   4687   2169    389    386   -431       N  
ATOM    396  CA  ILE A  73      -3.565   7.442  -3.913  1.00 22.42           C  
ANISOU  396  CA  ILE A  73     2153   4413   1952    440    372   -308       C  
ATOM    397  C   ILE A  73      -4.744   7.302  -2.925  1.00 23.59           C  
ANISOU  397  C   ILE A  73     2323   4536   2105    305    340   -223       C  
ATOM    398  O   ILE A  73      -4.662   6.557  -1.949  1.00 20.93           O  
ANISOU  398  O   ILE A  73     2037   4104   1813    304    318   -133       O  
ATOM    399  CB  ILE A  73      -2.767   8.764  -3.652  1.00 25.00           C  
ANISOU  399  CB  ILE A  73     2354   4913   2233    487    381   -262       C  
ATOM    400  CG1 ILE A  73      -1.546   8.916  -4.572  1.00 24.82           C  
ANISOU  400  CG1 ILE A  73     2277   4974   2178    596    411   -319       C  
ATOM    401  CG2 ILE A  73      -2.362   8.894  -2.191  1.00 25.89           C  
ANISOU  401  CG2 ILE A  73     2432   5046   2357    506    362   -148       C  
ATOM    402  CD1 ILE A  73      -1.079  10.403  -4.792  1.00 27.15           C  
ANISOU  402  CD1 ILE A  73     2463   5447   2404    556    413   -289       C  
ATOM    403  N   ILE A  74      -5.830   8.038  -3.191  1.00 20.31           N  
ANISOU  403  N   ILE A  74     1853   4235   1629    199    336   -240       N  
ATOM    404  CA  ILE A  74      -7.045   8.031  -2.384  1.00 19.96           C  
ANISOU  404  CA  ILE A  74     1787   4247   1552     75    313   -171       C  
ATOM    405  C   ILE A  74      -7.662   6.622  -2.353  1.00 25.93           C  
ANISOU  405  C   ILE A  74     2654   4857   2340    -48    287   -157       C  
ATOM    406  O   ILE A  74      -8.030   6.140  -1.284  1.00 25.88           O  
ANISOU  406  O   ILE A  74     2661   4831   2339   -122    261    -47       O  
ATOM    407  CB  ILE A  74      -8.021   9.147  -2.853  1.00 22.67           C  
ANISOU  407  CB  ILE A  74     2035   4767   1812     36    318   -201       C  
ATOM    408  CG1 ILE A  74      -7.509  10.541  -2.440  1.00 22.95           C  
ANISOU  408  CG1 ILE A  74     2000   4892   1829    136    329   -183       C  
ATOM    409  CG2 ILE A  74      -9.437   8.926  -2.340  1.00 23.47           C  
ANISOU  409  CG2 ILE A  74     2093   4973   1851    -96    299   -152       C  
ATOM    410  CD1 ILE A  74      -8.040  11.683  -3.304  1.00 33.58           C  
ANISOU  410  CD1 ILE A  74     3292   6345   3123    159    335   -219       C  
ATOM    411  N   GLY A  75      -7.700   5.962  -3.506  1.00 24.14           N  
ANISOU  411  N   GLY A  75     2515   4526   2129    -76    290   -268       N  
ATOM    412  CA  GLY A  75      -8.243   4.615  -3.645  1.00 24.57           C  
ANISOU  412  CA  GLY A  75     2718   4398   2220   -217    259   -286       C  
ATOM    413  C   GLY A  75      -7.420   3.520  -3.001  1.00 28.97           C  
ANISOU  413  C   GLY A  75     3423   4697   2887   -141    243   -227       C  
ATOM    414  O   GLY A  75      -7.953   2.736  -2.206  1.00 28.27           O  
ANISOU  414  O   GLY A  75     3416   4500   2826   -274    202   -115       O  
ATOM    415  N   ALA A  76      -6.112   3.465  -3.346  1.00 25.50           N  
ANISOU  415  N   ALA A  76     3010   4178   2500     79    272   -286       N  
ATOM    416  CA  ALA A  76      -5.177   2.454  -2.845  1.00 24.67           C  
ANISOU  416  CA  ALA A  76     3037   3840   2499    224    261   -233       C  
ATOM    417  C   ALA A  76      -4.707   2.693  -1.430  1.00 27.32           C  
ANISOU  417  C   ALA A  76     3294   4239   2847    287    246    -40       C  
ATOM    418  O   ALA A  76      -4.695   1.746  -0.645  1.00 26.32           O  
ANISOU  418  O   ALA A  76     3282   3930   2788    272    208     85       O  
ATOM    419  CB  ALA A  76      -3.986   2.309  -3.781  1.00 25.24           C  
ANISOU  419  CB  ALA A  76     3129   3869   2591    456    303   -374       C  
ATOM    420  N   PHE A  77      -4.321   3.938  -1.093  1.00 24.67           N  
ANISOU  420  N   PHE A  77     2775   4156   2443    345    270    -11       N  
ATOM    421  CA  PHE A  77      -3.782   4.255   0.234  1.00 25.31           C  
ANISOU  421  CA  PHE A  77     2764   4342   2510    400    256    147       C  
ATOM    422  C   PHE A  77      -4.850   4.726   1.221  1.00 29.82           C  
ANISOU  422  C   PHE A  77     3258   5061   3012    221    234    246       C  
ATOM    423  O   PHE A  77      -5.238   3.951   2.099  1.00 30.36           O  
ANISOU  423  O   PHE A  77     3379   5059   3096    135    197    385       O  
ATOM    424  CB  PHE A  77      -2.601   5.254   0.127  1.00 27.09           C  
ANISOU  424  CB  PHE A  77     2850   4750   2692    553    289    116       C  
ATOM    425  CG  PHE A  77      -2.033   5.746   1.430  1.00 29.04           C  
ANISOU  425  CG  PHE A  77     2982   5160   2894    580    274    249       C  
ATOM    426  CD1 PHE A  77      -1.048   5.026   2.093  1.00 32.93           C  
ANISOU  426  CD1 PHE A  77     3478   5615   3418    716    258    372       C  
ATOM    427  CD2 PHE A  77      -2.471   6.941   1.992  1.00 31.35           C  
ANISOU  427  CD2 PHE A  77     3161   5649   3102    480    275    247       C  
ATOM    428  CE1 PHE A  77      -0.521   5.488   3.305  1.00 33.80           C  
ANISOU  428  CE1 PHE A  77     3462   5920   3460    722    241    495       C  
ATOM    429  CE2 PHE A  77      -1.954   7.393   3.209  1.00 33.98           C  
ANISOU  429  CE2 PHE A  77     3392   6144   3374    487    260    343       C  
ATOM    430  CZ  PHE A  77      -0.970   6.673   3.847  1.00 32.13           C  
ANISOU  430  CZ  PHE A  77     3144   5908   3157    595    243    467       C  
ATOM    431  N   SER A  78      -5.309   5.990   1.077  1.00 25.52           N  
ANISOU  431  N   SER A  78     2588   4723   2384    177    255    180       N  
ATOM    432  CA  SER A  78      -6.265   6.665   1.954  1.00 24.82           C  
ANISOU  432  CA  SER A  78     2399   4825   2207     63    246    236       C  
ATOM    433  C   SER A  78      -7.458   5.824   2.361  1.00 30.18           C  
ANISOU  433  C   SER A  78     3117   5484   2865   -117    215    321       C  
ATOM    434  O   SER A  78      -7.666   5.650   3.558  1.00 29.97           O  
ANISOU  434  O   SER A  78     3044   5549   2795   -175    193    456       O  
ATOM    435  CB  SER A  78      -6.734   7.974   1.344  1.00 26.15           C  
ANISOU  435  CB  SER A  78     2481   5142   2312     67    272    122       C  
ATOM    436  OG  SER A  78      -5.643   8.834   1.075  1.00 30.48           O  
ANISOU  436  OG  SER A  78     2993   5721   2867    189    292     68       O  
ATOM    437  N   MET A  79      -8.215   5.289   1.377  1.00 27.99           N  
ANISOU  437  N   MET A  79     2918   5114   2603   -226    209    250       N  
ATOM    438  CA  MET A  79      -9.414   4.475   1.580  1.00 28.84           C  
ANISOU  438  CA  MET A  79     3064   5218   2676   -450    173    323       C  
ATOM    439  C   MET A  79      -9.150   3.253   2.433  1.00 34.76           C  
ANISOU  439  C   MET A  79     3933   5786   3489   -516    129    487       C  
ATOM    440  O   MET A  79      -9.827   3.058   3.446  1.00 36.04           O  
ANISOU  440  O   MET A  79     4033   6082   3580   -661    102    637       O  
ATOM    441  CB  MET A  79     -10.004   4.015   0.239  1.00 31.58           C  
ANISOU  441  CB  MET A  79     3500   5463   3034   -556    169    196       C  
ATOM    442  CG  MET A  79     -10.918   5.020  -0.421  1.00 35.32           C  
ANISOU  442  CG  MET A  79     3830   6190   3398   -595    191    107       C  
ATOM    443  SD  MET A  79     -11.767   4.267  -1.838  1.00 38.96           S  
ANISOU  443  SD  MET A  79     4379   6589   3835   -791    171    -11       S  
ATOM    444  CE  MET A  79     -12.587   5.618  -2.452  1.00 35.15           C  
ANISOU  444  CE  MET A  79     3693   6441   3222   -755    200    -72       C  
ATOM    445  N   ASN A  80      -8.160   2.439   2.030  1.00 31.07           N  
ANISOU  445  N   ASN A  80     3631   5028   3147   -396    122    468       N  
ATOM    446  CA  ASN A  80      -7.821   1.188   2.697  1.00 30.97           C  
ANISOU  446  CA  ASN A  80     3776   4770   3221   -421     74    629       C  
ATOM    447  C   ASN A  80      -7.298   1.380   4.091  1.00 35.20           C  
ANISOU  447  C   ASN A  80     4209   5439   3725   -347     62    820       C  
ATOM    448  O   ASN A  80      -7.761   0.691   4.991  1.00 34.70           O  
ANISOU  448  O   ASN A  80     4181   5357   3647   -497     15   1014       O  
ATOM    449  CB  ASN A  80      -6.873   0.349   1.852  1.00 29.83           C  
ANISOU  449  CB  ASN A  80     3833   4287   3213   -252     76    533       C  
ATOM    450  CG  ASN A  80      -7.514  -0.154   0.584  1.00 47.08           C  
ANISOU  450  CG  ASN A  80     6162   6306   5422   -380     72    356       C  
ATOM    451  OD1 ASN A  80      -8.686  -0.571   0.552  1.00 41.96           O  
ANISOU  451  OD1 ASN A  80     5567   5641   4734   -658     33    388       O  
ATOM    452  ND2 ASN A  80      -6.757  -0.124  -0.491  1.00 36.66           N  
ANISOU  452  ND2 ASN A  80     4892   4892   4144   -195    111    165       N  
ATOM    453  N   LEU A  81      -6.387   2.345   4.278  1.00 32.36           N  
ANISOU  453  N   LEU A  81     3714   5243   3337   -147    101    772       N  
ATOM    454  CA  LEU A  81      -5.784   2.662   5.573  1.00 32.12           C  
ANISOU  454  CA  LEU A  81     3564   5389   3252    -73     92    926       C  
ATOM    455  C   LEU A  81      -6.794   3.295   6.548  1.00 33.82           C  
ANISOU  455  C   LEU A  81     3617   5913   3319   -242     87    997       C  
ATOM    456  O   LEU A  81      -6.718   3.023   7.748  1.00 32.80           O  
ANISOU  456  O   LEU A  81     3430   5899   3134   -280     58   1182       O  
ATOM    457  CB  LEU A  81      -4.558   3.571   5.366  1.00 32.34           C  
ANISOU  457  CB  LEU A  81     3493   5523   3274    146    131    826       C  
ATOM    458  CG  LEU A  81      -3.544   3.665   6.493  1.00 36.92           C  
ANISOU  458  CG  LEU A  81     3973   6240   3813    261    117    972       C  
ATOM    459  CD1 LEU A  81      -2.704   2.406   6.584  1.00 37.55           C  
ANISOU  459  CD1 LEU A  81     4182   6083   4003    408     86   1109       C  
ATOM    460  CD2 LEU A  81      -2.662   4.864   6.302  1.00 38.40           C  
ANISOU  460  CD2 LEU A  81     4023   6625   3941    374    153    851       C  
ATOM    461  N   TYR A  82      -7.732   4.124   6.038  1.00 29.29           N  
ANISOU  461  N   TYR A  82     2962   5495   2670   -326    116    856       N  
ATOM    462  CA  TYR A  82      -8.738   4.755   6.884  1.00 28.85           C  
ANISOU  462  CA  TYR A  82     2744   5756   2461   -448    121    894       C  
ATOM    463  C   TYR A  82      -9.762   3.743   7.351  1.00 32.90           C  
ANISOU  463  C   TYR A  82     3286   6283   2933   -685     76   1063       C  
ATOM    464  O   TYR A  82     -10.224   3.853   8.481  1.00 32.36           O  
ANISOU  464  O   TYR A  82     3087   6472   2735   -775     65   1190       O  
ATOM    465  CB  TYR A  82      -9.401   5.958   6.191  1.00 30.05           C  
ANISOU  465  CB  TYR A  82     2801   6069   2546   -420    164    703       C  
ATOM    466  CG  TYR A  82     -10.348   6.741   7.078  1.00 30.46           C  
ANISOU  466  CG  TYR A  82     2676   6467   2431   -475    178    711       C  
ATOM    467  CD1 TYR A  82      -9.938   7.216   8.320  1.00 32.45           C  
ANISOU  467  CD1 TYR A  82     2824   6913   2594   -423    181    764       C  
ATOM    468  CD2 TYR A  82     -11.638   7.049   6.654  1.00 30.69           C  
ANISOU  468  CD2 TYR A  82     2627   6661   2374   -562    191    651       C  
ATOM    469  CE1 TYR A  82     -10.810   7.921   9.150  1.00 33.97           C  
ANISOU  469  CE1 TYR A  82     2853   7441   2615   -452    199    745       C  
ATOM    470  CE2 TYR A  82     -12.511   7.780   7.461  1.00 31.63           C  
ANISOU  470  CE2 TYR A  82     2568   7126   2324   -569    211    644       C  
ATOM    471  CZ  TYR A  82     -12.095   8.203   8.716  1.00 39.39           C  
ANISOU  471  CZ  TYR A  82     3464   8283   3222   -510    217    682       C  
ATOM    472  OH  TYR A  82     -12.932   8.911   9.542  1.00 37.46           O  
ANISOU  472  OH  TYR A  82     3043   8394   2795   -497    241    651       O  
ATOM    473  N   THR A  83     -10.077   2.733   6.510  1.00 30.80           N  
ANISOU  473  N   THR A  83     3193   5745   2764   -800     47   1067       N  
ATOM    474  CA  THR A  83     -11.028   1.663   6.848  1.00 30.68           C  
ANISOU  474  CA  THR A  83     3245   5690   2721  -1077     -8   1237       C  
ATOM    475  C   THR A  83     -10.478   0.745   7.932  1.00 34.59           C  
ANISOU  475  C   THR A  83     3813   6074   3254  -1102    -60   1492       C  
ATOM    476  O   THR A  83     -11.231   0.361   8.835  1.00 35.28           O  
ANISOU  476  O   THR A  83     3831   6340   3234  -1317    -96   1688       O  
ATOM    477  CB  THR A  83     -11.484   0.903   5.616  1.00 34.35           C  
ANISOU  477  CB  THR A  83     3898   5875   3278  -1204    -30   1142       C  
ATOM    478  OG1 THR A  83     -11.991   1.859   4.688  1.00 34.59           O  
ANISOU  478  OG1 THR A  83     3820   6077   3247  -1169     17    932       O  
ATOM    479  CG2 THR A  83     -12.565  -0.127   5.942  1.00 28.16           C  
ANISOU  479  CG2 THR A  83     3187   5061   2451  -1550    -95   1312       C  
ATOM    480  N   VAL A  84      -9.169   0.414   7.855  1.00 29.45           N  
ANISOU  480  N   VAL A  84     3285   5165   2740   -876    -63   1504       N  
ATOM    481  CA  VAL A  84      -8.503  -0.419   8.851  1.00 28.66           C  
ANISOU  481  CA  VAL A  84     3251   4956   2682   -839   -112   1759       C  
ATOM    482  C   VAL A  84      -8.532   0.323  10.194  1.00 33.17           C  
ANISOU  482  C   VAL A  84     3572   5953   3077   -844   -102   1878       C  
ATOM    483  O   VAL A  84      -8.815  -0.295  11.214  1.00 33.54           O  
ANISOU  483  O   VAL A  84     3598   6085   3061   -988   -152   2134       O  
ATOM    484  CB  VAL A  84      -7.074  -0.849   8.422  1.00 31.56           C  
ANISOU  484  CB  VAL A  84     3768   5009   3214   -548   -110   1731       C  
ATOM    485  CG1 VAL A  84      -6.419  -1.733   9.481  1.00 31.41           C  
ANISOU  485  CG1 VAL A  84     3812   4889   3235   -490   -169   2027       C  
ATOM    486  CG2 VAL A  84      -7.105  -1.586   7.091  1.00 30.79           C  
ANISOU  486  CG2 VAL A  84     3918   4511   3269   -536   -115   1577       C  
ATOM    487  N   TYR A  85      -8.310   1.652  10.173  1.00 29.25           N  
ANISOU  487  N   TYR A  85     2895   5724   2492   -709    -42   1688       N  
ATOM    488  CA  TYR A  85      -8.317   2.509  11.353  1.00 28.83           C  
ANISOU  488  CA  TYR A  85     2615   6078   2262   -698    -24   1728       C  
ATOM    489  C   TYR A  85      -9.684   2.490  12.066  1.00 34.64           C  
ANISOU  489  C   TYR A  85     3219   7119   2823   -946    -36   1833       C  
ATOM    490  O   TYR A  85      -9.726   2.449  13.294  1.00 34.80           O  
ANISOU  490  O   TYR A  85     3106   7410   2705  -1009    -55   2005       O  
ATOM    491  CB  TYR A  85      -7.889   3.940  10.978  1.00 29.10           C  
ANISOU  491  CB  TYR A  85     2540   6260   2257   -524     38   1466       C  
ATOM    492  CG  TYR A  85      -7.924   4.921  12.130  1.00 29.70           C  
ANISOU  492  CG  TYR A  85     2407   6731   2146   -510     58   1450       C  
ATOM    493  CD1 TYR A  85      -7.271   4.644  13.323  1.00 31.48           C  
ANISOU  493  CD1 TYR A  85     2555   7112   2294   -501     27   1637       C  
ATOM    494  CD2 TYR A  85      -8.646   6.110  12.042  1.00 29.96           C  
ANISOU  494  CD2 TYR A  85     2324   6992   2068   -500    105   1248       C  
ATOM    495  CE1 TYR A  85      -7.326   5.526  14.400  1.00 31.62           C  
ANISOU  495  CE1 TYR A  85     2382   7515   2116   -504     45   1599       C  
ATOM    496  CE2 TYR A  85      -8.697   7.009  13.108  1.00 30.19           C  
ANISOU  496  CE2 TYR A  85     2184   7368   1919   -477    125   1198       C  
ATOM    497  CZ  TYR A  85      -8.020   6.717  14.281  1.00 35.55           C  
ANISOU  497  CZ  TYR A  85     2786   8208   2512   -488     95   1362       C  
ATOM    498  OH  TYR A  85      -8.036   7.579  15.349  1.00 30.67           O  
ANISOU  498  OH  TYR A  85     2004   7948   1701   -476    113   1294       O  
ATOM    499  N   ILE A  86     -10.786   2.482  11.299  1.00 31.44           N  
ANISOU  499  N   ILE A  86     2832   6707   2407  -1093    -27   1740       N  
ATOM    500  CA  ILE A  86     -12.163   2.456  11.822  1.00 30.52           C  
ANISOU  500  CA  ILE A  86     2567   6922   2108  -1335    -35   1829       C  
ATOM    501  C   ILE A  86     -12.518   1.070  12.365  1.00 35.88           C  
ANISOU  501  C   ILE A  86     3342   7499   2793  -1598   -112   2136       C  
ATOM    502  O   ILE A  86     -13.074   0.974  13.460  1.00 36.04           O  
ANISOU  502  O   ILE A  86     3200   7859   2633  -1755   -130   2321       O  
ATOM    503  CB  ILE A  86     -13.170   2.937  10.744  1.00 33.00           C  
ANISOU  503  CB  ILE A  86     2847   7295   2395  -1390     -2   1629       C  
ATOM    504  CG1 ILE A  86     -12.950   4.419  10.397  1.00 31.92           C  
ANISOU  504  CG1 ILE A  86     2600   7303   2226  -1138     69   1364       C  
ATOM    505  CG2 ILE A  86     -14.613   2.694  11.206  1.00 34.95           C  
ANISOU  505  CG2 ILE A  86     2932   7902   2446  -1663    -17   1750       C  
ATOM    506  CD1 ILE A  86     -13.445   4.794   9.107  1.00 31.82           C  
ANISOU  506  CD1 ILE A  86     2623   7204   2261  -1114     94   1179       C  
ATOM    507  N   ILE A  87     -12.208   0.005  11.593  1.00 34.19           N  
ANISOU  507  N   ILE A  87     3396   6818   2775  -1651   -159   2186       N  
ATOM    508  CA  ILE A  87     -12.463  -1.397  11.953  1.00 34.94           C  
ANISOU  508  CA  ILE A  87     3661   6691   2921  -1902   -245   2475       C  
ATOM    509  C   ILE A  87     -11.681  -1.806  13.238  1.00 42.12           C  
ANISOU  509  C   ILE A  87     4547   7648   3810  -1840   -285   2756       C  
ATOM    510  O   ILE A  87     -12.289  -2.357  14.158  1.00 40.73           O  
ANISOU  510  O   ILE A  87     4309   7656   3512  -2090   -337   3031       O  
ATOM    511  CB  ILE A  87     -12.220  -2.348  10.734  1.00 37.14           C  
ANISOU  511  CB  ILE A  87     4270   6411   3431  -1923   -281   2403       C  
ATOM    512  CG1 ILE A  87     -13.351  -2.198   9.697  1.00 36.51           C  
ANISOU  512  CG1 ILE A  87     4186   6381   3305  -2133   -269   2225       C  
ATOM    513  CG2 ILE A  87     -12.060  -3.825  11.162  1.00 38.23           C  
ANISOU  513  CG2 ILE A  87     4662   6179   3684  -2082   -377   2705       C  
ATOM    514  CD1 ILE A  87     -13.109  -2.901   8.401  1.00 41.25           C  
ANISOU  514  CD1 ILE A  87     5076   6499   4098  -2124   -287   2067       C  
ATOM    515  N   MET A  88     -10.354  -1.514  13.290  1.00 41.93           N  
ANISOU  515  N   MET A  88     4547   7503   3880  -1521   -262   2696       N  
ATOM    516  CA  MET A  88      -9.477  -1.811  14.429  1.00 43.58           C  
ANISOU  516  CA  MET A  88     4710   7789   4060  -1418   -296   2945       C  
ATOM    517  C   MET A  88      -9.809  -0.933  15.624  1.00 47.29           C  
ANISOU  517  C   MET A  88     4863   8838   4268  -1467   -268   2987       C  
ATOM    518  O   MET A  88      -9.496  -1.296  16.757  1.00 46.94           O  
ANISOU  518  O   MET A  88     4740   8967   4130  -1501   -310   3256       O  
ATOM    519  CB  MET A  88      -7.997  -1.652  14.062  1.00 46.96           C  
ANISOU  519  CB  MET A  88     5218   7988   4637  -1066   -276   2847       C  
ATOM    520  CG  MET A  88      -7.396  -2.876  13.414  1.00 52.44           C  
ANISOU  520  CG  MET A  88     6225   8130   5568   -979   -326   2936       C  
ATOM    521  SD  MET A  88      -5.582  -2.730  13.233  1.00 58.84           S  
ANISOU  521  SD  MET A  88     7057   8803   6498   -538   -302   2874       S  
ATOM    522  CE  MET A  88      -5.025  -3.279  14.860  1.00 55.05           C  
ANISOU  522  CE  MET A  88     6483   8507   5926   -517   -372   3298       C  
ATOM    523  N   GLY A  89     -10.421   0.215  15.350  1.00 43.68           N  
ANISOU  523  N   GLY A  89     4234   8674   3690  -1452   -198   2718       N  
ATOM    524  CA  GLY A  89     -10.852   1.174  16.354  1.00 44.11           C  
ANISOU  524  CA  GLY A  89     3997   9276   3486  -1472   -158   2678       C  
ATOM    525  C   GLY A  89      -9.734   1.991  16.952  1.00 50.18           C  
ANISOU  525  C   GLY A  89     4655  10206   4204  -1232   -129   2592       C  
ATOM    526  O   GLY A  89      -9.975   2.784  17.870  1.00 51.03           O  
ANISOU  526  O   GLY A  89     4537  10762   4090  -1237   -100   2547       O  
ATOM    527  N   HIS A  90      -8.502   1.794  16.449  1.00 46.27           N  
ANISOU  527  N   HIS A  90     4312   9373   3897  -1026   -138   2563       N  
ATOM    528  CA  HIS A  90      -7.331   2.509  16.926  1.00 45.63           C  
ANISOU  528  CA  HIS A  90     4130   9437   3771   -819   -119   2491       C  
ATOM    529  C   HIS A  90      -6.205   2.460  15.902  1.00 45.69           C  
ANISOU  529  C   HIS A  90     4300   9066   3993   -595   -111   2373       C  
ATOM    530  O   HIS A  90      -6.263   1.674  14.954  1.00 44.73           O  
ANISOU  530  O   HIS A  90     4385   8550   4058   -588   -128   2389       O  
ATOM    531  CB  HIS A  90      -6.892   1.973  18.306  1.00 47.17           C  
ANISOU  531  CB  HIS A  90     4213   9877   3834   -866   -173   2805       C  
ATOM    532  CG  HIS A  90      -6.112   0.707  18.235  1.00 50.95           C  
ANISOU  532  CG  HIS A  90     4871  10004   4485   -799   -241   3085       C  
ATOM    533  ND1 HIS A  90      -6.706  -0.481  17.866  1.00 53.00           N  
ANISOU  533  ND1 HIS A  90     5333   9929   4876   -945   -293   3280       N  
ATOM    534  CD2 HIS A  90      -4.797   0.493  18.474  1.00 52.99           C  
ANISOU  534  CD2 HIS A  90     5137  10200   4798   -591   -265   3189       C  
ATOM    535  CE1 HIS A  90      -5.740  -1.381  17.897  1.00 52.66           C  
ANISOU  535  CE1 HIS A  90     5436   9593   4977   -798   -345   3490       C  
ATOM    536  NE2 HIS A  90      -4.570  -0.837  18.250  1.00 52.89           N  
ANISOU  536  NE2 HIS A  90     5339   9794   4962   -567   -328   3449       N  
ATOM    537  N   TRP A  91      -5.202   3.331  16.088  1.00 40.15           N  
ANISOU  537  N   TRP A  91     3497   8513   3246   -426    -84   2240       N  
ATOM    538  CA  TRP A  91      -4.028   3.452  15.237  1.00 38.83           C  
ANISOU  538  CA  TRP A  91     3421   8105   3229   -212    -71   2127       C  
ATOM    539  C   TRP A  91      -2.871   2.753  15.942  1.00 43.78           C  
ANISOU  539  C   TRP A  91     4018   8760   3856    -91   -120   2378       C  
ATOM    540  O   TRP A  91      -2.508   3.126  17.063  1.00 43.32           O  
ANISOU  540  O   TRP A  91     3777   9064   3620   -112   -133   2464       O  
ATOM    541  CB  TRP A  91      -3.724   4.933  14.973  1.00 36.84           C  
ANISOU  541  CB  TRP A  91     3066   8024   2906   -145    -15   1824       C  
ATOM    542  CG  TRP A  91      -2.612   5.146  14.002  1.00 37.47           C  
ANISOU  542  CG  TRP A  91     3219   7899   3118     36      2   1700       C  
ATOM    543  CD1 TRP A  91      -1.320   5.466  14.296  1.00 40.38           C  
ANISOU  543  CD1 TRP A  91     3496   8399   3446    159     -5   1712       C  
ATOM    544  CD2 TRP A  91      -2.672   4.983  12.584  1.00 37.08           C  
ANISOU  544  CD2 TRP A  91     3329   7518   3243    105     27   1564       C  
ATOM    545  NE1 TRP A  91      -0.572   5.515  13.149  1.00 39.38           N  
ANISOU  545  NE1 TRP A  91     3454   8054   3454    304     16   1597       N  
ATOM    546  CE2 TRP A  91      -1.377   5.236  12.079  1.00 40.86           C  
ANISOU  546  CE2 TRP A  91     3798   7953   3774    279     38   1497       C  
ATOM    547  CE3 TRP A  91      -3.709   4.695  11.681  1.00 38.20           C  
ANISOU  547  CE3 TRP A  91     3601   7437   3478     24     41   1484       C  
ATOM    548  CZ2 TRP A  91      -1.087   5.205  10.714  1.00 40.27           C  
ANISOU  548  CZ2 TRP A  91     3838   7625   3837    382     67   1353       C  
ATOM    549  CZ3 TRP A  91      -3.419   4.644  10.330  1.00 39.87           C  
ANISOU  549  CZ3 TRP A  91     3936   7383   3830    123     65   1336       C  
ATOM    550  CH2 TRP A  91      -2.122   4.902   9.857  1.00 40.68           C  
ANISOU  550  CH2 TRP A  91     4025   7451   3979    305     80   1270       C  
ATOM    551  N   ALA A  92      -2.310   1.723  15.292  1.00 40.92           N  
ANISOU  551  N   ALA A  92     3835   8029   3683     45   -147   2494       N  
ATOM    552  CA  ALA A  92      -1.253   0.904  15.881  1.00 40.94           C  
ANISOU  552  CA  ALA A  92     3829   8021   3706    203   -198   2764       C  
ATOM    553  C   ALA A  92       0.147   1.091  15.281  1.00 43.09           C  
ANISOU  553  C   ALA A  92     4088   8230   4052    478   -178   2670       C  
ATOM    554  O   ALA A  92       1.100   0.523  15.803  1.00 41.94           O  
ANISOU  554  O   ALA A  92     3890   8150   3895    642   -217   2888       O  
ATOM    555  CB  ALA A  92      -1.669  -0.561  15.812  1.00 42.04           C  
ANISOU  555  CB  ALA A  92     4186   7800   3988    168   -259   3031       C  
ATOM    556  N   LEU A  93       0.272   1.895  14.210  1.00 39.62           N  
ANISOU  556  N   LEU A  93     3676   7708   3672    527   -120   2365       N  
ATOM    557  CA  LEU A  93       1.516   2.129  13.474  1.00 39.03           C  
ANISOU  557  CA  LEU A  93     3578   7596   3654    761    -94   2252       C  
ATOM    558  C   LEU A  93       2.455   3.229  14.043  1.00 42.46           C  
ANISOU  558  C   LEU A  93     3769   8453   3913    783    -83   2187       C  
ATOM    559  O   LEU A  93       3.582   3.368  13.557  1.00 42.03           O  
ANISOU  559  O   LEU A  93     3657   8438   3875    963    -69   2140       O  
ATOM    560  CB  LEU A  93       1.189   2.414  12.005  1.00 39.27           C  
ANISOU  560  CB  LEU A  93     3747   7360   3813    775    -42   1978       C  
ATOM    561  CG  LEU A  93       0.502   1.288  11.213  1.00 44.31           C  
ANISOU  561  CG  LEU A  93     4643   7561   4633    778    -54   2000       C  
ATOM    562  CD1 LEU A  93       0.078   1.781   9.849  1.00 43.96           C  
ANISOU  562  CD1 LEU A  93     4687   7354   4663    752     -1   1712       C  
ATOM    563  CD2 LEU A  93       1.377   0.038  11.109  1.00 47.56           C  
ANISOU  563  CD2 LEU A  93     5178   7721   5169   1029    -88   2181       C  
ATOM    564  N   GLY A  94       2.014   3.959  15.072  1.00 38.26           N  
ANISOU  564  N   GLY A  94     3089   8248   3199    597    -90   2183       N  
ATOM    565  CA  GLY A  94       2.813   5.008  15.701  1.00 36.98           C  
ANISOU  565  CA  GLY A  94     2716   8483   2853    568    -88   2105       C  
ATOM    566  C   GLY A  94       2.505   6.420  15.244  1.00 39.28           C  
ANISOU  566  C   GLY A  94     2991   8841   3093    441    -42   1783       C  
ATOM    567  O   GLY A  94       1.882   6.606  14.200  1.00 39.90           O  
ANISOU  567  O   GLY A  94     3210   8652   3298    431     -5   1615       O  
ATOM    568  N   ALA A  95       2.935   7.422  16.028  1.00 33.65           N  
ANISOU  568  N   ALA A  95     2114   8482   2189    340    -48   1698       N  
ATOM    569  CA  ALA A  95       2.723   8.849  15.787  1.00 32.88           C  
ANISOU  569  CA  ALA A  95     2014   8455   2026    213    -16   1401       C  
ATOM    570  C   ALA A  95       3.419   9.372  14.549  1.00 37.97           C  
ANISOU  570  C   ALA A  95     2715   8937   2773    277      9   1244       C  
ATOM    571  O   ALA A  95       2.909  10.298  13.921  1.00 38.47           O  
ANISOU  571  O   ALA A  95     2867   8877   2873    202     40   1020       O  
ATOM    572  CB  ALA A  95       3.136   9.663  16.997  1.00 33.43           C  
ANISOU  572  CB  ALA A  95     1912   8931   1859     85    -41   1358       C  
ATOM    573  N   LEU A  96       4.575   8.808  14.185  1.00 34.95           N  
ANISOU  573  N   LEU A  96     2276   8576   2429    424     -4   1367       N  
ATOM    574  CA  LEU A  96       5.263   9.288  12.986  1.00 34.87           C  
ANISOU  574  CA  LEU A  96     2293   8467   2490    477     23   1229       C  
ATOM    575  C   LEU A  96       4.586   8.798  11.698  1.00 36.95           C  
ANISOU  575  C   LEU A  96     2743   8343   2954    571     61   1161       C  
ATOM    576  O   LEU A  96       4.356   9.600  10.799  1.00 36.52           O  
ANISOU  576  O   LEU A  96     2757   8175   2944    510     91    972       O  
ATOM    577  CB  LEU A  96       6.752   8.956  13.007  1.00 35.10           C  
ANISOU  577  CB  LEU A  96     2159   8722   2455    607      2   1362       C  
ATOM    578  CG  LEU A  96       7.600   9.979  12.302  1.00 38.87           C  
ANISOU  578  CG  LEU A  96     2570   9320   2877    532     14   1205       C  
ATOM    579  CD1 LEU A  96       8.558  10.622  13.254  1.00 38.33           C  
ANISOU  579  CD1 LEU A  96     2294   9678   2593    408    -27   1242       C  
ATOM    580  CD2 LEU A  96       8.283   9.374  11.137  1.00 42.39           C  
ANISOU  580  CD2 LEU A  96     3028   9645   3432    735     42   1231       C  
ATOM    581  N   ALA A  97       4.191   7.512  11.655  1.00 32.02           N  
ANISOU  581  N   ALA A  97     2210   7515   2442    694     55   1318       N  
ATOM    582  CA  ALA A  97       3.479   6.891  10.547  1.00 31.21           C  
ANISOU  582  CA  ALA A  97     2294   7049   2515    759     82   1259       C  
ATOM    583  C   ALA A  97       2.123   7.548  10.348  1.00 36.84           C  
ANISOU  583  C   ALA A  97     3096   7663   3239    583    103   1103       C  
ATOM    584  O   ALA A  97       1.647   7.642   9.216  1.00 37.29           O  
ANISOU  584  O   ALA A  97     3266   7506   3396    588    134    968       O  
ATOM    585  CB  ALA A  97       3.290   5.412  10.820  1.00 31.57           C  
ANISOU  585  CB  ALA A  97     2434   6905   2656    879     55   1473       C  
ATOM    586  N   CYS A  98       1.518   8.013  11.451  1.00 33.77           N  
ANISOU  586  N   CYS A  98     2638   7464   2728    442     87   1120       N  
ATOM    587  CA  CYS A  98       0.215   8.672  11.507  1.00 33.79           C  
ANISOU  587  CA  CYS A  98     2686   7451   2702    303    106    985       C  
ATOM    588  C   CYS A  98       0.224  10.018  10.792  1.00 36.18           C  
ANISOU  588  C   CYS A  98     3007   7742   2996    262    136    746       C  
ATOM    589  O   CYS A  98      -0.594  10.226   9.896  1.00 35.62           O  
ANISOU  589  O   CYS A  98     3037   7491   3008    251    162    635       O  
ATOM    590  CB  CYS A  98      -0.247   8.808  12.956  1.00 34.53           C  
ANISOU  590  CB  CYS A  98     2672   7814   2635    195     84   1062       C  
ATOM    591  SG  CYS A  98      -1.625   9.947  13.191  1.00 39.00           S  
ANISOU  591  SG  CYS A  98     3239   8470   3108     68    115    852       S  
ATOM    592  N   ASP A  99       1.139  10.926  11.195  1.00 31.44           N  
ANISOU  592  N   ASP A  99     2314   7339   2292    224    125    681       N  
ATOM    593  CA  ASP A  99       1.278  12.268  10.629  1.00 30.54           C  
ANISOU  593  CA  ASP A  99     2234   7205   2163    157    140    476       C  
ATOM    594  C   ASP A  99       1.664  12.237   9.181  1.00 29.39           C  
ANISOU  594  C   ASP A  99     2159   6867   2141    226    161    434       C  
ATOM    595  O   ASP A  99       1.249  13.119   8.435  1.00 28.28           O  
ANISOU  595  O   ASP A  99     2098   6614   2035    181    178    289       O  
ATOM    596  CB  ASP A  99       2.297  13.096  11.417  1.00 33.78           C  
ANISOU  596  CB  ASP A  99     2537   7871   2427     65    111    438       C  
ATOM    597  CG  ASP A  99       1.932  13.383  12.866  1.00 47.69           C  
ANISOU  597  CG  ASP A  99     4224   9868   4028    -27     92    424       C  
ATOM    598  OD1 ASP A  99       0.753  13.134  13.251  1.00 48.59           O  
ANISOU  598  OD1 ASP A  99     4367   9958   4139    -21    107    428       O  
ATOM    599  OD2 ASP A  99       2.839  13.829  13.633  1.00 52.27           O  
ANISOU  599  OD2 ASP A  99     4700  10694   4467   -115     62    411       O  
ATOM    600  N   LEU A 100       2.455  11.219   8.773  1.00 23.86           N  
ANISOU  600  N   LEU A 100     1429   6137   1499    351    160    561       N  
ATOM    601  CA  LEU A 100       2.863  11.020   7.377  1.00 22.10           C  
ANISOU  601  CA  LEU A 100     1257   5764   1376    442    185    519       C  
ATOM    602  C   LEU A 100       1.664  10.541   6.543  1.00 24.14           C  
ANISOU  602  C   LEU A 100     1657   5761   1753    466    210    468       C  
ATOM    603  O   LEU A 100       1.463  11.011   5.427  1.00 24.39           O  
ANISOU  603  O   LEU A 100     1746   5687   1833    458    233    357       O  
ATOM    604  CB  LEU A 100       4.044  10.034   7.254  1.00 21.39           C  
ANISOU  604  CB  LEU A 100     1088   5741   1298    608    181    652       C  
ATOM    605  CG  LEU A 100       5.372  10.473   7.848  1.00 24.89           C  
ANISOU  605  CG  LEU A 100     1356   6494   1608    592    158    710       C  
ATOM    606  CD1 LEU A 100       6.384   9.349   7.804  1.00 24.93           C  
ANISOU  606  CD1 LEU A 100     1274   6575   1623    811    155    865       C  
ATOM    607  CD2 LEU A 100       5.889  11.729   7.195  1.00 25.66           C  
ANISOU  607  CD2 LEU A 100     1419   6681   1649    465    164    578       C  
ATOM    608  N   ALA A 101       0.877   9.615   7.099  1.00 19.22           N  
ANISOU  608  N   ALA A 101     1079   5060   1162    473    200    563       N  
ATOM    609  CA  ALA A 101      -0.324   9.056   6.495  1.00 18.99           C  
ANISOU  609  CA  ALA A 101     1172   4823   1221    452    213    535       C  
ATOM    610  C   ALA A 101      -1.345  10.163   6.249  1.00 23.95           C  
ANISOU  610  C   ALA A 101     1818   5467   1816    347    229    392       C  
ATOM    611  O   ALA A 101      -1.954  10.187   5.182  1.00 24.92           O  
ANISOU  611  O   ALA A 101     2015   5454   2001    345    249    310       O  
ATOM    612  CB  ALA A 101      -0.926   7.988   7.408  1.00 19.44           C  
ANISOU  612  CB  ALA A 101     1253   4849   1283    425    186    694       C  
ATOM    613  N   LEU A 102      -1.527  11.069   7.236  1.00 18.67           N  
ANISOU  613  N   LEU A 102     1081   4974   1040    274    220    359       N  
ATOM    614  CA  LEU A 102      -2.433  12.214   7.185  1.00 17.42           C  
ANISOU  614  CA  LEU A 102      940   4841    837    216    234    219       C  
ATOM    615  C   LEU A 102      -1.944  13.224   6.180  1.00 21.13           C  
ANISOU  615  C   LEU A 102     1451   5236   1339    225    244    102       C  
ATOM    616  O   LEU A 102      -2.770  13.816   5.497  1.00 22.89           O  
ANISOU  616  O   LEU A 102     1732   5377   1588    225    259     13       O  
ATOM    617  CB  LEU A 102      -2.537  12.889   8.562  1.00 17.31           C  
ANISOU  617  CB  LEU A 102      852   5035    690    160    221    193       C  
ATOM    618  CG  LEU A 102      -3.245  12.140   9.687  1.00 20.88           C  
ANISOU  618  CG  LEU A 102     1239   5629   1066    123    212    305       C  
ATOM    619  CD1 LEU A 102      -2.976  12.815  11.007  1.00 20.40           C  
ANISOU  619  CD1 LEU A 102     1086   5815    852     75    199    270       C  
ATOM    620  CD2 LEU A 102      -4.749  12.010   9.425  1.00 20.83           C  
ANISOU  620  CD2 LEU A 102     1256   5596   1062    102    232    277       C  
ATOM    621  N   ALA A 103      -0.608  13.421   6.079  1.00 16.87           N  
ANISOU  621  N   ALA A 103      885   4698    826    227    153    122       N  
ATOM    622  CA  ALA A 103       0.021  14.334   5.109  1.00 16.43           C  
ANISOU  622  CA  ALA A 103      863   4561    818    199     99     49       C  
ATOM    623  C   ALA A 103      -0.207  13.848   3.682  1.00 21.88           C  
ANISOU  623  C   ALA A 103     1584   5200   1529    267    260     38       C  
ATOM    624  O   ALA A 103      -0.610  14.646   2.833  1.00 22.57           O  
ANISOU  624  O   ALA A 103     1727   5210   1636    241    267    -36       O  
ATOM    625  CB  ALA A 103       1.506  14.463   5.382  1.00 16.78           C  
ANISOU  625  CB  ALA A 103      815   4778    781    173    108     94       C  
ATOM    626  N   LEU A 104       0.004  12.535   3.422  1.00 18.20           N  
ANISOU  626  N   LEU A 104     1110   4691   1115    355    271    112       N  
ATOM    627  CA  LEU A 104      -0.217  11.944   2.101  1.00 18.03           C  
ANISOU  627  CA  LEU A 104     1144   4541   1167    415    295     80       C  
ATOM    628  C   LEU A 104      -1.682  12.046   1.696  1.00 22.48           C  
ANISOU  628  C   LEU A 104     1780   5004   1758    370    303     25       C  
ATOM    629  O   LEU A 104      -1.996  12.343   0.543  1.00 23.57           O  
ANISOU  629  O   LEU A 104     1950   5090   1916    368    317    -38       O  
ATOM    630  CB  LEU A 104       0.263  10.485   2.065  1.00 17.99           C  
ANISOU  630  CB  LEU A 104     1149   4475   1213    531    300    153       C  
ATOM    631  CG  LEU A 104       0.087   9.715   0.730  1.00 22.70           C  
ANISOU  631  CG  LEU A 104     1821   4927   1878    601    325     89       C  
ATOM    632  CD1 LEU A 104       0.630  10.498  -0.473  1.00 21.85           C  
ANISOU  632  CD1 LEU A 104     1673   4893   1738    603    348      7       C  
ATOM    633  CD2 LEU A 104       0.778   8.382   0.791  1.00 26.74           C  
ANISOU  633  CD2 LEU A 104     2359   5362   2439    749    327    147       C  
ATOM    634  N   ASP A 105      -2.555  11.842   2.656  1.00 18.40           N  
ANISOU  634  N   ASP A 105     1266   4506   1221    330    292     58       N  
ATOM    635  CA  ASP A 105      -3.990  11.903   2.496  1.00 18.92           C  
ANISOU  635  CA  ASP A 105     1360   4547   1281    284    297     24       C  
ATOM    636  C   ASP A 105      -4.508  13.286   2.091  1.00 24.14           C  
ANISOU  636  C   ASP A 105     2026   5237   1911    278    303    -66       C  
ATOM    637  O   ASP A 105      -5.294  13.383   1.154  1.00 24.56           O  
ANISOU  637  O   ASP A 105     2101   5251   1977    279    313   -103       O  
ATOM    638  CB  ASP A 105      -4.671  11.437   3.793  1.00 20.60           C  
ANISOU  638  CB  ASP A 105     1540   4843   1446    237    283     97       C  
ATOM    639  CG  ASP A 105      -6.160  11.268   3.654  1.00 34.07           C  
ANISOU  639  CG  ASP A 105     3245   6576   3125    178    288     85       C  
ATOM    640  OD1 ASP A 105      -6.614  10.891   2.558  1.00 33.39           O  
ANISOU  640  OD1 ASP A 105     3204   6401   3082    162    294     54       O  
ATOM    641  OD2 ASP A 105      -6.872  11.510   4.637  1.00 47.37           O  
ANISOU  641  OD2 ASP A 105     4868   8404   4727    145    285    103       O  
ATOM    642  N   TYR A 106      -4.113  14.328   2.821  1.00 21.17           N  
ANISOU  642  N   TYR A 106     1634   4923   1486    270    292    -99       N  
ATOM    643  CA  TYR A 106      -4.561  15.701   2.636  1.00 21.57           C  
ANISOU  643  CA  TYR A 106     1723   4958   1514    280    290   -184       C  
ATOM    644  C   TYR A 106      -3.980  16.376   1.402  1.00 25.19           C  
ANISOU  644  C   TYR A 106     2230   5330   2013    276    287   -202       C  
ATOM    645  O   TYR A 106      -4.651  17.201   0.778  1.00 27.08           O  
ANISOU  645  O   TYR A 106     2516   5515   2259    304    286   -238       O  
ATOM    646  CB  TYR A 106      -4.247  16.508   3.897  1.00 24.21           C  
ANISOU  646  CB  TYR A 106     2052   5366   1780    257    275   -231       C  
ATOM    647  CG  TYR A 106      -5.221  17.619   4.185  1.00 27.90           C  
ANISOU  647  CG  TYR A 106     2563   5830   2208    308    278   -331       C  
ATOM    648  CD1 TYR A 106      -5.147  18.829   3.505  1.00 30.94           C  
ANISOU  648  CD1 TYR A 106     3047   6087   2621    329    266   -397       C  
ATOM    649  CD2 TYR A 106      -6.234  17.457   5.118  1.00 28.74           C  
ANISOU  649  CD2 TYR A 106     2612   6065   2243    348    292   -350       C  
ATOM    650  CE1 TYR A 106      -6.066  19.847   3.737  1.00 33.08           C  
ANISOU  650  CE1 TYR A 106     3377   6326   2866    423    268   -491       C  
ATOM    651  CE2 TYR A 106      -7.142  18.481   5.382  1.00 30.28           C  
ANISOU  651  CE2 TYR A 106     2835   6281   2389    441    301   -456       C  
ATOM    652  CZ  TYR A 106      -7.048  19.680   4.692  1.00 40.91           C  
ANISOU  652  CZ  TYR A 106     4299   7465   3780    496    289   -532       C  
ATOM    653  OH  TYR A 106      -7.927  20.711   4.914  1.00 47.35           O  
ANISOU  653  OH  TYR A 106     5164   8268   4558    631    297   -639       O  
ATOM    654  N   VAL A 107      -2.738  16.053   1.063  1.00 19.33           N  
ANISOU  654  N   VAL A 107     1463   4599   1284    247    284   -163       N  
ATOM    655  CA  VAL A 107      -2.061  16.616  -0.091  1.00 18.27           C  
ANISOU  655  CA  VAL A 107     1345   4436   1162    220    281   -159       C  
ATOM    656  C   VAL A 107      -2.673  16.050  -1.380  1.00 22.21           C  
ANISOU  656  C   VAL A 107     1846   4901   1693    263    303   -157       C  
ATOM    657  O   VAL A 107      -2.868  16.814  -2.327  1.00 22.43           O  
ANISOU  657  O   VAL A 107     1902   4902   1719    249    298   -158       O  
ATOM    658  CB  VAL A 107      -0.539  16.390   0.014  1.00 22.57           C  
ANISOU  658  CB  VAL A 107     1822   5075   1679    182    275   -116       C  
ATOM    659  CG1 VAL A 107       0.164  16.553  -1.335  1.00 22.21           C  
ANISOU  659  CG1 VAL A 107     1752   5061   1627    161    283    -94       C  
ATOM    660  CG2 VAL A 107       0.071  17.317   1.062  1.00 22.70           C  
ANISOU  660  CG2 VAL A 107     1842   5144   1641     89    243   -130       C  
ATOM    661  N   ALA A 108      -3.001  14.733  -1.409  1.00 17.08           N  
ANISOU  661  N   ALA A 108     1194   4192   1105    292    236   -139       N  
ATOM    662  CA  ALA A 108      -3.616  14.071  -2.569  1.00 16.14           C  
ANISOU  662  CA  ALA A 108     1104   3988   1040    295    164   -149       C  
ATOM    663  C   ALA A 108      -5.058  14.534  -2.794  1.00 21.80           C  
ANISOU  663  C   ALA A 108     1798   4823   1660    308    334   -191       C  
ATOM    664  O   ALA A 108      -5.475  14.713  -3.941  1.00 21.09           O  
ANISOU  664  O   ALA A 108     1705   4753   1555    305    338   -205       O  
ATOM    665  CB  ALA A 108      -3.561  12.563  -2.412  1.00 16.34           C  
ANISOU  665  CB  ALA A 108     1136   4001   1071    325    222   -152       C  
ATOM    666  N   SER A 109      -5.806  14.748  -1.695  1.00 20.36           N  
ANISOU  666  N   SER A 109     1613   4662   1462    311    325   -187       N  
ATOM    667  CA  SER A 109      -7.184  15.238  -1.692  1.00 20.51           C  
ANISOU  667  CA  SER A 109     1615   4735   1442    334    324   -199       C  
ATOM    668  C   SER A 109      -7.244  16.681  -2.198  1.00 25.95           C  
ANISOU  668  C   SER A 109     2338   5397   2126    389    313   -209       C  
ATOM    669  O   SER A 109      -8.167  17.016  -2.941  1.00 26.77           O  
ANISOU  669  O   SER A 109     2423   5543   2204    428    313   -201       O  
ATOM    670  CB  SER A 109      -7.761  15.149  -0.290  1.00 24.42           C  
ANISOU  670  CB  SER A 109     2080   5299   1899    338    323   -197       C  
ATOM    671  OG  SER A 109      -7.782  13.797   0.134  1.00 34.12           O  
ANISOU  671  OG  SER A 109     3290   6539   3136    272    323   -154       O  
ATOM    672  N   ASN A 110      -6.256  17.524  -1.810  1.00 22.09           N  
ANISOU  672  N   ASN A 110     1902   4838   1655    380    299   -216       N  
ATOM    673  CA  ASN A 110      -6.182  18.908  -2.259  1.00 21.52           C  
ANISOU  673  CA  ASN A 110     1902   4684   1591    406    278   -212       C  
ATOM    674  C   ASN A 110      -5.684  18.973  -3.690  1.00 26.00           C  
ANISOU  674  C   ASN A 110     2464   5247   2166    364    274   -154       C  
ATOM    675  O   ASN A 110      -6.124  19.852  -4.423  1.00 26.23           O  
ANISOU  675  O   ASN A 110     2533   5240   2194    400    257   -115       O  
ATOM    676  CB  ASN A 110      -5.314  19.761  -1.342  1.00 22.92           C  
ANISOU  676  CB  ASN A 110     2151   4785   1773    362    255   -244       C  
ATOM    677  CG  ASN A 110      -5.448  21.249  -1.629  1.00 45.05           C  
ANISOU  677  CG  ASN A 110     5076   7448   4595    392    225   -250       C  
ATOM    678  OD1 ASN A 110      -6.432  21.899  -1.260  1.00 30.88           O  
ANISOU  678  OD1 ASN A 110     3331   5610   2794    510    223   -299       O  
ATOM    679  ND2 ASN A 110      -4.459  21.833  -2.288  1.00 39.96           N  
ANISOU  679  ND2 ASN A 110     4486   6731   3967    289    198   -194       N  
ATOM    680  N   ALA A 111      -4.769  18.052  -4.095  1.00 22.93           N  
ANISOU  680  N   ALA A 111     2024   4912   1777    303    289   -145       N  
ATOM    681  CA  ALA A 111      -4.206  17.983  -5.452  1.00 22.16           C  
ANISOU  681  CA  ALA A 111     1895   4867   1659    265    294   -106       C  
ATOM    682  C   ALA A 111      -5.292  17.703  -6.470  1.00 25.92           C  
ANISOU  682  C   ALA A 111     2339   5403   2107    300    303   -103       C  
ATOM    683  O   ALA A 111      -5.224  18.213  -7.585  1.00 26.68           O  
ANISOU  683  O   ALA A 111     2422   5544   2169    282    294    -51       O  
ATOM    684  CB  ALA A 111      -3.131  16.917  -5.537  1.00 22.78           C  
ANISOU  684  CB  ALA A 111     1914   5011   1730    245    317   -126       C  
ATOM    685  N   ALA A 112      -6.297  16.913  -6.081  1.00 22.05           N  
ANISOU  685  N   ALA A 112     1826   4937   1615    330    315   -146       N  
ATOM    686  CA  ALA A 112      -7.465  16.600  -6.897  1.00 21.30           C  
ANISOU  686  CA  ALA A 112     1685   4937   1473    338    318   -148       C  
ATOM    687  C   ALA A 112      -8.287  17.882  -7.153  1.00 25.72           C  
ANISOU  687  C   ALA A 112     2249   5512   2009    413    295    -85       C  
ATOM    688  O   ALA A 112      -8.640  18.135  -8.301  1.00 25.48           O  
ANISOU  688  O   ALA A 112     2181   5570   1931    415    288    -37       O  
ATOM    689  CB  ALA A 112      -8.318  15.535  -6.217  1.00 21.73           C  
ANISOU  689  CB  ALA A 112     1714   5021   1521    316    328   -193       C  
ATOM    690  N   VAL A 113      -8.536  18.711  -6.101  1.00 22.57           N  
ANISOU  690  N   VAL A 113     1904   5031   1640    487    284    -85       N  
ATOM    691  CA  VAL A 113      -9.257  20.000  -6.169  1.00 22.37           C  
ANISOU  691  CA  VAL A 113     1919   4970   1610    607    261    -37       C  
ATOM    692  C   VAL A 113      -8.488  20.991  -7.078  1.00 27.17           C  
ANISOU  692  C   VAL A 113     2601   5482   2240    582    232     51       C  
ATOM    693  O   VAL A 113      -9.102  21.679  -7.901  1.00 26.86           O  
ANISOU  693  O   VAL A 113     2561   5469   2176    655    211    138       O  
ATOM    694  CB  VAL A 113      -9.503  20.617  -4.769  1.00 26.33           C  
ANISOU  694  CB  VAL A 113     2484   5386   2135    698    259    -97       C  
ATOM    695  CG1 VAL A 113     -10.308  21.912  -4.875  1.00 26.17           C  
ANISOU  695  CG1 VAL A 113     2523   5307   2112    869    238    -65       C  
ATOM    696  CG2 VAL A 113     -10.188  19.628  -3.825  1.00 26.43           C  
ANISOU  696  CG2 VAL A 113     2406   5531   2105    695    286   -159       C  
ATOM    697  N   MET A 114      -7.147  21.039  -6.932  1.00 24.59           N  
ANISOU  697  N   MET A 114     2325   5072   1946    470    226     49       N  
ATOM    698  CA  MET A 114      -6.253  21.898  -7.720  1.00 25.55           C  
ANISOU  698  CA  MET A 114     2504   5130   2073    390    196    147       C  
ATOM    699  C   MET A 114      -6.262  21.515  -9.184  1.00 29.79           C  
ANISOU  699  C   MET A 114     2945   5832   2543    348    202    219       C  
ATOM    700  O   MET A 114      -6.165  22.403 -10.033  1.00 29.30           O  
ANISOU  700  O   MET A 114     2915   5754   2464    327    170    344       O  
ATOM    701  CB  MET A 114      -4.810  21.827  -7.201  1.00 28.22           C  
ANISOU  701  CB  MET A 114     2866   5428   2427    257    193    123       C  
ATOM    702  CG  MET A 114      -4.635  22.390  -5.828  1.00 32.24           C  
ANISOU  702  CG  MET A 114     3477   5790   2981    262    177     55       C  
ATOM    703  SD  MET A 114      -3.793  23.966  -5.880  1.00 36.92           S  
ANISOU  703  SD  MET A 114     4235   6189   3603    141    115    130       S  
ATOM    704  CE  MET A 114      -5.211  25.066  -6.103  1.00 33.13           C  
ANISOU  704  CE  MET A 114     3888   5532   3167    326     86    170       C  
ATOM    705  N   ASN A 115      -6.355  20.189  -9.474  1.00 27.10           N  
ANISOU  705  N   ASN A 115     2495   5641   2160    328    241    141       N  
ATOM    706  CA  ASN A 115      -6.417  19.637 -10.831  1.00 27.30           C  
ANISOU  706  CA  ASN A 115     2421   5851   2100    286    255    160       C  
ATOM    707  C   ASN A 115      -7.745  19.957 -11.490  1.00 31.79           C  
ANISOU  707  C   ASN A 115     2947   6516   2617    358    239    221       C  
ATOM    708  O   ASN A 115      -7.777  20.188 -12.695  1.00 31.76           O  
ANISOU  708  O   ASN A 115     2884   6649   2534    327    227    304       O  
ATOM    709  CB  ASN A 115      -6.152  18.138 -10.842  1.00 28.34           C  
ANISOU  709  CB  ASN A 115     2491   6063   2212    252    297     30       C  
ATOM    710  CG  ASN A 115      -4.691  17.802 -10.728  1.00 57.59           C  
ANISOU  710  CG  ASN A 115     6190   9767   5925    202    315      1       C  
ATOM    711  OD1 ASN A 115      -3.822  18.395 -11.388  1.00 50.25           O  
ANISOU  711  OD1 ASN A 115     5233   8909   4950    144    306     77       O  
ATOM    712  ND2 ASN A 115      -4.386  16.835  -9.884  1.00 52.87           N  
ANISOU  712  ND2 ASN A 115     5604   9111   5373    222    338    -92       N  
ATOM    713  N   LEU A 116      -8.840  20.002 -10.700  1.00 28.39           N  
ANISOU  713  N   LEU A 116     2525   6053   2209    457    237    191       N  
ATOM    714  CA  LEU A 116     -10.176  20.347 -11.192  1.00 27.97           C  
ANISOU  714  CA  LEU A 116     2405   6130   2092    553    220    258       C  
ATOM    715  C   LEU A 116     -10.163  21.817 -11.591  1.00 30.80           C  
ANISOU  715  C   LEU A 116     2840   6392   2472    642    178    413       C  
ATOM    716  O   LEU A 116     -10.727  22.175 -12.626  1.00 30.98           O  
ANISOU  716  O   LEU A 116     2796   6557   2420    680    156    529       O  
ATOM    717  CB  LEU A 116     -11.245  20.090 -10.123  1.00 28.23           C  
ANISOU  717  CB  LEU A 116     2413   6182   2131    645    232    192       C  
ATOM    718  CG  LEU A 116     -11.602  18.639  -9.834  1.00 33.00           C  
ANISOU  718  CG  LEU A 116     2938   6903   2696    543    260     80       C  
ATOM    719  CD1 LEU A 116     -12.157  18.497  -8.453  1.00 32.93           C  
ANISOU  719  CD1 LEU A 116     2937   6861   2716    597    271     25       C  
ATOM    720  CD2 LEU A 116     -12.596  18.120 -10.820  1.00 37.52           C  
ANISOU  720  CD2 LEU A 116     3379   7726   3149    502    255     97       C  
ATOM    721  N   LEU A 117      -9.464  22.656 -10.795  1.00 25.97           N  
ANISOU  721  N   LEU A 117     2377   5534   1958    657    160    420       N  
ATOM    722  CA  LEU A 117      -9.281  24.081 -11.071  1.00 25.03           C  
ANISOU  722  CA  LEU A 117     2388   5239   1882    711    110    563       C  
ATOM    723  C   LEU A 117      -8.456  24.263 -12.358  1.00 27.83           C  
ANISOU  723  C   LEU A 117     2714   5675   2184    565     89    700       C  
ATOM    724  O   LEU A 117      -8.786  25.120 -13.179  1.00 27.52           O  
ANISOU  724  O   LEU A 117     2700   5634   2122    614     46    872       O  
ATOM    725  CB  LEU A 117      -8.614  24.784  -9.879  1.00 24.75           C  
ANISOU  725  CB  LEU A 117     2530   4923   1952    705     94    502       C  
ATOM    726  CG  LEU A 117      -9.526  25.130  -8.717  1.00 28.49           C  
ANISOU  726  CG  LEU A 117     3064   5296   2465    896    101    404       C  
ATOM    727  CD1 LEU A 117      -8.746  25.285  -7.450  1.00 28.52           C  
ANISOU  727  CD1 LEU A 117     3182   5122   2533    831    104    279       C  
ATOM    728  CD2 LEU A 117     -10.292  26.400  -8.987  1.00 30.74           C  
ANISOU  728  CD2 LEU A 117     3458   5443   2777   1095     59    513       C  
ATOM    729  N   LEU A 118      -7.428  23.412 -12.562  1.00 23.38           N  
ANISOU  729  N   LEU A 118     2081   5215   1587    401    119    631       N  
ATOM    730  CA  LEU A 118      -6.613  23.433 -13.782  1.00 22.71           C  
ANISOU  730  CA  LEU A 118     1927   5286   1417    261    112    737       C  
ATOM    731  C   LEU A 118      -7.458  23.050 -15.011  1.00 26.77           C  
ANISOU  731  C   LEU A 118     2295   6068   1807    295    116    794       C  
ATOM    732  O   LEU A 118      -7.340  23.703 -16.039  1.00 28.69           O  
ANISOU  732  O   LEU A 118     2513   6404   1982    252     82    969       O  
ATOM    733  CB  LEU A 118      -5.371  22.519 -13.670  1.00 22.14           C  
ANISOU  733  CB  LEU A 118     1788   5304   1318    129    153    622       C  
ATOM    734  CG  LEU A 118      -4.211  22.982 -12.801  1.00 25.10           C  
ANISOU  734  CG  LEU A 118     2260   5515   1762     35    140    616       C  
ATOM    735  CD1 LEU A 118      -3.166  21.899 -12.705  1.00 24.59           C  
ANISOU  735  CD1 LEU A 118     2090   5598   1653    -36    188    500       C  
ATOM    736  CD2 LEU A 118      -3.568  24.240 -13.347  1.00 26.80           C  
ANISOU  736  CD2 LEU A 118     2550   5668   1965    -89     83    809       C  
ATOM    737  N   ILE A 119      -8.314  22.018 -14.904  1.00 21.51           N  
ANISOU  737  N   ILE A 119     1533   5538   1102    350    152    657       N  
ATOM    738  CA  ILE A 119      -9.198  21.592 -15.996  1.00 21.04           C  
ANISOU  738  CA  ILE A 119     1328   5760    908    358    153    685       C  
ATOM    739  C   ILE A 119     -10.161  22.742 -16.340  1.00 26.42           C  
ANISOU  739  C   ILE A 119     2019   6442   1575    495    101    883       C  
ATOM    740  O   ILE A 119     -10.356  23.025 -17.518  1.00 26.50           O  
ANISOU  740  O   ILE A 119     1939   6658   1472    472     77   1025       O  
ATOM    741  CB  ILE A 119      -9.959  20.276 -15.626  1.00 23.99           C  
ANISOU  741  CB  ILE A 119     1624   6239   1251    355    191    494       C  
ATOM    742  CG1 ILE A 119      -8.995  19.080 -15.491  1.00 23.52           C  
ANISOU  742  CG1 ILE A 119     1567   6170   1200    243    237    315       C  
ATOM    743  CG2 ILE A 119     -11.112  19.963 -16.614  1.00 25.75           C  
ANISOU  743  CG2 ILE A 119     1697   6764   1324    355    181    525       C  
ATOM    744  CD1 ILE A 119      -9.500  17.919 -14.624  1.00 27.95           C  
ANISOU  744  CD1 ILE A 119     2138   6681   1801    235    265    144       C  
ATOM    745  N   SER A 120     -10.756  23.396 -15.305  1.00 24.07           N  
ANISOU  745  N   SER A 120     1830   5931   1386    653     86    890       N  
ATOM    746  CA  SER A 120     -11.707  24.503 -15.443  1.00 23.73           C  
ANISOU  746  CA  SER A 120     1820   5846   1348    849     40   1060       C  
ATOM    747  C   SER A 120     -11.085  25.734 -16.081  1.00 27.82           C  
ANISOU  747  C   SER A 120     2457   6215   1898    833    -17   1283       C  
ATOM    748  O   SER A 120     -11.694  26.285 -16.994  1.00 26.65           O  
ANISOU  748  O   SER A 120     2250   6202   1674    915    -56   1477       O  
ATOM    749  CB  SER A 120     -12.327  24.858 -14.099  1.00 27.81           C  
ANISOU  749  CB  SER A 120     2437   6162   1969   1032     46    972       C  
ATOM    750  OG  SER A 120     -12.950  23.724 -13.521  1.00 38.60           O  
ANISOU  750  OG  SER A 120     3681   7696   3290   1024     92    800       O  
ATOM    751  N   PHE A 121      -9.863  26.149 -15.638  1.00 25.74           N  
ANISOU  751  N   PHE A 121     2351   5697   1732    706    -28   1276       N  
ATOM    752  CA  PHE A 121      -9.169  27.324 -16.200  1.00 25.89           C  
ANISOU  752  CA  PHE A 121     2502   5553   1780    630    -90   1501       C  
ATOM    753  C   PHE A 121      -8.691  27.103 -17.644  1.00 30.32           C  
ANISOU  753  C   PHE A 121     2911   6417   2191    463    -99   1649       C  
ATOM    754  O   PHE A 121      -8.841  27.992 -18.491  1.00 29.76           O  
ANISOU  754  O   PHE A 121     2867   6357   2083    477   -157   1902       O  
ATOM    755  CB  PHE A 121      -8.035  27.811 -15.300  1.00 27.90           C  
ANISOU  755  CB  PHE A 121     2950   5495   2155    503   -104   1447       C  
ATOM    756  CG  PHE A 121      -8.447  28.759 -14.190  1.00 30.15           C  
ANISOU  756  CG  PHE A 121     3463   5408   2586    672   -135   1410       C  
ATOM    757  CD1 PHE A 121      -8.713  28.287 -12.910  1.00 34.07           C  
ANISOU  757  CD1 PHE A 121     3979   5825   3140    760    -91   1175       C  
ATOM    758  CD2 PHE A 121      -8.516  30.129 -14.412  1.00 32.52           C  
ANISOU  758  CD2 PHE A 121     3967   5429   2958    743   -211   1608       C  
ATOM    759  CE1 PHE A 121      -9.052  29.166 -11.875  1.00 35.21           C  
ANISOU  759  CE1 PHE A 121     4329   5653   3397    922   -114   1113       C  
ATOM    760  CE2 PHE A 121      -8.861  31.006 -13.381  1.00 35.34           C  
ANISOU  760  CE2 PHE A 121     4559   5420   3447    918   -237   1539       C  
ATOM    761  CZ  PHE A 121      -9.122  30.520 -12.119  1.00 34.04           C  
ANISOU  761  CZ  PHE A 121     4397   5215   3324   1007   -185   1279       C  
ATOM    762  N   ASP A 122      -8.175  25.901 -17.939  1.00 26.49           N  
ANISOU  762  N   ASP A 122     2265   6189   1610    323    -40   1492       N  
ATOM    763  CA  ASP A 122      -7.742  25.533 -19.281  1.00 26.04           C  
ANISOU  763  CA  ASP A 122     2039   6474   1382    178    -34   1576       C  
ATOM    764  C   ASP A 122      -8.919  25.573 -20.246  1.00 32.43           C  
ANISOU  764  C   ASP A 122     2710   7546   2064    282    -55   1698       C  
ATOM    765  O   ASP A 122      -8.790  26.124 -21.327  1.00 33.28           O  
ANISOU  765  O   ASP A 122     2757   7825   2062    218    -95   1922       O  
ATOM    766  CB  ASP A 122      -7.125  24.143 -19.277  1.00 27.36           C  
ANISOU  766  CB  ASP A 122     2080   6835   1481     72     39   1330       C  
ATOM    767  CG  ASP A 122      -6.568  23.763 -20.615  1.00 35.54           C  
ANISOU  767  CG  ASP A 122     2943   8236   2326    -66     54   1378       C  
ATOM    768  OD1 ASP A 122      -5.612  24.436 -21.073  1.00 35.92           O  
ANISOU  768  OD1 ASP A 122     3000   8316   2334   -200     27   1546       O  
ATOM    769  OD2 ASP A 122      -7.086  22.806 -21.215  1.00 41.60           O  
ANISOU  769  OD2 ASP A 122     3564   9272   2970    -57     91   1245       O  
ATOM    770  N   ARG A 123     -10.072  25.011 -19.847  1.00 30.43           N  
ANISOU  770  N   ARG A 123     2397   7356   1810    429    -32   1568       N  
ATOM    771  CA  ARG A 123     -11.311  25.012 -20.633  1.00 30.03           C  
ANISOU  771  CA  ARG A 123     2192   7591   1626    536    -53   1672       C  
ATOM    772  C   ARG A 123     -11.830  26.434 -20.789  1.00 35.48           C  
ANISOU  772  C   ARG A 123     2980   8134   2366    709   -126   1964       C  
ATOM    773  O   ARG A 123     -12.424  26.746 -21.813  1.00 35.66           O  
ANISOU  773  O   ARG A 123     2877   8418   2253    750   -163   2163       O  
ATOM    774  CB  ARG A 123     -12.391  24.154 -19.949  1.00 27.95           C  
ANISOU  774  CB  ARG A 123     1854   7404   1361    638    -16   1471       C  
ATOM    775  CG  ARG A 123     -12.264  22.671 -20.177  1.00 34.90           C  
ANISOU  775  CG  ARG A 123     2606   8513   2141    475     40   1225       C  
ATOM    776  CD  ARG A 123     -12.758  22.286 -21.537  1.00 50.66           C  
ANISOU  776  CD  ARG A 123     4401  10931   3915    390     30   1280       C  
ATOM    777  NE  ARG A 123     -12.298  20.945 -21.884  1.00 69.88           N  
ANISOU  777  NE  ARG A 123     6765  13527   6261    210     83   1030       N  
ATOM    778  CZ  ARG A 123     -11.398  20.674 -22.825  1.00 90.67           C  
ANISOU  778  CZ  ARG A 123     9333  16344   8775     72     99   1009       C  
ATOM    779  NH1 ARG A 123     -10.853  21.656 -23.538  1.00 78.82           N  
ANISOU  779  NH1 ARG A 123     7812  14916   7219     59     63   1251       N  
ATOM    780  NH2 ARG A 123     -11.039  19.420 -23.067  1.00 79.89           N  
ANISOU  780  NH2 ARG A 123     7925  15092   7338    -50    149    749       N  
ATOM    781  N   TYR A 124     -11.611  27.292 -19.772  1.00 33.47           N  
ANISOU  781  N   TYR A 124     2958   7457   2302    816   -149   1985       N  
ATOM    782  CA  TYR A 124     -12.042  28.686 -19.770  1.00 33.79           C  
ANISOU  782  CA  TYR A 124     3158   7252   2428   1008   -222   2236       C  
ATOM    783  C   TYR A 124     -11.273  29.504 -20.766  1.00 38.48           C  
ANISOU  783  C   TYR A 124     3808   7827   2984    862   -284   2522       C  
ATOM    784  O   TYR A 124     -11.891  30.191 -21.571  1.00 38.09           O  
ANISOU  784  O   TYR A 124     3726   7877   2871    979   -341   2789       O  
ATOM    785  CB  TYR A 124     -11.959  29.308 -18.361  1.00 35.34           C  
ANISOU  785  CB  TYR A 124     3609   6986   2831   1143   -226   2128       C  
ATOM    786  CG  TYR A 124     -12.154  30.809 -18.336  1.00 37.84           C  
ANISOU  786  CG  TYR A 124     4163   6952   3263   1318   -306   2366       C  
ATOM    787  CD1 TYR A 124     -13.422  31.370 -18.451  1.00 39.91           C  
ANISOU  787  CD1 TYR A 124     4409   7240   3516   1646   -336   2492       C  
ATOM    788  CD2 TYR A 124     -11.069  31.670 -18.202  1.00 39.23           C  
ANISOU  788  CD2 TYR A 124     4584   6769   3552   1157   -357   2469       C  
ATOM    789  CE1 TYR A 124     -13.606  32.753 -18.430  1.00 41.44           C  
ANISOU  789  CE1 TYR A 124     4851   7067   3829   1843   -413   2711       C  
ATOM    790  CE2 TYR A 124     -11.239  33.055 -18.198  1.00 40.62           C  
ANISOU  790  CE2 TYR A 124     5020   6567   3845   1302   -440   2690       C  
ATOM    791  CZ  TYR A 124     -12.510  33.594 -18.309  1.00 50.28           C  
ANISOU  791  CZ  TYR A 124     6249   7778   5075   1663   -467   2807       C  
ATOM    792  OH  TYR A 124     -12.675  34.963 -18.299  1.00 53.24           O  
ANISOU  792  OH  TYR A 124     6911   7737   5579   1840   -553   3024       O  
ATOM    793  N   PHE A 125      -9.932  29.452 -20.704  1.00 36.14           N  
ANISOU  793  N   PHE A 125     3587   7427   2718    605   -277   2487       N  
ATOM    794  CA  PHE A 125      -9.059  30.225 -21.590  1.00 35.80           C  
ANISOU  794  CA  PHE A 125     3594   7382   2628    410   -337   2766       C  
ATOM    795  C   PHE A 125      -9.040  29.724 -23.031  1.00 41.23           C  
ANISOU  795  C   PHE A 125     4013   8578   3075    284   -330   2888       C  
ATOM    796  O   PHE A 125      -8.882  30.542 -23.930  1.00 42.06           O  
ANISOU  796  O   PHE A 125     4128   8741   3113    216   -397   3208       O  
ATOM    797  CB  PHE A 125      -7.646  30.335 -21.018  1.00 36.91           C  
ANISOU  797  CB  PHE A 125     3871   7304   2851    166   -332   2691       C  
ATOM    798  CG  PHE A 125      -7.539  31.172 -19.769  1.00 37.87           C  
ANISOU  798  CG  PHE A 125     4294   6903   3190    241   -367   2642       C  
ATOM    799  CD1 PHE A 125      -7.817  32.534 -19.798  1.00 40.82           C  
ANISOU  799  CD1 PHE A 125     4914   6922   3673    333   -457   2891       C  
ATOM    800  CD2 PHE A 125      -7.099  30.616 -18.581  1.00 40.04           C  
ANISOU  800  CD2 PHE A 125     4621   7038   3555    210   -313   2350       C  
ATOM    801  CE1 PHE A 125      -7.711  33.311 -18.643  1.00 41.85           C  
ANISOU  801  CE1 PHE A 125     5347   6555   3998    400   -490   2810       C  
ATOM    802  CE2 PHE A 125      -6.987  31.394 -17.425  1.00 43.07           C  
ANISOU  802  CE2 PHE A 125     5279   6970   4117    265   -345   2284       C  
ATOM    803  CZ  PHE A 125      -7.290  32.737 -17.464  1.00 41.24           C  
ANISOU  803  CZ  PHE A 125     5300   6381   3991    356   -432   2499       C  
ATOM    804  N   SER A 126      -9.239  28.413 -23.265  1.00 37.71           N  
ANISOU  804  N   SER A 126     3338   8494   2496    250   -254   2644       N  
ATOM    805  CA  SER A 126      -9.290  27.849 -24.616  1.00 37.59           C  
ANISOU  805  CA  SER A 126     3063   8988   2232    136   -240   2703       C  
ATOM    806  C   SER A 126     -10.590  28.208 -25.374  1.00 43.23           C  
ANISOU  806  C   SER A 126     3657   9936   2832    308   -287   2913       C  
ATOM    807  O   SER A 126     -10.596  28.239 -26.607  1.00 42.98           O  
ANISOU  807  O   SER A 126     3448  10288   2594    211   -310   3092       O  
ATOM    808  CB  SER A 126      -9.037  26.343 -24.595  1.00 40.53           C  
ANISOU  808  CB  SER A 126     3273   9621   2507     40   -149   2351       C  
