HEADER    MEMBRANE PROTEIN                        15-AUG-19   6KPC              
TITLE     CRYSTAL STRUCTURE OF AN AGONIST BOUND GPCR                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CANNABINOID RECEPTOR 2,ENDOLYSIN;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HCB2,CX5,LYSIS PROTEIN,LYSOZYME,MURAMIDASE;                 
COMPND   5 EC: 3.2.1.17;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 OTHER_DETAILS: CB2, T4 LYSOZYME, CB2 FUSION,CB2, T4 LYSOZYME, CB2    
COMPND   9 FUSION,CB2, T4 LYSOZYME, CB2 FUSION,CB2, T4 LYSOZYME, CB2 FUSION,CB2,
COMPND  10 T4 LYSOZYME, CB2 FUSION,CB2, T4 LYSOZYME, CB2 FUSION,CB2, T4         
COMPND  11 LYSOZYME, CB2 FUSION,CB2, T4 LYSOZYME, CB2 FUSION,CB2, T4 LYSOZYME,  
COMPND  12 CB2 FUSION,CB2, T4 LYSOZYME, CB2 FUSION,CB2, T4 LYSOZYME, CB2 FUSION,
COMPND  13 CB2, T4 LYSOZYME, CB2 FUSION,CB2, T4 LYSOZYME, CB2 FUSION,CB2, T4    
COMPND  14 LYSOZYME, CB2 FUSION,CB2, T4 LYSOZYME, CB2 FUSION,CB2, T4 LYSOZYME,  
COMPND  15 CB2 FUSION,CB2, T4 LYSOZYME, CB2 FUSION,CB2, T4 LYSOZYME, CB2 FUSION,
COMPND  16 CB2, T4 LYSOZYME, CB2 FUSION,CB2, T4 LYSOZYME, CB2 FUSION,CB2, T4    
COMPND  17 LYSOZYME, CB2 FUSION,CB2, T4 LYSOZYME, CB2 FUSION,CB2, T4 LYSOZYME,  
COMPND  18 CB2 FUSION,CB2, T4 LYSOZYME, CB2 FUSION,CB2, T4 LYSOZYME, CB2 FUSION,
COMPND  19 CB2, T4 LYSOZYME, CB2 FUSION,CB2, T4 LYSOZYME, CB2 FUSION            
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE RB59;        
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606, 697290;                                        
SOURCE   5 GENE: CNR2, CB2A, CB2B, E, RB59_126;                                 
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    GPCR, LCP, AGONIST, MEMBRANE PROTEIN                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.T.LI,T.HUA,L.J.WU,A.MAKRIYANNIS,M.WU,Z.J.LIU                        
REVDAT   3   27-APR-22 6KPC    1       COMPND SOURCE REMARK HET                 
REVDAT   3 2                   1       HETNAM FORMUL ATOM                       
REVDAT   2   11-MAR-20 6KPC    1       JRNL                                     
REVDAT   1   12-FEB-20 6KPC    0                                                
JRNL        AUTH   T.HUA,X.LI,L.WU,C.ILIOPOULOS-TSOUTSOUVAS,Y.WANG,M.WU,L.SHEN, 
JRNL        AUTH 2 C.A.JOHNSTON,S.P.NIKAS,F.SONG,X.SONG,S.YUAN,Q.SUN,Y.WU,      
JRNL        AUTH 3 S.JIANG,T.W.GRIM,O.BENCHAMA,E.L.STAHL,N.ZVONOK,S.ZHAO,       
JRNL        AUTH 4 L.M.BOHN,A.MAKRIYANNIS,Z.J.LIU                               
JRNL        TITL   ACTIVATION AND SIGNALING MECHANISM REVEALED BY CANNABINOID   
JRNL        TITL 2 RECEPTOR-GICOMPLEX STRUCTURES.                               
JRNL        REF    CELL                          V. 180   655 2020              
JRNL        REFN                   ISSN 1097-4172                               
JRNL        PMID   32004463                                                     
JRNL        DOI    10.1016/J.CELL.2020.01.008                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.3                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.78                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 87.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 11475                          
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)  : 0.231                          
REMARK   3   R VALUE            (WORKING SET)  : 0.230                          
REMARK   3   FREE R VALUE                      : 0.262                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.630                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 531                            
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               : 6                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.20                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.50                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 88.31                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2690                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2337                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2560                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2316                   
REMARK   3   BIN FREE R VALUE                        : 0.2744                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.83                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 130                      
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            : 3471                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 29                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 96.93                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 118.2                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 20.71690                                             
REMARK   3    B22 (A**2) : -22.83080                                            
REMARK   3    B33 (A**2) : 2.11380                                              
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) : 0.530               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.480               
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      : 0.905                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.871                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3581   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 4871   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1211   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : NULL   ; NULL   ; NULL                
REMARK   3    GENERAL PLANES            : 578    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3581   ; 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   : 473    ; 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   : 4227   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.009                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.03                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 1.95                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 19.89                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|19 - 315 }                                         
REMARK   3    ORIGIN FOR THE GROUP (A):   10.6139   -2.8231  -32.6508           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.4219 T22:   -0.1101                                    
REMARK   3     T33:   -0.3133 T12:   -0.0599                                    
REMARK   3     T13:    0.0676 T23:    0.3040                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.1904 L22:    7.0911                                    
REMARK   3     L33:   10.9773 L12:   -1.0658                                    
REMARK   3     L13:   -0.3788 L23:   -5.8208                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1812 S12:    0.0118 S13:    0.1515                     
REMARK   3     S21:    0.1045 S22:   -0.5129 S23:   -0.2743                     
REMARK   3     S31:   -0.6384 S32:    0.8462 S33:    0.3318                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { A|1001 - 1160 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):   -5.1493  -22.9251    9.9196           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1209 T22:    0.0746                                    
REMARK   3     T33:   -0.2662 T12:   -0.0578                                    
REMARK   3     T13:    0.0458 T23:   -0.1068                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.2757 L22:    1.1369                                    
REMARK   3     L33:    1.7562 L12:    0.0526                                    
REMARK   3     L13:   -1.6960 L23:    0.5983                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1452 S12:   -0.5418 S13:    0.3725                     
REMARK   3     S21:    0.1831 S22:    0.0799 S23:    0.1184                     
REMARK   3     S31:   -0.1573 S32:    0.0554 S33:   -0.2250                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6KPC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-AUG-19.                  
REMARK 100 THE DEPOSITION ID IS D_1300013422.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-OCT-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11476                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.780                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 87.6                               
REMARK 200  DATA REDUNDANCY                : 2.847                              
REMARK 200  R MERGE                    (I) : 0.17100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.2600                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.67300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.220                              