ATOM    809  OG  SER A 126     -10.037  25.606 -23.916  1.00 51.01           O  
ANISOU  809  OG  SER A 126     4577  10923   3883    190   -113   2125       O  
ATOM    810  N   VAL A 127     -11.672  28.499 -24.642  1.00 41.14           N  
ANISOU  810  N   VAL A 127     3472   9476   2685    568   -303   2900       N  
ATOM    811  CA  VAL A 127     -12.958  28.864 -25.225  1.00 42.01           C  
ANISOU  811  CA  VAL A 127     3458   9811   2692    777   -347   3099       C  
ATOM    812  C   VAL A 127     -13.038  30.384 -25.391  1.00 48.55           C  
ANISOU  812  C   VAL A 127     4476  10348   3622    924   -442   3480       C  
ATOM    813  O   VAL A 127     -13.400  30.853 -26.470  1.00 50.05           O  
ANISOU  813  O   VAL A 127     4550  10801   3666    950   -499   3783       O  
ATOM    814  CB  VAL A 127     -14.147  28.264 -24.410  1.00 46.61           C  
ANISOU  814  CB  VAL A 127     3976  10427   3306    987   -308   2876       C  
ATOM    815  CG1 VAL A 127     -15.495  28.814 -24.867  1.00 46.40           C  
ANISOU  815  CG1 VAL A 127     3824  10622   3183   1246   -360   3107       C  
ATOM    816  CG2 VAL A 127     -14.150  26.740 -24.487  1.00 46.78           C  
ANISOU  816  CG2 VAL A 127     3811  10763   3201    808   -231   2546       C  
ATOM    817  N   THR A 128     -12.687  31.147 -24.338  1.00 46.13           N  
ANISOU  817  N   THR A 128     4470   9498   3559   1013   -463   3466       N  
ATOM    818  CA  THR A 128     -12.740  32.616 -24.334  1.00 46.53           C  
ANISOU  818  CA  THR A 128     4776   9157   3747   1161   -557   3791       C  
ATOM    819  C   THR A 128     -11.650  33.243 -25.183  1.00 52.69           C  
ANISOU  819  C   THR A 128     5627   9909   4484    884   -618   4078       C  
ATOM    820  O   THR A 128     -11.895  34.257 -25.845  1.00 52.81           O  
ANISOU  820  O   THR A 128     5720   9856   4491    965   -707   4453       O  
ATOM    821  CB  THR A 128     -12.740  33.188 -22.903  1.00 52.29           C  
ANISOU  821  CB  THR A 128     5816   9314   4738   1334   -558   3637       C  
ATOM    822  OG1 THR A 128     -11.550  32.790 -22.219  1.00 48.89           O  
ANISOU  822  OG1 THR A 128     5491   8695   4391   1066   -516   3409       O  
ATOM    823  CG2 THR A 128     -13.992  32.808 -22.104  1.00 48.54           C  
ANISOU  823  CG2 THR A 128     5266   8888   4289   1660   -511   3427       C  
ATOM    824  N   ARG A 129     -10.445  32.644 -25.163  1.00 50.85           N  
ANISOU  824  N   ARG A 129     5357   9750   4213    560   -572   3918       N  
ATOM    825  CA  ARG A 129      -9.291  33.116 -25.931  1.00 51.46           C  
ANISOU  825  CA  ARG A 129     5457   9879   4215    248   -619   4163       C  
ATOM    826  C   ARG A 129      -8.686  32.005 -26.851  1.00 57.39           C  
ANISOU  826  C   ARG A 129     5881  11220   4705     -7   -552   4052       C  
ATOM    827  O   ARG A 129      -7.547  31.605 -26.610  1.00 56.93           O  
ANISOU  827  O   ARG A 129     5821  11168   4641   -243   -510   3899       O  
ATOM    828  CB  ARG A 129      -8.229  33.748 -24.994  1.00 51.68           C  
ANISOU  828  CB  ARG A 129     5793   9396   4448     87   -645   4127       C  
ATOM    829  CG  ARG A 129      -8.651  35.068 -24.340  1.00 63.38           C  
ANISOU  829  CG  ARG A 129     7639  10280   6164    285   -734   4304       C  
ATOM    830  CD  ARG A 129      -7.679  35.493 -23.255  1.00 78.20           C  
ANISOU  830  CD  ARG A 129     9807  11675   8229    114   -748   4172       C  
ATOM    831  NE  ARG A 129      -7.000  36.750 -23.582  1.00 93.81           N  
ANISOU  831  NE  ARG A 129    12050  13317  10277    -82   -862   4523       N  
ATOM    832  CZ  ARG A 129      -5.852  37.152 -23.041  1.00110.62           C  
ANISOU  832  CZ  ARG A 129    14380  15159  12493   -385   -893   4502       C  
ATOM    833  NH1 ARG A 129      -5.232  36.396 -22.140  1.00 96.55           N  
ANISOU  833  NH1 ARG A 129    12548  13405  10734   -502   -815   4149       N  
ATOM    834  NH2 ARG A 129      -5.311  38.308 -23.401  1.00 98.04           N  
ANISOU  834  NH2 ARG A 129    13035  13262  10954   -589  -1008   4848       N  
ATOM    835  N   PRO A 130      -9.403  31.531 -27.926  1.00 56.21           N  
ANISOU  835  N   PRO A 130     5452  11582   4323     40   -543   4128       N  
ATOM    836  CA  PRO A 130      -8.833  30.517 -28.848  1.00 56.77           C  
ANISOU  836  CA  PRO A 130     5229  12211   4131   -190   -481   4003       C  
ATOM    837  C   PRO A 130      -7.570  30.942 -29.621  1.00 61.71           C  
ANISOU  837  C   PRO A 130     5819  12996   4632   -498   -510   4231       C  
ATOM    838  O   PRO A 130      -6.916  30.072 -30.201  1.00 62.50           O  
ANISOU  838  O   PRO A 130     5699  13516   4533   -680   -444   4066       O  
ATOM    839  CB  PRO A 130      -9.992  30.247 -29.842  1.00 58.50           C  
ANISOU  839  CB  PRO A 130     5198  12899   4131    -67   -495   4112       C  
ATOM    840  CG  PRO A 130     -11.210  30.669 -29.134  1.00 62.83           C  
ANISOU  840  CG  PRO A 130     5867  13163   4842    255   -526   4140       C  
ATOM    841  CD  PRO A 130     -10.782  31.868 -28.334  1.00 58.24           C  
ANISOU  841  CD  PRO A 130     5635  11963   4530    315   -589   4312       C  
ATOM    842  N   LEU A 131      -7.216  32.248 -29.635  1.00 57.10           N  
ANISOU  842  N   LEU A 131     5451  12088   4156   -562   -609   4603       N  
ATOM    843  CA  LEU A 131      -6.057  32.736 -30.395  1.00 56.42           C  
ANISOU  843  CA  LEU A 131     5324  12180   3934   -888   -649   4873       C  
ATOM    844  C   LEU A 131      -4.814  32.913 -29.537  1.00 60.72           C  
ANISOU  844  C   LEU A 131     6048  12402   4622  -1099   -638   4762       C  
ATOM    845  O   LEU A 131      -3.778  32.320 -29.848  1.00 60.51           O  
ANISOU  845  O   LEU A 131     5840  12714   4436  -1330   -579   4638       O  
ATOM    846  CB  LEU A 131      -6.416  34.030 -31.154  1.00 55.84           C  
ANISOU  846  CB  LEU A 131     5352  12022   3844   -886   -776   5405       C  
ATOM    847  CG  LEU A 131      -5.482  34.488 -32.268  1.00 58.95           C  
ANISOU  847  CG  LEU A 131     5620  12763   4014  -1226   -828   5765       C  
ATOM    848  CD1 LEU A 131      -5.646  33.645 -33.506  1.00 58.85           C  
ANISOU  848  CD1 LEU A 131     5202  13511   3648  -1284   -775   5738       C  
ATOM    849  CD2 LEU A 131      -5.743  35.926 -32.618  1.00 59.31           C  
ANISOU  849  CD2 LEU A 131     5894  12493   4147  -1224   -970   6293       C  
ATOM    850  N   SER A 132      -4.930  33.715 -28.458  1.00 57.23           N  
ANISOU  850  N   SER A 132     5950  11329   4465  -1007   -692   4789       N  
ATOM    851  CA  SER A 132      -3.854  34.020 -27.516  1.00 56.86           C  
ANISOU  851  CA  SER A 132     6112  10919   4572  -1206   -698   4695       C  
ATOM    852  C   SER A 132      -3.483  32.844 -26.646  1.00 62.39           C  
ANISOU  852  C   SER A 132     6721  11678   5305  -1175   -584   4227       C  
ATOM    853  O   SER A 132      -2.289  32.606 -26.432  1.00 63.00           O  
ANISOU  853  O   SER A 132     6751  11850   5335  -1422   -555   4139       O  
ATOM    854  CB  SER A 132      -4.234  35.193 -26.619  1.00 59.24           C  
ANISOU  854  CB  SER A 132     6821  10527   5162  -1085   -788   4821       C  
ATOM    855  OG  SER A 132      -4.304  36.407 -27.342  1.00 68.49           O  
ANISOU  855  OG  SER A 132     8141  11552   6331  -1166   -910   5291       O  
ATOM    856  N   TYR A 133      -4.491  32.139 -26.096  1.00 58.73           N  
ANISOU  856  N   TYR A 133     6236  11156   4922   -876   -525   3944       N  
ATOM    857  CA  TYR A 133      -4.234  31.025 -25.192  1.00 58.18           C  
ANISOU  857  CA  TYR A 133     6111  11090   4906   -829   -425   3519       C  
ATOM    858  C   TYR A 133      -3.688  29.777 -25.884  1.00 64.04           C  
ANISOU  858  C   TYR A 133     6535  12382   5414   -937   -334   3323       C  
ATOM    859  O   TYR A 133      -2.888  29.068 -25.273  1.00 63.55           O  
ANISOU  859  O   TYR A 133     6440  12335   5372  -1006   -269   3063       O  
ATOM    860  CB  TYR A 133      -5.457  30.688 -24.327  1.00 57.99           C  
ANISOU  860  CB  TYR A 133     6173  10826   5036   -507   -397   3296       C  
ATOM    861  CG  TYR A 133      -5.156  29.648 -23.272  1.00 57.28           C  
ANISOU  861  CG  TYR A 133     6067  10675   5023   -477   -309   2899       C  
ATOM    862  CD1 TYR A 133      -4.253  29.909 -22.245  1.00 58.58           C  
ANISOU  862  CD1 TYR A 133     6405  10523   5329   -592   -312   2807       C  
ATOM    863  CD2 TYR A 133      -5.734  28.384 -23.328  1.00 57.29           C  
ANISOU  863  CD2 TYR A 133     5876  10949   4942   -359   -227   2628       C  
ATOM    864  CE1 TYR A 133      -3.950  28.946 -21.288  1.00 58.16           C  
ANISOU  864  CE1 TYR A 133     6323  10440   5333   -560   -236   2473       C  
ATOM    865  CE2 TYR A 133      -5.449  27.419 -22.368  1.00 57.73           C  
ANISOU  865  CE2 TYR A 133     5931  10931   5072   -334   -154   2295       C  
ATOM    866  CZ  TYR A 133      -4.546  27.699 -21.358  1.00 62.07           C  
ANISOU  866  CZ  TYR A 133     6641  11184   5761   -425   -157   2227       C  
ATOM    867  OH  TYR A 133      -4.255  26.739 -20.425  1.00 60.53           O  
ANISOU  867  OH  TYR A 133     6432  10939   5627   -392    -89   1927       O  
ATOM    868  N   ARG A 134      -4.064  29.522 -27.146  1.00 62.37           N  
ANISOU  868  N   ARG A 134     6095  12626   4975   -950   -331   3446       N  
ATOM    869  CA  ARG A 134      -3.579  28.323 -27.837  1.00 63.26           C  
ANISOU  869  CA  ARG A 134     5921  13259   4855  -1033   -242   3223       C  
ATOM    870  C   ARG A 134      -2.106  28.453 -28.341  1.00 69.59           C  
ANISOU  870  C   ARG A 134     6606  14334   5500  -1319   -234   3328       C  
ATOM    871  O   ARG A 134      -1.516  27.464 -28.799  1.00 69.43           O  
ANISOU  871  O   ARG A 134     6361  14724   5294  -1370   -151   3109       O  
ATOM    872  CB  ARG A 134      -4.552  27.875 -28.924  1.00 64.15           C  
ANISOU  872  CB  ARG A 134     5821  13790   4764   -942   -232   3245       C  
ATOM    873  CG  ARG A 134      -5.884  27.412 -28.325  1.00 74.42           C  
ANISOU  873  CG  ARG A 134     7178  14912   6187   -682   -215   3046       C  
ATOM    874  CD  ARG A 134      -6.251  25.984 -28.679  1.00 84.93           C  
ANISOU  874  CD  ARG A 134     8299  16613   7358   -644   -130   2704       C  
ATOM    875  NE  ARG A 134      -7.702  25.780 -28.637  1.00 92.38           N  
ANISOU  875  NE  ARG A 134     9224  17560   8319   -457   -142   2658       N  
ATOM    876  CZ  ARG A 134      -8.308  24.605 -28.793  1.00103.56           C  
ANISOU  876  CZ  ARG A 134    10504  19213   9630   -420    -85   2362       C  
ATOM    877  NH1 ARG A 134      -7.595  23.497 -28.952  1.00 95.55           N  
ANISOU  877  NH1 ARG A 134     9397  18393   8515   -522     -7   2061       N  
ATOM    878  NH2 ARG A 134      -9.633  24.527 -28.760  1.00 80.34           N  
ANISOU  878  NH2 ARG A 134     7530  16308   6688   -277   -107   2360       N  
ATOM    879  N   ALA A 135      -1.497  29.644 -28.175  1.00 67.05           N  
ANISOU  879  N   ALA A 135     6450  13769   5256  -1501   -319   3641       N  
ATOM    880  CA  ALA A 135      -0.080  29.858 -28.448  1.00 66.93           C  
ANISOU  880  CA  ALA A 135     6343  13978   5110  -1801   -321   3755       C  
ATOM    881  C   ALA A 135       0.663  29.258 -27.245  1.00 70.77           C  
ANISOU  881  C   ALA A 135     6891  14269   5731  -1790   -258   3428       C  
ATOM    882  O   ALA A 135       1.701  28.626 -27.423  1.00 72.02           O  
ANISOU  882  O   ALA A 135     6849  14784   5731  -1907   -193   3298       O  
ATOM    883  CB  ALA A 135       0.218  31.345 -28.553  1.00 67.73           C  
ANISOU  883  CB  ALA A 135     6645  13810   5278  -2019   -447   4194       C  
ATOM    884  N   LYS A 136       0.090  29.427 -26.028  1.00 65.19           N  
ANISOU  884  N   LYS A 136     6444  13027   5299  -1624   -274   3294       N  
ATOM    885  CA  LYS A 136       0.593  28.931 -24.734  1.00 63.41           C  
ANISOU  885  CA  LYS A 136     6310  12555   5228  -1583   -225   3000       C  
ATOM    886  C   LYS A 136       0.084  27.509 -24.424  1.00 63.96           C  
ANISOU  886  C   LYS A 136     6264  12735   5304  -1334   -121   2609       C  
ATOM    887  O   LYS A 136       0.538  26.923 -23.443  1.00 64.48           O  
ANISOU  887  O   LYS A 136     6366  12665   5467  -1289    -73   2365       O  
ATOM    888  CB  LYS A 136       0.131  29.845 -23.569  1.00 65.20           C  
ANISOU  888  CB  LYS A 136     6881  12159   5735  -1523   -296   3044       C  
ATOM    889  CG  LYS A 136       0.303  31.348 -23.757  1.00 73.92           C  
ANISOU  889  CG  LYS A 136     8201  12985   6898  -1719   -418   3424       C  
ATOM    890  CD  LYS A 136      -0.334  32.136 -22.601  1.00 82.31           C  
ANISOU  890  CD  LYS A 136     9619  13416   8239  -1579   -477   3399       C  
ATOM    891  CE  LYS A 136       0.619  32.437 -21.464  1.00 91.72           C  
ANISOU  891  CE  LYS A 136    10980  14322   9549  -1756   -495   3290       C  
ATOM    892  NZ  LYS A 136       0.022  33.362 -20.462  1.00 97.01           N  
ANISOU  892  NZ  LYS A 136    12013  14381  10465  -1639   -562   3284       N  
ATOM    893  N   ARG A 137      -0.886  26.973 -25.194  1.00 56.19           N  
ANISOU  893  N   ARG A 137     5157  11972   4220  -1183    -94   2556       N  
ATOM    894  CA  ARG A 137      -1.435  25.650 -24.898  1.00 54.02           C  
ANISOU  894  CA  ARG A 137     4808  11760   3959   -983     -9   2196       C  
ATOM    895  C   ARG A 137      -0.626  24.531 -25.552  1.00 55.63           C  
ANISOU  895  C   ARG A 137     4768  12418   3952  -1026     78   1988       C  
ATOM    896  O   ARG A 137      -1.041  23.917 -26.539  1.00 55.53           O  
ANISOU  896  O   ARG A 137     4585  12759   3756   -988    113   1913       O  
ATOM    897  CB  ARG A 137      -2.927  25.582 -25.230  1.00 52.98           C  
ANISOU  897  CB  ARG A 137     4683  11610   3835   -809    -27   2206       C  
ATOM    898  CG  ARG A 137      -3.687  24.486 -24.504  1.00 55.10           C  
ANISOU  898  CG  ARG A 137     4978  11756   4203   -619     33   1874       C  
ATOM    899  CD  ARG A 137      -5.168  24.777 -24.505  1.00 49.12           C  
ANISOU  899  CD  ARG A 137     4266  10902   3494   -460     -7   1946       C  
ATOM    900  NE  ARG A 137      -5.929  23.613 -24.082  1.00 54.11           N  
ANISOU  900  NE  ARG A 137     4861  11551   4148   -336     50   1645       N  
ATOM    901  CZ  ARG A 137      -6.474  22.734 -24.912  1.00 70.49           C  
ANISOU  901  CZ  ARG A 137     6764  13972   6046   -337     83   1513       C  
ATOM    902  NH1 ARG A 137      -6.342  22.881 -26.223  1.00 59.74           N  
ANISOU  902  NH1 ARG A 137     5233  13005   4460   -438     73   1645       N  
ATOM    903  NH2 ARG A 137      -7.141  21.690 -24.437  1.00 59.75           N  
ANISOU  903  NH2 ARG A 137     5402  12579   4721   -260    125   1246       N  
ATOM    904  N   THR A 138       0.558  24.298 -24.988  1.00 50.18           N  
ANISOU  904  N   THR A 138     4061  11728   3278  -1100    112   1892       N  
ATOM    905  CA  THR A 138       1.509  23.252 -25.366  1.00 48.73           C  
ANISOU  905  CA  THR A 138     3666  11927   2921  -1097    200   1673       C  
ATOM    906  C   THR A 138       1.522  22.209 -24.215  1.00 51.85           C  
ANISOU  906  C   THR A 138     4147  12071   3482   -914    262   1340       C  
ATOM    907  O   THR A 138       1.183  22.591 -23.086  1.00 51.44           O  
ANISOU  907  O   THR A 138     4297  11596   3653   -876    225   1351       O  
ATOM    908  CB  THR A 138       2.914  23.866 -25.543  1.00 50.99           C  
ANISOU  908  CB  THR A 138     3845  12444   3085  -1323    185   1865       C  
ATOM    909  OG1 THR A 138       3.366  24.393 -24.294  1.00 48.32           O  
ANISOU  909  OG1 THR A 138     3684  11731   2944  -1384    147   1904       O  
ATOM    910  CG2 THR A 138       2.951  24.959 -26.594  1.00 46.99           C  
ANISOU  910  CG2 THR A 138     3272  12160   2422  -1539    113   2237       C  
ATOM    911  N   PRO A 139       1.942  20.922 -24.439  1.00 47.27           N  
ANISOU  911  N   PRO A 139     3430  11733   2797   -797    351   1050       N  
ATOM    912  CA  PRO A 139       1.993  19.940 -23.320  1.00 46.34           C  
ANISOU  912  CA  PRO A 139     3410  11355   2843   -627    400    772       C  
ATOM    913  C   PRO A 139       2.992  20.293 -22.204  1.00 48.20           C  
ANISOU  913  C   PRO A 139     3701  11423   3190   -678    387    827       C  
ATOM    914  O   PRO A 139       2.791  19.912 -21.050  1.00 47.15           O  
ANISOU  914  O   PRO A 139     3706  10967   3243   -572    393    698       O  
ATOM    915  CB  PRO A 139       2.378  18.625 -24.024  1.00 47.90           C  
ANISOU  915  CB  PRO A 139     3445  11886   2869   -504    490    494       C  
ATOM    916  CG  PRO A 139       2.005  18.841 -25.466  1.00 52.03           C  
ANISOU  916  CG  PRO A 139     3821  12783   3165   -586    485    576       C  
ATOM    917  CD  PRO A 139       2.342  20.284 -25.708  1.00 47.83           C  
ANISOU  917  CD  PRO A 139     3265  12314   2594   -798    410    954       C  
ATOM    918  N   ARG A 140       4.061  21.031 -22.561  1.00 44.09           N  
ANISOU  918  N   ARG A 140     3059  11155   2537   -864    366   1029       N  
ATOM    919  CA  ARG A 140       5.134  21.516 -21.677  1.00 43.19           C  
ANISOU  919  CA  ARG A 140     2959  10978   2473   -983    343   1120       C  
ATOM    920  C   ARG A 140       4.576  22.462 -20.595  1.00 45.76           C  
ANISOU  920  C   ARG A 140     3546  10807   3034  -1052    262   1240       C  
ATOM    921  O   ARG A 140       4.916  22.301 -19.420  1.00 47.26           O  
ANISOU  921  O   ARG A 140     3821  10781   3354  -1012    264   1145       O  
ATOM    922  CB  ARG A 140       6.226  22.200 -22.523  1.00 42.84           C  
ANISOU  922  CB  ARG A 140     2717  11361   2199  -1222    324   1351       C  
ATOM    923  CG  ARG A 140       7.516  22.531 -21.800  1.00 55.96           C  
ANISOU  923  CG  ARG A 140     4311  13116   3834  -1366    313   1421       C  
ATOM    924  CD  ARG A 140       8.758  22.058 -22.554  1.00 71.53           C  
ANISOU  924  CD  ARG A 140     5961  15693   5526  -1386    379   1396       C  
ATOM    925  NE  ARG A 140       9.057  22.861 -23.745  1.00 89.20           N  
ANISOU  925  NE  ARG A 140     8046  18307   7538  -1636    345   1663       N  
ATOM    926  CZ  ARG A 140       9.972  23.826 -23.794  1.00108.68           C  
ANISOU  926  CZ  ARG A 140    10439  20956   9899  -1956    284   1940       C  
ATOM    927  NH1 ARG A 140      10.687  24.130 -22.716  1.00 97.69           N  
ANISOU  927  NH1 ARG A 140     9108  19411   8599  -2070    251   1969       N  
ATOM    928  NH2 ARG A 140      10.175  24.499 -24.922  1.00 94.90           N  
ANISOU  928  NH2 ARG A 140     8554  19563   7941  -2187    251   2199       N  
ATOM    929  N   ARG A 141       3.704  23.414 -20.981  1.00 39.58           N  
ANISOU  929  N   ARG A 141     2889   9850   2299  -1130    193   1438       N  
ATOM    930  CA  ARG A 141       3.074  24.347 -20.051  1.00 39.08           C  
ANISOU  930  CA  ARG A 141     3087   9311   2450  -1156    119   1536       C  
ATOM    931  C   ARG A 141       2.046  23.619 -19.168  1.00 40.62           C  
ANISOU  931  C   ARG A 141     3407   9208   2820   -912    150   1303       C  
ATOM    932  O   ARG A 141       1.850  24.029 -18.029  1.00 39.58           O  
ANISOU  932  O   ARG A 141     3453   8728   2857   -896    118   1282       O  
ATOM    933  CB  ARG A 141       2.444  25.547 -20.781  1.00 41.84           C  
ANISOU  933  CB  ARG A 141     3536   9568   2794  -1268     36   1826       C  
ATOM    934  CG  ARG A 141       2.231  26.766 -19.873  1.00 61.47           C  
ANISOU  934  CG  ARG A 141     6299  11585   5471  -1356    -53   1970       C  
ATOM    935  CD  ARG A 141       1.355  27.842 -20.491  1.00 76.94           C  
ANISOU  935  CD  ARG A 141     8400  13367   7468  -1371   -133   2231       C  
ATOM    936  NE  ARG A 141       1.111  28.949 -19.563  1.00 89.36           N  
ANISOU  936  NE  ARG A 141    10273  14442   9238  -1406   -213   2320       N  
ATOM    937  CZ  ARG A 141      -0.006  29.112 -18.860  1.00105.48           C  
ANISOU  937  CZ  ARG A 141    12499  16126  11453  -1179   -224   2227       C  
ATOM    938  NH1 ARG A 141      -1.007  28.247 -18.977  1.00 91.47           N  
ANISOU  938  NH1 ARG A 141    10629  14448   9677   -930   -166   2068       N  
ATOM    939  NH2 ARG A 141      -0.132  30.143 -18.035  1.00 94.69           N  
ANISOU  939  NH2 ARG A 141    11410  14316  10250  -1207   -295   2287       N  
ATOM    940  N   ALA A 142       1.411  22.536 -19.683  1.00 35.87           N  
ANISOU  940  N   ALA A 142     2707   8758   2162   -744    211   1123       N  
ATOM    941  CA  ALA A 142       0.454  21.716 -18.925  1.00 34.53           C  
ANISOU  941  CA  ALA A 142     2632   8358   2131   -548    241    908       C  
ATOM    942  C   ALA A 142       1.202  21.004 -17.802  1.00 37.40           C  
ANISOU  942  C   ALA A 142     3010   8626   2575   -491    280    735       C  
ATOM    943  O   ALA A 142       0.740  21.013 -16.661  1.00 37.35           O  
ANISOU  943  O   ALA A 142     3145   8317   2728   -422    267    671       O  
ATOM    944  CB  ALA A 142      -0.211  20.697 -19.833  1.00 35.25           C  
ANISOU  944  CB  ALA A 142     2610   8670   2114   -443    291    758       C  
ATOM    945  N   LEU A 143       2.399  20.464 -18.110  1.00 33.21           N  
ANISOU  945  N   LEU A 143     2319   8382   1919   -518    326    678       N  
ATOM    946  CA  LEU A 143       3.269  19.784 -17.147  1.00 32.10           C  
ANISOU  946  CA  LEU A 143     2154   8220   1823   -450    362    545       C  
ATOM    947  C   LEU A 143       3.806  20.734 -16.068  1.00 35.42           C  
ANISOU  947  C   LEU A 143     2672   8450   2336   -587    306    668       C  
ATOM    948  O   LEU A 143       3.949  20.328 -14.907  1.00 34.61           O  
ANISOU  948  O   LEU A 143     2632   8178   2340   -511    315    564       O  
ATOM    949  CB  LEU A 143       4.398  19.039 -17.867  1.00 31.93           C  
ANISOU  949  CB  LEU A 143     1913   8602   1617   -416    425    469       C  
ATOM    950  CG  LEU A 143       3.964  17.847 -18.733  1.00 36.50           C  
ANISOU  950  CG  LEU A 143     2423   9328   2118   -241    492    257       C  
ATOM    951  CD1 LEU A 143       5.039  17.457 -19.665  1.00 36.43           C  
ANISOU  951  CD1 LEU A 143     2188   9767   1887   -228    546    221       C  
ATOM    952  CD2 LEU A 143       3.550  16.658 -17.894  1.00 40.85           C  
ANISOU  952  CD2 LEU A 143     3077   9632   2810    -41    528     33       C  
ATOM    953  N   LEU A 144       4.043  22.011 -16.434  1.00 32.40           N  
ANISOU  953  N   LEU A 144     2320   8078   1912   -801    242    894       N  
ATOM    954  CA  LEU A 144       4.501  23.045 -15.499  1.00 32.86           C  
ANISOU  954  CA  LEU A 144     2507   7928   2051   -975    175   1010       C  
ATOM    955  C   LEU A 144       3.409  23.367 -14.471  1.00 37.85           C  
ANISOU  955  C   LEU A 144     3374   8125   2883   -876    143    948       C  
ATOM    956  O   LEU A 144       3.701  23.424 -13.275  1.00 37.54           O  
ANISOU  956  O   LEU A 144     3412   7925   2928   -887    132    877       O  
ATOM    957  CB  LEU A 144       4.933  24.312 -16.258  1.00 33.05           C  
ANISOU  957  CB  LEU A 144     2540   8032   1984  -1241    106   1276       C  
ATOM    958  CG  LEU A 144       5.204  25.576 -15.433  1.00 38.23           C  
ANISOU  958  CG  LEU A 144     3396   8395   2736  -1458     17   1409       C  
ATOM    959  CD1 LEU A 144       6.434  25.422 -14.527  1.00 38.06           C  
ANISOU  959  CD1 LEU A 144     3292   8499   2670  -1584     21   1355       C  
ATOM    960  CD2 LEU A 144       5.337  26.778 -16.340  1.00 41.36           C  
ANISOU  960  CD2 LEU A 144     3846   8805   3065  -1702    -59   1690       C  
ATOM    961  N   MET A 145       2.158  23.549 -14.948  1.00 34.80           N  
ANISOU  961  N   MET A 145     3074   7599   2549   -773    132    971       N  
ATOM    962  CA  MET A 145       0.976  23.839 -14.144  1.00 35.38           C  
ANISOU  962  CA  MET A 145     3336   7326   2782   -644    108    917       C  
ATOM    963  C   MET A 145       0.576  22.672 -13.252  1.00 33.40           C  
ANISOU  963  C   MET A 145     3069   7020   2600   -465    164    695       C  
ATOM    964  O   MET A 145       0.089  22.909 -12.155  1.00 33.87           O  
ANISOU  964  O   MET A 145     3262   6832   2776   -408    147    634       O  
ATOM    965  CB  MET A 145      -0.201  24.259 -15.033  1.00 39.84           C  
ANISOU  965  CB  MET A 145     3940   7852   3344   -567     86   1019       C  
ATOM    966  CG  MET A 145      -0.024  25.608 -15.691  1.00 46.47           C  
ANISOU  966  CG  MET A 145     4865   8630   4159   -725     10   1276       C  
ATOM    967  SD  MET A 145       0.210  26.927 -14.473  1.00 54.08           S  
ANISOU  967  SD  MET A 145     6097   9180   5272   -842    -67   1332       S  
ATOM    968  CE  MET A 145       1.196  28.117 -15.489  1.00 51.43           C  
ANISOU  968  CE  MET A 145     5784   8924   4835  -1155   -148   1652       C  
ATOM    969  N   ILE A 146       0.773  21.424 -13.713  1.00 25.52           N  
ANISOU  969  N   ILE A 146     1920   6249   1527   -379    228    574       N  
ATOM    970  CA  ILE A 146       0.475  20.200 -12.961  1.00 23.33           C  
ANISOU  970  CA  ILE A 146     1636   5917   1312   -227    276    382       C  
ATOM    971  C   ILE A 146       1.388  20.091 -11.742  1.00 27.08           C  
ANISOU  971  C   ILE A 146     2123   6334   1832   -253    276    342       C  
ATOM    972  O   ILE A 146       0.895  19.891 -10.634  1.00 27.52           O  
ANISOU  972  O   ILE A 146     2270   6197   1989   -183    272    268       O  
ATOM    973  CB  ILE A 146       0.531  18.939 -13.875  1.00 25.42           C  
ANISOU  973  CB  ILE A 146     1768   6409   1483   -136    338    261       C  
ATOM    974  CG1 ILE A 146      -0.767  18.813 -14.699  1.00 24.84           C  
ANISOU  974  CG1 ILE A 146     1706   6345   1387    -90    336    248       C  
ATOM    975  CG2 ILE A 146       0.821  17.649 -13.067  1.00 25.04           C  
ANISOU  975  CG2 ILE A 146     1711   6315   1487    -10    383     90       C  
ATOM    976  CD1 ILE A 146      -0.661  18.057 -15.932  1.00 25.55           C  
ANISOU  976  CD1 ILE A 146     1670   6700   1339    -71    377    174       C  
ATOM    977  N   GLY A 147       2.694  20.250 -11.960  1.00 23.65           N  
ANISOU  977  N   GLY A 147     1578   6107   1302   -361    278    402       N  
ATOM    978  CA  GLY A 147       3.727  20.172 -10.932  1.00 22.66           C  
ANISOU  978  CA  GLY A 147     1417   6015   1177   -408    274    386       C  
ATOM    979  C   GLY A 147       3.579  21.219  -9.856  1.00 27.01           C  
ANISOU  979  C   GLY A 147     2125   6322   1815   -522    213    433       C  
ATOM    980  O   GLY A 147       3.706  20.891  -8.672  1.00 27.94           O  
ANISOU  980  O   GLY A 147     2270   6358   1986   -477    215    354       O  
ATOM    981  N   LEU A 148       3.272  22.482 -10.254  1.00 22.50           N  
ANISOU  981  N   LEU A 148     1672   5621   1257   -662    156    558       N  
ATOM    982  CA  LEU A 148       3.037  23.602  -9.323  1.00 21.24           C  
ANISOU  982  CA  LEU A 148     1708   5177   1186   -763     92    583       C  
ATOM    983  C   LEU A 148       1.789  23.355  -8.499  1.00 25.20           C  
ANISOU  983  C   LEU A 148     2329   5439   1806   -573    104    459       C  
ATOM    984  O   LEU A 148       1.778  23.668  -7.321  1.00 24.89           O  
ANISOU  984  O   LEU A 148     2387   5249   1820   -590     83    390       O  
ATOM    985  CB  LEU A 148       2.936  24.962 -10.043  1.00 20.84           C  
ANISOU  985  CB  LEU A 148     1784   5001   1133   -928     24    756       C  
ATOM    986  CG  LEU A 148       4.222  25.517 -10.669  1.00 24.70           C  
ANISOU  986  CG  LEU A 148     2180   5711   1494  -1196     -9    917       C  
ATOM    987  CD1 LEU A 148       3.917  26.608 -11.656  1.00 24.05           C  
ANISOU  987  CD1 LEU A 148     2210   5519   1408  -1323    -70   1115       C  
ATOM    988  CD2 LEU A 148       5.193  26.022  -9.612  1.00 27.76           C  
ANISOU  988  CD2 LEU A 148     2599   6087   1862  -1402    -50    905       C  
ATOM    989  N   ALA A 149       0.750  22.762  -9.099  1.00 22.74           N  
ANISOU  989  N   ALA A 149     1993   5132   1516   -405    139    425       N  
ATOM    990  CA  ALA A 149      -0.484  22.433  -8.390  1.00 23.16           C  
ANISOU  990  CA  ALA A 149     2122   5025   1655   -235    154    319       C  
ATOM    991  C   ALA A 149      -0.260  21.391  -7.279  1.00 27.15           C  
ANISOU  991  C   ALA A 149     2570   5568   2177   -169    191    193       C  
ATOM    992  O   ALA A 149      -0.834  21.518  -6.204  1.00 28.66           O  
ANISOU  992  O   ALA A 149     2843   5622   2425   -113    183    124       O  
ATOM    993  CB  ALA A 149      -1.529  21.944  -9.376  1.00 24.01           C  
ANISOU  993  CB  ALA A 149     2179   5196   1747   -114    180    323       C  
ATOM    994  N   TRP A 150       0.576  20.379  -7.540  1.00 23.11           N  
ANISOU  994  N   TRP A 150     1919   5253   1610   -163    229    169       N  
ATOM    995  CA  TRP A 150       0.931  19.318  -6.593  1.00 23.03           C  
ANISOU  995  CA  TRP A 150     1850   5287   1612    -88    259     85       C  
ATOM    996  C   TRP A 150       1.874  19.845  -5.514  1.00 24.85           C  
ANISOU  996  C   TRP A 150     2087   5529   1826   -198    228    100       C  
ATOM    997  O   TRP A 150       1.800  19.418  -4.370  1.00 24.15           O  
ANISOU  997  O   TRP A 150     2005   5407   1765   -148    232     44       O  
ATOM    998  CB  TRP A 150       1.628  18.175  -7.337  1.00 22.37           C  
ANISOU  998  CB  TRP A 150     1628   5402   1469    -22    306     60       C  
ATOM    999  CG  TRP A 150       0.693  17.159  -7.912  1.00 23.36           C  
ANISOU  999  CG  TRP A 150     1757   5500   1619    104    342    -18       C  
ATOM   1000  CD1 TRP A 150       0.211  17.120  -9.182  1.00 25.95           C  
ANISOU 1000  CD1 TRP A 150     2062   5895   1903    109    355    -19       C  
ATOM   1001  CD2 TRP A 150       0.139  16.022  -7.233  1.00 23.58           C  
ANISOU 1001  CD2 TRP A 150     1815   5437   1709    213    363   -102       C  
ATOM   1002  NE1 TRP A 150      -0.602  16.025  -9.345  1.00 25.39           N  
ANISOU 1002  NE1 TRP A 150     2008   5781   1859    204    383   -118       N  
ATOM   1003  CE2 TRP A 150      -0.654  15.323  -8.169  1.00 27.23           C  
ANISOU 1003  CE2 TRP A 150     2281   5901   2162    263    387   -164       C  
ATOM   1004  CE3 TRP A 150       0.244  15.516  -5.922  1.00 25.17           C  
ANISOU 1004  CE3 TRP A 150     2037   5566   1960    255    360   -119       C  
ATOM   1005  CZ2 TRP A 150      -1.345  14.146  -7.838  1.00 26.74           C  
ANISOU 1005  CZ2 TRP A 150     2265   5746   2151    332    403   -244       C  
ATOM   1006  CZ3 TRP A 150      -0.425  14.343  -5.597  1.00 26.88           C  
ANISOU 1006  CZ3 TRP A 150     2291   5696   2227    338    378   -176       C  
ATOM   1007  CH2 TRP A 150      -1.209  13.671  -6.548  1.00 27.59           C  
ANISOU 1007  CH2 TRP A 150     2403   5762   2317    367    397   -239       C  
ATOM   1008  N   LEU A 151       2.764  20.759  -5.892  1.00 21.17           N  
ANISOU 1008  N   LEU A 151     1610   5132   1300   -369    193    186       N  
ATOM   1009  CA  LEU A 151       3.746  21.379  -5.019  1.00 21.23           C  
ANISOU 1009  CA  LEU A 151     1618   5185   1265   -532    153    208       C  
ATOM   1010  C   LEU A 151       3.090  22.363  -4.073  1.00 25.72           C  
ANISOU 1010  C   LEU A 151     2375   5499   1900   -584    108    158       C  
ATOM   1011  O   LEU A 151       3.450  22.360  -2.902  1.00 27.06           O  
ANISOU 1011  O   LEU A 151     2546   5683   2053   -626     94    101       O  
ATOM   1012  CB  LEU A 151       4.856  22.037  -5.858  1.00 21.60           C  
ANISOU 1012  CB  LEU A 151     1589   5407   1209   -735    125    329       C  
ATOM   1013  CG  LEU A 151       6.118  22.504  -5.163  1.00 26.69           C  
ANISOU 1013  CG  LEU A 151     2168   6209   1763   -942     86    368       C  
ATOM   1014  CD1 LEU A 151       6.864  21.349  -4.491  1.00 26.65           C  
ANISOU 1014  CD1 LEU A 151     1972   6456   1698   -824    128    328       C  
ATOM   1015  CD2 LEU A 151       7.017  23.179  -6.161  1.00 29.68           C  
ANISOU 1015  CD2 LEU A 151     2477   6767   2034  -1169     55    510       C  
ATOM   1016  N   VAL A 152       2.113  23.168  -4.548  1.00 21.47           N  
ANISOU 1016  N   VAL A 152     1988   4743   1426   -559     86    174       N  
ATOM   1017  CA  VAL A 152       1.335  24.124  -3.733  1.00 21.00           C  
ANISOU 1017  CA  VAL A 152     2126   4418   1434   -546     49    105       C  
ATOM   1018  C   VAL A 152       0.481  23.358  -2.706  1.00 24.01           C  
ANISOU 1018  C   VAL A 152     2488   4787   1848   -363     88    -19       C  
ATOM   1019  O   VAL A 152       0.422  23.763  -1.536  1.00 23.98           O  
ANISOU 1019  O   VAL A 152     2561   4707   1844   -384     69   -112       O  
ATOM   1020  CB  VAL A 152       0.510  25.114  -4.609  1.00 25.32           C  
ANISOU 1020  CB  VAL A 152     2827   4756   2039   -517     18    177       C  
ATOM   1021  CG1 VAL A 152      -0.580  25.834  -3.817  1.00 24.65           C  
ANISOU 1021  CG1 VAL A 152     2927   4411   2029   -388      1     78       C  
ATOM   1022  CG2 VAL A 152       1.433  26.124  -5.301  1.00 25.49           C  
ANISOU 1022  CG2 VAL A 152     2913   4746   2026   -760    -41    314       C  
ATOM   1023  N   SER A 153      -0.115  22.214  -3.126  1.00 19.18           N  
ANISOU 1023  N   SER A 153     1767   4272   1247   -208    140    -23       N  
ATOM   1024  CA  SER A 153      -0.917  21.346  -2.244  1.00 18.71           C  
ANISOU 1024  CA  SER A 153     1672   4229   1206    -67    174   -107       C  
ATOM   1025  C   SER A 153      -0.064  20.827  -1.075  1.00 23.39           C  
ANISOU 1025  C   SER A 153     2193   4939   1757   -119    175   -140       C  
ATOM   1026  O   SER A 153      -0.520  20.791   0.072  1.00 21.97           O  
ANISOU 1026  O   SER A 153     2037   4740   1572    -78    175   -212       O  
ATOM   1027  CB  SER A 153      -1.499  20.174  -3.028  1.00 21.08           C  
ANISOU 1027  CB  SER A 153     1879   4613   1518     45    218    -91       C  
ATOM   1028  OG  SER A 153      -2.495  20.615  -3.935  1.00 29.35           O  
ANISOU 1028  OG  SER A 153     2975   5590   2587    106    216    -67       O  
ATOM   1029  N   PHE A 154       1.188  20.462  -1.380  1.00 21.81           N  
ANISOU 1029  N   PHE A 154     1886   4894   1507   -205    175    -79       N  
ATOM   1030  CA  PHE A 154       2.183  19.954  -0.443  1.00 22.31           C  
ANISOU 1030  CA  PHE A 154     1845   5122   1510   -249    172    -75       C  
ATOM   1031  C   PHE A 154       2.665  21.037   0.541  1.00 27.51           C  
ANISOU 1031  C   PHE A 154     2572   5763   2119   -413    122   -117       C  
ATOM   1032  O   PHE A 154       2.625  20.827   1.754  1.00 25.45           O  
ANISOU 1032  O   PHE A 154     2292   5554   1825   -402    118   -170       O  
ATOM   1033  CB  PHE A 154       3.370  19.340  -1.221  1.00 24.06           C  
ANISOU 1033  CB  PHE A 154     1916   5550   1676   -265    189      5       C  
ATOM   1034  CG  PHE A 154       4.356  18.619  -0.340  1.00 25.34           C  
ANISOU 1034  CG  PHE A 154     1941   5914   1772   -252    191     31       C  
ATOM   1035  CD1 PHE A 154       5.503  19.254   0.103  1.00 27.41           C  
ANISOU 1035  CD1 PHE A 154     2133   6345   1935   -425    152     66       C  
ATOM   1036  CD2 PHE A 154       4.111  17.318   0.086  1.00 27.73           C  
ANISOU 1036  CD2 PHE A 154     2188   6241   2107    -77    224     32       C  
ATOM   1037  CE1 PHE A 154       6.385  18.604   0.959  1.00 28.07           C  
ANISOU 1037  CE1 PHE A 154     2069   6655   1941   -401    151    105       C  
ATOM   1038  CE2 PHE A 154       5.000  16.667   0.941  1.00 29.94           C  
ANISOU 1038  CE2 PHE A 154     2344   6706   2326    -41    220     82       C  
ATOM   1039  CZ  PHE A 154       6.139  17.307   1.354  1.00 27.41           C  
ANISOU 1039  CZ  PHE A 154     1929   6590   1897   -191    186    120       C  
ATOM   1040  N   VAL A 155       3.124  22.182   0.003  1.00 26.65           N  
ANISOU 1040  N   VAL A 155     2546   5585   1994   -582     80    -90       N  
ATOM   1041  CA  VAL A 155       3.648  23.334   0.740  1.00 27.89           C  
ANISOU 1041  CA  VAL A 155     2808   5686   2104   -788     21   -136       C  
ATOM   1042  C   VAL A 155       2.598  23.929   1.665  1.00 35.01           C  
ANISOU 1042  C   VAL A 155     3879   6375   3049   -717     10   -276       C  
ATOM   1043  O   VAL A 155       2.944  24.437   2.728  1.00 36.79           O  
ANISOU 1043  O   VAL A 155     4154   6610   3215   -834    -23   -366       O  
ATOM   1044  CB  VAL A 155       4.242  24.375  -0.254  1.00 32.29           C  
ANISOU 1044  CB  VAL A 155     3441   6177   2651   -992    -25    -47       C  
ATOM   1045  CG1 VAL A 155       4.493  25.737   0.394  1.00 32.57           C  
ANISOU 1045  CG1 VAL A 155     3677   6023   2673  -1212    -98   -112       C  
ATOM   1046  CG2 VAL A 155       5.518  23.847  -0.890  1.00 31.97           C  
ANISOU 1046  CG2 VAL A 155     3189   6447   2510  -1100    -18     74       C  
ATOM   1047  N   LEU A 156       1.327  23.857   1.276  1.00 32.51           N  
ANISOU 1047  N   LEU A 156     3632   5903   2815   -523     40   -302       N  
ATOM   1048  CA  LEU A 156       0.244  24.401   2.080  1.00 32.35           C  
ANISOU 1048  CA  LEU A 156     3749   5721   2821   -414     39   -437       C  
ATOM   1049  C   LEU A 156      -0.238  23.511   3.203  1.00 34.95           C  
ANISOU 1049  C   LEU A 156     3971   6201   3107   -292     77   -506       C  
ATOM   1050  O   LEU A 156      -0.535  24.039   4.268  1.00 34.40           O  
ANISOU 1050  O   LEU A 156     3977   6098   2996   -285     66   -637       O  
ATOM   1051  CB  LEU A 156      -0.943  24.811   1.205  1.00 32.62           C  
ANISOU 1051  CB  LEU A 156     3896   5557   2943   -255     48   -423       C  
ATOM   1052  CG  LEU A 156      -1.096  26.309   0.996  1.00 37.60           C  
ANISOU 1052  CG  LEU A 156     4765   5905   3618   -319     -7   -454       C  
ATOM   1053  CD1 LEU A 156      -0.033  26.847   0.028  1.00 37.84           C  
ANISOU 1053  CD1 LEU A 156     4823   5909   3646   -551    -54   -315       C  
ATOM   1054  CD2 LEU A 156      -2.492  26.639   0.511  1.00 40.37           C  
ANISOU 1054  CD2 LEU A 156     5212   6088   4040    -86      7   -460       C  
ATOM   1055  N   TRP A 157      -0.347  22.188   2.984  1.00 31.93           N  
ANISOU 1055  N   TRP A 157     3427   5978   2729   -201    119   -423       N  
ATOM   1056  CA  TRP A 157      -0.928  21.288   3.983  1.00 32.73           C  
ANISOU 1056  CA  TRP A 157     3435   6209   2793    -98    150   -453       C  
ATOM   1057  C   TRP A 157       0.054  20.434   4.778  1.00 37.00           C  
ANISOU 1057  C   TRP A 157     3830   6966   3260   -165    147   -397       C  
ATOM   1058  O   TRP A 157      -0.113  20.342   5.993  1.00 36.83           O  
ANISOU 1058  O   TRP A 157     3777   7051   3166   -167    144   -452       O  
ATOM   1059  CB  TRP A 157      -2.008  20.413   3.345  1.00 32.31           C  
ANISOU 1059  CB  TRP A 157     3334   6145   2796     55    191   -403       C  
ATOM   1060  CG  TRP A 157      -3.083  21.253   2.701  1.00 33.90           C  
ANISOU 1060  CG  TRP A 157     3648   6187   3045    148    193   -449       C  
ATOM   1061  CD1 TRP A 157      -3.312  21.396   1.365  1.00 36.73           C  
ANISOU 1061  CD1 TRP A 157     4036   6458   3463    176    195   -384       C  
ATOM   1062  CD2 TRP A 157      -3.939  22.215   3.359  1.00 34.05           C  
ANISOU 1062  CD2 TRP A 157     3769   6124   3045    231    187   -569       C  
ATOM   1063  NE1 TRP A 157      -4.304  22.327   1.149  1.00 36.29           N  
ANISOU 1063  NE1 TRP A 157     4086   6271   3430    281    188   -431       N  
ATOM   1064  CE2 TRP A 157      -4.711  22.841   2.354  1.00 37.91           C  
ANISOU 1064  CE2 TRP A 157     4342   6469   3594    333    186   -552       C  
ATOM   1065  CE3 TRP A 157      -4.164  22.572   4.707  1.00 35.54           C  
ANISOU 1065  CE3 TRP A 157     3976   6370   3157    250    186   -694       C  
ATOM   1066  CZ2 TRP A 157      -5.677  23.817   2.647  1.00 37.19           C  
ANISOU 1066  CZ2 TRP A 157     4359   6270   3501    480    184   -652       C  
ATOM   1067  CZ3 TRP A 157      -5.128  23.530   4.996  1.00 37.01           C  
ANISOU 1067  CZ3 TRP A 157     4271   6456   3335    389    189   -819       C  
ATOM   1068  CH2 TRP A 157      -5.876  24.137   3.974  1.00 37.60           C  
ANISOU 1068  CH2 TRP A 157     4434   6370   3482    516    188   -795       C  
ATOM   1069  N   ALA A 158       1.069  19.827   4.128  1.00 33.22           N  
ANISOU 1069  N   ALA A 158     3255   6582   2787   -204    148   -288       N  
ATOM   1070  CA  ALA A 158       2.061  18.989   4.810  1.00 31.94           C  
ANISOU 1070  CA  ALA A 158     2943   6641   2554   -228    144   -211       C  
ATOM   1071  C   ALA A 158       2.816  19.696   5.962  1.00 34.36           C  
ANISOU 1071  C   ALA A 158     3227   7087   2742   -386    102   -264       C  
ATOM   1072  O   ALA A 158       2.870  19.079   7.024  1.00 33.74           O  
ANISOU 1072  O   ALA A 158     3054   7171   2595   -357    102   -241       O  
ATOM   1073  CB  ALA A 158       3.031  18.379   3.814  1.00 32.63           C  
ANISOU 1073  CB  ALA A 158     2931   6812   2654   -213    155   -105       C  
ATOM   1074  N   PRO A 159       3.356  20.955   5.862  1.00 30.41           N  
ANISOU 1074  N   PRO A 159     2817   6534   2203   -569     59   -332       N  
ATOM   1075  CA  PRO A 159       4.063  21.530   7.019  1.00 29.60           C  
ANISOU 1075  CA  PRO A 159     2692   6585   1970   -745     15   -399       C  
ATOM   1076  C   PRO A 159       3.194  21.698   8.258  1.00 33.06           C  
ANISOU 1076  C   PRO A 159     3182   7020   2359   -695     19   -531       C  
ATOM   1077  O   PRO A 159       3.658  21.417   9.357  1.00 33.15           O  
ANISOU 1077  O   PRO A 159     3080   7269   2247   -754      3   -533       O  
ATOM   1078  CB  PRO A 159       4.593  22.868   6.486  1.00 31.19           C  
ANISOU 1078  CB  PRO A 159     3033   6650   2166   -962    -34   -453       C  
ATOM   1079  CG  PRO A 159       4.675  22.690   5.026  1.00 35.48           C  
ANISOU 1079  CG  PRO A 159     3574   7103   2802   -914    -15   -342       C  
ATOM   1080  CD  PRO A 159       3.444  21.882   4.715  1.00 31.67           C  
ANISOU 1080  CD  PRO A 159     3100   6508   2423   -655     42   -336       C  
ATOM   1081  N   ALA A 160       1.929  22.106   8.085  1.00 28.97           N  
ANISOU 1081  N   ALA A 160     2809   6278   1919   -572     42   -632       N  
ATOM   1082  CA  ALA A 160       1.012  22.302   9.204  1.00 27.74           C  
ANISOU 1082  CA  ALA A 160     2690   6151   1701   -498     54   -770       C  
ATOM   1083  C   ALA A 160       0.580  20.982   9.826  1.00 28.99           C  
ANISOU 1083  C   ALA A 160     2674   6519   1820   -374     90   -668       C  
ATOM   1084  O   ALA A 160       0.425  20.940  11.045  1.00 28.82           O  
ANISOU 1084  O   ALA A 160     2593   6680   1676   -391     87   -731       O  
ATOM   1085  CB  ALA A 160      -0.196  23.102   8.764  1.00 28.60           C  
ANISOU 1085  CB  ALA A 160     2980   5993   1895   -370     71   -890       C  
ATOM   1086  N   ILE A 161       0.396  19.905   9.009  1.00 22.55           N  
ANISOU 1086  N   ILE A 161     1787   5682   1101   -264    120   -511       N  
ATOM   1087  CA  ILE A 161       0.017  18.573   9.516  1.00 20.66           C  
ANISOU 1087  CA  ILE A 161     1413   5592    843   -168    144   -386       C  
ATOM   1088  C   ILE A 161       1.111  17.972  10.448  1.00 24.61           C  
ANISOU 1088  C   ILE A 161     1760   6358   1232   -241    118   -282       C  
ATOM   1089  O   ILE A 161       0.792  17.489  11.539  1.00 25.99           O  
ANISOU 1089  O   ILE A 161     1849   6715   1312   -228    118   -249       O  
ATOM   1090  CB  ILE A 161      -0.397  17.597   8.379  1.00 22.02           C  
ANISOU 1090  CB  ILE A 161     1582   5637   1147    -54    174   -266       C  
ATOM   1091  CG1 ILE A 161      -1.711  18.035   7.727  1.00 21.27           C  
ANISOU 1091  CG1 ILE A 161     1592   5369   1121     29    200   -349       C  
ATOM   1092  CG2 ILE A 161      -0.502  16.146   8.885  1.00 21.96           C  
ANISOU 1092  CG2 ILE A 161     1463   5750   1132      8    183   -109       C  
ATOM   1093  CD1 ILE A 161      -2.024  17.364   6.430  1.00 20.10           C  
ANISOU 1093  CD1 ILE A 161     1460   5091   1087     99    221   -270       C  
ATOM   1094  N   LEU A 162       2.375  18.032  10.029  1.00 19.41           N  
ANISOU 1094  N   LEU A 162     1052   5755    566   -319     94   -220       N  
ATOM   1095  CA  LEU A 162       3.495  17.462  10.764  1.00 19.09           C  
ANISOU 1095  CA  LEU A 162      843   5995    416   -366     67    -99       C  
ATOM   1096  C   LEU A 162       4.031  18.312  11.919  1.00 25.70           C  
ANISOU 1096  C   LEU A 162     1639   7048   1077   -544     25   -201       C  
ATOM   1097  O   LEU A 162       4.488  17.747  12.922  1.00 25.08           O  
ANISOU 1097  O   LEU A 162     1407   7247    874   -558      7   -106       O  
ATOM   1098  CB  LEU A 162       4.673  17.174   9.809  1.00 18.81           C  
ANISOU 1098  CB  LEU A 162      736   5996    417   -364     61     10       C  
ATOM   1099  CG  LEU A 162       4.460  16.565   8.438  1.00 21.58           C  
ANISOU 1099  CG  LEU A 162     1134   6147    920   -222     99     70       C  
ATOM   1100  CD1 LEU A 162       5.745  16.599   7.676  1.00 21.10           C  
ANISOU 1100  CD1 LEU A 162      977   6205    836   -250     91    140       C  
ATOM   1101  CD2 LEU A 162       3.968  15.146   8.531  1.00 23.17           C  
ANISOU 1101  CD2 LEU A 162     1304   6308   1191    -41    125    192       C  
ATOM   1102  N   PHE A 163       4.054  19.652  11.760  1.00 25.30           N  
ANISOU 1102  N   PHE A 163     1730   6872   1011   -690      4   -385       N  
ATOM   1103  CA  PHE A 163       4.689  20.535  12.741  1.00 27.09           C  
ANISOU 1103  CA  PHE A 163     1946   7280   1068   -900    -45   -510       C  
ATOM   1104  C   PHE A 163       3.767  21.348  13.649  1.00 37.56           C  
ANISOU 1104  C   PHE A 163     3395   8556   2321   -922    -44   -736       C  
ATOM   1105  O   PHE A 163       4.287  22.133  14.462  1.00 38.32           O  
ANISOU 1105  O   PHE A 163     3501   8794   2265  -1110    -86   -874       O  
ATOM   1106  CB  PHE A 163       5.682  21.478  12.050  1.00 28.64           C  
ANISOU 1106  CB  PHE A 163     2209   7414   1260  -1109    -87   -552       C  
ATOM   1107  CG  PHE A 163       6.927  20.754  11.600  1.00 29.80           C  
ANISOU 1107  CG  PHE A 163     2155   7794   1375  -1133    -99   -346       C  
ATOM   1108  CD1 PHE A 163       8.006  20.594  12.461  1.00 31.49           C  
ANISOU 1108  CD1 PHE A 163     2171   8390   1402  -1265   -139   -278       C  
ATOM   1109  CD2 PHE A 163       7.017  20.218  10.318  1.00 30.94           C  
ANISOU 1109  CD2 PHE A 163     2289   7810   1656  -1004    -66   -224       C  
ATOM   1110  CE1 PHE A 163       9.146  19.897  12.055  1.00 31.75           C  
ANISOU 1110  CE1 PHE A 163     1994   8677   1393  -1242   -146    -82       C  
ATOM   1111  CE2 PHE A 163       8.157  19.515   9.917  1.00 33.38           C  
ANISOU 1111  CE2 PHE A 163     2399   8361   1921   -982    -69    -49       C  
ATOM   1112  CZ  PHE A 163       9.208  19.353  10.793  1.00 30.86           C  
ANISOU 1112  CZ  PHE A 163     1879   8423   1421  -1086   -107     25       C  
ATOM   1113  N   TRP A 164       2.439  21.133  13.585  1.00 37.68           N  
ANISOU 1113  N   TRP A 164     3482   8418   2416   -735      4   -781       N  
ATOM   1114  CA  TRP A 164       1.524  21.853  14.462  1.00 39.92           C  
ANISOU 1114  CA  TRP A 164     3856   8701   2611   -711     14  -1002       C  
ATOM   1115  C   TRP A 164       1.810  21.593  15.966  1.00 40.44           C  
ANISOU 1115  C   TRP A 164     3759   9153   2453   -793     -3  -1023       C  
ATOM   1116  O   TRP A 164       1.837  22.531  16.767  1.00 38.39           O  
ANISOU 1116  O   TRP A 164     3572   8956   2058   -902    -24  -1250       O  
ATOM   1117  CB  TRP A 164       0.082  21.530  14.117  1.00 41.08           C  
ANISOU 1117  CB  TRP A 164     4050   8704   2856   -488     70  -1009       C  
ATOM   1118  CG  TRP A 164      -0.890  22.379  14.871  1.00 44.12           C  
ANISOU 1118  CG  TRP A 164     4530   9084   3152   -420     88  -1254       C  
ATOM   1119  CD1 TRP A 164      -1.717  21.979  15.878  1.00 47.28           C  
ANISOU 1119  CD1 TRP A 164     4812   9734   3418   -331    120  -1286       C  
ATOM   1120  CD2 TRP A 164      -1.070  23.795  14.738  1.00 45.07           C  
ANISOU 1120  CD2 TRP A 164     4882   8950   3292   -433     73  -1506       C  
ATOM   1121  NE1 TRP A 164      -2.450  23.045  16.339  1.00 47.47           N  
ANISOU 1121  NE1 TRP A 164     4966   9698   3373   -256    135  -1560       N  
ATOM   1122  CE2 TRP A 164      -2.074  24.175  15.657  1.00 49.69           C  
ANISOU 1122  CE2 TRP A 164     5480   9641   3757   -305    105  -1705       C  
ATOM   1123  CE3 TRP A 164      -0.500  24.780  13.906  1.00 47.03           C  
ANISOU 1123  CE3 TRP A 164     5339   8884   3648   -536     33  -1575       C  
ATOM   1124  CZ2 TRP A 164      -2.522  25.498  15.771  1.00 49.73           C  
ANISOU 1124  CZ2 TRP A 164     5716   9421   3759   -242    101  -1989       C  
ATOM   1125  CZ3 TRP A 164      -0.934  26.091  14.028  1.00 49.23           C  
ANISOU 1125  CZ3 TRP A 164     5860   8913   3932   -506     20  -1833       C  
ATOM   1126  CH2 TRP A 164      -1.942  26.438  14.940  1.00 50.14           C  
ANISOU 1126  CH2 TRP A 164     6000   9110   3941   -340     56  -2046       C  
ATOM   1127  N   GLN A 165       2.080  20.322  16.307  1.00 35.71           N  
ANISOU 1127  N   GLN A 165     2949   8803   1815   -746      2   -782       N  
ATOM   1128  CA  GLN A 165       2.404  19.836  17.640  1.00 34.74           C  
ANISOU 1128  CA  GLN A 165     2633   9083   1484   -809    -17   -717       C  
ATOM   1129  C   GLN A 165       3.621  20.560  18.230  1.00 40.26           C  
ANISOU 1129  C   GLN A 165     3288   9995   2014  -1044    -76   -810       C  
ATOM   1130  O   GLN A 165       3.663  20.798  19.436  1.00 40.65           O  
ANISOU 1130  O   GLN A 165     3253  10342   1851  -1139    -94   -910       O  
ATOM   1131  CB  GLN A 165       2.588  18.298  17.623  1.00 35.54           C  
ANISOU 1131  CB  GLN A 165     2552   9327   1623   -699    -10   -391       C  
ATOM   1132  CG  GLN A 165       3.720  17.785  16.729  1.00 39.68           C  
ANISOU 1132  CG  GLN A 165     3027   9798   2253   -695    -30   -204       C  
ATOM   1133  CD  GLN A 165       3.861  16.284  16.678  1.00 53.87           C  
ANISOU 1133  CD  GLN A 165     4690  11672   4106   -548    -24     95       C  
ATOM   1134  OE1 GLN A 165       4.086  15.609  17.693  1.00 48.17           O  
ANISOU 1134  OE1 GLN A 165     3806  11248   3248   -547    -45    249       O  
ATOM   1135  NE2 GLN A 165       3.784  15.733  15.471  1.00 46.90           N  
ANISOU 1135  NE2 GLN A 165     3881  10517   3421   -420      1    186       N  
ATOM   1136  N   TYR A 166       4.595  20.933  17.375  1.00 37.03           N  
ANISOU 1136  N   TYR A 166     2926   9463   1680  -1158   -107   -783       N  
ATOM   1137  CA  TYR A 166       5.818  21.638  17.792  1.00 35.75           C  
ANISOU 1137  CA  TYR A 166     2717   9511   1356  -1426   -171   -855       C  
ATOM   1138  C   TYR A 166       5.584  23.140  17.997  1.00 40.15           C  
ANISOU 1138  C   TYR A 166     3513   9878   1866  -1599   -196  -1189       C  
ATOM   1139  O   TYR A 166       6.215  23.738  18.865  1.00 38.62           O  
ANISOU 1139  O   TYR A 166     3288   9917   1470  -1828   -247  -1326       O  
ATOM   1140  CB  TYR A 166       6.973  21.343  16.811  1.00 34.82           C  
ANISOU 1140  CB  TYR A 166     2518   9401   1311  -1485   -195   -662       C  
ATOM   1141  CG  TYR A 166       7.235  19.860  16.679  1.00 33.39           C  
ANISOU 1141  CG  TYR A 166     2122   9391   1171  -1282   -171   -356       C  
ATOM   1142  CD1 TYR A 166       7.748  19.126  17.744  1.00 34.91           C  
ANISOU 1142  CD1 TYR A 166     2079   9999   1187  -1279   -194   -201       C  
ATOM   1143  CD2 TYR A 166       6.907  19.175  15.514  1.00 32.98           C  
ANISOU 1143  CD2 TYR A 166     2120   9075   1334  -1081   -128   -226       C  
ATOM   1144  CE1 TYR A 166       7.944  17.753  17.652  1.00 34.39           C  
ANISOU 1144  CE1 TYR A 166     1851  10039   1175  -1067   -178     88       C  
ATOM   1145  CE2 TYR A 166       7.114  17.801  15.402  1.00 33.61           C  
ANISOU 1145  CE2 TYR A 166     2046   9260   1465   -882   -109     32       C  
ATOM   1146  CZ  TYR A 166       7.622  17.093  16.483  1.00 42.40           C  
ANISOU 1146  CZ  TYR A 166     2947  10745   2417   -867   -135    193       C  
ATOM   1147  OH  TYR A 166       7.845  15.744  16.433  1.00 45.67           O  
ANISOU 1147  OH  TYR A 166     3234  11232   2886   -657   -124    458       O  
ATOM   1148  N   LEU A 167       4.654  23.731  17.213  1.00 38.46           N  
ANISOU 1148  N   LEU A 167     3542   9238   1832  -1480   -164  -1322       N  
ATOM   1149  CA  LEU A 167       4.288  25.141  17.302  1.00 38.35           C  
ANISOU 1149  CA  LEU A 167     3805   8949   1816  -1578   -185  -1636       C  
ATOM   1150  C   LEU A 167       3.373  25.376  18.491  1.00 44.46           C  
ANISOU 1150  C   LEU A 167     4599   9846   2448  -1483   -157  -1861       C  
ATOM   1151  O   LEU A 167       3.508  26.408  19.149  1.00 45.60           O  
ANISOU 1151  O   LEU A 167     4889   9969   2468  -1638   -192  -2140       O  
ATOM   1152  CB  LEU A 167       3.632  25.625  16.011  1.00 38.20           C  
ANISOU 1152  CB  LEU A 167     4019   8456   2039  -1452   -163  -1654       C  
ATOM   1153  CG  LEU A 167       4.480  25.554  14.726  1.00 42.44           C  
ANISOU 1153  CG  LEU A 167     4547   8868   2709  -1545   -186  -1449       C  
ATOM   1154  CD1 LEU A 167       3.600  25.653  13.494  1.00 42.43           C  
ANISOU 1154  CD1 LEU A 167     4710   8479   2934  -1348   -148  -1414       C  
ATOM   1155  CD2 LEU A 167       5.544  26.642  14.693  1.00 44.27           C  
ANISOU 1155  CD2 LEU A 167     4877   9082   2862  -1893   -266  -1531       C  
ATOM   1156  N   VAL A 168       2.454  24.419  18.781  1.00 40.66           N  
ANISOU 1156  N   VAL A 168     3969   9511   1968  -1242    -97  -1745       N  
ATOM   1157  CA  VAL A 168       1.538  24.452  19.938  1.00 39.86           C  
ANISOU 1157  CA  VAL A 168     3819   9626   1698  -1136    -61  -1914       C  
ATOM   1158  C   VAL A 168       2.355  24.186  21.209  1.00 45.06           C  
ANISOU 1158  C   VAL A 168     4265  10769   2086  -1329   -100  -1901       C  
ATOM   1159  O   VAL A 168       2.174  24.875  22.214  1.00 45.86           O  
ANISOU 1159  O   VAL A 168     4402  11033   1989  -1399   -107  -2169       O  
ATOM   1160  CB  VAL A 168       0.352  23.466  19.756  1.00 42.88           C  
ANISOU 1160  CB  VAL A 168     4095  10035   2162   -865      8  -1751       C  
ATOM   1161  CG1 VAL A 168      -0.344  23.147  21.057  1.00 42.71           C  
ANISOU 1161  CG1 VAL A 168     3915  10396   1917   -800     39  -1821       C  
ATOM   1162  CG2 VAL A 168      -0.653  24.034  18.794  1.00 42.89           C  
ANISOU 1162  CG2 VAL A 168     4313   9624   2359   -675     46  -1861       C  
ATOM   1163  N   GLY A 169       3.265  23.220  21.127  1.00 41.79           N  
ANISOU 1163  N   GLY A 169     3633  10586   1657  -1403   -127  -1596       N  
ATOM   1164  CA  GLY A 169       4.160  22.835  22.211  1.00 41.64           C  
ANISOU 1164  CA  GLY A 169     3375  11059   1388  -1574   -171  -1508       C  
ATOM   1165  C   GLY A 169       3.868  21.463  22.781  1.00 46.04           C  
ANISOU 1165  C   GLY A 169     3669  11947   1876  -1430   -146  -1216       C  
ATOM   1166  O   GLY A 169       4.569  21.023  23.706  1.00 47.14           O  
ANISOU 1166  O   GLY A 169     3584  12527   1800  -1543   -183  -1095       O  
ATOM   1167  N   GLU A 170       2.810  20.788  22.239  1.00 40.10           N  
ANISOU 1167  N   GLU A 170     2948  10990   1298  -1193    -88  -1093       N  
ATOM   1168  CA  GLU A 170       2.339  19.456  22.640  1.00 39.02           C  
ANISOU 1168  CA  GLU A 170     2613  11074   1137  -1058    -65   -801       C  
ATOM   1169  C   GLU A 170       1.592  18.744  21.518  1.00 38.96           C  
ANISOU 1169  C   GLU A 170     2689  10719   1395   -862    -21   -637       C  
ATOM   1170  O   GLU A 170       0.933  19.392  20.704  1.00 38.48           O  
ANISOU 1170  O   GLU A 170     2825  10310   1487   -786     11   -811       O  
ATOM   1171  CB  GLU A 170       1.380  19.559  23.847  1.00 40.72           C  
ANISOU 1171  CB  GLU A 170     2746  11595   1132  -1034    -36   -930       C  
ATOM   1172  CG  GLU A 170       2.065  19.634  25.202  1.00 53.43           C  
ANISOU 1172  CG  GLU A 170     4156  13716   2428  -1207    -80   -942       C  
ATOM   1173  CD  GLU A 170       2.257  18.319  25.929  1.00 75.58           C  
ANISOU 1173  CD  GLU A 170     6691  16906   5121  -1190   -100   -561       C  
ATOM   1174  OE1 GLU A 170       1.685  17.291  25.496  1.00 76.51           O  
ANISOU 1174  OE1 GLU A 170     6786  16889   5398  -1040    -76   -293       O  
ATOM   1175  OE2 GLU A 170       2.967  18.329  26.961  1.00 63.43           O  
ANISOU 1175  OE2 GLU A 170     4968  15808   3326  -1336   -145   -528       O  
ATOM   1176  N   ARG A 171       1.668  17.405  21.508  1.00 32.88           N  
ANISOU 1176  N   ARG A 171     1774  10047    671   -781    -24   -302       N  
ATOM   1177  CA  ARG A 171       0.917  16.539  20.614  1.00 31.29           C  
ANISOU 1177  CA  ARG A 171     1634   9569    687   -621     12   -131       C  
ATOM   1178  C   ARG A 171      -0.316  16.183  21.443  1.00 35.82           C  
ANISOU 1178  C   ARG A 171     2128  10341   1139   -578     43   -113       C  
ATOM   1179  O   ARG A 171      -0.190  15.509  22.481  1.00 35.54           O  
ANISOU 1179  O   ARG A 171     1910  10663    931   -625     21     68       O  
ATOM   1180  CB  ARG A 171       1.728  15.290  20.225  1.00 27.98           C  
ANISOU 1180  CB  ARG A 171     1106   9117    410   -565    -15    206       C  
ATOM   1181  CG  ARG A 171       0.918  14.305  19.393  1.00 29.56           C  
ANISOU 1181  CG  ARG A 171     1399   9052    780   -423     15    376       C  
ATOM   1182  CD  ARG A 171       1.715  13.119  18.888  1.00 30.16           C  
ANISOU 1182  CD  ARG A 171     1436   9040    985   -334     -9    667       C  
ATOM   1183  NE  ARG A 171       0.903  12.265  18.017  1.00 39.52           N  
ANISOU 1183  NE  ARG A 171     2734   9912   2370   -224     18    776       N  
ATOM   1184  CZ  ARG A 171       0.740  12.462  16.707  1.00 55.08           C  
ANISOU 1184  CZ  ARG A 171     4855  11542   4532   -161     46    674       C  
ATOM   1185  NH1 ARG A 171       1.338  13.482  16.102  1.00 39.87           N  
ANISOU 1185  NH1 ARG A 171     2988   9531   2630   -194     50    482       N  
ATOM   1186  NH2 ARG A 171      -0.034  11.650  15.997  1.00 40.64           N  
ANISOU 1186  NH2 ARG A 171     3118   9467   2857    -87     65    766       N  
ATOM   1187  N   THR A 172      -1.486  16.733  21.050  1.00 32.00           N  
ANISOU 1187  N   THR A 172     1767   9678    716   -495     92   -308       N  
ATOM   1188  CA  THR A 172      -2.754  16.554  21.776  1.00 31.24           C  
ANISOU 1188  CA  THR A 172     1582   9804    482   -449    129   -329       C  
ATOM   1189  C   THR A 172      -3.523  15.318  21.305  1.00 35.51           C  
ANISOU 1189  C   THR A 172     2090  10255   1149   -386    144    -49       C  
ATOM   1190  O   THR A 172      -4.486  14.923  21.945  1.00 33.39           O  
ANISOU 1190  O   THR A 172     1708  10226    752   -386    165     16       O  
ATOM   1191  CB  THR A 172      -3.584  17.832  21.744  1.00 35.05           C  
ANISOU 1191  CB  THR A 172     2186  10210    920   -375    173   -694       C  
ATOM   1192  OG1 THR A 172      -4.074  18.073  20.429  1.00 29.52           O  
ANISOU 1192  OG1 THR A 172     1641   9081    493   -260    191   -740       O  
ATOM   1193  CG2 THR A 172      -2.815  19.042  22.287  1.00 33.67           C  
ANISOU 1193  CG2 THR A 172     2080  10097    616   -468    149   -984       C  
ATOM   1194  N   VAL A 173      -3.066  14.696  20.203  1.00 34.97           N  
ANISOU 1194  N   VAL A 173     2115   9857   1315   -350    129    113       N  
ATOM   1195  CA  VAL A 173      -3.616  13.458  19.645  1.00 35.47           C  
ANISOU 1195  CA  VAL A 173     2186   9771   1521   -313    130    374       C  
ATOM   1196  C   VAL A 173      -3.037  12.322  20.516  1.00 43.51           C  
ANISOU 1196  C   VAL A 173     3059  11021   2450   -376     84    694       C  
ATOM   1197  O   VAL A 173      -1.804  12.186  20.616  1.00 43.86           O  
ANISOU 1197  O   VAL A 173     3073  11091   2501   -382     46    780       O  
ATOM   1198  CB  VAL A 173      -3.221  13.294  18.148  1.00 38.37           C  
ANISOU 1198  CB  VAL A 173     2717   9707   2153   -241    132    386       C  
ATOM   1199  CG1 VAL A 173      -3.728  11.981  17.581  1.00 37.36           C  
ANISOU 1199  CG1 VAL A 173     2620   9408   2166   -219    129    630       C  
ATOM   1200  CG2 VAL A 173      -3.720  14.463  17.304  1.00 38.57           C  
ANISOU 1200  CG2 VAL A 173     2882   9517   2257   -181    170    101       C  
ATOM   1201  N   LEU A 174      -3.911  11.527  21.154  1.00 41.05           N  
ANISOU 1201  N   LEU A 174     2649  10901   2045   -426     82    885       N  
ATOM   1202  CA  LEU A 174      -3.454  10.435  22.021  1.00 41.34           C  
ANISOU 1202  CA  LEU A 174     2558  11153   1994   -487     31   1224       C  
ATOM   1203  C   LEU A 174      -2.831   9.279  21.254  1.00 45.79           C  
ANISOU 1203  C   LEU A 174     3227  11382   2789   -424     -5   1489       C  
ATOM   1204  O   LEU A 174      -3.095   9.137  20.064  1.00 45.81           O  
ANISOU 1204  O   LEU A 174     3390  11010   3005   -362     15   1429       O  
ATOM   1205  CB  LEU A 174      -4.618   9.921  22.874  1.00 41.28           C  
ANISOU 1205  CB  LEU A 174     2428  11434   1823   -584     36   1372       C  
ATOM   1206  CG  LEU A 174      -4.698  10.548  24.240  1.00 45.96           C  
ANISOU 1206  CG  LEU A 174     2823  12542   2097   -657     44   1274       C  
ATOM   1207  CD1 LEU A 174      -6.094  10.993  24.532  1.00 46.43           C  
ANISOU 1207  CD1 LEU A 174     2819  12803   2021   -679     97   1123       C  
ATOM   1208  CD2 LEU A 174      -4.158   9.617  25.303  1.00 48.02           C  
ANISOU 1208  CD2 LEU A 174     2920  13120   2206   -747    -16   1624       C  
ATOM   1209  N   ALA A 175      -2.014   8.442  21.926  1.00 42.02           N  
ANISOU 1209  N   ALA A 175     2659  11046   2261   -426    -60   1783       N  
ATOM   1210  CA  ALA A 175      -1.469   7.247  21.282  1.00 41.97           C  
ANISOU 1210  CA  ALA A 175     2764  10716   2469   -329    -96   2048       C  
ATOM   1211  C   ALA A 175      -2.669   6.310  20.964  1.00 47.57           C  
ANISOU 1211  C   ALA A 175     3577  11214   3281   -395    -97   2206       C  
ATOM   1212  O   ALA A 175      -3.573   6.153  21.807  1.00 49.10           O  
ANISOU 1212  O   ALA A 175     3667  11681   3309   -533   -102   2302       O  
ATOM   1213  CB  ALA A 175      -0.481   6.557  22.201  1.00 42.25           C  
ANISOU 1213  CB  ALA A 175     2666  10983   2404   -300   -157   2351       C  
ATOM   1214  N   GLY A 176      -2.703   5.767  19.744  1.00 41.90           N  
ANISOU 1214  N   GLY A 176     3056  10050   2814   -317    -92   2207       N  
ATOM   1215  CA  GLY A 176      -3.820   4.935  19.308  1.00 40.55           C  
ANISOU 1215  CA  GLY A 176     3006   9657   2745   -411    -97   2319       C  
ATOM   1216  C   GLY A 176      -4.885   5.767  18.622  1.00 41.11           C  
ANISOU 1216  C   GLY A 176     3109   9689   2821   -461    -38   2028       C  
ATOM   1217  O   GLY A 176      -5.957   5.269  18.284  1.00 39.72           O  
ANISOU 1217  O   GLY A 176     2997   9406   2688   -569    -36   2080       O  
ATOM   1218  N   GLN A 177      -4.603   7.055  18.448  1.00 36.71           N  
ANISOU 1218  N   GLN A 177     2505   9234   2209   -392      6   1730       N  
ATOM   1219  CA  GLN A 177      -5.468   7.995  17.751  1.00 36.12           C  
ANISOU 1219  CA  GLN A 177     2469   9107   2147   -388     61   1444       C  
ATOM   1220  C   GLN A 177      -4.684   8.600  16.603  1.00 37.78           C  
ANISOU 1220  C   GLN A 177     2804   9028   2524   -260     81   1248       C  
ATOM   1221  O   GLN A 177      -3.483   8.857  16.735  1.00 36.07           O  
ANISOU 1221  O   GLN A 177     2566   8829   2309   -193     66   1240       O  
ATOM   1222  CB  GLN A 177      -5.951   9.122  18.673  1.00 37.58           C  