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: 5ZTY                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.19                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES SODIUM PH 7.0, 25% PEG      
REMARK 280  400, 220 MM SODIUM SULFATE DECAHYDRATE, 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       16.98000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       78.13000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       70.11000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       78.13000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       16.98000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       70.11000            
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 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     MET A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     ILE A     5                                                      
REMARK 465     ILE A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     LEU A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     TYR A    10                                                      
REMARK 465     ILE A    11                                                      
REMARK 465     PHE A    12                                                      
REMARK 465     CYS A    13                                                      
REMARK 465     LEU A    14                                                      
REMARK 465     VAL A    15                                                      
REMARK 465     PHE A    16                                                      
REMARK 465     ALA A    17                                                      
REMARK 465     GLY A    18                                                      
REMARK 465     HIS A   316                                                      
REMARK 465     TRP A   317                                                      
REMARK 465     LYS A   318                                                      
REMARK 465     LYS A   319                                                      
REMARK 465     CYS A   320                                                      
REMARK 465     VAL A   321                                                      
REMARK 465     ARG A   322                                                      
REMARK 465     GLY A   323                                                      
REMARK 465     LEU A   324                                                      
REMARK 465     GLY A   325                                                      
REMARK 465     GLU A   326                                                      
REMARK 465     PHE A   327                                                      
REMARK 465     LEU A   328                                                      
REMARK 465     GLU A   329                                                      
REMARK 465     VAL A   330                                                      
REMARK 465     LEU A   331                                                      
REMARK 465     PHE A   332                                                      
REMARK 465     GLN A   333                                                      
REMARK 465     GLY A   334                                                      
REMARK 465     PRO A   335                                                      
REMARK 465     HIS A   336                                                      
REMARK 465     HIS A   337                                                      
REMARK 465     HIS A   338                                                      
REMARK 465     HIS A   339                                                      
REMARK 465     HIS A   340                                                      
REMARK 465     HIS A   341                                                      
REMARK 465     HIS A   342                                                      
REMARK 465     HIS A   343                                                      
REMARK 465     HIS A   344                                                      
REMARK 465     HIS A   345                                                      
REMARK 465     ASP A   346                                                      
REMARK 465     TYR A   347                                                      
REMARK 465     LYS A   348                                                      
REMARK 465     ASP A   349                                                      
REMARK 465     ASP A   350                                                      
REMARK 465     ASP A   351                                                      
REMARK 465     ASP A   352                                                      
REMARK 465     LYS A   353                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  33    CG   CD   CE   NZ                                   
REMARK 470     ARG A  66    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 144    CG   CD1  CD2                                       
REMARK 470     LEU A 145    CG   CD1  CD2                                       
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    MET A 170     -119.25    -68.65                                   
REMARK 500    CYS A 175      -86.27   -105.35                                   
REMARK 500    LEU A 185       -6.81     67.10                                   
REMARK 500    HIS A1030       96.07    -69.80                                   
REMARK 500    SER A1035      143.58    -39.95                                   
REMARK 500    ARG A1079       30.47    -87.67                                   
REMARK 500    PHE A1113       49.63    -74.27                                   
REMARK 500    SER A 303      106.77    -48.00                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue E3R A 1201                
DBREF  6KPC A   21   222  UNP    P34972   CNR2_HUMAN      21    222             
DBREF1 6KPC A 1001  1160  UNP                  A0A097J809_BPT4                  
DBREF2 6KPC A     A0A097J809                          2         161             
DBREF  6KPC A  235   325  UNP    P34972   CNR2_HUMAN     235    325             
SEQADV 6KPC MET A    2  UNP  P34972              INITIATING METHIONINE          
SEQADV 6KPC LYS A    3  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC THR A    4  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC ILE A    5  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC ILE A    6  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC ALA A    7  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC LEU A    8  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC SER A    9  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC TYR A   10  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC ILE A   11  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC PHE A   12  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC CYS A   13  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC LEU A   14  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC VAL A   15  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC PHE A   16  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC ALA A   17  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC GLY A   18  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC ALA A   19  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC PRO A   20  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC LEU A   78  UNP  P34972    GLY    78 ENGINEERED MUTATION            
SEQADV 6KPC ALA A  127  UNP  P34972    THR   127 ENGINEERED MUTATION            
SEQADV 6KPC LEU A  153  UNP  P34972    THR   153 ENGINEERED MUTATION            
SEQADV 6KPC ALA A  210  UNP  P34972    GLY   210 ENGINEERED MUTATION            
SEQADV 6KPC THR A 1053  UNP  A0A097J80 CYS    54 ENGINEERED MUTATION            
SEQADV 6KPC ALA A 1096  UNP  A0A097J80 CYS    97 ENGINEERED MUTATION            
SEQADV 6KPC GLU A  242  UNP  P34972    ARG   242 ENGINEERED MUTATION            
SEQADV 6KPC GLU A  304  UNP  P34972    GLY   304 ENGINEERED MUTATION            
SEQADV 6KPC GLU A  326  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC PHE A  327  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC LEU A  328  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC GLU A  329  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC VAL A  330  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC LEU A  331  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC PHE A  332  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC GLN A  333  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC GLY A  334  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC PRO A  335  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC HIS A  336  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC HIS A  337  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC HIS A  338  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC HIS A  339  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC HIS A  340  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC HIS A  341  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC HIS A  342  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC HIS A  343  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC HIS A  344  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC HIS A  345  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC ASP A  346  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC TYR A  347  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC LYS A  348  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC ASP A  349  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC ASP A  350  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC ASP A  351  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC ASP A  352  UNP  P34972              EXPRESSION TAG                 
SEQADV 6KPC LYS A  353  UNP  P34972              EXPRESSION TAG                 
SEQRES   1 A  500  MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU          
SEQRES   2 A  500  VAL PHE ALA GLY ALA PRO PRO MET LYS ASP TYR MET ILE          
SEQRES   3 A  500  LEU SER GLY PRO GLN LYS THR ALA VAL ALA VAL LEU CYS          
SEQRES   4 A  500  THR LEU LEU GLY LEU LEU SER ALA LEU GLU ASN VAL ALA          
SEQRES   5 A  500  VAL LEU TYR LEU ILE LEU SER SER HIS GLN LEU ARG ARG          
SEQRES   6 A  500  LYS PRO SER TYR LEU PHE ILE GLY SER LEU ALA LEU ALA          
SEQRES   7 A  500  ASP PHE LEU ALA SER VAL VAL PHE ALA CYS SER PHE VAL          
SEQRES   8 A  500  ASN PHE HIS VAL PHE HIS GLY VAL ASP SER LYS ALA VAL          
SEQRES   9 A  500  PHE LEU LEU LYS ILE GLY SER VAL THR MET THR PHE THR          
SEQRES  10 A  500  ALA SER VAL GLY SER LEU LEU LEU ALA ALA ILE ASP ARG          
SEQRES  11 A  500  TYR LEU CYS LEU ARG TYR PRO PRO SER TYR LYS ALA LEU          
SEQRES  12 A  500  LEU THR ARG GLY ARG ALA LEU VAL LEU LEU GLY ILE MET          
SEQRES  13 A  500  TRP VAL LEU SER ALA LEU VAL SER TYR LEU PRO LEU MET          
SEQRES  14 A  500  GLY TRP THR CYS CYS PRO ARG PRO CYS SER GLU LEU PHE          
SEQRES  15 A  500  PRO LEU ILE PRO ASN ASP TYR LEU LEU SER TRP LEU LEU          
SEQRES  16 A  500  PHE ILE ALA PHE LEU PHE SER GLY ILE ILE TYR THR TYR          
SEQRES  17 A  500  ALA HIS VAL LEU TRP LYS ALA HIS GLN HIS VAL ALA SER          
SEQRES  18 A  500  ASN ILE PHE GLU MET LEU ARG ILE ASP GLU GLY LEU ARG          
SEQRES  19 A  500  LEU LYS ILE TYR LYS ASP THR GLU GLY TYR TYR THR ILE          
SEQRES  20 A  500  GLY ILE GLY HIS LEU LEU THR LYS SER PRO SER LEU ASN          
SEQRES  21 A  500  ALA ALA LYS SER GLU LEU ASP LYS ALA ILE GLY ARG ASN          
SEQRES  22 A  500  THR ASN GLY VAL ILE THR LYS ASP GLU ALA GLU LYS LEU          
SEQRES  23 A  500  PHE ASN GLN ASP VAL ASP ALA ALA VAL ARG GLY ILE LEU          
SEQRES  24 A  500  ARG ASN ALA LYS LEU LYS PRO VAL TYR ASP SER LEU ASP          
SEQRES  25 A  500  ALA VAL ARG ARG ALA ALA LEU ILE ASN MET VAL PHE GLN          
SEQRES  26 A  500  MET GLY GLU THR GLY VAL ALA GLY PHE THR ASN SER LEU          
SEQRES  27 A  500  ARG MET LEU GLN GLN LYS ARG TRP ASP GLU ALA ALA VAL          
SEQRES  28 A  500  ASN LEU ALA LYS SER ARG TRP TYR ASN GLN THR PRO ASN          
SEQRES  29 A  500  ARG ALA LYS ARG VAL ILE THR THR PHE ARG THR GLY THR          
SEQRES  30 A  500  TRP ASP ALA TYR ALA ARG MET ARG LEU ASP VAL GLU LEU          
SEQRES  31 A  500  ALA LYS THR LEU GLY LEU VAL LEU ALA VAL LEU LEU ILE          
SEQRES  32 A  500  CYS TRP PHE PRO VAL LEU ALA LEU MET ALA HIS SER LEU          
SEQRES  33 A  500  ALA THR THR LEU SER ASP GLN VAL LYS LYS ALA PHE ALA          
SEQRES  34 A  500  PHE CYS SER MET LEU CYS LEU ILE ASN SER MET VAL ASN          
SEQRES  35 A  500  PRO VAL ILE TYR ALA LEU ARG SER GLU GLU ILE ARG SER          
SEQRES  36 A  500  SER ALA HIS HIS CYS LEU ALA HIS TRP LYS LYS CYS VAL          
SEQRES  37 A  500  ARG GLY LEU GLY GLU PHE LEU GLU VAL LEU PHE GLN GLY          
SEQRES  38 A  500  PRO HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS ASP TYR          
SEQRES  39 A  500  LYS ASP ASP ASP ASP LYS                                      
HET    E3R  A1201      29                                                       
HETNAM     E3R 7-[(6AR,9R,10AR)-1-HYDROXY-9-(HYDROXYMETHYL)-6,6-                
HETNAM   2 E3R  DIMETHYL-6A,7,8,9,10,10A-HEXAHYDRO-6H-BENZO[C]CHROMEN-          
HETNAM   3 E3R  3-YL]- 7-METHYLOCTANENITRILE                                    
FORMUL   2  E3R    C25 H37 N O3                                                 
HELIX    1 AA1 MET A   22  MET A   26  5                                   5    
HELIX    2 AA2 GLY A   30  SER A   61  1                                  32    
HELIX    3 AA3 SER A   61  ARG A   66  1                                   6    
HELIX    4 AA4 PRO A   68  HIS A   95  1                                  28    
HELIX    5 AA5 SER A  102  TYR A  137  1                                  36    
HELIX    6 AA6 SER A  140  LEU A  145  1                                   6    
HELIX    7 AA7 THR A  146  TYR A  166  1                                  21    
HELIX    8 AA8 PRO A  187  VAL A  220  1                                  34    
HELIX    9 AA9 ASN A 1001  GLU A 1010  1                                  10    
HELIX   10 AB1 SER A 1037  GLY A 1050  1                                  14    
HELIX   11 AB2 THR A 1058  ARG A 1079  1                                  22    
HELIX   12 AB3 LEU A 1083  LEU A 1090  1                                   8    
HELIX   13 AB4 VAL A 1093  GLY A 1106  1                                  14    
HELIX   14 AB5 GLY A 1106  ALA A 1111  1                                   6    
HELIX   15 AB6 PHE A 1113  GLN A 1122  1                                  10    
HELIX   16 AB7 ARG A 1124  ALA A 1133  1                                  10    
HELIX   17 AB8 SER A 1135  THR A 1141  1                                   7    
HELIX   18 AB9 THR A 1141  GLY A 1155  1                                  15    
HELIX   19 AC1 TRP A 1157  ALA A  235  5                                   5    
HELIX   20 AC2 MET A  237  THR A  271  1                                  35    
HELIX   21 AC3 SER A  274  ALA A  300  1                                  27    
HELIX   22 AC4 SER A  303  ALA A  310  1                                   8    
SHEET    1 AA1 3 TYR A1017  LYS A1018  0                                        
SHEET    2 AA1 3 TYR A1024  ILE A1026 -1  O  THR A1025   N  TYR A1017           
SHEET    3 AA1 3 HIS A1030  THR A1033 -1  O  LEU A1032   N  TYR A1024           
SSBOND   1 CYS A  174    CYS A  179                          1555   1555  2.04  
SITE     1 AC1 16 PHE A  87  SER A  90  PHE A  91  PHE A  94                    
SITE     2 AC1 16 HIS A  95  VAL A 113  THR A 114  PHE A 117                    
SITE     3 AC1 16 LEU A 182  PHE A 183  TYR A 190  LEU A 191                    
SITE     4 AC1 16 VAL A 261  MET A 265  PHE A 281  SER A 285                    
CRYST1   33.960  140.220  156.260  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      0.029446  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007132  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006400        0.00000                         
ATOM      1  N   ALA A  19      15.810  -1.879 -63.453  1.00181.56           N  
ANISOU    1  N   ALA A  19    28610  27520  12853   7550   5207   5710       N  
ATOM      2  CA  ALA A  19      15.524  -1.353 -62.122  1.00176.99           C  
ANISOU    2  CA  ALA A  19    27290  26989  12969   7402   5100   5988       C  
ATOM      3  C   ALA A  19      14.446  -0.252 -62.166  1.00177.95           C  
ANISOU    3  C   ALA A  19    27174  27052  13385   6762   4474   5975       C  
ATOM      4  O   ALA A  19      14.516   0.626 -63.031  1.00180.68           O  
ANISOU    4  O   ALA A  19    27528  27662  13459   6907   4645   6402       O  
ATOM      5  CB  ALA A  19      16.798  -0.825 -61.479  1.00176.90           C  
ANISOU    5  CB  ALA A  19    26269  27372  13574   7422   5714   6695       C  
ATOM      6  N   PRO A  20      13.440  -0.283 -61.252  1.00169.09           N  
ANISOU    6  N   PRO A  20    25842  25603  12802   6109   3789   5541       N  
ATOM      7  CA  PRO A  20      12.377   0.741 -61.282  1.00166.27           C  
ANISOU    7  CA  PRO A  20    25260  25205  12710   5611   3246   5578       C  
ATOM      8  C   PRO A  20      12.826   2.113 -60.763  1.00166.97           C  
ANISOU    8  C   PRO A  20    24493  25449  13500   5295   3480   6166       C  