ANISOU 1222  CB  GLN A 177     2501   9681   2096   -419     93   1251       C  
ATOM   1223  CG  GLN A 177      -7.160   8.785  19.526  1.00 44.63           C  
ANISOU 1223  CG  GLN A 177     3254  10902   2801   -546     97   1366       C  
ATOM   1224  CD  GLN A 177      -7.450   9.842  20.569  1.00 58.78           C  
ANISOU 1224  CD  GLN A 177     4882  13118   4334   -545    130   1168       C  
ATOM   1225  OE1 GLN A 177      -6.862  10.939  20.602  1.00 52.03           O  
ANISOU 1225  OE1 GLN A 177     4046  12275   3448   -458    150    908       O  
ATOM   1226  NE2 GLN A 177      -8.347   9.505  21.476  1.00 53.47           N  
ANISOU 1226  NE2 GLN A 177     4046  12813   3455   -654    132   1292       N  
ATOM   1227  N   CYS A 178      -5.370   8.819  15.475  1.00 34.19           N  
ANISOU 1227  N   CYS A 178     2459   8341   2190   -238    113   1105       N  
ATOM   1228  CA  CYS A 178      -4.797   9.459  14.305  1.00 33.28           C  
ANISOU 1228  CA  CYS A 178     2454   7975   2216   -135    135    919       C  
ATOM   1229  C   CYS A 178      -5.779  10.401  13.663  1.00 33.63           C  
ANISOU 1229  C   CYS A 178     2532   7987   2261   -123    177    694       C  
ATOM   1230  O   CYS A 178      -6.779   9.955  13.113  1.00 34.24           O  
ANISOU 1230  O   CYS A 178     2647   7978   2386   -161    187    721       O  
ATOM   1231  CB  CYS A 178      -4.256   8.448  13.308  1.00 34.48           C  
ANISOU 1231  CB  CYS A 178     2737   7801   2564    -76    118   1036       C  
ATOM   1232  SG  CYS A 178      -3.165   9.186  12.060  1.00 39.07           S  
ANISOU 1232  SG  CYS A 178     3399   8174   3271     51    139    852       S  
ATOM   1233  N   TYR A 179      -5.518  11.705  13.774  1.00 27.31           N  
ANISOU 1233  N   TYR A 179     1719   7262   1397    -75    198    479       N  
ATOM   1234  CA  TYR A 179      -6.333  12.776  13.207  1.00 26.53           C  
ANISOU 1234  CA  TYR A 179     1664   7118   1298    -21    235    258       C  
ATOM   1235  C   TYR A 179      -5.523  14.052  13.125  1.00 31.80           C  
ANISOU 1235  C   TYR A 179     2386   7737   1960     25    237     60       C  
ATOM   1236  O   TYR A 179      -4.459  14.123  13.750  1.00 32.35           O  
ANISOU 1236  O   TYR A 179     2416   7898   1975    -14    212     88       O  
ATOM   1237  CB  TYR A 179      -7.645  12.982  13.987  1.00 27.16           C  
ANISOU 1237  CB  TYR A 179     1635   7471   1214    -38    259    218       C  
ATOM   1238  CG  TYR A 179      -7.489  13.447  15.414  1.00 27.99           C  
ANISOU 1238  CG  TYR A 179     1620   7900   1114    -62    258    166       C  
ATOM   1239  CD1 TYR A 179      -7.373  12.532  16.457  1.00 29.83           C  
ANISOU 1239  CD1 TYR A 179     1729   8371   1232   -163    232    377       C  
ATOM   1240  CD2 TYR A 179      -7.533  14.802  15.735  1.00 29.06           C  
ANISOU 1240  CD2 TYR A 179     1772   8111   1159     14    281    -94       C  
ATOM   1241  CE1 TYR A 179      -7.245  12.953  17.779  1.00 28.96           C  
ANISOU 1241  CE1 TYR A 179     1489   8608    905   -195    231    328       C  
ATOM   1242  CE2 TYR A 179      -7.399  15.238  17.054  1.00 30.50           C  
ANISOU 1242  CE2 TYR A 179     1847   8607   1133    -14    281   -175       C  
ATOM   1243  CZ  TYR A 179      -7.268  14.306  18.074  1.00 37.70           C  
ANISOU 1243  CZ  TYR A 179     2610   9801   1915   -122    258     35       C  
ATOM   1244  OH  TYR A 179      -7.155  14.719  19.382  1.00 40.82           O  
ANISOU 1244  OH  TYR A 179     2880  10552   2077   -158    259    -44       O  
ATOM   1245  N   ILE A 180      -6.011  15.059  12.354  1.00 29.11           N  
ANISOU 1245  N   ILE A 180     2136   7256   1669     98    261   -124       N  
ATOM   1246  CA  ILE A 180      -5.311  16.341  12.185  1.00 28.86           C  
ANISOU 1246  CA  ILE A 180     2196   7123   1646    118    255   -308       C  
ATOM   1247  C   ILE A 180      -5.497  17.219  13.429  1.00 33.05           C  
ANISOU 1247  C   ILE A 180     2686   7873   1999    114    259   -472       C  
ATOM   1248  O   ILE A 180      -6.630  17.542  13.802  1.00 32.46           O  
ANISOU 1248  O   ILE A 180     2575   7923   1835    190    290   -565       O  
ATOM   1249  CB  ILE A 180      -5.629  17.081  10.852  1.00 30.96           C  
ANISOU 1249  CB  ILE A 180     2596   7124   2042    195    269   -411       C  
ATOM   1250  CG1 ILE A 180      -5.052  16.325   9.662  1.00 31.17           C  
ANISOU 1250  CG1 ILE A 180     2661   6962   2219    178    261   -279       C  
ATOM   1251  CG2 ILE A 180      -5.081  18.499  10.862  1.00 30.41           C  
ANISOU 1251  CG2 ILE A 180     2641   6948   1964    194    255   -598       C  
ATOM   1252  CD1 ILE A 180      -6.020  16.219   8.485  1.00 43.75           C  
ANISOU 1252  CD1 ILE A 180     4295   8431   3898    242    283   -271       C  
ATOM   1253  N   GLN A 181      -4.360  17.592  14.050  1.00 29.42           N  
ANISOU 1253  N   GLN A 181     2221   7484   1473     26    229   -513       N  
ATOM   1254  CA  GLN A 181      -4.311  18.399  15.243  1.00 29.66           C  
ANISOU 1254  CA  GLN A 181     2221   7726   1321     -8    225   -686       C  
ATOM   1255  C   GLN A 181      -4.750  19.844  15.029  1.00 36.64           C  
ANISOU 1255  C   GLN A 181     3264   8450   2209     69    238   -964       C  
ATOM   1256  O   GLN A 181      -5.463  20.347  15.893  1.00 36.16           O  
ANISOU 1256  O   GLN A 181     3172   8566   2000    132    261  -1125       O  
ATOM   1257  CB  GLN A 181      -2.928  18.328  15.883  1.00 30.79           C  
ANISOU 1257  CB  GLN A 181     2305   8008   1385   -150    180   -638       C  
ATOM   1258  CG  GLN A 181      -2.972  18.556  17.392  1.00 37.00           C  
ANISOU 1258  CG  GLN A 181     2975   9150   1933   -210    175   -725       C  
ATOM   1259  CD  GLN A 181      -1.620  18.543  18.057  1.00 54.12           C  
ANISOU 1259  CD  GLN A 181     5062  11508   3992   -362    126   -679       C  
ATOM   1260  OE1 GLN A 181      -0.848  17.580  17.954  1.00 49.62           O  
ANISOU 1260  OE1 GLN A 181     4392  11003   3460   -395    101   -433       O  
ATOM   1261  NE2 GLN A 181      -1.305  19.616  18.775  1.00 49.15           N  
ANISOU 1261  NE2 GLN A 181     4474  10985   3215   -451    109   -920       N  
ATOM   1262  N   PHE A 182      -4.340  20.526  13.921  1.00 35.75           N  
ANISOU 1262  N   PHE A 182     3320   8012   2251     75    224  -1020       N  
ATOM   1263  CA  PHE A 182      -4.740  21.932  13.715  1.00 37.48           C  
ANISOU 1263  CA  PHE A 182     3726   8029   2488    157    227  -1266       C  
ATOM   1264  C   PHE A 182      -6.230  22.103  13.350  1.00 48.81           C  
ANISOU 1264  C   PHE A 182     5173   9426   3946    373    274  -1321       C  
ATOM   1265  O   PHE A 182      -6.778  23.198  13.526  1.00 50.30           O  
ANISOU 1265  O   PHE A 182     5482   9529   4100    500    286  -1540       O  
ATOM   1266  CB  PHE A 182      -3.836  22.693  12.727  1.00 38.96           C  
ANISOU 1266  CB  PHE A 182     4094   7896   2811     70    187  -1293       C  
ATOM   1267  CG  PHE A 182      -3.923  22.290  11.275  1.00 40.28           C  
ANISOU 1267  CG  PHE A 182     4290   7858   3156    113    193  -1127       C  
ATOM   1268  CD1 PHE A 182      -4.833  22.899  10.415  1.00 43.07           C  
ANISOU 1268  CD1 PHE A 182     4761   7997   3608    267    211  -1178       C  
ATOM   1269  CD2 PHE A 182      -3.043  21.361  10.743  1.00 42.70           C  
ANISOU 1269  CD2 PHE A 182     4507   8196   3521     10    179   -930       C  
ATOM   1270  CE1 PHE A 182      -4.920  22.516   9.066  1.00 43.63           C  
ANISOU 1270  CE1 PHE A 182     4841   7917   3817    293    215  -1028       C  
ATOM   1271  CE2 PHE A 182      -3.116  20.992   9.388  1.00 45.21           C  
ANISOU 1271  CE2 PHE A 182     4850   8345   3983     52    187   -805       C  
ATOM   1272  CZ  PHE A 182      -4.070  21.554   8.567  1.00 42.89           C  
ANISOU 1272  CZ  PHE A 182     4658   7866   3771    180    205   -854       C  
ATOM   1273  N   LEU A 183      -6.892  21.028  12.877  1.00 48.16           N  
ANISOU 1273  N   LEU A 183     4966   9422   3910    418    299  -1129       N  
ATOM   1274  CA  LEU A 183      -8.316  21.050  12.545  1.00 48.99           C  
ANISOU 1274  CA  LEU A 183     5032   9574   4008    595    341  -1148       C  
ATOM   1275  C   LEU A 183      -9.182  20.780  13.787  1.00 57.08           C  
ANISOU 1275  C   LEU A 183     5885  10976   4825    649    375  -1197       C  
ATOM   1276  O   LEU A 183     -10.346  20.414  13.630  1.00 57.64           O  
ANISOU 1276  O   LEU A 183     5849  11196   4856    752    409  -1148       O  
ATOM   1277  CB  LEU A 183      -8.586  19.982  11.473  1.00 48.76           C  
ANISOU 1277  CB  LEU A 183     4943   9485   4099    566    344   -924       C  
ATOM   1278  CG  LEU A 183      -8.828  20.393  10.031  1.00 52.64           C  
ANISOU 1278  CG  LEU A 183     5548   9709   4742    651    343   -912       C  
ATOM   1279  CD1 LEU A 183      -8.356  21.803   9.722  1.00 52.46           C  
ANISOU 1279  CD1 LEU A 183     5727   9420   4786    702    321  -1071       C  
ATOM   1280  CD2 LEU A 183      -8.263  19.372   9.080  1.00 55.23           C  
ANISOU 1280  CD2 LEU A 183     5856   9936   5191    540    328   -718       C  
ATOM   1281  N   SER A 184      -8.626  20.958  15.007  1.00 56.38           N  
ANISOU 1281  N   SER A 184     5753  11083   4587    566    365  -1289       N  
ATOM   1282  CA ASER A 184      -9.344  20.718  16.254  0.84 57.53           C  
ANISOU 1282  CA ASER A 184     5718  11638   4504    598    397  -1335       C  
ATOM   1283  CA BSER A 184      -9.380  20.706  16.231  0.16 57.26           C  
ANISOU 1283  CA BSER A 184     5683  11603   4472    601    398  -1333       C  
ATOM   1284  C   SER A 184     -10.471  21.742  16.478  1.00 63.40           C  
ANISOU 1284  C   SER A 184     6490  12452   5149    839    443  -1588       C  
ATOM   1285  O   SER A 184     -11.618  21.351  16.752  1.00 63.95           O  
ANISOU 1285  O   SER A 184     6384  12819   5094    937    486  -1549       O  
ATOM   1286  CB ASER A 184      -8.376  20.683  17.440  0.84 61.09           C  
ANISOU 1286  CB ASER A 184     6113  12291   4808    441    369  -1370       C  
ATOM   1287  CB BSER A 184      -8.455  20.566  17.433  0.16 60.94           C  
ANISOU 1287  CB BSER A 184     6079  12288   4787    442    371  -1350       C  
ATOM   1288  OG ASER A 184      -8.995  20.476  18.701  0.84 66.08           O  
ANISOU 1288  OG ASER A 184     6561  13356   5190    459    398  -1423       O  
ATOM   1289  OG BSER A 184      -7.626  19.426  17.282  0.16 69.50           O  
ANISOU 1289  OG BSER A 184     7088  13381   5939    270    335  -1074       O  
ATOM   1290  N   GLN A 185     -10.145  23.054  16.359  1.00 60.87           N  
ANISOU 1290  N   GLN A 185     6391  11859   4877    935    433  -1842       N  
ATOM   1291  CA  GLN A 185     -11.143  24.108  16.572  1.00 60.77           C  
ANISOU 1291  CA  GLN A 185     6443  11863   4784   1210    475  -2105       C  
ATOM   1292  C   GLN A 185     -12.032  24.232  15.324  1.00 63.28           C  
ANISOU 1292  C   GLN A 185     6802  11991   5249   1403    493  -2027       C  
ATOM   1293  O   GLN A 185     -11.471  24.245  14.231  1.00 62.51           O  
ANISOU 1293  O   GLN A 185     6845  11548   5356   1329    456  -1913       O  
ATOM   1294  CB  GLN A 185     -10.471  25.444  16.948  1.00 62.22           C  
ANISOU 1294  CB  GLN A 185     6881  11793   4967   1233    448  -2409       C  
ATOM   1295  CG  GLN A 185     -11.432  26.464  17.579  1.00 78.27           C  
ANISOU 1295  CG  GLN A 185     8966  13917   6856   1528    496  -2729       C  
ATOM   1296  CD  GLN A 185     -10.758  27.721  18.081  1.00 98.89           C  
ANISOU 1296  CD  GLN A 185    11855  16265   9454   1522    464  -3054       C  
ATOM   1297  OE1 GLN A 185      -9.826  28.256  17.464  1.00 98.31           O  
ANISOU 1297  OE1 GLN A 185    12027  15769   9558   1384    403  -3056       O  
ATOM   1298  NE2 GLN A 185     -11.234  28.231  19.214  1.00 84.35           N  
ANISOU 1298  NE2 GLN A 185     9983  14679   7388   1662    502  -3344       N  
ATOM   1299  N   PRO A 186     -13.392  24.310  15.448  1.00 59.39           N  
ANISOU 1299  N   PRO A 186     6168  11759   4637   1643    548  -2076       N  
ATOM   1300  CA  PRO A 186     -14.254  24.371  14.245  1.00 59.22           C  
ANISOU 1300  CA  PRO A 186     6151  11616   4733   1819    561  -1977       C  
ATOM   1301  C   PRO A 186     -14.058  25.570  13.309  1.00 62.67           C  
ANISOU 1301  C   PRO A 186     6878  11576   5358   1985    535  -2092       C  
ATOM   1302  O   PRO A 186     -14.307  25.419  12.105  1.00 63.12           O  
ANISOU 1302  O   PRO A 186     6959  11466   5560   2014    522  -1930       O  
ATOM   1303  CB  PRO A 186     -15.681  24.337  14.816  1.00 60.86           C  
ANISOU 1303  CB  PRO A 186     6127  12275   4721   2053    626  -2046       C  
ATOM   1304  CG  PRO A 186     -15.537  23.738  16.168  1.00 65.17           C  
ANISOU 1304  CG  PRO A 186     6483  13230   5049   1897    643  -2055       C  
ATOM   1305  CD  PRO A 186     -14.217  24.261  16.669  1.00 60.61           C  
ANISOU 1305  CD  PRO A 186     6112  12397   4520   1754    601  -2199       C  
ATOM   1306  N   ILE A 187     -13.602  26.736  13.832  1.00 57.57           N  
ANISOU 1306  N   ILE A 187     6460  10705   4707   2072    521  -2361       N  
ATOM   1307  CA  ILE A 187     -13.355  27.942  13.024  1.00 56.53           C  
ANISOU 1307  CA  ILE A 187     6646  10075   4758   2204    484  -2464       C  
ATOM   1308  C   ILE A 187     -12.181  27.736  12.029  1.00 59.09           C  
ANISOU 1308  C   ILE A 187     7106  10054   5290   1923    420  -2269       C  
ATOM   1309  O   ILE A 187     -12.283  28.183  10.885  1.00 59.55           O  
ANISOU 1309  O   ILE A 187     7306   9809   5510   2006    395  -2183       O  
ATOM   1310  CB  ILE A 187     -13.208  29.226  13.892  1.00 59.51           C  
ANISOU 1310  CB  ILE A 187     7261  10280   5072   2349    480  -2818       C  
ATOM   1311  CG1 ILE A 187     -13.384  30.508  13.050  1.00 59.26           C  
ANISOU 1311  CG1 ILE A 187     7550   9755   5213   2591    451  -2917       C  
ATOM   1312  CG2 ILE A 187     -11.915  29.253  14.731  1.00 60.86           C  
ANISOU 1312  CG2 ILE A 187     7523  10401   5201   2026    437  -2918       C  
ATOM   1313  CD1 ILE A 187     -14.840  30.999  12.946  1.00 64.41           C  
ANISOU 1313  CD1 ILE A 187     8138  10536   5798   3054    509  -3005       C  
ATOM   1314  N   ILE A 188     -11.108  27.025  12.444  1.00 53.21           N  
ANISOU 1314  N   ILE A 188     6295   9400   4524   1608    395  -2184       N  
ATOM   1315  CA  ILE A 188      -9.962  26.714  11.575  1.00 51.90           C  
ANISOU 1315  CA  ILE A 188     6205   8998   4515   1344    341  -1999       C  
ATOM   1316  C   ILE A 188     -10.400  25.668  10.535  1.00 51.25           C  
ANISOU 1316  C   ILE A 188     5964   8992   4517   1338    356  -1730       C  
ATOM   1317  O   ILE A 188      -9.940  25.725   9.395  1.00 51.23           O  
ANISOU 1317  O   ILE A 188     6061   8733   4669   1268    324  -1602       O  
ATOM   1318  CB  ILE A 188      -8.683  26.284  12.373  1.00 55.32           C  
ANISOU 1318  CB  ILE A 188     6579   9569   4872   1050    314  -1989       C  
ATOM   1319  CG1 ILE A 188      -8.438  27.197  13.600  1.00 56.35           C  
ANISOU 1319  CG1 ILE A 188     6841   9696   4873   1046    302  -2286       C  
ATOM   1320  CG2 ILE A 188      -7.438  26.222  11.468  1.00 55.09           C  
ANISOU 1320  CG2 ILE A 188     6621   9323   4988    805    261  -1814       C  
ATOM   1321  CD1 ILE A 188      -7.692  26.546  14.755  1.00 67.24           C  
ANISOU 1321  CD1 ILE A 188     8067  11395   6086    829    295  -2297       C  
ATOM   1322  N   THR A 189     -11.315  24.743  10.923  1.00 44.25           N  
ANISOU 1322  N   THR A 189     4831   8471   3512   1399    402  -1650       N  
ATOM   1323  CA  THR A 189     -11.880  23.714  10.036  1.00 42.73           C  
ANISOU 1323  CA  THR A 189     4484   8384   3369   1377    415  -1422       C  
ATOM   1324  C   THR A 189     -12.703  24.398   8.952  1.00 45.21           C  
ANISOU 1324  C   THR A 189     4876   8537   3766   1600    420  -1420       C  
ATOM   1325  O   THR A 189     -12.667  23.977   7.802  1.00 43.22           O  
ANISOU 1325  O   THR A 189     4619   8179   3625   1539    404  -1254       O  
ATOM   1326  CB  THR A 189     -12.711  22.685  10.817  1.00 42.15           C  
ANISOU 1326  CB  THR A 189     4146   8744   3128   1359    455  -1348       C  
ATOM   1327  OG1 THR A 189     -12.013  22.318  12.002  1.00 39.18           O  
ANISOU 1327  OG1 THR A 189     3712   8531   2643   1205    449  -1381       O  
ATOM   1328  CG2 THR A 189     -13.000  21.436   9.994  1.00 37.02           C  
ANISOU 1328  CG2 THR A 189     3365   8166   2535   1227    451  -1103       C  
ATOM   1329  N   PHE A 190     -13.414  25.474   9.332  1.00 43.18           N  
ANISOU 1329  N   PHE A 190     4695   8261   3448   1870    440  -1612       N  
ATOM   1330  CA  PHE A 190     -14.220  26.298   8.439  1.00 43.66           C  
ANISOU 1330  CA  PHE A 190     4846   8167   3577   2142    442  -1623       C  
ATOM   1331  C   PHE A 190     -13.312  27.103   7.508  1.00 44.92           C  
ANISOU 1331  C   PHE A 190     5283   7855   3931   2078    383  -1594       C  
ATOM   1332  O   PHE A 190     -13.646  27.293   6.343  1.00 45.71           O  
ANISOU 1332  O   PHE A 190     5418   7824   4127   2164    368  -1464       O  
ATOM   1333  CB  PHE A 190     -15.179  27.210   9.243  1.00 46.46           C  
ANISOU 1333  CB  PHE A 190     5211   8639   3801   2484    482  -1854       C  
ATOM   1334  CG  PHE A 190     -15.971  28.168   8.386  1.00 49.14           C  
ANISOU 1334  CG  PHE A 190     5659   8801   4213   2814    479  -1863       C  
ATOM   1335  CD1 PHE A 190     -16.995  27.708   7.562  1.00 53.69           C  
ANISOU 1335  CD1 PHE A 190     6030   9612   4758   2935    500  -1686       C  
ATOM   1336  CD2 PHE A 190     -15.653  29.522   8.355  1.00 51.80           C  
ANISOU 1336  CD2 PHE A 190     6313   8719   4649   2987    448  -2030       C  
ATOM   1337  CE1 PHE A 190     -17.685  28.585   6.719  1.00 54.94           C  
ANISOU 1337  CE1 PHE A 190     6274   9622   4977   3248    492  -1663       C  
ATOM   1338  CE2 PHE A 190     -16.352  30.400   7.527  1.00 55.34           C  
ANISOU 1338  CE2 PHE A 190     6877   8974   5176   3308    438  -2004       C  
ATOM   1339  CZ  PHE A 190     -17.371  29.928   6.722  1.00 53.95           C  
ANISOU 1339  CZ  PHE A 190     6469   9071   4960   3451    462  -1815       C  
ATOM   1340  N   GLY A 191     -12.178  27.549   8.029  1.00 38.64           N  
ANISOU 1340  N   GLY A 191     4666   6845   3171   1907    348  -1704       N  
ATOM   1341  CA  GLY A 191     -11.179  28.283   7.267  1.00 37.36           C  
ANISOU 1341  CA  GLY A 191     4758   6267   3168   1776    286  -1669       C  
ATOM   1342  C   GLY A 191     -10.611  27.437   6.151  1.00 39.37           C  
ANISOU 1342  C   GLY A 191     4927   6513   3517   1564    266  -1418       C  
ATOM   1343  O   GLY A 191     -10.484  27.916   5.025  1.00 39.02           O  
ANISOU 1343  O   GLY A 191     5004   6231   3592   1578    233  -1309       O  
ATOM   1344  N   THR A 192     -10.302  26.158   6.447  1.00 34.90           N  
ANISOU 1344  N   THR A 192     4152   6216   2892   1381    287  -1322       N  
ATOM   1345  CA  THR A 192      -9.789  25.201   5.464  1.00 33.92           C  
ANISOU 1345  CA  THR A 192     3934   6114   2842   1201    277  -1111       C  
ATOM   1346  C   THR A 192     -10.883  24.804   4.484  1.00 37.75           C  
ANISOU 1346  C   THR A 192     4303   6702   3339   1342    299   -988       C  
ATOM   1347  O   THR A 192     -10.587  24.630   3.308  1.00 38.07           O  
ANISOU 1347  O   THR A 192     4361   6639   3466   1268    280   -850       O  
ATOM   1348  CB  THR A 192      -9.116  23.992   6.121  1.00 38.72           C  
ANISOU 1348  CB  THR A 192     4387   6933   3390    994    286  -1054       C  
ATOM   1349  OG1 THR A 192     -10.093  23.231   6.821  1.00 44.15           O  
ANISOU 1349  OG1 THR A 192     4888   7927   3961   1073    329  -1057       O  
ATOM   1350  CG2 THR A 192      -7.965  24.378   7.043  1.00 32.98           C  
ANISOU 1350  CG2 THR A 192     3750   6149   2631    839    257  -1160       C  
ATOM   1351  N   ALA A 193     -12.144  24.705   4.953  1.00 34.43           N  
ANISOU 1351  N   ALA A 193     3754   6515   2812   1540    339  -1040       N  
ATOM   1352  CA  ALA A 193     -13.324  24.385   4.134  1.00 34.79           C  
ANISOU 1352  CA  ALA A 193     3660   6729   2831   1679    360   -934       C  
ATOM   1353  C   ALA A 193     -13.591  25.470   3.080  1.00 41.36           C  
ANISOU 1353  C   ALA A 193     4640   7321   3753   1859    333   -901       C  
ATOM   1354  O   ALA A 193     -14.037  25.151   1.968  1.00 41.23           O  
ANISOU 1354  O   ALA A 193     4542   7364   3758   1869    328   -755       O  
ATOM   1355  CB  ALA A 193     -14.546  24.225   5.018  1.00 35.32           C  
ANISOU 1355  CB  ALA A 193     3549   7135   2735   1855    407  -1011       C  
ATOM   1356  N   MET A 194     -13.331  26.752   3.437  1.00 38.83           N  
ANISOU 1356  N   MET A 194     4545   6727   3481   1994    311  -1035       N  
ATOM   1357  CA  MET A 194     -13.488  27.896   2.535  1.00 38.83           C  
ANISOU 1357  CA  MET A 194     4738   6435   3583   2165    274   -993       C  
ATOM   1358  C   MET A 194     -12.443  27.800   1.430  1.00 41.07           C  
ANISOU 1358  C   MET A 194     5110   6511   3985   1921    227   -829       C  
ATOM   1359  O   MET A 194     -12.780  27.949   0.263  1.00 42.01           O  
ANISOU 1359  O   MET A 194     5219   6596   4146   1983    209   -676       O  
ATOM   1360  CB  MET A 194     -13.332  29.234   3.281  1.00 41.60           C  
ANISOU 1360  CB  MET A 194     5353   6488   3965   2326    253  -1192       C  
ATOM   1361  CG  MET A 194     -14.504  29.596   4.152  1.00 46.35           C  
ANISOU 1361  CG  MET A 194     5889   7275   4447   2664    301  -1363       C  
ATOM   1362  SD  MET A 194     -16.027  29.907   3.240  1.00 52.31           S  
ANISOU 1362  SD  MET A 194     6526   8175   5173   3054    319  -1242       S  
ATOM   1363  CE  MET A 194     -15.687  31.569   2.566  1.00 49.47           C  
ANISOU 1363  CE  MET A 194     6575   7224   4996   3237    247  -1244       C  
ATOM   1364  N   ALA A 195     -11.192  27.492   1.795  1.00 34.68           N  
ANISOU 1364  N   ALA A 195     4353   5620   3205   1643    209   -852       N  
ATOM   1365  CA  ALA A 195     -10.068  27.369   0.875  1.00 33.22           C  
ANISOU 1365  CA  ALA A 195     4226   5293   3104   1396    170   -711       C  
ATOM   1366  C   ALA A 195     -10.099  26.119   0.005  1.00 35.24           C  
ANISOU 1366  C   ALA A 195     4269   5779   3340   1282    192   -558       C  
ATOM   1367  O   ALA A 195      -9.607  26.177  -1.113  1.00 35.72           O  
ANISOU 1367  O   ALA A 195     4359   5759   3456   1179    166   -424       O  
ATOM   1368  CB  ALA A 195      -8.761  27.428   1.650  1.00 33.81           C  
ANISOU 1368  CB  ALA A 195     4393   5267   3186   1156    147   -795       C  
ATOM   1369  N   THR A 196     -10.646  24.994   0.503  1.00 30.27           N  
ANISOU 1369  N   THR A 196     3438   5435   2627   1282    237   -578       N  
ATOM   1370  CA  THR A 196     -10.665  23.710  -0.223  1.00 29.34           C  
ANISOU 1370  CA  THR A 196     3148   5507   2492   1155    255   -462       C  
ATOM   1371  C   THR A 196     -12.004  23.342  -0.891  1.00 30.33           C  
ANISOU 1371  C   THR A 196     3127   5837   2558   1288    275   -393       C  
ATOM   1372  O   THR A 196     -12.024  22.414  -1.708  1.00 27.70           O  
ANISOU 1372  O   THR A 196     2689   5620   2217   1173    280   -303       O  
ATOM   1373  CB  THR A 196     -10.202  22.555   0.689  1.00 38.90           C  
ANISOU 1373  CB  THR A 196     4253   6867   3659   1005    279   -497       C  
ATOM   1374  OG1 THR A 196     -11.058  22.451   1.829  1.00 38.28           O  
ANISOU 1374  OG1 THR A 196     4094   6963   3487   1113    307   -587       O  
ATOM   1375  CG2 THR A 196      -8.770  22.696   1.133  1.00 39.32           C  
ANISOU 1375  CG2 THR A 196     4400   6786   3752    842    256   -527       C  
ATOM   1376  N   PHE A 197     -13.113  24.023  -0.522  1.00 27.40           N  
ANISOU 1376  N   PHE A 197     2741   5538   2133   1528    287   -445       N  
ATOM   1377  CA  PHE A 197     -14.422  23.718  -1.099  1.00 27.66           C  
ANISOU 1377  CA  PHE A 197     2602   5827   2081   1658    303   -372       C  
ATOM   1378  C   PHE A 197     -15.201  24.940  -1.557  1.00 33.37           C  
ANISOU 1378  C   PHE A 197     3387   6486   2807   1946    288   -348       C  
ATOM   1379  O   PHE A 197     -15.418  25.070  -2.750  1.00 32.08           O  
ANISOU 1379  O   PHE A 197     3201   6330   2657   1967    266   -215       O  
ATOM   1380  CB  PHE A 197     -15.269  22.855  -0.148  1.00 29.10           C  
ANISOU 1380  CB  PHE A 197     2588   6333   2135   1657    343   -423       C  
ATOM   1381  CG  PHE A 197     -16.607  22.401  -0.693  1.00 30.27           C  
ANISOU 1381  CG  PHE A 197     2523   6811   2165   1732    358   -342       C  
ATOM   1382  CD1 PHE A 197     -16.680  21.426  -1.687  1.00 32.72           C  
ANISOU 1382  CD1 PHE A 197     2735   7234   2464   1541    347   -233       C  
ATOM   1383  CD2 PHE A 197     -17.795  22.915  -0.184  1.00 31.92           C  
ANISOU 1383  CD2 PHE A 197     2620   7250   2259   1989    382   -386       C  
ATOM   1384  CE1 PHE A 197     -17.918  20.977  -2.163  1.00 33.00           C  
ANISOU 1384  CE1 PHE A 197     2563   7607   2369   1567    354   -163       C  
ATOM   1385  CE2 PHE A 197     -19.031  22.464  -0.660  1.00 34.59           C  
ANISOU 1385  CE2 PHE A 197     2727   7956   2461   2037    392   -299       C  
ATOM   1386  CZ  PHE A 197     -19.083  21.495  -1.644  1.00 32.35           C  
ANISOU 1386  CZ  PHE A 197     2348   7780   2164   1806    375   -184       C  
ATOM   1387  N   TYR A 198     -15.620  25.827  -0.627  1.00 33.02           N  
ANISOU 1387  N   TYR A 198     3419   6385   2740   2181    300   -476       N  
ATOM   1388  CA  TYR A 198     -16.462  27.000  -0.910  1.00 33.73           C  
ANISOU 1388  CA  TYR A 198     3578   6410   2829   2523    289   -469       C  
ATOM   1389  C   TYR A 198     -15.874  27.967  -1.932  1.00 37.57           C  
ANISOU 1389  C   TYR A 198     4287   6537   3450   2544    231   -357       C  
ATOM   1390  O   TYR A 198     -16.596  28.325  -2.859  1.00 38.36           O  
ANISOU 1390  O   TYR A 198     4337   6702   3535   2717    214   -219       O  
ATOM   1391  CB  TYR A 198     -16.873  27.732   0.365  1.00 35.72           C  
ANISOU 1391  CB  TYR A 198     3900   6639   3034   2773    315   -668       C  
ATOM   1392  CG  TYR A 198     -17.696  26.869   1.292  1.00 38.83           C  
ANISOU 1392  CG  TYR A 198     4032   7464   3258   2790    373   -746       C  
ATOM   1393  CD1 TYR A 198     -19.036  26.604   1.024  1.00 40.97           C  
ANISOU 1393  CD1 TYR A 198     4051   8128   3387   2973    401   -678       C  
ATOM   1394  CD2 TYR A 198     -17.129  26.287   2.420  1.00 40.38           C  
ANISOU 1394  CD2 TYR A 198     4215   7712   3417   2602    394   -865       C  
ATOM   1395  CE1 TYR A 198     -19.807  25.817   1.883  1.00 41.48           C  
ANISOU 1395  CE1 TYR A 198     3862   8622   3276   2957    450   -730       C  
ATOM   1396  CE2 TYR A 198     -17.889  25.496   3.287  1.00 42.04           C  
ANISOU 1396  CE2 TYR A 198     4180   8334   3458   2597    442   -909       C  
ATOM   1397  CZ  TYR A 198     -19.230  25.266   3.015  1.00 49.25           C  
ANISOU 1397  CZ  TYR A 198     4850   9630   4231   2765    470   -841       C  
ATOM   1398  OH  TYR A 198     -19.983  24.483   3.860  1.00 50.81           O  
ANISOU 1398  OH  TYR A 198     4796  10264   4246   2723    512   -863       O  
ATOM   1399  N   LEU A 199     -14.594  28.359  -1.809  1.00 33.06           N  
ANISOU 1399  N   LEU A 199     3940   5627   2993   2352    196   -391       N  
ATOM   1400  CA  LEU A 199     -13.956  29.225  -2.804  1.00 33.20           C  
ANISOU 1400  CA  LEU A 199     4165   5321   3128   2309    135   -255       C  
ATOM   1401  C   LEU A 199     -13.701  28.474  -4.137  1.00 34.58           C  
ANISOU 1401  C   LEU A 199     4196   5651   3291   2110    123    -55       C  
ATOM   1402  O   LEU A 199     -14.201  28.972  -5.144  1.00 34.50           O  
ANISOU 1402  O   LEU A 199     4186   5636   3286   2244     95    104       O  
ATOM   1403  CB  LEU A 199     -12.701  29.938  -2.282  1.00 34.02           C  
ANISOU 1403  CB  LEU A 199     4543   5047   3335   2138     95   -343       C  
ATOM   1404  CG  LEU A 199     -12.948  31.341  -1.712  1.00 40.14           C  
ANISOU 1404  CG  LEU A 199     5597   5480   4174   2385     64   -460       C  
ATOM   1405  CD1 LEU A 199     -13.164  31.313  -0.204  1.00 40.39           C  
ANISOU 1405  CD1 LEU A 199     5638   5569   4141   2472    106   -727       C  
ATOM   1406  CD2 LEU A 199     -11.792  32.258  -2.025  1.00 44.97           C  
ANISOU 1406  CD2 LEU A 199     6510   5664   4912   2192    -11   -400       C  
ATOM   1407  N   PRO A 200     -13.065  27.260  -4.192  1.00 28.63           N  
ANISOU 1407  N   PRO A 200     3303   5067   2506   1829    147    -58       N  
ATOM   1408  CA  PRO A 200     -12.924  26.566  -5.492  1.00 27.59           C  
ANISOU 1408  CA  PRO A 200     3038   5098   2346   1677    141     98       C  
ATOM   1409  C   PRO A 200     -14.240  26.309  -6.248  1.00 30.27           C  
ANISOU 1409  C   PRO A 200     3186   5729   2588   1841    151    196       C  
ATOM   1410  O   PRO A 200     -14.272  26.517  -7.455  1.00 29.13           O  
ANISOU 1410  O   PRO A 200     3018   5615   2434   1826    122    354       O  
ATOM   1411  CB  PRO A 200     -12.208  25.257  -5.128  1.00 29.10           C  
ANISOU 1411  CB  PRO A 200     3121   5422   2514   1424    174     25       C  
ATOM   1412  CG  PRO A 200     -11.501  25.560  -3.883  1.00 34.15           C  
ANISOU 1412  CG  PRO A 200     3892   5881   3201   1380    176   -112       C  
ATOM   1413  CD  PRO A 200     -12.402  26.485  -3.121  1.00 29.74           C  
ANISOU 1413  CD  PRO A 200     3412   5254   2634   1651    177   -199       C  
ATOM   1414  N   VAL A 201     -15.324  25.901  -5.541  1.00 26.96           N  
ANISOU 1414  N   VAL A 201     2614   5554   2076   1987    190    112       N  
ATOM   1415  CA  VAL A 201     -16.652  25.648  -6.122  1.00 26.77           C  
ANISOU 1415  CA  VAL A 201     2374   5870   1928   2135    200    199       C  
ATOM   1416  C   VAL A 201     -17.242  26.946  -6.743  1.00 30.88           C  
ANISOU 1416  C   VAL A 201     2974   6294   2467   2438    162    324       C  
ATOM   1417  O   VAL A 201     -17.705  26.912  -7.883  1.00 29.48           O  
ANISOU 1417  O   VAL A 201     2682   6290   2229   2459    140    486       O  
ATOM   1418  CB  VAL A 201     -17.628  24.929  -5.137  1.00 30.00           C  
ANISOU 1418  CB  VAL A 201     2586   6599   2214   2193    247     91       C  
ATOM   1419  CG1 VAL A 201     -19.073  25.002  -5.620  1.00 29.45           C  
ANISOU 1419  CG1 VAL A 201     2297   6890   2001   2404    252    182       C  
ATOM   1420  CG2 VAL A 201     -17.223  23.471  -4.943  1.00 29.72           C  
ANISOU 1420  CG2 VAL A 201     2444   6701   2146   1873    270     45       C  
ATOM   1421  N   THR A 202     -17.186  28.077  -6.007  1.00 27.61           N  
ANISOU 1421  N   THR A 202     2768   5587   2135   2665    151    248       N  
ATOM   1422  CA  THR A 202     -17.663  29.385  -6.472  1.00 26.87           C  
ANISOU 1422  CA  THR A 202     2812   5309   2087   2983    109    359       C  
ATOM   1423  C   THR A 202     -16.916  29.782  -7.743  1.00 28.42           C  
ANISOU 1423  C   THR A 202     3128   5308   2362   2833     48    566       C  
ATOM   1424  O   THR A 202     -17.556  30.126  -8.730  1.00 29.48           O  
ANISOU 1424  O   THR A 202     3190   5559   2452   2988     18    757       O  
ATOM   1425  CB  THR A 202     -17.555  30.437  -5.333  1.00 37.54           C  
ANISOU 1425  CB  THR A 202     4418   6318   3527   3206    108    189       C  
ATOM   1426  OG1 THR A 202     -18.237  29.958  -4.173  1.00 34.05           O  
ANISOU 1426  OG1 THR A 202     3820   6141   2977   3327    170      1       O  
ATOM   1427  CG2 THR A 202     -18.121  31.810  -5.717  1.00 37.74           C  
ANISOU 1427  CG2 THR A 202     4627   6095   3616   3579     62    289       C  
ATOM   1428  N   VAL A 203     -15.582  29.673  -7.731  1.00 23.02           N  
ANISOU 1428  N   VAL A 203     2593   4385   1769   2525     32    541       N  
ATOM   1429  CA  VAL A 203     -14.686  29.990  -8.852  1.00 22.31           C  
ANISOU 1429  CA  VAL A 203     2603   4139   1735   2322    -22    727       C  
ATOM   1430  C   VAL A 203     -15.011  29.139 -10.089  1.00 28.04           C  
ANISOU 1430  C   VAL A 203     3071   5245   2340   2211    -15    877       C  
ATOM   1431  O   VAL A 203     -15.098  29.684 -11.189  1.00 27.95           O  
ANISOU 1431  O   VAL A 203     3072   5233   2316   2254    -63   1092       O  
ATOM   1432  CB  VAL A 203     -13.193  29.888  -8.415  1.00 24.96           C  
ANISOU 1432  CB  VAL A 203     3089   4239   2154   2000    -28    637       C  
ATOM   1433  CG1 VAL A 203     -12.231  29.872  -9.602  1.00 24.30           C  
ANISOU 1433  CG1 VAL A 203     3012   4147   2075   1732    -66    819       C  
ATOM   1434  CG2 VAL A 203     -12.837  31.015  -7.460  1.00 24.84           C  
ANISOU 1434  CG2 VAL A 203     3375   3807   2256   2086    -59    531       C  
ATOM   1435  N   MET A 204     -15.207  27.817  -9.896  1.00 25.61           N  
ANISOU 1435  N   MET A 204     2540   5255   1936   2066     38    763       N  
ATOM   1436  CA  MET A 204     -15.497  26.859 -10.961  1.00 26.19           C  
ANISOU 1436  CA  MET A 204     2380   5690   1883   1922     48    846       C  
ATOM   1437  C   MET A 204     -16.877  27.013 -11.567  1.00 32.91           C  
ANISOU 1437  C   MET A 204     3045   6848   2610   2150     38    968       C  
ATOM   1438  O   MET A 204     -17.051  26.742 -12.749  1.00 32.74           O  
ANISOU 1438  O   MET A 204     2887   7062   2492   2067     19   1107       O  
ATOM   1439  CB  MET A 204     -15.259  25.425 -10.504  1.00 28.65           C  
ANISOU 1439  CB  MET A 204     2559   6179   2146   1694    100    678       C  
ATOM   1440  CG  MET A 204     -13.800  25.092 -10.405  1.00 33.49           C  
ANISOU 1440  CG  MET A 204     3289   6594   2842   1440    104    617       C  
ATOM   1441  SD  MET A 204     -13.511  23.345 -10.102  1.00 39.36           S  
ANISOU 1441  SD  MET A 204     3891   7530   3533   1198    156    456       S  
ATOM   1442  CE  MET A 204     -13.777  23.261  -8.300  1.00 35.12           C  
ANISOU 1442  CE  MET A 204     3401   6900   3043   1292    187    291       C  
ATOM   1443  N   CYS A 205     -17.846  27.452 -10.776  1.00 33.00           N  
ANISOU 1443  N   CYS A 205     3037   6894   2606   2440     52    917       N  
ATOM   1444  CA  CYS A 205     -19.210  27.669 -11.221  1.00 34.68           C  
ANISOU 1444  CA  CYS A 205     3053   7435   2687   2704     44   1034       C  
ATOM   1445  C   CYS A 205     -19.278  28.924 -12.059  1.00 39.33           C  
ANISOU 1445  C   CYS A 205     3767   7851   3324   2923    -18   1262       C  
ATOM   1446  O   CYS A 205     -19.969  28.939 -13.088  1.00 38.43           O  
ANISOU 1446  O   CYS A 205     3473   8040   3087   2996    -44   1448       O  
ATOM   1447  CB  CYS A 205     -20.156  27.742 -10.033  1.00 36.67           C  
ANISOU 1447  CB  CYS A 205     3234   7803   2895   2961     85    896       C  
ATOM   1448  SG  CYS A 205     -20.547  26.133  -9.309  1.00 41.79           S  
ANISOU 1448  SG  CYS A 205     3635   8828   3414   2707    147    715       S  
ATOM   1449  N   THR A 206     -18.560  29.980 -11.618  1.00 36.48           N  
ANISOU 1449  N   THR A 206     3722   7004   3137   3014    -48   1257       N  
ATOM   1450  CA  THR A 206     -18.477  31.268 -12.322  1.00 36.42           C  
ANISOU 1450  CA  THR A 206     3910   6716   3211   3201   -119   1484       C  
ATOM   1451  C   THR A 206     -17.769  31.077 -13.667  1.00 39.25           C  
ANISOU 1451  C   THR A 206     4230   7146   3537   2914   -160   1691       C  
ATOM   1452  O   THR A 206     -18.196  31.642 -14.664  1.00 39.36           O  
ANISOU 1452  O   THR A 206     4203   7252   3501   3048   -211   1945       O  
ATOM   1453  CB  THR A 206     -17.869  32.363 -11.422  1.00 45.58           C  
ANISOU 1453  CB  THR A 206     5441   7316   4562   3319   -143   1390       C  
ATOM   1454  OG1 THR A 206     -16.628  31.912 -10.881  1.00 52.46           O  
ANISOU 1454  OG1 THR A 206     6426   7999   5509   2972   -123   1221       O  
ATOM   1455  CG2 THR A 206     -18.810  32.783 -10.282  1.00 38.80           C  
ANISOU 1455  CG2 THR A 206     4607   6433   3703   3718   -109   1224       C  
ATOM   1456  N   LEU A 207     -16.741  30.219 -13.692  1.00 35.39           N  
ANISOU 1456  N   LEU A 207     3723   6670   3052   2536   -134   1583       N  
ATOM   1457  CA  LEU A 207     -15.988  29.846 -14.884  1.00 34.94           C  
ANISOU 1457  CA  LEU A 207     3597   6744   2936   2242   -157   1723       C  
ATOM   1458  C   LEU A 207     -16.872  29.046 -15.832  1.00 39.21           C  
ANISOU 1458  C   LEU A 207     3816   7806   3277   2228   -143   1797       C  
ATOM   1459  O   LEU A 207     -16.857  29.329 -17.023  1.00 38.94           O  
ANISOU 1459  O   LEU A 207     3716   7916   3163   2190   -187   2022       O  
ATOM   1460  CB  LEU A 207     -14.751  29.024 -14.492  1.00 34.86           C  
ANISOU 1460  CB  LEU A 207     3626   6650   2969   1899   -119   1541       C  
ATOM   1461  CG  LEU A 207     -13.405  29.739 -14.506  1.00 39.24           C  
ANISOU 1461  CG  LEU A 207     4429   6833   3647   1717   -159   1604       C  
ATOM   1462  CD1 LEU A 207     -13.414  30.992 -13.640  1.00 39.90           C  
ANISOU 1462  CD1 LEU A 207     4808   6464   3887   1913   -198   1600       C  
ATOM   1463  CD2 LEU A 207     -12.322  28.817 -14.023  1.00 40.84           C  
ANISOU 1463  CD2 LEU A 207     4614   7039   3863   1431   -113   1410       C  
ATOM   1464  N   TYR A 208     -17.665  28.081 -15.310  1.00 36.11           N  
ANISOU 1464  N   TYR A 208     3222   7711   2789   2244    -89   1621       N  
ATOM   1465  CA  TYR A 208     -18.581  27.265 -16.114  1.00 36.19           C  
ANISOU 1465  CA  TYR A 208     2925   8234   2593   2196    -80   1664       C  
ATOM   1466  C   TYR A 208     -19.706  28.092 -16.778  1.00 43.35           C  
ANISOU 1466  C   TYR A 208     3712   9361   3399   2504   -127   1909       C  
ATOM   1467  O   TYR A 208     -20.041  27.811 -17.929  1.00 42.15           O  
ANISOU 1467  O   TYR A 208     3364   9567   3084   2417   -151   2053       O  
ATOM   1468  CB  TYR A 208     -19.162  26.082 -15.313  1.00 36.44           C  
ANISOU 1468  CB  TYR A 208     2792   8506   2549   2109    -21   1433       C  
ATOM   1469  CG  TYR A 208     -19.974  25.133 -16.167  1.00 36.83           C  
ANISOU 1469  CG  TYR A 208     2545   9070   2380   1975    -18   1455       C  
ATOM   1470  CD1 TYR A 208     -19.357  24.162 -16.941  1.00 38.61           C  
ANISOU 1470  CD1 TYR A 208     2710   9427   2534   1644    -10   1389       C  
ATOM   1471  CD2 TYR A 208     -21.360  25.235 -16.234  1.00 37.33           C  
ANISOU 1471  CD2 TYR A 208     2384   9508   2290   2182    -27   1537       C  
ATOM   1472  CE1 TYR A 208     -20.096  23.311 -17.760  1.00 40.62           C  
ANISOU 1472  CE1 TYR A 208     2713  10144   2578   1497    -13   1388       C  
ATOM   1473  CE2 TYR A 208     -22.113  24.384 -17.040  1.00 38.35           C  
ANISOU 1473  CE2 TYR A 208     2234  10138   2198   2022    -33   1558       C  
ATOM   1474  CZ  TYR A 208     -21.476  23.422 -17.806  1.00 50.30           C  
ANISOU 1474  CZ  TYR A 208     3717  11745   3650   1666    -28   1476       C  
ATOM   1475  OH  TYR A 208     -22.208  22.595 -18.633  1.00 56.79           O  
ANISOU 1475  OH  TYR A 208     4283  13050   4244   1485    -39   1475       O  
ATOM   1476  N   TRP A 209     -20.296  29.088 -16.060  1.00 43.37           N  
ANISOU 1476  N   TRP A 209     3824   9172   3483   2876   -139   1949       N  
ATOM   1477  CA  TRP A 209     -21.367  29.936 -16.612  1.00 44.78           C  
ANISOU 1477  CA  TRP A 209     3899   9539   3576   3235   -183   2190       C  
ATOM   1478  C   TRP A 209     -20.825  30.762 -17.785  1.00 47.28           C  
ANISOU 1478  C   TRP A 209     4336   9703   3925   3220   -258   2485       C  
ATOM   1479  O   TRP A 209     -21.542  30.980 -18.770  1.00 47.04           O  
ANISOU 1479  O   TRP A 209     4117  10008   3746   3346   -299   2725       O  
ATOM   1480  CB  TRP A 209     -22.076  30.814 -15.524  1.00 44.69           C  
ANISOU 1480  CB  TRP A 209     3998   9334   3649   3676   -173   2134       C  
ATOM   1481  CG  TRP A 209     -23.459  31.343 -15.885  1.00 46.78           C  
ANISOU 1481  CG  TRP A 209     4057   9944   3774   4089   -197   2325       C  
ATOM   1482  CD1 TRP A 209     -24.099  31.221 -17.088  1.00 50.27           C  
ANISOU 1482  CD1 TRP A 209     4236  10837   4027   4099   -235   2564       C  
ATOM   1483  CD2 TRP A 209     -24.339  32.118 -15.046  1.00 47.01           C  
ANISOU 1483  CD2 TRP A 209     4123   9907   3830   4573   -185   2295       C  
ATOM   1484  NE1 TRP A 209     -25.327  31.850 -17.045  1.00 50.24           N  
ANISOU 1484  NE1 TRP A 209     4088  11072   3930   4560   -249   2702       N  
ATOM   1485  CE2 TRP A 209     -25.500  32.409 -15.806  1.00 51.35           C  
ANISOU 1485  CE2 TRP A 209     4411  10896   4202   4873   -217   2536       C  
ATOM   1486  CE3 TRP A 209     -24.274  32.575 -13.712  1.00 48.55           C  
ANISOU 1486  CE3 TRP A 209     4533   9750   4163   4792   -149   2075       C  
ATOM   1487  CZ2 TRP A 209     -26.569  33.158 -15.292  1.00 50.55           C  
ANISOU 1487  CZ2 TRP A 209     4258  10881   4066   5411   -211   2571       C  
ATOM   1488  CZ3 TRP A 209     -25.341  33.308 -13.199  1.00 50.03           C  
ANISOU 1488  CZ3 TRP A 209     4679  10015   4313   5315   -140   2086       C  
ATOM   1489  CH2 TRP A 209     -26.470  33.592 -13.983  1.00 50.75           C  
ANISOU 1489  CH2 TRP A 209     4510  10538   4236   5633   -170   2334       C  
ATOM   1490  N   ARG A 210     -19.548  31.171 -17.690  1.00 42.84           N  
ANISOU 1490  N   ARG A 210     4064   8677   3535   3038   -277   2478       N  
ATOM   1491  CA  ARG A 210     -18.889  31.923 -18.746  1.00 42.71           C  
ANISOU 1491  CA  ARG A 210     4173   8506   3547   2958   -350   2765       C  
ATOM   1492  C   ARG A 210     -18.554  31.031 -19.936  1.00 44.26           C  
ANISOU 1492  C   ARG A 210     4131   9126   3562   2618   -347   2831       C  
ATOM   1493  O   ARG A 210     -18.713  31.479 -21.066  1.00 43.67           O  
ANISOU 1493  O   ARG A 210     3977   9231   3386   2643   -404   3120       O  
ATOM   1494  CB  ARG A 210     -17.650  32.671 -18.237  1.00 45.37           C  
ANISOU 1494  CB  ARG A 210     4884   8248   4106   2841   -377   2745       C  
ATOM   1495  CG  ARG A 210     -17.485  34.031 -18.949  1.00 60.67           C  
ANISOU 1495  CG  ARG A 210     7040   9889   6123   2979   -474   3094       C  
ATOM   1496  CD  ARG A 210     -16.392  34.911 -18.362  1.00 74.29           C  
ANISOU 1496  CD  ARG A 210     9165  10992   8069   2873   -514   3079       C  
ATOM   1497  NE  ARG A 210     -16.667  35.315 -16.977  1.00 83.09           N  
ANISOU 1497  NE  ARG A 210    10491  11744   9334   3122   -489   2839       N  
ATOM   1498  CZ  ARG A 210     -15.822  36.005 -16.216  1.00 93.92           C  
ANISOU 1498  CZ  ARG A 210    12213  12580  10891   3040   -514   2744       C  
ATOM   1499  NH1 ARG A 210     -14.638  36.374 -16.692  1.00 81.59           N  
ANISOU 1499  NH1 ARG A 210    10825  10785   9389   2700   -569   2886       N  
ATOM   1500  NH2 ARG A 210     -16.150  36.325 -14.971  1.00 75.83           N  
ANISOU 1500  NH2 ARG A 210    10089  10016   8706   3279   -487   2502       N  
ATOM   1501  N   ILE A 211     -18.105  29.779 -19.683  1.00 38.46           N  
ANISOU 1501  N   ILE A 211     3286   8550   2777   2316   -281   2563       N  
ATOM   1502  CA  ILE A 211     -17.751  28.800 -20.714  1.00 36.88           C  
ANISOU 1502  CA  ILE A 211     2876   8736   2402   1995   -265   2547       C  
ATOM   1503  C   ILE A 211     -18.984  28.415 -21.513  1.00 43.16           C  
ANISOU 1503  C   ILE A 211     3353  10082   2962   2079   -276   2646       C  
ATOM   1504  O   ILE A 211     -18.907  28.377 -22.741  1.00 44.75           O  
ANISOU 1504  O   ILE A 211     3414  10581   3006   1954   -309   2822       O  
ATOM   1505  CB  ILE A 211     -17.028  27.570 -20.120  1.00 38.70           C  
ANISOU 1505  CB  ILE A 211     3103   8944   2659   1711   -194   2219       C  
ATOM   1506  CG1 ILE A 211     -15.615  27.936 -19.641  1.00 38.26           C  
ANISOU 1506  CG1 ILE A 211     3312   8443   2784   1564   -193   2170       C  
ATOM   1507  CG2 ILE A 211     -16.986  26.392 -21.097  1.00 38.86           C  
ANISOU 1507  CG2 ILE A 211     2882   9410   2474   1441   -169   2141       C  
ATOM   1508  CD1 ILE A 211     -15.077  27.019 -18.504  1.00 36.77           C  
ANISOU 1508  CD1 ILE A 211     3178   8109   2683   1425   -125   1850       C  
ATOM   1509  N   TYR A 212     -20.116  28.157 -20.834  1.00 38.71           N  
ANISOU 1509  N   TYR A 212     2661   9694   2355   2279   -251   2544       N  
ATOM   1510  CA  TYR A 212     -21.360  27.795 -21.502  1.00 38.48           C  
ANISOU 1510  CA  TYR A 212     2305  10233   2083   2353   -264   2637       C  
ATOM   1511  C   TYR A 212     -21.924  28.943 -22.337  1.00 43.47           C  
ANISOU 1511  C   TYR A 212     2890  10978   2650   2640   -339   3007       C  
ATOM   1512  O   TYR A 212     -22.428  28.699 -23.431  1.00 42.78           O  
ANISOU 1512  O   TYR A 212     2547  11371   2336   2570   -369   3160       O  
ATOM   1513  CB  TYR A 212     -22.404  27.287 -20.497  1.00 39.69           C  
ANISOU 1513  CB  TYR A 212     2322  10565   2195   2489   -220   2453       C  
ATOM   1514  CG  TYR A 212     -23.605  26.653 -21.162  1.00 41.56           C  
ANISOU 1514  CG  TYR A 212     2189  11451   2149   2462   -229   2505       C  
ATOM   1515  CD1 TYR A 212     -23.644  25.285 -21.416  1.00 43.28           C  
ANISOU 1515  CD1 TYR A 212     2236  11991   2216   2093   -198   2300       C  
ATOM   1516  CD2 TYR A 212     -24.704  27.422 -21.547  1.00 42.63           C  
ANISOU 1516  CD2 TYR A 212     2151  11884   2162   2807   -274   2760       C  
ATOM   1517  CE1 TYR A 212     -24.749  24.696 -22.027  1.00 44.79           C  
ANISOU 1517  CE1 TYR A 212     2092  12793   2133   2023   -214   2339       C  
ATOM   1518  CE2 TYR A 212     -25.806  26.848 -22.176  1.00 43.64           C  
ANISOU 1518  CE2 TYR A 212     1912  12664   2005   2763   -288   2818       C  
ATOM   1519  CZ  TYR A 212     -25.829  25.483 -22.399  1.00 51.67           C  
ANISOU 1519  CZ  TYR A 212     2764  14001   2868   2350   -259   2601       C  
ATOM   1520  OH  TYR A 212     -26.921  24.923 -22.996  1.00 55.28           O  
ANISOU 1520  OH  TYR A 212     2865  15106   3032   2271   -279   2650       O  
ATOM   1521  N   ARG A 213     -21.869  30.176 -21.815  1.00 42.07           N  
ANISOU 1521  N   ARG A 213     2960  10362   2663   2965   -372   3147       N  
ATOM   1522  CA  ARG A 213     -22.367  31.362 -22.511  1.00 43.17           C  
ANISOU 1522  CA  ARG A 213     3116  10470   2815   3220   -348   3445       C  
ATOM   1523  C   ARG A 213     -21.505  31.663 -23.758  1.00 46.58           C  
ANISOU 1523  C   ARG A 213     3587  10944   3168   3045   -508   3771       C  
ATOM   1524  O   ARG A 213     -22.057  31.970 -24.802  1.00 46.84           O  
ANISOU 1524  O   ARG A 213     3424  11305   3067   3086   -482   3998       O  
ATOM   1525  CB  ARG A 213     -22.411  32.555 -21.546  1.00 44.81           C  
ANISOU 1525  CB  ARG A 213     3643  10139   3243   3633   -418   3516       C  
ATOM   1526  CG  ARG A 213     -23.110  33.783 -22.113  1.00 57.10           C  
ANISOU 1526  CG  ARG A 213     5225  11693   4778   4089   -550   3931       C  
ATOM   1527  CD  ARG A 213     -23.146  34.919 -21.113  1.00 71.12           C  
ANISOU 1527  CD  ARG A 213     7353  12870   6801   4480   -567   3918       C  
ATOM   1528  NE  ARG A 213     -24.062  34.659 -20.000  1.00 85.68           N  
ANISOU 1528  NE  ARG A 213     9092  14834   8628   4767   -500   3665       N  
ATOM   1529  CZ  ARG A 213     -25.346  35.015 -19.982  1.00102.14           C  
ANISOU 1529  CZ  ARG A 213    10980  17230  10597   5217   -507   3779       C  
ATOM   1530  NH1 ARG A 213     -25.886  35.635 -21.026  1.00 88.00           N  
ANISOU 1530  NH1 ARG A 213     9077  15658   8701   5444   -581   4152       N  
ATOM   1531  NH2 ARG A 213     -26.099  34.751 -18.921  1.00 88.96           N  
ANISOU 1531  NH2 ARG A 213     9205  15696   8897   5448   -440   3534       N  
ATOM   1532  N   GLU A 214     -20.169  31.523 -23.650  1.00 42.45           N  
ANISOU 1532  N   GLU A 214     3269  10059   2800   2705   -445   3622       N  
ATOM   1533  CA  GLU A 214     -19.212  31.739 -24.728  1.00 42.19           C  
ANISOU 1533  CA  GLU A 214     3254  10022   2753   2415   -448   3788       C  
ATOM   1534  C   GLU A 214     -19.374  30.666 -25.807  1.00 47.37           C  
ANISOU 1534  C   GLU A 214     3588  11352   3059   2192   -515   3829       C  
ATOM   1535  O   GLU A 214     -19.458  31.013 -26.988  1.00 47.40           O  
ANISOU 1535  O   GLU A 214     3459  11652   2900   2160   -572   4124       O  
ATOM   1536  CB  GLU A 214     -17.780  31.736 -24.181  1.00 43.38           C  
ANISOU 1536  CB  GLU A 214     3707   9743   3031   2200   -514   3710       C  
ATOM   1537  CG  GLU A 214     -16.748  32.344 -25.113  1.00 55.60           C  
ANISOU 1537  CG  GLU A 214     5360  11196   4571   1980   -574   3983       C  
ATOM   1538  CD  GLU A 214     -16.472  33.827 -24.944  1.00 77.49           C  
ANISOU 1538  CD  GLU A 214     8464  13438   7539   2153   -660   4276       C  
ATOM   1539  OE1 GLU A 214     -17.044  34.444 -24.015  1.00 71.50           O  
ANISOU 1539  OE1 GLU A 214     7894  12321   6950   2481   -669   4234       O  
ATOM   1540  OE2 GLU A 214     -15.667  34.369 -25.738  1.00 66.56           O  
ANISOU 1540  OE2 GLU A 214     7160  11996   6134   1952   -719   4544       O  
ATOM   1541  N   THR A 215     -19.432  29.373 -25.406  1.00 44.33           N  
ANISOU 1541  N   THR A 215     3065  11170   2606   1995   -438   3470       N  
ATOM   1542  CA  THR A 215     -19.585  28.224 -26.311  1.00 44.39           C  
ANISOU 1542  CA  THR A 215     2778  11738   2349   1715   -412   3354       C  
ATOM   1543  C   THR A 215     -20.821  28.369 -27.197  1.00 50.76           C  
ANISOU 1543  C   THR A 215     3284  13096   2905   1862   -460   3585       C  
ATOM   1544  O   THR A 215     -20.699  28.240 -28.417  1.00 51.39           O  
ANISOU 1544  O   THR A 215     3189  13567   2771   1692   -490   3732       O  
ATOM   1545  CB  THR A 215     -19.542  26.887 -25.530  1.00 46.64           C  
ANISOU 1545  CB  THR A 215     3029  12045   2649   1524   -329   2932       C  
ATOM   1546  OG1 THR A 215     -18.303  26.796 -24.836  1.00 40.74           O  
ANISOU 1546  OG1 THR A 215     2539  10829   2112   1391   -291   2761       O  
ATOM   1547  CG2 THR A 215     -19.687  25.654 -26.427  1.00 43.65           C  
ANISOU 1547  CG2 THR A 215     2391  12184   2008   1222   -304   2771       C  
ATOM   1548  N   GLU A 216     -21.988  28.674 -26.599  1.00 49.07           N  
ANISOU 1548  N   GLU A 216     2997  12948   2701   2183   -469   3626       N  
ATOM   1549  CA  GLU A 216     -23.232  28.846 -27.348  1.00 50.51           C  
ANISOU 1549  CA  GLU A 216     2869  13689   2635   2361   -517   3858       C  
ATOM   1550  C   GLU A 216     -23.228  30.097 -28.236  1.00 55.46           C  
ANISOU 1550  C   GLU A 216     3524  14310   3237   2572   -606   4315       C  
ATOM   1551  O   GLU A 216     -23.887  30.100 -29.271  1.00 55.33           O  
ANISOU 1551  O   GLU A 216     3223  14842   2959   2583   -652   4536       O  
ATOM   1552  CB  GLU A 216     -24.480  28.792 -26.441  1.00 52.57           C  
ANISOU 1552  CB  GLU A 216     3010  14077   2888   2656   -496   3775       C  
ATOM   1553  CG  GLU A 216     -24.683  29.956 -25.482  1.00 65.89           C  
ANISOU 1553  CG  GLU A 216     4940  15276   4819   3102   -510   3887       C  
ATOM   1554  CD  GLU A 216     -26.105  30.055 -24.970  1.00 89.38           C  
ANISOU 1554  CD  GLU A 216     7700  18563   7696   3453   -503   3897       C  
ATOM   1555  OE1 GLU A 216     -26.989  30.439 -25.772  1.00 80.81           O  
ANISOU 1555  OE1 GLU A 216     6356  17944   6404   3657   -556   4175       O  
ATOM   1556  OE2 GLU A 216     -26.343  29.737 -23.780  1.00 85.76           O  
ANISOU 1556  OE2 GLU A 216     7309  17931   7347   3524   -444   3636       O  
ATOM   1557  N   ASN A 217     -22.477  31.138 -27.839  1.00 52.87           N  
ANISOU 1557  N   ASN A 217     3544  13372   3172   2716   -635   4461       N  
ATOM   1558  CA  ASN A 217     -22.355  32.378 -28.597  1.00 52.98           C  
ANISOU 1558  CA  ASN A 217     3629  13214   3285   2836   -612   4818       C  
ATOM   1559  C   ASN A 217     -21.514  32.175 -29.838  1.00 55.46           C  
ANISOU 1559  C   ASN A 217     3878  13824   3371   2522   -738   5043       C  
ATOM   1560  O   ASN A 217     -21.891  32.634 -30.912  1.00 56.46           O  
ANISOU 1560  O   ASN A 217     3799  14258   3395   2537   -708   5316       O  
ATOM   1561  CB  ASN A 217     -21.782  33.500 -27.736  1.00 56.52           C  
ANISOU 1561  CB  ASN A 217     4537  12945   3991   3115   -755   4990       C  
ATOM   1562  CG  ASN A 217     -22.680  34.713 -27.737  1.00 94.14           C  
ANISOU 1562  CG  ASN A 217     9371  17584   8812   3615   -832   5340       C  
ATOM   1563  OD1 ASN A 217     -22.852  35.395 -28.766  1.00 94.13           O  
ANISOU 1563  OD1 ASN A 217     9303  17760   8702   3702   -916   5753       O  
ATOM   1564  ND2 ASN A 217     -23.306  34.987 -26.595  1.00 84.91           N  
ANISOU 1564  ND2 ASN A 217     8324  16137   7801   3975   -803   5188       N  
ATOM   1565  N   ARG A 218     -20.401  31.464 -29.694  1.00 50.70           N  
ANISOU 1565  N   ARG A 218     3336  13031   2898   2115   -597   4697       N  
ATOM   1566  CA  ARG A 218     -19.465  31.165 -30.760  1.00 50.45           C  
ANISOU 1566  CA  ARG A 218     3205  13221   2743   1746   -588   4745       C  
ATOM   1567  C   ARG A 218     -19.998  30.104 -31.717  1.00 56.55           C  
ANISOU 1567  C   ARG A 218     3647  14802   3039   1595   -682   4742       C  
ATOM   1568  O   ARG A 218     -19.775  30.232 -32.917  1.00 58.77           O  
ANISOU 1568  O   ARG A 218     3766  15463   3100   1442   -724   4973       O  
ATOM   1569  CB  ARG A 218     -18.119  30.714 -30.175  1.00 49.40           C  
ANISOU 1569  CB  ARG A 218     3334  12753   2681   1502   -616   4532       C  
ATOM   1570  CG  ARG A 218     -17.301  31.820 -29.519  1.00 56.14           C  
ANISOU 1570  CG  ARG A 218     4586  12946   3800   1593   -680   4706       C  
ATOM   1571  CD  ARG A 218     -16.010  31.258 -28.938  1.00 67.93           C  
ANISOU 1571  CD  ARG A 218     6239  14153   5420   1301   -614   4399       C  
ATOM   1572  NE  ARG A 218     -15.210  32.267 -28.237  1.00 70.79           N  
ANISOU 1572  NE  ARG A 218     6965  13881   6053   1333   -652   4511       N  
ATOM   1573  CZ  ARG A 218     -14.320  33.066 -28.820  1.00 81.38           C  
ANISOU 1573  CZ  ARG A 218     8436  15076   7410   1166   -715   4804       C  
ATOM   1574  NH1 ARG A 218     -14.114  33.001 -30.131  1.00 62.85           N  
ANISOU 1574  NH1 ARG A 218     5870  13195   4815    976   -743   5032       N  
ATOM   1575  NH2 ARG A 218     -13.643  33.949 -28.099  1.00 68.04           N  
ANISOU 1575  NH2 ARG A 218     7093  12792   5967   1170   -753   4878       N  
ATOM   1576  N   ALA A 219     -20.708  29.071 -31.204  1.00 52.49           N  
ANISOU 1576  N   ALA A 219     2981  14503   2459   1575   -621   4399       N  
ATOM   1577  CA  ALA A 219     -21.214  27.913 -31.969  1.00 60.59           C  
ANISOU 1577  CA  ALA A 219     3671  16185   3165   1333   -595   4211       C  
ATOM   1578  C   ALA A 219     -21.644  28.234 -33.393  1.00 68.21           C  
ANISOU 1578  C   ALA A 219     4354  17749   3814   1302   -665   4546       C  
ATOM   1579  O   ALA A 219     -22.715  27.867 -33.850  1.00 52.36           O  
ANISOU 1579  O   ALA A 219     1906  16042   1948   1236   -347   4365       O  
ATOM   1580  CB  ALA A 219     -22.324  27.209 -31.213  1.00 61.23           C  
ANISOU 1580  CB  ALA A 219     3622  16425   3218   1428   -561   3971       C  
ATOM   1581  N   ASN A1002     -23.217  30.143 -32.419  1.00 38.93           N  
ANISOU 1581  N   ASN A1002     3360   9352   2079     47    643   3663       N  
ATOM   1582  CA  ASN A1002     -24.173  30.747 -33.306  1.00 38.81           C  
ANISOU 1582  CA  ASN A1002     3338   9221   2187    -93    578   3482       C  
ATOM   1583  C   ASN A1002     -23.456  31.442 -34.431  1.00 43.69           C  
ANISOU 1583  C   ASN A1002     4189   9622   2789   -253    362   3039       C  
ATOM   1584  O   ASN A1002     -23.960  31.402 -35.545  1.00 44.23           O  
ANISOU 1584  O   ASN A1002     4257   9461   3087   -456    279   2908       O  
ATOM   1585  CB  ASN A1002     -25.054  31.690 -32.522  1.00 39.19           C  
ANISOU 1585  CB  ASN A1002     3347   9631   1914    178    675   3536       C  
ATOM   1586  CG  ASN A1002     -25.958  30.974 -31.543  1.00 55.97           C  
ANISOU 1586  CG  ASN A1002     5171  12009   4088    340    944   4061       C  
ATOM   1587  OD1 ASN A1002     -26.510  29.901 -31.824  1.00 50.64           O  
ANISOU 1587  OD1 ASN A1002     4239  11143   3859    127   1018   4387       O  
ATOM   1588  ND2 ASN A1002     -26.132  31.552 -30.366  1.00 44.87           N  
ANISOU 1588  ND2 ASN A1002     3782  11027   2242    736   1080   4157       N  
ATOM   1589  N   ILE A1003     -22.255  32.037 -34.173  1.00 39.99           N  
ANISOU 1589  N   ILE A1003     3899   9231   2066   -172    256   2842       N  
ATOM   1590  CA  ILE A1003     -21.451  32.710 -35.218  1.00 39.23           C  
ANISOU 1590  CA  ILE A1003     3976   8956   1972   -325     76   2509       C  
ATOM   1591  C   ILE A1003     -20.987  31.673 -36.245  1.00 44.20           C  
ANISOU 1591  C   ILE A1003     4586   9293   2917   -510     93   2509       C  
ATOM   1592  O   ILE A1003     -21.038  31.952 -37.438  1.00 43.26           O  
ANISOU 1592  O   ILE A1003     4557   9000   2879   -651     10   2300       O  
ATOM   1593  CB  ILE A1003     -20.278  33.584 -34.672  1.00 41.26           C  
ANISOU 1593  CB  ILE A1003     4368   9352   1956   -234    -75   2359       C  
ATOM   1594  CG1 ILE A1003     -20.728  34.452 -33.485  1.00 41.60           C  
ANISOU 1594  CG1 ILE A1003     4491   9671   1646     20   -114   2327       C  
ATOM   1595  CG2 ILE A1003     -19.691  34.471 -35.777  1.00 39.89           C  
ANISOU 1595  CG2 ILE A1003     4321   9013   1823   -405   -244   2092       C  
ATOM   1596  CD1 ILE A1003     -19.616  34.880 -32.503  1.00 51.84           C  
ANISOU 1596  CD1 ILE A1003     5890  11140   2668    151   -284   2264       C  
ATOM   1597  N   PHE A1004     -20.588  30.463 -35.779  1.00 42.44           N  
ANISOU 1597  N   PHE A1004     4261   9013   2851   -473    204   2751       N  
ATOM   1598  CA  PHE A1004     -20.163  29.361 -36.642  1.00 42.72           C  
ANISOU 1598  CA  PHE A1004     4314   8731   3186   -579    225   2742       C  
ATOM   1599  C   PHE A1004     -21.271  28.884 -37.559  1.00 46.28           C  
ANISOU 1599  C   PHE A1004     4763   8914   3909   -753    182   2681       C  
ATOM   1600  O   PHE A1004     -21.015  28.705 -38.748  1.00 46.19           O  
ANISOU 1600  O   PHE A1004     4892   8675   3983   -842    100   2442       O  
ATOM   1601  CB  PHE A1004     -19.545  28.202 -35.841  1.00 44.90           C  
ANISOU 1601  CB  PHE A1004     4489   8978   3594   -467    343   3043       C  
ATOM   1602  CG  PHE A1004     -19.106  27.012 -36.666  1.00 47.15           C  
ANISOU 1602  CG  PHE A1004     4829   8886   4200   -516    366   3019       C  
ATOM   1603  CD1 PHE A1004     -17.969  27.080 -37.468  1.00 50.14           C  
ANISOU 1603  CD1 PHE A1004     5327   9196   4529   -468    347   2810       C  
ATOM   1604  CD2 PHE A1004     -19.813  25.814 -36.621  1.00 50.00           C  
ANISOU 1604  CD2 PHE A1004     5120   8950   4926   -586    406   3225       C  
ATOM   1605  CE1 PHE A1004     -17.562  25.981 -38.228  1.00 51.02           C  
ANISOU 1605  CE1 PHE A1004     5533   8965   4888   -429    385   2754       C  
ATOM   1606  CE2 PHE A1004     -19.402  24.713 -37.378  1.00 52.81           C  
ANISOU 1606  CE2 PHE A1004     5591   8893   5581   -597    389   3148       C  
ATOM   1607  CZ  PHE A1004     -18.280  24.805 -38.175  1.00 50.64           C  
ANISOU 1607  CZ  PHE A1004     5479   8573   5190   -486    388   2888       C  
ATOM   1608  N   GLU A1005     -22.494  28.711 -37.024  1.00 42.42           N  
ANISOU 1608  N   GLU A1005     4104   8481   3535   -785    225   2905       N  
ATOM   1609  CA  GLU A1005     -23.652  28.268 -37.810  1.00 42.20           C  
ANISOU 1609  CA  GLU A1005     4009   8211   3816   -989    127   2894       C  
ATOM   1610  C   GLU A1005     -24.161  29.340 -38.786  1.00 42.86           C  
ANISOU 1610  C   GLU A1005     4195   8337   3751  -1065    -21   2588       C  
ATOM   1611  O   GLU A1005     -24.663  28.989 -39.851  1.00 42.25           O  
ANISOU 1611  O   GLU A1005     4170   8012   3872  -1237   -179   2433       O  
ATOM   1612  CB  GLU A1005     -24.781  27.738 -36.904  1.00 44.24           C  
ANISOU 1612  CB  GLU A1005     3968   8551   4291  -1008    235   3326       C  
ATOM   1613  CG  GLU A1005     -24.480  26.418 -36.190  1.00 58.25           C  
ANISOU 1613  CG  GLU A1005     5619  10166   6347   -996    353   3694       C  
ATOM   1614  CD  GLU A1005     -24.078  25.225 -37.042  1.00 85.23           C  
ANISOU 1614  CD  GLU A1005     9163  13066  10155  -1157    223   3584       C  
ATOM   1615  OE1 GLU A1005     -24.682  25.028 -38.122  1.00 93.19           O  
ANISOU 1615  OE1 GLU A1005    10239  13774  11395  -1370     13   3360       O  
ATOM   1616  OE2 GLU A1005     -23.154  24.486 -36.625  1.00 70.14           O  
ANISOU 1616  OE2 GLU A1005     7301  11046   8304  -1042    315   3709       O  
ATOM   1617  N   MET A1006     -23.992  30.637 -38.433  1.00 37.50           N  
ANISOU 1617  N   MET A1006     3572   7950   2727   -927      1   2491       N  
ATOM   1618  CA  MET A1006     -24.361  31.813 -39.237  1.00 36.24           C  
ANISOU 1618  CA  MET A1006     3519   7843   2406   -956   -125   2242       C  
ATOM   1619  C   MET A1006     -23.494  31.882 -40.492  1.00 40.45           C  
ANISOU 1619  C   MET A1006     4269   8198   2901  -1040   -231   1963       C  
ATOM   1620  O   MET A1006     -24.019  32.034 -41.589  1.00 40.78           O  
ANISOU 1620  O   MET A1006     4379   8131   2983  -1146   -363   1803       O  
ATOM   1621  CB  MET A1006     -24.178  33.094 -38.406  1.00 38.30           C  
ANISOU 1621  CB  MET A1006     3831   8385   2337   -761    -91   2210       C  
ATOM   1622  CG  MET A1006     -24.786  34.321 -39.012  1.00 41.84           C  
ANISOU 1622  CG  MET A1006     4357   8877   2665   -752   -202   2034       C  
ATOM   1623  SD  MET A1006     -24.195  35.820 -38.204  1.00 46.24           S  
ANISOU 1623  SD  MET A1006     5084   9614   2870   -536   -243   1896       S  
ATOM   1624  CE  MET A1006     -25.455  37.008 -38.746  1.00 42.97           C  
ANISOU 1624  CE  MET A1006     4691   9224   2411   -471   -325   1799       C  
ATOM   1625  N   LEU A1007     -22.173  31.774 -40.324  1.00 37.58           N  
ANISOU 1625  N   LEU A1007     3992   7844   2444   -967   -167   1934       N  
ATOM   1626  CA  LEU A1007     -21.197  31.799 -41.406  1.00 37.30           C  
ANISOU 1626  CA  LEU A1007     4117   7709   2347   -982   -195   1746       C  
ATOM   1627  C   LEU A1007     -21.193  30.496 -42.210  1.00 44.11           C  
ANISOU 1627  C   LEU A1007     5056   8292   3411  -1021   -206   1671       C  
ATOM   1628  O   LEU A1007     -20.759  30.513 -43.351  1.00 44.95           O  
ANISOU 1628  O   LEU A1007     5327   8324   3428  -1002   -240   1475       O  
ATOM   1629  CB  LEU A1007     -19.787  32.130 -40.864  1.00 36.97           C  
ANISOU 1629  CB  LEU A1007     4068   7806   2172   -883   -124   1805       C  
ATOM   1630  CG  LEU A1007     -19.337  33.613 -40.802  1.00 40.69           C  
ANISOU 1630  CG  LEU A1007     4577   8444   2440   -888   -209   1742       C  
ATOM   1631  CD1 LEU A1007     -19.234  34.244 -42.193  1.00 40.98           C  
ANISOU 1631  CD1 LEU A1007     4728   8430   2414   -956   -262   1598       C  
ATOM   1632  CD2 LEU A1007     -20.176  34.451 -39.825  1.00 39.79           C  
ANISOU 1632  CD2 LEU A1007     4438   8460   2219   -843   -276   1762       C  
ATOM   1633  N   ARG A1008     -21.692  29.380 -41.639  1.00 42.89           N  
ANISOU 1633  N   ARG A1008     4799   7970   3526  -1059   -187   1830       N  
ATOM   1634  CA  ARG A1008     -21.798  28.081 -42.318  1.00 43.93           C  
ANISOU 1634  CA  ARG A1008     5032   7739   3919  -1110   -258   1741       C  
ATOM   1635  C   ARG A1008     -22.890  28.168 -43.379  1.00 50.76           C  