ATOM      9  O   PRO A  20      13.699   2.164 -59.890  1.00164.09           O  
ANISOU    9  O   PRO A  20    23553  25131  13662   5162   3805   6383       O  
ATOM     10  CB  PRO A  20      11.267   0.137 -60.404  1.00163.21           C  
ANISOU   10  CB  PRO A  20    24891  24456  12665   5106   2549   4988       C  
ATOM     11  CG  PRO A  20      11.703  -1.281 -60.105  1.00168.71           C  
ANISOU   11  CG  PRO A  20    26008  24951  13145   5348   2686   4586       C  
ATOM     12  CD  PRO A  20      13.191  -1.260 -60.176  1.00166.66           C  
ANISOU   12  CD  PRO A  20    25505  24961  12855   5851   3509   5043       C  
ATOM     13  N   PRO A  21      12.242   3.232 -61.276  1.00163.98           N  
ANISOU   13  N   PRO A  21    24055  25128  13122   5151   3295   6448       N  
ATOM     14  CA  PRO A  21      12.679   4.567 -60.823  1.00161.79           C  
ANISOU   14  CA  PRO A  21    23114  24891  13470   4831   3518   7008       C  
ATOM     15  C   PRO A  21      12.335   4.894 -59.377  1.00157.82           C  
ANISOU   15  C   PRO A  21    22084  24079  13801   4236   3218   6835       C  
ATOM     16  O   PRO A  21      11.375   4.355 -58.825  1.00153.46           O  
ANISOU   16  O   PRO A  21    21634  23299  13374   4039   2729   6325       O  
ATOM     17  CB  PRO A  21      11.985   5.530 -61.797  1.00166.78           C  
ANISOU   17  CB  PRO A  21    23980  25590  13797   4911   3358   7287       C  
ATOM     18  CG  PRO A  21      11.497   4.679 -62.926  1.00175.90           C  
ANISOU   18  CG  PRO A  21    25903  26877  14055   5353   3175   6978       C  
ATOM     19  CD  PRO A  21      11.208   3.347 -62.323  1.00168.89           C  
ANISOU   19  CD  PRO A  21    25247  25781  13142   5278   2878   6321       C  
ATOM     20  N   MET A  22      13.136   5.789 -58.774  1.00152.84           N  
ANISOU   20  N   MET A  22    20913  23446  13712   3930   3508   7293       N  
ATOM     21  CA  MET A  22      13.000   6.235 -57.389  1.00147.13           C  
ANISOU   21  CA  MET A  22    19758  22416  13729   3364   3293   7192       C  
ATOM     22  C   MET A  22      11.734   7.063 -57.146  1.00147.97           C  
ANISOU   22  C   MET A  22    19958  22195  14070   3128   2864   7062       C  
ATOM     23  O   MET A  22      11.144   6.952 -56.074  1.00143.06           O  
ANISOU   23  O   MET A  22    19197  21301  13859   2829   2561   6719       O  
ATOM     24  CB  MET A  22      14.248   7.007 -56.955  1.00150.86           C  
ANISOU   24  CB  MET A  22    19730  22977  14612   3054   3676   7767       C  
ATOM     25  CG  MET A  22      14.498   6.950 -55.479  1.00150.24           C  
ANISOU   25  CG  MET A  22    19259  22686  15140   2543   3518   7595       C  
ATOM     26  SD  MET A  22      15.698   5.695 -55.016  1.00154.77           S  
ANISOU   26  SD  MET A  22    19477  23618  15708   2698   3821   7607       S  
ATOM     27  CE  MET A  22      16.426   6.463 -53.588  1.00149.87           C  
ANISOU   27  CE  MET A  22    18264  22866  15815   1919   3731   7883       C  
ATOM     28  N   LYS A  23      11.321   7.888 -58.125  1.00147.90           N  
ANISOU   28  N   LYS A  23    20178  22233  13786   3315   2874   7381       N  
ATOM     29  CA  LYS A  23      10.115   8.713 -58.002  1.00146.65           C  
ANISOU   29  CA  LYS A  23    20101  21810  13808   3217   2527   7363       C  
ATOM     30  C   LYS A  23       8.824   7.875 -58.045  1.00148.87           C  
ANISOU   30  C   LYS A  23    20567  22124  13873   3339   2015   6868       C  
ATOM     31  O   LYS A  23       7.808   8.305 -57.501  1.00146.88           O  
ANISOU   31  O   LYS A  23    20216  21668  13923   3213   1713   6785       O  
ATOM     32  CB  LYS A  23      10.095   9.871 -59.028  1.00153.75           C  
ANISOU   32  CB  LYS A  23    21171  22757  14489   3403   2709   7929       C  
ATOM     33  CG  LYS A  23       9.986   9.462 -60.498  1.00171.73           C  
ANISOU   33  CG  LYS A  23    23821  25433  15994   3891   2742   8034       C  
ATOM     34  CD  LYS A  23       9.847  10.687 -61.403  1.00186.41           C  
ANISOU   34  CD  LYS A  23    25830  27315  17684   4063   2891   8624       C  
ATOM     35  CE  LYS A  23       9.770  10.348 -62.876  1.00200.38           C  
ANISOU   35  CE  LYS A  23    28012  29500  18622   4557   2931   8766       C  
ATOM     36  NZ  LYS A  23       8.420   9.869 -63.275  1.00208.32           N  
ANISOU   36  NZ  LYS A  23    29318  30535  19301   4601   2279   8323       N  
ATOM     37  N   ASP A  24       8.882   6.670 -58.657  1.00146.54           N  
ANISOU   37  N   ASP A  24    20556  22072  13052   3575   1927   6569       N  
ATOM     38  CA  ASP A  24       7.759   5.730 -58.795  1.00145.94           C  
ANISOU   38  CA  ASP A  24    20716  22035  12698   3594   1386   6112       C  
ATOM     39  C   ASP A  24       7.217   5.197 -57.457  1.00143.76           C  
ANISOU   39  C   ASP A  24    20145  21526  12952   3245   1098   5713       C  
ATOM     40  O   ASP A  24       6.086   4.704 -57.405  1.00142.99           O  
ANISOU   40  O   ASP A  24    20094  21445  12792   3150    599   5459       O  
ATOM     41  CB  ASP A  24       8.139   4.573 -59.738  1.00151.54           C  
ANISOU   41  CB  ASP A  24    21956  22947  12674   3903   1414   5875       C  
ATOM     42  CG  ASP A  24       8.130   4.928 -61.215  1.00168.24           C  
ANISOU   42  CG  ASP A  24    24513  25333  14079   4284   1482   6172       C  
ATOM     43  OD1 ASP A  24       8.664   6.003 -61.575  1.00170.38           O  
ANISOU   43  OD1 ASP A  24    24627  25689  14422   4406   1870   6698       O  
ATOM     44  OD2 ASP A  24       7.604   4.126 -62.012  1.00178.58           O  
ANISOU   44  OD2 ASP A  24    26369  26751  14732   4434   1134   5889       O  
ATOM     45  N   TYR A  25       8.014   5.308 -56.384  1.00136.33           N  
ANISOU   45  N   TYR A  25    18878  20404  12517   3030   1391   5708       N  
ATOM     46  CA  TYR A  25       7.640   4.866 -55.042  1.00131.36           C  
ANISOU   46  CA  TYR A  25    17973  19556  12380   2720   1194   5374       C  
ATOM     47  C   TYR A  25       7.086   6.022 -54.196  1.00133.28           C  
ANISOU   47  C   TYR A  25    17939  19551  13149   2521   1160   5550       C  
ATOM     48  O   TYR A  25       6.683   5.808 -53.050  1.00129.37           O  
ANISOU   48  O   TYR A  25    17234  18873  13048   2303   1025   5317       O  
ATOM     49  CB  TYR A  25       8.829   4.177 -54.352  1.00130.44           C  
ANISOU   49  CB  TYR A  25    17720  19415  12425   2631   1498   5249       C  
ATOM     50  CG  TYR A  25       9.315   2.944 -55.081  1.00134.54           C  
ANISOU   50  CG  TYR A  25    18595  20108  12414   2928   1584   5048       C  
ATOM     51  CD1 TYR A  25       8.672   1.720 -54.927  1.00135.87           C  
ANISOU   51  CD1 TYR A  25    19014  20190  12421   2901   1233   4580       C  
ATOM     52  CD2 TYR A  25      10.416   3.001 -55.929  1.00139.10           C  
ANISOU   52  CD2 TYR A  25    19309  20913  12630   3256   2041   5355       C  
ATOM     53  CE1 TYR A  25       9.113   0.582 -55.600  1.00139.96           C  
ANISOU   53  CE1 TYR A  25    20025  20757  12395   3206   1326   4364       C  
ATOM     54  CE2 TYR A  25      10.868   1.869 -56.606  1.00143.20           C  
ANISOU   54  CE2 TYR A  25    20263  21551  12594   3643   2196   5174       C  
ATOM     55  CZ  TYR A  25      10.215   0.659 -56.436  1.00149.80           C  
ANISOU   55  CZ  TYR A  25    21461  22211  13245   3624   1833   4648       C  
ATOM     56  OH  TYR A  25      10.657  -0.465 -57.091  1.00154.31           O  
ANISOU   56  OH  TYR A  25    22616  22791  13224   4030   1998   4436       O  
ATOM     57  N   MET A  26       7.044   7.236 -54.777  1.00132.85           N  
ANISOU   57  N   MET A  26    17953  19465  13062   2641   1306   5971       N  
ATOM     58  CA  MET A  26       6.531   8.443 -54.129  1.00132.56           C  
ANISOU   58  CA  MET A  26    17819  19113  13436   2555   1336   6181       C  
ATOM     59  C   MET A  26       5.104   8.681 -54.615  1.00141.66           C  
ANISOU   59  C   MET A  26    18996  20381  14447   2809   1009   6275       C  
ATOM     60  O   MET A  26       4.912   9.155 -55.739  1.00145.42           O  
ANISOU   60  O   MET A  26    19643  21035  14574   3064   1001   6592       O  
ATOM     61  CB  MET A  26       7.409   9.668 -54.462  1.00137.32           C  
ANISOU   61  CB  MET A  26    18527  19546  14100   2514   1715   6648       C  
ATOM     62  CG  MET A  26       8.882   9.447 -54.249  1.00139.83           C  
ANISOU   62  CG  MET A  26    18731  19908  14489   2266   2022   6720       C  
ATOM     63  SD  MET A  26       9.858  10.884 -54.710  1.00147.73           S  
ANISOU   63  SD  MET A  26    19812  20746  15572   2113   2408   7367       S  
ATOM     64  CE  MET A  26      11.435  10.379 -54.153  1.00143.61           C  
ANISOU   64  CE  MET A  26    18958  20384  15224   1744   2655   7437       C  
ATOM     65  N   ILE A  27       4.099   8.308 -53.801  1.00138.43           N  
ANISOU   65  N   ILE A  27    18375  19937  14287   2751    732   6055       N  
ATOM     66  CA  ILE A  27       2.697   8.494 -54.190  1.00142.20           C  
ANISOU   66  CA  ILE A  27    18736  20619  14673   2982    399   6238       C  
ATOM     67  C   ILE A  27       1.951   9.339 -53.152  1.00148.20           C  
ANISOU   67  C   ILE A  27    19315  21098  15894   3080    508   6388       C  
ATOM     68  O   ILE A  27       1.786   8.915 -52.002  1.00144.22           O  
ANISOU   68  O   ILE A  27    18633  20453  15713   2910    499   6120       O  
ATOM     69  CB  ILE A  27       1.951   7.174 -54.548  1.00145.90           C  
ANISOU   69  CB  ILE A  27    19110  21462  14864   2885   -116   5971       C  
ATOM     70  CG1 ILE A  27       2.806   6.249 -55.443  1.00147.16           C  
ANISOU   70  CG1 ILE A  27    19622  21777  14516   2831   -151   5734       C  
ATOM     71  CG2 ILE A  27       0.619   7.487 -55.240  1.00151.46           C  
ANISOU   71  CG2 ILE A  27    19659  22501  15387   3097   -502   6314       C  
ATOM     72  CD1 ILE A  27       2.983   4.880 -54.910  1.00150.97           C  
ANISOU   72  CD1 ILE A  27    20123  22231  15008   2571   -323   5256       C  
ATOM     73  N   LEU A  28       1.531  10.556 -53.571  1.00150.80           N  
ANISOU   73  N   LEU A  28    19751  21324  16220   3410    657   6840       N  
ATOM     74  CA  LEU A  28       0.801  11.528 -52.746  1.00152.76           C  
ANISOU   74  CA  LEU A  28    19969  21253  16820   3666    851   7064       C  
ATOM     75  C   LEU A  28      -0.347  12.163 -53.523  1.00162.34           C  
ANISOU   75  C   LEU A  28    21066  22733  17884   4150    727   7576       C  
ATOM     76  O   LEU A  28      -0.129  13.089 -54.310  1.00165.59           O  
ANISOU   76  O   LEU A  28    21751  23036  18131   4383    907   7948       O  
ATOM     77  CB  LEU A  28       1.702  12.663 -52.205  1.00153.32           C  
ANISOU   77  CB  LEU A  28    20458  20685  17111   3592   1310   7142       C  
ATOM     78  CG  LEU A  28       3.185  12.421 -51.975  1.00155.96           C  
ANISOU   78  CG  LEU A  28    20958  20822  17478   3113   1468   6890       C  
ATOM     79  CD1 LEU A  28       3.975  13.682 -52.279  1.00159.56           C  
ANISOU   79  CD1 LEU A  28    21822  20847  17958   3060   1797   7234       C  
ATOM     80  CD2 LEU A  28       3.446  11.904 -50.561  1.00154.96           C  
ANISOU   80  CD2 LEU A  28    20745  20472  17659   2794   1482   6470       C  
ATOM     81  N   SER A  29      -1.568  11.693 -53.282  1.00160.08           N  
ANISOU   81  N   SER A  29    20339  22816  17670   4299    427   7661       N  
ATOM     82  CA  SER A  29      -2.755  12.248 -53.913  1.00165.68           C  
ANISOU   82  CA  SER A  29    20799  23879  18273   4776    277   8231       C  
ATOM     83  C   SER A  29      -3.216  13.491 -53.137  1.00171.21           C  
ANISOU   83  C   SER A  29    21614  24137  19300   5284    753   8574       C  
ATOM     84  O   SER A  29      -4.140  13.416 -52.322  1.00172.03           O  
ANISOU   84  O   SER A  29    21363  24343  19657   5521    781   8689       O  
ATOM     85  CB  SER A  29      -3.855  11.195 -54.017  1.00171.06           C  
ANISOU   85  CB  SER A  29    20892  25210  18892   4660   -288   8266       C  
ATOM     86  OG  SER A  29      -3.501  10.205 -54.967  1.00180.88           O  
ANISOU   86  OG  SER A  29    22221  26796  19708   4270   -744   8009       O  
ATOM     87  N   GLY A  30      -2.519  14.603 -53.376  1.00168.18           N  
ANISOU   87  N   GLY A  30    21779  23229  18892   5440   1151   8736       N  
ATOM     88  CA  GLY A  30      -2.786  15.914 -52.790  1.00170.81           C  
ANISOU   88  CA  GLY A  30    22483  22970  19446   5930   1645   9049       C  
ATOM     89  C   GLY A  30      -2.696  16.022 -51.277  1.00170.31           C  
ANISOU   89  C   GLY A  30    22622  22368  19719   5881   1957   8715       C  
ATOM     90  O   GLY A  30      -1.594  15.955 -50.725  1.00165.43           O  
ANISOU   90  O   GLY A  30    22380  21292  19184   5383   2078   8279       O  
ATOM     91  N   PRO A  31      -3.857  16.201 -50.581  1.00168.70           N  
ANISOU   91  N   PRO A  31    22162  22248  19687   6419   2100   8962       N  
ATOM     92  CA  PRO A  31      -3.841  16.377 -49.111  1.00166.48           C  
ANISOU   92  CA  PRO A  31    22170  21430  19653   6477   2456   8670       C  
ATOM     93  C   PRO A  31      -3.190  15.271 -48.273  1.00161.14           C  
ANISOU   93  C   PRO A  31    21353  20784  19088   5807   2266   8030       C  
ATOM     94  O   PRO A  31      -2.865  15.533 -47.112  1.00159.22           O  
ANISOU   94  O   PRO A  31    21530  19987  18980   5747   2559   7735       O  
ATOM     95  CB  PRO A  31      -5.324  16.529 -48.756  1.00173.18           C  
ANISOU   95  CB  PRO A  31    22559  22635  20608   7234   2597   9160       C  
ATOM     96  CG  PRO A  31      -5.958  17.040 -49.999  1.00183.43           C  
ANISOU   96  CG  PRO A  31    23623  24338  21735   7700   2487   9810       C  
ATOM     97  CD  PRO A  31      -5.231  16.341 -51.109  1.00175.70           C  
ANISOU   97  CD  PRO A  31    22497  23737  20525   7055   1984   9599       C  
ATOM     98  N   GLN A  32      -2.981  14.061 -48.840  1.00152.29           N  
ANISOU   98  N   GLN A  32    19730  20260  17874   5323   1788   7815       N  
ATOM     99  CA  GLN A  32      -2.336  12.964 -48.110  1.00145.43           C  
ANISOU   99  CA  GLN A  32    18739  19420  17100   4730   1618   7246       C  
ATOM    100  C   GLN A  32      -0.829  13.212 -47.902  1.00144.90           C  
ANISOU  100  C   GLN A  32    19227  18811  17016   4234   1768   6877       C  
ATOM    101  O   GLN A  32      -0.228  12.581 -47.035  1.00140.05           O  
ANISOU  101  O   GLN A  32    18623  18075  16514   3824   1743   6452       O  
ATOM    102  CB  GLN A  32      -2.629  11.578 -48.717  1.00144.50           C  
ANISOU  102  CB  GLN A  32    18021  20014  16868   4406   1084   7134       C  
ATOM    103  CG  GLN A  32      -2.318  11.422 -50.196  1.00155.18           C  
ANISOU  103  CG  GLN A  32    19384  21693  17884   4289    788   7258       C  
ATOM    104  CD  GLN A  32      -2.502   9.999 -50.673  1.00167.92           C  
ANISOU  104  CD  GLN A  32    20616  23859  19327   3906    257   7035       C  
ATOM    105  OE1 GLN A  32      -1.534   9.280 -50.936  1.00160.43           O  
ANISOU  105  OE1 GLN A  32    19859  22876  18221   3501    151   6647       O  
ATOM    106  NE2 GLN A  32      -3.746   9.561 -50.812  1.00159.82           N  
ANISOU  106  NE2 GLN A  32    19064  23348  18312   4025    -91   7314       N  
ATOM    107  N   LYS A  33      -0.241  14.164 -48.656  1.00143.50           N  
ANISOU  107  N   LYS A  33    19481  18327  16714   4272   1926   7106       N  
ATOM    108  CA  LYS A  33       1.160  14.571 -48.518  1.00141.60           C  
ANISOU  108  CA  LYS A  33    19723  17596  16482   3783   2072   6912       C  
ATOM    109  C   LYS A  33       1.303  15.426 -47.260  1.00145.81           C  
ANISOU  109  C   LYS A  33    20836  17375  17189   3784   2390   6785       C  
ATOM    110  O   LYS A  33       2.258  15.247 -46.508  1.00142.53           O  
ANISOU  110  O   LYS A  33    20625  16676  16853   3251   2383   6444       O  
ATOM    111  CB  LYS A  33       1.623  15.369 -49.746  1.00147.75           C  
ANISOU  111  CB  LYS A  33    20762  18301  17075   3839   2152   7296       C  
ATOM    112  N   THR A  34       0.342  16.344 -47.026  1.00146.77           N  
ANISOU  112  N   THR A  34    21254  17179  17335   4411   2668   7080       N  
ATOM    113  CA  THR A  34       0.327  17.219 -45.853  1.00149.23           C  
ANISOU  113  CA  THR A  34    22284  16696  17720   4544   3013   6964       C  
ATOM    114  C   THR A  34      -0.228  16.471 -44.627  1.00150.28           C  
ANISOU  114  C   THR A  34    22168  16979  17953   4636   3024   6651       C  
ATOM    115  O   THR A  34       0.008  16.903 -43.497  1.00151.12           O  
ANISOU  115  O   THR A  34    22880  16473  18065   4569   3239   6397       O  
ATOM    116  CB  THR A  34      -0.377  18.557 -46.150  1.00164.20           C  
ANISOU  116  CB  THR A  34    24730  18106  19553   5255   3387   7436       C  
ATOM    117  OG1 THR A  34      -0.234  18.889 -47.534  1.00164.85           O  
ANISOU  117  OG1 THR A  34    24690  18415  19530   5312   3298   7837       O  