ANISOU 1635  C   ARG A1008     5978   8464   4846  -1270   -487   1534       C  
ATOM   1636  O   ARG A1008     -22.757  27.554 -44.439  1.00 52.43           O  
ANISOU 1636  O   ARG A1008     6408   8425   5089  -1269   -613   1279       O  
ATOM   1637  CB  ARG A1008     -22.123  26.969 -41.315  1.00 45.82           C  
ANISOU 1637  CB  ARG A1008     5101   7815   4492  -1144   -198   2045       C  
ATOM   1638  CG  ARG A1008     -21.862  25.570 -41.841  1.00 59.24           C  
ANISOU 1638  CG  ARG A1008     6946   9072   6491  -1147   -261   1963       C  
ATOM   1639  CD  ARG A1008     -21.951  24.540 -40.731  1.00 73.28           C  
ANISOU 1639  CD  ARG A1008     8540  10698   8605  -1154   -166   2346       C  
ATOM   1640  NE  ARG A1008     -22.114  23.195 -41.282  1.00 84.46           N  
ANISOU 1640  NE  ARG A1008    10094  11573  10426  -1227   -312   2268       N  
ATOM   1641  CZ  ARG A1008     -23.082  22.353 -40.934  1.00 97.78           C  
ANISOU 1641  CZ  ARG A1008    11623  12955  12573  -1441   -432   2514       C  
ATOM   1642  NH1 ARG A1008     -23.966  22.695 -40.005  1.00 84.34           N  
ANISOU 1642  NH1 ARG A1008     9584  11506  10955  -1565   -362   2901       N  
ATOM   1643  NH2 ARG A1008     -23.168  21.159 -41.505  1.00 83.65           N  
ANISOU 1643  NH2 ARG A1008    10009  10595  11177  -1517   -625   2390       N  
ATOM   1644  N   ILE A1009     -23.956  28.951 -43.098  1.00 47.28           N  
ANISOU 1644  N   ILE A1009     5368   8204   4393  -1371   -551   1636       N  
ATOM   1645  CA  ILE A1009     -25.074  29.213 -44.011  1.00 46.92           C  
ANISOU 1645  CA  ILE A1009     5333   8101   4393  -1521   -788   1494       C  
ATOM   1646  C   ILE A1009     -24.646  30.236 -45.101  1.00 51.74           C  
ANISOU 1646  C   ILE A1009     6163   8858   4638  -1437   -839   1226       C  
ATOM   1647  O   ILE A1009     -24.778  29.951 -46.289  1.00 51.23           O  
ANISOU 1647  O   ILE A1009     6295   8648   4522  -1466  -1021    975       O  
ATOM   1648  CB  ILE A1009     -26.327  29.673 -43.201  1.00 49.47           C  
ANISOU 1648  CB  ILE A1009     5339   8610   4845  -1600   -785   1774       C  
ATOM   1649  CG1 ILE A1009     -26.911  28.506 -42.365  1.00 49.46           C  
ANISOU 1649  CG1 ILE A1009     5087   8443   5263  -1717   -756   2101       C  
ATOM   1650  CG2 ILE A1009     -27.389  30.287 -44.114  1.00 49.85           C  
ANISOU 1650  CG2 ILE A1009     5363   8703   4877  -1710  -1019   1653       C  
ATOM   1651  CD1 ILE A1009     -27.823  28.906 -41.198  1.00 52.16           C  
ANISOU 1651  CD1 ILE A1009     5072   9080   5665  -1678   -600   2498       C  
ATOM   1652  N   ASP A1010     -24.099  31.394 -44.675  1.00 49.56           N  
ANISOU 1652  N   ASP A1010     5865   8854   4111  -1324   -692   1292       N  
ATOM   1653  CA  ASP A1010     -23.692  32.527 -45.507  1.00 50.16           C  
ANISOU 1653  CA  ASP A1010     6087   9083   3890  -1260   -712   1156       C  
ATOM   1654  C   ASP A1010     -22.432  32.321 -46.350  1.00 55.94           C  
ANISOU 1654  C   ASP A1010     7022   9791   4441  -1146   -629   1019       C  
ATOM   1655  O   ASP A1010     -22.480  32.528 -47.560  1.00 56.32           O  
ANISOU 1655  O   ASP A1010     7239   9849   4311  -1115   -719    854       O  
ATOM   1656  CB  ASP A1010     -23.537  33.791 -44.640  1.00 52.41           C  
ANISOU 1656  CB  ASP A1010     6275   9588   4048  -1197   -622   1291       C  
ATOM   1657  CG  ASP A1010     -24.824  34.341 -44.047  1.00 67.27           C  
ANISOU 1657  CG  ASP A1010     7995  11568   5998  -1213   -679   1401       C  
ATOM   1658  OD1 ASP A1010     -25.914  34.048 -44.601  1.00 68.37           O  
ANISOU 1658  OD1 ASP A1010     8066  11648   6262  -1308   -822   1385       O  
ATOM   1659  OD2 ASP A1010     -24.745  35.077 -43.040  1.00 73.71           O  
ANISOU 1659  OD2 ASP A1010     8750  12527   6730  -1110   -594   1499       O  
ATOM   1660  N   GLU A1011     -21.299  31.982 -45.719  1.00 53.50           N  
ANISOU 1660  N   GLU A1011     6679   9500   4148  -1051   -448   1117       N  
ATOM   1661  CA  GLU A1011     -20.017  31.817 -46.411  1.00 53.64           C  
ANISOU 1661  CA  GLU A1011     6819   9555   4008   -899   -314   1062       C  
ATOM   1662  C   GLU A1011     -19.787  30.397 -46.958  1.00 58.25           C  
ANISOU 1662  C   GLU A1011     7565   9898   4672   -789   -302    904       C  
ATOM   1663  O   GLU A1011     -19.260  30.260 -48.055  1.00 58.31           O  
ANISOU 1663  O   GLU A1011     7761   9923   4470   -627   -257    749       O  
ATOM   1664  CB  GLU A1011     -18.856  32.271 -45.505  1.00 55.05           C  
ANISOU 1664  CB  GLU A1011     6844   9899   4174   -845   -156   1271       C  
ATOM   1665  CG  GLU A1011     -17.546  32.550 -46.225  1.00 67.39           C  
ANISOU 1665  CG  GLU A1011     8430  11601   5576   -711     -8   1317       C  
ATOM   1666  CD  GLU A1011     -17.470  33.878 -46.953  1.00 95.15           C  
ANISOU 1666  CD  GLU A1011    11960  15284   8909   -758    -40   1357       C  
ATOM   1667  OE1 GLU A1011     -17.279  34.914 -46.274  1.00 87.75           O  
ANISOU 1667  OE1 GLU A1011    10894  14437   8009   -867    -92   1500       O  
ATOM   1668  OE2 GLU A1011     -17.587  33.883 -48.201  1.00 91.59           O  
ANISOU 1668  OE2 GLU A1011    11666  14862   8272   -672    -28   1249       O  
ATOM   1669  N   GLY A1012     -20.169  29.374 -46.197  1.00 55.46           N  
ANISOU 1669  N   GLY A1012     7146   9318   4610   -848   -336    957       N  
ATOM   1670  CA  GLY A1012     -20.002  27.974 -46.581  1.00 55.70           C  
ANISOU 1670  CA  GLY A1012     7347   9019   4799   -754   -364    809       C  
ATOM   1671  C   GLY A1012     -18.814  27.300 -45.918  1.00 60.99           C  
ANISOU 1671  C   GLY A1012     7960   9658   5555   -568   -140    963       C  
ATOM   1672  O   GLY A1012     -17.754  27.915 -45.770  1.00 61.14           O  
ANISOU 1672  O   GLY A1012     7890   9950   5392   -439     46   1088       O  
ATOM   1673  N   LEU A1013     -18.983  26.023 -45.511  1.00 57.70           N  
ANISOU 1673  N   LEU A1013     7572   8893   5457   -563   -176    989       N  
ATOM   1674  CA  LEU A1013     -17.954  25.210 -44.845  1.00 57.43           C  
ANISOU 1674  CA  LEU A1013     7484   8779   5560   -367     18   1164       C  
ATOM   1675  C   LEU A1013     -17.397  24.154 -45.798  1.00 62.18           C  
ANISOU 1675  C   LEU A1013     8390   9064   6172   -102     34    898       C  
ATOM   1676  O   LEU A1013     -18.168  23.423 -46.418  1.00 62.44           O  
ANISOU 1676  O   LEU A1013     8653   8708   6365   -168   -194    643       O  
ATOM   1677  CB  LEU A1013     -18.547  24.543 -43.584  1.00 57.40           C  
ANISOU 1677  CB  LEU A1013     7280   8605   5925   -519    -12   1460       C  
ATOM   1678  CG  LEU A1013     -17.627  23.653 -42.737  1.00 61.93           C  
ANISOU 1678  CG  LEU A1013     7767   9084   6678   -330    165   1714       C  
ATOM   1679  CD1 LEU A1013     -16.847  24.464 -41.731  1.00 61.79           C  
ANISOU 1679  CD1 LEU A1013     7497   9516   6466   -266    330   1997       C  
ATOM   1680  CD2 LEU A1013     -18.431  22.611 -41.992  1.00 64.32           C  
ANISOU 1680  CD2 LEU A1013     7984   9037   7418   -474     80   1939       C  
ATOM   1681  N   ARG A1014     -16.063  24.072 -45.908  1.00 58.66           N  
ANISOU 1681  N   ARG A1014     7943   8781   5564    212    286    956       N  
ATOM   1682  CA  ARG A1014     -15.387  23.097 -46.763  1.00 58.38           C  
ANISOU 1682  CA  ARG A1014     8201   8496   5485    575    368    716       C  
ATOM   1683  C   ARG A1014     -14.420  22.252 -45.938  1.00 62.11           C  
ANISOU 1683  C   ARG A1014     8545   8873   6179    807    573    977       C  
ATOM   1684  O   ARG A1014     -13.498  22.784 -45.321  1.00 61.51           O  
ANISOU 1684  O   ARG A1014     8181   9177   6013    885    781   1283       O  
ATOM   1685  CB  ARG A1014     -14.663  23.787 -47.922  1.00 59.54           C  
ANISOU 1685  CB  ARG A1014     8469   8980   5171    837    526    556       C  
ATOM   1686  CG  ARG A1014     -15.582  24.282 -49.029  1.00 74.32           C  
ANISOU 1686  CG  ARG A1014    10588  10857   6794    723    303    227       C  
ATOM   1687  CD  ARG A1014     -15.811  25.777 -48.950  1.00 88.49           C  
ANISOU 1687  CD  ARG A1014    12144  13084   8394    482    309    412       C  
ATOM   1688  NE  ARG A1014     -16.236  26.327 -50.237  1.00103.09           N  
ANISOU 1688  NE  ARG A1014    14226  15062   9880    532    206    155       N  
ATOM   1689  CZ  ARG A1014     -16.432  27.621 -50.473  1.00119.06           C  
ANISOU 1689  CZ  ARG A1014    16116  17426  11697    382    204    282       C  
ATOM   1690  NH1 ARG A1014     -16.815  28.030 -51.676  1.00106.65           N  
ANISOU 1690  NH1 ARG A1014    14768  15973   9781    463    112     74       N  
ATOM   1691  NH2 ARG A1014     -16.248  28.516 -49.508  1.00104.04           N  
ANISOU 1691  NH2 ARG A1014    13877  15733   9922    168    272    610       N  
ATOM   1692  N   LEU A1015     -14.648  20.939 -45.911  1.00 58.72           N  
ANISOU 1692  N   LEU A1015     8322   7915   6073    901    479    870       N  
ATOM   1693  CA  LEU A1015     -13.829  20.011 -45.141  1.00 58.80           C  
ANISOU 1693  CA  LEU A1015     8237   7761   6344   1139    651   1132       C  
ATOM   1694  C   LEU A1015     -12.478  19.688 -45.800  1.00 65.27           C  
ANISOU 1694  C   LEU A1015     9172   8684   6944   1670    931   1048       C  
ATOM   1695  O   LEU A1015     -11.551  19.260 -45.108  1.00 65.92           O  
ANISOU 1695  O   LEU A1015     9060   8827   7159   1901   1135   1355       O  
ATOM   1696  CB  LEU A1015     -14.621  18.725 -44.814  1.00 58.50           C  
ANISOU 1696  CB  LEU A1015     8362   7057   6807   1023    431   1105       C  
ATOM   1697  CG  LEU A1015     -15.801  18.806 -43.814  1.00 62.35           C  
ANISOU 1697  CG  LEU A1015     8605   7462   7623    553    243   1393       C  
ATOM   1698  CD1 LEU A1015     -15.538  19.785 -42.661  1.00 61.97           C  
ANISOU 1698  CD1 LEU A1015     8135   7992   7418    432    414   1822       C  
ATOM   1699  CD2 LEU A1015     -17.118  19.108 -44.511  1.00 64.18           C  
ANISOU 1699  CD2 LEU A1015     8978   7536   7872    217    -76   1097       C  
ATOM   1700  N   LYS A1016     -12.360  19.908 -47.121  1.00 62.47           N  
ANISOU 1700  N   LYS A1016     9112   8394   6231   1894    954    668       N  
ATOM   1701  CA  LYS A1016     -11.140  19.647 -47.896  1.00 62.53           C  
ANISOU 1701  CA  LYS A1016     9242   8561   5957   2464   1261    581       C  
ATOM   1702  C   LYS A1016     -10.489  20.971 -48.352  1.00 65.79           C  
ANISOU 1702  C   LYS A1016     9406   9656   5936   2504   1485    740       C  
ATOM   1703  O   LYS A1016     -11.204  21.966 -48.548  1.00 66.39           O  
ANISOU 1703  O   LYS A1016     9433   9934   5859   2146   1328    695       O  
ATOM   1704  CB  LYS A1016     -11.492  18.766 -49.110  1.00 65.55           C  
ANISOU 1704  CB  LYS A1016    10208   8473   6224   2776   1121     15       C  
ATOM   1705  CG  LYS A1016     -10.336  17.941 -49.658  1.00 84.56           C  
ANISOU 1705  CG  LYS A1016    12825  10814   8490   3470   1425    -91       C  
ATOM   1706  CD  LYS A1016     -10.818  16.970 -50.738  1.00 96.30           C  
ANISOU 1706  CD  LYS A1016    14974  11723   9891   3780   1201   -725       C  
ATOM   1707  CE  LYS A1016      -9.719  16.085 -51.276  1.00107.35           C  
ANISOU 1707  CE  LYS A1016    16637  13025  11126   4553   1515   -873       C  
ATOM   1708  NZ  LYS A1016      -8.880  16.784 -52.285  1.00116.65           N  
ANISOU 1708  NZ  LYS A1016    17787  14873  11661   5017   1899   -876       N  
ATOM   1709  N   ILE A1017      -9.140  20.978 -48.523  1.00 60.00           N  
ANISOU 1709  N   ILE A1017     8489   9266   5042   2939   1851    965       N  
ATOM   1710  CA  ILE A1017      -8.365  22.149 -48.984  1.00 58.76           C  
ANISOU 1710  CA  ILE A1017     8039   9745   4543   3005   2095   1209       C  
ATOM   1711  C   ILE A1017      -8.866  22.611 -50.357  1.00 59.53           C  
ANISOU 1711  C   ILE A1017     8476   9941   4204   3089   2061    852       C  
ATOM   1712  O   ILE A1017      -9.024  21.788 -51.249  1.00 58.44           O  
ANISOU 1712  O   ILE A1017     8801   9521   3884   3462   2052    435       O  
ATOM   1713  CB  ILE A1017      -6.820  21.892 -48.984  1.00 61.87           C  
ANISOU 1713  CB  ILE A1017     8148  10468   4893   3511   2507   1552       C  
ATOM   1714  CG1 ILE A1017      -6.318  21.438 -47.586  1.00 62.37           C  
ANISOU 1714  CG1 ILE A1017     7864  10456   5377   3436   2502   1928       C  
ATOM   1715  CG2 ILE A1017      -6.039  23.125 -49.486  1.00 62.06           C  
ANISOU 1715  CG2 ILE A1017     7802  11146   4630   3526   2747   1885       C  
ATOM   1716  CD1 ILE A1017      -4.801  21.010 -47.497  1.00 66.42           C  
ANISOU 1716  CD1 ILE A1017     8060  11257   5921   3964   2882   2298       C  
ATOM   1717  N   TYR A1018      -9.147  23.913 -50.498  1.00 55.63           N  
ANISOU 1717  N   TYR A1018     7776   9817   3544   2749   2008   1005       N  
ATOM   1718  CA  TYR A1018      -9.621  24.543 -51.734  1.00 55.78           C  
ANISOU 1718  CA  TYR A1018     8047  10013   3135   2789   1973    768       C  
ATOM   1719  C   TYR A1018      -8.881  25.861 -51.997  1.00 62.45           C  
ANISOU 1719  C   TYR A1018     8497  11456   3775   2738   2209   1200       C  
ATOM   1720  O   TYR A1018      -8.249  26.399 -51.088  1.00 63.56           O  
ANISOU 1720  O   TYR A1018     8175  11803   4172   2522   2274   1628       O  
ATOM   1721  CB  TYR A1018     -11.146  24.783 -51.674  1.00 56.40           C  
ANISOU 1721  CB  TYR A1018     8341   9787   3300   2317   1537    471       C  
ATOM   1722  CG  TYR A1018     -11.598  25.807 -50.649  1.00 57.67           C  
ANISOU 1722  CG  TYR A1018     8128  10072   3711   1765   1375    771       C  
ATOM   1723  CD1 TYR A1018     -11.752  25.460 -49.308  1.00 59.07           C  
ANISOU 1723  CD1 TYR A1018     8101  10038   4304   1515   1266    936       C  
ATOM   1724  CD2 TYR A1018     -11.940  27.102 -51.030  1.00 58.22           C  
ANISOU 1724  CD2 TYR A1018     8090  10447   3582   1524   1317    873       C  
ATOM   1725  CE1 TYR A1018     -12.173  26.393 -48.363  1.00 58.92           C  
ANISOU 1725  CE1 TYR A1018     7793  10148   4444   1083   1120   1168       C  
ATOM   1726  CE2 TYR A1018     -12.377  28.041 -50.095  1.00 58.92           C  
ANISOU 1726  CE2 TYR A1018     7896  10605   3886   1072   1152   1095       C  
ATOM   1727  CZ  TYR A1018     -12.489  27.681 -48.761  1.00 65.87           C  
ANISOU 1727  CZ  TYR A1018     8598  11302   5129    870   1055   1219       C  
ATOM   1728  OH  TYR A1018     -12.921  28.597 -47.829  1.00 66.41           O  
ANISOU 1728  OH  TYR A1018     8435  11455   5341    497    897   1397       O  
ATOM   1729  N   LYS A1019      -8.971  26.388 -53.224  1.00 59.16           N  
ANISOU 1729  N   LYS A1019     8260  11306   2911   2924   2306   1104       N  
ATOM   1730  CA  LYS A1019      -8.365  27.672 -53.558  1.00 58.89           C  
ANISOU 1730  CA  LYS A1019     7858  11801   2715   2843   2511   1555       C  
ATOM   1731  C   LYS A1019      -9.427  28.774 -53.450  1.00 62.35           C  
ANISOU 1731  C   LYS A1019     8289  12204   3195   2300   2178   1531       C  
ATOM   1732  O   LYS A1019     -10.547  28.586 -53.931  1.00 61.69           O  
ANISOU 1732  O   LYS A1019     8598  11878   2965   2225   1911   1116       O  
ATOM   1733  CB  LYS A1019      -7.751  27.644 -54.968  1.00 61.23           C  
ANISOU 1733  CB  LYS A1019     8314  12481   2469   3424   2877   1570       C  
ATOM   1734  CG  LYS A1019      -6.391  26.945 -55.050  1.00 73.36           C  
ANISOU 1734  CG  LYS A1019     9665  14246   3962   3996   3328   1812       C  
ATOM   1735  CD  LYS A1019      -5.803  27.045 -56.453  1.00 83.95           C  
ANISOU 1735  CD  LYS A1019    11131  16061   4706   4608   3740   1889       C  
ATOM   1736  CE  LYS A1019      -4.469  26.343 -56.598  1.00 96.42           C  
ANISOU 1736  CE  LYS A1019    12516  17914   6207   5259   4236   2147       C  
ATOM   1737  NZ  LYS A1019      -3.881  26.534 -57.961  1.00103.43           N  
ANISOU 1737  NZ  LYS A1019    13485  19354   6461   5897   4693   2293       N  
ATOM   1738  N   ASP A1020      -9.083  29.913 -52.807  1.00 58.56           N  
ANISOU 1738  N   ASP A1020     7367  11942   2942   1928   2163   1969       N  
ATOM   1739  CA  ASP A1020      -9.985  31.065 -52.677  1.00 57.80           C  
ANISOU 1739  CA  ASP A1020     7247  11817   2897   1463   1876   1986       C  
ATOM   1740  C   ASP A1020      -9.979  31.942 -53.966  1.00 62.05           C  
ANISOU 1740  C   ASP A1020     7843  12692   3043   1585   2009   2124       C  
ATOM   1741  O   ASP A1020      -9.427  31.522 -54.989  1.00 59.92           O  
ANISOU 1741  O   ASP A1020     7698  12667   2399   2060   2311   2131       O  
ATOM   1742  CB  ASP A1020      -9.709  31.878 -51.378  1.00 58.55           C  
ANISOU 1742  CB  ASP A1020     6927  11913   3408   1024   1731   2316       C  
ATOM   1743  CG  ASP A1020      -8.325  32.494 -51.202  1.00 62.91           C  
ANISOU 1743  CG  ASP A1020     7000  12811   4093   1036   1955   2854       C  
ATOM   1744  OD1 ASP A1020      -7.751  32.358 -50.108  1.00 61.91           O  
ANISOU 1744  OD1 ASP A1020     6591  12654   4277    918   1907   3029       O  
ATOM   1745  OD2 ASP A1020      -7.847  33.156 -52.132  1.00 70.51           O  
ANISOU 1745  OD2 ASP A1020     7843  14082   4865   1136   2152   3134       O  
ATOM   1746  N   THR A1021     -10.610  33.141 -53.909  1.00 61.22           N  
ANISOU 1746  N   THR A1021     7661  12599   3001   1198   1793   2243       N  
ATOM   1747  CA  THR A1021     -10.704  34.098 -55.026  1.00 61.85           C  
ANISOU 1747  CA  THR A1021     7769  12971   2760   1253   1879   2442       C  
ATOM   1748  C   THR A1021      -9.336  34.661 -55.403  1.00 68.00           C  
ANISOU 1748  C   THR A1021     8150  14178   3510   1418   2263   3032       C  
ATOM   1749  O   THR A1021      -9.090  34.905 -56.588  1.00 68.37           O  
ANISOU 1749  O   THR A1021     8267  14564   3145   1737   2517   3197       O  
ATOM   1750  CB  THR A1021     -11.754  35.198 -54.759  1.00 69.11           C  
ANISOU 1750  CB  THR A1021     8698  13734   3827    807   1536   2436       C  
ATOM   1751  OG1 THR A1021     -11.599  35.724 -53.438  1.00 70.49           O  
ANISOU 1751  OG1 THR A1021     8569  13741   4473    414   1372   2611       O  
ATOM   1752  CG2 THR A1021     -13.180  34.705 -54.959  1.00 66.17           C  
ANISOU 1752  CG2 THR A1021     8730  13086   3326    763   1223   1917       C  
ATOM   1753  N   GLU A1022      -8.440  34.828 -54.404  1.00 65.56           N  
ANISOU 1753  N   GLU A1022     7408  13877   3624   1220   2302   3369       N  
ATOM   1754  CA  GLU A1022      -7.064  35.298 -54.585  1.00 65.86           C  
ANISOU 1754  CA  GLU A1022     6958  14301   3764   1313   2628   3992       C  
ATOM   1755  C   GLU A1022      -6.131  34.172 -55.104  1.00 69.99           C  
ANISOU 1755  C   GLU A1022     7461  15096   4033   1915   3066   4037       C  
ATOM   1756  O   GLU A1022      -5.038  34.458 -55.601  1.00 70.42           O  
ANISOU 1756  O   GLU A1022     7135  15576   4044   2134   3435   4577       O  
ATOM   1757  CB  GLU A1022      -6.521  35.911 -53.281  1.00 67.59           C  
ANISOU 1757  CB  GLU A1022     6733  14397   4550    848   2409   4291       C  
ATOM   1758  CG  GLU A1022      -6.420  37.428 -53.312  1.00 84.04           C  
ANISOU 1758  CG  GLU A1022     8540  16518   6874    425   2251   4718       C  
ATOM   1759  CD  GLU A1022      -5.126  37.989 -53.884  1.00118.92           C  
ANISOU 1759  CD  GLU A1022    12444  21353  11388    500   2576   5438       C  
ATOM   1760  OE1 GLU A1022      -4.155  38.150 -53.109  1.00114.50           O  
ANISOU 1760  OE1 GLU A1022    11416  20838  11252    293   2525   5797       O  
ATOM   1761  OE2 GLU A1022      -5.087  38.289 -55.102  1.00116.04           O  
ANISOU 1761  OE2 GLU A1022    12120  21291  10678    762   2872   5677       O  
ATOM   1762  N   GLY A1023      -6.580  32.921 -54.995  1.00 65.89           N  
ANISOU 1762  N   GLY A1023     7341  14322   3374   2186   3022   3497       N  
ATOM   1763  CA  GLY A1023      -5.843  31.749 -55.458  1.00 65.43           C  
ANISOU 1763  CA  GLY A1023     7376  14418   3068   2809   3393   3422       C  
ATOM   1764  C   GLY A1023      -5.060  31.010 -54.393  1.00 69.00           C  
ANISOU 1764  C   GLY A1023     7541  14765   3910   2846   3446   3534       C  
ATOM   1765  O   GLY A1023      -4.378  30.030 -54.709  1.00 69.78           O  
ANISOU 1765  O   GLY A1023     7686  14979   3848   3397   3771   3508       O  
ATOM   1766  N   TYR A1024      -5.148  31.468 -53.130  1.00 63.75           N  
ANISOU 1766  N   TYR A1024     6597  13894   3731   2304   3127   3656       N  
ATOM   1767  CA  TYR A1024      -4.446  30.856 -52.005  1.00 63.01           C  
ANISOU 1767  CA  TYR A1024     6212  13719   4010   2292   3116   3794       C  
ATOM   1768  C   TYR A1024      -5.246  29.698 -51.394  1.00 65.52           C  
ANISOU 1768  C   TYR A1024     6943  13556   4397   2334   2901   3256       C  
ATOM   1769  O   TYR A1024      -6.484  29.728 -51.374  1.00 64.48           O  
ANISOU 1769  O   TYR A1024     7187  13101   4210   2094   2603   2846       O  
ATOM   1770  CB  TYR A1024      -4.153  31.888 -50.908  1.00 64.67           C  
ANISOU 1770  CB  TYR A1024     5956  13950   4665   1719   2834   4163       C  
ATOM   1771  CG  TYR A1024      -3.515  33.188 -51.346  1.00 67.16           C  
ANISOU 1771  CG  TYR A1024     5849  14611   5058   1502   2909   4709       C  
ATOM   1772  CD1 TYR A1024      -2.311  33.197 -52.046  1.00 69.22           C  
ANISOU 1772  CD1 TYR A1024     5711  15335   5255   1846   3341   5231       C  
ATOM   1773  CD2 TYR A1024      -4.046  34.411 -50.950  1.00 68.48           C  
ANISOU 1773  CD2 TYR A1024     5962  14629   5428    947   2541   4761       C  
ATOM   1774  CE1 TYR A1024      -1.692  34.394 -52.405  1.00 70.37           C  
ANISOU 1774  CE1 TYR A1024     5399  15783   5555   1600   3401   5828       C  
ATOM   1775  CE2 TYR A1024      -3.432  35.613 -51.294  1.00 69.80           C  
ANISOU 1775  CE2 TYR A1024     5726  15037   5758    703   2565   5300       C  
ATOM   1776  CZ  TYR A1024      -2.259  35.602 -52.028  1.00 77.82           C  
ANISOU 1776  CZ  TYR A1024     6323  16507   6736   1005   2991   5856       C  
ATOM   1777  OH  TYR A1024      -1.670  36.795 -52.366  1.00 80.25           O  
ANISOU 1777  OH  TYR A1024     6193  17031   7268    723   3004   6458       O  
ATOM   1778  N   TYR A1025      -4.525  28.695 -50.860  1.00 61.18           N  
ANISOU 1778  N   TYR A1025     6276  12959   4011   2626   3047   3318       N  
ATOM   1779  CA  TYR A1025      -5.122  27.521 -50.227  1.00 60.45           C  
ANISOU 1779  CA  TYR A1025     6513  12398   4056   2688   2876   2918       C  
ATOM   1780  C   TYR A1025      -5.817  27.863 -48.900  1.00 61.48           C  
ANISOU 1780  C   TYR A1025     6558  12277   4526   2124   2468   2891       C  
ATOM   1781  O   TYR A1025      -5.234  28.474 -47.996  1.00 59.82           O  
ANISOU 1781  O   TYR A1025     5919  12246   4565   1856   2375   3256       O  
ATOM   1782  CB  TYR A1025      -4.107  26.380 -50.078  1.00 62.18           C  
ANISOU 1782  CB  TYR A1025     6628  12642   4355   3212   3173   3041       C  
ATOM   1783  CG  TYR A1025      -3.613  25.824 -51.396  1.00 64.73           C  
ANISOU 1783  CG  TYR A1025     7176  13142   4275   3884   3579   2938       C  
ATOM   1784  CD1 TYR A1025      -4.400  24.957 -52.149  1.00 66.95           C  
ANISOU 1784  CD1 TYR A1025     8098  13060   4282   4189   3530   2350       C  
ATOM   1785  CD2 TYR A1025      -2.347  26.141 -51.878  1.00 65.71           C  
ANISOU 1785  CD2 TYR A1025     6869  13806   4291   4240   4001   3435       C  
ATOM   1786  CE1 TYR A1025      -3.951  24.441 -53.361  1.00 68.16           C  
ANISOU 1786  CE1 TYR A1025     8525  13382   3992   4873   3885   2198       C  
ATOM   1787  CE2 TYR A1025      -1.884  25.626 -53.087  1.00 67.05           C  
ANISOU 1787  CE2 TYR A1025     7255  14197   4025   4943   4422   3354       C  
ATOM   1788  CZ  TYR A1025      -2.691  24.778 -53.828  1.00 75.56           C  
ANISOU 1788  CZ  TYR A1025     9040  14904   4764   5282   4361   2702       C  
ATOM   1789  OH  TYR A1025      -2.247  24.284 -55.032  1.00 76.28           O  
ANISOU 1789  OH  TYR A1025     9410  15222   4350   6033   4757   2566       O  
ATOM   1790  N   THR A1026      -7.088  27.473 -48.824  1.00 56.65           N  
ANISOU 1790  N   THR A1026     6361  11262   3902   1966   2214   2455       N  
ATOM   1791  CA  THR A1026      -8.008  27.742 -47.730  1.00 55.93           C  
ANISOU 1791  CA  THR A1026     6274  10932   4046   1501   1861   2373       C  
ATOM   1792  C   THR A1026      -8.713  26.437 -47.280  1.00 59.04           C  
ANISOU 1792  C   THR A1026     6966  10863   4604   1582   1748   2083       C  
ATOM   1793  O   THR A1026      -8.696  25.444 -48.009  1.00 59.35           O  
ANISOU 1793  O   THR A1026     7306  10691   4551   1949   1871   1836       O  
ATOM   1794  CB  THR A1026      -8.992  28.833 -48.226  1.00 60.45           C  
ANISOU 1794  CB  THR A1026     6987  11525   4456   1175   1662   2220       C  
ATOM   1795  OG1 THR A1026      -8.261  29.879 -48.857  1.00 53.67           O  
ANISOU 1795  OG1 THR A1026     5889  11049   3455   1177   1814   2515       O  
ATOM   1796  CG2 THR A1026      -9.813  29.444 -47.125  1.00 61.52           C  
ANISOU 1796  CG2 THR A1026     7049  11537   4788    725   1345   2217       C  
ATOM   1797  N   ILE A1027      -9.317  26.452 -46.075  1.00 54.17           N  
ANISOU 1797  N   ILE A1027     6265  10086   4233   1255   1512   2132       N  
ATOM   1798  CA  ILE A1027     -10.088  25.349 -45.476  1.00 53.44           C  
ANISOU 1798  CA  ILE A1027     6372   9565   4369   1234   1381   1974       C  
ATOM   1799  C   ILE A1027     -11.159  25.900 -44.508  1.00 56.01           C  
ANISOU 1799  C   ILE A1027     6634   9833   4815    801   1111   1997       C  
ATOM   1800  O   ILE A1027     -10.985  26.993 -43.972  1.00 55.41           O  
ANISOU 1800  O   ILE A1027     6322  10048   4683    584   1038   2179       O  
ATOM   1801  CB  ILE A1027      -9.170  24.263 -44.845  1.00 56.46           C  
ANISOU 1801  CB  ILE A1027     6628   9861   4963   1541   1544   2187       C  
ATOM   1802  CG1 ILE A1027      -9.895  22.910 -44.750  1.00 56.62           C  
ANISOU 1802  CG1 ILE A1027     6963   9334   5216   1633   1457   1971       C  
ATOM   1803  CG2 ILE A1027      -8.556  24.708 -43.499  1.00 57.13           C  
ANISOU 1803  CG2 ILE A1027     6295  10225   5187   1383   1500   2597       C  
ATOM   1804  CD1 ILE A1027      -9.045  21.732 -45.026  1.00 64.22           C  
ANISOU 1804  CD1 ILE A1027     8031  10100   6271   2117   1670   1972       C  
ATOM   1805  N   GLY A1028     -12.255  25.162 -44.333  1.00 52.00           N  
ANISOU 1805  N   GLY A1028     6338   8947   4475    695    959   1818       N  
ATOM   1806  CA  GLY A1028     -13.357  25.537 -43.452  1.00 51.61           C  
ANISOU 1806  CA  GLY A1028     6219   8852   4539    353    753   1870       C  
ATOM   1807  C   GLY A1028     -14.128  26.747 -43.937  1.00 54.58           C  
ANISOU 1807  C   GLY A1028     6636   9385   4718    113    615   1724       C  
ATOM   1808  O   GLY A1028     -14.588  26.778 -45.085  1.00 54.06           O  
ANISOU 1808  O   GLY A1028     6798   9217   4524    133    565   1454       O  
ATOM   1809  N   ILE A1029     -14.260  27.757 -43.063  1.00 50.03           N  
ANISOU 1809  N   ILE A1029     5856   9055   4096    -84    537   1893       N  
ATOM   1810  CA  ILE A1029     -14.953  29.003 -43.387  1.00 48.98           C  
ANISOU 1810  CA  ILE A1029     5747   9061   3802   -289    404   1791       C  
ATOM   1811  C   ILE A1029     -13.940  30.132 -43.605  1.00 52.78           C  
ANISOU 1811  C   ILE A1029     6086   9846   4122   -289    450   1910       C  
ATOM   1812  O   ILE A1029     -13.710  30.951 -42.709  1.00 53.62           O  
ANISOU 1812  O   ILE A1029     6026  10121   4225   -412    356   2056       O  
ATOM   1813  CB  ILE A1029     -16.055  29.373 -42.358  1.00 51.42           C  
ANISOU 1813  CB  ILE A1029     5988   9371   4179   -487    257   1847       C  
ATOM   1814  CG1 ILE A1029     -16.882  28.148 -41.942  1.00 51.24           C  
ANISOU 1814  CG1 ILE A1029     5998   9067   4403   -501    239   1875       C  
ATOM   1815  CG2 ILE A1029     -16.935  30.507 -42.898  1.00 51.68           C  
ANISOU 1815  CG2 ILE A1029     6094   9472   4072   -646    122   1699       C  
ATOM   1816  CD1 ILE A1029     -18.095  28.447 -41.119  1.00 56.51           C  
ANISOU 1816  CD1 ILE A1029     6572   9767   5132   -659    144   1970       C  
ATOM   1817  N   GLY A1030     -13.339  30.153 -44.786  1.00 48.01           N  
ANISOU 1817  N   GLY A1030     5551   9303   3388   -140    582   1858       N  
ATOM   1818  CA  GLY A1030     -12.368  31.172 -45.164  1.00 47.70           C  
ANISOU 1818  CA  GLY A1030     5336   9544   3242   -148    652   2042       C  
ATOM   1819  C   GLY A1030     -11.103  31.227 -44.332  1.00 51.04           C  
ANISOU 1819  C   GLY A1030     5450  10158   3787   -112    709   2346       C  
ATOM   1820  O   GLY A1030     -10.566  32.315 -44.121  1.00 51.15           O  
ANISOU 1820  O   GLY A1030     5262  10358   3813   -271    623   2529       O  
ATOM   1821  N   HIS A1031     -10.607  30.072 -43.863  1.00 47.40           N  
ANISOU 1821  N   HIS A1031     4936   9632   3441     90    823   2419       N  
ATOM   1822  CA  HIS A1031      -9.376  30.037 -43.071  1.00 47.85           C  
ANISOU 1822  CA  HIS A1031     4667   9896   3616    151    860   2734       C  
ATOM   1823  C   HIS A1031      -8.146  29.866 -43.967  1.00 53.80           C  
ANISOU 1823  C   HIS A1031     5251  10852   4340    412   1129   2927       C  
ATOM   1824  O   HIS A1031      -7.941  28.782 -44.526  1.00 53.74           O  
ANISOU 1824  O   HIS A1031     5373  10739   4307    745   1352   2851       O  
ATOM   1825  CB  HIS A1031      -9.430  28.977 -41.946  1.00 48.24           C  
ANISOU 1825  CB  HIS A1031     4696   9822   3813    249    842   2800       C  
ATOM   1826  CG  HIS A1031      -8.183  28.932 -41.125  1.00 51.42           C  
ANISOU 1826  CG  HIS A1031     4755  10464   4317    323    841   3132       C  
ATOM   1827  ND1 HIS A1031      -7.977  29.820 -40.089  1.00 53.19           N  
ANISOU 1827  ND1 HIS A1031     4794  10875   4542     93    580   3260       N  
ATOM   1828  CD2 HIS A1031      -7.090  28.144 -41.251  1.00 53.11           C  
ANISOU 1828  CD2 HIS A1031     4785  10769   4626    617   1046   3349       C  
ATOM   1829  CE1 HIS A1031      -6.781  29.532 -39.602  1.00 52.62           C  
ANISOU 1829  CE1 HIS A1031     4413  11007   4576    216    601   3559       C  
ATOM   1830  NE2 HIS A1031      -6.209  28.531 -40.270  1.00 52.91           N  
ANISOU 1830  NE2 HIS A1031     4414  11006   4682    538    899   3647       N  
ATOM   1831  N   LEU A1032      -7.325  30.935 -44.090  1.00 51.35           N  
ANISOU 1831  N   LEU A1032     4643  10820   4048    276   1103   3194       N  
ATOM   1832  CA  LEU A1032      -6.101  30.931 -44.904  1.00 51.58           C  
ANISOU 1832  CA  LEU A1032     4408  11124   4065    512   1385   3489       C  
ATOM   1833  C   LEU A1032      -5.027  30.059 -44.249  1.00 58.39           C  
ANISOU 1833  C   LEU A1032     4983  12108   5093    756   1507   3754       C  
ATOM   1834  O   LEU A1032      -4.731  30.222 -43.051  1.00 57.32           O  
ANISOU 1834  O   LEU A1032     4629  12021   5127    573   1273   3908       O  
ATOM   1835  CB  LEU A1032      -5.584  32.360 -45.123  1.00 51.21           C  
ANISOU 1835  CB  LEU A1032     4067  11310   4079    228   1283   3776       C  
ATOM   1836  CG  LEU A1032      -4.588  32.538 -46.247  1.00 56.18           C  
ANISOU 1836  CG  LEU A1032     4441  12251   4654    455   1619   4114       C  
ATOM   1837  CD1 LEU A1032      -5.275  32.928 -47.519  1.00 56.61           C  
ANISOU 1837  CD1 LEU A1032     4785  12294   4431    517   1753   3950       C  
ATOM   1838  CD2 LEU A1032      -3.583  33.604 -45.907  1.00 60.19           C  
ANISOU 1838  CD2 LEU A1032     4438  13004   5427    168   1482   4589       C  
ATOM   1839  N   LEU A1033      -4.474  29.105 -45.033  1.00 57.12           N  
ANISOU 1839  N   LEU A1033     4853  11995   4855   1213   1866   3788       N  
ATOM   1840  CA  LEU A1033      -3.423  28.185 -44.568  1.00 57.37           C  
ANISOU 1840  CA  LEU A1033     4619  12140   5041   1542   2040   4056       C  
ATOM   1841  C   LEU A1033      -2.053  28.767 -44.882  1.00 60.83           C  
ANISOU 1841  C   LEU A1033     4522  13026   5563   1619   2214   4555       C  
ATOM   1842  O   LEU A1033      -1.218  28.904 -43.989  1.00 60.40           O  
ANISOU 1842  O   LEU A1033     4041  13164   5743   1518   2083   4904       O  
ATOM   1843  CB  LEU A1033      -3.581  26.770 -45.172  1.00 57.52           C  
ANISOU 1843  CB  LEU A1033     4988  11907   4959   2046   2319   3803       C  
ATOM   1844  CG  LEU A1033      -4.874  26.011 -44.814  1.00 62.64           C  
ANISOU 1844  CG  LEU A1033     6105  12065   5630   1962   2130   3380       C  
ATOM   1845  CD1 LEU A1033      -5.191  24.944 -45.836  1.00 62.57           C  
ANISOU 1845  CD1 LEU A1033     6532  11763   5480   2383   2335   3033       C  
ATOM   1846  CD2 LEU A1033      -4.806  25.407 -43.424  1.00 66.43           C  
ANISOU 1846  CD2 LEU A1033     6452  12424   6364   1902   1978   3535       C  
ATOM   1847  N   THR A1034      -1.843  29.135 -46.146  1.00 58.28           N  
ANISOU 1847  N   THR A1034     4202  12893   5047   1790   2492   4621       N  
ATOM   1848  CA  THR A1034      -0.611  29.738 -46.652  1.00 59.23           C  
ANISOU 1848  CA  THR A1034     3788  13475   5242   1875   2722   5163       C  
ATOM   1849  C   THR A1034      -0.866  30.532 -47.923  1.00 65.96           C  
ANISOU 1849  C   THR A1034     4744  14475   5843   1870   2899   5180       C  
ATOM   1850  O   THR A1034      -1.844  30.277 -48.629  1.00 65.02           O  
ANISOU 1850  O   THR A1034     5149  14137   5417   1996   2947   4737       O  
ATOM   1851  CB  THR A1034       0.527  28.694 -46.827  1.00 65.17           C  
ANISOU 1851  CB  THR A1034     4268  14464   6029   2460   3122   5454       C  
ATOM   1852  OG1 THR A1034       1.749  29.375 -47.135  1.00 63.98           O  
ANISOU 1852  OG1 THR A1034     3472  14806   6031   2466   3303   6084       O  
ATOM   1853  CG2 THR A1034       0.220  27.635 -47.893  1.00 62.53           C  
ANISOU 1853  CG2 THR A1034     4413  14003   5344   3078   3515   5104       C  
ATOM   1854  N   LYS A1035       0.032  31.484 -48.214  1.00 65.24           N  
ANISOU 1854  N   LYS A1035     4126  14761   5901   1719   2979   5731       N  
ATOM   1855  CA  LYS A1035      -0.005  32.294 -49.427  1.00 66.12           C  
ANISOU 1855  CA  LYS A1035     4223  15094   5804   1736   3196   5915       C  
ATOM   1856  C   LYS A1035       0.940  31.685 -50.477  1.00 75.01           C  
ANISOU 1856  C   LYS A1035     5151  16653   6697   2395   3797   6243       C  
ATOM   1857  O   LYS A1035       0.991  32.153 -51.622  1.00 75.88           O  
ANISOU 1857  O   LYS A1035     5272  17029   6531   2573   4091   6423       O  
ATOM   1858  CB  LYS A1035       0.360  33.757 -49.120  1.00 67.59           C  
ANISOU 1858  CB  LYS A1035     3953  15389   6341   1143   2903   6366       C  
ATOM   1859  CG  LYS A1035      -0.779  34.556 -48.509  1.00 74.42           C  
ANISOU 1859  CG  LYS A1035     5157  15839   7282    596   2385   5977       C  
ATOM   1860  CD  LYS A1035      -0.419  36.027 -48.395  1.00 80.08           C  
ANISOU 1860  CD  LYS A1035     5489  16604   8333     65   2107   6400       C  
ATOM   1861  CE  LYS A1035      -1.498  36.802 -47.684  1.00 92.18           C  
ANISOU 1861  CE  LYS A1035     7365  17710   9949   -414   1584   5995       C  
ATOM   1862  NZ  LYS A1035      -1.369  36.711 -46.203  1.00 97.14           N  
ANISOU 1862  NZ  LYS A1035     7871  18181  10857   -684   1151   5898       N  
ATOM   1863  N   SER A1036       1.675  30.624 -50.083  1.00 74.36           N  
ANISOU 1863  N   SER A1036     4899  16654   6700   2805   3996   6329       N  
ATOM   1864  CA  SER A1036       2.634  29.911 -50.929  1.00 75.62           C  
ANISOU 1864  CA  SER A1036     4861  17220   6651   3527   4586   6628       C  
ATOM   1865  C   SER A1036       1.917  29.087 -52.010  1.00 82.13           C  
ANISOU 1865  C   SER A1036     6398  17900   6909   4109   4874   6063       C  
ATOM   1866  O   SER A1036       0.885  28.472 -51.710  1.00 80.96           O  
ANISOU 1866  O   SER A1036     6839  17245   6676   4049   4602   5420       O  
ATOM   1867  CB  SER A1036       3.551  29.027 -50.084  1.00 79.53           C  
ANISOU 1867  CB  SER A1036     4999  17781   7437   3786   4653   6849       C  
ATOM   1868  OG  SER A1036       4.544  29.780 -49.406  1.00 88.90           O  
ANISOU 1868  OG  SER A1036     5419  19260   9100   3377   4471   7496       O  
ATOM   1869  N   PRO A1037       2.440  29.065 -53.270  1.00 81.90           N  
ANISOU 1869  N   PRO A1037     6322  18316   6481   4683   5405   6301       N  
ATOM   1870  CA  PRO A1037       1.771  28.290 -54.329  1.00 82.58           C  
ANISOU 1870  CA  PRO A1037     7140  18268   5970   5272   5626   5709       C  
ATOM   1871  C   PRO A1037       2.136  26.797 -54.295  1.00 88.29           C  
ANISOU 1871  C   PRO A1037     8125  18836   6585   5984   5874   5412       C  
ATOM   1872  O   PRO A1037       2.708  26.281 -55.263  1.00 88.79           O  
ANISOU 1872  O   PRO A1037     8274  19231   6234   6760   6387   5473       O  
ATOM   1873  CB  PRO A1037       2.248  28.989 -55.607  1.00 84.28           C  
ANISOU 1873  CB  PRO A1037     7165  19026   5830   5603   6001   6148       C  
ATOM   1874  CG  PRO A1037       3.606  29.511 -55.272  1.00 88.16           C  
ANISOU 1874  CG  PRO A1037     6749  20026   6720   5549   6245   7044       C  
ATOM   1875  CD  PRO A1037       3.660  29.733 -53.788  1.00 83.58           C  
ANISOU 1875  CD  PRO A1037     5827  19146   6785   4846   5753   7130       C  
ATOM   1876  N   SER A1038       1.820  26.104 -53.172  1.00 84.59           N  
ANISOU 1876  N   SER A1038     7787  17869   6485   5755   5522   5117       N  
ATOM   1877  CA  SER A1038       2.133  24.684 -52.987  1.00 84.43           C  
ANISOU 1877  CA  SER A1038     8006  17598   6475   6361   5690   4863       C  
ATOM   1878  C   SER A1038       1.069  23.977 -52.180  1.00 88.22           C  
ANISOU 1878  C   SER A1038     9001  17354   7167   6047   5211   4264       C  
ATOM   1879  O   SER A1038       0.634  24.500 -51.152  1.00 88.29           O  
ANISOU 1879  O   SER A1038     8824  17183   7538   5354   4789   4332       O  
ATOM   1880  CB  SER A1038       3.494  24.521 -52.317  1.00 88.61           C  
ANISOU 1880  CB  SER A1038     7794  18494   7380   6542   5925   5533       C  
ATOM   1881  OG  SER A1038       3.835  23.159 -52.113  1.00 98.85           O  
ANISOU 1881  OG  SER A1038     9304  19536   8718   7156   6095   5331       O  
ATOM   1882  N   LEU A1039       0.652  22.783 -52.641  1.00 84.66           N  
ANISOU 1882  N   LEU A1039     9194  16479   6493   6571   5269   3690       N  
ATOM   1883  CA  LEU A1039      -0.361  21.970 -51.967  1.00 84.89           C  
ANISOU 1883  CA  LEU A1039     9716  15778   6758   6321   4840   3153       C  
ATOM   1884  C   LEU A1039       0.203  21.323 -50.689  1.00 89.59           C  
ANISOU 1884  C   LEU A1039     9970  16211   7857   6296   4781   3445       C  
ATOM   1885  O   LEU A1039      -0.482  21.303 -49.662  1.00 88.30           O  
ANISOU 1885  O   LEU A1039     9836  15681   8031   5753   4371   3357       O  
ATOM   1886  CB  LEU A1039      -0.948  20.915 -52.926  1.00 84.84           C  
ANISOU 1886  CB  LEU A1039    10512  15328   6397   6874   4870   2454       C  
ATOM   1887  CG  LEU A1039      -2.138  20.088 -52.414  1.00 89.55           C  
ANISOU 1887  CG  LEU A1039    11650  15118   7256   6572   4386   1887       C  
ATOM   1888  CD1 LEU A1039      -3.430  20.918 -52.361  1.00 89.69           C  
ANISOU 1888  CD1 LEU A1039    11832  14988   7258   5839   3943   1647       C  
ATOM   1889  CD2 LEU A1039      -2.333  18.843 -53.260  1.00 91.78           C  
ANISOU 1889  CD2 LEU A1039    12643  14934   7295   7249   4445   1281       C  
ATOM   1890  N   ASN A1040       1.458  20.820 -50.756  1.00 87.28           N  
ANISOU 1890  N   ASN A1040     9328  16239   7594   6911   5207   3834       N  
ATOM   1891  CA  ASN A1040       2.148  20.196 -49.622  1.00 87.22           C  
ANISOU 1891  CA  ASN A1040     8942  16163   8035   6983   5194   4188       C  
ATOM   1892  C   ASN A1040       2.457  21.199 -48.498  1.00 90.89           C  
ANISOU 1892  C   ASN A1040     8725  16951   8857   6283   4924   4729       C  
ATOM   1893  O   ASN A1040       2.443  20.820 -47.323  1.00 90.99           O  
ANISOU 1893  O   ASN A1040     8599  16742   9232   6055   4667   4847       O  
ATOM   1894  CB  ASN A1040       3.408  19.458 -50.082  1.00 87.91           C  
ANISOU 1894  CB  ASN A1040     8813  16553   8037   7871   5736   4479       C  
ATOM   1895  CG  ASN A1040       3.132  18.226 -50.913  1.00111.00           C  
ANISOU 1895  CG  ASN A1040    12484  19003  10687   8620   5922   3880       C  
ATOM   1896  OD1 ASN A1040       2.226  17.428 -50.636  1.00104.30           O  
ANISOU 1896  OD1 ASN A1040    12206  17432   9991   8519   5595   3364       O  
ATOM   1897  ND2 ASN A1040       3.929  18.027 -51.942  1.00105.07           N  
ANISOU 1897  ND2 ASN A1040    11742  18643   9536   9410   6445   3948       N  
ATOM   1898  N   ALA A1041       2.705  22.481 -48.862  1.00 86.09           N  
ANISOU 1898  N   ALA A1041     7728  16843   8140   5945   4954   5048       N  
ATOM   1899  CA  ALA A1041       2.964  23.572 -47.915  1.00 84.84           C  
ANISOU 1899  CA  ALA A1041     6979  16958   8299   5252   4636   5500       C  
ATOM   1900  C   ALA A1041       1.673  23.914 -47.168  1.00 84.78           C  
ANISOU 1900  C   ALA A1041     7329  16496   8386   4575   4101   5097       C  
ATOM   1901  O   ALA A1041       1.717  24.222 -45.977  1.00 84.10           O  
ANISOU 1901  O   ALA A1041     6954  16402   8598   4134   3761   5298       O  
ATOM   1902  CB  ALA A1041       3.492  24.796 -48.650  1.00 85.70           C  
ANISOU 1902  CB  ALA A1041     6655  17620   8286   5100   4808   5913       C  
ATOM   1903  N   ALA A1042       0.528  23.825 -47.868  1.00 78.76           N  
ANISOU 1903  N   ALA A1042     7196  15381   7349   4537   4028   4532       N  
ATOM   1904  CA  ALA A1042      -0.790  24.059 -47.303  1.00 77.72           C  
ANISOU 1904  CA  ALA A1042     7427  14823   7279   3979   3579   4139       C  
ATOM   1905  C   ALA A1042      -1.153  22.913 -46.366  1.00 81.56           C  
ANISOU 1905  C   ALA A1042     8133  14840   8017   4042   3416   3966       C  
ATOM   1906  O   ALA A1042      -1.785  23.150 -45.334  1.00 81.36           O  
ANISOU 1906  O   ALA A1042     8093  14636   8182   3562   3059   3944       O  
ATOM   1907  CB  ALA A1042      -1.814  24.171 -48.408  1.00 78.12           C  
ANISOU 1907  CB  ALA A1042     8038  14665   6979   3999   3570   3635       C  
ATOM   1908  N   LYS A1043      -0.726  21.678 -46.717  1.00 77.52           N  
ANISOU 1908  N   LYS A1043     7820  14132   7500   4669   3692   3871       N  
ATOM   1909  CA  LYS A1043      -0.944  20.463 -45.932  1.00 76.92           C  
ANISOU 1909  CA  LYS A1043     7950  13572   7704   4819   3587   3769       C  
ATOM   1910  C   LYS A1043      -0.111  20.495 -44.646  1.00 80.88           C  
ANISOU 1910  C   LYS A1043     7881  14329   8521   4709   3517   4316       C  
ATOM   1911  O   LYS A1043      -0.619  20.123 -43.586  1.00 79.15           O  
ANISOU 1911  O   LYS A1043     7715  13822   8534   4446   3244   4325       O  
ATOM   1912  CB  LYS A1043      -0.625  19.209 -46.762  1.00 78.83           C  
ANISOU 1912  CB  LYS A1043     8576  13523   7852   5575   3904   3516       C  
ATOM   1913  CG  LYS A1043      -1.737  18.817 -47.725  1.00 86.37           C  
ANISOU 1913  CG  LYS A1043    10251  13988   8580   5636   3794   2847       C  
ATOM   1914  CD  LYS A1043      -1.386  17.572 -48.512  1.00 91.44           C  
ANISOU 1914  CD  LYS A1043    11328  14296   9120   6419   4057   2544       C  
ATOM   1915  CE  LYS A1043      -2.457  17.234 -49.512  1.00 98.14           C  
ANISOU 1915  CE  LYS A1043    12903  14672   9715   6472   3878   1846       C  
ATOM   1916  NZ  LYS A1043      -2.158  15.965 -50.220  1.00106.28           N  
ANISOU 1916  NZ  LYS A1043    14442  15284  10657   7251   4064   1473       N  
ATOM   1917  N   SER A1044       1.163  20.956 -44.745  1.00 78.81           N  
ANISOU 1917  N   SER A1044     7046  14637   8260   4908   3753   4807       N  
ATOM   1918  CA  SER A1044       2.093  21.083 -43.617  1.00 79.05           C  
ANISOU 1918  CA  SER A1044     6465  14998   8572   4813   3655   5363       C  
ATOM   1919  C   SER A1044       1.582  22.112 -42.623  1.00 83.02           C  
ANISOU 1919  C   SER A1044     6795  15592   9158   4074   3187   5430       C  
ATOM   1920  O   SER A1044       1.670  21.874 -41.420  1.00 83.00           O  
ANISOU 1920  O   SER A1044     6622  15561   9352   3924   2945   5628       O  
ATOM   1921  CB  SER A1044       3.484  21.480 -44.097  1.00 83.55           C  
ANISOU 1921  CB  SER A1044     6431  16178   9138   5130   3984   5878       C  
ATOM   1922  OG  SER A1044       4.053  20.484 -44.929  1.00 96.22           O  
ANISOU 1922  OG  SER A1044     8174  17745  10642   5919   4456   5849       O  
ATOM   1923  N   GLU A1045       1.028  23.243 -43.124  1.00 78.91           N  
ANISOU 1923  N   GLU A1045     6350  15173   8461   3652   3058   5257       N  
ATOM   1924  CA  GLU A1045       0.457  24.310 -42.295  1.00 78.31           C  
ANISOU 1924  CA  GLU A1045     6191  15142   8423   2990   2615   5243       C  
ATOM   1925  C   GLU A1045      -0.873  23.891 -41.643  1.00 80.44           C  
ANISOU 1925  C   GLU A1045     6941  14938   8686   2761   2357   4854       C  
ATOM   1926  O   GLU A1045      -1.221  24.405 -40.581  1.00 79.49           O  
ANISOU 1926  O   GLU A1045     6730  14852   8620   2365   2011   4908       O  
ATOM   1927  CB  GLU A1045       0.314  25.623 -43.085  1.00 79.75           C  
ANISOU 1927  CB  GLU A1045     6312  15538   8451   2666   2583   5207       C  
ATOM   1928  CG  GLU A1045       1.610  26.415 -43.221  1.00 92.92           C  
ANISOU 1928  CG  GLU A1045     7325  17730  10249   2613   2648   5752       C  
ATOM   1929  CD  GLU A1045       2.215  26.989 -41.948  1.00118.88           C  
ANISOU 1929  CD  GLU A1045    10134  21235  13800   2232   2245   6105       C  
ATOM   1930  OE1 GLU A1045       3.314  26.534 -41.550  1.00101.18           O  
ANISOU 1930  OE1 GLU A1045     7423  19269  11752   2478   2330   6536       O  
ATOM   1931  OE2 GLU A1045       1.593  27.897 -41.350  1.00121.43           O  
ANISOU 1931  OE2 GLU A1045    10559  21458  14123   1713   1826   5940       O  
ATOM   1932  N   LEU A1046      -1.596  22.946 -42.267  1.00 76.33           N  
ANISOU 1932  N   LEU A1046     6919  13982   8102   3028   2515   4479       N  
ATOM   1933  CA  LEU A1046      -2.858  22.407 -41.758  1.00 75.85           C  
ANISOU 1933  CA  LEU A1046     7278  13442   8101   2838   2305   4166       C  
ATOM   1934  C   LEU A1046      -2.573  21.412 -40.629  1.00 80.75           C  
ANISOU 1934  C   LEU A1046     7789  13922   8969   3008   2268   4427       C  
ATOM   1935  O   LEU A1046      -3.218  21.480 -39.581  1.00 80.19           O  
ANISOU 1935  O   LEU A1046     7736  13766   8967   2702   2012   4471       O  
ATOM   1936  CB  LEU A1046      -3.651  21.737 -42.901  1.00 75.57           C  
ANISOU 1936  CB  LEU A1046     7785  12969   7959   3053   2435   3692       C  
ATOM   1937  CG  LEU A1046      -5.001  21.085 -42.574  1.00 79.53           C  
ANISOU 1937  CG  LEU A1046     8707  12921   8590   2853   2218   3381       C  
ATOM   1938  CD1 LEU A1046      -6.031  22.116 -42.151  1.00 79.11           C  
ANISOU 1938  CD1 LEU A1046     8663  12937   8458   2290   1924   3283       C  
ATOM   1939  CD2 LEU A1046      -5.535  20.351 -43.776  1.00 82.44           C  
ANISOU 1939  CD2 LEU A1046     9581  12861   8882   3120   2308   2924       C  
ATOM   1940  N   ASP A1047      -1.585  20.509 -40.840  1.00 78.45           N  
ANISOU 1940  N   ASP A1047     7373  13640   8795   3535   2544   4632       N  
ATOM   1941  CA  ASP A1047      -1.144  19.501 -39.865  1.00 78.71           C  
ANISOU 1941  CA  ASP A1047     7271  13555   9080   3787   2550   4946       C  
ATOM   1942  C   ASP A1047      -0.548  20.149 -38.598  1.00 82.20           C  
ANISOU 1942  C   ASP A1047     7205  14465   9562   3527   2310   5392       C  
ATOM   1943  O   ASP A1047      -0.625  19.562 -37.522  1.00 82.28           O  
ANISOU 1943  O   ASP A1047     7167  14384   9713   3546   2184   5614       O  
ATOM   1944  CB  ASP A1047      -0.127  18.525 -40.500  1.00 80.85           C  
ANISOU 1944  CB  ASP A1047     7498  13777   9443   4468   2924   5069       C  
ATOM   1945  CG  ASP A1047      -0.638  17.691 -41.672  1.00 93.72           C  
ANISOU 1945  CG  ASP A1047     9700  14885  11023   4832   3126   4590       C  
ATOM   1946  OD1 ASP A1047      -1.863  17.715 -41.936  1.00 94.39           O  
ANISOU 1946  OD1 ASP A1047    10224  14578  11061   4524   2939   4171       O  
ATOM   1947  OD2 ASP A1047       0.190  17.020 -42.329  1.00100.88           O  
ANISOU 1947  OD2 ASP A1047    10617  15782  11929   5447   3455   4629       O  
ATOM   1948  N   LYS A1048       0.036  21.358 -38.744  1.00 77.55           N  
ANISOU 1948  N   LYS A1048     6252  14361   8852   3286   2224   5528       N  
ATOM   1949  CA  LYS A1048       0.643  22.196 -37.704  1.00 76.64           C  
ANISOU 1949  CA  LYS A1048     5667  14698   8754   2984   1913   5878       C  
ATOM   1950  C   LYS A1048      -0.466  22.795 -36.828  1.00 79.03           C  
ANISOU 1950  C   LYS A1048     6196  14903   8929   2502   1540   5670       C  
ATOM   1951  O   LYS A1048      -0.339  22.811 -35.604  1.00 79.45           O  
ANISOU 1951  O   LYS A1048     6081  15124   8985   2400   1280   5894       O  
ATOM   1952  CB  LYS A1048       1.428  23.331 -38.396  1.00 78.89           C  
ANISOU 1952  CB  LYS A1048     5573  15404   8996   2836   1933   6018       C  
ATOM   1953  CG  LYS A1048       2.585  23.941 -37.626  1.00 90.08           C  
ANISOU 1953  CG  LYS A1048     6370  17315  10543   2681   1678   6491       C  
ATOM   1954  CD  LYS A1048       3.324  24.921 -38.549  1.00 96.04           C  
ANISOU 1954  CD  LYS A1048     6746  18409  11334   2571   1778   6675       C  
ATOM   1955  CE  LYS A1048       4.512  25.604 -37.920  1.00102.29           C  
ANISOU 1955  CE  LYS A1048     6860  19675  12332   2367   1490   7177       C  
ATOM   1956  NZ  LYS A1048       5.225  26.470 -38.900  1.00109.25           N  
ANISOU 1956  NZ  LYS A1048     7326  20867  13315   2287   1649   7448       N  
ATOM   1957  N   ALA A1049      -1.548  23.281 -37.464  1.00 73.81           N  
ANISOU 1957  N   ALA A1049     5913  14002   8129   2250   1523   5253       N  
ATOM   1958  CA  ALA A1049      -2.692  23.913 -36.814  1.00 73.17           C  
ANISOU 1958  CA  ALA A1049     6063  13831   7908   1841   1229   5028       C  
ATOM   1959  C   ALA A1049      -3.573  22.931 -36.078  1.00 76.57           C  
ANISOU 1959  C   ALA A1049     6760  13935   8396   1915   1222   5005       C  
ATOM   1960  O   ALA A1049      -4.108  23.293 -35.040  1.00 75.85           O  
ANISOU 1960  O   ALA A1049     6679  13947   8193   1697    980   5048       O  
ATOM   1961  CB  ALA A1049      -3.515  24.686 -37.831  1.00 73.81           C  
ANISOU 1961  CB  ALA A1049     6420  13774   7853   1602   1244   4640       C  
ATOM   1962  N   ILE A1050      -3.738  21.706 -36.605  1.00 73.87           N  
ANISOU 1962  N   ILE A1050     6642  13194   8230   2230   1479   4947       N  
ATOM   1963  CA  ILE A1050      -4.582  20.671 -35.995  1.00 74.33           C  
ANISOU 1963  CA  ILE A1050     6939  12862   8443   2287   1482   4981       C  
ATOM   1964  C   ILE A1050      -3.785  19.805 -35.002  1.00 81.84           C  
ANISOU 1964  C   ILE A1050     7644  13902   9548   2585   1513   5444       C  
ATOM   1965  O   ILE A1050      -4.219  19.631 -33.858  1.00 81.68           O  
ANISOU 1965  O   ILE A1050     7597  13926   9512   2491   1371   5664       O  
ATOM   1966  CB  ILE A1050      -5.333  19.857 -37.081  1.00 76.95           C  
ANISOU 1966  CB  ILE A1050     7689  12624   8925   2405   1649   4634       C  
ATOM   1967  CG1 ILE A1050      -6.268  20.798 -37.824  1.00 77.27           C  
ANISOU 1967  CG1 ILE A1050     7947  12636   8777   2062   1549   4227       C  
ATOM   1968  CG2 ILE A1050      -6.129  18.674 -36.492  1.00 77.36           C  
ANISOU 1968  CG2 ILE A1050     7945  12197   9252   2448   1638   4737       C  
ATOM   1969  CD1 ILE A1050      -6.360  20.560 -39.091  1.00 88.39           C  
ANISOU 1969  CD1 ILE A1050     9608  13798  10178   2212   1688   3910       C  
ATOM   1970  N   GLY A1051      -2.633  19.304 -35.437  1.00 80.89           N  
ANISOU 1970  N   GLY A1051     7332  13850   9553   2971   1710   5619       N  
ATOM   1971  CA  GLY A1051      -1.763  18.468 -34.616  1.00 81.93           C  
ANISOU 1971  CA  GLY A1051     7198  14081   9851   3313   1756   6085       C  
ATOM   1972  C   GLY A1051      -1.679  17.018 -35.057  1.00 88.86           C  
ANISOU 1972  C   GLY A1051     8294  14437  11033   3772   2027   6114       C  
ATOM   1973  O   GLY A1051      -1.030  16.212 -34.383  1.00 88.92           O  
ANISOU 1973  O   GLY A1051     8106  14461  11217   4102   2087   6522       O  
ATOM   1974  N   ARG A1052      -2.328  16.677 -36.193  1.00 86.98           N  
ANISOU 1974  N   ARG A1052     8478  13714  10857   3814   2163   5673       N  
ATOM   1975  CA  ARG A1052      -2.342  15.326 -36.769  1.00 87.46           C  
ANISOU 1975  CA  ARG A1052     8855  13168  11208   4248   2371   5574       C  
ATOM   1976  C   ARG A1052      -2.184  15.359 -38.288  1.00 94.06           C  
ANISOU 1976  C   ARG A1052     9955  13850  11933   4491   2575   5123       C  
ATOM   1977  O   ARG A1052      -2.450  16.394 -38.907  1.00 93.81           O  
ANISOU 1977  O   ARG A1052     9940  14076  11626   4213   2528   4853       O  
ATOM   1978  CB  ARG A1052      -3.623  14.567 -36.373  1.00 86.62           C  
ANISOU 1978  CB  ARG A1052     9105  12450  11355   4039   2235   5498       C  
ATOM   1979  CG  ARG A1052      -4.915  15.172 -36.913  1.00 93.17           C  
ANISOU 1979  CG  ARG A1052    10238  13095  12065   3576   2076   5046       C  
ATOM   1980  CD  ARG A1052      -6.085  14.229 -36.767  1.00100.86           C  
ANISOU 1980  CD  ARG A1052    11546  13383  13393   3433   1969   4983       C  
ATOM   1981  NE  ARG A1052      -7.282  14.754 -37.425  1.00110.97           N  
ANISOU 1981  NE  ARG A1052    13096  14482  14588   3027   1810   4545       N  
ATOM   1982  CZ  ARG A1052      -7.632  14.488 -38.681  1.00125.18           C  
ANISOU 1982  CZ  ARG A1052    15285  15860  16416   3098   1801   4040       C  
ATOM   1983  NH1 ARG A1052      -6.874  13.703 -39.438  1.00112.44           N  
ANISOU 1983  NH1 ARG A1052    13877  13954  14889   3596   1966   3874       N  
ATOM   1984  NH2 ARG A1052      -8.738  15.011 -39.192  1.00111.87           N  
ANISOU 1984  NH2 ARG A1052    13795  14064  14647   2708   1620   3691       N  
ATOM   1985  N   ASN A1053      -1.775  14.222 -38.888  1.00 92.72           N  
ANISOU 1985  N   ASN A1053    10022  13248  11959   5043   2798   5040       N  
ATOM   1986  CA  ASN A1053      -1.608  14.093 -40.339  1.00 93.51           C  
ANISOU 1986  CA  ASN A1053    10447  13179  11903   5400   3013   4588       C  
ATOM   1987  C   ASN A1053      -2.989  13.955 -41.019  1.00 97.92           C  
ANISOU 1987  C   ASN A1053    11578  13168  12461   5104   2818   4018       C  
ATOM   1988  O   ASN A1053      -3.504  12.845 -41.199  1.00 97.26           O  
ANISOU 1988  O   ASN A1053    11918  12370  12666   5268   2756   3804       O  
ATOM   1989  CB  ASN A1053      -0.643  12.943 -40.688  1.00 97.39           C  
ANISOU 1989  CB  ASN A1053    11010  13421  12571   6161   3311   4682       C  
ATOM   1990  CG  ASN A1053       0.795  13.150 -40.230  1.00129.56           C  
ANISOU 1990  CG  ASN A1053    14469  18130  16628   6499   3526   5247       C  
ATOM   1991  OD1 ASN A1053       1.077  13.763 -39.189  1.00125.43           O  
ANISOU 1991  OD1 ASN A1053    13464  18079  16114   6166   3364   5685       O  
ATOM   1992  ND2 ASN A1053       1.744  12.622 -40.996  1.00122.22           N  
ANISOU 1992  ND2 ASN A1053    13539  17233  15667   7199   3882   5251       N  
ATOM   1993  N   THR A1054      -3.594  15.117 -41.348  1.00 94.97           N  
ANISOU 1993  N   THR A1054    11187  13103  11795   4639   2682   3802       N  
ATOM   1994  CA  THR A1054      -4.930  15.265 -41.948  1.00 94.88           C  
ANISOU 1994  CA  THR A1054    11610  12706  11736   4271   2455   3312       C  
ATOM   1995  C   THR A1054      -4.981  14.903 -43.437  1.00 98.36           C  
ANISOU 1995  C   THR A1054    12534  12846  11993   4645   2561   2766       C  
ATOM   1996  O   THR A1054      -5.952  14.280 -43.871  1.00 98.06           O  
ANISOU 1996  O   THR A1054    12969  12185  12105   4551   2350   2362       O  
ATOM   1997  CB  THR A1054      -5.478  16.685 -41.711  1.00103.41           C  
ANISOU 1997  CB  THR A1054    12466  14265  12560   3697   2285   3326       C  
ATOM   1998  OG1 THR A1054      -4.604  17.627 -42.329  1.00103.15           O  
ANISOU 1998  OG1 THR A1054    12189  14811  12191   3828   2472   3364       O  
ATOM   1999  CG2 THR A1054      -5.648  17.018 -40.231  1.00102.53           C  
ANISOU 1999  CG2 THR A1054    11993  14388  12577   3335   2122   3767       C  
ATOM   2000  N   ASN A1055      -3.948  15.320 -44.210  1.00 94.08           N  
ANISOU 2000  N   ASN A1055    11857  12771  11118   5063   2871   2772       N  
ATOM   2001  CA  ASN A1055      -3.770  15.108 -45.654  1.00 93.40           C  
ANISOU 2001  CA  ASN A1055    12182  12588  10717   5543   3054   2309       C  
ATOM   2002  C   ASN A1055      -4.955  15.648 -46.491  1.00 95.27           C  
ANISOU 2002  C   ASN A1055    12814  12675  10711   5171   2799   1793       C  
ATOM   2003  O   ASN A1055      -5.597  14.915 -47.252  1.00 94.78           O  
ANISOU 2003  O   ASN A1055    13323  12042  10648   5332   2651   1275       O  
ATOM   2004  CB  ASN A1055      -3.438  13.634 -45.984  1.00 95.45           C  
ANISOU 2004  CB  ASN A1055    12851  12232  11182   6193   3171   2103       C  
ATOM   2005  CG  ASN A1055      -2.892  13.402 -47.382  1.00123.91           C  
ANISOU 2005  CG  ASN A1055    16812  15888  14380   6891   3463   1712       C  
ATOM   2006  OD1 ASN A1055      -2.160  14.224 -47.947  1.00120.39           O  
ANISOU 2006  OD1 ASN A1055    16096  16123  13524   7084   3758   1847       O  
ATOM   2007  ND2 ASN A1055      -3.233  12.264 -47.972  1.00116.44           N  
ANISOU 2007  ND2 ASN A1055    16489  14215  13538   7308   3382   1230       N  
ATOM   2008  N   GLY A1056      -5.224  16.937 -46.333  1.00 90.15           N  
ANISOU 2008  N   GLY A1056    11856  12526   9869   4680   2718   1940       N  
ATOM   2009  CA  GLY A1056      -6.282  17.612 -47.071  1.00 89.08           C  
ANISOU 2009  CA  GLY A1056    12001  12356   9488   4320   2492   1541       C  
ATOM   2010  C   GLY A1056      -7.639  17.704 -46.398  1.00 90.43           C  
ANISOU 2010  C   GLY A1056    12241  12190   9928   3682   2088   1465       C  
ATOM   2011  O   GLY A1056      -8.230  18.786 -46.383  1.00 89.59           O  
ANISOU 2011  O   GLY A1056    11994  12384   9662   3240   1951   1477       O  
ATOM   2012  N   VAL A1057      -8.168  16.572 -45.874  1.00 85.26           N  
ANISOU 2012  N   VAL A1057    11800  10896   9697   3646   1902   1406       N  
ATOM   2013  CA  VAL A1057      -9.502  16.503 -45.238  1.00 83.85           C  
ANISOU 2013  CA  VAL A1057    11662  10364   9832   3073   1542   1393       C  
ATOM   2014  C   VAL A1057      -9.439  16.682 -43.701  1.00 83.88           C  
ANISOU 2014  C   VAL A1057    11198  10575  10097   2785   1544   1961       C  
ATOM   2015  O   VAL A1057      -8.559  16.115 -43.043  1.00 83.50           O  
ANISOU 2015  O   VAL A1057    10962  10544  10221   3074   1720   2301       O  
ATOM   2016  CB  VAL A1057     -10.276  15.212 -45.657  1.00 87.76           C  
ANISOU 2016  CB  VAL A1057    12663  10009  10673   3125   1279   1011       C  
ATOM   2017  CG1 VAL A1057     -11.553  15.001 -44.839  1.00 87.56           C  
ANISOU 2017  CG1 VAL A1057    12554   9621  11095   2554    955   1176       C  
ATOM   2018  CG2 VAL A1057     -10.600  15.224 -47.149  1.00 87.50           C  
ANISOU 2018  CG2 VAL A1057    13125   9815  10306   3289   1152    383       C  
ATOM   2019  N   ILE A1058     -10.383  17.491 -43.154  1.00 76.97           N  
ANISOU 2019  N   ILE A1058    10150   9880   9214   2255   1347   2057       N  
ATOM   2020  CA  ILE A1058     -10.561  17.794 -41.723  1.00 75.28           C  
ANISOU 2020  CA  ILE A1058     9553   9901   9149   1964   1309   2531       C  
ATOM   2021  C   ILE A1058     -12.044  17.665 -41.310  1.00 77.06           C  
ANISOU 2021  C   ILE A1058     9841   9810   9628   1515   1044   2524       C  
ATOM   2022  O   ILE A1058     -12.920  17.695 -42.178  1.00 76.99           O  
ANISOU 2022  O   ILE A1058    10106   9527   9620   1347    858   2141       O  
ATOM   2023  CB  ILE A1058      -9.978  19.176 -41.312  1.00 77.83           C  
ANISOU 2023  CB  ILE A1058     9504  10946   9123   1842   1389   2742       C  
ATOM   2024  CG1 ILE A1058     -10.698  20.342 -42.024  1.00 77.90           C  
ANISOU 2024  CG1 ILE A1058     9593  11163   8841   1540   1264   2444       C  
ATOM   2025  CG2 ILE A1058      -8.468  19.220 -41.502  1.00 78.17           C  
ANISOU 2025  CG2 ILE A1058     9355  11322   9022   2251   1645   2904       C  
ATOM   2026  CD1 ILE A1058     -10.712  21.633 -41.265  1.00 83.38           C  
ANISOU 2026  CD1 ILE A1058     9971  12369   9342   1251   1204   2659       C  
ATOM   2027  N   THR A1059     -12.322  17.546 -39.989  1.00 70.82           N  
ANISOU 2027  N   THR A1059     8772   9102   9032   1338   1029   2977       N  
ATOM   2028  CA  THR A1059     -13.685  17.424 -39.459  1.00 68.88           C  
ANISOU 2028  CA  THR A1059     8487   8645   9038    944    841   3102       C  
ATOM   2029  C   THR A1059     -14.306  18.800 -39.185  1.00 68.82           C  
ANISOU 2029  C   THR A1059     8293   9153   8701    635    779   3097       C  
ATOM   2030  O   THR A1059     -13.583  19.799 -39.163  1.00 67.43           O  
ANISOU 2030  O   THR A1059     7991   9479   8151    709    867   3073       O  
ATOM   2031  CB  THR A1059     -13.725  16.488 -38.239  1.00 76.42           C  
ANISOU 2031  CB  THR A1059     9261   9408  10368    970    890   3630       C  
ATOM   2032  OG1 THR A1059     -12.906  17.021 -37.200  1.00 75.67           O  
ANISOU 2032  OG1 THR A1059     8850   9889  10011   1106   1047   4005       O  
ATOM   2033  CG2 THR A1059     -13.301  15.057 -38.577  1.00 74.47           C  
ANISOU 2033  CG2 THR A1059     9251   8503  10540   1250    902   3612       C  
ATOM   2034  N   LYS A1060     -15.651  18.846 -38.998  1.00 63.59           N  
ANISOU 2034  N   LYS A1060     7605   8342   8213    294    616   3132       N  
ATOM   2035  CA  LYS A1060     -16.439  20.057 -38.715  1.00 62.57           C  
ANISOU 2035  CA  LYS A1060     7318   8634   7823     30    554   3137       C  
ATOM   2036  C   LYS A1060     -15.969  20.737 -37.416  1.00 65.07           C  
ANISOU 2036  C   LYS A1060     7345   9501   7875     99    686   3504       C  
ATOM   2037  O   LYS A1060     -15.860  21.965 -37.380  1.00 64.49           O  
ANISOU 2037  O   LYS A1060     7211   9859   7434     50    672   3386       O  
ATOM   2038  CB  LYS A1060     -17.945  19.714 -38.652  1.00 64.84           C  
ANISOU 2038  CB  LYS A1060     7567   8624   8443   -295    385   3219       C  
ATOM   2039  CG  LYS A1060     -18.891  20.918 -38.561  1.00 76.78           C  
ANISOU 2039  CG  LYS A1060     8944  10517   9712   -528    318   3177       C  
ATOM   2040  CD  LYS A1060     -20.340  20.494 -38.280  1.00 84.19           C  
ANISOU 2040  CD  LYS A1060     9723  11233  11031   -819    197   3418       C  
ATOM   2041  CE  LYS A1060     -20.955  21.218 -37.103  1.00 94.11           C  
ANISOU 2041  CE  LYS A1060    10665  12984  12108   -865    326   3802       C  
ATOM   2042  NZ  LYS A1060     -20.361  20.796 -35.803  1.00103.61           N  
ANISOU 2042  NZ  LYS A1060    11695  14390  13283   -662    536   4272       N  
ATOM   2043  N   ASP A1061     -15.676  19.932 -36.366  1.00 60.44           N  
ANISOU 2043  N   ASP A1061     6607   8880   7478    227    788   3943       N  
ATOM   2044  CA  ASP A1061     -15.199  20.405 -35.063  1.00 59.55           C  
ANISOU 2044  CA  ASP A1061     6250   9277   7099    341    878   4308       C  
ATOM   2045  C   ASP A1061     -13.787  21.011 -35.135  1.00 61.97           C  
ANISOU 2045  C   ASP A1061     6517   9935   7092    548    913   4203       C  
ATOM   2046  O   ASP A1061     -13.511  21.986 -34.432  1.00 61.80           O  
ANISOU 2046  O   ASP A1061     6357  10396   6727    542    871   4271       O  
ATOM   2047  CB  ASP A1061     -15.288  19.287 -34.020  1.00 61.37           C  
ANISOU 2047  CB  ASP A1061     6339   9357   7623    446    974   4838       C  
ATOM   2048  CG  ASP A1061     -16.693  18.758 -33.771  1.00 73.03           C  
ANISOU 2048  CG  ASP A1061     7756  10537   9456    211    947   5077       C  