ATOM    118  CG2 THR A  34       0.162  19.701 -45.296  1.00166.96           C  
ANISOU  118  CG2 THR A  34    26176  17381  19882   5148   3709   7295       C  
ATOM    119  N   ALA A  35      -0.937  15.336 -44.853  1.00143.57           N  
ANISOU  119  N   ALA A  35    20470  16927  17152   4739   2768   6675       N  
ATOM    120  CA  ALA A  35      -1.483  14.478 -43.791  1.00140.65           C  
ANISOU  120  CA  ALA A  35    19735  16810  16895   4778   2746   6445       C  
ATOM    121  C   ALA A  35      -0.351  13.699 -43.113  1.00138.86           C  
ANISOU  121  C   ALA A  35    19556  16498  16708   4029   2553   5909       C  
ATOM    122  O   ALA A  35      -0.344  13.585 -41.887  1.00137.37           O  
ANISOU  122  O   ALA A  35    19585  16051  16560   3988   2691   5644       O  
ATOM    123  CB  ALA A  35      -2.520  13.520 -44.358  1.00140.69           C  
ANISOU  123  CB  ALA A  35    18835  17672  16947   4986   2460   6696       C  
ATOM    124  N   VAL A  36       0.614  13.183 -43.911  1.00132.65           N  
ANISOU  124  N   VAL A  36    18581  15944  15876   3491   2263   5789       N  
ATOM    125  CA  VAL A  36       1.804  12.472 -43.425  1.00128.19           C  
ANISOU  125  CA  VAL A  36    18005  15359  15342   2819   2094   5384       C  
ATOM    126  C   VAL A  36       2.700  13.509 -42.736  1.00135.40           C  
ANISOU  126  C   VAL A  36    19678  15529  16240   2520   2284   5276       C  
ATOM    127  O   VAL A  36       3.198  13.256 -41.645  1.00133.22           O  
ANISOU  127  O   VAL A  36    19575  15046  15995   2177   2261   4959       O  
ATOM    128  CB  VAL A  36       2.542  11.698 -44.560  1.00129.07           C  
ANISOU  128  CB  VAL A  36    17732  15942  15367   2474   1818   5380       C  
ATOM    129  CG1 VAL A  36       3.876  11.124 -44.082  1.00125.37           C  
ANISOU  129  CG1 VAL A  36    17265  15439  14931   1862   1724   5076       C  
ATOM    130  CG2 VAL A  36       1.666  10.586 -45.126  1.00127.35           C  
ANISOU  130  CG2 VAL A  36    16903  16375  15111   2661   1551   5409       C  
ATOM    131  N   ALA A  37       2.835  14.701 -43.348  1.00137.57           N  
ANISOU  131  N   ALA A  37    20445  15378  16446   2647   2452   5565       N  
ATOM    132  CA  ALA A  37       3.618  15.825 -42.832  1.00141.66           C  
ANISOU  132  CA  ALA A  37    21798  15097  16930   2315   2593   5526       C  
ATOM    133  C   ALA A  37       3.170  16.284 -41.440  1.00148.79           C  
ANISOU  133  C   ALA A  37    23330  15416  17787   2514   2805   5292       C  
ATOM    134  O   ALA A  37       4.014  16.678 -40.637  1.00150.10           O  
ANISOU  134  O   ALA A  37    24081  15049  17899   1980   2754   5056       O  
ATOM    135  CB  ALA A  37       3.554  16.994 -43.802  1.00147.57           C  
ANISOU  135  CB  ALA A  37    22966  15489  17613   2553   2768   5945       C  
ATOM    136  N   VAL A  38       1.856  16.241 -41.153  1.00146.68           N  
ANISOU  136  N   VAL A  38    22950  15271  17512   3276   3039   5392       N  
ATOM    137  CA  VAL A  38       1.345  16.673 -39.856  1.00149.74           C  
ANISOU  137  CA  VAL A  38    23965  15132  17796   3617   3334   5212       C  
ATOM    138  C   VAL A  38       1.401  15.521 -38.826  1.00149.61           C  
ANISOU  138  C   VAL A  38    23535  15491  17818   3364   3181   4844       C  
ATOM    139  O   VAL A  38       1.741  15.775 -37.672  1.00150.71           O  
ANISOU  139  O   VAL A  38    24315  15129  17817   3169   3255   4536       O  
ATOM    140  CB  VAL A  38      -0.046  17.373 -39.951  1.00158.89           C  
ANISOU  140  CB  VAL A  38    25303  16165  18902   4653   3775   5595       C  
ATOM    141  CG1 VAL A  38      -1.179  16.402 -40.286  1.00156.22           C  
ANISOU  141  CG1 VAL A  38    23901  16751  18705   5144   3729   5851       C  
ATOM    142  CG2 VAL A  38      -0.359  18.181 -38.695  1.00164.14           C  
ANISOU  142  CG2 VAL A  38    26979  16027  19361   5050   4189   5431       C  
ATOM    143  N   LEU A  39       1.122  14.269 -39.248  1.00141.55           N  
ANISOU  143  N   LEU A  39    21528  15303  16951   3320   2943   4871       N  
ATOM    144  CA  LEU A  39       1.118  13.106 -38.355  1.00137.32           C  
ANISOU  144  CA  LEU A  39    20558  15143  16474   3106   2803   4581       C  
ATOM    145  C   LEU A  39       2.512  12.557 -38.053  1.00137.41           C  
ANISOU  145  C   LEU A  39    20564  15155  16490   2268   2485   4246       C  
ATOM    146  O   LEU A  39       2.900  12.517 -36.887  1.00136.93           O  
ANISOU  146  O   LEU A  39    20876  14811  16339   2019   2491   3961       O  
ATOM    147  CB  LEU A  39       0.192  11.990 -38.880  1.00134.63           C  
ANISOU  147  CB  LEU A  39    19251  15615  16289   3373   2663   4769       C  
ATOM    148  CG  LEU A  39      -1.317  12.258 -38.845  1.00143.60           C  
ANISOU  148  CG  LEU A  39    20162  16945  17455   4193   2953   5160       C  
ATOM    149  CD1 LEU A  39      -2.038  11.423 -39.884  1.00142.53           C  
ANISOU  149  CD1 LEU A  39    19118  17587  17449   4277   2666   5459       C  
ATOM    150  CD2 LEU A  39      -1.903  11.985 -37.464  1.00147.12           C  
ANISOU  150  CD2 LEU A  39    20666  17350  17885   4479   3215   5058       C  
ATOM    151  N   CYS A  40       3.255  12.141 -39.097  1.00131.59           N  
ANISOU  151  N   CYS A  40    19407  14764  15828   1880   2225   4320       N  
ATOM    152  CA  CYS A  40       4.595  11.552 -39.012  1.00128.65           C  
ANISOU  152  CA  CYS A  40    18865  14535  15480   1171   1955   4135       C  
ATOM    153  C   CYS A  40       5.623  12.452 -38.323  1.00136.05           C  
ANISOU  153  C   CYS A  40    20508  14862  16323    640   1928   4029       C  
ATOM    154  O   CYS A  40       6.469  11.939 -37.595  1.00134.31           O  
ANISOU  154  O   CYS A  40    20210  14722  16098    128   1731   3830       O  
ATOM    155  CB  CYS A  40       5.076  11.105 -40.388  1.00127.15           C  
ANISOU  155  CB  CYS A  40    18179  14802  15329   1037   1797   4326       C  
ATOM    156  SG  CYS A  40       6.510  10.001 -40.360  1.00127.39           S  
ANISOU  156  SG  CYS A  40    17762  15241  15400    405   1543   4183       S  
ATOM    157  N   THR A  41       5.554  13.775 -38.540  1.00137.92           N  
ANISOU  157  N   THR A  41    21447  14483  16471    733   2095   4185       N  
ATOM    158  CA  THR A  41       6.489  14.717 -37.917  1.00142.28           C  
ANISOU  158  CA  THR A  41    22792  14359  16907    139   2011   4101       C  
ATOM    159  C   THR A  41       6.161  14.907 -36.433  1.00148.86           C  
ANISOU  159  C   THR A  41    24282  14729  17551    202   2089   3764       C  
ATOM    160  O   THR A  41       7.078  14.987 -35.614  1.00149.65           O  
ANISOU  160  O   THR A  41    24731  14586  17544   -467   1842   3567       O  
ATOM    161  CB  THR A  41       6.553  16.037 -38.700  1.00155.29           C  
ANISOU  161  CB  THR A  41    25045  15442  18517    177   2152   4397       C  
ATOM    162  OG1 THR A  41       6.527  15.758 -40.101  1.00152.07           O  
ANISOU  162  OG1 THR A  41    23986  15561  18233    355   2155   4724       O  
ATOM    163  CG2 THR A  41       7.793  16.861 -38.367  1.00158.89           C  
ANISOU  163  CG2 THR A  41    26143  15321  18906   -692   1932   4404       C  
ATOM    164  N   LEU A  42       4.861  14.960 -36.090  1.00147.05           N  
ANISOU  164  N   LEU A  42    24191  14428  17254   1012   2428   3740       N  
ATOM    165  CA  LEU A  42       4.401  15.124 -34.713  1.00150.04           C  
ANISOU  165  CA  LEU A  42    25211  14402  17397   1251   2608   3459       C  
ATOM    166  C   LEU A  42       4.633  13.847 -33.890  1.00151.19           C  
ANISOU  166  C   LEU A  42    24772  15098  17575    987   2402   3214       C  
ATOM    167  O   LEU A  42       5.193  13.934 -32.796  1.00152.72           O  
ANISOU  167  O   LEU A  42    25503  14972  17551    575   2267   2933       O  
ATOM    168  CB  LEU A  42       2.921  15.544 -34.682  1.00152.99           C  
ANISOU  168  CB  LEU A  42    25784  14640  17705   2296   3109   3635       C  
ATOM    169  CG  LEU A  42       2.393  16.133 -33.377  1.00162.87           C  
ANISOU  169  CG  LEU A  42    28016  15252  18615   2729   3456   3420       C  
ATOM    170  CD1 LEU A  42       2.674  17.626 -33.292  1.00170.77           C  
ANISOU  170  CD1 LEU A  42    30352  15191  19343   2699   3608   3384       C  
ATOM    171  CD2 LEU A  42       0.906  15.895 -33.249  1.00165.92           C  
ANISOU  171  CD2 LEU A  42    28033  15979  19030   3779   3927   3668       C  
ATOM    172  N   LEU A  43       4.224  12.671 -34.423  1.00143.53           N  
ANISOU  172  N   LEU A  43    22763  14922  16849   1192   2347   3328       N  
ATOM    173  CA  LEU A  43       4.373  11.366 -33.762  1.00139.24           C  
ANISOU  173  CA  LEU A  43    21620  14912  16373    996   2174   3150       C  
ATOM    174  C   LEU A  43       5.830  10.940 -33.603  1.00141.57           C  
ANISOU  174  C   LEU A  43    21766  15340  16684    156   1777   3022       C  
ATOM    175  O   LEU A  43       6.178  10.361 -32.578  1.00140.07           O  
ANISOU  175  O   LEU A  43    21569  15246  16403   -100   1648   2816       O  
ATOM    176  CB  LEU A  43       3.582  10.266 -34.490  1.00135.06           C  
ANISOU  176  CB  LEU A  43    20126  15103  16089   1362   2177   3327       C  
ATOM    177  CG  LEU A  43       2.063  10.303 -34.373  1.00141.98           C  
ANISOU  177  CG  LEU A  43    20864  16094  16989   2152   2514   3518       C  
ATOM    178  CD1 LEU A  43       1.415   9.717 -35.611  1.00140.16           C  
ANISOU  178  CD1 LEU A  43    19839  16439  16975   2379   2415   3806       C  
ATOM    179  CD2 LEU A  43       1.586   9.564 -33.129  1.00143.93           C  
ANISOU  179  CD2 LEU A  43    20988  16510  17188   2306   2624   3383       C  
ATOM    180  N   GLY A  44       6.650  11.227 -34.613  1.00138.69           N  
ANISOU  180  N   GLY A  44    21245  15026  16425   -225   1610   3206       N  
ATOM    181  CA  GLY A  44       8.074  10.902 -34.635  1.00138.04           C  
ANISOU  181  CA  GLY A  44    20907  15155  16387   -982   1271   3232       C  
ATOM    182  C   GLY A  44       8.903  11.686 -33.638  1.00147.57           C  
ANISOU  182  C   GLY A  44    22853  15834  17381  -1611   1066   3101       C  
ATOM    183  O   GLY A  44       9.884  11.163 -33.101  1.00146.60           O  
ANISOU  183  O   GLY A  44    22474  15977  17249  -2185    763   3073       O  
ATOM    184  N   LEU A  45       8.520  12.953 -33.394  1.00150.27           N  
ANISOU  184  N   LEU A  45    24159  15411  17528  -1513   1212   3044       N  
ATOM    185  CA  LEU A  45       9.188  13.838 -32.440  1.00156.42           C  
ANISOU  185  CA  LEU A  45    25888  15523  18022  -2130    990   2878       C  
ATOM    186  C   LEU A  45       8.725  13.508 -31.017  1.00162.31           C  
ANISOU  186  C   LEU A  45    27055  16133  18482  -1934   1038   2520       C  
ATOM    187  O   LEU A  45       9.528  13.565 -30.083  1.00164.53           O  
ANISOU  187  O   LEU A  45    27715  16258  18540  -2592    691   2359       O  
ATOM    188  CB  LEU A  45       8.899  15.309 -32.780  1.00162.64           C  
ANISOU  188  CB  LEU A  45    27681  15445  18672  -2031   1170   2945       C  
ATOM    189  CG  LEU A  45       9.865  16.339 -32.209  1.00174.36           C  
ANISOU  189  CG  LEU A  45    30146  16192  19910  -2922    822   2877       C  
ATOM    190  CD1 LEU A  45      11.117  16.456 -33.067  1.00175.02           C  
ANISOU  190  CD1 LEU A  45    29705  16554  20242  -3762    467   3261       C  
ATOM    191  CD2 LEU A  45       9.197  17.687 -32.093  1.00183.66           C  
ANISOU  191  CD2 LEU A  45    32632  16329  20821  -2564   1116   2784       C  
ATOM    192  N   LEU A  46       7.434  13.152 -30.863  1.00158.07           N  
ANISOU  192  N   LEU A  46    26411  15707  17942  -1043   1454   2448       N  
ATOM    193  CA  LEU A  46       6.834  12.775 -29.584  1.00159.08           C  
ANISOU  193  CA  LEU A  46    26851  15787  17807   -700   1609   2182       C  
ATOM    194  C   LEU A  46       7.311  11.389 -29.140  1.00158.85           C  
ANISOU  194  C   LEU A  46    25958  16496  17903   -997   1348   2137       C  
ATOM    195  O   LEU A  46       7.408  11.145 -27.938  1.00160.06           O  
ANISOU  195  O   LEU A  46    26460  16581  17775  -1114   1273   1914       O  
ATOM    196  CB  LEU A  46       5.302  12.813 -29.674  1.00159.19           C  
ANISOU  196  CB  LEU A  46    26852  15798  17836    356   2164   2263       C  
ATOM    197  CG  LEU A  46       4.559  13.043 -28.363  1.00168.30           C  
ANISOU  197  CG  LEU A  46    28782  16575  18588    867   2498   2043       C  
ATOM    198  CD1 LEU A  46       4.412  14.531 -28.066  1.00176.92           C  
ANISOU  198  CD1 LEU A  46    31281  16656  19285   1054   2725   1923       C  
ATOM    199  CD2 LEU A  46       3.197  12.397 -28.401  1.00168.58           C  
ANISOU  199  CD2 LEU A  46    28169  17099  18785   1783   2947   2248       C  
ATOM    200  N   SER A  47       7.605  10.488 -30.105  1.00150.60           N  
ANISOU  200  N   SER A  47    23862  16123  17235  -1081   1229   2355       N  
ATOM    201  CA  SER A  47       8.102   9.134 -29.837  1.00146.06           C  
ANISOU  201  CA  SER A  47    22473  16220  16804  -1309   1014   2360       C  
ATOM    202  C   SER A  47       9.538   9.194 -29.310  1.00152.64           C  
ANISOU  202  C   SER A  47    23407  17073  17516  -2172    563   2352       C  
ATOM    203  O   SER A  47       9.867   8.483 -28.360  1.00151.71           O  
ANISOU  203  O   SER A  47    23152  17209  17284  -2362    396   2250       O  
ATOM    204  CB  SER A  47       8.034   8.273 -31.095  1.00144.68           C  
ANISOU  204  CB  SER A  47    21349  16631  16992  -1122   1037   2585       C  
ATOM    205  OG  SER A  47       8.326   6.912 -30.822  1.00149.83           O  
ANISOU  205  OG  SER A  47    21314  17848  17765  -1194    911   2579       O  
ATOM    206  N   ALA A  48      10.375  10.068 -29.904  1.00152.73           N  
ANISOU  206  N   ALA A  48    23650  16834  17548  -2710    355   2513       N  
ATOM    207  CA  ALA A  48      11.767  10.275 -29.502  1.00156.38           C  
ANISOU  207  CA  ALA A  48    24161  17339  17919  -3628   -122   2621       C  
ATOM    208  C   ALA A  48      11.860  11.036 -28.166  1.00167.57           C  
ANISOU  208  C   ALA A  48    26657  18133  18879  -4011   -333   2329       C  
ATOM    209  O   ALA A  48      12.910  11.009 -27.521  1.00170.46           O  
ANISOU  209  O   ALA A  48    27052  18614  19099  -4786   -802   2384       O  
ATOM    210  CB  ALA A  48      12.517  11.021 -30.593  1.00159.57           C  
ANISOU  210  CB  ALA A  48    24474  17658  18498  -4074   -244   2952       C  
ATOM    211  N   LEU A  49      10.754  11.698 -27.755  1.00167.14           N  
ANISOU  211  N   LEU A  49    27498  17441  18566  -3436     19   2049       N  
ATOM    212  CA  LEU A  49      10.621  12.458 -26.506  1.00173.83           C  
ANISOU  212  CA  LEU A  49    29588  17581  18880  -3591    -58   1711       C  
ATOM    213  C   LEU A  49      10.432  11.505 -25.308  1.00176.25           C  
ANISOU  213  C   LEU A  49    29753  18251  18961  -3419    -79   1513       C  
ATOM    214  O   LEU A  49      10.987  11.751 -24.235  1.00180.44           O  
ANISOU  214  O   LEU A  49    30961  18533  19065  -3961   -434   1323       O  
ATOM    215  CB  LEU A  49       9.428  13.429 -26.627  1.00177.18           C  
ANISOU  215  CB  LEU A  49    30945  17252  19124  -2820    465   1560       C  
ATOM    216  CG  LEU A  49       9.230  14.450 -25.508  1.00190.40           C  
ANISOU  216  CG  LEU A  49    34180  17987  20176  -2863    486   1201       C  
ATOM    217  CD1 LEU A  49       9.038  15.839 -26.076  1.00196.62           C  
ANISOU  217  CD1 LEU A  49    35967  17873  20867  -2810    648   1217       C  
ATOM    218  CD2 LEU A  49       8.044  14.080 -24.635  1.00192.57           C  
ANISOU  218  CD2 LEU A  49    34739  18253  20174  -1910   1000    988       C  
ATOM    219  N   GLU A  50       9.635  10.436 -25.497  1.00167.08           N  
ANISOU  219  N   GLU A  50    27756  17661  18066  -2699    279   1577       N  
ATOM    220  CA  GLU A  50       9.335   9.429 -24.475  1.00165.13           C  
ANISOU  220  CA  GLU A  50    27260  17806  17676  -2445    337   1463       C  
ATOM    221  C   GLU A  50      10.488   8.445 -24.295  1.00167.14           C  
ANISOU  221  C   GLU A  50    26702  18729  18074  -3077   -129   1627       C  
ATOM    222  O   GLU A  50      10.804   8.090 -23.160  1.00168.69           O  
ANISOU  222  O   GLU A  50    27116  19027  17952  -3310   -344   1510       O  
ATOM    223  CB  GLU A  50       8.039   8.674 -24.813  1.00161.45           C  
ANISOU  223  CB  GLU A  50    26185  17679  17480  -1516    866   1544       C  
ATOM    224  CG  GLU A  50       6.785   9.534 -24.757  1.00175.89           C  
ANISOU  224  CG  GLU A  50    28745  18963  19123   -745   1394   1459       C  
ATOM    225  CD  GLU A  50       5.767   9.293 -25.856  1.00193.68           C  
ANISOU  225  CD  GLU A  50    30307  21490  21795    -69   1775   1711       C  
ATOM    226  OE1 GLU A  50       6.117   8.653 -26.874  1.00184.09           O  
ANISOU  226  OE1 GLU A  50    28194  20758  20995   -274   1593   1904       O  
ATOM    227  OE2 GLU A  50       4.616   9.763 -25.704  1.00190.80           O  