ATOM   2049  OD1 ASP A1061     -17.659  19.300 -34.375  1.00 72.80           O  
ANISOU 2049  OD1 ASP A1061     7772  10467   9420    -40    840   4826       O  
ATOM   2050  OD2 ASP A1061     -16.834  17.814 -32.963  1.00 80.67           O  
ANISOU 2050  OD2 ASP A1061     8597  11325  10728    273   1032   5563       O  
ATOM   2051  N   GLU A1062     -12.910  20.456 -36.008  1.00 56.60           N  
ANISOU 2051  N   GLU A1062     5956   9010   6539    741    975   4036       N  
ATOM   2052  CA  GLU A1062     -11.557  20.966 -36.253  1.00 55.06           C  
ANISOU 2052  CA  GLU A1062     5669   9134   6115    939   1033   3981       C  
ATOM   2053  C   GLU A1062     -11.647  22.281 -37.038  1.00 56.17           C  
ANISOU 2053  C   GLU A1062     5863   9517   5962    763    952   3631       C  
ATOM   2054  O   GLU A1062     -10.856  23.192 -36.806  1.00 55.50           O  
ANISOU 2054  O   GLU A1062     5608   9841   5639    768    917   3674       O  
ATOM   2055  CB  GLU A1062     -10.717  19.940 -37.021  1.00 56.39           C  
ANISOU 2055  CB  GLU A1062     5952   8971   6503   1254   1172   3924       C  
ATOM   2056  CG  GLU A1062     -10.273  18.763 -36.167  1.00 70.13           C  
ANISOU 2056  CG  GLU A1062     7591  10536   8518   1495   1261   4336       C  
ATOM   2057  CD  GLU A1062      -9.718  17.552 -36.899  1.00 99.34           C  
ANISOU 2057  CD  GLU A1062    11482  13745  12517   1830   1386   4259       C  
ATOM   2058  OE1 GLU A1062      -9.029  16.737 -36.244  1.00104.02           O  
ANISOU 2058  OE1 GLU A1062    11950  14274  13297   2102   1483   4622       O  
ATOM   2059  OE2 GLU A1062      -9.982  17.404 -38.115  1.00 94.06           O  
ANISOU 2059  OE2 GLU A1062    11108  12749  11881   1854   1377   3832       O  
ATOM   2060  N   ALA A1063     -12.643  22.386 -37.941  1.00 51.24           N  
ANISOU 2060  N   ALA A1063     5461   8628   5382    587    888   3311       N  
ATOM   2061  CA  ALA A1063     -12.911  23.585 -38.741  1.00 50.52           C  
ANISOU 2061  CA  ALA A1063     5442   8719   5035    417    806   3004       C  
ATOM   2062  C   ALA A1063     -13.513  24.695 -37.866  1.00 52.36           C  
ANISOU 2062  C   ALA A1063     5545   9285   5065    201    683   3085       C  
ATOM   2063  O   ALA A1063     -13.329  25.880 -38.160  1.00 52.08           O  
ANISOU 2063  O   ALA A1063     5489   9504   4795    104    610   2942       O  
ATOM   2064  CB  ALA A1063     -13.850  23.248 -39.891  1.00 51.26           C  
ANISOU 2064  CB  ALA A1063     5811   8428   5236    318    739   2667       C  
ATOM   2065  N   GLU A1064     -14.232  24.299 -36.794  1.00 46.80           N  
ANISOU 2065  N   GLU A1064     4759   8570   4453    154    669   3334       N  
ATOM   2066  CA  GLU A1064     -14.844  25.201 -35.818  1.00 45.70           C  
ANISOU 2066  CA  GLU A1064     4520   8759   4085     49    587   3433       C  
ATOM   2067  C   GLU A1064     -13.754  25.821 -34.935  1.00 49.42           C  
ANISOU 2067  C   GLU A1064     4843   9635   4300    167    534   3576       C  
ATOM   2068  O   GLU A1064     -13.845  26.994 -34.570  1.00 48.14           O  
ANISOU 2068  O   GLU A1064     4675   9752   3865     90    398   3469       O  
ATOM   2069  CB  GLU A1064     -15.880  24.445 -34.972  1.00 46.58           C  
ANISOU 2069  CB  GLU A1064     4560   8768   4370     25    643   3729       C  
ATOM   2070  CG  GLU A1064     -16.852  25.351 -34.240  1.00 52.07           C  
ANISOU 2070  CG  GLU A1064     5194   9766   4823    -51    600   3776       C  
ATOM   2071  CD  GLU A1064     -18.052  24.688 -33.590  1.00 68.93           C  
ANISOU 2071  CD  GLU A1064     7212  11831   7146    -90    692   4104       C  
ATOM   2072  OE1 GLU A1064     -18.115  23.437 -33.538  1.00 67.83           O  
ANISOU 2072  OE1 GLU A1064     7019  11382   7371    -82    770   4365       O  
ATOM   2073  OE2 GLU A1064     -18.937  25.439 -33.123  1.00 56.71           O  
ANISOU 2073  OE2 GLU A1064     5612  10537   5398   -115    691   4127       O  
ATOM   2074  N   LYS A1065     -12.716  25.028 -34.621  1.00 47.25           N  
ANISOU 2074  N   LYS A1065     4455   9365   4131    361    609   3807       N  
ATOM   2075  CA  LYS A1065     -11.561  25.422 -33.816  1.00 47.93           C  
ANISOU 2075  CA  LYS A1065     4360   9818   4032    480    521   3983       C  
ATOM   2076  C   LYS A1065     -10.768  26.519 -34.549  1.00 53.13           C  
ANISOU 2076  C   LYS A1065     4984  10632   4572    379    407   3755       C  
ATOM   2077  O   LYS A1065     -10.341  27.489 -33.915  1.00 53.50           O  
ANISOU 2077  O   LYS A1065     4940  10986   4403    314    201   3757       O  
ATOM   2078  CB  LYS A1065     -10.690  24.178 -33.535  1.00 50.90           C  
ANISOU 2078  CB  LYS A1065     4611  10104   4623    730    653   4298       C  
ATOM   2079  CG  LYS A1065      -9.577  24.366 -32.501  1.00 72.23           C  
ANISOU 2079  CG  LYS A1065     7080  13206   7159    875    538   4572       C  
ATOM   2080  CD  LYS A1065      -8.183  24.473 -33.159  1.00 81.95           C  
ANISOU 2080  CD  LYS A1065     8140  14522   8474    967    546   4573       C  
ATOM   2081  CE  LYS A1065      -7.033  24.372 -32.177  1.00 86.11           C  
ANISOU 2081  CE  LYS A1065     8385  15395   8939   1138    431   4917       C  
ATOM   2082  NZ  LYS A1065      -6.742  22.965 -31.792  1.00 89.60           N  
ANISOU 2082  NZ  LYS A1065     8766  15678   9599   1432    617   5265       N  
ATOM   2083  N   LEU A1066     -10.597  26.364 -35.884  1.00 49.19           N  
ANISOU 2083  N   LEU A1066     4567   9910   4212    372    526   3569       N  
ATOM   2084  CA  LEU A1066      -9.884  27.309 -36.753  1.00 48.16           C  
ANISOU 2084  CA  LEU A1066     4381   9911   4006    290    483   3425       C  
ATOM   2085  C   LEU A1066     -10.710  28.573 -36.936  1.00 49.06           C  
ANISOU 2085  C   LEU A1066     4620  10072   3949     38    316   3182       C  
ATOM   2086  O   LEU A1066     -10.151  29.672 -36.998  1.00 47.25           O  
ANISOU 2086  O   LEU A1066     4294  10032   3625    -88    161   3154       O  
ATOM   2087  CB  LEU A1066      -9.610  26.681 -38.136  1.00 48.19           C  
ANISOU 2087  CB  LEU A1066     4484   9688   4139    431    702   3304       C  
ATOM   2088  CG  LEU A1066      -8.663  25.484 -38.199  1.00 52.83           C  
ANISOU 2088  CG  LEU A1066     4976  10194   4902    754    901   3503       C  
ATOM   2089  CD1 LEU A1066      -8.830  24.738 -39.515  1.00 52.79           C  
ANISOU 2089  CD1 LEU A1066     5215   9870   4974    931   1093   3270       C  
ATOM   2090  CD2 LEU A1066      -7.211  25.908 -38.016  1.00 55.15           C  
ANISOU 2090  CD2 LEU A1066     4930  10847   5178    852    903   3762       C  
ATOM   2091  N   PHE A1067     -12.043  28.405 -37.036  1.00 44.81           N  
ANISOU 2091  N   PHE A1067     4276   9339   3411    -37    335   3032       N  
ATOM   2092  CA  PHE A1067     -12.981  29.502 -37.221  1.00 44.35           C  
ANISOU 2092  CA  PHE A1067     4343   9301   3208   -226    203   2814       C  
ATOM   2093  C   PHE A1067     -12.997  30.422 -35.989  1.00 49.20           C  
ANISOU 2093  C   PHE A1067     4906  10176   3609   -264     -1   2856       C  
ATOM   2094  O   PHE A1067     -13.058  31.646 -36.146  1.00 50.13           O  
ANISOU 2094  O   PHE A1067     5079  10363   3605   -396   -171   2692       O  
ATOM   2095  CB  PHE A1067     -14.374  28.961 -37.586  1.00 45.72           C  
ANISOU 2095  CB  PHE A1067     4672   9223   3478   -275    272   2705       C  
ATOM   2096  CG  PHE A1067     -15.496  29.962 -37.484  1.00 46.97           C  
ANISOU 2096  CG  PHE A1067     4914   9439   3495   -414    155   2555       C  
ATOM   2097  CD1 PHE A1067     -15.834  30.767 -38.566  1.00 50.24           C  
ANISOU 2097  CD1 PHE A1067     5441   9788   3860   -536     95   2323       C  
ATOM   2098  CD2 PHE A1067     -16.214  30.103 -36.306  1.00 48.72           C  
ANISOU 2098  CD2 PHE A1067     5097   9805   3608   -375    124   2673       C  
ATOM   2099  CE1 PHE A1067     -16.863  31.704 -38.461  1.00 50.97           C  
ANISOU 2099  CE1 PHE A1067     5603   9928   3837   -626    -10   2205       C  
ATOM   2100  CE2 PHE A1067     -17.226  31.049 -36.198  1.00 51.58           C  
ANISOU 2100  CE2 PHE A1067     5532  10240   3826   -435     42   2541       C  
ATOM   2101  CZ  PHE A1067     -17.551  31.839 -37.277  1.00 49.69           C  
ANISOU 2101  CZ  PHE A1067     5400   9901   3580   -564    -31   2305       C  
ATOM   2102  N   ASN A1068     -12.903  29.840 -34.777  1.00 44.30           N  
ANISOU 2102  N   ASN A1068     4205   9693   2934   -124      1   3075       N  
ATOM   2103  CA  ASN A1068     -12.904  30.608 -33.538  1.00 43.94           C  
ANISOU 2103  CA  ASN A1068     4159   9924   2612    -86   -206   3091       C  
ATOM   2104  C   ASN A1068     -11.633  31.432 -33.349  1.00 48.45           C  
ANISOU 2104  C   ASN A1068     4621  10670   3116   -151   -462   3073       C  
ATOM   2105  O   ASN A1068     -11.679  32.475 -32.701  1.00 48.56           O  
ANISOU 2105  O   ASN A1068     4718  10822   2911   -194   -728   2930       O  
ATOM   2106  CB  ASN A1068     -13.208  29.725 -32.343  1.00 44.74           C  
ANISOU 2106  CB  ASN A1068     4208  10164   2628    115   -115   3366       C  
ATOM   2107  CG  ASN A1068     -14.682  29.409 -32.229  1.00 59.01           C  
ANISOU 2107  CG  ASN A1068     6102  11881   4440    132     45   3390       C  
ATOM   2108  OD1 ASN A1068     -15.546  30.301 -32.218  1.00 49.14           O  
ANISOU 2108  OD1 ASN A1068     4967  10683   3020     88    -21   3197       O  
ATOM   2109  ND2 ASN A1068     -15.002  28.129 -32.156  1.00 50.17           N  
ANISOU 2109  ND2 ASN A1068     4905  10604   3554    196    252   3654       N  
ATOM   2110  N   GLN A1069     -10.519  31.002 -33.955  1.00 45.32           N  
ANISOU 2110  N   GLN A1069     4039  10253   2927   -154   -396   3212       N  
ATOM   2111  CA  GLN A1069      -9.260  31.746 -33.960  1.00 44.85           C  
ANISOU 2111  CA  GLN A1069     3787  10349   2905   -261   -628   3267       C  
ATOM   2112  C   GLN A1069      -9.445  32.963 -34.900  1.00 50.84           C  
ANISOU 2112  C   GLN A1069     4633  10984   3699   -499   -734   3042       C  
ATOM   2113  O   GLN A1069      -8.993  34.059 -34.569  1.00 50.80           O  
ANISOU 2113  O   GLN A1069     4592  11052   3657   -661  -1059   2980       O  
ATOM   2114  CB  GLN A1069      -8.120  30.857 -34.457  1.00 45.62           C  
ANISOU 2114  CB  GLN A1069     3623  10476   3233   -145   -442   3533       C  
ATOM   2115  CG  GLN A1069      -7.658  29.820 -33.446  1.00 54.79           C  
ANISOU 2115  CG  GLN A1069     4643  11786   4389     86   -410   3816       C  
ATOM   2116  CD  GLN A1069      -6.868  28.704 -34.081  1.00 73.68           C  
ANISOU 2116  CD  GLN A1069     6856  14109   7029    284   -125   4043       C  
ATOM   2117  OE1 GLN A1069      -6.450  28.768 -35.246  1.00 73.17           O  
ANISOU 2117  OE1 GLN A1069     6730  13965   7106    268     30   4008       O  
ATOM   2118  NE2 GLN A1069      -6.667  27.633 -33.332  1.00 61.87           N  
ANISOU 2118  NE2 GLN A1069     5287  12645   5574    521    -28   4295       N  
ATOM   2119  N   ASP A1070     -10.157  32.764 -36.048  1.00 48.02           N  
ANISOU 2119  N   ASP A1070     4408  10419   3418   -518   -491   2922       N  
ATOM   2120  CA  ASP A1070     -10.486  33.798 -37.040  1.00 47.50           C  
ANISOU 2120  CA  ASP A1070     4443  10233   3371   -703   -539   2747       C  
ATOM   2121  C   ASP A1070     -11.493  34.812 -36.489  1.00 49.72           C  
ANISOU 2121  C   ASP A1070     4947  10466   3478   -789   -760   2510       C  
ATOM   2122  O   ASP A1070     -11.464  35.968 -36.896  1.00 49.41           O  
ANISOU 2122  O   ASP A1070     4960  10355   3460   -960   -938   2403       O  
ATOM   2123  CB  ASP A1070     -11.030  33.182 -38.344  1.00 49.39           C  
ANISOU 2123  CB  ASP A1070     4789  10300   3677   -645   -244   2674       C  
ATOM   2124  CG  ASP A1070     -10.081  32.275 -39.105  1.00 59.14           C  
ANISOU 2124  CG  ASP A1070     5869  11557   5043   -494      2   2847       C  
ATOM   2125  OD1 ASP A1070      -8.852  32.514 -39.047  1.00 60.54           O  
ANISOU 2125  OD1 ASP A1070     5785  11910   5308   -505    -38   3065       O  
ATOM   2126  OD2 ASP A1070     -10.569  31.342 -39.784  1.00 62.64           O  
ANISOU 2126  OD2 ASP A1070     6452  11837   5512   -353    221   2763       O  
ATOM   2127  N   VAL A1071     -12.392  34.379 -35.593  1.00 45.23           N  
ANISOU 2127  N   VAL A1071     4503   9934   2748   -645   -727   2460       N  
ATOM   2128  CA  VAL A1071     -13.367  35.261 -34.944  1.00 45.36           C  
ANISOU 2128  CA  VAL A1071     4726   9958   2550   -627   -890   2254       C  
ATOM   2129  C   VAL A1071     -12.605  36.187 -33.978  1.00 52.22           C  
ANISOU 2129  C   VAL A1071     5607  10950   3284   -658  -1267   2190       C  
ATOM   2130  O   VAL A1071     -12.863  37.388 -33.957  1.00 52.59           O  
ANISOU 2130  O   VAL A1071     5818  10898   3267   -746  -1508   1973       O  
ATOM   2131  CB  VAL A1071     -14.502  34.463 -34.241  1.00 48.50           C  
ANISOU 2131  CB  VAL A1071     5192  10421   2815   -427   -700   2305       C  
ATOM   2132  CG1 VAL A1071     -15.241  35.303 -33.203  1.00 48.29           C  
ANISOU 2132  CG1 VAL A1071     5341  10527   2481   -291   -858   2154       C  
ATOM   2133  CG2 VAL A1071     -15.482  33.904 -35.252  1.00 47.92           C  
ANISOU 2133  CG2 VAL A1071     5150  10155   2902   -471   -459   2284       C  
ATOM   2134  N   ASP A1072     -11.642  35.624 -33.215  1.00 49.88           N  
ANISOU 2134  N   ASP A1072     5143  10843   2966   -587  -1350   2376       N  
ATOM   2135  CA  ASP A1072     -10.788  36.357 -32.274  1.00 50.35           C  
ANISOU 2135  CA  ASP A1072     5186  11035   2909   -629  -1773   2328       C  
ATOM   2136  C   ASP A1072      -9.908  37.371 -32.996  1.00 53.81           C  
ANISOU 2136  C   ASP A1072     5512  11324   3610   -935  -2037   2303       C  
ATOM   2137  O   ASP A1072      -9.727  38.475 -32.493  1.00 53.91           O  
ANISOU 2137  O   ASP A1072     5651  11270   3560  -1046  -2455   2108       O  
ATOM   2138  CB  ASP A1072      -9.925  35.390 -31.441  1.00 52.75           C  
ANISOU 2138  CB  ASP A1072     5278  11597   3169   -484  -1782   2598       C  
ATOM   2139  CG  ASP A1072     -10.521  34.999 -30.105  1.00 68.03           C  
ANISOU 2139  CG  ASP A1072     7366  13763   4719   -191  -1795   2595       C  
ATOM   2140  OD1 ASP A1072     -11.717  34.622 -30.069  1.00 70.72           O  
ANISOU 2140  OD1 ASP A1072     7851  14079   4939    -36  -1510   2571       O  
ATOM   2141  OD2 ASP A1072      -9.796  35.050 -29.102  1.00 74.30           O  
ANISOU 2141  OD2 ASP A1072     8113  14787   5330   -108  -2088   2649       O  
ATOM   2142  N   ALA A1073      -9.388  36.999 -34.183  1.00 49.57           N  
ANISOU 2142  N   ALA A1073     4747  10722   3367  -1054  -1794   2510       N  
ATOM   2143  CA  ALA A1073      -8.556  37.849 -35.032  1.00 48.58           C  
ANISOU 2143  CA  ALA A1073     4443  10491   3527  -1333  -1943   2607       C  
ATOM   2144  C   ALA A1073      -9.399  38.996 -35.611  1.00 52.26           C  
ANISOU 2144  C   ALA A1073     5165  10696   3995  -1471  -2035   2365       C  
ATOM   2145  O   ALA A1073      -8.908  40.120 -35.695  1.00 52.22           O  
ANISOU 2145  O   ALA A1073     5131  10550   4159  -1715  -2376   2349       O  
ATOM   2146  CB  ALA A1073      -7.944  37.019 -36.145  1.00 49.01           C  
ANISOU 2146  CB  ALA A1073     4223  10606   3794  -1304  -1560   2899       C  
ATOM   2147  N   ALA A1074     -10.678  38.717 -35.962  1.00 48.46           N  
ANISOU 2147  N   ALA A1074     4921  10136   3356  -1319  -1762   2200       N  
ATOM   2148  CA  ALA A1074     -11.646  39.694 -36.478  1.00 48.52           C  
ANISOU 2148  CA  ALA A1074     5177   9923   3337  -1382  -1812   1984       C  
ATOM   2149  C   ALA A1074     -12.053  40.718 -35.414  1.00 55.08           C  
ANISOU 2149  C   ALA A1074     6273  10661   3992  -1347  -2197   1698       C  
ATOM   2150  O   ALA A1074     -12.069  41.909 -35.711  1.00 54.01           O  
ANISOU 2150  O   ALA A1074     6258  10289   3975  -1509  -2451   1582       O  
ATOM   2151  CB  ALA A1074     -12.877  38.987 -37.018  1.00 48.98           C  
ANISOU 2151  CB  ALA A1074     5359   9968   3282  -1215  -1450   1917       C  
ATOM   2152  N   VAL A1075     -12.354  40.253 -34.172  1.00 54.57           N  
ANISOU 2152  N   VAL A1075     6316  10782   3638  -1109  -2244   1597       N  
ATOM   2153  CA  VAL A1075     -12.727  41.076 -33.005  1.00 55.19           C  
ANISOU 2153  CA  VAL A1075     6690  10845   3435   -962  -2592   1295       C  
ATOM   2154  C   VAL A1075     -11.517  41.938 -32.542  1.00 62.02           C  
ANISOU 2154  C   VAL A1075     7524  11608   4434  -1190  -3134   1236       C  
ATOM   2155  O   VAL A1075     -11.705  43.061 -32.066  1.00 61.44           O  
ANISOU 2155  O   VAL A1075     7736  11325   4281  -1194  -3525    932       O  
ATOM   2156  CB  VAL A1075     -13.359  40.221 -31.861  1.00 58.64           C  
ANISOU 2156  CB  VAL A1075     7216  11586   3480   -598  -2425   1281       C  
ATOM   2157  CG1 VAL A1075     -13.574  41.037 -30.591  1.00 58.52           C  
ANISOU 2157  CG1 VAL A1075     7521  11626   3089   -374  -2794    966       C  
ATOM   2158  CG2 VAL A1075     -14.678  39.590 -32.301  1.00 58.20           C  
ANISOU 2158  CG2 VAL A1075     7187  11563   3364   -427  -1973   1336       C  
ATOM   2159  N   ARG A1076     -10.282  41.429 -32.728  1.00 61.31           N  
ANISOU 2159  N   ARG A1076     7076  11638   4581  -1379  -3174   1534       N  
ATOM   2160  CA  ARG A1076      -9.046  42.160 -32.404  1.00 62.69           C  
ANISOU 2160  CA  ARG A1076     7106  11730   4983  -1661  -3700   1572       C  
ATOM   2161  C   ARG A1076      -8.910  43.384 -33.315  1.00 68.39           C  
ANISOU 2161  C   ARG A1076     7839  12071   6074  -1993  -3904   1559       C  
ATOM   2162  O   ARG A1076      -8.554  44.462 -32.842  1.00 67.98           O  
ANISOU 2162  O   ARG A1076     7927  11774   6129  -2174  -4455   1368       O  
ATOM   2163  CB  ARG A1076      -7.812  41.252 -32.556  1.00 64.40           C  
ANISOU 2163  CB  ARG A1076     6852  12200   5417  -1764  -3600   1986       C  
ATOM   2164  CG  ARG A1076      -7.061  41.008 -31.255  1.00 76.91           C  
ANISOU 2164  CG  ARG A1076     8370  14022   6829  -1693  -3988   1981       C  
ATOM   2165  CD  ARG A1076      -5.871  40.082 -31.448  1.00 94.53           C  
ANISOU 2165  CD  ARG A1076    10101  16515   9302  -1757  -3857   2431       C  
ATOM   2166  NE  ARG A1076      -4.747  40.735 -32.127  1.00112.05           N  
ANISOU 2166  NE  ARG A1076    11944  18620  12011  -2152  -4104   2694       N  
ATOM   2167  CZ  ARG A1076      -4.240  40.352 -33.299  1.00131.46           C  
ANISOU 2167  CZ  ARG A1076    14031  21121  14798  -2250  -3717   3079       C  
ATOM   2168  NH1 ARG A1076      -4.765  39.320 -33.953  1.00119.87           N  
ANISOU 2168  NH1 ARG A1076    12574  19754  13218  -1987  -3109   3173       N  
ATOM   2169  NH2 ARG A1076      -3.211  41.001 -33.829  1.00120.45           N  
ANISOU 2169  NH2 ARG A1076    12255  19664  13847  -2600  -3944   3379       N  
ATOM   2170  N   GLY A1077      -9.232  43.195 -34.597  1.00 66.09           N  
ANISOU 2170  N   GLY A1077     7428  11721   5961  -2052  -3479   1757       N  
ATOM   2171  CA  GLY A1077      -9.196  44.237 -35.613  1.00 66.45           C  
ANISOU 2171  CA  GLY A1077     7460  11450   6338  -2326  -3564   1836       C  
ATOM   2172  C   GLY A1077     -10.262  45.300 -35.430  1.00 71.43           C  
ANISOU 2172  C   GLY A1077     8538  11754   6849  -2248  -3767   1456       C  
ATOM   2173  O   GLY A1077      -9.978  46.489 -35.604  1.00 71.75           O  
ANISOU 2173  O   GLY A1077     8651  11438   7174  -2502  -4153   1419       O  
ATOM   2174  N   ILE A1078     -11.500  44.875 -35.086  1.00 67.75           N  
ANISOU 2174  N   ILE A1078     8353  11395   5994  -1888  -3503   1206       N  
ATOM   2175  CA  ILE A1078     -12.654  45.751 -34.834  1.00 67.63           C  
ANISOU 2175  CA  ILE A1078     8757  11142   5797  -1696  -3616    847       C  
ATOM   2176  C   ILE A1078     -12.355  46.730 -33.678  1.00 74.30           C  
ANISOU 2176  C   ILE A1078     9901  11767   6561  -1683  -4222    497       C  
ATOM   2177  O   ILE A1078     -12.581  47.930 -33.823  1.00 74.49           O  
ANISOU 2177  O   ILE A1078    10178  11385   6741  -1765  -4533    302       O  
ATOM   2178  CB  ILE A1078     -13.967  44.927 -34.613  1.00 69.89           C  
ANISOU 2178  CB  ILE A1078     9178  11682   5696  -1298  -3179    741       C  
ATOM   2179  CG1 ILE A1078     -14.391  44.196 -35.899  1.00 69.30           C  
ANISOU 2179  CG1 ILE A1078     8892  11693   5747  -1346  -2695   1004       C  
ATOM   2180  CG2 ILE A1078     -15.118  45.803 -34.097  1.00 70.29           C  
ANISOU 2180  CG2 ILE A1078     9641  11568   5497  -1007  -3303    374       C  
ATOM   2181  CD1 ILE A1078     -15.273  42.977 -35.692  1.00 69.29           C  
ANISOU 2181  CD1 ILE A1078     8855  11979   5491  -1073  -2285   1037       C  
ATOM   2182  N   LEU A1079     -11.818  46.218 -32.557  1.00 72.57           N  
ANISOU 2182  N   LEU A1079     9670  11800   6105  -1574  -4416    417       N  
ATOM   2183  CA  LEU A1079     -11.480  47.017 -31.377  1.00 73.09           C  
ANISOU 2183  CA  LEU A1079    10047  11710   6014  -1524  -5039     43       C  
ATOM   2184  C   LEU A1079     -10.282  47.951 -31.625  1.00 80.20           C  
ANISOU 2184  C   LEU A1079    10805  12236   7433  -2020  -5619    123       C  
ATOM   2185  O   LEU A1079     -10.211  49.024 -31.019  1.00 79.38           O  
ANISOU 2185  O   LEU A1079    11051  11769   7343  -2054  -6206   -246       O  
ATOM   2186  CB  LEU A1079     -11.259  46.117 -30.150  1.00 72.82           C  
ANISOU 2186  CB  LEU A1079    10015  12118   5535  -1242  -5062    -14       C  
ATOM   2187  CG  LEU A1079     -12.476  45.297 -29.670  1.00 77.22           C  
ANISOU 2187  CG  LEU A1079    10730  13036   5575   -733  -4556    -77       C  
ATOM   2188  CD1 LEU A1079     -12.038  44.102 -28.853  1.00 77.60           C  
ANISOU 2188  CD1 LEU A1079    10582  13555   5348   -566  -4428    120       C  
ATOM   2189  CD2 LEU A1079     -13.464  46.144 -28.874  1.00 79.03           C  
ANISOU 2189  CD2 LEU A1079    11490  13158   5381   -324  -4732   -553       C  
ATOM   2190  N   ARG A1080      -9.369  47.558 -32.546  1.00 79.38           N  
ANISOU 2190  N   ARG A1080    10189  12205   7768  -2390  -5452    618       N  
ATOM   2191  CA  ARG A1080      -8.194  48.352 -32.939  1.00 80.12           C  
ANISOU 2191  CA  ARG A1080    10006  11994   8442  -2904  -5915    857       C  
ATOM   2192  C   ARG A1080      -8.551  49.389 -34.023  1.00 85.08           C  
ANISOU 2192  C   ARG A1080    10706  12161   9460  -3128  -5910    945       C  
ATOM   2193  O   ARG A1080      -7.739  50.271 -34.313  1.00 85.96           O  
ANISOU 2193  O   ARG A1080    10659  11911  10088  -3559  -6354   1120       O  
ATOM   2194  CB  ARG A1080      -7.024  47.449 -33.384  1.00 81.29           C  
ANISOU 2194  CB  ARG A1080     9530  12497   8857  -3132  -5700   1405       C  
ATOM   2195  CG  ARG A1080      -6.269  46.820 -32.220  1.00 95.74           C  
ANISOU 2195  CG  ARG A1080    11240  14647  10490  -3063  -5997   1364       C  
ATOM   2196  CD  ARG A1080      -5.383  45.660 -32.646  1.00108.43           C  
ANISOU 2196  CD  ARG A1080    12272  16686  12242  -3112  -5612   1889       C  
ATOM   2197  NE  ARG A1080      -5.009  44.817 -31.505  1.00119.24           N  
ANISOU 2197  NE  ARG A1080    13601  18430  13275  -2888  -5740   1828       N  
ATOM   2198  CZ  ARG A1080      -3.868  44.919 -30.828  1.00134.37           C  
ANISOU 2198  CZ  ARG A1080    15253  20439  15362  -3103  -6274   1944       C  
ATOM   2199  NH1 ARG A1080      -2.959  45.823 -31.174  1.00122.51           N  
ANISOU 2199  NH1 ARG A1080    13467  18662  14420  -3587  -6744   2146       N  
ATOM   2200  NH2 ARG A1080      -3.623  44.112 -29.804  1.00120.88           N  
ANISOU 2200  NH2 ARG A1080    13532  19105  13290  -2845  -6355   1901       N  
ATOM   2201  N   ASN A1081      -9.771  49.293 -34.599  1.00 80.69           N  
ANISOU 2201  N   ASN A1081    10371  11612   8677  -2842  -5433    854       N  
ATOM   2202  CA  ASN A1081     -10.296  50.213 -35.614  1.00 80.17           C  
ANISOU 2202  CA  ASN A1081    10416  11155   8891  -2960  -5373    931       C  
ATOM   2203  C   ASN A1081     -11.185  51.261 -34.914  1.00 82.85           C  
ANISOU 2203  C   ASN A1081    11348  11078   9053  -2723  -5747    384       C  
ATOM   2204  O   ASN A1081     -12.202  50.901 -34.314  1.00 82.60           O  
ANISOU 2204  O   ASN A1081    11626  11244   8515  -2260  -5529     47       O  
ATOM   2205  CB  ASN A1081     -11.079  49.439 -36.685  1.00 80.45           C  
ANISOU 2205  CB  ASN A1081    10318  11477   8770  -2771  -4662   1166       C  
ATOM   2206  CG  ASN A1081     -11.414  50.260 -37.899  1.00103.92           C  
ANISOU 2206  CG  ASN A1081    13291  14142  12050  -2929  -4564   1384       C  
ATOM   2207  OD1 ASN A1081     -12.431  50.963 -37.947  1.00 97.27           O  
ANISOU 2207  OD1 ASN A1081    12814  13029  11114  -2740  -4602   1126       O  
ATOM   2208  ND2 ASN A1081     -10.561  50.187 -38.908  1.00 96.36           N  
ANISOU 2208  ND2 ASN A1081    11910  13247  11454  -3245  -4417   1901       N  
ATOM   2209  N   ALA A1082     -10.782  52.550 -34.972  1.00 77.92           N  
ANISOU 2209  N   ALA A1082    10871   9871   8863  -3024  -6311    318       N  
ATOM   2210  CA  ALA A1082     -11.466  53.673 -34.312  1.00 76.91           C  
ANISOU 2210  CA  ALA A1082    11343   9242   8638  -2808  -6761   -226       C  
ATOM   2211  C   ALA A1082     -12.879  53.955 -34.810  1.00 78.67           C  
ANISOU 2211  C   ALA A1082    11864   9380   8648  -2423  -6362   -361       C  
ATOM   2212  O   ALA A1082     -13.660  54.583 -34.097  1.00 77.46           O  
ANISOU 2212  O   ALA A1082    12228   8981   8223  -2047  -6577   -860       O  
ATOM   2213  CB  ALA A1082     -10.619  54.930 -34.408  1.00 77.74           C  
ANISOU 2213  CB  ALA A1082    11483   8678   9377  -3291  -7469   -188       C  
ATOM   2214  N   LYS A1083     -13.202  53.490 -36.024  1.00 74.90           N  
ANISOU 2214  N   LYS A1083    11064   9123   8270  -2485  -5796     78       N  
ATOM   2215  CA  LYS A1083     -14.503  53.675 -36.664  1.00 74.33           C  
ANISOU 2215  CA  LYS A1083    11175   9029   8039  -2169  -5404     45       C  
ATOM   2216  C   LYS A1083     -15.494  52.529 -36.385  1.00 77.86           C  
ANISOU 2216  C   LYS A1083    11624  10041   7917  -1712  -4862    -73       C  
ATOM   2217  O   LYS A1083     -16.697  52.729 -36.548  1.00 77.71           O  
ANISOU 2217  O   LYS A1083    11821  10013   7691  -1361  -4632   -216       O  
ATOM   2218  CB  LYS A1083     -14.310  53.866 -38.170  1.00 76.62           C  
ANISOU 2218  CB  LYS A1083    11131   9242   8737  -2488  -5149    591       C  
ATOM   2219  CG  LYS A1083     -15.172  54.963 -38.765  1.00 89.14           C  
ANISOU 2219  CG  LYS A1083    12998  10391  10480  -2370  -5189    558       C  
ATOM   2220  CD  LYS A1083     -14.823  55.164 -40.225  1.00 98.22           C  
ANISOU 2220  CD  LYS A1083    13804  11497  12019  -2701  -4974   1154       C  
ATOM   2221  CE  LYS A1083     -15.695  56.187 -40.905  1.00107.59           C  
ANISOU 2221  CE  LYS A1083    15239  12277  13363  -2575  -4994   1190       C  
ATOM   2222  NZ  LYS A1083     -15.532  56.135 -42.384  1.00115.11           N  
ANISOU 2222  NZ  LYS A1083    15847  13371  14518  -2780  -4649   1793       N  
ATOM   2223  N   LEU A1084     -14.992  51.343 -35.962  1.00 73.90           N  
ANISOU 2223  N   LEU A1084    10862  10013   7202  -1720  -4674     21       N  
ATOM   2224  CA  LEU A1084     -15.797  50.146 -35.667  1.00 73.27           C  
ANISOU 2224  CA  LEU A1084    10725  10451   6664  -1355  -4182    -11       C  
ATOM   2225  C   LEU A1084     -15.898  49.796 -34.174  1.00 77.80           C  
ANISOU 2225  C   LEU A1084    11522  11249   6790  -1017  -4324   -361       C  
ATOM   2226  O   LEU A1084     -16.756  48.995 -33.792  1.00 77.43           O  
ANISOU 2226  O   LEU A1084    11485  11577   6357   -654  -3943   -400       O  
ATOM   2227  CB  LEU A1084     -15.263  48.935 -36.446  1.00 72.94           C  
ANISOU 2227  CB  LEU A1084    10217  10783   6714  -1565  -3775    416       C  
ATOM   2228  CG  LEU A1084     -15.380  48.990 -37.954  1.00 77.20           C  
ANISOU 2228  CG  LEU A1084    10544  11266   7521  -1762  -3495    766       C  
ATOM   2229  CD1 LEU A1084     -14.389  48.065 -38.586  1.00 77.28           C  
ANISOU 2229  CD1 LEU A1084    10135  11548   7678  -2007  -3268   1151       C  
ATOM   2230  CD2 LEU A1084     -16.790  48.653 -38.414  1.00 79.49           C  
ANISOU 2230  CD2 LEU A1084    10927  11704   7574  -1458  -3107    715       C  
ATOM   2231  N   LYS A1085     -15.013  50.368 -33.339  1.00 74.55           N  
ANISOU 2231  N   LYS A1085    11270  10625   6430  -1140  -4883   -582       N  
ATOM   2232  CA  LYS A1085     -14.986  50.128 -31.896  1.00 74.31           C  
ANISOU 2232  CA  LYS A1085    11490  10815   5929   -809  -5097   -929       C  
ATOM   2233  C   LYS A1085     -16.235  50.685 -31.157  1.00 79.88           C  
ANISOU 2233  C   LYS A1085    12698  11475   6179   -228  -5081  -1374       C  
ATOM   2234  O   LYS A1085     -16.787  49.931 -30.351  1.00 79.24           O  
ANISOU 2234  O   LYS A1085    12665  11851   5593    190  -4802  -1445       O  
ATOM   2235  CB  LYS A1085     -13.667  50.646 -31.278  1.00 76.36           C  
ANISOU 2235  CB  LYS A1085    11787  10836   6390  -1128  -5781  -1058       C  
ATOM   2236  CG  LYS A1085     -13.477  50.321 -29.796  1.00 84.59           C  
ANISOU 2236  CG  LYS A1085    13068  12164   6907   -802  -6052  -1393       C  
ATOM   2237  CD  LYS A1085     -12.469  51.240 -29.124  1.00 87.95           C  
ANISOU 2237  CD  LYS A1085    13706  12201   7512  -1055  -6890  -1689       C  
ATOM   2238  CE  LYS A1085     -12.518  51.110 -27.618  1.00 96.66           C  
ANISOU 2238  CE  LYS A1085    15193  13565   7970   -611  -7201  -2135       C  
ATOM   2239  NZ  LYS A1085     -11.416  51.864 -26.945  1.00104.46           N  
ANISOU 2239  NZ  LYS A1085    16351  14206   9133   -903  -8093  -2422       N  
ATOM   2240  N   PRO A1086     -16.710  51.953 -31.374  1.00 78.51           N  
ANISOU 2240  N   PRO A1086    12889  10786   6155   -147  -5347  -1644       N  
ATOM   2241  CA  PRO A1086     -17.876  52.436 -30.601  1.00 78.92           C  
ANISOU 2241  CA  PRO A1086    13416  10844   5725    496  -5300  -2069       C  
ATOM   2242  C   PRO A1086     -19.173  51.687 -30.884  1.00 83.08           C  
ANISOU 2242  C   PRO A1086    13773  11817   5977    875  -4600  -1860       C  
ATOM   2243  O   PRO A1086     -19.953  51.462 -29.960  1.00 84.03           O  
ANISOU 2243  O   PRO A1086    14099  12268   5563   1438  -4410  -2063       O  
ATOM   2244  CB  PRO A1086     -17.986  53.919 -30.987  1.00 80.84           C  
ANISOU 2244  CB  PRO A1086    14029  10370   6318    432  -5734  -2327       C  
ATOM   2245  CG  PRO A1086     -16.684  54.267 -31.615  1.00 85.20           C  
ANISOU 2245  CG  PRO A1086    14343  10534   7494   -266  -6153  -2093       C  
ATOM   2246  CD  PRO A1086     -16.216  53.014 -32.278  1.00 80.46           C  
ANISOU 2246  CD  PRO A1086    13139  10422   7009   -589  -5696  -1553       C  
ATOM   2247  N   VAL A1087     -19.383  51.280 -32.145  1.00 78.03           N  
ANISOU 2247  N   VAL A1087    12743  11214   5692    573  -4231  -1436       N  
ATOM   2248  CA  VAL A1087     -20.575  50.544 -32.563  1.00 77.12           C  
ANISOU 2248  CA  VAL A1087    12407  11477   5417    830  -3633  -1200       C  
ATOM   2249  C   VAL A1087     -20.553  49.095 -31.999  1.00 80.83           C  
ANISOU 2249  C   VAL A1087    12590  12538   5583    926  -3274   -992       C  
ATOM   2250  O   VAL A1087     -21.571  48.660 -31.470  1.00 81.14           O  
ANISOU 2250  O   VAL A1087    12636  12929   5263   1370  -2932   -985       O  
ATOM   2251  CB  VAL A1087     -20.833  50.634 -34.096  1.00 80.05           C  
ANISOU 2251  CB  VAL A1087    12512  11677   6225    503  -3429   -863       C  
ATOM   2252  CG1 VAL A1087     -19.658  50.113 -34.916  1.00 79.63           C  
ANISOU 2252  CG1 VAL A1087    12106  11611   6539    -67  -3459   -532       C  
ATOM   2253  CG2 VAL A1087     -22.131  49.946 -34.489  1.00 79.63           C  
ANISOU 2253  CG2 VAL A1087    12251  11986   6020    766  -2904   -660       C  
ATOM   2254  N   TYR A1088     -19.394  48.391 -32.040  1.00 76.23           N  
ANISOU 2254  N   TYR A1088    11754  12057   5151    544  -3362   -803       N  
ATOM   2255  CA  TYR A1088     -19.245  47.022 -31.517  1.00 75.36           C  
ANISOU 2255  CA  TYR A1088    11379  12442   4812    611  -3063   -579       C  
ATOM   2256  C   TYR A1088     -19.535  46.918 -30.011  1.00 78.37           C  
ANISOU 2256  C   TYR A1088    12019  13132   4627   1115  -3110   -816       C  
ATOM   2257  O   TYR A1088     -20.208  45.972 -29.598  1.00 78.07           O  
ANISOU 2257  O   TYR A1088    11819  13527   4318   1392  -2693   -613       O  
ATOM   2258  CB  TYR A1088     -17.856  46.443 -31.849  1.00 76.09           C  
ANISOU 2258  CB  TYR A1088    11177  12535   5199    142  -3196   -347       C  
ATOM   2259  CG  TYR A1088     -17.684  44.985 -31.474  1.00 77.26           C  
ANISOU 2259  CG  TYR A1088    11034  13130   5192    192  -2872    -70       C  
ATOM   2260  CD1 TYR A1088     -18.153  43.971 -32.304  1.00 79.19           C  
ANISOU 2260  CD1 TYR A1088    10965  13530   5594    103  -2412    257       C  
ATOM   2261  CD2 TYR A1088     -17.038  44.617 -30.296  1.00 77.84           C  
ANISOU 2261  CD2 TYR A1088    11159  13444   4975    329  -3062   -133       C  
ATOM   2262  CE1 TYR A1088     -17.995  42.627 -31.966  1.00 80.16           C  
ANISOU 2262  CE1 TYR A1088    10840  13984   5633    145  -2139    519       C  
ATOM   2263  CE2 TYR A1088     -16.879  43.276 -29.944  1.00 78.55           C  
ANISOU 2263  CE2 TYR A1088    10979  13919   4948    390  -2761    167       C  
ATOM   2264  CZ  TYR A1088     -17.357  42.283 -30.785  1.00 85.94           C  
ANISOU 2264  CZ  TYR A1088    11610  14949   6093    292  -2296    497       C  
ATOM   2265  OH  TYR A1088     -17.206  40.958 -30.453  1.00 86.68           O  
ANISOU 2265  OH  TYR A1088    11459  15346   6129    349  -2021    798       O  
ATOM   2266  N   ASP A1089     -19.024  47.879 -29.203  1.00 74.23           N  
ANISOU 2266  N   ASP A1089    11897  12382   3924   1235  -3631  -1230       N  
ATOM   2267  CA  ASP A1089     -19.226  47.946 -27.745  1.00 73.71           C  
ANISOU 2267  CA  ASP A1089    12172  12598   3238   1770  -3757  -1534       C  
ATOM   2268  C   ASP A1089     -20.719  48.146 -27.398  1.00 75.38           C  
ANISOU 2268  C   ASP A1089    12567  13021   3052   2395  -3369  -1623       C  
ATOM   2269  O   ASP A1089     -21.187  47.646 -26.370  1.00 74.41           O  
ANISOU 2269  O   ASP A1089    12506  13377   2388   2887  -3138  -1610       O  
ATOM   2270  CB  ASP A1089     -18.407  49.111 -27.137  1.00 75.85           C  
ANISOU 2270  CB  ASP A1089    12900  12458   3462   1738  -4493  -2036       C  
ATOM   2271  CG  ASP A1089     -16.944  48.840 -26.811  1.00 87.76           C  
ANISOU 2271  CG  ASP A1089    14279  13950   5114   1326  -4950  -2003       C  
ATOM   2272  OD1 ASP A1089     -16.674  47.957 -25.957  1.00 87.31           O  
ANISOU 2272  OD1 ASP A1089    14130  14372   4672   1511  -4866  -1900       O  
ATOM   2273  OD2 ASP A1089     -16.072  49.569 -27.338  1.00 95.60           O  
ANISOU 2273  OD2 ASP A1089    15271  14456   6599    845  -5423  -2071       O  
ATOM   2274  N   SER A1090     -21.456  48.879 -28.261  1.00 70.26           N  
ANISOU 2274  N   SER A1090    11974  12044   2676   2392  -3285  -1666       N  
ATOM   2275  CA  SER A1090     -22.869  49.195 -28.064  1.00 69.15           C  
ANISOU 2275  CA  SER A1090    11967  12066   2243   2974  -2936  -1724       C  
ATOM   2276  C   SER A1090     -23.821  48.085 -28.481  1.00 72.03           C  
ANISOU 2276  C   SER A1090    11841  12877   2648   3022  -2292  -1217       C  
ATOM   2277  O   SER A1090     -24.928  48.010 -27.947  1.00 72.03           O  
ANISOU 2277  O   SER A1090    11853  13218   2296   3571  -1939  -1163       O  
ATOM   2278  CB  SER A1090     -23.236  50.505 -28.756  1.00 71.89           C  
ANISOU 2278  CB  SER A1090    12593  11851   2872   2983  -3168  -1982       C  
ATOM   2279  OG  SER A1090     -23.035  50.438 -30.154  1.00 79.27           O  
ANISOU 2279  OG  SER A1090    13205  12505   4409   2405  -3128  -1683       O  
ATOM   2280  N   LEU A1091     -23.419  47.242 -29.446  1.00 67.23           N  
ANISOU 2280  N   LEU A1091    10803  12259   2482   2467  -2150   -841       N  
ATOM   2281  CA  LEU A1091     -24.274  46.158 -29.934  1.00 66.38           C  
ANISOU 2281  CA  LEU A1091    10239  12486   2498   2429  -1628   -381       C  
ATOM   2282  C   LEU A1091     -24.301  44.950 -28.994  1.00 69.61           C  
ANISOU 2282  C   LEU A1091    10438  13412   2601   2614  -1339   -108       C  
ATOM   2283  O   LEU A1091     -23.327  44.705 -28.283  1.00 68.88           O  
ANISOU 2283  O   LEU A1091    10450  13396   2324   2570  -1556   -196       O  
ATOM   2284  CB  LEU A1091     -23.867  45.721 -31.355  1.00 66.14           C  
ANISOU 2284  CB  LEU A1091     9893  12216   3021   1817  -1611   -135       C  
ATOM   2285  CG  LEU A1091     -23.972  46.761 -32.485  1.00 70.10           C  
ANISOU 2285  CG  LEU A1091    10503  12266   3867   1608  -1802   -254       C  
ATOM   2286  CD1 LEU A1091     -23.133  46.346 -33.675  1.00 69.78           C  
ANISOU 2286  CD1 LEU A1091    10218  12035   4259   1026  -1857    -47       C  
ATOM   2287  CD2 LEU A1091     -25.427  47.053 -32.875  1.00 71.35           C  
ANISOU 2287  CD2 LEU A1091    10592  12500   4018   1911  -1528   -166       C  
ATOM   2288  N   ASP A1092     -25.424  44.198 -29.001  1.00 65.44           N  
ANISOU 2288  N   ASP A1092     9583  13233   2049   2808   -863    265       N  
ATOM   2289  CA  ASP A1092     -25.622  42.969 -28.224  1.00 64.36           C  
ANISOU 2289  CA  ASP A1092     9168  13575   1712   2962   -521    652       C  
ATOM   2290  C   ASP A1092     -24.960  41.790 -28.951  1.00 65.52           C  
ANISOU 2290  C   ASP A1092     8964  13632   2298   2398   -471    966       C  
ATOM   2291  O   ASP A1092     -24.581  41.935 -30.108  1.00 65.47           O  
ANISOU 2291  O   ASP A1092     8906  13262   2708   1958   -627    903       O  
ATOM   2292  CB  ASP A1092     -27.121  42.704 -27.989  1.00 66.68           C  
ANISOU 2292  CB  ASP A1092     9207  14240   1887   3367    -52    979       C  
ATOM   2293  CG  ASP A1092     -27.950  42.572 -29.253  1.00 83.58           C  
ANISOU 2293  CG  ASP A1092    11024  16204   4530   3070     97   1194       C  
ATOM   2294  OD1 ASP A1092     -28.168  43.601 -29.929  1.00 85.90           O  
ANISOU 2294  OD1 ASP A1092    11506  16187   4945   3058    -87    920       O  
ATOM   2295  OD2 ASP A1092     -28.387  41.439 -29.561  1.00 90.26           O  
ANISOU 2295  OD2 ASP A1092    11436  17205   5654   2850    368   1641       O  
ATOM   2296  N   ALA A1093     -24.838  40.633 -28.285  1.00 60.09           N  
ANISOU 2296  N   ALA A1093     8049  13278   1506   2452   -242   1316       N  
ATOM   2297  CA  ALA A1093     -24.196  39.417 -28.795  1.00 59.07           C  
ANISOU 2297  CA  ALA A1093     7621  13071   1752   2012   -179   1617       C  
ATOM   2298  C   ALA A1093     -24.634  38.984 -30.185  1.00 61.06           C  
ANISOU 2298  C   ALA A1093     7609  13051   2541   1602    -77   1769       C  
ATOM   2299  O   ALA A1093     -23.785  38.557 -30.968  1.00 62.16           O  
ANISOU 2299  O   ALA A1093     7688  12934   2994   1200   -207   1758       O  
ATOM   2300  CB  ALA A1093     -24.378  38.274 -27.814  1.00 59.87           C  
ANISOU 2300  CB  ALA A1093     7496  13583   1669   2229    126   2049       C  
ATOM   2301  N   VAL A1094     -25.938  39.102 -30.497  1.00 54.60           N  
ANISOU 2301  N   VAL A1094     6631  12308   1805   1731    142   1909       N  
ATOM   2302  CA  VAL A1094     -26.506  38.732 -31.804  1.00 53.09           C  
ANISOU 2302  CA  VAL A1094     6198  11890   2084   1376    195   2038       C  
ATOM   2303  C   VAL A1094     -26.069  39.729 -32.885  1.00 52.53           C  
ANISOU 2303  C   VAL A1094     6352  11445   2160   1141   -101   1677       C  
ATOM   2304  O   VAL A1094     -25.589  39.303 -33.933  1.00 51.54           O  
ANISOU 2304  O   VAL A1094     6152  11078   2355    750   -187   1685       O  
ATOM   2305  CB  VAL A1094     -28.059  38.561 -31.764  1.00 57.24           C  
ANISOU 2305  CB  VAL A1094     6427  12647   2675   1580    484   2347       C  
ATOM   2306  CG1 VAL A1094     -28.608  38.079 -33.106  1.00 57.06           C  
ANISOU 2306  CG1 VAL A1094     6150  12389   3144   1179    462   2473       C  
ATOM   2307  CG2 VAL A1094     -28.496  37.618 -30.645  1.00 57.06           C  
ANISOU 2307  CG2 VAL A1094     6144  13023   2512   1829    808   2791       C  
ATOM   2308  N   ARG A1095     -26.237  41.045 -32.624  1.00 46.98           N  
ANISOU 2308  N   ARG A1095     5938  10695   1218   1410   -249   1379       N  
ATOM   2309  CA  ARG A1095     -25.890  42.129 -33.551  1.00 46.17           C  
ANISOU 2309  CA  ARG A1095     6058  10226   1260   1230   -531   1086       C  
ATOM   2310  C   ARG A1095     -24.386  42.291 -33.773  1.00 49.99           C  
ANISOU 2310  C   ARG A1095     6701  10464   1827    918   -822    911       C  
ATOM   2311  O   ARG A1095     -23.975  42.819 -34.811  1.00 49.96           O  
ANISOU 2311  O   ARG A1095     6755  10164   2064    636   -997    819       O  
ATOM   2312  CB  ARG A1095     -26.527  43.456 -33.129  1.00 45.03           C  
ANISOU 2312  CB  ARG A1095     6189  10052    868   1642   -613    834       C  
ATOM   2313  CG  ARG A1095     -28.019  43.514 -33.387  1.00 51.46           C  
ANISOU 2313  CG  ARG A1095     6793  11035   1726   1881   -356   1027       C  
ATOM   2314  CD  ARG A1095     -28.583  44.870 -33.041  1.00 56.76           C  
ANISOU 2314  CD  ARG A1095     7763  11636   2169   2330   -437    760       C  
ATOM   2315  NE  ARG A1095     -30.021  44.906 -33.272  1.00 60.79           N  
ANISOU 2315  NE  ARG A1095     8009  12356   2731   2591   -168    998       N  
ATOM   2316  CZ  ARG A1095     -30.932  44.681 -32.337  1.00 74.70           C  
ANISOU 2316  CZ  ARG A1095     9618  14540   4224   3071    151   1196       C  
ATOM   2317  NH1 ARG A1095     -30.563  44.402 -31.095  1.00 57.91           N  
ANISOU 2317  NH1 ARG A1095     7620  12681   1704   3369    246   1164       N  
ATOM   2318  NH2 ARG A1095     -32.220  44.728 -32.638  1.00 67.55           N  
ANISOU 2318  NH2 ARG A1095     8405  13828   3432   3272    383   1463       N  
ATOM   2319  N   ARG A1096     -23.571  41.836 -32.804  1.00 45.84           N  
ANISOU 2319  N   ARG A1096     6216  10093   1107    979   -867    915       N  
ATOM   2320  CA  ARG A1096     -22.108  41.853 -32.868  1.00 45.35           C  
ANISOU 2320  CA  ARG A1096     6225   9870   1135    697  -1136    820       C  
ATOM   2321  C   ARG A1096     -21.667  40.836 -33.899  1.00 48.79           C  
ANISOU 2321  C   ARG A1096     6387  10230   1919    323  -1006   1057       C  
ATOM   2322  O   ARG A1096     -20.764  41.124 -34.680  1.00 48.89           O  
ANISOU 2322  O   ARG A1096     6411  10020   2145     30  -1178   1006       O  
ATOM   2323  CB  ARG A1096     -21.489  41.508 -31.499  1.00 46.21           C  
ANISOU 2323  CB  ARG A1096     6408  10236    914    910  -1204    808       C  
ATOM   2324  CG  ARG A1096     -21.435  42.683 -30.548  1.00 51.67           C  
ANISOU 2324  CG  ARG A1096     7480  10910   1243   1230  -1498    446       C  
ATOM   2325  CD  ARG A1096     -20.756  42.338 -29.256  1.00 55.43           C  
ANISOU 2325  CD  ARG A1096     8048  11663   1349   1439  -1619    418       C  
ATOM   2326  NE  ARG A1096     -20.796  43.489 -28.363  1.00 65.81           N  
ANISOU 2326  NE  ARG A1096     9792  12943   2272   1791  -1939      3       N  
ATOM   2327  CZ  ARG A1096     -20.213  43.534 -27.175  1.00 81.65           C  
ANISOU 2327  CZ  ARG A1096    12006  15155   3864   2033  -2176   -157       C  
ATOM   2328  NH1 ARG A1096     -19.518  42.496 -26.731  1.00 76.61           N  
ANISOU 2328  NH1 ARG A1096    11148  14792   3168   1953  -2113    113       N  
ATOM   2329  NH2 ARG A1096     -20.318  44.620 -26.420  1.00 63.76           N  
ANISOU 2329  NH2 ARG A1096    10191  12812   1224   2384  -2502   -600       N  
ATOM   2330  N   ALA A1097     -22.333  39.655 -33.921  1.00 44.35           N  
ANISOU 2330  N   ALA A1097     5582   9844   1427    349   -701   1330       N  
ATOM   2331  CA  ALA A1097     -22.068  38.558 -34.851  1.00 43.47           C  
ANISOU 2331  CA  ALA A1097     5253   9638   1627     59   -574   1522       C  
ATOM   2332  C   ALA A1097     -22.381  38.955 -36.280  1.00 47.37           C  
ANISOU 2332  C   ALA A1097     5751   9902   2345   -157   -618   1445       C  
ATOM   2333  O   ALA A1097     -21.690  38.495 -37.186  1.00 48.26           O  
ANISOU 2333  O   ALA A1097     5808   9881   2648   -395   -629   1477       O  
ATOM   2334  CB  ALA A1097     -22.871  37.337 -34.460  1.00 44.07           C  
ANISOU 2334  CB  ALA A1097     5099   9890   1756    147   -298   1816       C  
ATOM   2335  N   ALA A1098     -23.404  39.818 -36.494  1.00 43.51           N  
ANISOU 2335  N   ALA A1098     5333   9390   1808    -32   -638   1356       N  
ATOM   2336  CA  ALA A1098     -23.781  40.312 -37.834  1.00 43.30           C  
ANISOU 2336  CA  ALA A1098     5321   9176   1953   -197   -702   1302       C  
ATOM   2337  C   ALA A1098     -22.715  41.262 -38.364  1.00 47.78           C  
ANISOU 2337  C   ALA A1098     6064   9530   2561   -356   -926   1156       C  
ATOM   2338  O   ALA A1098     -22.484  41.301 -39.571  1.00 47.66           O  
ANISOU 2338  O   ALA A1098     6023   9389   2695   -560   -949   1189       O  
ATOM   2339  CB  ALA A1098     -25.136  41.004 -37.798  1.00 43.72           C  
ANISOU 2339  CB  ALA A1098     5381   9287   1946     24   -667   1284       C  
ATOM   2340  N   LEU A1099     -22.047  42.006 -37.451  1.00 44.55           N  
ANISOU 2340  N   LEU A1099     5823   9087   2017   -261  -1108   1016       N  
ATOM   2341  CA  LEU A1099     -20.952  42.927 -37.761  1.00 44.24           C  
ANISOU 2341  CA  LEU A1099     5911   8820   2078   -448  -1372    922       C  
ATOM   2342  C   LEU A1099     -19.698  42.119 -38.109  1.00 48.10           C  
ANISOU 2342  C   LEU A1099     6229   9342   2704   -694  -1341   1075       C  
ATOM   2343  O   LEU A1099     -19.014  42.465 -39.070  1.00 47.95           O  
ANISOU 2343  O   LEU A1099     6170   9186   2862   -915  -1404   1151       O  
ATOM   2344  CB  LEU A1099     -20.683  43.886 -36.582  1.00 44.23           C  
ANISOU 2344  CB  LEU A1099     6153   8748   1903   -271  -1640    694       C  
ATOM   2345  CG  LEU A1099     -19.781  45.090 -36.867  1.00 49.18           C  
ANISOU 2345  CG  LEU A1099     6935   9047   2705   -476  -1996    585       C  
ATOM   2346  CD1 LEU A1099     -20.455  46.087 -37.825  1.00 50.68           C  
ANISOU 2346  CD1 LEU A1099     7231   8982   3043   -497  -2040    567       C  
ATOM   2347  CD2 LEU A1099     -19.401  45.785 -35.601  1.00 49.02           C  
ANISOU 2347  CD2 LEU A1099     7169   8951   2506   -316  -2320    320       C  
ATOM   2348  N   ILE A1100     -19.416  41.038 -37.339  1.00 44.34           N  
ANISOU 2348  N   ILE A1100     5637   9068   2144   -621  -1218   1162       N  
ATOM   2349  CA  ILE A1100     -18.305  40.106 -37.548  1.00 43.87           C  
ANISOU 2349  CA  ILE A1100     5398   9068   2202   -773  -1146   1326       C  
ATOM   2350  C   ILE A1100     -18.501  39.410 -38.906  1.00 49.84           C  
ANISOU 2350  C   ILE A1100     6047   9774   3116   -893   -940   1435       C  
ATOM   2351  O   ILE A1100     -17.534  39.290 -39.660  1.00 50.96           O  
ANISOU 2351  O   ILE A1100     6104   9878   3380  -1040   -926   1530       O  
ATOM   2352  CB  ILE A1100     -18.173  39.107 -36.364  1.00 46.44           C  
ANISOU 2352  CB  ILE A1100     5644   9610   2391   -610  -1053   1415       C  
ATOM   2353  CG1 ILE A1100     -17.750  39.829 -35.077  1.00 46.35           C  
ANISOU 2353  CG1 ILE A1100     5773   9674   2164   -481  -1317   1278       C  
ATOM   2354  CG2 ILE A1100     -17.195  37.972 -36.681  1.00 47.11           C  
ANISOU 2354  CG2 ILE A1100     5531   9740   2627   -715   -923   1612       C  
ATOM   2355  CD1 ILE A1100     -18.158  39.105 -33.770  1.00 53.38           C  
ANISOU 2355  CD1 ILE A1100     6659  10839   2783   -194  -1203   1345       C  
ATOM   2356  N   ASN A1101     -19.760  39.018 -39.242  1.00 46.29           N  
ANISOU 2356  N   ASN A1101     5599   9334   2654   -818   -800   1422       N  
ATOM   2357  CA  ASN A1101     -20.143  38.404 -40.532  1.00 45.98           C  
ANISOU 2357  CA  ASN A1101     5513   9231   2725   -913   -679   1458       C  
ATOM   2358  C   ASN A1101     -19.720  39.305 -41.699  1.00 49.29           C  
ANISOU 2358  C   ASN A1101     6002   9548   3178  -1037   -765   1439       C  
ATOM   2359  O   ASN A1101     -19.176  38.803 -42.681  1.00 48.94           O  
ANISOU 2359  O   ASN A1101     5921   9498   3174  -1107   -674   1498       O  
ATOM   2360  CB  ASN A1101     -21.662  38.178 -40.585  1.00 46.19           C  
ANISOU 2360  CB  ASN A1101     5518   9278   2755   -836   -622   1445       C  
ATOM   2361  CG  ASN A1101     -22.143  37.262 -41.682  1.00 60.27           C  
ANISOU 2361  CG  ASN A1101     7252  10991   4655   -932   -557   1459       C  
ATOM   2362  OD1 ASN A1101     -21.816  37.416 -42.856  1.00 58.69           O  
ANISOU 2362  OD1 ASN A1101     7122  10723   4453  -1018   -590   1407       O  
ATOM   2363  ND2 ASN A1101     -22.960  36.294 -41.325  1.00 50.70           N  
ANISOU 2363  ND2 ASN A1101     5921   9796   3547   -913   -481   1540       N  
ATOM   2364  N   MET A1102     -19.963  40.630 -41.576  1.00 45.97           N  
ANISOU 2364  N   MET A1102     5693   9045   2730  -1030   -932   1371       N  
ATOM   2365  CA  MET A1102     -19.623  41.656 -42.566  1.00 45.82           C  
ANISOU 2365  CA  MET A1102     5734   8904   2773  -1147  -1032   1415       C  
ATOM   2366  C   MET A1102     -18.112  41.834 -42.696  1.00 51.30           C  
ANISOU 2366  C   MET A1102     6337   9583   3571  -1300  -1075   1556       C  
ATOM   2367  O   MET A1102     -17.633  42.118 -43.796  1.00 51.49           O  
ANISOU 2367  O   MET A1102     6318   9595   3650  -1398  -1028   1705       O  
ATOM   2368  CB  MET A1102     -20.283  42.993 -42.211  1.00 47.79           C  
ANISOU 2368  CB  MET A1102     6139   9007   3012  -1076  -1221   1311       C  
ATOM   2369  CG  MET A1102     -21.745  43.059 -42.559  1.00 50.84           C  
ANISOU 2369  CG  MET A1102     6562   9420   3336   -938  -1167   1259       C  
ATOM   2370  SD  MET A1102     -22.508  44.637 -42.121  1.00 54.51           S  
ANISOU 2370  SD  MET A1102     7224   9701   3786   -765  -1361   1137       S  
ATOM   2371  CE  MET A1102     -21.823  45.709 -43.379  1.00 51.02           C  
ANISOU 2371  CE  MET A1102     6848   9031   3508   -971  -1503   1281       C  
ATOM   2372  N   VAL A1103     -17.371  41.683 -41.577  1.00 47.98           N  
ANISOU 2372  N   VAL A1103     5864   9196   3170  -1305  -1166   1545       N  
ATOM   2373  CA  VAL A1103     -15.907  41.787 -41.527  1.00 48.24           C  
ANISOU 2373  CA  VAL A1103     5742   9247   3342  -1459  -1241   1714       C  
ATOM   2374  C   VAL A1103     -15.269  40.582 -42.261  1.00 52.93           C  
ANISOU 2374  C   VAL A1103     6159  10006   3946  -1438   -963   1882       C  
ATOM   2375  O   VAL A1103     -14.272  40.752 -42.966  1.00 52.03           O  
ANISOU 2375  O   VAL A1103     5893   9935   3941  -1539   -912   2099       O  
ATOM   2376  CB  VAL A1103     -15.401  41.954 -40.062  1.00 52.07           C  
ANISOU 2376  CB  VAL A1103     6235   9741   3810  -1445  -1474   1627       C  
ATOM   2377  CG1 VAL A1103     -13.888  41.779 -39.952  1.00 51.95           C  
ANISOU 2377  CG1 VAL A1103     5980   9800   3958  -1602  -1548   1841       C  
ATOM   2378  CG2 VAL A1103     -15.822  43.302 -39.484  1.00 51.77           C  
ANISOU 2378  CG2 VAL A1103     6421   9487   3762  -1445  -1792   1431       C  
ATOM   2379  N   PHE A1104     -15.862  39.380 -42.102  1.00 50.82           N  
ANISOU 2379  N   PHE A1104     5912   9817   3579  -1290   -782   1800       N  
ATOM   2380  CA  PHE A1104     -15.411  38.148 -42.751  1.00 51.71           C  
ANISOU 2380  CA  PHE A1104     5933  10020   3695  -1214   -538   1888       C  
ATOM   2381  C   PHE A1104     -15.611  38.186 -44.286  1.00 59.09           C  
ANISOU 2381  C   PHE A1104     6932  10952   4568  -1201   -408   1903       C  
ATOM   2382  O   PHE A1104     -14.852  37.536 -45.012  1.00 60.58           O  
ANISOU 2382  O   PHE A1104     7052  11231   4736  -1117   -221   2004       O  
ATOM   2383  CB  PHE A1104     -16.136  36.933 -42.155  1.00 53.49           C  
ANISOU 2383  CB  PHE A1104     6192  10244   3887  -1086   -438   1795       C  
ATOM   2384  CG  PHE A1104     -15.480  36.260 -40.974  1.00 55.49           C  
ANISOU 2384  CG  PHE A1104     6325  10582   4176  -1020   -430   1888       C  
ATOM   2385  CD1 PHE A1104     -15.287  36.944 -39.778  1.00 59.20           C  
ANISOU 2385  CD1 PHE A1104     6782  11111   4601  -1040   -629   1883       C  
ATOM   2386  CD2 PHE A1104     -15.149  34.911 -41.019  1.00 58.21           C  
ANISOU 2386  CD2 PHE A1104     6604  10932   4580   -908   -247   1962       C  
ATOM   2387  CE1 PHE A1104     -14.707  36.310 -38.671  1.00 59.96           C  
ANISOU 2387  CE1 PHE A1104     6775  11327   4680   -953   -642   1982       C  
ATOM   2388  CE2 PHE A1104     -14.585  34.273 -39.904  1.00 61.22           C  
ANISOU 2388  CE2 PHE A1104     6868  11401   4992   -825   -240   2090       C  
ATOM   2389  CZ  PHE A1104     -14.353  34.984 -38.743  1.00 59.09           C  
ANISOU 2389  CZ  PHE A1104     6561  11245   4645   -850   -437   2113       C  
ATOM   2390  N   GLN A1105     -16.618  38.945 -44.778  1.00 55.39           N  
ANISOU 2390  N   GLN A1105     6603  10404   4040  -1238   -503   1809       N  
ATOM   2391  CA  GLN A1105     -16.923  39.077 -46.207  1.00 54.75           C  
ANISOU 2391  CA  GLN A1105     6607  10351   3845  -1206   -423   1824       C  
ATOM   2392  C   GLN A1105     -16.176  40.235 -46.873  1.00 58.62           C  
ANISOU 2392  C   GLN A1105     7031  10872   4372  -1303   -445   2060       C  
ATOM   2393  O   GLN A1105     -15.489  40.005 -47.861  1.00 58.69           O  
ANISOU 2393  O   GLN A1105     6980  11022   4297  -1236   -265   2224       O  
ATOM   2394  CB  GLN A1105     -18.444  39.217 -46.420  1.00 55.86           C  
ANISOU 2394  CB  GLN A1105     6896  10414   3915  -1185   -525   1644       C  
ATOM   2395  CG  GLN A1105     -18.899  39.166 -47.879  1.00 58.75           C  
ANISOU 2395  CG  GLN A1105     7375  10833   4115  -1127   -487   1619       C  
ATOM   2396  CD  GLN A1105     -20.369  39.469 -48.070  1.00 68.28           C  
ANISOU 2396  CD  GLN A1105     8671  11983   5287  -1128   -639   1494       C  
ATOM   2397  OE1 GLN A1105     -21.152  39.558 -47.120  1.00 65.50           O  
ANISOU 2397  OE1 GLN A1105     8285  11564   5037  -1142   -726   1421       O  
ATOM   2398  NE2 GLN A1105     -20.781  39.629 -49.318  1.00 55.76           N  
ANISOU 2398  NE2 GLN A1105     7186  10463   3537  -1083   -666   1492       N  
ATOM   2399  N   MET A1106     -16.337  41.467 -46.354  1.00 55.63           N  
ANISOU 2399  N   MET A1106     6668  10351   4119  -1435   -662   2090       N  
ATOM   2400  CA  MET A1106     -15.768  42.705 -46.899  1.00 56.18           C  
ANISOU 2400  CA  MET A1106     6677  10358   4310  -1576   -747   2344       C  
ATOM   2401  C   MET A1106     -14.366  43.064 -46.399  1.00 62.17           C  
ANISOU 2401  C   MET A1106     7206  11111   5303  -1742   -819   2585       C  
ATOM   2402  O   MET A1106     -13.531  43.521 -47.177  1.00 62.78           O  
ANISOU 2402  O   MET A1106     7115  11256   5481  -1833   -743   2923       O  
ATOM   2403  CB  MET A1106     -16.712  43.885 -46.627  1.00 58.65           C  
ANISOU 2403  CB  MET A1106     7158  10441   4686  -1623   -989   2237       C  
ATOM   2404  CG  MET A1106     -18.032  43.822 -47.387  1.00 62.69           C  
ANISOU 2404  CG  MET A1106     7828  10979   5012  -1487   -944   2114       C  
ATOM   2405  SD  MET A1106     -19.458  44.299 -46.375  1.00 67.19           S  
ANISOU 2405  SD  MET A1106     8561  11381   5587  -1389  -1138   1830       S  
ATOM   2406  CE  MET A1106     -19.038  45.956 -45.984  1.00 63.93           C  
ANISOU 2406  CE  MET A1106     8224  10664   5401  -1506  -1405   1921       C  
ATOM   2407  N   GLY A1107     -14.147  42.922 -45.104  1.00 59.87           N  
ANISOU 2407  N   GLY A1107     6893  10755   5099  -1784   -984   2445       N  
ATOM   2408  CA  GLY A1107     -12.892  43.285 -44.462  1.00 60.29           C  
ANISOU 2408  CA  GLY A1107     6727  10788   5392  -1966  -1151   2635       C  
ATOM   2409  C   GLY A1107     -13.083  44.383 -43.438  1.00 65.21           C  
ANISOU 2409  C   GLY A1107     7488  11131   6158  -2104  -1558   2471       C  
ATOM   2410  O   GLY A1107     -14.201  44.853 -43.228  1.00 64.69           O  
ANISOU 2410  O   GLY A1107     7687  10906   5987  -2011  -1657   2220       O  
ATOM   2411  N   GLU A1108     -11.990  44.805 -42.798  1.00 62.96           N  
ANISOU 2411  N   GLU A1108     7026  10781   6116  -2309  -1817   2606       N  
ATOM   2412  CA  GLU A1108     -12.009  45.848 -41.778  1.00 63.38           C  
ANISOU 2412  CA  GLU A1108     7244  10531   6308  -2440  -2282   2408       C  
ATOM   2413  C   GLU A1108     -12.428  47.215 -42.326  1.00 67.53           C  
ANISOU 2413  C   GLU A1108     7931  10706   7022  -2572  -2479   2443       C  
ATOM   2414  O   GLU A1108     -13.377  47.800 -41.806  1.00 66.89           O  
ANISOU 2414  O   GLU A1108     8177  10398   6839  -2448  -2666   2114       O  
ATOM   2415  CB  GLU A1108     -10.642  45.952 -41.103  1.00 65.10           C  
ANISOU 2415  CB  GLU A1108     7195  10758   6782  -2672  -2567   2578       C  
ATOM   2416  CG  GLU A1108     -10.731  46.172 -39.610  1.00 77.54           C  
ANISOU 2416  CG  GLU A1108     8989  12207   8267  -2634  -2979   2211       C  
ATOM   2417  CD  GLU A1108     -10.461  44.897 -38.846  1.00103.02           C  
ANISOU 2417  CD  GLU A1108    12102  15772  11268  -2455  -2844   2161       C  
ATOM   2418  OE1 GLU A1108      -9.306  44.416 -38.887  1.00 98.45           O  
ANISOU 2418  OE1 GLU A1108    11167  15369  10871  -2593  -2853   2456       O  
ATOM   2419  OE2 GLU A1108     -11.403  44.367 -38.216  1.00101.74           O  
ANISOU 2419  OE2 GLU A1108    12176  15711  10768  -2167  -2714   1878       O  
ATOM   2420  N   THR A1109     -11.720  47.719 -43.365  1.00 64.37           N  
ANISOU 2420  N   THR A1109     7291  10274   6895  -2791  -2418   2876       N  
ATOM   2421  CA  THR A1109     -11.973  49.021 -43.997  1.00 64.44           C  
ANISOU 2421  CA  THR A1109     7398   9939   7149  -2945  -2589   3033       C  
ATOM   2422  C   THR A1109     -13.323  49.101 -44.744  1.00 68.38           C  
ANISOU 2422  C   THR A1109     8162  10439   7383  -2695  -2365   2897       C  
ATOM   2423  O   THR A1109     -13.909  50.186 -44.812  1.00 67.50           O  
ANISOU 2423  O   THR A1109     8274   9975   7399  -2716  -2588   2828       O  
ATOM   2424  CB  THR A1109     -10.805  49.421 -44.902  1.00 73.91           C  
ANISOU 2424  CB  THR A1109     8199  11180   8703  -3231  -2526   3634       C  
ATOM   2425  OG1 THR A1109     -10.470  48.313 -45.741  1.00 76.23           O  
ANISOU 2425  OG1 THR A1109     8249  11951   8764  -3064  -2029   3878       O  
ATOM   2426  CG2 THR A1109      -9.581  49.892 -44.116  1.00 70.10           C  
ANISOU 2426  CG2 THR A1109     7466  10520   8650  -3581  -2941   3796       C  
ATOM   2427  N   GLY A1110     -13.789  47.967 -45.284  1.00 65.37           N  
ANISOU 2427  N   GLY A1110     7753  10424   6661  -2462  -1966   2858       N  
ATOM   2428  CA  GLY A1110     -15.056  47.851 -46.010  1.00 65.06           C  
ANISOU 2428  CA  GLY A1110     7915  10448   6358  -2234  -1775   2734       C  
ATOM   2429  C   GLY A1110     -16.278  48.179 -45.171  1.00 68.65           C  
ANISOU 2429  C   GLY A1110     8676  10707   6700  -2059  -1957   2322       C  
ATOM   2430  O   GLY A1110     -17.109  48.996 -45.579  1.00 67.81           O  
ANISOU 2430  O   GLY A1110     8741  10412   6611  -1988  -2032   2304       O  
ATOM   2431  N   VAL A1111     -16.383  47.553 -43.975  1.00 65.54           N  
ANISOU 2431  N   VAL A1111     8338  10384   6181  -1954  -2011   2023       N  
ATOM   2432  CA  VAL A1111     -17.471  47.769 -43.003  1.00 65.36           C  
ANISOU 2432  CA  VAL A1111     8576  10256   6002  -1724  -2137   1652       C  
ATOM   2433  C   VAL A1111     -17.389  49.215 -42.454  1.00 70.86           C  
ANISOU 2433  C   VAL A1111     9491  10521   6910  -1786  -2539   1538       C  
ATOM   2434  O   VAL A1111     -18.427  49.847 -42.229  1.00 70.75           O  
ANISOU 2434  O   VAL A1111     9724  10339   6819  -1568  -2619   1330       O  
ATOM   2435  CB  VAL A1111     -17.477  46.709 -41.864  1.00 68.40           C  
ANISOU 2435  CB  VAL A1111     8938  10869   6182  -1584  -2069   1444       C  
ATOM   2436  CG1 VAL A1111     -18.757  46.785 -41.048  1.00 68.35           C  
ANISOU 2436  CG1 VAL A1111     9151  10867   5953  -1277  -2079   1146       C  
ATOM   2437  CG2 VAL A1111     -17.294  45.301 -42.407  1.00 67.85           C  
ANISOU 2437  CG2 VAL A1111     8655  11125   6002  -1571  -1730   1583       C  
ATOM   2438  N   ALA A1112     -16.147  49.743 -42.291  1.00 67.72           N  
ANISOU 2438  N   ALA A1112     8989   9929   6813  -2082  -2804   1694       N  
ATOM   2439  CA  ALA A1112     -15.855  51.110 -41.835  1.00 67.47           C  
ANISOU 2439  CA  ALA A1112     9154   9405   7077  -2223  -3269   1606       C  
ATOM   2440  C   ALA A1112     -16.340  52.169 -42.841  1.00 70.64           C  
ANISOU 2440  C   ALA A1112     9650   9496   7693  -2265  -3301   1806       C  
ATOM   2441  O   ALA A1112     -16.505  53.335 -42.472  1.00 70.15           O  
ANISOU 2441  O   ALA A1112     9851   8958   7844  -2277  -3669   1658       O  
ATOM   2442  CB  ALA A1112     -14.364  51.270 -41.582  1.00 68.27           C  
ANISOU 2442  CB  ALA A1112     9022   9410   7509  -2593  -3543   1815       C  
ATOM   2443  N   GLY A1113     -16.583  51.742 -44.086  1.00 66.36           N  
ANISOU 2443  N   GLY A1113     8923   9219   7072  -2255  -2933   2123       N  
ATOM   2444  CA  GLY A1113     -17.094  52.583 -45.161  1.00 65.49           C  
ANISOU 2444  CA  GLY A1113     8870   8922   7092  -2253  -2900   2376       C  
ATOM   2445  C   GLY A1113     -18.540  52.979 -44.956  1.00 68.02           C  
ANISOU 2445  C   GLY A1113     9499   9117   7228  -1907  -2921   2069       C  
ATOM   2446  O   GLY A1113     -18.992  53.978 -45.518  1.00 67.66           O  
ANISOU 2446  O   GLY A1113     9582   8772   7354  -1877  -3027   2206       O  
ATOM   2447  N   PHE A1114     -19.269  52.210 -44.132  1.00 64.20           N  
ANISOU 2447  N   PHE A1114     9109   8871   6413  -1628  -2810   1698       N  
ATOM   2448  CA  PHE A1114     -20.671  52.440 -43.797  1.00 64.27           C  
ANISOU 2448  CA  PHE A1114     9344   8855   6219  -1249  -2780   1425       C  
ATOM   2449  C   PHE A1114     -20.825  53.421 -42.627  1.00 70.72           C  
ANISOU 2449  C   PHE A1114    10504   9257   7108  -1080  -3134   1067       C  
ATOM   2450  O   PHE A1114     -21.514  53.112 -41.656  1.00 70.26           O  
ANISOU 2450  O   PHE A1114    10588   9337   6769   -749  -3089    736       O  
ATOM   2451  CB  PHE A1114     -21.347  51.105 -43.464  1.00 65.79           C  
ANISOU 2451  CB  PHE A1114     9420   9522   6055  -1041  -2474   1274       C  
ATOM   2452  CG  PHE A1114     -21.762  50.270 -44.646  1.00 67.08           C  
ANISOU 2452  CG  PHE A1114     9366  10028   6093  -1069  -2170   1506       C  
ATOM   2453  CD1 PHE A1114     -22.888  50.603 -45.391  1.00 69.37           C  
ANISOU 2453  CD1 PHE A1114     9687  10341   6329   -900  -2105   1584       C  
ATOM   2454  CD2 PHE A1114     -21.077  49.106 -44.968  1.00 68.75           C  
ANISOU 2454  CD2 PHE A1114     9359  10542   6219  -1224  -1972   1614       C  
ATOM   2455  CE1 PHE A1114     -23.297  49.805 -46.455  1.00 69.82           C  
ANISOU 2455  CE1 PHE A1114     9575  10716   6236   -918  -1892   1747       C  
ATOM   2456  CE2 PHE A1114     -21.489  48.310 -46.034  1.00 70.71           C  
ANISOU 2456  CE2 PHE A1114     9474  11075   6319  -1212  -1739   1753       C  
ATOM   2457  CZ  PHE A1114     -22.589  48.668 -46.771  1.00 68.68           C  
ANISOU 2457  CZ  PHE A1114     9265  10835   5996  -1073  -1722   1806       C  
ATOM   2458  N   THR A1115     -20.205  54.616 -42.738  1.00 69.58           N  
ANISOU 2458  N   THR A1115    10501   8596   7342  -1288  -3492   1146       N  
ATOM   2459  CA  THR A1115     -20.203  55.696 -41.730  1.00 70.30           C  
ANISOU 2459  CA  THR A1115    10981   8166   7563  -1162  -3930    781       C  
ATOM   2460  C   THR A1115     -21.613  56.032 -41.212  1.00 75.15           C  
ANISOU 2460  C   THR A1115    11903   8750   7902   -611  -3865    439       C  
ATOM   2461  O   THR A1115     -21.817  56.160 -40.004  1.00 74.96           O  
ANISOU 2461  O   THR A1115    12162   8655   7664   -317  -4029      6       O  
ATOM   2462  CB  THR A1115     -19.503  56.950 -42.292  1.00 81.91           C  
ANISOU 2462  CB  THR A1115    12517   9031   9574  -1499  -4298   1034       C  
ATOM   2463  OG1 THR A1115     -18.342  56.567 -43.033  1.00 85.27           O  
ANISOU 2463  OG1 THR A1115    12548   9606  10243  -1968  -4227   1499       O  
ATOM   2464  CG2 THR A1115     -19.116  57.946 -41.202  1.00 80.53           C  
ANISOU 2464  CG2 THR A1115    12733   8256   9608  -1496  -4864    636       C  
ATOM   2465  N   ASN A1116     -22.571  56.169 -42.137  1.00 72.05           N  
ANISOU 2465  N   ASN A1116    11439   8446   7491   -446  -3624    655       N  
ATOM   2466  CA  ASN A1116     -23.968  56.483 -41.857  1.00 71.86           C  
ANISOU 2466  CA  ASN A1116    11609   8445   7249     82  -3512    446       C  
ATOM   2467  C   ASN A1116     -24.672  55.344 -41.097  1.00 75.60           C  
ANISOU 2467  C   ASN A1116    11967   9486   7274    394  -3195    248       C  
ATOM   2468  O   ASN A1116     -25.345  55.598 -40.094  1.00 75.24           O  
ANISOU 2468  O   ASN A1116    12165   9428   6995    844  -3216    -89       O  
ATOM   2469  CB  ASN A1116     -24.715  56.844 -43.164  1.00 71.93           C  
ANISOU 2469  CB  ASN A1116    11491   8459   7382    121  -3353    812       C  
ATOM   2470  CG  ASN A1116     -24.108  56.293 -44.454  1.00 84.74           C  
ANISOU 2470  CG  ASN A1116    12764  10321   9113   -304  -3188   1281       C  
ATOM   2471  OD1 ASN A1116     -24.045  55.075 -44.701  1.00 70.08           O  
ANISOU 2471  OD1 ASN A1116    10629   8970   7027   -405  -2912   1363       O  
ATOM   2472  ND2 ASN A1116     -23.653  57.193 -45.313  1.00 76.54           N  
ANISOU 2472  ND2 ASN A1116    11746   8912   8423   -533  -3351   1610       N  
ATOM   2473  N   SER A1117     -24.495  54.096 -41.579  1.00 71.85           N  
ANISOU 2473  N   SER A1117    11124   9493   6683    167  -2903    477       N  
ATOM   2474  CA  SER A1117     -25.092  52.874 -41.033  1.00 71.43           C  
ANISOU 2474  CA  SER A1117    10882   9967   6293    362  -2592    405       C  
ATOM   2475  C   SER A1117     -24.607  52.553 -39.628  1.00 75.02           C  
ANISOU 2475  C   SER A1117    11475  10492   6538    476  -2678    100       C  
ATOM   2476  O   SER A1117     -25.431  52.220 -38.776  1.00 75.83           O  
ANISOU 2476  O   SER A1117    11613  10858   6339    878  -2509    -63       O  
ATOM   2477  CB  SER A1117     -24.811  51.688 -41.945  1.00 74.66           C  
ANISOU 2477  CB  SER A1117    10925  10741   6703     41  -2346    703       C  
ATOM   2478  OG  SER A1117     -25.135  51.998 -43.288  1.00 83.69           O  
ANISOU 2478  OG  SER A1117    11967  11843   7987    -69  -2304    982       O  
ATOM   2479  N   LEU A1118     -23.275  52.651 -39.383  1.00 69.54           N  
ANISOU 2479  N   LEU A1118    10832   9598   5994    138  -2940     60       N  
ATOM   2480  CA  LEU A1118     -22.644  52.365 -38.084  1.00 67.61           C  
ANISOU 2480  CA  LEU A1118    10717   9420   5550    204  -3095   -217       C  
ATOM   2481  C   LEU A1118     -23.111  53.315 -36.990  1.00 71.59           C  
ANISOU 2481  C   LEU A1118    11669   9666   5866    651  -3345   -644       C  
ATOM   2482  O   LEU A1118     -23.261  52.893 -35.846  1.00 71.30           O  
ANISOU 2482  O   LEU A1118    11744   9888   5459    961  -3304   -883       O  
ATOM   2483  CB  LEU A1118     -21.111  52.384 -38.185  1.00 66.80           C  
ANISOU 2483  CB  LEU A1118    10529   9135   5718   -285  -3375   -119       C  
ATOM   2484  CG  LEU A1118     -20.453  51.369 -39.121  1.00 70.45           C  
ANISOU 2484  CG  LEU A1118    10572   9887   6310   -665  -3121    274       C  
ATOM   2485  CD1 LEU A1118     -19.053  51.798 -39.478  1.00 70.26           C  
ANISOU 2485  CD1 LEU A1118    10448   9593   6655  -1119  -3409    459       C  
ATOM   2486  CD2 LEU A1118     -20.481  49.951 -38.558  1.00 72.12           C  
ANISOU 2486  CD2 LEU A1118    10582  10593   6228   -572  -2834    277       C  
ATOM   2487  N   ARG A1119     -23.348  54.586 -37.347  1.00 69.08           N  
ANISOU 2487  N   ARG A1119    11624   8841   5785    722  -3596   -732       N  
ATOM   2488  CA  ARG A1119     -23.812  55.649 -36.455  1.00 69.73           C  
ANISOU 2488  CA  ARG A1119    12201   8563   5730   1186  -3871  -1171       C  
ATOM   2489  C   ARG A1119     -25.241  55.393 -35.951  1.00 73.98           C  
ANISOU 2489  C   ARG A1119    12777   9491   5841   1839  -3491  -1280       C  
ATOM   2490  O   ARG A1119     -25.539  55.727 -34.802  1.00 74.35           O  
ANISOU 2490  O   ARG A1119    13179   9532   5537   2330  -3589  -1677       O  
ATOM   2491  CB  ARG A1119     -23.748  56.995 -37.190  1.00 71.75           C  
ANISOU 2491  CB  ARG A1119    12679   8147   6435   1060  -4193  -1135       C  
ATOM   2492  CG  ARG A1119     -22.969  58.111 -36.495  1.00 88.07           C  
ANISOU 2492  CG  ARG A1119    15236   9542   8686   1040  -4808  -1537       C  
ATOM   2493  CD  ARG A1119     -22.809  59.353 -37.382  1.00104.03           C  
ANISOU 2493  CD  ARG A1119    17386  10864  11278    787  -5117  -1362       C  
ATOM   2494  NE  ARG A1119     -23.740  59.383 -38.522  1.00115.57           N  
ANISOU 2494  NE  ARG A1119    18612  12467  12832    880  -4731   -967       N  
ATOM   2495  CZ  ARG A1119     -23.852  60.385 -39.391  1.00129.77           C  
ANISOU 2495  CZ  ARG A1119    20486  13757  15062    764  -4886   -733       C  
ATOM   2496  NH1 ARG A1119     -23.099  61.471 -39.265  1.00117.65           N  
ANISOU 2496  NH1 ARG A1119    19255  11476  13971    522  -5426   -838       N  
ATOM   2497  NH2 ARG A1119     -24.727  60.313 -40.386  1.00114.65           N  
ANISOU 2497  NH2 ARG A1119    18340  12065  13156    882  -4533   -372       N  
ATOM   2498  N   MET A1120     -26.113  54.813 -36.800  1.00 69.93           N  
ANISOU 2498  N   MET A1120    11892   9330   5349   1859  -3075   -921       N  
ATOM   2499  CA  MET A1120     -27.510  54.519 -36.457  1.00 70.14           C  
ANISOU 2499  CA  MET A1120    11824   9768   5058   2419  -2689   -900       C  
ATOM   2500  C   MET A1120     -27.664  53.229 -35.662  1.00 73.09           C  
ANISOU 2500  C   MET A1120    11949  10753   5070   2535  -2368   -842       C  
ATOM   2501  O   MET A1120     -28.654  53.083 -34.942  1.00 72.63           O  
ANISOU 2501  O   MET A1120    11886  11032   4679   3079  -2099   -889       O  
ATOM   2502  CB  MET A1120     -28.389  54.479 -37.707  1.00 73.06           C  
ANISOU 2502  CB  MET A1120    11877  10236   5646   2357  -2455   -523       C  
ATOM   2503  CG  MET A1120     -28.659  55.833 -38.296  1.00 77.32           C  
ANISOU 2503  CG  MET A1120    12682  10245   6452   2479  -2685   -559       C  
ATOM   2504  SD  MET A1120     -28.990  55.666 -40.054  1.00 82.27           S  
ANISOU 2504  SD  MET A1120    12913  10938   7409   2092  -2555    -44       S  
ATOM   2505  CE  MET A1120     -28.342  57.214 -40.634  1.00 79.16           C  
ANISOU 2505  CE  MET A1120    12891   9751   7437   1927  -2993    -67       C  
ATOM   2506  N   LEU A1121     -26.697  52.292 -35.803  1.00 69.47           N  
ANISOU 2506  N   LEU A1121    11259  10446   4688   2046  -2373   -694       N  
ATOM   2507  CA  LEU A1121     -26.672  51.022 -35.066  1.00 69.49           C  
ANISOU 2507  CA  LEU A1121    11026  10968   4407   2093  -2105   -599       C  
ATOM   2508  C   LEU A1121     -26.296  51.251 -33.581  1.00 76.18           C  
ANISOU 2508  C   LEU A1121    12230  11858   4855   2455  -2275   -970       C  
ATOM   2509  O   LEU A1121     -26.864  50.604 -32.693  1.00 75.49           O  
ANISOU 2509  O   LEU A1121    12062  12234   4386   2842  -1986   -936       O  
ATOM   2510  CB  LEU A1121     -25.699  50.022 -35.712  1.00 68.86           C  
ANISOU 2510  CB  LEU A1121    10633  10978   4554   1501  -2084   -344       C  
ATOM   2511  CG  LEU A1121     -26.096  49.405 -37.043  1.00 72.35           C  
ANISOU 2511  CG  LEU A1121    10703  11533   5255   1200  -1858     15       C  
ATOM   2512  CD1 LEU A1121     -24.905  48.732 -37.695  1.00 71.91           C  
ANISOU 2512  CD1 LEU A1121    10468  11445   5410    673  -1918    177       C  
ATOM   2513  CD2 LEU A1121     -27.258  48.425 -36.890  1.00 74.16           C  
ANISOU 2513  CD2 LEU A1121    10617  12224   5336   1425  -1468    229       C  
ATOM   2514  N   GLN A1122     -25.343  52.178 -33.322  1.00 74.84           N  
ANISOU 2514  N   GLN A1122    12450  11207   4778   2328  -2766  -1302       N  
ATOM   2515  CA  GLN A1122     -24.912  52.543 -31.972  1.00 75.71           C  
ANISOU 2515  CA  GLN A1122    12979  11281   4507   2658  -3053  -1732       C  
ATOM   2516  C   GLN A1122     -25.938  53.460 -31.309  1.00 81.96           C  
ANISOU 2516  C   GLN A1122    14181  11998   4964   3386  -3038  -2069       C  
ATOM   2517  O   GLN A1122     -25.903  53.638 -30.088  1.00 82.65           O  
ANISOU 2517  O   GLN A1122    14626  12201   4577   3847  -3162  -2431       O  
ATOM   2518  CB  GLN A1122     -23.487  53.149 -31.954  1.00 77.23           C  
ANISOU 2518  CB  GLN A1122    13400  10970   4976   2199  -3649  -1950       C  
ATOM   2519  CG  GLN A1122     -23.347  54.555 -32.538  1.00 95.63           C  
ANISOU 2519  CG  GLN A1122    16042  12586   7709   2072  -4062  -2128       C  
ATOM   2520  CD  GLN A1122     -21.941  55.084 -32.431  1.00118.51           C  
ANISOU 2520  CD  GLN A1122    19094  15011  10923   1584  -4664  -2280       C  
ATOM   2521  OE1 GLN A1122     -21.567  55.734 -31.445  1.00112.62           O  
ANISOU 2521  OE1 GLN A1122    18808  13977  10004   1783  -5137  -2750       O  
ATOM   2522  NE2 GLN A1122     -21.139  54.837 -33.459  1.00113.90           N  
ANISOU 2522  NE2 GLN A1122    18123  14343  10810    946  -4676  -1879       N  
ATOM   2523  N   GLN A1123     -26.846  54.041 -32.118  1.00 79.38           N  
ANISOU 2523  N   GLN A1123    13807  11496   4856   3528  -2884  -1948       N  
ATOM   2524  CA  GLN A1123     -27.925  54.915 -31.664  1.00 80.08           C  
ANISOU 2524  CA  GLN A1123    14225  11518   4683   4259  -2803  -2199       C  
ATOM   2525  C   GLN A1123     -29.214  54.114 -31.408  1.00 86.10           C  
ANISOU 2525  C   GLN A1123    14612  12978   5125   4730  -2180  -1882       C  
ATOM   2526  O   GLN A1123     -30.228  54.695 -31.008  1.00 86.42           O  
ANISOU 2526  O   GLN A1123    14824  13101   4909   5410  -1999  -2001       O  
ATOM   2527  CB  GLN A1123     -28.168  56.039 -32.682  1.00 81.40           C  
ANISOU 2527  CB  GLN A1123    14533  11084   5310   4159  -3009  -2198       C  
ATOM   2528  CG  GLN A1123     -27.292  57.268 -32.449  1.00 98.55           C  
ANISOU 2528  CG  GLN A1123    17278  12489   7678   4058  -3653  -2655       C  
ATOM   2529  CD  GLN A1123     -27.547  58.387 -33.434  1.00121.24           C  
ANISOU 2529  CD  GLN A1123    20293  14739  11032   3983  -3848  -2601       C  
ATOM   2530  OE1 GLN A1123     -28.629  58.514 -34.026  1.00118.24           O  
ANISOU 2530  OE1 GLN A1123    19736  14495  10695   4278  -3512  -2364       O  
ATOM   2531  NE2 GLN A1123     -26.551  59.240 -33.624  1.00113.88           N  
ANISOU 2531  NE2 GLN A1123    19666  13102  10502   3578  -4416  -2784       N  
ATOM   2532  N   LYS A1124     -29.159  52.774 -31.629  1.00 83.13           N  
ANISOU 2532  N   LYS A1124    13710  13085   4790   4373  -1862  -1458       N  
ATOM   2533  CA  LYS A1124     -30.252  51.797 -31.465  1.00 82.93           C  
ANISOU 2533  CA  LYS A1124    13209  13712   4586   4639  -1301  -1044       C  
ATOM   2534  C   LYS A1124     -31.447  52.073 -32.408  1.00 86.12           C  
ANISOU 2534  C   LYS A1124    13324  14135   5263   4750  -1066   -754       C  
ATOM   2535  O   LYS A1124     -32.576  51.665 -32.123  1.00 85.76           O  
ANISOU 2535  O   LYS A1124    12964  14572   5050   5161   -645   -474       O  
ATOM   2536  CB  LYS A1124     -30.695  51.649 -29.988  1.00 85.47           C  
ANISOU 2536  CB  LYS A1124    13698  14504   4271   5363  -1065  -1179       C  
ATOM   2537  CG  LYS A1124     -29.675  50.907 -29.137  1.00102.00           C  
ANISOU 2537  CG  LYS A1124    15858  16802   6094   5191  -1174  -1257       C  
ATOM   2538  CD  LYS A1124     -30.266  50.362 -27.849  1.00112.15           C  
ANISOU 2538  CD  LYS A1124    17107  18743   6763   5850   -785  -1159       C  
ATOM   2539  CE  LYS A1124     -29.525  49.135 -27.368  1.00120.09           C  
ANISOU 2539  CE  LYS A1124    17864  20105   7660   5538   -701   -913       C  
ATOM   2540  NZ  LYS A1124     -28.145  49.448 -26.907  1.00123.97           N  
ANISOU 2540  NZ  LYS A1124    18782  20297   8026   5316  -1229  -1341       N  
ATOM   2541  N   ARG A1125     -31.174  52.740 -33.545  1.00 82.09           N  
ANISOU 2541  N   ARG A1125    12881  13122   5187   4366  -1342   -770       N  
ATOM   2542  CA  ARG A1125     -32.150  53.056 -34.590  1.00 81.70           C  
ANISOU 2542  CA  ARG A1125    12576  13038   5430   4393  -1209   -493       C  
ATOM   2543  C   ARG A1125     -31.884  52.044 -35.702  1.00 84.66           C  
ANISOU 2543  C   ARG A1125    12480  13538   6147   3702  -1150   -107       C  
ATOM   2544  O   ARG A1125     -31.229  52.366 -36.694  1.00 83.75           O  
ANISOU 2544  O   ARG A1125    12421  13045   6355   3234  -1409    -90       O  
ATOM   2545  CB  ARG A1125     -31.965  54.508 -35.080  1.00 81.54           C  
ANISOU 2545  CB  ARG A1125    12991  12359   5631   4462  -1577   -760       C  
ATOM   2546  CG  ARG A1125     -32.296  55.565 -34.031  1.00 86.12           C  
ANISOU 2546  CG  ARG A1125    14098  12744   5880   5209  -1667  -1198       C  
ATOM   2547  CD  ARG A1125     -31.752  56.928 -34.413  1.00 87.58           C  
ANISOU 2547  CD  ARG A1125    14789  12136   6350   5144  -2150  -1516       C  
ATOM   2548  NE  ARG A1125     -32.546  57.575 -35.457  1.00 86.10           N  
ANISOU 2548  NE  ARG A1125    14474  11747   6492   5221  -2100  -1267       N  
ATOM   2549  CZ  ARG A1125     -32.168  58.663 -36.121  1.00 92.96           C  
ANISOU 2549  CZ  ARG A1125    15650  11934   7737   5056  -2473  -1359       C  
ATOM   2550  NH1 ARG A1125     -30.991  59.227 -35.875  1.00 72.71           N  
ANISOU 2550  NH1 ARG A1125    13513   8795   5318   4756  -2945  -1689       N  
ATOM   2551  NH2 ARG A1125     -32.956  59.187 -37.046  1.00 82.40           N  
ANISOU 2551  NH2 ARG A1125    14167  10482   6660   5173  -2396  -1083       N  
ATOM   2552  N   TRP A1126     -32.336  50.791 -35.480  1.00 81.55           N  
ANISOU 2552  N   TRP A1126    11643  13674   5669   3652   -815    205       N  
ATOM   2553  CA  TRP A1126     -32.098  49.641 -36.355  1.00 81.87           C  
ANISOU 2553  CA  TRP A1126    11270  13859   5979   3056   -754    524       C  
ATOM   2554  C   TRP A1126     -32.862  49.681 -37.669  1.00 84.28           C  
ANISOU 2554  C   TRP A1126    11279  14147   6598   2866   -744    798       C  
ATOM   2555  O   TRP A1126     -32.339  49.181 -38.667  1.00 83.46           O  
ANISOU 2555  O   TRP A1126    11045  13939   6728   2340   -862    911       O  
ATOM   2556  CB  TRP A1126     -32.338  48.317 -35.624  1.00 81.38           C  
ANISOU 2556  CB  TRP A1126    10862  14293   5765   3078   -442    766       C  
ATOM   2557  CG  TRP A1126     -31.567  48.201 -34.342  1.00 83.06           C  
ANISOU 2557  CG  TRP A1126    11353  14585   5623   3275   -456    533       C  
ATOM   2558  CD1 TRP A1126     -30.210  48.162 -34.193  1.00 86.09           C  
ANISOU 2558  CD1 TRP A1126    11997  14718   5996   2950   -729    299       C  
ATOM   2559  CD2 TRP A1126     -32.117  48.155 -33.022  1.00 83.32           C  
ANISOU 2559  CD2 TRP A1126    11424  15004   5228   3880   -196    528       C  
ATOM   2560  NE1 TRP A1126     -29.880  48.096 -32.857  1.00 85.61           N  
ANISOU 2560  NE1 TRP A1126    12153  14850   5525   3298   -701    121       N  
ATOM   2561  CE2 TRP A1126     -31.033  48.086 -32.116  1.00 87.22           C  
ANISOU 2561  CE2 TRP A1126    12247  15456   5436   3890   -363    250       C  
ATOM   2562  CE3 TRP A1126     -33.427  48.160 -32.513  1.00 84.96           C  
ANISOU 2562  CE3 TRP A1126    11395  15633   5252   4443    174    765       C  
ATOM   2563  CZ2 TRP A1126     -31.219  48.006 -30.734  1.00 86.92           C  
ANISOU 2563  CZ2 TRP A1126    12349  15790   4886   4456   -179    179       C  
ATOM   2564  CZ3 TRP A1126     -33.612  48.092 -31.141  1.00 86.67           C  
ANISOU 2564  CZ3 TRP A1126    11732  16232   4969   5024    405    724       C  
ATOM   2565  CH2 TRP A1126     -32.518  48.022 -30.266  1.00 87.57           C  
ANISOU 2565  CH2 TRP A1126    12221  16299   4753   5039    223    417       C  
ATOM   2566  N   ASP A1127     -34.076  50.274 -37.689  1.00 79.68           N  
ANISOU 2566  N   ASP A1127    10593  13685   5998   3321   -612    907       N  
ATOM   2567  CA  ASP A1127     -34.860  50.405 -38.927  1.00 78.36           C  
ANISOU 2567  CA  ASP A1127    10143  13519   6110   3186   -646   1174       C  
ATOM   2568  C   ASP A1127     -34.206  51.389 -39.902  1.00 78.57           C  
ANISOU 2568  C   ASP A1127    10492  13038   6325   2953   -975   1031       C  
ATOM   2569  O   ASP A1127     -34.225  51.156 -41.110  1.00 77.43           O  
ANISOU 2569  O   ASP A1127    10161  12864   6394   2574  -1079   1228       O  
ATOM   2570  CB  ASP A1127     -36.355  50.729 -38.671  1.00 80.47           C  
ANISOU 2570  CB  ASP A1127    10147  14098   6331   3759   -405   1388       C  
ATOM   2571  CG  ASP A1127     -36.700  51.733 -37.573  1.00 93.57           C  
ANISOU 2571  CG  ASP A1127    12146  15720   7686   4493   -295   1143       C  
ATOM   2572  OD1 ASP A1127     -36.391  51.455 -36.386  1.00 94.07           O  
ANISOU 2572  OD1 ASP A1127    12356  15951   7434   4732   -153    984       O  
ATOM   2573  OD2 ASP A1127     -37.330  52.766 -37.891  1.00100.21           O  
ANISOU 2573  OD2 ASP A1127    13105  16386   8582   4872   -343   1118       O  
ATOM   2574  N   GLU A1128     -33.586  52.455 -39.355  1.00 73.36           N  
ANISOU 2574  N   GLU A1128    10324  11974   5577   3174  -1157    696       N  
ATOM   2575  CA  GLU A1128     -32.877  53.512 -40.077  1.00 72.29           C  
ANISOU 2575  CA  GLU A1128    10530  11283   5653   2980  -1486    575       C  
ATOM   2576  C   GLU A1128     -31.600  52.976 -40.709  1.00 72.14           C  
ANISOU 2576  C   GLU A1128    10497  11129   5784   2327  -1648    615       C  
ATOM   2577  O   GLU A1128     -31.369  53.251 -41.887  1.00 72.09           O  
ANISOU 2577  O   GLU A1128    10451  10942   5999   2023  -1779    795       O  
ATOM   2578  CB  GLU A1128     -32.545  54.692 -39.135  1.00 74.13           C  
ANISOU 2578  CB  GLU A1128    11300  11092   5772   3383  -1677    173       C  
ATOM   2579  CG  GLU A1128     -33.633  55.748 -38.986  1.00 88.32           C  
ANISOU 2579  CG  GLU A1128    13255  12765   7538   4029  -1634    119       C  
ATOM   2580  CD  GLU A1128     -34.909  55.361 -38.263  1.00111.23           C  
ANISOU 2580  CD  GLU A1128    15901  16203  10159   4630  -1249    216       C  
ATOM   2581  OE1 GLU A1128     -34.834  55.001 -37.065  1.00105.78           O  
ANISOU 2581  OE1 GLU A1128    15321  15743   9128   4928  -1107     12       O  
ATOM   2582  OE2 GLU A1128     -35.990  55.443 -38.891  1.00103.55           O  
ANISOU 2582  OE2 GLU A1128    14599  15443   9302   4823  -1091    527       O  
ATOM   2583  N   ALA A1129     -30.774  52.205 -39.943  1.00 64.76           N  
ANISOU 2583  N   ALA A1129     9583  10314   4710   2148  -1620    478       N  
ATOM   2584  CA  ALA A1129     -29.511  51.617 -40.421  1.00 62.59           C  
ANISOU 2584  CA  ALA A1129     9266   9959   4556   1585  -1733    524       C  
ATOM   2585  C   ALA A1129     -29.720  50.548 -41.495  1.00 62.45           C  
ANISOU 2585  C   ALA A1129     8860  10237   4633   1244  -1585    829       C  
ATOM   2586  O   ALA A1129     -28.875  50.396 -42.372  1.00 61.82           O  
ANISOU 2586  O   ALA A1129     8761  10036   4690    843  -1685    928       O  
ATOM   2587  CB  ALA A1129     -28.741  51.029 -39.266  1.00 63.16           C  
ANISOU 2587  CB  ALA A1129     9421  10142   4436   1567  -1722    330       C  
ATOM   2588  N   ALA A1130     -30.848  49.825 -41.426  1.00 56.23           N  
ANISOU 2588  N   ALA A1130     7762   9831   3773   1419  -1359    982       N  
ATOM   2589  CA  ALA A1130     -31.252  48.777 -42.356  1.00 54.75           C  
ANISOU 2589  CA  ALA A1130     7217   9908   3678   1139  -1270   1228       C  
ATOM   2590  C   ALA A1130     -31.472  49.321 -43.785  1.00 57.25           C  
ANISOU 2590  C   ALA A1130     7523  10094   4137    994  -1422   1379       C  
ATOM   2591  O   ALA A1130     -31.196  48.615 -44.761  1.00 56.12           O  
ANISOU 2591  O   ALA A1130     7249  10035   4039    657  -1457   1492       O  
ATOM   2592  CB  ALA A1130     -32.519  48.117 -41.844  1.00 55.34           C  
ANISOU 2592  CB  ALA A1130     6955  10365   3707   1394  -1050   1385       C  
ATOM   2593  N   VAL A1131     -31.973  50.573 -43.894  1.00 52.99           N  
ANISOU 2593  N   VAL A1131     7142   9351   3642   1291  -1513   1378       N  
ATOM   2594  CA  VAL A1131     -32.233  51.267 -45.159  1.00 52.19           C  
ANISOU 2594  CA  VAL A1131     7054   9116   3661   1230  -1660   1560       C  
ATOM   2595  C   VAL A1131     -30.897  51.630 -45.827  1.00 55.89           C  
ANISOU 2595  C   VAL A1131     7741   9283   4210    875  -1815   1567       C  
ATOM   2596  O   VAL A1131     -30.753  51.439 -47.037  1.00 56.21           O  
ANISOU 2596  O   VAL A1131     7691   9397   4269    638  -1864   1764       O  
ATOM   2597  CB  VAL A1131     -33.155  52.509 -44.983  1.00 55.55           C  
ANISOU 2597  CB  VAL A1131     7593   9376   4138   1697  -1702   1579       C  
ATOM   2598  CG1 VAL A1131     -33.525  53.125 -46.334  1.00 55.25           C  
ANISOU 2598  CG1 VAL A1131     7517   9258   4218   1647  -1845   1837       C  
ATOM   2599  CG2 VAL A1131     -34.416  52.160 -44.193  1.00 55.16           C  
ANISOU 2599  CG2 VAL A1131     7288   9674   3997   2107  -1495   1610       C  
ATOM   2600  N   ASN A1132     -29.929  52.146 -45.035  1.00 51.47           N  
ANISOU 2600  N   ASN A1132     7455   8410   3691    849  -1901   1371       N  
ATOM   2601  CA  ASN A1132     -28.594  52.538 -45.503  1.00 50.48           C  
ANISOU 2601  CA  ASN A1132     7486   7989   3704    503  -2052   1423       C  
ATOM   2602  C   ASN A1132     -27.725  51.347 -45.885  1.00 52.64           C  
ANISOU 2602  C   ASN A1132     7583   8507   3911    132  -1950   1490       C  
ATOM   2603  O   ASN A1132     -26.925  51.461 -46.809  1.00 52.81           O  
ANISOU 2603  O   ASN A1132     7597   8458   4011   -137  -1994   1684       O  
ATOM   2604  CB  ASN A1132     -27.880  53.418 -44.476  1.00 49.42           C  
ANISOU 2604  CB  ASN A1132     7670   7436   3669    576  -2241   1181       C  
ATOM   2605  CG  ASN A1132     -28.267  54.881 -44.518  1.00 64.37           C  
ANISOU 2605  CG  ASN A1132     9835   8884   5740    827  -2439   1167       C  
ATOM   2606  OD1 ASN A1132     -27.444  55.755 -44.814  1.00 59.83           O  
ANISOU 2606  OD1 ASN A1132     9446   7868   5418    625  -2670   1235       O  
ATOM   2607  ND2 ASN A1132     -29.519  55.191 -44.206  1.00 51.16           N  
ANISOU 2607  ND2 ASN A1132     8172   7295   3971   1281  -2355   1108       N  
ATOM   2608  N   LEU A1133     -27.880  50.214 -45.184  1.00 48.02           N  
ANISOU 2608  N   LEU A1133     6851   8211   3184    148  -1795   1363       N  
ATOM   2609  CA  LEU A1133     -27.125  48.987 -45.456  1.00 47.59           C  
ANISOU 2609  CA  LEU A1133     6642   8367   3072   -146  -1688   1401       C  
ATOM   2610  C   LEU A1133     -27.594  48.292 -46.735  1.00 53.83           C  
ANISOU 2610  C   LEU A1133     7253   9397   3803   -261  -1628   1571       C  
ATOM   2611  O   LEU A1133     -26.766  47.733 -47.461  1.00 54.52           O  
ANISOU 2611  O   LEU A1133     7311   9549   3856   -494  -1593   1650       O  
ATOM   2612  CB  LEU A1133     -27.186  48.011 -44.271  1.00 46.78           C  
ANISOU 2612  CB  LEU A1133     6450   8460   2865    -72  -1555   1245       C  
ATOM   2613  CG  LEU A1133     -26.347  48.341 -43.051  1.00 49.45           C  
ANISOU 2613  CG  LEU A1133     6967   8637   3184    -27  -1631   1056       C  
ATOM   2614  CD1 LEU A1133     -26.888  47.635 -41.856  1.00 49.50           C  
ANISOU 2614  CD1 LEU A1133     6896   8886   3028    203  -1481    948       C  
ATOM   2615  CD2 LEU A1133     -24.889  47.982 -43.264  1.00 48.77           C  
ANISOU 2615  CD2 LEU A1133     6874   8486   3171   -360  -1678   1100       C  
ATOM   2616  N   ALA A1134     -28.915  48.324 -47.007  1.00 50.06           N  
ANISOU 2616  N   ALA A1134     6655   9064   3302    -74  -1631   1625       N  
ATOM   2617  CA  ALA A1134     -29.501  47.713 -48.197  1.00 49.96           C  
ANISOU 2617  CA  ALA A1134     6486   9274   3222   -167  -1657   1751       C  
ATOM   2618  C   ALA A1134     -29.184  48.503 -49.453  1.00 52.57           C  
ANISOU 2618  C   ALA A1134     6933   9520   3523   -226  -1764   1936       C  
ATOM   2619  O   ALA A1134     -29.152  47.914 -50.524  1.00 53.43           O  
ANISOU 2619  O   ALA A1134     6992   9810   3497   -348  -1787   2009       O  
ATOM   2620  CB  ALA A1134     -31.007  47.577 -48.034  1.00 50.92           C  
ANISOU 2620  CB  ALA A1134     6394   9583   3372     39  -1668   1795       C  
ATOM   2621  N   LYS A1135     -28.977  49.830 -49.330  1.00 47.19           N  
ANISOU 2621  N   LYS A1135     6418   8553   2957   -118  -1840   2017       N  
ATOM   2622  CA  LYS A1135     -28.667  50.727 -50.440  1.00 46.33           C  
ANISOU 2622  CA  LYS A1135     6410   8325   2867   -159  -1931   2275       C  
ATOM   2623  C   LYS A1135     -27.145  50.790 -50.633  1.00 50.47           C  
ANISOU 2623  C   LYS A1135     7020   8719   3438   -417  -1889   2367       C  
ATOM   2624  O   LYS A1135     -26.524  51.827 -50.392  1.00 51.19           O  
ANISOU 2624  O   LYS A1135     7245   8471   3736   -458  -1976   2465       O  
ATOM   2625  CB  LYS A1135     -29.290  52.114 -50.196  1.00 48.03           C  
ANISOU 2625  CB  LYS A1135     6751   8246   3254     95  -2050   2348       C  
ATOM   2626  CG  LYS A1135     -30.559  52.391 -50.998  1.00 60.19           C  
ANISOU 2626  CG  LYS A1135     8183   9953   4732    308  -2121   2524       C  
ATOM   2627  CD  LYS A1135     -30.263  53.410 -52.114  1.00 67.25           C  
ANISOU 2627  CD  LYS A1135     9198  10673   5682    294  -2223   2860       C  
ATOM   2628  CE  LYS A1135     -31.454  54.215 -52.595  1.00 75.45           C  
ANISOU 2628  CE  LYS A1135    10201  11711   6754    595  -2334   3050       C  
ATOM   2629  NZ  LYS A1135     -32.359  53.438 -53.486  1.00 81.03           N  
ANISOU 2629  NZ  LYS A1135    10683  12881   7222    617  -2376   3135       N  
ATOM   2630  N   SER A1136     -26.543  49.648 -51.041  1.00 46.05           N  
ANISOU 2630  N   SER A1136     6370   8415   2711   -585  -1767   2340       N  
ATOM   2631  CA  SER A1136     -25.097  49.490 -51.232  1.00 45.28           C  
ANISOU 2631  CA  SER A1136     6280   8289   2636   -799  -1675   2456       C  
ATOM   2632  C   SER A1136     -24.728  48.391 -52.241  1.00 48.72           C  
ANISOU 2632  C   SER A1136     6648   9065   2797   -859  -1536   2503       C  
ATOM   2633  O   SER A1136     -25.526  47.486 -52.494  1.00 48.32           O  
ANISOU 2633  O   SER A1136     6559   9230   2570   -788  -1544   2334       O  
ATOM   2634  CB  SER A1136     -24.422  49.186 -49.896  1.00 47.89           C  
ANISOU 2634  CB  SER A1136     6609   8481   3108   -886  -1657   2242       C  
ATOM   2635  OG  SER A1136     -24.839  47.935 -49.367  1.00 52.68           O  
ANISOU 2635  OG  SER A1136     7127   9302   3588   -848  -1564   2002       O  
ATOM   2636  N   ARG A1137     -23.475  48.447 -52.753  1.00 44.88           N  
ANISOU 2636  N   ARG A1137     6141   8615   2295   -983  -1416   2730       N  
ATOM   2637  CA  ARG A1137     -22.882  47.483 -53.683  1.00 44.70           C  
ANISOU 2637  CA  ARG A1137     6089   8912   1985   -977  -1241   2785       C  
ATOM   2638  C   ARG A1137     -22.853  46.068 -53.083  1.00 48.04           C  
ANISOU 2638  C   ARG A1137     6479   9439   2336   -986  -1170   2445       C  
ATOM   2639  O   ARG A1137     -22.962  45.087 -53.820  1.00 47.66           O  
ANISOU 2639  O   ARG A1137     6470   9621   2018   -907  -1110   2336       O  
ATOM   2640  CB  ARG A1137     -21.468  47.929 -54.090  1.00 46.40           C  
ANISOU 2640  CB  ARG A1137     6225   9137   2269  -1087  -1088   3150       C  
ATOM   2641  CG  ARG A1137     -21.436  49.120 -55.059  1.00 64.41           C  
ANISOU 2641  CG  ARG A1137     8520  11393   4561  -1066  -1108   3594       C  
ATOM   2642  CD  ARG A1137     -20.113  49.246 -55.814  1.00 83.20           C  
ANISOU 2642  CD  ARG A1137    10766  13952   6895  -1123   -877   4036       C  
ATOM   2643  NE  ARG A1137     -18.974  49.568 -54.944  1.00 99.74           N  
ANISOU 2643  NE  ARG A1137    12697  15812   9387  -1365   -872   4171       N  
ATOM   2644  CZ  ARG A1137     -18.038  48.698 -54.569  1.00114.93           C  
ANISOU 2644  CZ  ARG A1137    14487  17879  11304  -1418   -712   4103       C  
ATOM   2645  NH1 ARG A1137     -18.097  47.433 -54.973  1.00 99.86           N  
ANISOU 2645  NH1 ARG A1137    12621  16305   9017  -1229   -526   3879       N  
ATOM   2646  NH2 ARG A1137     -17.048  49.082 -53.773  1.00102.70           N  
ANISOU 2646  NH2 ARG A1137    12765  16116  10142  -1655   -770   4250       N  
ATOM   2647  N   TRP A1138     -22.729  45.977 -51.743  1.00 44.95           N  
ANISOU 2647  N   TRP A1138     6039   8859   2179  -1063  -1198   2276       N  
ATOM   2648  CA  TRP A1138     -22.729  44.737 -50.962  1.00 44.91           C  
ANISOU 2648  CA  TRP A1138     5985   8907   2173  -1076  -1136   2011       C  
ATOM   2649  C   TRP A1138     -24.047  43.968 -51.133  1.00 47.25           C  
ANISOU 2649  C   TRP A1138     6285   9305   2363   -991  -1218   1805       C  
ATOM   2650  O   TRP A1138     -24.016  42.763 -51.400  1.00 47.51           O  
ANISOU 2650  O   TRP A1138     6317   9448   2285   -993  -1167   1661       O  
ATOM   2651  CB  TRP A1138     -22.461  45.049 -49.484  1.00 43.88           C  
ANISOU 2651  CB  TRP A1138     5819   8578   2277  -1133  -1183   1921       C  
ATOM   2652  CG  TRP A1138     -22.783  43.947 -48.509  1.00 45.39           C  
ANISOU 2652  CG  TRP A1138     5951   8816   2478  -1106  -1136   1693       C  
ATOM   2653  CD1 TRP A1138     -22.255  42.686 -48.482  1.00 48.46           C  
ANISOU 2653  CD1 TRP A1138     6284   9317   2811  -1135  -1006   1624       C  
ATOM   2654  CD2 TRP A1138     -23.606  44.063 -47.336  1.00 45.30           C  
ANISOU 2654  CD2 TRP A1138     5928   8737   2548  -1018  -1201   1552       C  
ATOM   2655  NE1 TRP A1138     -22.741  41.994 -47.392  1.00 47.89           N  
ANISOU 2655  NE1 TRP A1138     6152   9234   2809  -1105   -998   1479       N  
ATOM   2656  CE2 TRP A1138     -23.572  42.816 -46.674  1.00 49.32           C  
ANISOU 2656  CE2 TRP A1138     6347   9340   3053  -1024  -1100   1445       C  
ATOM   2657  CE3 TRP A1138     -24.405  45.091 -46.804  1.00 46.59           C  
ANISOU 2657  CE3 TRP A1138     6150   8778   2772   -890  -1317   1521       C  
ATOM   2658  CZ2 TRP A1138     -24.294  42.574 -45.500  1.00 48.97           C  
ANISOU 2658  CZ2 TRP A1138     6244   9315   3049   -920  -1090   1357       C  
ATOM   2659  CZ3 TRP A1138     -25.132  44.844 -45.654  1.00 48.29           C  
ANISOU 2659  CZ3 TRP A1138     6324   9029   2994   -746  -1297   1392       C  
ATOM   2660  CH2 TRP A1138     -25.069  43.601 -45.010  1.00 49.09           C  
ANISOU 2660  CH2 TRP A1138     6308   9267   3077   -768  -1175   1334       C  
ATOM   2661  N   TYR A1139     -25.190  44.660 -50.992  1.00 41.27           N  
ANISOU 2661  N   TYR A1139     5520   8492   1669   -916  -1361   1806       N  
ATOM   2662  CA  TYR A1139     -26.499  44.044 -51.146  1.00 40.69           C  
ANISOU 2662  CA  TYR A1139     5376   8527   1560   -861  -1472   1682       C  
ATOM   2663  C   TYR A1139     -26.690  43.554 -52.573  1.00 47.23           C  
ANISOU 2663  C   TYR A1139     6273   9536   2135   -849  -1551   1678       C  
ATOM   2664  O   TYR A1139     -27.223  42.466 -52.759  1.00 47.91           O  
ANISOU 2664  O   TYR A1139     6328   9693   2182   -884  -1633   1504       O  
ATOM   2665  CB  TYR A1139     -27.620  45.008 -50.710  1.00 41.10           C  
ANISOU 2665  CB  TYR A1139     5369   8513   1736   -734  -1584   1740       C  
ATOM   2666  CG  TYR A1139     -29.011  44.405 -50.712  1.00 42.12           C  
ANISOU 2666  CG  TYR A1139     5329   8776   1897   -689  -1698   1678       C  
ATOM   2667  CD1 TYR A1139     -29.787  44.388 -51.875  1.00 44.45           C  
ANISOU 2667  CD1 TYR A1139     5604   9217   2069   -669  -1878   1733       C  
ATOM   2668  CD2 TYR A1139     -29.569  43.888 -49.549  1.00 42.05           C  
ANISOU 2668  CD2 TYR A1139     5155   8771   2049   -663  -1639   1608       C  
ATOM   2669  CE1 TYR A1139     -31.061  43.823 -51.888  1.00 44.39           C  
ANISOU 2669  CE1 TYR A1139     5389   9329   2147   -671  -2034   1706       C  
ATOM   2670  CE2 TYR A1139     -30.853  43.338 -49.545  1.00 42.90           C  
ANISOU 2670  CE2 TYR A1139     5035   9013   2253   -651  -1741   1632       C  
ATOM   2671  CZ  TYR A1139     -31.599  43.316 -50.717  1.00 51.42           C  
ANISOU 2671  CZ  TYR A1139     6070  10208   3259   -676  -1958   1678       C  
ATOM   2672  OH  TYR A1139     -32.867  42.779 -50.748  1.00 52.53           O  
ANISOU 2672  OH  TYR A1139     5937  10476   3545   -705  -2114   1730       O  
ATOM   2673  N   ASN A1140     -26.235  44.335 -53.576  1.00 44.49           N  
ANISOU 2673  N   ASN A1140     6032   9257   1615   -794  -1541   1879       N  
ATOM   2674  CA  ASN A1140     -26.350  43.966 -54.982  1.00 44.04           C  
ANISOU 2674  CA  ASN A1140     6086   9426   1223   -718  -1611   1885       C  
ATOM   2675  C   ASN A1140     -25.516  42.735 -55.390  1.00 49.09           C  
ANISOU 2675  C   ASN A1140     6827  10169   1657   -713  -1491   1713       C  
ATOM   2676  O   ASN A1140     -25.938  42.001 -56.286  1.00 49.99           O  
ANISOU 2676  O   ASN A1140     7056  10427   1511   -642  -1629   1543       O  
ATOM   2677  CB  ASN A1140     -26.050  45.141 -55.885  1.00 44.29           C  
ANISOU 2677  CB  ASN A1140     6106   9449   1274   -641  -1524   2154       C  
ATOM   2678  CG  ASN A1140     -26.579  44.890 -57.262  1.00 63.76           C  
ANISOU 2678  CG  ASN A1140     8767  12273   3186   -492  -1734   2216       C  
ATOM   2679  OD1 ASN A1140     -27.795  44.829 -57.490  1.00 62.68           O  
ANISOU 2679  OD1 ASN A1140     8592  12192   3032   -461  -1988   2120       O  
ATOM   2680  ND2 ASN A1140     -25.683  44.663 -58.193  1.00 53.03           N  
ANISOU 2680  ND2 ASN A1140     7538  11120   1490   -390  -1584   2322       N  
ATOM   2681  N   GLN A1141     -24.343  42.520 -54.751  1.00 45.53           N  
ANISOU 2681  N   GLN A1141     6342   9639   1318   -767  -1263   1746       N  
ATOM   2682  CA  GLN A1141     -23.430  41.394 -55.003  1.00 45.19           C  
ANISOU 2682  CA  GLN A1141     6376   9674   1120   -714  -1101   1612       C  
ATOM   2683  C   GLN A1141     -23.954  40.092 -54.364  1.00 48.67           C  
ANISOU 2683  C   GLN A1141     6806   9986   1701   -780  -1198   1287       C  
ATOM   2684  O   GLN A1141     -24.049  39.075 -55.056  1.00 47.93           O  
ANISOU 2684  O   GLN A1141     6862   9939   1410   -701  -1268   1061       O  
ATOM   2685  CB  GLN A1141     -22.017  41.726 -54.494  1.00 46.57           C  
ANISOU 2685  CB  GLN A1141     6451   9821   1422   -754   -843   1831       C  
ATOM   2686  CG  GLN A1141     -20.907  40.967 -55.202  1.00 64.00           C  
ANISOU 2686  CG  GLN A1141     8727  12216   3373   -599   -609   1850       C  
ATOM   2687  CD  GLN A1141     -19.735  41.859 -55.555  1.00 92.50           C  
ANISOU 2687  CD  GLN A1141    12227  15963   6956   -575   -387   2274       C  
ATOM   2688  OE1 GLN A1141     -19.882  42.984 -56.065  1.00 90.41           O  
ANISOU 2688  OE1 GLN A1141    11948  15748   6657   -587   -424   2560       O  
ATOM   2689  NE2 GLN A1141     -18.534  41.364 -55.314  1.00 87.15           N  
ANISOU 2689  NE2 GLN A1141    11441  15351   6322   -540   -149   2370       N  
ATOM   2690  N   THR A1142     -24.281  40.123 -53.044  1.00 45.12           N  
ANISOU 2690  N   THR A1142     6191   9363   1587   -909  -1209   1274       N  
ATOM   2691  CA  THR A1142     -24.830  38.973 -52.300  1.00 44.04           C  
ANISOU 2691  CA  THR A1142     5985   9100   1649   -991  -1278   1071       C  
ATOM   2692  C   THR A1142     -26.194  39.334 -51.690  1.00 45.85           C  
ANISOU 2692  C   THR A1142     6049   9285   2087  -1059  -1451   1096       C  
ATOM   2693  O   THR A1142     -26.260  39.581 -50.493  1.00 46.68           O  
ANISOU 2693  O   THR A1142     6016   9321   2400  -1085  -1367   1167       O  
ATOM   2694  CB  THR A1142     -23.831  38.430 -51.270  1.00 49.06           C  
ANISOU 2694  CB  THR A1142     6554   9643   2443  -1020  -1070   1081       C  
ATOM   2695  OG1 THR A1142     -23.422  39.492 -50.404  1.00 48.30           O  
ANISOU 2695  OG1 THR A1142     6356   9525   2471  -1051   -988   1261       O  
ATOM   2696  CG2 THR A1142     -22.629  37.775 -51.913  1.00 47.31           C  
ANISOU 2696  CG2 THR A1142     6458   9481   2035   -912   -900   1043       C  
ATOM   2697  N   PRO A1143     -27.290  39.383 -52.482  1.00 40.54           N  
ANISOU 2697  N   PRO A1143     5376   8684   1344  -1058  -1693   1054       N  
ATOM   2698  CA  PRO A1143     -28.587  39.801 -51.917  1.00 39.85           C  
ANISOU 2698  CA  PRO A1143     5070   8601   1469  -1087  -1828   1143       C  
ATOM   2699  C   PRO A1143     -29.136  38.924 -50.799  1.00 43.62           C  
ANISOU 2699  C   PRO A1143     5332   8988   2253  -1187  -1812   1125       C  
ATOM   2700  O   PRO A1143     -29.620  39.473 -49.813  1.00 43.61           O  
ANISOU 2700  O   PRO A1143     5152   9008   2410  -1133  -1730   1265       O  
ATOM   2701  CB  PRO A1143     -29.512  39.838 -53.140  1.00 41.55           C  
ANISOU 2701  CB  PRO A1143     5317   8936   1534  -1077  -2123   1106       C  
ATOM   2702  CG  PRO A1143     -28.842  38.984 -54.157  1.00 45.20           C  
ANISOU 2702  CG  PRO A1143     6034   9415   1726  -1065  -2175    901       C  
ATOM   2703  CD  PRO A1143     -27.392  39.155 -53.940  1.00 41.12           C  
ANISOU 2703  CD  PRO A1143     5633   8865   1125   -993  -1847    945       C  
ATOM   2704  N   ASN A1144     -29.027  37.585 -50.922  1.00 40.04           N  
ANISOU 2704  N   ASN A1144     4907   8427   1880  -1303  -1877    972       N  
ATOM   2705  CA  ASN A1144     -29.529  36.625 -49.922  1.00 39.03           C  
ANISOU 2705  CA  ASN A1144     4556   8190   2086  -1425  -1866   1018       C  
ATOM   2706  C   ASN A1144     -28.796  36.691 -48.611  1.00 40.85           C  
ANISOU 2706  C   ASN A1144     4727   8399   2395  -1364  -1568   1127       C  
ATOM   2707  O   ASN A1144     -29.424  36.586 -47.564  1.00 41.42           O  
ANISOU 2707  O   ASN A1144     4558   8503   2675  -1366  -1495   1290       O  
ATOM   2708  CB  ASN A1144     -29.526  35.196 -50.449  1.00 39.81           C  
ANISOU 2708  CB  ASN A1144     4743   8098   2284  -1568  -2049    822       C  
ATOM   2709  CG  ASN A1144     -30.268  35.033 -51.741  1.00 59.00           C  
ANISOU 2709  CG  ASN A1144     7260  10540   4616  -1633  -2424    663       C  
ATOM   2710  OD1 ASN A1144     -31.473  35.302 -51.832  1.00 57.14           O  
ANISOU 2710  OD1 ASN A1144     6787  10386   4537  -1718  -2644    782       O  
ATOM   2711  ND2 ASN A1144     -29.554  34.592 -52.768  1.00 47.81           N  
ANISOU 2711  ND2 ASN A1144     6182   9072   2913  -1561  -2507    398       N  
ATOM   2712  N   ARG A1145     -27.473  36.854 -48.657  1.00 35.41           N  
ANISOU 2712  N   ARG A1145     4235   7689   1530  -1294  -1400   1064       N  
ATOM   2713  CA  ARG A1145     -26.649  36.970 -47.465  1.00 34.28           C  
ANISOU 2713  CA  ARG A1145     4055   7541   1429  -1238  -1171   1151       C  
ATOM   2714  C   ARG A1145     -26.868  38.331 -46.808  1.00 38.49           C  
ANISOU 2714  C   ARG A1145     4542   8168   1916  -1123  -1121   1262       C  
ATOM   2715  O   ARG A1145     -27.091  38.368 -45.604  1.00 39.93           O  
ANISOU 2715  O   ARG A1145     4601   8386   2184  -1056  -1020   1347       O  
ATOM   2716  CB  ARG A1145     -25.173  36.759 -47.801  1.00 34.74           C  
ANISOU 2716  CB  ARG A1145     4290   7564   1345  -1207  -1043   1082       C  
ATOM   2717  CG  ARG A1145     -24.236  36.877 -46.606  1.00 43.21           C  
ANISOU 2717  CG  ARG A1145     5311   8644   2463  -1166   -862   1175       C  
ATOM   2718  CD  ARG A1145     -22.820  36.628 -47.051  1.00 51.11           C  
ANISOU 2718  CD  ARG A1145     6421   9642   3356  -1135   -744   1155       C  
ATOM   2719  NE  ARG A1145     -21.885  36.652 -45.933  1.00 44.59           N  
ANISOU 2719  NE  ARG A1145     5517   8834   2592  -1114   -619   1254       N  
ATOM   2720  CZ  ARG A1145     -20.600  36.347 -46.042  1.00 57.73           C  
ANISOU 2720  CZ  ARG A1145     7193  10520   4223  -1079   -498   1298       C  
ATOM   2721  NH1 ARG A1145     -20.089  35.998 -47.218  1.00 39.35           N  
ANISOU 2721  NH1 ARG A1145     4969   8211   1773  -1022   -439   1251       N  
ATOM   2722  NH2 ARG A1145     -19.813  36.380 -44.974  1.00 48.82           N  
ANISOU 2722  NH2 ARG A1145     5966   9425   3160  -1071   -437   1399       N  
ATOM   2723  N   ALA A1146     -26.829  39.435 -47.585  1.00 34.53           N  
ANISOU 2723  N   ALA A1146     4154   7698   1268  -1073  -1196   1265       N  
ATOM   2724  CA  ALA A1146     -27.030  40.794 -47.076  1.00 34.38           C  
ANISOU 2724  CA  ALA A1146     4147   7687   1231   -948  -1192   1342       C  
ATOM   2725  C   ALA A1146     -28.367  40.978 -46.381  1.00 41.28           C  
ANISOU 2725  C   ALA A1146     4835   8638   2211   -833  -1213   1414       C  
ATOM   2726  O   ALA A1146     -28.379  41.538 -45.287  1.00 42.19           O  
ANISOU 2726  O   ALA A1146     4944   8760   2327   -681  -1124   1435       O  
ATOM   2727  CB  ALA A1146     -26.859  41.818 -48.176  1.00 34.64           C  
ANISOU 2727  CB  ALA A1146     4307   7692   1163   -931  -1272   1378       C  
ATOM   2728  N   LYS A1147     -29.480  40.459 -46.966  1.00 38.92           N  
ANISOU 2728  N   LYS A1147     4375   8415   2000   -888  -1336   1456       N  
ATOM   2729  CA  LYS A1147     -30.813  40.528 -46.345  1.00 39.09           C  
ANISOU 2729  CA  LYS A1147     4126   8560   2166   -780  -1334   1602       C  
ATOM   2730  C   LYS A1147     -30.829  39.840 -44.965  1.00 40.30           C  
ANISOU 2730  C   LYS A1147     4120   8767   2426   -732  -1137   1691       C  
ATOM   2731  O   LYS A1147     -31.312  40.435 -44.000  1.00 39.75           O  
ANISOU 2731  O   LYS A1147     3962   8812   2330   -494  -1008   1788       O  
ATOM   2732  CB  LYS A1147     -31.949  40.024 -47.278  1.00 43.34           C  
ANISOU 2732  CB  LYS A1147     4468   9167   2831   -905  -1560   1663       C  
ATOM   2733  CG  LYS A1147     -31.914  38.549 -47.720  1.00 68.70           C  
ANISOU 2733  CG  LYS A1147     7634  12287   6181  -1166  -1688   1586       C  
ATOM   2734  CD  LYS A1147     -32.847  37.603 -46.923  1.00 80.16           C  
ANISOU 2734  CD  LYS A1147     8720  13773   7963  -1265  -1677   1783       C  
ATOM   2735  CE  LYS A1147     -32.770  36.144 -47.356  1.00 84.86           C  
ANISOU 2735  CE  LYS A1147     9310  14176   8759  -1545  -1860   1690       C  
ATOM   2736  NZ  LYS A1147     -33.384  35.902 -48.696  1.00 89.73           N  
ANISOU 2736  NZ  LYS A1147     9968  14749   9377  -1698  -2245   1552       N  
ATOM   2737  N   ARG A1148     -30.215  38.640 -44.860  1.00 34.63           N  
ANISOU 2737  N   ARG A1148     3401   7965   1792   -910  -1101   1657       N  
ATOM   2738  CA  ARG A1148     -30.122  37.874 -43.612  1.00 33.32           C  
ANISOU 2738  CA  ARG A1148     3089   7846   1724   -877   -913   1786       C  
ATOM   2739  C   ARG A1148     -29.352  38.627 -42.540  1.00 37.63           C  
ANISOU 2739  C   ARG A1148     3788   8446   2064   -660   -750   1745       C  
ATOM   2740  O   ARG A1148     -29.774  38.630 -41.383  1.00 37.36           O  
ANISOU 2740  O   ARG A1148     3616   8572   2006   -468   -590   1888       O  
ATOM   2741  CB  ARG A1148     -29.498  36.495 -43.845  1.00 29.88           C  
ANISOU 2741  CB  ARG A1148     2676   7248   1429  -1098   -933   1745       C  
ATOM   2742  CG  ARG A1148     -30.468  35.491 -44.427  1.00 33.50           C  
ANISOU 2742  CG  ARG A1148     2925   7627   2178  -1310  -1111   1826       C  
ATOM   2743  CD  ARG A1148     -29.938  34.074 -44.409  1.00 38.85           C  
ANISOU 2743  CD  ARG A1148     3628   8084   3050  -1487  -1125   1803       C  
ATOM   2744  NE  ARG A1148     -28.730  33.913 -45.222  1.00 52.65           N  
ANISOU 2744  NE  ARG A1148     5714   9679   4614  -1506  -1164   1525       N  
ATOM   2745  CZ  ARG A1148     -28.722  33.548 -46.502  1.00 70.78           C  
ANISOU 2745  CZ  ARG A1148     8183  11830   6882  -1613  -1391   1304       C  
ATOM   2746  NH1 ARG A1148     -29.862  33.303 -47.137  1.00 57.09           N  
ANISOU 2746  NH1 ARG A1148     6324  10052   5315  -1759  -1664   1301       N  
ATOM   2747  NH2 ARG A1148     -27.573  33.432 -47.158  1.00 61.20           N  
ANISOU 2747  NH2 ARG A1148     7259  10540   5454  -1552  -1354   1094       N  
ATOM   2748  N   VAL A1149     -28.238  39.278 -42.928  1.00 34.15           N  
ANISOU 2748  N   VAL A1149     3619   7888   1470   -681   -805   1566       N  
ATOM   2749  CA  VAL A1149     -27.399  40.066 -42.026  1.00 34.61           C  
ANISOU 2749  CA  VAL A1149     3848   7939   1364   -529   -751   1489       C  
ATOM   2750  C   VAL A1149     -28.131  41.342 -41.604  1.00 40.22           C  
ANISOU 2750  C   VAL A1149     4613   8697   1972   -264   -774   1467       C  
ATOM   2751  O   VAL A1149     -28.115  41.675 -40.419  1.00 40.28           O  
ANISOU 2751  O   VAL A1149     4668   8790   1847    -31   -692   1446       O  
ATOM   2752  CB  VAL A1149     -25.982  40.335 -42.609  1.00 38.87           C  
ANISOU 2752  CB  VAL A1149     4591   8327   1850   -676   -826   1372       C  
ATOM   2753  CG1 VAL A1149     -25.141  41.205 -41.673  1.00 38.64           C  
ANISOU 2753  CG1 VAL A1149     4716   8258   1709   -568   -857   1292       C  
ATOM   2754  CG2 VAL A1149     -25.256  39.027 -42.894  1.00 38.71           C  
ANISOU 2754  CG2 VAL A1149     4523   8278   1906   -844   -761   1390       C  
ATOM   2755  N   ILE A1150     -28.788  42.035 -42.559  1.00 37.80           N  
ANISOU 2755  N   ILE A1150     4315   8344   1703   -259   -888   1469       N  
ATOM   2756  CA  ILE A1150     -29.553  43.259 -42.285  1.00 38.25           C  
ANISOU 2756  CA  ILE A1150     4428   8411   1694     28   -913   1458       C  
ATOM   2757  C   ILE A1150     -30.742  42.986 -41.359  1.00 43.29           C  
ANISOU 2757  C   ILE A1150     4820   9301   2328    297   -742   1611       C  
ATOM   2758  O   ILE A1150     -31.016  43.801 -40.480  1.00 42.14           O  
ANISOU 2758  O   ILE A1150     4776   9204   2031    645   -674   1557       O  
ATOM   2759  CB  ILE A1150     -29.950  43.988 -43.583  1.00 41.51           C  
ANISOU 2759  CB  ILE A1150     4883   8728   2161    -26  -1074   1480       C  
ATOM   2760  CG1 ILE A1150     -28.717  44.656 -44.212  1.00 41.98           C  
ANISOU 2760  CG1 ILE A1150     5209   8555   2188   -182  -1196   1383       C  
ATOM   2761  CG2 ILE A1150     -31.055  45.023 -43.341  1.00 42.40           C  
ANISOU 2761  CG2 ILE A1150     4969   8883   2257    310  -1077   1529       C  
ATOM   2762  CD1 ILE A1150     -28.819  44.872 -45.741  1.00 49.07           C  
ANISOU 2762  CD1 ILE A1150     6120   9419   3105   -328  -1321   1464       C  
ATOM   2763  N   THR A1151     -31.415  41.830 -41.527  1.00 42.65           N  
ANISOU 2763  N   THR A1151     4418   9371   2416    149   -677   1812       N  
ATOM   2764  CA  THR A1151     -32.550  41.420 -40.686  1.00 43.62           C  
ANISOU 2764  CA  THR A1151     4206   9770   2596    359   -486   2070       C  
ATOM   2765  C   THR A1151     -32.062  41.155 -39.278  1.00 51.19           C  
ANISOU 2765  C   THR A1151     5219  10857   3375    560   -276   2087       C  
ATOM   2766  O   THR A1151     -32.754  41.519 -38.331  1.00 52.01           O  
ANISOU 2766  O   THR A1151     5222  11201   3337    942    -86   2210       O  
ATOM   2767  CB  THR A1151     -33.332  40.257 -41.324  1.00 49.60           C  
ANISOU 2767  CB  THR A1151     4592  10588   3665     70   -544   2306       C  
ATOM   2768  OG1 THR A1151     -33.735  40.646 -42.638  1.00 48.88           O  
ANISOU 2768  OG1 THR A1151     4511  10403   3659    -70   -785   2244       O  
ATOM   2769  CG2 THR A1151     -34.565  39.872 -40.541  1.00 47.68           C  
ANISOU 2769  CG2 THR A1151     3915  10645   3555    254   -349   2671       C  
ATOM   2770  N   THR A1152     -30.844  40.578 -39.138  1.00 49.95           N  
ANISOU 2770  N   THR A1152     5231  10564   3183    352   -309   1967       N  
ATOM   2771  CA  THR A1152     -30.195  40.300 -37.843  1.00 50.42           C  
ANISOU 2771  CA  THR A1152     5374  10743   3042    520   -162   1969       C  
ATOM   2772  C   THR A1152     -29.961  41.616 -37.085  1.00 55.10           C  
ANISOU 2772  C   THR A1152     6277  11346   3312    895   -191   1736       C  
ATOM   2773  O   THR A1152     -30.214  41.658 -35.886  1.00 54.91           O  
ANISOU 2773  O   THR A1152     6250  11566   3047   1246    -20   1797       O  
ATOM   2774  CB  THR A1152     -28.936  39.432 -38.036  1.00 59.64           C  
ANISOU 2774  CB  THR A1152     6631  11746   4282    208   -228   1903       C  
ATOM   2775  OG1 THR A1152     -29.307  38.235 -38.722  1.00 60.10           O  
ANISOU 2775  OG1 THR A1152     6444  11750   4643    -83   -223   2082       O  
ATOM   2776  CG2 THR A1152     -28.262  39.058 -36.724  1.00 58.25           C  
ANISOU 2776  CG2 THR A1152     6508  11718   3906    372   -102   1947       C  
ATOM   2777  N   PHE A1153     -29.541  42.690 -37.793  1.00 52.31           N  
ANISOU 2777  N   PHE A1153     6196  10726   2955    840   -414   1484       N  
ATOM   2778  CA  PHE A1153     -29.346  44.030 -37.224  1.00 52.75           C  
ANISOU 2778  CA  PHE A1153     6588  10672   2781   1161   -524   1225       C  
ATOM   2779  C   PHE A1153     -30.689  44.690 -36.858  1.00 59.50           C  
ANISOU 2779  C   PHE A1153     7374  11706   3529   1618   -383   1293       C  
ATOM   2780  O   PHE A1153     -30.756  45.457 -35.897  1.00 59.68           O  
ANISOU 2780  O   PHE A1153     7639  11769   3268   2044   -366   1115       O  
ATOM   2781  CB  PHE A1153     -28.598  44.949 -38.202  1.00 54.23           C  
ANISOU 2781  CB  PHE A1153     7028  10484   3094    930   -803   1030       C  
ATOM   2782  CG  PHE A1153     -27.108  44.748 -38.313  1.00 55.62           C  
ANISOU 2782  CG  PHE A1153     7342  10478   3312    608   -960    925       C  
ATOM   2783  CD1 PHE A1153     -26.285  44.873 -37.198  1.00 57.83           C  
ANISOU 2783  CD1 PHE A1153     7809  10759   3403    716  -1040    764       C  
ATOM   2784  CD2 PHE A1153     -26.514  44.519 -39.549  1.00 57.90           C  
ANISOU 2784  CD2 PHE A1153     7577  10614   3809    230  -1044    992       C  
ATOM   2785  CE1 PHE A1153     -24.906  44.718 -37.309  1.00 58.77           C  
ANISOU 2785  CE1 PHE A1153     7997  10731   3600    414  -1203    710       C  
ATOM   2786  CE2 PHE A1153     -25.131  44.365 -39.660  1.00 60.46           C  
ANISOU 2786  CE2 PHE A1153     7977  10809   4184    -29  -1155    948       C  
ATOM   2787  CZ  PHE A1153     -24.336  44.477 -38.541  1.00 58.40           C  
ANISOU 2787  CZ  PHE A1153     7848  10547   3794     46  -1241    821       C  
ATOM   2788  N   ARG A1154     -31.738  44.405 -37.634  1.00 57.53           N  
ANISOU 2788  N   ARG A1154     6802  11562   3497   1550   -305   1537       N  
ATOM   2789  CA  ARG A1154     -33.072  44.957 -37.459  1.00 58.67           C  
ANISOU 2789  CA  ARG A1154     6781  11906   3605   1959   -161   1680       C  
ATOM   2790  C   ARG A1154     -33.772  44.352 -36.227  1.00 66.35           C  
ANISOU 2790  C   ARG A1154     7492  13312   4404   2320    177   1934       C  
ATOM   2791  O   ARG A1154     -34.219  45.097 -35.344  1.00 66.83           O  
ANISOU 2791  O   ARG A1154     7687  13534   4170   2871    321   1863       O  
ATOM   2792  CB  ARG A1154     -33.877  44.730 -38.762  1.00 60.29           C  
ANISOU 2792  CB  ARG A1154     6674  12100   4132   1694   -244   1894       C  
ATOM   2793  CG  ARG A1154     -35.330  45.227 -38.790  1.00 75.49           C  
ANISOU 2793  CG  ARG A1154     8324  14254   6105   2063   -121   2119       C  
ATOM   2794  CD  ARG A1154     -35.473  46.696 -39.163  1.00 88.05           C  
ANISOU 2794  CD  ARG A1154    10215  15614   7625   2350   -263   1917       C  
ATOM   2795  NE  ARG A1154     -36.876  47.125 -39.233  1.00 98.30           N  
ANISOU 2795  NE  ARG A1154    11205  17157   8986   2732   -132   2170       N  
ATOM   2796  CZ  ARG A1154     -37.612  47.512 -38.190  1.00111.51           C  
ANISOU 2796  CZ  ARG A1154    12814  19101  10453   3327    142   2248       C  
ATOM   2797  NH1 ARG A1154     -37.092  47.526 -36.967  1.00 92.88           N  
ANISOU 2797  NH1 ARG A1154    10720  16805   7767   3620    292   2062       N  
ATOM   2798  NH2 ARG A1154     -38.873  47.893 -38.363  1.00100.58           N  
ANISOU 2798  NH2 ARG A1154    11099  17956   9162   3669    266   2522       N  
ATOM   2799  N   THR A1155     -33.852  43.007 -36.167  1.00 64.45           N  
ANISOU 2799  N   THR A1155     6896  13251   4341   2034    306   2239       N  
ATOM   2800  CA  THR A1155     -34.533  42.271 -35.096  1.00 64.51           C  
ANISOU 2800  CA  THR A1155     6566  13687   4260   2303    649   2611       C  
ATOM   2801  C   THR A1155     -33.660  41.982 -33.872  1.00 69.17           C  
ANISOU 2801  C   THR A1155     7383  14399   4501   2487    762   2521       C  
ATOM   2802  O   THR A1155     -34.182  42.016 -32.762  1.00 69.69           O  
ANISOU 2802  O   THR A1155     7363  14847   4270   2974   1052   2701       O  
ATOM   2803  CB  THR A1155     -35.178  40.971 -35.627  1.00 72.09           C  
ANISOU 2803  CB  THR A1155     6994  14741   5657   1896    705   3047       C  
ATOM   2804  OG1 THR A1155     -34.168  40.078 -36.105  1.00 71.78           O  
ANISOU 2804  OG1 THR A1155     7056  14423   5792   1393    525   2940       O  
ATOM   2805  CG2 THR A1155     -36.242  41.226 -36.713  1.00 69.86           C  
ANISOU 2805  CG2 THR A1155     6417  14435   5693   1772    583   3192       C  
ATOM   2806  N   GLY A1156     -32.378  41.672 -34.077  1.00 65.84           N  
ANISOU 2806  N   GLY A1156     7215  13701   4101   2128    548   2287       N  
ATOM   2807  CA  GLY A1156     -31.453  41.317 -33.002  1.00 65.74           C  
ANISOU 2807  CA  GLY A1156     7393  13794   3788   2242    594   2217       C  
ATOM   2808  C   GLY A1156     -31.638  39.887 -32.524  1.00 70.35           C  
ANISOU 2808  C   GLY A1156     7591  14632   4505   2118    842   2673       C  
ATOM   2809  O   GLY A1156     -31.248  39.548 -31.401  1.00 69.87           O  
ANISOU 2809  O   GLY A1156     7591  14816   4140   2359    986   2761       O  
ATOM   2810  N   THR A1157     -32.246  39.039 -33.388  1.00 67.57           N  
ANISOU 2810  N   THR A1157     6848  14206   4621   1738    862   2975       N  
ATOM   2811  CA  THR A1157     -32.555  37.623 -33.142  1.00 67.57           C  
ANISOU 2811  CA  THR A1157     6434  14336   4903   1530   1047   3454       C  
ATOM   2812  C   THR A1157     -32.073  36.762 -34.308  1.00 71.24           C  
ANISOU 2812  C   THR A1157     6850  14401   5817    938    805   3402       C  
ATOM   2813  O   THR A1157     -31.753  37.298 -35.365  1.00 71.55           O  
ANISOU 2813  O   THR A1157     7096  14156   5935    730    548   3067       O  
ATOM   2814  CB  THR A1157     -34.079  37.427 -32.947  1.00 75.50           C  
ANISOU 2814  CB  THR A1157     6933  15672   6080   1714   1310   3947       C  
ATOM   2815  OG1 THR A1157     -34.770  37.965 -34.079  1.00 71.98           O  
ANISOU 2815  OG1 THR A1157     6397  15066   5888   1560   1124   3844       O  
ATOM   2816  CG2 THR A1157     -34.610  38.018 -31.625  1.00 74.02           C  
ANISOU 2816  CG2 THR A1157     6731  15983   5409   2391   1657   4113       C  
ATOM   2817  N   TRP A1158     -32.049  35.430 -34.122  1.00 67.91           N  
ANISOU 2817  N   TRP A1158     6163  13956   5683    699    894   3747       N  
ATOM   2818  CA  TRP A1158     -31.650  34.456 -35.141  1.00 67.99           C  
ANISOU 2818  CA  TRP A1158     6143  13573   6119    193    674   3701       C  
ATOM   2819  C   TRP A1158     -32.875  33.912 -35.912  1.00 73.79           C  
ANISOU 2819  C   TRP A1158     6472  14232   7331    -79    595   3976       C  
ATOM   2820  O   TRP A1158     -33.047  32.695 -36.034  1.00 73.93           O  
ANISOU 2820  O   TRP A1158     6246  14083   7760   -379    565   4255       O  
ATOM   2821  CB  TRP A1158     -30.870  33.296 -34.499  1.00 66.52           C  
ANISOU 2821  CB  TRP A1158     5935  13325   6016     93    770   3902       C  
ATOM   2822  CG  TRP A1158     -29.677  33.706 -33.692  1.00 67.20           C  
ANISOU 2822  CG  TRP A1158     6355  13516   5663    338    811   3689       C  
ATOM   2823  CD1 TRP A1158     -29.525  33.580 -32.347  1.00 69.93           C  
ANISOU 2823  CD1 TRP A1158     6668  14198   5705    672   1044   3932       C  
ATOM   2824  CD2 TRP A1158     -28.459  34.285 -34.182  1.00 66.99           C  
ANISOU 2824  CD2 TRP A1158     6720  13274   5461    259    589   3222       C  
ATOM   2825  NE1 TRP A1158     -28.288  34.040 -31.964  1.00 69.13           N  
ANISOU 2825  NE1 TRP A1158     6927  14087   5250    790    931   3607       N  
ATOM   2826  CE2 TRP A1158     -27.612  34.482 -33.068  1.00 70.72           C  
ANISOU 2826  CE2 TRP A1158     7368  13944   5557    524    656   3190       C  
ATOM   2827  CE3 TRP A1158     -28.009  34.687 -35.454  1.00 68.02           C  
ANISOU 2827  CE3 TRP A1158     7051  13093   5702      4    339   2862       C  
ATOM   2828  CZ2 TRP A1158     -26.339  35.048 -33.184  1.00 70.09           C  
ANISOU 2828  CZ2 TRP A1158     7617  13734   5280    493    451   2822       C  
ATOM   2829  CZ3 TRP A1158     -26.747  35.245 -35.568  1.00 69.47           C  
ANISOU 2829  CZ3 TRP A1158     7547  13168   5680     -3    196   2541       C  
ATOM   2830  CH2 TRP A1158     -25.926  35.419 -34.443  1.00 70.15           C  
ANISOU 2830  CH2 TRP A1158     7764  13428   5461    216    237   2527       C  
ATOM   2831  N   ASP A1159     -33.716  34.813 -36.442  1.00 70.88           N  
ANISOU 2831  N   ASP A1159     6033  13959   6939     18    523   3901       N  
ATOM   2832  CA  ASP A1159     -34.920  34.437 -37.184  1.00 70.53           C  
ANISOU 2832  CA  ASP A1159     5579  13885   7335   -228    394   4161       C  
ATOM   2833  C   ASP A1159     -34.678  34.296 -38.679  1.00 73.84           C  
ANISOU 2833  C   ASP A1159     6180  13916   7961   -625     -5   3810       C  
ATOM   2834  O   ASP A1159     -35.414  33.565 -39.346  1.00 73.65           O  
ANISOU 2834  O   ASP A1159     5866  13753   8366   -952   -212   3980       O  
ATOM   2835  CB  ASP A1159     -36.074  35.402 -36.880  1.00 72.47           C  
ANISOU 2835  CB  ASP A1159     5561  14512   7462    142    562   4371       C  
ATOM   2836  CG  ASP A1159     -36.575  35.339 -35.441  1.00 85.16           C  
ANISOU 2836  CG  ASP A1159     6882  16570   8904    557    992   4834       C  
ATOM   2837  OD1 ASP A1159     -36.513  34.241 -34.829  1.00 84.84           O  
ANISOU 2837  OD1 ASP A1159     6616  16554   9064    420   1133   5203       O  
ATOM   2838  OD2 ASP A1159     -37.047  36.378 -34.933  1.00 93.77           O  
ANISOU 2838  OD2 ASP A1159     7976  17992   9659   1047   1195   4846       O  
ATOM   2839  N   ALA A1160     -33.632  34.974 -39.195  1.00 69.71           N  
ANISOU 2839  N   ALA A1160     6133  13223   7131   -596   -126   3338       N  
ATOM   2840  CA  ALA A1160     -33.227  34.938 -40.597  1.00 68.91           C  
ANISOU 2840  CA  ALA A1160     6268  12811   7103   -886   -454   2993       C  
ATOM   2841  C   ALA A1160     -32.520  33.623 -40.939  1.00 73.10           C  
ANISOU 2841  C   ALA A1160     6885  13024   7865  -1203   -569   2930       C  
ATOM   2842  O   ALA A1160     -32.463  33.263 -42.114  1.00 72.50           O  
ANISOU 2842  O   ALA A1160     6929  12699   7920  -1454   -854   2711       O  
ATOM   2843  CB  ALA A1160     -32.307  36.117 -40.902  1.00 69.41           C  
ANISOU 2843  CB  ALA A1160     6758  12838   6775   -718   -486   2613       C  
ATOM   2844  N   TYR A1161     -32.007  32.895 -39.919  1.00 70.44           N  
ANISOU 2844  N   TYR A1161     6502  12698   7564  -1156   -356   3123       N  
ATOM   2845  CA  TYR A1161     -31.211  31.688 -40.136  1.00 70.87           C  
ANISOU 2845  CA  TYR A1161     6678  12428   7824  -1385   -434   3061       C  
ATOM   2846  C   TYR A1161     -31.800  30.345 -39.699  1.00 82.06           C  
ANISOU 2846  C   TYR A1161     7755  13707   9716  -1590   -416   3466       C  
ATOM   2847  O   TYR A1161     -31.375  29.331 -40.260  1.00 82.02           O  
ANISOU 2847  O   TYR A1161     7876  13322   9965  -1826   -589   3350       O  
ATOM   2848  CB  TYR A1161     -29.831  31.849 -39.486  1.00 69.75           C  
ANISOU 2848  CB  TYR A1161     6823  12318   7361  -1197   -259   2919       C  
ATOM   2849  CG  TYR A1161     -29.027  32.991 -40.065  1.00 67.85           C  
ANISOU 2849  CG  TYR A1161     6928  12095   6758  -1091   -335   2527       C  
ATOM   2850  CD1 TYR A1161     -29.081  34.262 -39.503  1.00 68.78           C  
ANISOU 2850  CD1 TYR A1161     7111  12468   6555   -823   -237   2482       C  
ATOM   2851  CD2 TYR A1161     -28.222  32.807 -41.184  1.00 67.59           C  
ANISOU 2851  CD2 TYR A1161     7158  11814   6709  -1240   -504   2220       C  
ATOM   2852  CE1 TYR A1161     -28.370  35.326 -40.052  1.00 67.32           C  
ANISOU 2852  CE1 TYR A1161     7219  12242   6116   -768   -338   2172       C  
ATOM   2853  CE2 TYR A1161     -27.496  33.860 -41.733  1.00 67.71           C  
ANISOU 2853  CE2 TYR A1161     7434  11862   6430  -1158   -552   1953       C  
ATOM   2854  CZ  TYR A1161     -27.570  35.118 -41.162  1.00 70.91           C  
ANISOU 2854  CZ  TYR A1161     7875  12476   6593   -953   -483   1946       C  
ATOM   2855  OH  TYR A1161     -26.853  36.153 -41.706  1.00 69.20           O  
ANISOU 2855  OH  TYR A1161     7896  12234   6162   -913   -559   1729       O  
ATOM   2856  N   THR A 354     -32.739  30.307 -38.726  1.00 84.19           N  
ANISOU 2856  N   THR A 354     8781  19835   3375    907  -2437   6362       N  
ATOM   2857  CA  THR A 354     -33.345  29.060 -38.203  1.00 84.83           C  
ANISOU 2857  CA  THR A 354     8724  20142   3368    749  -2701   6021       C  
ATOM   2858  C   THR A 354     -32.247  28.230 -37.503  1.00 89.66           C  
ANISOU 2858  C   THR A 354     9559  20413   4094    497  -2591   5558       C  
ATOM   2859  O   THR A 354     -31.601  27.394 -38.147  1.00 90.86           O  
ANISOU 2859  O   THR A 354     9784  20758   3979    229  -2597   5244       O  
ATOM   2860  CB  THR A 354     -34.109  28.264 -39.311  1.00 94.93           C  
ANISOU 2860  CB  THR A 354     9827  22203   4040    611  -3084   6011       C  
ATOM   2861  OG1 THR A 354     -34.582  29.141 -40.340  1.00 90.37           O  
ANISOU 2861  OG1 THR A 354     9034  21845   3457    756  -2970   6344       O  
ATOM   2862  CG2 THR A 354     -35.243  27.419 -38.749  1.00 96.16           C  
ANISOU 2862  CG2 THR A 354     9673  22558   4307    540  -3320   5802       C  
ATOM   2863  N   PHE A 355     -31.998  28.505 -36.209  1.00 84.47           N  
ANISOU 2863  N   PHE A 355     8976  19206   3914    582  -2418   5481       N  
ATOM   2864  CA  PHE A 355     -30.916  27.867 -35.466  1.00 83.79           C  
ANISOU 2864  CA  PHE A 355     9047  18726   4064    363  -2235   5048       C  
ATOM   2865  C   PHE A 355     -31.331  26.728 -34.537  1.00 88.65           C  
ANISOU 2865  C   PHE A 355     9505  19276   4904    218  -2326   4632       C  
ATOM   2866  O   PHE A 355     -32.396  26.772 -33.919  1.00 89.00           O  
ANISOU 2866  O   PHE A 355     9343  19362   5110    354  -2451   4723       O  
ATOM   2867  CB  PHE A 355     -30.119  28.927 -34.675  1.00 85.09           C  
ANISOU 2867  CB  PHE A 355     9442  18309   4581    501  -1958   5212       C  
ATOM   2868  CG  PHE A 355     -28.996  29.625 -35.410  1.00 85.55           C  
ANISOU 2868  CG  PHE A 355     9742  18283   4478    457  -1771   5395       C  
ATOM   2869  CD1 PHE A 355     -28.692  29.299 -36.727  1.00 87.33           C  
ANISOU 2869  CD1 PHE A 355     9979  18955   4248    322  -1834   5407       C  
ATOM   2870  CD2 PHE A 355     -28.236  30.603 -34.779  1.00 87.04           C  
ANISOU 2870  CD2 PHE A 355    10151  17958   4963    535  -1529   5550       C  
ATOM   2871  CE1 PHE A 355     -27.657  29.940 -37.399  1.00 87.93           C  
ANISOU 2871  CE1 PHE A 355    10262  18976   4171    279  -1647   5595       C  
ATOM   2872  CE2 PHE A 355     -27.203  31.246 -35.456  1.00 89.69           C  
ANISOU 2872  CE2 PHE A 355    10695  18226   5159    465  -1355   5736       C  
ATOM   2873  CZ  PHE A 355     -26.929  30.918 -36.765  1.00 87.45           C  
ANISOU 2873  CZ  PHE A 355    10399  18403   4424    345  -1411   5774       C  
ATOM   2874  N   SER A 356     -30.441  25.729 -34.411  1.00 84.75           N  
ANISOU 2874  N   SER A 356     9110  18662   4427    -48  -2241   4191       N  
ATOM   2875  CA  SER A 356     -30.606  24.564 -33.545  1.00 84.32           C  
ANISOU 2875  CA  SER A 356     8957  18489   4590   -217  -2289   3771       C  
ATOM   2876  C   SER A 356     -30.129  24.868 -32.117  1.00 87.66           C  
ANISOU 2876  C   SER A 356     9462  18359   5484   -132  -2087   3708       C  
ATOM   2877  O   SER A 356     -29.373  25.821 -31.892  1.00 87.26           O  
ANISOU 2877  O   SER A 356     9593  17996   5564    -20  -1887   3888       O  
ATOM   2878  CB  SER A 356     -29.835  23.370 -34.106  1.00 88.11           C  
ANISOU 2878  CB  SER A 356     9528  19091   4859   -509  -2279   3343       C  
ATOM   2879  OG  SER A 356     -28.433  23.493 -33.912  1.00 97.77           O  
ANISOU 2879  OG  SER A 356    10974  19988   6187   -558  -2017   3222       O  
ATOM   2880  N   LEU A 357     -30.537  24.023 -31.164  1.00 83.51           N  
ANISOU 2880  N   LEU A 357     8808  17721   5200   -211  -2141   3440       N  
ATOM   2881  CA  LEU A 357     -30.155  24.162 -29.767  1.00 83.22           C  
ANISOU 2881  CA  LEU A 357     8826  17214   5581   -148  -1974   3345       C  
ATOM   2882  C   LEU A 357     -28.655  23.908 -29.547  1.00 87.80           C  
ANISOU 2882  C   LEU A 357     9623  17491   6245   -295  -1755   3097       C  
ATOM   2883  O   LEU A 357     -27.929  23.529 -30.471  1.00 88.21           O  
ANISOU 2883  O   LEU A 357     9774  17703   6039   -443  -1726   2975       O  
ATOM   2884  CB  LEU A 357     -31.012  23.244 -28.872  1.00 83.02           C  
ANISOU 2884  CB  LEU A 357     8589  17199   5756   -207  -2095   3142       C  
ATOM   2885  CG  LEU A 357     -32.453  23.683 -28.641  1.00 87.35           C  
ANISOU 2885  CG  LEU A 357     8894  17947   6346     -6  -2253   3424       C  
ATOM   2886  CD1 LEU A 357     -33.331  22.496 -28.339  1.00 87.37           C  
ANISOU 2886  CD1 LEU A 357     8656  18153   6388   -176  -2434   3202       C  
ATOM   2887  CD2 LEU A 357     -32.550  24.708 -27.523  1.00 89.73           C  
ANISOU 2887  CD2 LEU A 357     9237  17883   6973    274  -2096   3639       C  
ATOM   2888  N   VAL A 358     -28.202  24.164 -28.320  1.00 83.52           N  
ANISOU 2888  N   VAL A 358     9144  16535   6053   -239  -1599   3037       N  
ATOM   2889  CA  VAL A 358     -26.828  24.004 -27.861  1.00 82.94           C  
ANISOU 2889  CA  VAL A 358     9236  16159   6118   -356  -1393   2829       C  
ATOM   2890  C   VAL A 358     -26.317  22.553 -28.032  1.00 84.57           C  
ANISOU 2890  C   VAL A 358     9421  16462   6252   -585  -1410   2425       C  
ATOM   2891  O   VAL A 358     -26.884  21.608 -27.472  1.00 84.23           O  
ANISOU 2891  O   VAL A 358     9253  16414   6336   -648  -1502   2215       O  
ATOM   2892  CB  VAL A 358     -26.674  24.538 -26.399  1.00 87.12           C  
ANISOU 2892  CB  VAL A 358     9805  16266   7032   -243  -1262   2851       C  
ATOM   2893  CG1 VAL A 358     -27.648  23.852 -25.432  1.00 86.86           C  
ANISOU 2893  CG1 VAL A 358     9586  16219   7199   -205  -1369   2725       C  
ATOM   2894  CG2 VAL A 358     -25.228  24.455 -25.900  1.00 86.96           C  
ANISOU 2894  CG2 VAL A 358     9934  15962   7146   -369  -1060   2667       C  
ATOM   2895  N   LYS A 359     -25.252  22.392 -28.825  1.00 78.87           N  
ANISOU 2895  N   LYS A 359     8825  15822   5320   -701  -1310   2330       N  
ATOM   2896  CA  LYS A 359     -24.612  21.096 -29.014  1.00 77.23           C  
ANISOU 2896  CA  LYS A 359     8637  15666   5040   -882  -1280   1951       C  
ATOM   2897  C   LYS A 359     -23.575  20.996 -27.890  1.00 76.07           C  
ANISOU 2897  C   LYS A 359     8553  15150   5201   -896  -1082   1812       C  
ATOM   2898  O   LYS A 359     -22.508  21.604 -27.979  1.00 76.27           O  
ANISOU 2898  O   LYS A 359     8689  15071   5218   -900   -909   1894       O  
ATOM   2899  CB  LYS A 359     -23.971  20.998 -30.413  1.00 80.25           C  
ANISOU 2899  CB  LYS A 359     9120  16339   5034   -966  -1246   1927       C  
ATOM   2900  CG  LYS A 359     -23.536  19.591 -30.809  1.00 95.44           C  
ANISOU 2900  CG  LYS A 359    11064  18393   6807  -1129  -1262   1527       C  
ATOM   2901  CD  LYS A 359     -23.757  19.339 -32.303  1.00103.56           C  
ANISOU 2901  CD  LYS A 359    12131  19844   7372  -1197  -1358   1518       C  
ATOM   2902  CE  LYS A 359     -22.509  19.545 -33.135  1.00110.51           C  
ANISOU 2902  CE  LYS A 359    13154  20805   8031  -1222  -1154   1496       C  
ATOM   2903  NZ  LYS A 359     -22.751  19.254 -34.572  1.00115.68           N  
ANISOU 2903  NZ  LYS A 359    13853  21893   8208  -1290  -1246   1449       N  
ATOM   2904  N   GLU A 360     -23.932  20.307 -26.797  1.00 68.04           N  
ANISOU 2904  N   GLU A 360     7449  13948   4455   -905  -1112   1640       N  
ATOM   2905  CA  GLU A 360     -23.056  20.153 -25.636  1.00 66.14           C  
ANISOU 2905  CA  GLU A 360     7240  13386   4503   -911   -950   1516       C  
ATOM   2906  C   GLU A 360     -21.968  19.126 -25.933  1.00 64.58           C  
ANISOU 2906  C   GLU A 360     7099  13204   4235  -1033   -839   1225       C  
ATOM   2907  O   GLU A 360     -22.202  17.915 -25.828  1.00 63.00           O  
ANISOU 2907  O   GLU A 360     6857  13022   4060  -1107   -898    966       O  
ATOM   2908  CB  GLU A 360     -23.856  19.800 -24.360  1.00 67.84           C  
ANISOU 2908  CB  GLU A 360     7339  13427   5012   -861  -1017   1464       C  
ATOM   2909  CG  GLU A 360     -24.639  20.967 -23.771  1.00 79.87           C  
ANISOU 2909  CG  GLU A 360     8827  14858   6663   -693  -1053   1753       C  
ATOM   2910  CD  GLU A 360     -25.900  20.605 -23.006  1.00 95.92           C  
ANISOU 2910  CD  GLU A 360    10694  16896   8856   -630  -1183   1754       C  
ATOM   2911  OE1 GLU A 360     -25.805  19.819 -22.036  1.00 85.89           O  
ANISOU 2911  OE1 GLU A 360     9372  15465   7795   -672  -1148   1572       O  
ATOM   2912  OE2 GLU A 360     -26.984  21.115 -23.375  1.00 84.83           O  
ANISOU 2912  OE2 GLU A 360     9197  15673   7361   -530  -1316   1958       O  
ATOM   2913  N   LYS A 361     -20.775  19.626 -26.328  1.00 58.30           N  
ANISOU 2913  N   LYS A 361     6400  12401   3350  -1051   -669   1279       N  
ATOM   2914  CA  LYS A 361     -19.611  18.812 -26.693  1.00 56.72           C  
ANISOU 2914  CA  LYS A 361     6246  12245   3059  -1129   -527   1044       C  
ATOM   2915  C   LYS A 361     -19.102  18.045 -25.484  1.00 57.62           C  
ANISOU 2915  C   LYS A 361     6311  12115   3466  -1133   -448    839       C  
ATOM   2916  O   LYS A 361     -19.245  18.542 -24.367  1.00 56.42           O  
ANISOU 2916  O   LYS A 361     6116  11748   3572  -1086   -445    938       O  
ATOM   2917  CB  LYS A 361     -18.490  19.684 -27.288  1.00 59.02           C  
ANISOU 2917  CB  LYS A 361     6614  12596   3213  -1144   -355   1208       C  
ATOM   2918  CG  LYS A 361     -18.935  20.642 -28.395  1.00 73.58           C  
ANISOU 2918  CG  LYS A 361     8516  14659   4782  -1125   -412   1483       C  
ATOM   2919  CD  LYS A 361     -18.767  20.080 -29.815  1.00 82.39           C  
ANISOU 2919  CD  LYS A 361     9675  16124   5507  -1176   -425   1373       C  
ATOM   2920  CE  LYS A 361     -19.505  20.884 -30.867  1.00 88.51           C  
ANISOU 2920  CE  LYS A 361    10480  17152   5999  -1143   -539   1652       C  
ATOM   2921  NZ  LYS A 361     -19.046  22.299 -30.928  1.00 96.32           N  
ANISOU 2921  NZ  LYS A 361    11531  18060   7005  -1108   -422   2009       N  
ATOM   2922  N   ALA A 362     -18.511  16.836 -25.706  1.00 52.85           N  
ANISOU 2922  N   ALA A 362     5723  11545   2813  -1175   -381    557       N  
ATOM   2923  CA  ALA A 362     -17.951  15.932 -24.678  1.00 51.73           C  
ANISOU 2923  CA  ALA A 362     5538  11195   2921  -1162   -296    357       C  
ATOM   2924  C   ALA A 362     -17.154  16.649 -23.563  1.00 52.85           C  
ANISOU 2924  C   ALA A 362     5631  11144   3306  -1126   -175    486       C  
ATOM   2925  O   ALA A 362     -17.346  16.333 -22.390  1.00 52.59           O  
ANISOU 2925  O   ALA A 362     5533  10921   3527  -1097   -197    442       O  
ATOM   2926  CB  ALA A 362     -17.104  14.848 -25.329  1.00 52.35           C  
ANISOU 2926  CB  ALA A 362     5674  11356   2860  -1175   -178     96       C  
ATOM   2927  N   ALA A 363     -16.313  17.642 -23.934  1.00 47.02           N  
ANISOU 2927  N   ALA A 363     4924  10467   2476  -1143    -59    656       N  
ATOM   2928  CA  ALA A 363     -15.501  18.463 -23.027  1.00 45.31           C  
ANISOU 2928  CA  ALA A 363     4672  10096   2446  -1155     48    784       C  
ATOM   2929  C   ALA A 363     -16.355  19.297 -22.056  1.00 45.55           C  
ANISOU 2929  C   ALA A 363     4701   9932   2676  -1122    -54    941       C  
ATOM   2930  O   ALA A 363     -16.021  19.392 -20.885  1.00 44.48           O  
ANISOU 2930  O   ALA A 363     4518   9623   2761  -1117    -17    924       O  
ATOM   2931  CB  ALA A 363     -14.598  19.376 -23.834  1.00 45.95           C  
ANISOU 2931  CB  ALA A 363     4798  10304   2355  -1217    176    950       C  
ATOM   2932  N   LEU A 364     -17.443  19.899 -22.550  1.00 40.78           N  
ANISOU 2932  N   LEU A 364     4142   9374   1977  -1086   -177   1094       N  
ATOM   2933  CA  LEU A 364     -18.378  20.714 -21.777  1.00 39.50           C  
ANISOU 2933  CA  LEU A 364     3984   9049   1975  -1012   -266   1254       C  
ATOM   2934  C   LEU A 364     -19.171  19.827 -20.813  1.00 41.21           C  
ANISOU 2934  C   LEU A 364     4103   9179   2376   -963   -361   1107       C  
ATOM   2935  O   LEU A 364     -19.359  20.211 -19.663  1.00 41.93           O  
ANISOU 2935  O   LEU A 364     4172   9085   2675   -914   -356   1148       O  
ATOM   2936  CB  LEU A 364     -19.336  21.456 -22.742  1.00 39.44           C  
ANISOU 2936  CB  LEU A 364     4029   9172   1784   -958   -371   1468       C  
ATOM   2937  CG  LEU A 364     -20.173  22.584 -22.148  1.00 43.85           C  
ANISOU 2937  CG  LEU A 364     4619   9566   2475   -845   -424   1693       C  
ATOM   2938  CD1 LEU A 364     -19.383  23.877 -22.082  1.00 44.30           C  
ANISOU 2938  CD1 LEU A 364     4806   9461   2564   -871   -297   1885       C  
ATOM   2939  CD2 LEU A 364     -21.438  22.789 -22.943  1.00 43.65           C  
ANISOU 2939  CD2 LEU A 364     4568   9723   2292   -751   -576   1847       C  
ATOM   2940  N   ARG A 365     -19.627  18.645 -21.283  1.00 35.09           N  
ANISOU 2940  N   ARG A 365     3280   8536   1519   -987   -441    935       N  
ATOM   2941  CA  ARG A 365     -20.380  17.675 -20.493  1.00 33.85           C  
ANISOU 2941  CA  ARG A 365     3029   8308   1525   -973   -529    799       C  
ATOM   2942  C   ARG A 365     -19.521  17.053 -19.378  1.00 35.48           C  
ANISOU 2942  C   ARG A 365     3197   8344   1940   -976   -419    659       C  
ATOM   2943  O   ARG A 365     -20.022  16.878 -18.270  1.00 35.75           O  
ANISOU 2943  O   ARG A 365     3160   8251   2171   -934   -454    660       O  
ATOM   2944  CB  ARG A 365     -21.013  16.595 -21.384  1.00 33.96           C  
ANISOU 2944  CB  ARG A 365     3029   8493   1383  -1039   -642    642       C  
ATOM   2945  CG  ARG A 365     -22.192  17.090 -22.216  1.00 39.69           C  
ANISOU 2945  CG  ARG A 365     3734   9414   1932  -1030   -805    791       C  
ATOM   2946  CD  ARG A 365     -22.999  15.930 -22.767  1.00 51.43           C  
ANISOU 2946  CD  ARG A 365     5177  11045   3318  -1129   -949    611       C  
ATOM   2947  NE  ARG A 365     -24.218  15.705 -21.985  1.00 63.06           N  
ANISOU 2947  NE  ARG A 365     6513  12487   4958  -1118  -1084    658       N  
ATOM   2948  CZ  ARG A 365     -24.559  14.551 -21.417  1.00 66.49           C  
ANISOU 2948  CZ  ARG A 365     6888  12835   5540  -1199  -1126    479       C  
ATOM   2949  NH1 ARG A 365     -23.781  13.481 -21.548  1.00 41.88           N  
ANISOU 2949  NH1 ARG A 365     3855   9624   2433  -1278  -1042    230       N  
ATOM   2950  NH2 ARG A 365     -25.690  14.451 -20.730  1.00 48.11           N  
ANISOU 2950  NH2 ARG A 365     4415  10513   3350  -1193  -1242    562       N  
ATOM   2951  N   THR A 366     -18.234  16.756 -19.658  1.00 29.59           N  
ANISOU 2951  N   THR A 366     2482   7620   1140  -1014   -281    561       N  
ATOM   2952  CA  THR A 366     -17.288  16.182 -18.692  1.00 27.53           C  
ANISOU 2952  CA  THR A 366     2167   7243   1051  -1002   -169    453       C  
ATOM   2953  C   THR A 366     -17.026  17.169 -17.558  1.00 28.67           C  
ANISOU 2953  C   THR A 366     2285   7252   1356   -984   -134    589       C  
ATOM   2954  O   THR A 366     -17.045  16.770 -16.397  1.00 28.66           O  
ANISOU 2954  O   THR A 366     2215   7137   1539   -950   -133    543       O  
ATOM   2955  CB  THR A 366     -15.982  15.745 -19.401  1.00 33.52           C  
ANISOU 2955  CB  THR A 366     2946   8107   1683  -1025    -23    348       C  
ATOM   2956  OG1 THR A 366     -16.296  14.811 -20.436  1.00 24.74           O  
ANISOU 2956  OG1 THR A 366     1888   7104    407  -1036    -56    189       O  
ATOM   2957  CG2 THR A 366     -14.956  15.128 -18.441  1.00 33.93           C  
ANISOU 2957  CG2 THR A 366     2916   8075   1902   -989     94    261       C  
ATOM   2958  N   LEU A 367     -16.789  18.450 -17.889  1.00 24.16           N  
ANISOU 2958  N   LEU A 367     1783   6687    709  -1013   -105    756       N  
ATOM   2959  CA  LEU A 367     -16.496  19.521 -16.926  1.00 23.78           C  
ANISOU 2959  CA  LEU A 367     1755   6490    790  -1023    -67    871       C  
ATOM   2960  C   LEU A 367     -17.644  19.704 -15.940  1.00 29.52           C  
ANISOU 2960  C   LEU A 367     2463   7087   1665   -933   -163    909       C  
ATOM   2961  O   LEU A 367     -17.412  19.828 -14.740  1.00 30.07           O  
ANISOU 2961  O   LEU A 367     2501   7039   1885   -921   -135    886       O  
ATOM   2962  CB  LEU A 367     -16.181  20.837 -17.670  1.00 23.30           C  
ANISOU 2962  CB  LEU A 367     1807   6437    609  -1080    -24   1053       C  
ATOM   2963  CG  LEU A 367     -15.774  22.054 -16.847  1.00 26.94           C  
ANISOU 2963  CG  LEU A 367     2336   6717   1184  -1129     26   1163       C  
ATOM   2964  CD1 LEU A 367     -14.423  21.835 -16.146  1.00 27.09           C  
ANISOU 2964  CD1 LEU A 367     2277   6739   1278  -1235    128   1072       C  
ATOM   2965  CD2 LEU A 367     -15.743  23.293 -17.723  1.00 26.70           C  
ANISOU 2965  CD2 LEU A 367     2444   6664   1039  -1173     53   1368       C  
ATOM   2966  N   SER A 368     -18.878  19.693 -16.458  1.00 26.00           N  
ANISOU 2966  N   SER A 368     2024   6695   1160   -868   -275    970       N  
ATOM   2967  CA  SER A 368     -20.102  19.805 -15.691  1.00 24.86           C  
ANISOU 2967  CA  SER A 368     1833   6481   1131   -765   -365   1023       C  
ATOM   2968  C   SER A 368     -20.275  18.576 -14.805  1.00 28.48           C  
ANISOU 2968  C   SER A 368     2173   6921   1728   -760   -384    875       C  
ATOM   2969  O   SER A 368     -20.592  18.744 -13.632  1.00 30.27           O  
ANISOU 2969  O   SER A 368     2359   7044   2097   -698   -380    893       O  
ATOM   2970  CB  SER A 368     -21.288  19.968 -16.631  1.00 28.88           C  
ANISOU 2970  CB  SER A 368     2337   7121   1516   -712   -484   1132       C  
ATOM   2971  OG  SER A 368     -22.500  20.090 -15.908  1.00 42.48           O  
ANISOU 2971  OG  SER A 368     3984   8811   3346   -599   -563   1205       O  
ATOM   2972  N   ALA A 369     -20.025  17.355 -15.337  1.00 23.13           N  
ANISOU 2972  N   ALA A 369     1456   6329   1004   -821   -391    728       N  
ATOM   2973  CA  ALA A 369     -20.121  16.096 -14.584  1.00 22.73           C  
ANISOU 2973  CA  ALA A 369     1314   6233   1091   -823   -398    596       C  
ATOM   2974  C   ALA A 369     -19.071  15.985 -13.448  1.00 29.27           C  
ANISOU 2974  C   ALA A 369     2110   6961   2052   -809   -289    555       C  
ATOM   2975  O   ALA A 369     -19.438  15.591 -12.339  1.00 29.69           O  
ANISOU 2975  O   ALA A 369     2087   6944   2251   -765   -303    552       O  
ATOM   2976  CB  ALA A 369     -20.031  14.901 -15.520  1.00 22.86           C  
ANISOU 2976  CB  ALA A 369     1342   6326   1018   -890   -416    440       C  
ATOM   2977  N   ILE A 370     -17.782  16.346 -13.710  1.00 25.93           N  
ANISOU 2977  N   ILE A 370     1726   6558   1567   -851   -184    541       N  
ATOM   2978  CA  ILE A 370     -16.710  16.292 -12.696  1.00 25.69           C  
ANISOU 2978  CA  ILE A 370     1639   6484   1637   -852    -93    515       C  
ATOM   2979  C   ILE A 370     -16.887  17.394 -11.628  1.00 30.54           C  
ANISOU 2979  C   ILE A 370     2268   7008   2327   -838   -103    611       C  
ATOM   2980  O   ILE A 370     -16.435  17.206 -10.496  1.00 31.57           O  
ANISOU 2980  O   ILE A 370     2331   7108   2557   -825    -72    586       O  
ATOM   2981  CB  ILE A 370     -15.253  16.253 -13.281  1.00 28.24           C  
ANISOU 2981  CB  ILE A 370     1958   6899   1873   -909     24    474       C  
ATOM   2982  CG1 ILE A 370     -14.896  17.558 -14.050  1.00 28.06           C  
ANISOU 2982  CG1 ILE A 370     2026   6917   1719   -990     53    583       C  
ATOM   2983  CG2 ILE A 370     -15.030  14.986 -14.125  1.00 28.40           C  
ANISOU 2983  CG2 ILE A 370     1971   6987   1834   -884     58    341       C  
ATOM   2984  CD1 ILE A 370     -13.449  17.801 -14.356  1.00 32.23           C  
ANISOU 2984  CD1 ILE A 370     2521   7545   2179  -1070    174    588       C  
ATOM   2985  N   LEU A 371     -17.520  18.536 -11.993  1.00 26.56           N  
ANISOU 2985  N   LEU A 371     1862   6463   1767   -832   -142    721       N  
ATOM   2986  CA  LEU A 371     -17.792  19.637 -11.062  1.00 26.56           C  
ANISOU 2986  CA  LEU A 371     1919   6341   1830   -800   -143    796       C  
ATOM   2987  C   LEU A 371     -18.960  19.255 -10.176  1.00 26.98           C  
ANISOU 2987  C   LEU A 371     1904   6362   1984   -684   -205    801       C  
ATOM   2988  O   LEU A 371     -18.889  19.497  -8.974  1.00 27.46           O  
ANISOU 2988  O   LEU A 371     1950   6359   2125   -651   -182    788       O  
ATOM   2989  CB  LEU A 371     -18.052  20.987 -11.785  1.00 27.50           C  
ANISOU 2989  CB  LEU A 371     2186   6395   1867   -806   -143    926       C  
ATOM   2990  CG  LEU A 371     -18.412  22.242 -10.924  1.00 33.09           C  
ANISOU 2990  CG  LEU A 371     3007   6927   2640   -753   -130    997       C  
ATOM   2991  CD1 LEU A 371     -17.406  22.474  -9.771  1.00 33.46           C  
ANISOU 2991  CD1 LEU A 371     3056   6906   2752   -844    -69    910       C  
ATOM   2992  CD2 LEU A 371     -18.498  23.492 -11.790  1.00 34.98           C  
ANISOU 2992  CD2 LEU A 371     3411   7077   2802   -764   -112   1140       C  
ATOM   2993  N   LEU A 372     -20.025  18.646 -10.752  1.00 20.55           N  
ANISOU 2993  N   LEU A 372     1038   5616   1155   -634   -285    820       N  
ATOM   2994  CA  LEU A 372     -21.175  18.177  -9.976  1.00 18.80           C  
ANISOU 2994  CA  LEU A 372      717   5399   1029   -543   -343    841       C  
ATOM   2995  C   LEU A 372     -20.760  17.020  -9.074  1.00 25.01           C  
ANISOU 2995  C   LEU A 372     1399   6184   1919   -563   -314    748       C  
ATOM   2996  O   LEU A 372     -21.297  16.909  -7.964  1.00 25.38           O  
ANISOU 2996  O   LEU A 372     1378   6211   2055   -493   -315    777       O  
ATOM   2997  CB  LEU A 372     -22.331  17.736 -10.849  1.00 17.75           C  
ANISOU 2997  CB  LEU A 372      632   5258    854   -535   -290    879       C  
ATOM   2998  CG  LEU A 372     -23.149  18.824 -11.518  1.00 21.81           C  
ANISOU 2998  CG  LEU A 372     1098   5914   1275   -454   -498   1027       C  
ATOM   2999  CD1 LEU A 372     -24.064  18.220 -12.550  1.00 21.36           C  
ANISOU 2999  CD1 LEU A 372      967   6017   1131   -487   -615   1047       C  
ATOM   3000  CD2 LEU A 372     -23.927  19.675 -10.510  1.00 22.92           C  
ANISOU 3000  CD2 LEU A 372     1229   5986   1495   -300   -484   1133       C  
ATOM   3001  N   ALA A 373     -19.770  16.192  -9.528  1.00 20.73           N  
ANISOU 3001  N   ALA A 373      849   5669   1360   -641   -273    651       N  
ATOM   3002  CA  ALA A 373     -19.249  15.048  -8.782  1.00 19.98           C  
ANISOU 3002  CA  ALA A 373      693   5547   1350   -634   -223    582       C  
ATOM   3003  C   ALA A 373     -18.588  15.535  -7.531  1.00 25.80           C  
ANISOU 3003  C   ALA A 373     1377   6279   2146   -613   -176    602       C  
ATOM   3004  O   ALA A 373     -18.792  14.939  -6.469  1.00 26.95           O  
ANISOU 3004  O   ALA A 373     1437   6420   2384   -562   -172    614       O  
ATOM   3005  CB  ALA A 373     -18.263  14.262  -9.625  1.00 20.58           C  
ANISOU 3005  CB  ALA A 373      756   5668   1395   -690   -179    481       C  
ATOM   3006  N   PHE A 374     -17.828  16.650  -7.643  1.00 21.33           N  
ANISOU 3006  N   PHE A 374      890   5707   1507   -661   -138    613       N  
ATOM   3007  CA  PHE A 374     -17.127  17.305  -6.540  1.00 19.70           C  
ANISOU 3007  CA  PHE A 374      702   5480   1302   -675    -97    613       C  
ATOM   3008  C   PHE A 374     -18.125  17.916  -5.528  1.00 24.52           C  
ANISOU 3008  C   PHE A 374     1316   6041   1959   -593   -126    657       C  
ATOM   3009  O   PHE A 374     -18.003  17.662  -4.330  1.00 24.45           O  
ANISOU 3009  O   PHE A 374     1240   6060   1990   -559   -113    644       O  
ATOM   3010  CB  PHE A 374     -16.151  18.345  -7.089  1.00 20.80           C  
ANISOU 3010  CB  PHE A 374      912   5626   1366   -793    -56    613       C  
ATOM   3011  CG  PHE A 374     -15.349  19.062  -6.043  1.00 23.01           C  
ANISOU 3011  CG  PHE A 374     1199   5902   1643   -863    -28    593       C  
ATOM   3012  CD1 PHE A 374     -14.594  18.352  -5.111  1.00 26.97           C  
ANISOU 3012  CD1 PHE A 374     1564   6506   2176   -866    -11    557       C  
ATOM   3013  CD2 PHE A 374     -15.327  20.448  -5.993  1.00 26.00           C  
ANISOU 3013  CD2 PHE A 374     1727   6172   1980   -933    -22    612       C  
ATOM   3014  CE1 PHE A 374     -13.859  19.018  -4.127  1.00 28.22           C  
ANISOU 3014  CE1 PHE A 374     1719   6698   2306   -953     -4    530       C  
ATOM   3015  CE2 PHE A 374     -14.569  21.115  -5.023  1.00 29.41           C  
ANISOU 3015  CE2 PHE A 374     2182   6596   2399  -1034     -6    567       C  
ATOM   3016  CZ  PHE A 374     -13.837  20.396  -4.101  1.00 27.68           C  
ANISOU 3016  CZ  PHE A 374     1808   6518   2190  -1053     -5    521       C  
ATOM   3017  N   ILE A 375     -19.140  18.665  -6.009  1.00 22.16           N  
ANISOU 3017  N   ILE A 375     1103   5681   1637   -537   -160    717       N  
ATOM   3018  CA  ILE A 375     -20.193  19.259  -5.163  1.00 22.10           C  
ANISOU 3018  CA  ILE A 375     1116   5625   1657   -415   -170    767       C  
ATOM   3019  C   ILE A 375     -20.970  18.157  -4.389  1.00 26.19           C  
ANISOU 3019  C   ILE A 375     1477   6220   2253   -335   -192    787       C  
ATOM   3020  O   ILE A 375     -21.059  18.230  -3.165  1.00 26.38           O  
ANISOU 3020  O   ILE A 375     1470   6257   2297   -276   -162    782       O  
ATOM   3021  CB  ILE A 375     -21.119  20.232  -5.971  1.00 24.92           C  
ANISOU 3021  CB  ILE A 375     1579   5916   1973   -341   -196    857       C  
ATOM   3022  CG1 ILE A 375     -20.297  21.419  -6.541  1.00 25.69           C  
ANISOU 3022  CG1 ILE A 375     1854   5903   2004   -428   -156    858       C  
ATOM   3023  CG2 ILE A 375     -22.266  20.755  -5.111  1.00 24.63           C  
ANISOU 3023  CG2 ILE A 375     1544   5848   1969   -172   -189    914       C  
ATOM   3024  CD1 ILE A 375     -20.936  22.154  -7.734  1.00 35.23           C  
ANISOU 3024  CD1 ILE A 375     3160   7070   3157   -380   -182    972       C  
ATOM   3025  N   LEU A 376     -21.460  17.120  -5.094  1.00 21.77           N  
ANISOU 3025  N   LEU A 376      828   5715   1730   -352   -240    805       N  
ATOM   3026  CA  LEU A 376     -22.211  15.990  -4.525  1.00 20.94           C  
ANISOU 3026  CA  LEU A 376      630   5638   1690   -314   -248    839       C  
ATOM   3027  C   LEU A 376     -21.486  15.245  -3.394  1.00 25.37           C  
ANISOU 3027  C   LEU A 376     1065   6244   2331   -320   -214    814       C  
ATOM   3028  O   LEU A 376     -22.087  15.001  -2.351  1.00 25.55           O  
ANISOU 3028  O   LEU A 376     1003   6308   2398   -248   -202    873       O  
ATOM   3029  CB  LEU A 376     -22.573  15.004  -5.658  1.00 20.70           C  
ANISOU 3029  CB  LEU A 376      633   5589   1643   -386   -282    825       C  
ATOM   3030  CG  LEU A 376     -23.294  13.714  -5.288  1.00 25.03           C  
ANISOU 3030  CG  LEU A 376      923   6230   2356   -412   -357    851       C  
ATOM   3031  CD1 LEU A 376     -24.750  13.976  -4.966  1.00 24.94           C  
ANISOU 3031  CD1 LEU A 376      812   6295   2368   -342   -403    967       C  
ATOM   3032  CD2 LEU A 376     -23.181  12.689  -6.405  1.00 25.78           C  
ANISOU 3032  CD2 LEU A 376     1032   6304   2458   -526   -402    771       C  
ATOM   3033  N   THR A 377     -20.209  14.868  -3.608  1.00 21.68           N  
ANISOU 3033  N   THR A 377      614   5770   1852   -391   -180    744       N  
ATOM   3034  CA  THR A 377     -19.422  14.064  -2.662  1.00 21.27           C  
ANISOU 3034  CA  THR A 377      566   5713   1803   -371   -127    743       C  
ATOM   3035  C   THR A 377     -18.785  14.834  -1.503  1.00 25.71           C  
ANISOU 3035  C   THR A 377     1042   6376   2350   -362   -104    736       C  
ATOM   3036  O   THR A 377     -18.475  14.221  -0.488  1.00 24.19           O  
ANISOU 3036  O   THR A 377      754   6253   2183   -324    -82    771       O  
ATOM   3037  CB  THR A 377     -18.356  13.279  -3.412  1.00 26.79           C  
ANISOU 3037  CB  THR A 377     1168   6450   2560   -433   -106    682       C  
ATOM   3038  OG1 THR A 377     -17.557  14.193  -4.167  1.00 28.75           O  
ANISOU 3038  OG1 THR A 377     1503   6709   2711   -502    -91    628       O  
ATOM   3039  CG2 THR A 377     -18.941  12.172  -4.286  1.00 20.69           C  
ANISOU 3039  CG2 THR A 377      619   5500   1742   -424   -113    664       C  
ATOM   3040  N   TRP A 378     -18.536  16.142  -1.662  1.00 24.45           N  
ANISOU 3040  N   TRP A 378     1000   6186   2105   -401   -102    693       N  
ATOM   3041  CA  TRP A 378     -17.899  16.947  -0.622  1.00 25.02           C  
ANISOU 3041  CA  TRP A 378     1105   6298   2104   -423    -81    654       C  
ATOM   3042  C   TRP A 378     -18.861  17.808   0.169  1.00 28.89           C  
ANISOU 3042  C   TRP A 378     1668   6752   2559   -333    -76    660       C  
ATOM   3043  O   TRP A 378     -18.463  18.362   1.189  1.00 28.49           O  
ANISOU 3043  O   TRP A 378     1649   6739   2436   -344    -59    609       O  
ATOM   3044  CB  TRP A 378     -16.774  17.788  -1.214  1.00 24.93           C  
ANISOU 3044  CB  TRP A 378     1183   6265   2024   -560    -71    588       C  
ATOM   3045  CG  TRP A 378     -15.509  17.031  -1.481  1.00 26.39           C  
ANISOU 3045  CG  TRP A 378     1258   6555   2213   -632    -52    577       C  
ATOM   3046  CD1 TRP A 378     -15.341  15.991  -2.349  1.00 29.50           C  
ANISOU 3046  CD1 TRP A 378     1585   6961   2663   -610    -37    594       C  
ATOM   3047  CD2 TRP A 378     -14.223  17.301  -0.922  1.00 26.41           C  
ANISOU 3047  CD2 TRP A 378     1204   6676   2154   -732    -41    544       C  
ATOM   3048  NE1 TRP A 378     -14.034  15.574  -2.339  1.00 29.51           N  
ANISOU 3048  NE1 TRP A 378     1488   7077   2648   -656     -2    584       N  
ATOM   3049  CE2 TRP A 378     -13.321  16.362  -1.473  1.00 30.93           C  
ANISOU 3049  CE2 TRP A 378     1654   7344   2756   -738    -10    565       C  
ATOM   3050  CE3 TRP A 378     -13.744  18.223   0.025  1.00 27.88           C  
ANISOU 3050  CE3 TRP A 378     1430   6909   2256   -822    -57    492       C  
ATOM   3051  CZ2 TRP A 378     -11.963  16.327  -1.119  1.00 30.27           C  
ANISOU 3051  CZ2 TRP A 378     1450   7430   2622   -816      5    563       C  
ATOM   3052  CZ3 TRP A 378     -12.398  18.192   0.370  1.00 29.40           C  
ANISOU 3052  CZ3 TRP A 378     1511   7268   2391   -939    -59    477       C  
ATOM   3053  CH2 TRP A 378     -11.517  17.280  -0.231  1.00 30.03           C  
ANISOU 3053  CH2 TRP A 378     1438   7468   2504   -932    -28    525       C  
ATOM   3054  N   THR A 379     -20.134  17.902  -0.270  1.00 25.86           N  
ANISOU 3054  N   THR A 379     1300   6312   2214   -239    -89    720       N  
ATOM   3055  CA  THR A 379     -21.179  18.667   0.416  1.00 24.84           C  
ANISOU 3055  CA  THR A 379     1221   6160   2057   -105    -66    743       C  
ATOM   3056  C   THR A 379     -21.462  18.062   1.807  1.00 28.95           C  
ANISOU 3056  C   THR A 379     1621   6807   2571    -24    -38    775       C  
ATOM   3057  O   THR A 379     -21.416  18.842   2.756  1.00 29.67           O  
ANISOU 3057  O   THR A 379     1791   6907   2577     25      1    718       O  
ATOM   3058  CB  THR A 379     -22.421  18.865  -0.489  1.00 24.41           C  
ANISOU 3058  CB  THR A 379     1173   6061   2041    -17    -91    827       C  
ATOM   3059  OG1 THR A 379     -22.112  19.916  -1.405  1.00 22.83           O  
ANISOU 3059  OG1 THR A 379     1141   5735   1800    -60    -94    799       O  
ATOM   3060  CG2 THR A 379     -23.685  19.234   0.272  1.00 18.76           C  
ANISOU 3060  CG2 THR A 379      505   5341   1282    157    -43    892       C  
ATOM   3061  N   PRO A 380     -21.692  16.734   2.004  1.00 25.14           N  
ANISOU 3061  N   PRO A 380      969   6418   2166    -17    -49    860       N  
ATOM   3062  CA  PRO A 380     -21.977  16.242   3.364  1.00 24.75           C  
ANISOU 3062  CA  PRO A 380      809   6498   2096     64    -12    920       C  
ATOM   3063  C   PRO A 380     -20.973  16.667   4.437  1.00 28.28           C  
ANISOU 3063  C   PRO A 380     1297   7024   2424     39     10    840       C  
ATOM   3064  O   PRO A 380     -21.397  17.171   5.486  1.00 27.04           O  
ANISOU 3064  O   PRO A 380     1162   6938   2173    131     50    827       O  
ATOM   3065  CB  PRO A 380     -22.034  14.724   3.181  1.00 26.35           C  
ANISOU 3065  CB  PRO A 380      858   6735   2417     29    -29   1021       C  
ATOM   3066  CG  PRO A 380     -22.523  14.554   1.809  1.00 30.68           C  
ANISOU 3066  CG  PRO A 380     1429   7184   3045    -23    -76   1020       C  
ATOM   3067  CD  PRO A 380     -21.808  15.630   1.028  1.00 26.59           C  
ANISOU 3067  CD  PRO A 380     1068   6581   2455    -78    -88    909       C  
ATOM   3068  N   TYR A 381     -19.654  16.515   4.157  1.00 24.75           N  
ANISOU 3068  N   TYR A 381      857   6583   1964    -86    -17    782       N  
ATOM   3069  CA  TYR A 381     -18.598  16.890   5.098  1.00 24.43           C  
ANISOU 3069  CA  TYR A 381      827   6655   1800   -148    -19    708       C  
ATOM   3070  C   TYR A 381     -18.595  18.383   5.349  1.00 27.12           C  
ANISOU 3070  C   TYR A 381     1359   6919   2026   -177     -9    571       C  
ATOM   3071  O   TYR A 381     -18.500  18.789   6.500  1.00 26.65           O  
ANISOU 3071  O   TYR A 381     1326   6958   1841   -156      4    513       O  
ATOM   3072  CB  TYR A 381     -17.223  16.380   4.638  1.00 26.34           C  
ANISOU 3072  CB  TYR A 381     1002   6944   2063   -269    -47    698       C  
ATOM   3073  CG  TYR A 381     -16.026  17.110   5.216  1.00 29.22           C  
ANISOU 3073  CG  TYR A 381     1395   7415   2292   -393    -71    598       C  
ATOM   3074  CD1 TYR A 381     -15.576  16.843   6.507  1.00 31.48           C  
ANISOU 3074  CD1 TYR A 381     1580   7910   2472   -377    -84    619       C  
ATOM   3075  CD2 TYR A 381     -15.294  18.010   4.446  1.00 30.72           C  
ANISOU 3075  CD2 TYR A 381     1698   7519   2456   -546    -87    497       C  
ATOM   3076  CE1 TYR A 381     -14.474  17.513   7.048  1.00 31.36           C  
ANISOU 3076  CE1 TYR A 381     1576   8025   2314   -520   -125    519       C  
ATOM   3077  CE2 TYR A 381     -14.182  18.677   4.970  1.00 32.23           C  
ANISOU 3077  CE2 TYR A 381     1903   7817   2525   -702   -119    406       C  
ATOM   3078  CZ  TYR A 381     -13.784  18.435   6.277  1.00 42.62           C  
ANISOU 3078  CZ  TYR A 381     3116   9352   3727   -694   -146    407       C  
ATOM   3079  OH  TYR A 381     -12.682  19.077   6.797  1.00 49.28           O  
ANISOU 3079  OH  TYR A 381     3956  10333   4434   -876   -196    311       O  
ATOM   3080  N   ASN A 382     -18.742  19.198   4.292  1.00 23.04           N  
ANISOU 3080  N   ASN A 382      989   6220   1546   -220    -12    521       N  
ATOM   3081  CA  ASN A 382     -18.722  20.650   4.420  1.00 22.80           C  
ANISOU 3081  CA  ASN A 382     1178   6054   1432   -251      8    397       C  
ATOM   3082  C   ASN A 382     -19.934  21.220   5.150  1.00 28.08           C  
ANISOU 3082  C   ASN A 382     1928   6686   2055    -64     65    387       C  
ATOM   3083  O   ASN A 382     -19.811  22.276   5.784  1.00 27.94           O  
ANISOU 3083  O   ASN A 382     2088   6597   1933    -71     95    255       O  
ATOM   3084  CB  ASN A 382     -18.501  21.304   3.087  1.00 21.37           C  
ANISOU 3084  CB  ASN A 382     1125   5689   1305   -340     -2    385       C  
ATOM   3085  CG  ASN A 382     -17.043  21.273   2.706  1.00 37.35           C  
ANISOU 3085  CG  ASN A 382     3125   7757   3308   -555    -36    338       C  
ATOM   3086  OD1 ASN A 382     -16.269  22.168   3.049  1.00 28.62           O  
ANISOU 3086  OD1 ASN A 382     2137   6615   2122   -701    -42    229       O  
ATOM   3087  ND2 ASN A 382     -16.623  20.235   2.009  1.00 30.14           N  
ANISOU 3087  ND2 ASN A 382     2058   6931   2464   -584    -55    414       N  
ATOM   3088  N   ILE A 383     -21.072  20.493   5.134  1.00 24.94           N  
ANISOU 3088  N   ILE A 383     1395   6351   1729     98     86    520       N  
ATOM   3089  CA  ILE A 383     -22.288  20.886   5.864  1.00 24.09           C  
ANISOU 3089  CA  ILE A 383     1307   6266   1578    305    156    544       C  
ATOM   3090  C   ILE A 383     -22.059  20.565   7.324  1.00 28.44           C  
ANISOU 3090  C   ILE A 383     1791   7010   2005    332    183    511       C  
ATOM   3091  O   ILE A 383     -22.450  21.354   8.187  1.00 29.69           O  
ANISOU 3091  O   ILE A 383     2067   7172   2043    442    248    422       O  
ATOM   3092  CB  ILE A 383     -23.572  20.233   5.277  1.00 27.17           C  
ANISOU 3092  CB  ILE A 383     1542   6693   2086    436    160    715       C  
ATOM   3093  CG1 ILE A 383     -23.905  20.768   3.845  1.00 28.17           C  
ANISOU 3093  CG1 ILE A 383     1759   6650   2294    434    130    744       C  
ATOM   3094  CG2 ILE A 383     -24.781  20.350   6.214  1.00 27.49           C  
ANISOU 3094  CG2 ILE A 383     1513   6852   2081    650    240    782       C  
ATOM   3095  CD1 ILE A 383     -24.021  22.366   3.629  1.00 38.39           C  
ANISOU 3095  CD1 ILE A 383     3311   7740   3536    519    180    658       C  
ATOM   3096  N   MET A 384     -21.365  19.430   7.602  1.00 23.32           N  
ANISOU 3096  N   MET A 384      967   6523   1372    239    138    581       N  
ATOM   3097  CA  MET A 384     -20.987  18.998   8.950  1.00 21.43           C  
ANISOU 3097  CA  MET A 384      636   6503   1001    252    149    584       C  
ATOM   3098  C   MET A 384     -20.026  19.992   9.572  1.00 25.18           C  
ANISOU 3098  C   MET A 384     1275   6986   1306    139    130    388       C  
ATOM   3099  O   MET A 384     -20.130  20.222  10.758  1.00 25.43           O  
ANISOU 3099  O   MET A 384     1328   7162   1174    201    163    330       O  
ATOM   3100  CB  MET A 384     -20.371  17.598   8.951  1.00 23.33           C  
ANISOU 3100  CB  MET A 384      668   6882   1317    187    105    724       C  
ATOM   3101  CG  MET A 384     -21.384  16.487   8.831  1.00 26.71           C  
ANISOU 3101  CG  MET A 384      927   7344   1876    292    134    919       C  
ATOM   3102  SD  MET A 384     -20.741  14.896   8.243  1.00 30.68           S  
ANISOU 3102  SD  MET A 384     1257   7855   2544    209     90   1066       S  
ATOM   3103  CE  MET A 384     -19.317  14.855   8.985  1.00 27.08           C  
ANISOU 3103  CE  MET A 384      775   7553   1962    136     58   1019       C  
ATOM   3104  N   VAL A 385     -19.117  20.590   8.780  1.00 23.12           N  
ANISOU 3104  N   VAL A 385     1130   6581   1072    -39     79    283       N  
ATOM   3105  CA  VAL A 385     -18.159  21.621   9.206  1.00 24.14           C  
ANISOU 3105  CA  VAL A 385     1430   6684   1059   -207     48     86       C  
ATOM   3106  C   VAL A 385     -18.917  22.918   9.582  1.00 32.45           C  
ANISOU 3106  C   VAL A 385     2744   7558   2027   -108    121    -66       C  
ATOM   3107  O   VAL A 385     -18.564  23.592  10.555  1.00 33.34           O  
ANISOU 3107  O   VAL A 385     2988   7718   1963   -163    125   -236       O  
ATOM   3108  CB  VAL A 385     -17.068  21.870   8.122  1.00 27.39           C  
ANISOU 3108  CB  VAL A 385     1874   6985   1546   -430    -13     52       C  
ATOM   3109  CG1 VAL A 385     -16.234  23.109   8.430  1.00 27.03           C  
ANISOU 3109  CG1 VAL A 385     2035   6858   1376   -633    -40   -153       C  
ATOM   3110  CG2 VAL A 385     -16.162  20.659   7.974  1.00 27.22           C  
ANISOU 3110  CG2 VAL A 385     1603   7171   1568   -508    -69    171       C  
ATOM   3111  N   LEU A 386     -19.945  23.251   8.807  1.00 31.23           N  
ANISOU 3111  N   LEU A 386     2667   7205   1992     44    179     -5       N  
ATOM   3112  CA  LEU A 386     -20.777  24.431   8.975  1.00 32.27           C  
ANISOU 3112  CA  LEU A 386     3042   7137   2083    196    268   -109       C  
ATOM   3113  C   LEU A 386     -21.618  24.321  10.240  1.00 38.84           C  
ANISOU 3113  C   LEU A 386     3837   8140   2781    411    350   -122       C  
ATOM   3114  O   LEU A 386     -21.682  25.286  11.003  1.00 39.19           O  
ANISOU 3114  O   LEU A 386     4102   8110   2679    455    409   -309       O  
ATOM   3115  CB  LEU A 386     -21.675  24.595   7.749  1.00 32.86           C  
ANISOU 3115  CB  LEU A 386     3138   7023   2325    328    297     21       C  
ATOM   3116  CG  LEU A 386     -21.896  26.005   7.250  1.00 38.98           C  
ANISOU 3116  CG  LEU A 386     4218   7478   3115    369    352    -81       C  
ATOM   3117  CD1 LEU A 386     -20.621  26.582   6.641  1.00 39.45           C  
ANISOU 3117  CD1 LEU A 386     4422   7371   3195     80    286   -171       C  
ATOM   3118  CD2 LEU A 386     -22.946  26.007   6.154  1.00 43.86           C  
ANISOU 3118  CD2 LEU A 386     4800   7994   3870    565    384     93       C  
ATOM   3119  N   VAL A 387     -22.236  23.147  10.495  1.00 35.59           N  
ANISOU 3119  N   VAL A 387     3158   7957   2409    533    361     70       N  
ATOM   3120  CA  VAL A 387     -23.040  22.948  11.707  1.00 35.56           C  
ANISOU 3120  CA  VAL A 387     3083   8159   2269    734    450     94       C  
ATOM   3121  C   VAL A 387     -22.133  22.801  12.971  1.00 39.59           C  
ANISOU 3121  C   VAL A 387     3588   8895   2560    619    417    -23       C  
ATOM   3122  O   VAL A 387     -22.555  23.181  14.049  1.00 38.71           O  
ANISOU 3122  O   VAL A 387     3549   8898   2262    751    497   -114       O  
ATOM   3123  CB  VAL A 387     -24.112  21.828  11.580  1.00 39.58           C  
ANISOU 3123  CB  VAL A 387     3314   8831   2894    891    484    354       C  
ATOM   3124  CG1 VAL A 387     -25.042  22.087  10.393  1.00 38.79           C  
ANISOU 3124  CG1 VAL A 387     3215   8549   2973    996    501    455       C  
ATOM   3125  CG2 VAL A 387     -23.490  20.446  11.482  1.00 39.69           C  
ANISOU 3125  CG2 VAL A 387     3089   9010   2981    745    397    506       C  
ATOM   3126  N   SER A 388     -20.871  22.341  12.804  1.00 36.39           N  
ANISOU 3126  N   SER A 388     3106   8560   2161    379    301    -29       N  
ATOM   3127  CA  SER A 388     -19.820  22.187  13.813  1.00 35.61           C  
ANISOU 3127  CA  SER A 388     2969   8697   1862    229    234   -118       C  
ATOM   3128  C   SER A 388     -19.444  23.534  14.422  1.00 42.72           C  
ANISOU 3128  C   SER A 388     4163   9506   2564    142    242   -414       C  
ATOM   3129  O   SER A 388     -19.075  23.577  15.595  1.00 43.88           O  
ANISOU 3129  O   SER A 388     4313   9887   2473    108    226   -516       O  
ATOM   3130  CB  SER A 388     -18.568  21.620  13.151  1.00 38.17           C  
ANISOU 3130  CB  SER A 388     3166   9055   2281     -2    114    -60       C  
ATOM   3131  OG  SER A 388     -17.923  20.619  13.911  1.00 50.34           O  
ANISOU 3131  OG  SER A 388     4488  10916   3724    -47     56     45       O  
ATOM   3132  N   THR A 389     -19.475  24.623  13.624  1.00 41.05           N  
ANISOU 3132  N   THR A 389     4206   8951   2441     88    262   -552       N  
ATOM   3133  CA  THR A 389     -19.102  25.971  14.074  1.00 42.11           C  
ANISOU 3133  CA  THR A 389     4668   8912   2420    -22    275   -849       C  
ATOM   3134  C   THR A 389     -20.162  26.568  15.012  1.00 51.28           C  
ANISOU 3134  C   THR A 389     6002  10056   3428    244    415   -969       C  
ATOM   3135  O   THR A 389     -19.806  27.150  16.034  1.00 51.34           O  
ANISOU 3135  O   THR A 389     6183  10126   3197    175    418  -1205       O  
ATOM   3136  CB  THR A 389     -18.738  26.902  12.888  1.00 43.23           C  
ANISOU 3136  CB  THR A 389     5032   8673   2723   -179    256   -927       C  
ATOM   3137  OG1 THR A 389     -19.843  27.026  12.003  1.00 44.61           O  
ANISOU 3137  OG1 THR A 389     5239   8628   3084     56    347   -790       O  
ATOM   3138  CG2 THR A 389     -17.538  26.421  12.103  1.00 35.70           C  
ANISOU 3138  CG2 THR A 389     3919   7776   1868   -463    128   -844       C  
ATOM   3139  N   PHE A 390     -21.452  26.392  14.684  1.00 52.26           N  
ANISOU 3139  N   PHE A 390     6063  10122   3671    546    530   -808       N  
ATOM   3140  CA  PHE A 390     -22.579  26.907  15.475  1.00 53.99           C  
ANISOU 3140  CA  PHE A 390     6408  10345   3762    851    689   -884       C  
ATOM   3141  C   PHE A 390     -23.049  25.942  16.557  1.00 61.25           C  
ANISOU 3141  C   PHE A 390     7075  11671   4524   1003    734   -757       C  
ATOM   3142  O   PHE A 390     -23.713  26.363  17.500  1.00 61.66           O  
ANISOU 3142  O   PHE A 390     7231  11811   4387   1215    861   -862       O  
ATOM   3143  CB  PHE A 390     -23.754  27.330  14.562  1.00 56.36           C  
ANISOU 3143  CB  PHE A 390     6767  10386   4262   1111    798   -769       C  
ATOM   3144  CG  PHE A 390     -23.332  28.166  13.370  1.00 59.08           C  
ANISOU 3144  CG  PHE A 390     7340  10336   4772    969    756   -838       C  
ATOM   3145  CD1 PHE A 390     -22.788  29.438  13.544  1.00 62.96           C  
ANISOU 3145  CD1 PHE A 390     8205  10545   5172    846    772  -1122       C  
ATOM   3146  CD2 PHE A 390     -23.410  27.654  12.079  1.00 62.10           C  
ANISOU 3146  CD2 PHE A 390     7567  10638   5391    926    693   -620       C  
ATOM   3147  CE1 PHE A 390     -22.339  30.186  12.444  1.00 64.16           C  
ANISOU 3147  CE1 PHE A 390     8563  10333   5481    686    734  -1158       C  
ATOM   3148  CE2 PHE A 390     -22.982  28.410  10.977  1.00 65.32           C  
ANISOU 3148  CE2 PHE A 390     8178  10710   5932    789    657   -661       C  
ATOM   3149  CZ  PHE A 390     -22.437  29.665  11.168  1.00 63.55           C  
ANISOU 3149  CZ  PHE A 390     8314  10205   5629    667    679   -915       C  
ATOM   3150  N   CYS A 391     -22.677  24.665  16.441  1.00 60.40           N  
ANISOU 3150  N   CYS A 391     6652  11809   4488    899    639   -530       N  
ATOM   3151  CA  CYS A 391     -23.063  23.571  17.336  1.00 61.62           C  
ANISOU 3151  CA  CYS A 391     6536  12342   4535   1016    671   -342       C  
ATOM   3152  C   CYS A 391     -21.796  22.844  17.823  1.00 66.93           C  
ANISOU 3152  C   CYS A 391     7064  13269   5099    775    530   -318       C  
ATOM   3153  O   CYS A 391     -21.221  22.063  17.066  1.00 66.21           O  
ANISOU 3153  O   CYS A 391     6800  13167   5190    634    429   -159       O  
ATOM   3154  CB  CYS A 391     -23.985  22.622  16.568  1.00 62.59           C  
ANISOU 3154  CB  CYS A 391     6399  12476   4905   1154    704    -30       C  
ATOM   3155  SG  CYS A 391     -25.357  21.933  17.528  1.00 66.84           S  
ANISOU 3155  SG  CYS A 391     6714  13335   5345   1452    859    182       S  
ATOM   3156  N   LYS A 392     -21.358  23.091  19.070  1.00 65.89           N  
ANISOU 3156  N   LYS A 392     6999  13377   4657    738    523   -475       N  
ATOM   3157  CA  LYS A 392     -20.153  22.433  19.594  1.00 66.42           C  
ANISOU 3157  CA  LYS A 392     6910  13735   4591    526    382   -438       C  
ATOM   3158  C   LYS A 392     -20.390  20.964  19.968  1.00 69.32           C  
ANISOU 3158  C   LYS A 392     6936  14412   4992    631    386    -96       C  
ATOM   3159  O   LYS A 392     -21.255  20.652  20.801  1.00 67.62           O  
ANISOU 3159  O   LYS A 392     6642  14402   4650    840    499     10       O  
ATOM   3160  CB  LYS A 392     -19.498  23.216  20.754  1.00 69.52           C  
ANISOU 3160  CB  LYS A 392     7487  14305   4621    413    345   -729       C  
ATOM   3161  CG  LYS A 392     -18.213  23.961  20.354  1.00 82.81           C  
ANISOU 3161  CG  LYS A 392     9321  15861   6283     74    194   -958       C  
ATOM   3162  CD  LYS A 392     -17.048  23.026  19.960  1.00 88.58           C  
ANISOU 3162  CD  LYS A 392     9766  16785   7105   -130     36   -762       C  
ATOM   3163  CE  LYS A 392     -15.717  23.737  20.003  1.00 90.85           C  
ANISOU 3163  CE  LYS A 392    10159  17065   7293   -477   -113   -987       C  
ATOM   3164  NZ  LYS A 392     -14.580  22.816  19.739  1.00 90.23           N  
ANISOU 3164  NZ  LYS A 392     9774  17225   7283   -637   -252   -782       N  
ATOM   3165  N   ASP A 393     -19.596  20.073  19.310  1.00 65.56           N  
ANISOU 3165  N   ASP A 393     6264  13952   4695    485    273     81       N  
ATOM   3166  CA  ASP A 393     -19.571  18.605  19.426  1.00 64.63           C  
ANISOU 3166  CA  ASP A 393     5840  14044   4671    540    257    416       C  
ATOM   3167  C   ASP A 393     -20.927  17.966  19.078  1.00 65.96           C  
ANISOU 3167  C   ASP A 393     5896  14124   5040    746    380    644       C  
ATOM   3168  O   ASP A 393     -21.274  16.896  19.589  1.00 65.61           O  
ANISOU 3168  O   ASP A 393     5639  14289   5002    844    419    909       O  
ATOM   3169  CB  ASP A 393     -19.029  18.145  20.798  1.00 66.32           C  
ANISOU 3169  CB  ASP A 393     5928  14688   4585    539    219    481       C  
ATOM   3170  CG  ASP A 393     -17.614  18.617  21.088  1.00 75.47           C  
ANISOU 3170  CG  ASP A 393     7135  15986   5556    301     68    293       C  
ATOM   3171  OD1 ASP A 393     -16.719  18.396  20.226  1.00 73.93           O  
ANISOU 3171  OD1 ASP A 393     6876  15677   5536    138    -32    318       O  
ATOM   3172  OD2 ASP A 393     -17.394  19.200  22.180  1.00 83.81           O  
ANISOU 3172  OD2 ASP A 393     8282  17286   6275    272     51    120       O  
ATOM   3173  N   CYS A 394     -21.662  18.615  18.161  1.00 60.47           N  
ANISOU 3173  N   CYS A 394     5338  13121   4519    796    432    557       N  
ATOM   3174  CA  CYS A 394     -22.962  18.155  17.700  1.00 59.41           C  
ANISOU 3174  CA  CYS A 394     5096  12902   4576    964    531    750       C  
ATOM   3175  C   CYS A 394     -22.840  17.039  16.716  1.00 54.91           C  
ANISOU 3175  C   CYS A 394     4348  12225   4292    884    471    970       C  
ATOM   3176  O   CYS A 394     -23.612  16.089  16.787  1.00 55.07           O  
ANISOU 3176  O   CYS A 394     4182  12321   4422    973    526   1213       O  
ATOM   3177  CB  CYS A 394     -23.792  19.307  17.154  1.00 61.33           C  
ANISOU 3177  CB  CYS A 394     5542  12898   4862   1075    611    584       C  
ATOM   3178  SG  CYS A 394     -24.549  20.312  18.454  1.00 66.49           S  
ANISOU 3178  SG  CYS A 394     6356  13707   5200   1298    763    410       S  
ATOM   3179  N   VAL A 395     -21.849  17.122  15.826  1.00 44.25           N  
ANISOU 3179  N   VAL A 395     3053  10705   3056    708    363    885       N  
ATOM   3180  CA  VAL A 395     -21.599  16.092  14.826  1.00 40.45           C  
ANISOU 3180  CA  VAL A 395     2431  10106   2831    630    309   1056       C  
ATOM   3181  C   VAL A 395     -20.924  14.840  15.484  1.00 40.07           C  
ANISOU 3181  C   VAL A 395     2181  10283   2760    608    276   1262       C  
ATOM   3182  O   VAL A 395     -19.810  14.952  16.016  1.00 38.37           O  
ANISOU 3182  O   VAL A 395     1965  10225   2388    526    209   1195       O  
ATOM   3183  CB  VAL A 395     -20.825  16.630  13.589  1.00 41.78           C  
ANISOU 3183  CB  VAL A 395     2726  10024   3123    474    228    905       C  
ATOM   3184  CG1 VAL A 395     -20.817  15.607  12.461  1.00 41.02           C  
ANISOU 3184  CG1 VAL A 395     2511   9789   3285    427    196   1061       C  
ATOM   3185  CG2 VAL A 395     -21.386  17.964  13.102  1.00 40.92           C  
ANISOU 3185  CG2 VAL A 395     2841   9705   3003    506    264    714       C  
ATOM   3186  N   PRO A 396     -21.596  13.658  15.452  1.00 34.24           N  
ANISOU 3186  N   PRO A 396     1270   9564   2175    679    322   1523       N  
ATOM   3187  CA  PRO A 396     -21.001  12.446  16.031  1.00 33.67           C  
ANISOU 3187  CA  PRO A 396     1025   9663   2104    682    305   1747       C  
ATOM   3188  C   PRO A 396     -19.837  11.881  15.235  1.00 39.41           C  
ANISOU 3188  C   PRO A 396     1721  10273   2979    573    220   1760       C  
ATOM   3189  O   PRO A 396     -19.708  12.147  14.047  1.00 38.82           O  
ANISOU 3189  O   PRO A 396     1731   9957   3061    492    187   1644       O  
ATOM   3190  CB  PRO A 396     -22.151  11.436  16.033  1.00 35.27           C  
ANISOU 3190  CB  PRO A 396     1089   9843   2468    763    387   2007       C  
ATOM   3191  CG  PRO A 396     -23.374  12.193  15.650  1.00 39.98           C  
ANISOU 3191  CG  PRO A 396     1756  10332   3102    815    445   1916       C  
ATOM   3192  CD  PRO A 396     -22.919  13.367  14.872  1.00 35.78           C  
ANISOU 3192  CD  PRO A 396     1417   9624   2553    747    387   1635       C  
ATOM   3193  N   GLU A 397     -19.011  11.056  15.908  1.00 38.14           N  
ANISOU 3193  N   GLU A 397     1426  10305   2761    593    195   1925       N  
ATOM   3194  CA  GLU A 397     -17.837  10.364  15.374  1.00 37.55           C  
ANISOU 3194  CA  GLU A 397     1281  10183   2804    542    136   1986       C  
ATOM   3195  C   GLU A 397     -18.216   9.600  14.100  1.00 40.46           C  
ANISOU 3195  C   GLU A 397     1659  10229   3485    525    161   2049       C  
ATOM   3196  O   GLU A 397     -17.534   9.757  13.089  1.00 41.44           O  
ANISOU 3196  O   GLU A 397     1838  10199   3707    444    117   1925       O  
ATOM   3197  CB  GLU A 397     -17.226   9.430  16.448  1.00 39.02           C  
ANISOU 3197  CB  GLU A 397     1295  10643   2890    631    134   2235       C  
ATOM   3198  CG  GLU A 397     -15.703   9.368  16.418  1.00 57.14           C  
ANISOU 3198  CG  GLU A 397     3511  13049   5153    591     52   2232       C  
ATOM   3199  CD  GLU A 397     -14.963   8.630  17.529  1.00 91.27           C  
ANISOU 3199  CD  GLU A 397     7651  17703   9323    687     29   2467       C  
ATOM   3200  OE1 GLU A 397     -13.719   8.772  17.593  1.00 92.55           O  
ANISOU 3200  OE1 GLU A 397     7735  18045   9386    642    -55   2428       O  
ATOM   3201  OE2 GLU A 397     -15.609   7.909  18.327  1.00 86.19           O  
ANISOU 3201  OE2 GLU A 397     6931  17159   8658    806     93   2709       O  
ATOM   3202  N   THR A 398     -19.354   8.865  14.123  1.00 35.22           N  
ANISOU 3202  N   THR A 398      951   9473   2960    581    231   2221       N  
ATOM   3203  CA  THR A 398     -19.904   8.078  13.009  1.00 34.74           C  
ANISOU 3203  CA  THR A 398      902   9117   3180    542    251   2280       C  
ATOM   3204  C   THR A 398     -20.198   8.932  11.753  1.00 37.93           C  
ANISOU 3204  C   THR A 398     1444   9313   3656    449    214   2043       C  
ATOM   3205  O   THR A 398     -19.814   8.527  10.643  1.00 38.22           O  
ANISOU 3205  O   THR A 398     1521   9142   3858    386    189   1994       O  
ATOM   3206  CB  THR A 398     -21.107   7.288  13.491  1.00 40.43           C  
ANISOU 3206  CB  THR A 398     1534   9841   3987    587    326   2508       C  
ATOM   3207  OG1 THR A 398     -20.698   6.512  14.626  1.00 42.98           O  
ANISOU 3207  OG1 THR A 398     1739  10359   4234    676    361   2746       O  
ATOM   3208  CG2 THR A 398     -21.705   6.397  12.405  1.00 33.31           C  
ANISOU 3208  CG2 THR A 398      643   8641   3371    510    336   2568       C  
ATOM   3209  N   LEU A 399     -20.833  10.114  11.936  1.00 31.63           N  
ANISOU 3209  N   LEU A 399      723   8572   2722    456    218   1901       N  
ATOM   3210  CA  LEU A 399     -21.133  11.052  10.847  1.00 30.08           C  
ANISOU 3210  CA  LEU A 399      662   8198   2569    392    188   1702       C  
ATOM   3211  C   LEU A 399     -19.872  11.572  10.160  1.00 32.93           C  
ANISOU 3211  C   LEU A 399     1116   8491   2905    299    125   1529       C  
ATOM   3212  O   LEU A 399     -19.824  11.595   8.928  1.00 33.18           O  
ANISOU 3212  O   LEU A 399     1213   8330   3063    229     98   1453       O  
ATOM   3213  CB  LEU A 399     -21.990  12.225  11.365  1.00 29.69           C  
ANISOU 3213  CB  LEU A 399      683   8227   2369    461    225   1608       C  
ATOM   3214  CG  LEU A 399     -23.531  12.155  11.262  1.00 32.99           C  
ANISOU 3214  CG  LEU A 399     1044   8624   2868    532    282   1710       C  
ATOM   3215  CD1 LEU A 399     -24.005  12.066   9.817  1.00 33.35           C  
ANISOU 3215  CD1 LEU A 399     1118   8446   3106    455    239   1681       C  
ATOM   3216  CD2 LEU A 399     -24.123  11.071  12.130  1.00 33.22           C  
ANISOU 3216  CD2 LEU A 399      899   8800   2922    588    343   1959       C  
ATOM   3217  N   TRP A 400     -18.841  11.955  10.946  1.00 29.07           N  
ANISOU 3217  N   TRP A 400      618   8185   2242    286     98   1478       N  
ATOM   3218  CA  TRP A 400     -17.554  12.420  10.410  1.00 28.80           C  
ANISOU 3218  CA  TRP A 400      632   8139   2173    177     39   1339       C  
ATOM   3219  C   TRP A 400     -16.895  11.356   9.560  1.00 33.95           C  
ANISOU 3219  C   TRP A 400     1209   8688   3003    164     35   1426       C  
ATOM   3220  O   TRP A 400     -16.386  11.682   8.485  1.00 34.34           O  
ANISOU 3220  O   TRP A 400     1328   8607   3112     79     12   1309       O  
ATOM   3221  CB  TRP A 400     -16.595  12.884  11.504  1.00 27.21           C  
ANISOU 3221  CB  TRP A 400      417   8188   1734    146      0   1293       C  
ATOM   3222  CG  TRP A 400     -16.986  14.164  12.182  1.00 27.26           C  
ANISOU 3222  CG  TRP A 400      536   8270   1553    126     -1   1123       C  
ATOM   3223  CD1 TRP A 400     -17.308  14.325  13.497  1.00 29.84           C  
ANISOU 3223  CD1 TRP A 400      840   8815   1683    201     20   1145       C  
ATOM   3224  CD2 TRP A 400     -16.998  15.476  11.602  1.00 26.48           C  
ANISOU 3224  CD2 TRP A 400      633   8010   1419     27    -18    899       C  
ATOM   3225  NE1 TRP A 400     -17.534  15.651  13.769  1.00 28.60           N  
ANISOU 3225  NE1 TRP A 400      866   8631   1370    160     23    924       N  
ATOM   3226  CE2 TRP A 400     -17.362  16.381  12.623  1.00 29.45           C  
ANISOU 3226  CE2 TRP A 400     1115   8488   1585     55      1    778       C  
ATOM   3227  CE3 TRP A 400     -16.717  15.981  10.319  1.00 27.35           C  
ANISOU 3227  CE3 TRP A 400      848   7898   1645    -79    -39    794       C  
ATOM   3228  CZ2 TRP A 400     -17.488  17.755  12.397  1.00 28.19           C  
ANISOU 3228  CZ2 TRP A 400     1182   8174   1357    -12      4    555       C  
ATOM   3229  CZ3 TRP A 400     -16.890  17.335  10.084  1.00 28.46           C  
ANISOU 3229  CZ3 TRP A 400     1197   7899   1718   -147    -39    604       C  
ATOM   3230  CH2 TRP A 400     -17.263  18.207  11.119  1.00 28.99           C  
ANISOU 3230  CH2 TRP A 400     1383   8031   1599   -112    -16    484       C  
ATOM   3231  N   GLU A 401     -16.954  10.077  10.018  1.00 30.59           N  
ANISOU 3231  N   GLU A 401      655   8305   2664    258     69   1636       N  
ATOM   3232  CA  GLU A 401     -16.414   8.893   9.326  1.00 30.33           C  
ANISOU 3232  CA  GLU A 401      566   8144   2815    286     89   1735       C  
ATOM   3233  C   GLU A 401     -17.090   8.679   7.965  1.00 33.58           C  
ANISOU 3233  C   GLU A 401     1078   8272   3408    231    100   1660       C  
ATOM   3234  O   GLU A 401     -16.407   8.338   7.004  1.00 33.58           O  
ANISOU 3234  O   GLU A 401     1105   8156   3498    205    101   1602       O  
ATOM   3235  CB  GLU A 401     -16.576   7.630  10.186  1.00 31.88           C  
ANISOU 3235  CB  GLU A 401      638   8396   3077    405    138   1992       C  
ATOM   3236  CG  GLU A 401     -15.783   7.679  11.476  1.00 48.02           C  
ANISOU 3236  CG  GLU A 401     2560  10755   4932    475    120   2100       C  
ATOM   3237  CD  GLU A 401     -15.705   6.405  12.297  1.00 81.66           C  
ANISOU 3237  CD  GLU A 401     6692  15084   9251    611    170   2390       C  
ATOM   3238  OE1 GLU A 401     -14.615   6.125  12.847  1.00 92.68           O  
ANISOU 3238  OE1 GLU A 401     7968  16698  10547    684    149   2495       O  
ATOM   3239  OE2 GLU A 401     -16.727   5.688  12.394  1.00 77.11           O  
ANISOU 3239  OE2 GLU A 401     6125  14352   8820    639    228   2528       O  
ATOM   3240  N   LEU A 402     -18.429   8.877   7.893  1.00 28.02           N  
ANISOU 3240  N   LEU A 402      445   7471   2729    216    107   1664       N  
ATOM   3241  CA  LEU A 402     -19.209   8.739   6.668  1.00 26.32           C  
ANISOU 3241  CA  LEU A 402      462   6958   2580    146     91   1600       C  
ATOM   3242  C   LEU A 402     -18.996   9.941   5.733  1.00 30.36           C  
ANISOU 3242  C   LEU A 402      915   7510   3112     73     57   1397       C  
ATOM   3243  O   LEU A 402     -18.917   9.764   4.514  1.00 30.76           O  
ANISOU 3243  O   LEU A 402     1030   7408   3251     12     42   1320       O  
ATOM   3244  CB  LEU A 402     -20.695   8.507   6.974  1.00 25.62           C  
ANISOU 3244  CB  LEU A 402      440   6800   2496    155    101   1705       C  
ATOM   3245  CG  LEU A 402     -21.039   7.247   7.782  1.00 29.08           C  
ANISOU 3245  CG  LEU A 402      476   7397   3175    208    167   1934       C  
ATOM   3246  CD1 LEU A 402     -22.414   7.347   8.345  1.00 28.93           C  
ANISOU 3246  CD1 LEU A 402      442   7436   3115    221    188   2041       C  
ATOM   3247  CD2 LEU A 402     -20.922   5.989   6.955  1.00 31.30           C  
ANISOU 3247  CD2 LEU A 402      780   7444   3670    155    175   1977       C  
ATOM   3248  N   GLY A 403     -18.869  11.135   6.307  1.00 25.80           N  
ANISOU 3248  N   GLY A 403      475   7006   2323     71     41   1313       N  
ATOM   3249  CA  GLY A 403     -18.591  12.355   5.557  1.00 25.35           C  
ANISOU 3249  CA  GLY A 403      482   6921   2227     -5     12   1142       C  
ATOM   3250  C   GLY A 403     -17.213  12.318   4.931  1.00 31.04           C  
ANISOU 3250  C   GLY A 403     1182   7656   2957    -80     -3   1072       C  
ATOM   3251  O   GLY A 403     -17.015  12.835   3.829  1.00 31.76           O  
ANISOU 3251  O   GLY A 403     1367   7641   3061   -157    -18    970       O  
ATOM   3252  N   TYR A 404     -16.245  11.692   5.630  1.00 27.86           N  
ANISOU 3252  N   TYR A 404      661   7395   2528    -48      6   1147       N  
ATOM   3253  CA  TYR A 404     -14.879  11.504   5.136  1.00 27.28           C  
ANISOU 3253  CA  TYR A 404      587   7347   2429    -90      4   1116       C  
ATOM   3254  C   TYR A 404     -14.882  10.510   3.980  1.00 32.10           C  
ANISOU 3254  C   TYR A 404     1161   7808   3226    -64     41   1134       C  
ATOM   3255  O   TYR A 404     -14.243  10.747   2.966  1.00 31.31           O  
ANISOU 3255  O   TYR A 404     1107   7660   3129   -126     46   1042       O  
ATOM   3256  CB  TYR A 404     -13.957  10.995   6.260  1.00 28.19           C  
ANISOU 3256  CB  TYR A 404      562   7683   2467    -27      4   1229       C  
ATOM   3257  CG  TYR A 404     -13.473  12.055   7.229  1.00 29.34           C  
ANISOU 3257  CG  TYR A 404      633   8074   2439   -103    -46   1162       C  
ATOM   3258  CD1 TYR A 404     -13.496  13.406   6.887  1.00 30.95           C  
ANISOU 3258  CD1 TYR A 404      980   8226   2553   -239    -78    987       C  
ATOM   3259  CD2 TYR A 404     -12.945  11.706   8.469  1.00 29.80           C  
ANISOU 3259  CD2 TYR A 404      548   8387   2388    -46    -65   1271       C  
ATOM   3260  CE1 TYR A 404     -13.043  14.383   7.769  1.00 31.48           C  
ANISOU 3260  CE1 TYR A 404     1068   8459   2433   -334   -126    896       C  
ATOM   3261  CE2 TYR A 404     -12.490  12.675   9.362  1.00 30.70           C  
ANISOU 3261  CE2 TYR A 404      661   8713   2290   -141   -124   1183       C  
ATOM   3262  CZ  TYR A 404     -12.549  14.014   9.010  1.00 38.69           C  
ANISOU 3262  CZ  TYR A 404     1837   9641   3222   -294   -154    981       C  
ATOM   3263  OH  TYR A 404     -12.105  14.981   9.877  1.00 39.75           O  
ANISOU 3263  OH  TYR A 404     2002   9952   3149   -411   -213    865       O  
ATOM   3264  N   TRP A 405     -15.634   9.417   4.126  1.00 31.18           N  
ANISOU 3264  N   TRP A 405     1015   7593   3239     16     69   1247       N  
ATOM   3265  CA  TRP A 405     -15.773   8.377   3.124  1.00 31.59           C  
ANISOU 3265  CA  TRP A 405     1104   7452   3448     32    102   1247       C  
ATOM   3266  C   TRP A 405     -16.455   8.859   1.861  1.00 34.91           C  
ANISOU 3266  C   TRP A 405     1653   7726   3885    -65     73   1113       C  
ATOM   3267  O   TRP A 405     -16.052   8.432   0.783  1.00 34.93           O  
ANISOU 3267  O   TRP A 405     1708   7625   3938    -83     94   1039       O  
ATOM   3268  CB  TRP A 405     -16.444   7.133   3.703  1.00 30.80           C  
ANISOU 3268  CB  TRP A 405      954   7265   3485    109    136   1407       C  
ATOM   3269  CG  TRP A 405     -15.460   6.002   3.778  1.00 32.28           C  
ANISOU 3269  CG  TRP A 405     1080   7427   3759    220    199   1498       C  
ATOM   3270  CD1 TRP A 405     -14.737   5.607   4.863  1.00 35.14           C  
ANISOU 3270  CD1 TRP A 405     1313   7952   4086    335    224   1654       C  
ATOM   3271  CD2 TRP A 405     -14.963   5.247   2.669  1.00 32.46           C  
ANISOU 3271  CD2 TRP A 405     1168   7274   3890    245    249   1427       C  
ATOM   3272  NE1 TRP A 405     -13.878   4.591   4.514  1.00 34.50           N  
ANISOU 3272  NE1 TRP A 405     1206   7792   4110    449    292   1710       N  
ATOM   3273  CE2 TRP A 405     -14.003   4.346   3.173  1.00 36.21           C  
ANISOU 3273  CE2 TRP A 405     1551   7789   4418    400    317   1561       C  
ATOM   3274  CE3 TRP A 405     -15.271   5.212   1.296  1.00 33.99           C  
ANISOU 3274  CE3 TRP A 405     1494   7288   4132    163    247   1265       C  
ATOM   3275  CZ2 TRP A 405     -13.370   3.403   2.361  1.00 36.01           C  
ANISOU 3275  CZ2 TRP A 405     1575   7601   4508    494    398   1530       C  
ATOM   3276  CZ3 TRP A 405     -14.636   4.287   0.493  1.00 35.61           C  
ANISOU 3276  CZ3 TRP A 405     1754   7345   4430    234    320   1217       C  
ATOM   3277  CH2 TRP A 405     -13.724   3.372   1.030  1.00 36.38           C  
ANISOU 3277  CH2 TRP A 405     1771   7453   4597    406    403   1346       C  
ATOM   3278  N   LEU A 406     -17.447   9.769   1.985  1.00 30.77           N  
ANISOU 3278  N   LEU A 406     1177   7212   3302   -110     29   1086       N  
ATOM   3279  CA  LEU A 406     -18.153  10.392   0.861  1.00 29.44           C  
ANISOU 3279  CA  LEU A 406     1116   6945   3125   -186    -10    989       C  
ATOM   3280  C   LEU A 406     -17.199  11.264   0.015  1.00 34.02           C  
ANISOU 3280  C   LEU A 406     1774   7542   3612   -252    -12    870       C  
ATOM   3281  O   LEU A 406     -17.309  11.262  -1.206  1.00 34.95           O  
ANISOU 3281  O   LEU A 406     1967   7572   3738   -304    -23    799       O  
ATOM   3282  CB  LEU A 406     -19.347  11.205   1.355  1.00 29.00           C  
ANISOU 3282  CB  LEU A 406     1073   6925   3023   -172    -40   1018       C  
ATOM   3283  CG  LEU A 406     -20.747  10.643   1.085  1.00 34.93           C  
ANISOU 3283  CG  LEU A 406     1790   7612   3871   -175    -64   1089       C  
ATOM   3284  CD1 LEU A 406     -20.750   9.495   0.059  1.00 35.71           C  
ANISOU 3284  CD1 LEU A 406     1910   7574   4085   -244    -78   1059       C  
ATOM   3285  CD2 LEU A 406     -21.484  10.280   2.363  1.00 38.57           C  
ANISOU 3285  CD2 LEU A 406     2139   8156   4361   -106    -36   1232       C  
ATOM   3286  N   CYS A 407     -16.226  11.951   0.657  1.00 29.39           N  
ANISOU 3286  N   CYS A 407     1160   7081   2925   -265     -3    855       N  
ATOM   3287  CA  CYS A 407     -15.204  12.752  -0.021  1.00 28.33           C  
ANISOU 3287  CA  CYS A 407     1075   6984   2707   -355      2    767       C  
ATOM   3288  C   CYS A 407     -14.341  11.847  -0.902  1.00 30.51           C  
ANISOU 3288  C   CYS A 407     1311   7250   3034   -341     50    751       C  
ATOM   3289  O   CYS A 407     -13.971  12.250  -2.000  1.00 31.76           O  
ANISOU 3289  O   CYS A 407     1537   7381   3150   -410     62    679       O  
ATOM   3290  CB  CYS A 407     -14.351  13.518   0.988  1.00 29.11           C  
ANISOU 3290  CB  CYS A 407     1127   7237   2695   -398     -8    759       C  
ATOM   3291  SG  CYS A 407     -15.219  14.868   1.829  1.00 33.33           S  
ANISOU 3291  SG  CYS A 407     1775   7753   3134   -422    -45    716       S  
ATOM   3292  N   TYR A 408     -14.036  10.623  -0.429  1.00 24.52           N  
ANISOU 3292  N   TYR A 408      563   6450   2304   -230     77    826       N  
ATOM   3293  CA  TYR A 408     -13.228   9.642  -1.154  1.00 23.10           C  
ANISOU 3293  CA  TYR A 408      518   6157   2102   -159    117    812       C  
ATOM   3294  C   TYR A 408     -13.988   9.079  -2.341  1.00 25.13           C  
ANISOU 3294  C   TYR A 408      616   6366   2566   -192    163    737       C  
ATOM   3295  O   TYR A 408     -13.352   8.665  -3.299  1.00 25.10           O  
ANISOU 3295  O   TYR A 408      643   6335   2559   -175    219    666       O  
ATOM   3296  CB  TYR A 408     -12.835   8.463  -0.253  1.00 24.27           C  
ANISOU 3296  CB  TYR A 408      506   6355   2360    -27    167    937       C  
ATOM   3297  CG  TYR A 408     -11.826   8.715   0.849  1.00 26.11           C  
ANISOU 3297  CG  TYR A 408      529   6852   2541      9    176   1029       C  
ATOM   3298  CD1 TYR A 408     -10.851   9.699   0.722  1.00 27.74           C  
ANISOU 3298  CD1 TYR A 408      564   7299   2678    -88    178    975       C  
ATOM   3299  CD2 TYR A 408     -11.794   7.911   1.987  1.00 26.58           C  
ANISOU 3299  CD2 TYR A 408      499   6961   2641    127    188   1182       C  
ATOM   3300  CE1 TYR A 408      -9.906   9.912   1.723  1.00 27.46           C  
ANISOU 3300  CE1 TYR A 408      555   7418   2461    -74    136   1052       C  
ATOM   3301  CE2 TYR A 408     -10.852   8.114   2.993  1.00 26.84           C  
ANISOU 3301  CE2 TYR A 408      457   7209   2533    160    167   1275       C  
ATOM   3302  CZ  TYR A 408      -9.914   9.117   2.859  1.00 32.88           C  
ANISOU 3302  CZ  TYR A 408      873   8314   3305     50    169   1200       C  
ATOM   3303  OH  TYR A 408      -8.981   9.295   3.850  1.00 33.02           O  
ANISOU 3303  OH  TYR A 408      715   8617   3214     60    137   1287       O  
ATOM   3304  N   VAL A 409     -15.338   9.018  -2.269  1.00 20.02           N  
ANISOU 3304  N   VAL A 409      503   5371   1733   -188     53    748       N  
ATOM   3305  CA  VAL A 409     -16.196   8.505  -3.350  1.00 19.64           C  
ANISOU 3305  CA  VAL A 409      506   5195   1760   -235     42    674       C  
ATOM   3306  C   VAL A 409     -16.017   9.364  -4.635  1.00 23.39           C  
ANISOU 3306  C   VAL A 409      652   5910   2327   -357     66    564       C  
ATOM   3307  O   VAL A 409     -16.232   8.855  -5.734  1.00 21.70           O  
ANISOU 3307  O   VAL A 409      520   5611   2112   -390     66    473       O  
ATOM   3308  CB  VAL A 409     -17.677   8.336  -2.882  1.00 23.06           C  
ANISOU 3308  CB  VAL A 409      595   5733   2432   -295     13    744       C  
ATOM   3309  CG1 VAL A 409     -18.643   8.109  -4.039  1.00 22.25           C  
ANISOU 3309  CG1 VAL A 409      596   5524   2335   -385    -42    663       C  
ATOM   3310  CG2 VAL A 409     -17.804   7.214  -1.851  1.00 22.99           C  
ANISOU 3310  CG2 VAL A 409      561   5645   2530   -219     44    864       C  
ATOM   3311  N   ASN A 410     -15.545  10.635  -4.489  1.00 21.11           N  
ANISOU 3311  N   ASN A 410      471   5680   1871   -385     46    569       N  
ATOM   3312  CA  ASN A 410     -15.287  11.551  -5.607  1.00 21.48           C  
ANISOU 3312  CA  ASN A 410      494   5813   1855   -481     51    503       C  
ATOM   3313  C   ASN A 410     -14.250  10.935  -6.539  1.00 26.36           C  
ANISOU 3313  C   ASN A 410     1116   6456   2444   -464    133    430       C  
ATOM   3314  O   ASN A 410     -14.380  11.037  -7.755  1.00 26.88           O  
ANISOU 3314  O   ASN A 410     1273   6506   2434   -511    134    357       O  
ATOM   3315  CB  ASN A 410     -14.818  12.922  -5.100  1.00 22.58           C  
ANISOU 3315  CB  ASN A 410      632   6039   1907   -539     43    534       C  
ATOM   3316  CG  ASN A 410     -14.694  13.993  -6.166  1.00 45.78           C  
ANISOU 3316  CG  ASN A 410     3677   8982   4734   -634     38    503       C  
ATOM   3317  OD1 ASN A 410     -15.368  13.969  -7.201  1.00 42.98           O  
ANISOU 3317  OD1 ASN A 410     3405   8578   4348   -650     10    478       O  
ATOM   3318  ND2 ASN A 410     -13.824  14.968  -5.935  1.00 36.42           N  
ANISOU 3318  ND2 ASN A 410     2491   7866   3480   -713     60    514       N  
ATOM   3319  N   ALA A 411     -13.265  10.239  -5.961  1.00 22.77           N  
ANISOU 3319  N   ALA A 411      556   6055   2041   -377    207    458       N  
ATOM   3320  CA  ALA A 411     -12.212   9.532  -6.668  1.00 22.45           C  
ANISOU 3320  CA  ALA A 411      515   6038   1976   -306    303    404       C  
ATOM   3321  C   ALA A 411     -12.752   8.301  -7.440  1.00 27.67           C  
ANISOU 3321  C   ALA A 411     1257   6540   2717   -253    337    310       C  
ATOM   3322  O   ALA A 411     -12.158   7.898  -8.448  1.00 28.40           O  
ANISOU 3322  O   ALA A 411     1399   6638   2753   -217    418    214       O  
ATOM   3323  CB  ALA A 411     -11.134   9.112  -5.688  1.00 22.65           C  
ANISOU 3323  CB  ALA A 411      492   6118   1997   -191    326    490       C  
ATOM   3324  N   THR A 412     -13.848   7.704  -6.954  1.00 23.51           N  
ANISOU 3324  N   THR A 412      762   5866   2304   -255    274    333       N  
ATOM   3325  CA  THR A 412     -14.483   6.528  -7.559  1.00 23.76           C  
ANISOU 3325  CA  THR A 412      902   5706   2418   -249    279    241       C  
ATOM   3326  C   THR A 412     -15.339   6.937  -8.770  1.00 28.45           C  
ANISOU 3326  C   THR A 412     1620   6286   2904   -383    199    128       C  
ATOM   3327  O   THR A 412     -15.374   6.219  -9.766  1.00 27.55           O  
ANISOU 3327  O   THR A 412     1619   6085   2764   -395    227    -12       O  
ATOM   3328  CB  THR A 412     -15.380   5.791  -6.511  1.00 29.99           C  
ANISOU 3328  CB  THR A 412     1658   6363   3373   -237    235    339       C  
ATOM   3329  OG1 THR A 412     -14.768   5.801  -5.225  1.00 29.39           O  
ANISOU 3329  OG1 THR A 412     1446   6369   3352   -132    274    486       O  
ATOM   3330  CG2 THR A 412     -15.725   4.359  -6.908  1.00 25.68           C  
ANISOU 3330  CG2 THR A 412     1219   5584   2955   -223    270    260       C  
ATOM   3331  N   ILE A 413     -16.067   8.057  -8.653  1.00 26.19           N  
ANISOU 3331  N   ILE A 413     1317   6084   2551   -472    100    191       N  
ATOM   3332  CA  ILE A 413     -17.010   8.496  -9.672  1.00 26.73           C  
ANISOU 3332  CA  ILE A 413     1472   6166   2518   -583      6    133       C  
ATOM   3333  C   ILE A 413     -16.345   9.389 -10.737  1.00 32.90           C  
ANISOU 3333  C   ILE A 413     2311   7076   3115   -614     35     87       C  
ATOM   3334  O   ILE A 413     -16.940   9.549 -11.808  1.00 33.59           O  
ANISOU 3334  O   ILE A 413     2483   7191   3090   -690    -27     24       O  
ATOM   3335  CB  ILE A 413     -18.334   9.118  -9.075  1.00 29.56           C  
ANISOU 3335  CB  ILE A 413     1781   6541   2911   -635   -112    244       C  
ATOM   3336  CG1 ILE A 413     -18.084  10.402  -8.248  1.00 29.21           C  
ANISOU 3336  CG1 ILE A 413     1679   6592   2829   -601   -109    358       C  
ATOM   3337  CG2 ILE A 413     -19.146   8.072  -8.258  1.00 29.56           C  
ANISOU 3337  CG2 ILE A 413     1725   6425   3081   -635   -139    289       C  
ATOM   3338  CD1 ILE A 413     -19.324  11.159  -7.885  1.00 29.71           C  
ANISOU 3338  CD1 ILE A 413     1718   6680   2891   -617   -201    449       C  
ATOM   3339  N   ASN A 414     -15.118   9.921 -10.489  1.00 29.26           N  
ANISOU 3339  N   ASN A 414     1795   6711   2613   -567    126    127       N  
ATOM   3340  CA  ASN A 414     -14.426  10.770 -11.477  1.00 29.42           C  
ANISOU 3340  CA  ASN A 414     1857   6860   2463   -613    169    109       C  
ATOM   3341  C   ASN A 414     -14.110  10.051 -12.807  1.00 37.16           C  
ANISOU 3341  C   ASN A 414     2929   7858   3334   -603    232    -35       C  
ATOM   3342  O   ASN A 414     -14.403  10.636 -13.863  1.00 36.75           O  
ANISOU 3342  O   ASN A 414     2958   7884   3121   -677    196    -57       O  
ATOM   3343  CB  ASN A 414     -13.182  11.441 -10.917  1.00 27.98           C  
ANISOU 3343  CB  ASN A 414     1576   6790   2266   -600    249    186       C  
ATOM   3344  CG  ASN A 414     -13.385  12.841 -10.376  1.00 52.67           C  
ANISOU 3344  CG  ASN A 414     4697   9949   5367   -683    188    294       C  
ATOM   3345  OD1 ASN A 414     -14.357  13.547 -10.688  1.00 44.14           O  
ANISOU 3345  OD1 ASN A 414     3699   8825   4245   -734    103    326       O  
ATOM   3346  ND2 ASN A 414     -12.450  13.279  -9.540  1.00 48.60           N  
ANISOU 3346  ND2 ASN A 414     4085   9511   4871   -695    231    352       N  
ATOM   3347  N   PRO A 415     -13.582   8.788 -12.825  1.00 35.66           N  
ANISOU 3347  N   PRO A 415     2744   7592   3213   -503    326   -137       N  
ATOM   3348  CA  PRO A 415     -13.347   8.126 -14.128  1.00 36.00           C  
ANISOU 3348  CA  PRO A 415     2907   7642   3131   -487    392   -306       C  
ATOM   3349  C   PRO A 415     -14.647   7.728 -14.825  1.00 42.35           C  
ANISOU 3349  C   PRO A 415     3842   8357   3894   -592    269   -415       C  
ATOM   3350  O   PRO A 415     -14.649   7.556 -16.046  1.00 43.23           O  
ANISOU 3350  O   PRO A 415     4067   8525   3833   -627    283   -551       O  
ATOM   3351  CB  PRO A 415     -12.528   6.881 -13.764  1.00 37.59           C  
ANISOU 3351  CB  PRO A 415     3089   7742   3453   -325    530   -373       C  
ATOM   3352  CG  PRO A 415     -12.133   7.056 -12.321  1.00 41.68           C  
ANISOU 3352  CG  PRO A 415     3443   8265   4128   -261    536   -206       C  
ATOM   3353  CD  PRO A 415     -13.182   7.905 -11.709  1.00 36.78           C  
ANISOU 3353  CD  PRO A 415     2800   7636   3538   -385    384   -101       C  
ATOM   3354  N   MET A 416     -15.746   7.576 -14.049  1.00 38.90           N  
ANISOU 3354  N   MET A 416     3376   7805   3598   -649    147   -354       N  
ATOM   3355  CA  MET A 416     -17.081   7.232 -14.538  1.00 38.69           C  
ANISOU 3355  CA  MET A 416     3425   7724   3552   -775      6   -425       C  
ATOM   3356  C   MET A 416     -17.649   8.401 -15.335  1.00 40.42           C  
ANISOU 3356  C   MET A 416     3655   8123   3579   -867    -98   -365       C  
ATOM   3357  O   MET A 416     -18.287   8.168 -16.359  1.00 39.83           O  
ANISOU 3357  O   MET A 416     3667   8097   3370   -962   -182   -471       O  
ATOM   3358  CB  MET A 416     -18.005   6.847 -13.379  1.00 41.75           C  
ANISOU 3358  CB  MET A 416     3735   7982   4148   -802    -76   -330       C  
ATOM   3359  CG  MET A 416     -17.592   5.567 -12.707  1.00 47.04           C  
ANISOU 3359  CG  MET A 416     4418   8450   5004   -722     18   -377       C  
ATOM   3360  SD  MET A 416     -18.460   5.204 -11.161  1.00 53.41           S  
ANISOU 3360  SD  MET A 416     5101   9141   6050   -729    -42   -204       S  
ATOM   3361  CE  MET A 416     -17.461   3.785 -10.585  1.00 50.44           C  
ANISOU 3361  CE  MET A 416     4765   8544   5855   -578    119   -241       C  
ATOM   3362  N   CYS A 417     -17.357   9.654 -14.906  1.00 35.95           N  
ANISOU 3362  N   CYS A 417     3012   7657   2990   -837    -90   -199       N  
ATOM   3363  CA  CYS A 417     -17.761  10.899 -15.570  1.00 35.71           C  
ANISOU 3363  CA  CYS A 417     3000   7771   2796   -892   -163    -99       C  
ATOM   3364  C   CYS A 417     -17.175  10.992 -16.981  1.00 39.47           C  
ANISOU 3364  C   CYS A 417     3574   8382   3039   -917   -109   -190       C  
ATOM   3365  O   CYS A 417     -17.912  11.331 -17.902  1.00 40.47           O  
ANISOU 3365  O   CYS A 417     3755   8617   3004   -987   -209   -186       O  
ATOM   3366  CB  CYS A 417     -17.388  12.116 -14.728  1.00 36.43           C  
ANISOU 3366  CB  CYS A 417     3023   7880   2938   -853   -134     75       C  
ATOM   3367  SG  CYS A 417     -18.286  12.244 -13.151  1.00 40.47           S  
ANISOU 3367  SG  CYS A 417     3431   8283   3662   -817   -207    191       S  
ATOM   3368  N   TYR A 418     -15.869  10.647 -17.153  1.00 34.68           N  
ANISOU 3368  N   TYR A 418     2977   7794   2405   -851     51   -264       N  
ATOM   3369  CA  TYR A 418     -15.131  10.616 -18.432  1.00 34.22           C  
ANISOU 3369  CA  TYR A 418     3000   7881   2122   -849    146   -359       C  
ATOM   3370  C   TYR A 418     -15.685   9.561 -19.379  1.00 37.23           C  
ANISOU 3370  C   TYR A 418     3507   8247   2391   -886    103   -574       C  
ATOM   3371  O   TYR A 418     -15.825   9.829 -20.569  1.00 37.23           O  
ANISOU 3371  O   TYR A 418     3590   8408   2148   -941     79   -621       O  
ATOM   3372  CB  TYR A 418     -13.623  10.361 -18.201  1.00 35.85           C  
ANISOU 3372  CB  TYR A 418     3146   8115   2359   -743    339   -380       C  
ATOM   3373  CG  TYR A 418     -12.860  11.597 -17.776  1.00 37.45           C  
ANISOU 3373  CG  TYR A 418     3248   8422   2559   -762    391   -189       C  
ATOM   3374  CD1 TYR A 418     -12.849  12.010 -16.447  1.00 39.70           C  
ANISOU 3374  CD1 TYR A 418     3429   8621   3033   -758    359    -67       C  
ATOM   3375  CD2 TYR A 418     -12.204  12.389 -18.713  1.00 37.56           C  
ANISOU 3375  CD2 TYR A 418     3280   8623   2370   -805    467   -129       C  
ATOM   3376  CE1 TYR A 418     -12.218  13.192 -16.064  1.00 40.52           C  
ANISOU 3376  CE1 TYR A 418     3466   8801   3128   -814    390     87       C  
ATOM   3377  CE2 TYR A 418     -11.565  13.568 -18.341  1.00 38.15           C  
ANISOU 3377  CE2 TYR A 418     3277   8767   2450   -865    505     50       C  
ATOM   3378  CZ  TYR A 418     -11.579  13.968 -17.016  1.00 47.05           C  
ANISOU 3378  CZ  TYR A 418     4318   9786   3773   -878    462    146       C  
ATOM   3379  OH  TYR A 418     -10.934  15.124 -16.650  1.00 51.32           O  
ANISOU 3379  OH  TYR A 418     4804  10379   4315   -966    494    296       O  
ATOM   3380  N   ALA A 419     -15.997   8.366 -18.846  1.00 33.14           N  
ANISOU 3380  N   ALA A 419     3013   7535   2045   -869     93   -702       N  
ATOM   3381  CA  ALA A 419     -16.580   7.250 -19.589  1.00 32.66           C  
ANISOU 3381  CA  ALA A 419     3092   7399   1919   -935     44   -933       C  
ATOM   3382  C   ALA A 419     -17.996   7.580 -20.080  1.00 35.80           C  
ANISOU 3382  C   ALA A 419     3504   7887   2212  -1100   -171   -912       C  
ATOM   3383  O   ALA A 419     -18.310   7.290 -21.225  1.00 34.42           O  
ANISOU 3383  O   ALA A 419     3443   7815   1819  -1184   -223  -1068       O  
ATOM   3384  CB  ALA A 419     -16.609   6.006 -18.716  1.00 33.47           C  
ANISOU 3384  CB  ALA A 419     3210   7231   2275   -888     83  -1025       C  
ATOM   3385  N   LEU A 420     -18.829   8.207 -19.223  1.00 33.65           N  
ANISOU 3385  N   LEU A 420     3106   7601   2078  -1134   -290   -716       N  
ATOM   3386  CA  LEU A 420     -20.211   8.587 -19.531  1.00 34.16           C  
ANISOU 3386  CA  LEU A 420     3131   7776   2071  -1260   -492   -646       C  
ATOM   3387  C   LEU A 420     -20.343   9.765 -20.487  1.00 40.85           C  
ANISOU 3387  C   LEU A 420     3984   8874   2664  -1273   -548   -526       C  
ATOM   3388  O   LEU A 420     -21.405   9.912 -21.100  1.00 41.11           O  
ANISOU 3388  O   LEU A 420     4004   9051   2565  -1374   -715   -506       O  
ATOM   3389  CB  LEU A 420     -20.988   8.917 -18.243  1.00 33.91           C  
ANISOU 3389  CB  LEU A 420     2952   7660   2273  -1250   -568   -461       C  
ATOM   3390  CG  LEU A 420     -21.428   7.747 -17.359  1.00 38.07           C  
ANISOU 3390  CG  LEU A 420     3455   7979   3032  -1299   -589   -537       C  
ATOM   3391  CD1 LEU A 420     -21.732   8.220 -15.927  1.00 37.48           C  
ANISOU 3391  CD1 LEU A 420     3231   7830   3178  -1224   -584   -335       C  
ATOM   3392  CD2 LEU A 420     -22.607   6.994 -17.967  1.00 39.86           C  
ANISOU 3392  CD2 LEU A 420     3702   8243   3201  -1488   -760   -645       C  
ATOM   3393  N   CYS A 421     -19.313  10.637 -20.564  1.00 38.25           N  
ANISOU 3393  N   CYS A 421     3656   8606   2270  -1177   -416   -420       N  
ATOM   3394  CA  CYS A 421     -19.351  11.848 -21.390  1.00 37.89           C  
ANISOU 3394  CA  CYS A 421     3624   8769   2003  -1181   -446   -263       C  
ATOM   3395  C   CYS A 421     -18.523  11.774 -22.670  1.00 43.30           C  
ANISOU 3395  C   CYS A 421     4421   9620   2413  -1187   -348   -372       C  
ATOM   3396  O   CYS A 421     -18.898  12.432 -23.638  1.00 44.16           O  
ANISOU 3396  O   CYS A 421     4562   9934   2283  -1227   -421   -286       O  
ATOM   3397  CB  CYS A 421     -18.978  13.072 -20.559  1.00 37.47           C  
ANISOU 3397  CB  CYS A 421     3498   8667   2070  -1105   -387    -27       C  
ATOM   3398  SG  CYS A 421     -20.132  13.419 -19.209  1.00 40.59           S  
ANISOU 3398  SG  CYS A 421     3774   8932   2717  -1077   -508    128       S  
ATOM   3399  N   ASN A 422     -17.397  11.022 -22.672  1.00 40.35           N  
ANISOU 3399  N   ASN A 422     4095   9177   2061  -1128   -176   -540       N  
ATOM   3400  CA  ASN A 422     -16.497  10.871 -23.822  1.00 40.36           C  
ANISOU 3400  CA  ASN A 422     4191   9342   1802  -1105    -44   -656       C  
ATOM   3401  C   ASN A 422     -16.543   9.446 -24.382  1.00 44.64           C  
ANISOU 3401  C   ASN A 422     4862   9828   2271  -1121    -24   -977       C  
ATOM   3402  O   ASN A 422     -16.152   8.509 -23.676  1.00 43.82           O  
ANISOU 3402  O   ASN A 422     4765   9508   2377  -1054     62  -1105       O  
ATOM   3403  CB  ASN A 422     -15.059  11.174 -23.425  1.00 44.33           C  
ANISOU 3403  CB  ASN A 422     4635   9838   2373  -1000    169   -587       C  
ATOM   3404  CG  ASN A 422     -14.707  12.611 -23.252  1.00 79.78           C  
ANISOU 3404  CG  ASN A 422     9047  14418   6846  -1013    192   -311       C  
ATOM   3405  OD1 ASN A 422     -14.221  13.277 -24.178  1.00 77.70           O  
ANISOU 3405  OD1 ASN A 422     8817  14355   6351  -1033    259   -228       O  
ATOM   3406  ND2 ASN A 422     -14.886  13.099 -22.040  1.00 72.50           N  
ANISOU 3406  ND2 ASN A 422     8033  13343   6171  -1006    152   -168       N  
ATOM   3407  N   LYS A 423     -16.982   9.288 -25.664  1.00 41.97           N  
ANISOU 3407  N   LYS A 423     4640   9684   1624  -1204    -98  -1106       N  
ATOM   3408  CA  LYS A 423     -17.067   7.993 -26.358  1.00 41.86           C  
ANISOU 3408  CA  LYS A 423     4791   9625   1489  -1244    -85  -1447       C  
ATOM   3409  C   LYS A 423     -15.673   7.356 -26.541  1.00 45.88           C  
ANISOU 3409  C   LYS A 423     5376  10081   1974  -1083    180  -1614       C  
ATOM   3410  O   LYS A 423     -15.548   6.135 -26.397  1.00 47.25           O  
ANISOU 3410  O   LYS A 423     5663  10042   2250  -1047    243  -1867       O  
ATOM   3411  CB  LYS A 423     -17.815   8.115 -27.706  1.00 44.93           C  
ANISOU 3411  CB  LYS A 423     5277  10286   1508  -1378   -232  -1535       C  
ATOM   3412  CG  LYS A 423     -18.062   6.782 -28.457  1.00 64.92           C  
ANISOU 3412  CG  LYS A 423     8009  12767   3891  -1464   -253  -1925       C  
ATOM   3413  CD  LYS A 423     -19.383   6.092 -28.056  1.00 78.80           C  
ANISOU 3413  CD  LYS A 423     9769  14353   5817  -1646   -473  -2028       C  
ATOM   3414  CE  LYS A 423     -19.417   4.603 -28.333  1.00 87.55           C  
ANISOU 3414  CE  LYS A 423    11092  15266   6906  -1729   -454  -2426       C  
ATOM   3415  NZ  LYS A 423     -20.354   3.887 -27.418  1.00 90.52           N  
ANISOU 3415  NZ  LYS A 423    11436  15365   7592  -1872   -596  -2465       N  
ATOM   3416  N   ALA A 424     -14.630   8.174 -26.832  1.00 39.33           N  
ANISOU 3416  N   ALA A 424     4482   9440   1022   -983    342  -1461       N  
ATOM   3417  CA  ALA A 424     -13.254   7.694 -26.987  1.00 37.68           C  
ANISOU 3417  CA  ALA A 424     4292   9239    785   -811    606  -1571       C  
ATOM   3418  C   ALA A 424     -12.699   7.088 -25.664  1.00 40.23           C  
ANISOU 3418  C   ALA A 424     4525   9283   1479   -682    708  -1560       C  
ATOM   3419  O   ALA A 424     -11.921   6.139 -25.725  1.00 39.82           O  
ANISOU 3419  O   ALA A 424     4536   9137   1456   -531    888  -1746       O  
ATOM   3420  CB  ALA A 424     -12.361   8.816 -27.484  1.00 38.16           C  
ANISOU 3420  CB  ALA A 424     4240   9565    694   -774    725  -1348       C  
ATOM   3421  N   PHE A 425     -13.137   7.592 -24.485  1.00 35.32           N  
ANISOU 3421  N   PHE A 425     3763   8530   1126   -729    594  -1348       N  
ATOM   3422  CA  PHE A 425     -12.706   7.045 -23.185  1.00 34.78           C  
ANISOU 3422  CA  PHE A 425     3601   8225   1388   -618    665  -1315       C  
ATOM   3423  C   PHE A 425     -13.422   5.735 -22.869  1.00 40.12           C  
ANISOU 3423  C   PHE A 425     4401   8617   2225   -633    601  -1528       C  
ATOM   3424  O   PHE A 425     -12.779   4.779 -22.445  1.00 40.47           O  
ANISOU 3424  O   PHE A 425     4475   8483   2421   -484    745  -1637       O  
ATOM   3425  CB  PHE A 425     -12.907   8.045 -22.035  1.00 35.55           C  
ANISOU 3425  CB  PHE A 425     3522   8298   1686   -665    573  -1031       C  
ATOM   3426  CG  PHE A 425     -11.721   8.920 -21.725  1.00 36.19           C  
ANISOU 3426  CG  PHE A 425     3452   8526   1771   -599    711   -839       C  
ATOM   3427  CD1 PHE A 425     -10.598   8.399 -21.091  1.00 38.99           C  
ANISOU 3427  CD1 PHE A 425     3708   8840   2265   -445    882   -845       C  
ATOM   3428  CD2 PHE A 425     -11.749  10.278 -22.009  1.00 38.25           C  
ANISOU 3428  CD2 PHE A 425     3663   8964   1908   -699    665   -635       C  
ATOM   3429  CE1 PHE A 425      -9.501   9.215 -20.795  1.00 40.08           C  
ANISOU 3429  CE1 PHE A 425     3680   9148   2399   -418    995   -664       C  
ATOM   3430  CE2 PHE A 425     -10.659  11.095 -21.703  1.00 41.30           C  
ANISOU 3430  CE2 PHE A 425     3913   9472   2306   -682    786   -460       C  
ATOM   3431  CZ  PHE A 425      -9.539  10.556 -21.102  1.00 39.56           C  
ANISOU 3431  CZ  PHE A 425     3576   9244   2209   -555    945   -481       C  
ATOM   3432  N   ARG A 426     -14.755   5.709 -23.064  1.00 36.70           N  
ANISOU 3432  N   ARG A 426     4031   8149   1766   -815    385  -1568       N  
ATOM   3433  CA  ARG A 426     -15.662   4.578 -22.850  1.00 36.96           C  
ANISOU 3433  CA  ARG A 426     4179   7931   1934   -907    280  -1754       C  
ATOM   3434  C   ARG A 426     -15.175   3.329 -23.594  1.00 44.10           C  
ANISOU 3434  C   ARG A 426     5301   8707   2747   -836    419  -2083       C  
ATOM   3435  O   ARG A 426     -15.051   2.269 -22.980  1.00 43.93           O  
ANISOU 3435  O   ARG A 426     5349   8386   2955   -766    489  -2191       O  
ATOM   3436  CB  ARG A 426     -17.058   4.971 -23.362  1.00 36.14           C  
ANISOU 3436  CB  ARG A 426     4087   7948   1696  -1133     29  -1740       C  
ATOM   3437  CG  ARG A 426     -18.232   4.213 -22.761  1.00 44.62           C  
ANISOU 3437  CG  ARG A 426     5172   8804   2977  -1283   -135  -1795       C  
ATOM   3438  CD  ARG A 426     -19.540   4.611 -23.436  1.00 49.03           C  
ANISOU 3438  CD  ARG A 426     5718   9560   3353  -1501   -379  -1784       C  
ATOM   3439  NE  ARG A 426     -19.691   6.068 -23.520  1.00 57.11           N  
ANISOU 3439  NE  ARG A 426     6591  10851   4259  -1477   -444  -1506       N  
ATOM   3440  CZ  ARG A 426     -20.436   6.704 -24.419  1.00 75.31           C  
ANISOU 3440  CZ  ARG A 426     8882  13423   6309  -1591   -604  -1455       C  
ATOM   3441  NH1 ARG A 426     -21.155   6.019 -25.303  1.00 70.14           N  
ANISOU 3441  NH1 ARG A 426     8337  12840   5472  -1765   -740  -1673       N  
ATOM   3442  NH2 ARG A 426     -20.500   8.028 -24.419  1.00 57.24           N  
ANISOU 3442  NH2 ARG A 426     6474  11328   3947  -1538   -637  -1179       N  
ATOM   3443  N   ASP A 427     -14.889   3.472 -24.911  1.00 42.62           N  
ANISOU 3443  N   ASP A 427     5231   8744   2217   -842    470  -2235       N  
ATOM   3444  CA  ASP A 427     -14.398   2.403 -25.786  1.00 43.39           C  
ANISOU 3444  CA  ASP A 427     5562   8764   2159   -762    619  -2575       C  
ATOM   3445  C   ASP A 427     -13.014   1.907 -25.357  1.00 47.43           C  
ANISOU 3445  C   ASP A 427     6054   9161   2808   -472    902  -2589       C  
ATOM   3446  O   ASP A 427     -12.780   0.700 -25.379  1.00 48.12           O  
ANISOU 3446  O   ASP A 427     6322   8981   2980   -369   1020  -2834       O  
ATOM   3447  CB  ASP A 427     -14.375   2.842 -27.269  1.00 45.42           C  
ANISOU 3447  CB  ASP A 427     5920   9357   1979   -824    611  -2694       C  
ATOM   3448  CG  ASP A 427     -15.725   3.193 -27.870  1.00 59.33           C  
ANISOU 3448  CG  ASP A 427     7717  11269   3555  -1097    330  -2713       C  
ATOM   3449  OD1 ASP A 427     -16.755   2.656 -27.386  1.00 60.29           O  
ANISOU 3449  OD1 ASP A 427     7866  11183   3860  -1262    152  -2772       O  
ATOM   3450  OD2 ASP A 427     -15.754   3.992 -28.839  1.00 66.58           O  
ANISOU 3450  OD2 ASP A 427     8626  12532   4139  -1146    289  -2655       O  
ATOM   3451  N   THR A 428     -12.111   2.827 -24.955  1.00 41.86           N  
ANISOU 3451  N   THR A 428     5129   8650   2126   -344   1011  -2322       N  
ATOM   3452  CA  THR A 428     -10.764   2.467 -24.524  1.00 40.61           C  
ANISOU 3452  CA  THR A 428     4889   8456   2085    -70   1269  -2287       C  
ATOM   3453  C   THR A 428     -10.809   1.736 -23.190  1.00 44.15           C  
ANISOU 3453  C   THR A 428     5287   8570   2917     16   1272  -2223       C  
ATOM   3454  O   THR A 428     -10.033   0.806 -22.996  1.00 44.09           O  
ANISOU 3454  O   THR A 428     5335   8397   3022    245   1468  -2326       O  
ATOM   3455  CB  THR A 428      -9.836   3.678 -24.551  1.00 44.55           C  
ANISOU 3455  CB  THR A 428     5161   9292   2475    -12   1362  -2025       C  
ATOM   3456  OG1 THR A 428      -9.942   4.313 -25.827  1.00 43.49           O  
ANISOU 3456  OG1 THR A 428     5096   9451   1978   -111   1345  -2072       O  
ATOM   3457  CG2 THR A 428      -8.392   3.297 -24.333  1.00 42.16           C  
ANISOU 3457  CG2 THR A 428     4754   9037   2230    267   1636  -2003       C  
ATOM   3458  N   PHE A 429     -11.736   2.132 -22.289  1.00 40.08           N  
ANISOU 3458  N   PHE A 429     4672   7963   2593   -152   1063  -2047       N  
ATOM   3459  CA  PHE A 429     -11.946   1.505 -20.983  1.00 39.21           C  
ANISOU 3459  CA  PHE A 429     4508   7560   2831   -106   1037  -1957       C  
ATOM   3460  C   PHE A 429     -12.335   0.051 -21.213  1.00 44.79           C  
ANISOU 3460  C   PHE A 429     5471   7918   3629    -94   1069  -2237       C  
ATOM   3461  O   PHE A 429     -11.705  -0.833 -20.634  1.00 43.85           O  
ANISOU 3461  O   PHE A 429     5379   7567   3713    113   1227  -2254       O  
ATOM   3462  CB  PHE A 429     -13.064   2.228 -20.224  1.00 40.49           C  
ANISOU 3462  CB  PHE A 429     4548   7729   3108   -319    798  -1756       C  
ATOM   3463  CG  PHE A 429     -12.680   3.360 -19.297  1.00 41.43           C  
ANISOU 3463  CG  PHE A 429     4413   8016   3310   -289    781  -1447       C  
ATOM   3464  CD1 PHE A 429     -11.587   4.172 -19.575  1.00 43.70           C  
ANISOU 3464  CD1 PHE A 429     4581   8563   3458   -191    909  -1343       C  
ATOM   3465  CD2 PHE A 429     -13.463   3.666 -18.189  1.00 42.30           C  
ANISOU 3465  CD2 PHE A 429     4411   8041   3620   -384    632  -1267       C  
ATOM   3466  CE1 PHE A 429     -11.259   5.236 -18.733  1.00 43.97           C  
ANISOU 3466  CE1 PHE A 429     4406   8736   3565   -204    880  -1082       C  
ATOM   3467  CE2 PHE A 429     -13.127   4.726 -17.347  1.00 44.23           C  
ANISOU 3467  CE2 PHE A 429     4454   8431   3922   -367    615  -1017       C  
ATOM   3468  CZ  PHE A 429     -12.029   5.502 -17.624  1.00 42.09           C  
ANISOU 3468  CZ  PHE A 429     4084   8387   3521   -289    733   -934       C  
ATOM   3469  N   ARG A 430     -13.338  -0.187 -22.118  1.00 43.14           N  
ANISOU 3469  N   ARG A 430     5456   7682   3254   -318    924  -2459       N  
ATOM   3470  CA  ARG A 430     -13.851  -1.502 -22.539  1.00 43.25           C  
ANISOU 3470  CA  ARG A 430     5756   7372   3304   -387    921  -2776       C  
ATOM   3471  C   ARG A 430     -12.722  -2.317 -23.186  1.00 47.68           C  
ANISOU 3471  C   ARG A 430     6502   7843   3774   -119   1197  -3016       C  
ATOM   3472  O   ARG A 430     -12.581  -3.511 -22.915  1.00 47.33           O  
ANISOU 3472  O   ARG A 430     6638   7424   3920     -9   1308  -3173       O  
ATOM   3473  CB  ARG A 430     -14.978  -1.337 -23.581  1.00 43.38           C  
ANISOU 3473  CB  ARG A 430     5905   7514   3064   -690    707  -2962       C  
ATOM   3474  CG  ARG A 430     -16.330  -0.895 -23.049  1.00 58.03           C  
ANISOU 3474  CG  ARG A 430     7635   9391   5024   -969    428  -2798       C  
ATOM   3475  CD  ARG A 430     -17.230  -0.439 -24.190  1.00 73.19           C  
ANISOU 3475  CD  ARG A 430     9610  11580   6617  -1218    229  -2913       C  
ATOM   3476  NE  ARG A 430     -18.548  -0.012 -23.709  1.00 83.49           N  
ANISOU 3476  NE  ARG A 430    10767  12938   8017  -1464    -34  -2741       N  
ATOM   3477  CZ  ARG A 430     -19.448   0.650 -24.433  1.00 94.06           C  
ANISOU 3477  CZ  ARG A 430    12057  14566   9114  -1670   -245  -2721       C  
ATOM   3478  NH1 ARG A 430     -19.186   0.982 -25.694  1.00 81.22           N  
ANISOU 3478  NH1 ARG A 430    10531  13208   7121  -1676   -233  -2862       N  
ATOM   3479  NH2 ARG A 430     -20.616   0.989 -23.901  1.00 72.39           N  
ANISOU 3479  NH2 ARG A 430     9153  11868   6483  -1856   -462  -2545       N  
ATOM   3480  N   LEU A 431     -11.921  -1.657 -24.039  1.00 44.48           N  
ANISOU 3480  N   LEU A 431     6048   7777   3073     -6   1317  -3032       N  
ATOM   3481  CA  LEU A 431     -10.823  -2.275 -24.778  1.00 44.78           C  
ANISOU 3481  CA  LEU A 431     6233   7816   2966    265   1594  -3249       C  
ATOM   3482  C   LEU A 431      -9.745  -2.794 -23.853  1.00 48.89           C  
ANISOU 3482  C   LEU A 431     6644   8175   3756    600   1822  -3114       C  
ATOM   3483  O   LEU A 431      -9.298  -3.918 -24.038  1.00 49.24           O  
ANISOU 3483  O   LEU A 431     6896   7950   3862    812   2015  -3334       O  
ATOM   3484  CB  LEU A 431     -10.246  -1.293 -25.808  1.00 45.01           C  
ANISOU 3484  CB  LEU A 431     6181   8306   2616    289   1662  -3228       C  
ATOM   3485  CG  LEU A 431      -9.431  -1.889 -26.930  1.00 50.00           C  
ANISOU 3485  CG  LEU A 431     7015   8997   2987    498   1910  -3525       C  
ATOM   3486  CD1 LEU A 431      -9.941  -1.404 -28.270  1.00 50.42           C  
ANISOU 3486  CD1 LEU A 431     7203   9336   2617    296   1808  -3704       C  
ATOM   3487  CD2 LEU A 431      -7.965  -1.542 -26.765  1.00 53.21           C  
ANISOU 3487  CD2 LEU A 431     7202   9636   3381    817   2181  -3341       C  
ATOM   3488  N   LEU A 432      -9.342  -1.992 -22.862  1.00 45.28           N  
ANISOU 3488  N   LEU A 432     5871   7881   3452    650   1801  -2758       N  
ATOM   3489  CA  LEU A 432      -8.313  -2.364 -21.899  1.00 45.27           C  
ANISOU 3489  CA  LEU A 432     5709   7798   3693    954   1987  -2580       C  
ATOM   3490  C   LEU A 432      -8.790  -3.442 -20.939  1.00 51.85           C  
ANISOU 3490  C   LEU A 432     6655   8175   4870    991   1961  -2588       C  
ATOM   3491  O   LEU A 432      -7.980  -4.280 -20.548  1.00 51.92           O  
ANISOU 3491  O   LEU A 432     6690   7999   5039   1297   2170  -2590       O  
ATOM   3492  CB  LEU A 432      -7.824  -1.150 -21.104  1.00 44.99           C  
ANISOU 3492  CB  LEU A 432     5311   8081   3703    942   1937  -2211       C  
ATOM   3493  CG  LEU A 432      -7.116  -0.039 -21.867  1.00 49.01           C  
ANISOU 3493  CG  LEU A 432     5661   9038   3923    938   2004  -2127       C  
ATOM   3494  CD1 LEU A 432      -7.176   1.253 -21.079  1.00 48.97           C  
ANISOU 3494  CD1 LEU A 432     5377   9255   3974    777   1852  -1803       C  
ATOM   3495  CD2 LEU A 432      -5.674  -0.408 -22.210  1.00 49.65           C  
ANISOU 3495  CD2 LEU A 432     5662   9268   3934   1277   2306  -2145       C  
ATOM   3496  N   LEU A 433     -10.087  -3.415 -20.541  1.00 49.95           N  
ANISOU 3496  N   LEU A 433     6466   7767   4746    691   1713  -2567       N  
ATOM   3497  CA  LEU A 433     -10.677  -4.404 -19.627  1.00 50.31           C  
ANISOU 3497  CA  LEU A 433     6617   7383   5117    670   1668  -2550       C  
ATOM   3498  C   LEU A 433     -10.779  -5.784 -20.284  1.00 59.48           C  
ANISOU 3498  C   LEU A 433     8152   8141   6305    732   1788  -2903       C  
ATOM   3499  O   LEU A 433     -10.480  -6.796 -19.639  1.00 59.29           O  
ANISOU 3499  O   LEU A 433     8223   7758   6545    930   1922  -2886       O  
ATOM   3500  CB  LEU A 433     -12.055  -3.955 -19.117  1.00 49.46           C  
ANISOU 3500  CB  LEU A 433     6446   7254   5094    318   1379  -2435       C  
ATOM   3501  CG  LEU A 433     -12.084  -2.902 -18.011  1.00 52.54           C  
ANISOU 3501  CG  LEU A 433     6504   7875   5582    287   1271  -2069       C  
ATOM   3502  CD1 LEU A 433     -13.475  -2.328 -17.866  1.00 52.06           C  
ANISOU 3502  CD1 LEU A 433     6401   7867   5512    -51   1000  -2008       C  
ATOM   3503  CD2 LEU A 433     -11.593  -3.458 -16.684  1.00 53.05           C  
ANISOU 3503  CD2 LEU A 433     6457   7746   5953    496   1368  -1851       C  
ATOM   3504  N   LEU A 434     -11.182  -5.820 -21.571  1.00 59.51           N  
ANISOU 3504  N   LEU A 434     8381   8203   6027    567   1744  -3223       N  
ATOM   3505  CA  LEU A 434     -11.309  -7.058 -22.336  1.00 61.08           C  
ANISOU 3505  CA  LEU A 434     8974   8035   6198    589   1848  -3616       C  
ATOM   3506  C   LEU A 434      -9.936  -7.617 -22.673  1.00 69.35           C  
ANISOU 3506  C   LEU A 434    10107   9037   7206   1025   2187  -3725       C  
ATOM   3507  O   LEU A 434      -9.797  -8.830 -22.800  1.00 69.40           O  
ANISOU 3507  O   LEU A 434    10414   8615   7340   1171   2341  -3957       O  
ATOM   3508  CB  LEU A 434     -12.151  -6.853 -23.608  1.00 61.25           C  
ANISOU 3508  CB  LEU A 434     9189   8197   5886    270   1684  -3922       C  
ATOM   3509  CG  LEU A 434     -13.659  -6.646 -23.400  1.00 66.42           C  
ANISOU 3509  CG  LEU A 434     9824   8820   6592   -168   1353  -3886       C  
ATOM   3510  CD1 LEU A 434     -14.272  -5.910 -24.569  1.00 66.80           C  
ANISOU 3510  CD1 LEU A 434     9897   9234   6250   -429   1177  -4037       C  
ATOM   3511  CD2 LEU A 434     -14.387  -7.969 -23.153  1.00 69.41           C  
ANISOU 3511  CD2 LEU A 434    10490   8664   7218   -326   1310  -4087       C  
ATOM   3512  N   ALA A 435      -8.922  -6.733 -22.800  1.00 68.80           N  
ANISOU 3512  N   ALA A 435     9769   9403   6970   1234   2310  -3546       N  
ATOM   3513  CA  ALA A 435      -7.536  -7.107 -23.083  1.00 69.88           C  
ANISOU 3513  CA  ALA A 435     9899   9601   7052   1668   2639  -3589       C  
ATOM   3514  C   ALA A 435      -6.865  -7.684 -21.838  1.00 78.07           C  
ANISOU 3514  C   ALA A 435    10796  10416   8451   1980   2780  -3330       C  
ATOM   3515  O   ALA A 435      -5.974  -8.517 -21.976  1.00 78.38           O  
ANISOU 3515  O   ALA A 435    10944  10291   8544   2359   3057  -3425       O  
ATOM   3516  CB  ALA A 435      -6.754  -5.906 -23.586  1.00 70.45           C  
ANISOU 3516  CB  ALA A 435     9692  10245   6832   1730   2698  -3444       C  
ATOM   3517  N   ARG A 436      -7.282  -7.245 -20.630  1.00 77.24           N  
ANISOU 3517  N   ARG A 436    10449  10320   8579   1841   2597  -2998       N  
ATOM   3518  CA  ARG A 436      -6.742  -7.737 -19.356  1.00 78.28           C  
ANISOU 3518  CA  ARG A 436    10425  10276   9040   2104   2693  -2714       C  
ATOM   3519  C   ARG A 436      -7.296  -9.116 -19.010  1.00 85.47           C  
ANISOU 3519  C   ARG A 436    11658  10581  10235   2131   2725  -2847       C  
ATOM   3520  O   ARG A 436      -6.560  -9.952 -18.484  1.00 84.39           O  
ANISOU 3520  O   ARG A 436    11543  10210  10311   2490   2933  -2753       O  
ATOM   3521  CB  ARG A 436      -6.972  -6.731 -18.216  1.00 78.17           C  
ANISOU 3521  CB  ARG A 436    10043  10528   9130   1943   2492  -2326       C  
ATOM   3522  CG  ARG A 436      -5.914  -5.627 -18.154  1.00 90.24           C  
ANISOU 3522  CG  ARG A 436    11208  12585  10493   2074   2560  -2102       C  
ATOM   3523  CD  ARG A 436      -4.669  -6.048 -17.377  1.00103.09           C  
ANISOU 3523  CD  ARG A 436    12626  14258  12288   2484   2773  -1872       C  
ATOM   3524  NE  ARG A 436      -3.459  -5.340 -17.812  1.00114.24           N  
ANISOU 3524  NE  ARG A 436    13774  16144  13489   2666   2925  -1781       N  
ATOM   3525  CZ  ARG A 436      -2.857  -4.375 -17.119  1.00128.91           C  
ANISOU 3525  CZ  ARG A 436    15249  18395  15336   2650   2870  -1470       C  
ATOM   3526  NH1 ARG A 436      -3.342  -3.987 -15.944  1.00115.99           N  
ANISOU 3526  NH1 ARG A 436    13458  16740  13873   2483   2672  -1230       N  
ATOM   3527  NH2 ARG A 436      -1.759  -3.797 -17.591  1.00114.04           N  
ANISOU 3527  NH2 ARG A 436    13135  16933  13262   2792   3018  -1399       N  
ATOM   3528  N   TRP A 437      -8.584  -9.358 -19.332  1.00 85.78           N  
ANISOU 3528  N   TRP A 437    11945  10372  10274   1750   2522  -3056       N  
ATOM   3529  CA  TRP A 437      -9.267 -10.638 -19.124  1.00 87.53           C  
ANISOU 3529  CA  TRP A 437    12509   9998  10750   1680   2525  -3216       C  
ATOM   3530  C   TRP A 437      -8.648 -11.717 -20.043  1.00 92.18           C  
ANISOU 3530  C   TRP A 437    13474  10269  11283   1960   2800  -3583       C  
ATOM   3531  O   TRP A 437      -8.512 -12.873 -19.636  1.00 91.79           O  
ANISOU 3531  O   TRP A 437    13652   9720  11505   2156   2950  -3617       O  
ATOM   3532  CB  TRP A 437     -10.792 -10.477 -19.327  1.00 87.21           C  
ANISOU 3532  CB  TRP A 437    12587   9870  10680   1158   2219  -3343       C  
ATOM   3533  CG  TRP A 437     -11.551 -11.766 -19.426  1.00 89.00           C  
ANISOU 3533  CG  TRP A 437    13212   9505  11099   1004   2212  -3595       C  
ATOM   3534  CD1 TRP A 437     -12.176 -12.265 -20.531  1.00 92.15           C  
ANISOU 3534  CD1 TRP A 437    13970   9711  11332    764   2162  -4024       C  
ATOM   3535  CD2 TRP A 437     -11.701 -12.753 -18.397  1.00 89.15           C  
ANISOU 3535  CD2 TRP A 437    13329   9034  11508   1085   2272  -3438       C  
ATOM   3536  NE1 TRP A 437     -12.729 -13.493 -20.248  1.00 92.00           N  
ANISOU 3536  NE1 TRP A 437    14273   9093  11589    661   2180  -4157       N  
ATOM   3537  CE2 TRP A 437     -12.448 -13.819 -18.946  1.00 93.54           C  
ANISOU 3537  CE2 TRP A 437    14319   9085  12136    863   2255  -3791       C  
ATOM   3538  CE3 TRP A 437     -11.275 -12.841 -17.060  1.00 90.56           C  
ANISOU 3538  CE3 TRP A 437    13274   9160  11974   1316   2337  -3027       C  
ATOM   3539  CZ2 TRP A 437     -12.788 -14.957 -18.200  1.00 93.00           C  
ANISOU 3539  CZ2 TRP A 437    14463   8434  12439    857   2308  -3730       C  
ATOM   3540  CZ3 TRP A 437     -11.607 -13.969 -16.326  1.00 92.23           C  
ANISOU 3540  CZ3 TRP A 437    13684   8823  12534   1334   2391  -2953       C  
ATOM   3541  CH2 TRP A 437     -12.358 -15.010 -16.893  1.00 92.95           C  
ANISOU 3541  CH2 TRP A 437    14214   8389  12713   1104   2381  -3294       C  
ATOM   3542  N   ASP A 438      -8.241 -11.306 -21.262  1.00 89.27           N  
ANISOU 3542  N   ASP A 438    13166  10199  10554   2000   2880  -3840       N  
ATOM   3543  CA  ASP A 438      -7.549 -12.109 -22.274  1.00 89.24           C  
ANISOU 3543  CA  ASP A 438    13483  10019  10406   2293   3162  -4205       C  
ATOM   3544  C   ASP A 438      -6.089 -12.242 -21.784  1.00 93.26           C  
ANISOU 3544  C   ASP A 438    13771  10644  11021   2847   3465  -3960       C  
ATOM   3545  O   ASP A 438      -5.420 -11.237 -21.536  1.00 92.45           O  
ANISOU 3545  O   ASP A 438    13264  11055  10809   2944   3467  -3673       O  
ATOM   3546  CB  ASP A 438      -7.678 -11.400 -23.646  1.00 91.24           C  
ANISOU 3546  CB  ASP A 438    13792  10674  10202   2110   3107  -4487       C  
ATOM   3547  CG  ASP A 438      -6.713 -11.784 -24.753  1.00105.20           C  
ANISOU 3547  CG  ASP A 438    15745  12526  11700   2457   3416  -4788       C  
ATOM   3548  OD1 ASP A 438      -6.447 -12.997 -24.921  1.00107.25           O  
ANISOU 3548  OD1 ASP A 438    16348  12317  12086   2720   3643  -5034       O  
ATOM   3549  OD2 ASP A 438      -6.252 -10.873 -25.479  1.00110.13           O  
ANISOU 3549  OD2 ASP A 438    16190  13676  11980   2461   3436  -4784       O  
ATOM   3550  N   HIS A 439      -5.635 -13.477 -21.562  1.00 90.33           N  
ANISOU 3550  N   HIS A 439    13652   9785  10884   3195   3709  -4044       N  
ATOM   3551  CA  HIS A 439      -4.317 -13.731 -20.986  1.00130.87           C  
ANISOU 3551  CA  HIS A 439    18573  14990  16161   3743   3992  -3781       C  
ATOM   3552  C   HIS A 439      -3.182 -13.576 -21.987  1.00174.96           C  
ANISOU 3552  C   HIS A 439    24118  20919  21442   4103   4273  -3941       C  
ATOM   3553  O   HIS A 439      -2.471 -12.573 -21.951  1.00141.21           O  
ANISOU 3553  O   HIS A 439    19444  17238  16973   4135   4261  -3723       O  
ATOM   3554  CB  HIS A 439      -4.291 -15.101 -20.289  1.00131.65           C  
ANISOU 3554  CB  HIS A 439    18950  14424  16648   4002   4148  -3763       C  
ATOM   3555  CG  HIS A 439      -5.434 -15.308 -19.338  1.00134.96           C  
ANISOU 3555  CG  HIS A 439    19414  14505  17359   3632   3885  -3600       C  
ATOM   3556  ND1 HIS A 439      -5.494 -14.646 -18.122  1.00136.65           N  
ANISOU 3556  ND1 HIS A 439    19214  14979  17726   3557   3718  -3136       N  
ATOM   3557  CD2 HIS A 439      -6.534 -16.086 -19.466  1.00136.57           C  
ANISOU 3557  CD2 HIS A 439    20022  14164  17705   3311   3770  -3848       C  
ATOM   3558  CE1 HIS A 439      -6.618 -15.046 -17.551  1.00135.92           C  
ANISOU 3558  CE1 HIS A 439    19278  14504  17861   3218   3522  -3105       C  
ATOM   3559  NE2 HIS A 439      -7.277 -15.913 -18.321  1.00136.47           N  
ANISOU 3559  NE2 HIS A 439    19828  14084  17941   3049   3542  -3515       N  
TER    3560      HIS A 439                                                      
HETATM 3561  N1  QK2 A1201      -7.569   9.638  10.562  1.00 21.70           N  
HETATM 3562  N3  QK2 A1201      -9.269  13.151   5.283  1.00 30.19           N  
HETATM 3563  C4  QK2 A1201      -5.594   7.486   8.212  1.00 22.28           C  
HETATM 3564  C5  QK2 A1201      -6.083   7.875   9.449  1.00 24.10           C  
HETATM 3565  C6  QK2 A1201      -6.934   8.989   9.516  1.00 23.55           C  
HETATM 3566  C7  QK2 A1201      -8.281  10.714  10.100  1.00 22.70           C  
HETATM 3567  C8  QK2 A1201      -8.779  11.712   7.813  1.00 26.03           C  
HETATM 3568  C10 QK2 A1201      -8.487  13.783   6.421  1.00 28.69           C  
HETATM 3569  C13 QK2 A1201     -10.009  14.135   4.454  1.00 36.72           C  
HETATM 3570  C15 QK2 A1201     -10.262  15.297   2.250  1.00 41.31           C  
HETATM 3571  C17 QK2 A1201     -10.370  15.483   5.090  1.00 40.17           C  
HETATM 3572  C1  QK2 A1201      -7.292   9.668   8.348  1.00 23.74           C  
HETATM 3573  C11 QK2 A1201     -10.217  12.097   5.782  1.00 28.16           C  
HETATM 3574  C12 QK2 A1201      -9.539  11.056   6.658  1.00 27.17           C  
HETATM 3575  C14 QK2 A1201      -9.441  14.317   3.051  1.00 39.57           C  
HETATM 3576  C16 QK2 A1201     -11.085  16.415   4.136  1.00 41.30           C  
HETATM 3577  C18 QK2 A1201      -5.374   7.729   5.728  1.00  9.75           C  
HETATM 3578  C2  QK2 A1201      -6.801   9.265   7.116  1.00 19.00           C  
HETATM 3579  C3  QK2 A1201      -5.930   8.183   7.051  1.00 16.21           C  
HETATM 3580  C9  QK2 A1201      -7.792  12.764   7.308  1.00 26.50           C  
HETATM 3581  F1  QK2 A1201      -5.719   7.195  10.551  1.00 25.75           F  
HETATM 3582  N2  QK2 A1201      -8.141  10.718   8.713  1.00 25.24           N  
HETATM 3583  O1  QK2 A1201     -10.354  16.552   2.921  1.00 41.45           O  
HETATM 3584  O2  QK2 A1201      -8.933  11.510  10.771  1.00 20.84           O  
HETATM 3585  N1  EPE A1202     -12.395  15.350  13.902  1.00108.09           N  
HETATM 3586  C2  EPE A1202     -13.351  15.570  12.799  1.00106.13           C  
HETATM 3587  C3  EPE A1202     -13.258  17.003  12.280  1.00104.78           C  
HETATM 3588  N4  EPE A1202     -13.672  17.937  13.345  1.00104.60           N  
HETATM 3589  C5  EPE A1202     -13.086  17.674  14.680  1.00105.87           C  
HETATM 3590  C6  EPE A1202     -12.039  16.556  14.688  1.00107.03           C  
HETATM 3591  C7  EPE A1202     -13.382  19.314  12.929  1.00103.43           C  
HETATM 3592  C8  EPE A1202     -14.595  20.218  13.131  1.00102.97           C  
HETATM 3593  O8  EPE A1202     -14.447  20.926  14.366  1.00103.03           O  
HETATM 3594  C9  EPE A1202     -12.886  14.278  14.781  1.00111.40           C  
HETATM 3595  C10 EPE A1202     -11.775  13.265  15.059  1.00115.12           C  
HETATM 3596  S   EPE A1202     -11.743  12.831  16.670  1.00118.55           S  
HETATM 3597  O1S EPE A1202     -10.773  11.726  16.862  1.00118.97           O  
HETATM 3598  O2S EPE A1202     -13.088  12.368  17.090  1.00119.08           O  
HETATM 3599  O3S EPE A1202     -11.330  13.981  17.510  1.00118.52           O  
HETATM 3600  C1  OLA A1203       0.752  11.148 -21.585  1.00 53.84           C  
HETATM 3601  O1  OLA A1203       0.066  11.724 -22.459  1.00 55.09           O  
HETATM 3602  O2  OLA A1203       1.696  10.371 -21.850  1.00 56.34           O  
HETATM 3603  C2  OLA A1203       0.431  11.412 -20.122  1.00 47.49           C  
HETATM 3604  C3  OLA A1203       1.151  12.585 -19.540  1.00 43.18           C  
HETATM 3605  C4  OLA A1203       1.270  12.510 -18.031  1.00 42.26           C  
HETATM 3606  C5  OLA A1203       1.224  13.855 -17.339  1.00 42.00           C  
HETATM 3607  C6  OLA A1203       0.922  13.799 -15.858  1.00 41.82           C  
HETATM 3608  C7  OLA A1203       2.142  13.565 -14.974  1.00 42.09           C  
HETATM 3609  C8  OLA A1203       1.818  13.096 -13.588  1.00 40.55           C  
HETATM 3610  C9  OLA A1203       1.802  14.206 -12.584  1.00 39.18           C  
HETATM 3611  C10 OLA A1203       2.364  14.192 -11.406  1.00 38.18           C  
HETATM 3612  C11 OLA A1203       1.729  13.658 -10.160  1.00 36.89           C  
HETATM 3613  C12 OLA A1203       2.524  13.911  -8.919  1.00 34.47           C  
HETATM 3614  C13 OLA A1203       3.103  12.657  -8.291  1.00 35.01           C  
HETATM 3615  C14 OLA A1203       2.298  12.093  -7.148  1.00 38.69           C  
HETATM 3616  C15 OLA A1203       2.882  10.830  -6.556  1.00 42.83           C  
HETATM 3617  C16 OLA A1203       2.578  10.625  -5.085  1.00 44.78           C  
HETATM 3618  C17 OLA A1203       2.787   9.216  -4.576  1.00 44.65           C  
HETATM 3619  C18 OLA A1203       3.040   9.139  -3.088  1.00 43.76           C  
HETATM 3620  C1  OLA A1204       4.905  16.687 -13.851  1.00 39.09           C  
HETATM 3621  O1  OLA A1204       4.203  17.715 -13.880  1.00 41.59           O  
HETATM 3622  O2  OLA A1204       5.331  16.111 -14.879  1.00 38.45           O  
HETATM 3623  C2  OLA A1204       5.239  16.094 -12.493  1.00 35.47           C  
HETATM 3624  C3  OLA A1204       6.122  16.940 -11.631  1.00 32.13           C  
HETATM 3625  C4  OLA A1204       6.279  16.378 -10.227  1.00 29.11           C  
HETATM 3626  C5  OLA A1204       6.045  17.391  -9.130  1.00 26.81           C  
HETATM 3627  C6  OLA A1204       5.179  16.895  -8.001  1.00 24.97           C  
HETATM 3628  C7  OLA A1204       5.373  17.636  -6.685  1.00 23.29           C  
HETATM 3629  C8  OLA A1204       5.686  16.749  -5.523  1.00 21.91           C  
HETATM 3630  C9  OLA A1204       4.893  17.066  -4.293  1.00 23.12           C  
HETATM 3631  C10 OLA A1204       4.423  16.204  -3.417  1.00 24.13           C  
HETATM 3632  C11 OLA A1204       3.406  15.133  -3.671  1.00 24.86           C  
HETATM 3633  C12 OLA A1204       2.897  14.506  -2.418  1.00 26.63           C  
HETATM 3634  C13 OLA A1204       3.164  13.013  -2.286  1.00 28.78           C  
HETATM 3635  C14 OLA A1204       4.073  12.630  -1.129  1.00 30.23           C  
HETATM 3636  C15 OLA A1204       3.443  12.718   0.254  1.00 30.62           C  
HETATM 3637  C16 OLA A1204       4.437  12.697   1.397  1.00 28.26           C  
HETATM 3638  C17 OLA A1204       4.090  13.462   2.654  1.00 22.16           C  
HETATM 3639  C18 OLA A1204       5.253  13.586   3.610  1.00 16.05           C  
HETATM 3640  C1  OLA A1205     -18.829   2.873  13.721  1.00 54.46           C  
HETATM 3641  O1  OLA A1205     -17.632   3.035  14.055  1.00 53.56           O  
HETATM 3642  O2  OLA A1205     -19.648   2.201  14.391  1.00 55.99           O  
HETATM 3643  C2  OLA A1205     -19.321   3.539  12.444  1.00 52.53           C  
HETATM 3644  C3  OLA A1205     -19.098   2.769  11.172  1.00 50.63           C  
HETATM 3645  C4  OLA A1205     -19.252   3.634   9.927  1.00 49.63           C  
HETATM 3646  C5  OLA A1205     -18.099   3.546   8.943  1.00 48.37           C  
HETATM 3647  C6  OLA A1205     -18.421   2.797   7.665  1.00 46.79           C  
HETATM 3648  C7  OLA A1205     -17.814   3.394   6.401  1.00 44.77           C  
HETATM 3649  C8  OLA A1205     -17.770   2.456   5.232  1.00 43.23           C  
HETATM 3650  C9  OLA A1205     -17.555   3.153   3.923  1.00 43.76           C  
HETATM 3651  C10 OLA A1205     -18.420   3.300   2.946  1.00 44.34           C  
HETATM 3652  C11 OLA A1205     -19.610   4.214   2.942  1.00 44.19           C  
HETATM 3653  C12 OLA A1205     -19.460   5.417   2.056  1.00 42.10           C  
HETATM 3654  C13 OLA A1205     -20.281   6.620   2.494  1.00 39.73           C  
HETATM 3655  C1  OLA A1206       2.705   6.468  19.773  1.00 56.56           C  
HETATM 3656  O1  OLA A1206       2.099   5.614  20.463  1.00 56.65           O  
HETATM 3657  O2  OLA A1206       2.414   7.690  19.788  1.00 57.67           O  
HETATM 3658  C2  OLA A1206       3.826   5.982  18.856  1.00 53.19           C  
HETATM 3659  C3  OLA A1206       5.074   6.826  18.744  1.00 48.36           C  
HETATM 3660  C4  OLA A1206       5.696   6.841  17.355  1.00 44.62           C  
HETATM 3661  C5  OLA A1206       6.581   5.666  17.014  1.00 41.02           C  
HETATM 3662  C6  OLA A1206       7.113   5.702  15.601  1.00 39.02           C  
HETATM 3663  C7  OLA A1206       6.306   4.890  14.596  1.00 39.26           C  
HETATM 3664  C8  OLA A1206       6.513   5.277  13.167  1.00 38.95           C  
HETATM 3665  C9  OLA A1206       6.574   4.119  12.216  1.00 39.22           C  
HETATM 3666  C10 OLA A1206       7.123   4.128  11.018  1.00 40.04           C  
HETATM 3667  C11 OLA A1206       6.682   4.921   9.821  1.00 39.56           C  
HETATM 3668  C12 OLA A1206       7.648   4.890   8.679  1.00 40.09           C  
HETATM 3669  C13 OLA A1206       7.062   5.315   7.340  1.00 41.85           C  
HETATM 3670  C14 OLA A1206       8.093   5.730   6.305  1.00 43.03           C  
HETATM 3671  C15 OLA A1206       7.548   6.613   5.199  1.00 43.72           C  
HETATM 3672  C16 OLA A1206       8.559   7.553   4.572  1.00 42.83           C  
HETATM 3673  C17 OLA A1206       8.579   7.562   3.060  1.00 41.71           C  
HETATM 3674  C18 OLA A1206       9.004   8.871   2.432  1.00 40.41           C  
HETATM 3675  C1  OLA A1207      -3.669   0.776  11.875  1.00 56.68           C  
HETATM 3676  O1  OLA A1207      -2.818   1.681  11.989  1.00 57.45           O  
HETATM 3677  O2  OLA A1207      -4.843   0.870  12.302  1.00 56.83           O  
HETATM 3678  C2  OLA A1207      -3.248  -0.518  11.199  1.00 54.72           C  
HETATM 3679  C3  OLA A1207      -2.963  -0.423   9.733  1.00 51.97           C  
HETATM 3680  C4  OLA A1207      -2.317  -1.685   9.195  1.00 50.83           C  
HETATM 3681  C5  OLA A1207      -1.773  -1.554   7.797  1.00 51.96           C  
HETATM 3682  C6  OLA A1207      -0.299  -1.218   7.725  1.00 53.54           C  
HETATM 3683  C7  OLA A1207       0.116  -0.492   6.449  1.00 53.37           C  
HETATM 3684  C8  OLA A1207       1.368   0.328   6.565  1.00 51.35           C  
HETATM 3685  C9  OLA A1207       1.146   1.787   6.301  1.00 48.65           C  
HETATM 3686  C10 OLA A1207       1.930   2.764   6.689  1.00 45.58           C  
HETATM 3687  C11 OLA A1207       1.701   4.220   6.426  1.00 42.59           C  
HETATM 3688  C12 OLA A1207       2.827   5.094   6.881  1.00 40.63           C  
HETATM 3689  C13 OLA A1207       2.793   6.490   6.285  1.00 40.84           C  
HETATM 3690  C14 OLA A1207       3.730   6.693   5.120  1.00 41.89           C  
HETATM 3691  C15 OLA A1207       3.091   7.312   3.902  1.00 43.30           C  
HETATM 3692  C16 OLA A1207       3.351   8.796   3.736  1.00 44.95           C  
HETATM 3693  C17 OLA A1207       4.298   9.191   2.626  1.00 45.02           C  
HETATM 3694  C18 OLA A1207       5.568   9.851   3.116  1.00 44.35           C  
HETATM 3695  C1  OLA A1208     -23.057   6.398  18.733  1.00 67.34           C  
HETATM 3696  O1  OLA A1208     -23.853   5.847  19.526  1.00 68.04           O  
HETATM 3697  O2  OLA A1208     -22.914   7.637  18.660  1.00 67.18           O  
HETATM 3698  C2  OLA A1208     -22.205   5.524  17.822  1.00 66.27           C  
HETATM 3699  C3  OLA A1208     -22.873   4.297  17.261  1.00 64.64           C  
HETATM 3700  C4  OLA A1208     -22.364   3.924  15.878  1.00 62.61           C  
HETATM 3701  C5  OLA A1208     -23.238   2.936  15.140  1.00 61.40           C  
HETATM 3702  C6  OLA A1208     -22.946   2.819  13.658  1.00 60.58           C  
HETATM 3703  C7  OLA A1208     -23.980   3.482  12.754  1.00 59.09           C  
HETATM 3704  C8  OLA A1208     -24.221   2.771  11.456  1.00 57.91           C  
HETATM 3705  C9  OLA A1208     -23.999   3.629  10.248  1.00 56.93           C  
HETATM 3706  C10 OLA A1208     -23.884   3.203   9.010  1.00 55.50           C  
HETATM 3707  C11 OLA A1208     -22.631   2.699   8.358  1.00 54.39           C  
HETATM 3708  C12 OLA A1208     -22.881   1.871   7.130  1.00 52.91           C  
HETATM 3709  C13 OLA A1208     -21.910   2.116   5.979  1.00 49.41           C  
HETATM 3710  C14 OLA A1208     -22.185   1.299   4.737  1.00 46.04           C  
HETATM 3711  C15 OLA A1208     -23.140   1.952   3.762  1.00 44.37           C  
HETATM 3712  C16 OLA A1208     -23.418   1.148   2.508  1.00 42.90           C  
HETATM 3713  C17 OLA A1208     -23.848   1.951   1.298  1.00 40.90           C  
HETATM 3714  C18 OLA A1208     -23.066   1.666   0.036  1.00 38.75           C  
HETATM 3715  P   PO4 A1209      -7.488  36.912 -27.724  1.00101.01           P  
HETATM 3716  O1  PO4 A1209      -7.124  37.512 -29.078  1.00100.97           O  
HETATM 3717  O2  PO4 A1209      -7.249  35.407 -27.753  1.00100.71           O  
HETATM 3718  O3  PO4 A1209      -8.957  37.187 -27.418  1.00101.59           O  
HETATM 3719  O4  PO4 A1209      -6.625  37.548 -26.642  1.00101.14           O  
HETATM 3720  O   HOH A1301      -6.533  13.323  21.792  1.00 29.16           O  
HETATM 3721  O   HOH A1302     -13.653   4.431 -10.704  1.00 22.36           O  
HETATM 3722  O   HOH A1303      -0.828   8.585  17.134  1.00 13.30           O  
HETATM 3723  O   HOH A1304      -9.760   9.637  15.044  1.00 18.86           O  
HETATM 3724  O   HOH A1305      -6.613  18.219  19.480  1.00 24.03           O  
HETATM 3725  O   HOH A1306      -9.743  16.287 -19.239  1.00 25.92           O  
HETATM 3726  O   HOH A1307     -10.781  16.637  17.579  1.00 31.80           O  
HETATM 3727  O   HOH A1308     -18.744  14.221   2.226  1.00  5.46           O  
HETATM 3728  O   HOH A1309      -1.860  14.970  13.631  1.00 22.02           O  
HETATM 3729  O   HOH A1310      -1.668  18.201  12.690  1.00  8.00           O  
HETATM 3730  O   HOH A1311     -11.346  13.214  -2.389  1.00 26.60           O  
HETATM 3731  O   HOH A1312       4.407  14.609 -22.205  1.00 32.70           O  
HETATM 3732  O   HOH A1313      -8.473  14.472  11.014  1.00 16.79           O  
HETATM 3733  O   HOH A1314       7.017  25.203  21.229  1.00 20.61           O  
HETATM 3734  O   HOH A1315     -13.342  18.832 -19.875  1.00  9.85           O  
HETATM 3735  O   HOH A1316       0.057  16.217  15.527  1.00 19.47           O  
HETATM 3736  O   HOH A1317     -24.218  42.279 -59.375  1.00 22.07           O  
HETATM 3737  O   HOH A1318     -26.692  35.532 -52.324  1.00 19.67           O  
HETATM 3738  O   HOH A1319     -21.532  50.724 -52.100  1.00 36.58           O  
HETATM 3739  O   HOH A1320      -9.280  16.264  12.926  1.00 29.49           O  
HETATM 3740  O   HOH A1321       0.172   4.594  17.740  1.00 22.85           O  
HETATM 3741  O   HOH A1322     -18.908  18.197  16.078  1.00 12.10           O  
HETATM 3742  O   HOH A1323      -1.330  25.233 -20.897  1.00 15.26           O  
CONECT  591 1232                                                                
CONECT 1232  591                                                                
CONECT 3155 3178                                                                
CONECT 3178 3155                                                                
CONECT 3561 3565 3566                                                           
CONECT 3562 3568 3569 3573                                                      
CONECT 3563 3564 3579                                                           
CONECT 3564 3563 3565 3581                                                      
CONECT 3565 3561 3564 3572                                                      
CONECT 3566 3561 3582 3584                                                      
CONECT 3567 3574 3580 3582                                                      
CONECT 3568 3562 3580                                                           
CONECT 3569 3562 3571 3575                                                      
CONECT 3570 3575 3583                                                           
CONECT 3571 3569 3576                                                           
CONECT 3572 3565 3578 3582                                                      
CONECT 3573 3562 3574                                                           
CONECT 3574 3567 3573                                                           
CONECT 3575 3569 3570                                                           
CONECT 3576 3571 3583                                                           
CONECT 3577 3579                                                                
CONECT 3578 3572 3579                                                           
CONECT 3579 3563 3577 3578                                                      
CONECT 3580 3567 3568                                                           
CONECT 3581 3564                                                                
CONECT 3582 3566 3567 3572                                                      
CONECT 3583 3570 3576                                                           
CONECT 3584 3566                                                                
CONECT 3585 3586 3590 3594                                                      
CONECT 3586 3585 3587                                                           
CONECT 3587 3586 3588                                                           
CONECT 3588 3587 3589 3591                                                      
CONECT 3589 3588 3590                                                           
CONECT 3590 3585 3589                                                           
CONECT 3591 3588 3592                                                           
CONECT 3592 3591 3593                                                           
CONECT 3593 3592                                                                
CONECT 3594 3585 3595                                                           
CONECT 3595 3594 3596                                                           
CONECT 3596 3595 3597 3598 3599                                                 
CONECT 3597 3596                                                                
CONECT 3598 3596                                                                
CONECT 3599 3596                                                                
CONECT 3600 3601 3602 3603                                                      
CONECT 3601 3600                                                                
CONECT 3602 3600                                                                
CONECT 3603 3600 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 3619                                                           
CONECT 3619 3618                                                                
CONECT 3620 3621 3622 3623                                                      
CONECT 3621 3620                                                                
CONECT 3622 3620                                                                
CONECT 3623 3620 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 3639                                                           
CONECT 3639 3638                                                                
CONECT 3640 3641 3642 3643                                                      
CONECT 3641 3640                                                                
CONECT 3642 3640                                                                
CONECT 3643 3640 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                                                                
CONECT 3655 3656 3657 3658                                                      
CONECT 3656 3655                                                                
CONECT 3657 3655                                                                
CONECT 3658 3655 3659                                                           
CONECT 3659 3658 3660                                                           
CONECT 3660 3659 3661                                                           
CONECT 3661 3660 3662                                                           
CONECT 3662 3661 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                                                                
CONECT 3675 3676 3677 3678                                                      
CONECT 3676 3675                                                                
CONECT 3677 3675                                                                
CONECT 3678 3675 3679                                                           
CONECT 3679 3678 3680                                                           
CONECT 3680 3679 3681                                                           
CONECT 3681 3680 3682                                                           
CONECT 3682 3681 3683                                                           
CONECT 3683 3682 3684                                                           
CONECT 3684 3683 3685                                                           
CONECT 3685 3684 3686                                                           
CONECT 3686 3685 3687                                                           
CONECT 3687 3686 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                                                                
CONECT 3695 3696 3697 3698                                                      
CONECT 3696 3695                                                                
CONECT 3697 3695                                                                
CONECT 3698 3695 3699                                                           
CONECT 3699 3698 3700                                                           
CONECT 3700 3699 3701                                                           
CONECT 3701 3700 3702                                                           
CONECT 3702 3701 3703                                                           
CONECT 3703 3702 3704                                                           
CONECT 3704 3703 3705                                                           
CONECT 3705 3704 3706                                                           
CONECT 3706 3705 3707                                                           
CONECT 3707 3706 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                                                                
CONECT 3715 3716 3717 3718 3719                                                 
CONECT 3716 3715                                                                
CONECT 3717 3715                                                                
CONECT 3718 3715                                                                
CONECT 3719 3715                                                                
MASTER      348    0    9   21    3    0   19    6 3738    1  163   35          
END