ANISOU  227  OE2 GLU A  50    30322  20864  21309    688   2259   1742       O  
ATOM    228  N   ASN A  51      11.103   7.997 -25.413  1.00160.41           N  
ANISOU  228  N   ASN A  51    24930  18348  17669  -3288   -254   1930       N  
ATOM    229  CA  ASN A  51      12.228   7.056 -25.424  1.00158.53           C  
ANISOU  229  CA  ASN A  51    23833  18790  17613  -3766   -613   2186       C  
ATOM    230  C   ASN A  51      13.433   7.597 -24.667  1.00169.33           C  
ANISOU  230  C   ASN A  51    25592  20070  18676  -4689  -1184   2238       C  
ATOM    231  O   ASN A  51      14.062   6.847 -23.919  1.00169.41           O  
ANISOU  231  O   ASN A  51    25239  20537  18591  -4967  -1467   2334       O  
ATOM    232  CB  ASN A  51      12.619   6.687 -26.853  1.00155.43           C  
ANISOU  232  CB  ASN A  51    22569  18809  17678  -3727   -552   2509       C  
ATOM    233  CG  ASN A  51      11.600   5.852 -27.582  1.00171.45           C  
ANISOU  233  CG  ASN A  51    24068  21080  19995  -2946   -128   2499       C  
ATOM    234  OD1 ASN A  51      11.019   4.908 -27.037  1.00162.86           O  
ANISOU  234  OD1 ASN A  51    22741  20222  18915  -2558     20   2405       O  
ATOM    235  ND2 ASN A  51      11.375   6.172 -28.844  1.00161.98           N  
ANISOU  235  ND2 ASN A  51    22679  19840  19026  -2746     41   2626       N  
ATOM    236  N   VAL A  52      13.733   8.901 -24.837  1.00171.76           N  
ANISOU  236  N   VAL A  52    26670  19776  18815  -5187  -1377   2199       N  
ATOM    237  CA  VAL A  52      14.833   9.574 -24.149  1.00179.14           C  
ANISOU  237  CA  VAL A  52    28109  20527  19429  -6202  -2001   2256       C  
ATOM    238  C   VAL A  52      14.495   9.751 -22.649  1.00187.60           C  
ANISOU  238  C   VAL A  52    30184  21203  19892  -6240  -2134   1853       C  
ATOM    239  O   VAL A  52      15.399   9.722 -21.813  1.00192.13           O  
ANISOU  239  O   VAL A  52    30885  21944  20173  -7000  -2705   1917       O  
ATOM    240  CB  VAL A  52      15.278  10.881 -24.868  1.00188.47           C  
ANISOU  240  CB  VAL A  52    29814  21153  20644  -6792  -2189   2382       C  
ATOM    241  CG1 VAL A  52      14.312  12.041 -24.627  1.00192.34           C  
ANISOU  241  CG1 VAL A  52    31695  20606  20779  -6471  -1914   1964       C  
ATOM    242  CG2 VAL A  52      16.707  11.265 -24.495  1.00195.39           C  
ANISOU  242  CG2 VAL A  52    30672  22176  21393  -8014  -2936   2683       C  
ATOM    243  N   ALA A  53      13.185   9.862 -22.317  1.00182.72           N  
ANISOU  243  N   ALA A  53    30204  20144  19075  -5377  -1591   1492       N  
ATOM    244  CA  ALA A  53      12.685   9.985 -20.943  1.00186.56           C  
ANISOU  244  CA  ALA A  53    31675  20260  18949  -5184  -1551   1114       C  
ATOM    245  C   ALA A  53      12.705   8.626 -20.216  1.00185.89           C  
ANISOU  245  C   ALA A  53    30836  20923  18873  -4953  -1556   1191       C  
ATOM    246  O   ALA A  53      12.504   8.573 -19.000  1.00188.89           O  
ANISOU  246  O   ALA A  53    31898  21153  18719  -4898  -1606    950       O  
ATOM    247  CB  ALA A  53      11.277  10.569 -20.947  1.00187.80           C  
ANISOU  247  CB  ALA A  53    32649  19770  18937  -4239   -876    827       C  
ATOM    248  N   VAL A  54      12.966   7.536 -20.968  1.00175.36           N  
ANISOU  248  N   VAL A  54    28165  20357  18108  -4804  -1493   1535       N  
ATOM    249  CA  VAL A  54      13.055   6.160 -20.476  1.00170.97           C  
ANISOU  249  CA  VAL A  54    26789  20513  17660  -4577  -1481   1684       C  
ATOM    250  C   VAL A  54      14.529   5.709 -20.435  1.00175.81           C  
ANISOU  250  C   VAL A  54    26687  21738  18375  -5376  -2085   2059       C  
ATOM    251  O   VAL A  54      14.960   5.153 -19.424  1.00177.76           O  
ANISOU  251  O   VAL A  54    26882  22318  18342  -5595  -2372   2109       O  
ATOM    252  CB  VAL A  54      12.136   5.203 -21.292  1.00167.03           C  
ANISOU  252  CB  VAL A  54    25442  20349  17672  -3731   -919   1787       C  
ATOM    253  CG1 VAL A  54      12.432   3.733 -20.996  1.00162.94           C  
ANISOU  253  CG1 VAL A  54    24014  20546  17350  -3603   -955   2014       C  
ATOM    254  CG2 VAL A  54      10.662   5.511 -21.035  1.00166.63           C  
ANISOU  254  CG2 VAL A  54    25996  19853  17465  -2939   -354   1519       C  
ATOM    255  N   LEU A  55      15.293   5.968 -21.522  1.00171.32           N  
ANISOU  255  N   LEU A  55    25557  21350  18188  -5776  -2256   2376       N  
ATOM    256  CA  LEU A  55      16.715   5.624 -21.659  1.00173.17           C  
ANISOU  256  CA  LEU A  55    24987  22231  18580  -6485  -2765   2864       C  
ATOM    257  C   LEU A  55      17.590   6.221 -20.560  1.00184.38           C  
ANISOU  257  C   LEU A  55    26986  23575  19495  -7433  -3469   2888       C  
ATOM    258  O   LEU A  55      18.506   5.553 -20.078  1.00185.70           O  
ANISOU  258  O   LEU A  55    26506  24412  19640  -7816  -3867   3250       O  
ATOM    259  CB  LEU A  55      17.244   6.066 -23.028  1.00172.98           C  
ANISOU  259  CB  LEU A  55    24458  22286  18981  -6716  -2749   3193       C  
ATOM    260  CG  LEU A  55      17.117   5.059 -24.156  1.00170.96           C  
ANISOU  260  CG  LEU A  55    23160  22549  19247  -6053  -2305   3447       C  
ATOM    261  CD1 LEU A  55      16.922   5.762 -25.484  1.00169.93           C  
ANISOU  261  CD1 LEU A  55    23030  22141  19394  -5954  -2060   3509       C  
ATOM    262  CD2 LEU A  55      18.328   4.141 -24.207  1.00174.27           C  
ANISOU  262  CD2 LEU A  55    22524  23828  19862  -6297  -2547   3999       C  
ATOM    263  N   TYR A  56      17.316   7.481 -20.178  1.00186.52           N  
ANISOU  263  N   TYR A  56    28513  23019  19339  -7813  -3639   2524       N  
ATOM    264  CA  TYR A  56      18.044   8.174 -19.120  1.00195.58           C  
ANISOU  264  CA  TYR A  56    30478  23930  19903  -8782  -4361   2459       C  
ATOM    265  C   TYR A  56      17.573   7.675 -17.754  1.00198.84           C  
ANISOU  265  C   TYR A  56    31284  24365  19903  -8259  -4255   2070       C  
ATOM    266  O   TYR A  56      18.408   7.487 -16.874  1.00199.51           O  
ANISOU  266  O   TYR A  56    30887  24867  20050  -8258  -4548   2009       O  
ATOM    267  CB  TYR A  56      17.870   9.701 -19.242  1.00198.29           C  
ANISOU  267  CB  TYR A  56    31496  23395  20451  -8472  -4123   1913       C  
ATOM    268  CG  TYR A  56      18.694  10.501 -18.255  1.00201.56           C  
ANISOU  268  CG  TYR A  56    31676  23758  21151  -8242  -4262   1422       C  
ATOM    269  CD1 TYR A  56      20.031  10.795 -18.508  1.00203.43           C  
ANISOU  269  CD1 TYR A  56    30899  24364  22030  -8452  -4458   1539       C  
ATOM    270  CD2 TYR A  56      18.129  10.992 -17.081  1.00203.90           C  
ANISOU  270  CD2 TYR A  56    32653  23677  21145  -7682  -4103    796       C  
ATOM    271  CE1 TYR A  56      20.793  11.536 -17.605  1.00206.73           C  
ANISOU  271  CE1 TYR A  56    31088  24734  22727  -8244  -4566   1027       C  
ATOM    272  CE2 TYR A  56      18.881  11.731 -16.169  1.00207.04           C  
ANISOU  272  CE2 TYR A  56    32732  24122  21811  -7497  -4253    325       C  
ATOM    273  CZ  TYR A  56      20.213  12.004 -16.437  1.00212.94           C  
ANISOU  273  CZ  TYR A  56    32241  25271  23398  -7454  -4317    314       C  
ATOM    274  OH  TYR A  56      20.958  12.738 -15.545  1.00215.67           O  
ANISOU  274  OH  TYR A  56    32312  25642  23990  -7315  -4466   -193       O  
ATOM    275  N   LEU A  57      16.244   7.452 -17.591  1.00192.23           N  
ANISOU  275  N   LEU A  57    31035  23148  18855  -7448  -3656   1738       N  
ATOM    276  CA  LEU A  57      15.576   6.987 -16.364  1.00192.95           C  
ANISOU  276  CA  LEU A  57    31677  23195  18439  -6957  -3469   1439       C  
ATOM    277  C   LEU A  57      16.174   5.700 -15.774  1.00195.20           C  
ANISOU  277  C   LEU A  57    31005  24384  18779  -7011  -3708   1784       C  
ATOM    278  O   LEU A  57      16.297   5.600 -14.551  1.00199.81           O  
ANISOU  278  O   LEU A  57    32165  24993  18761  -7205  -4000   1654       O  
ATOM    279  CB  LEU A  57      14.062   6.830 -16.615  1.00187.55           C  
ANISOU  279  CB  LEU A  57    31196  22178  17888  -5788  -2588   1161       C  
ATOM    280  CG  LEU A  57      13.176   6.382 -15.444  1.00193.04           C  
ANISOU  280  CG  LEU A  57    32433  22813  18102  -5120  -2224    906       C  
ATOM    281  CD1 LEU A  57      12.836   7.544 -14.522  1.00201.90           C  
ANISOU  281  CD1 LEU A  57    35248  23071  18393  -5208  -2270    441       C  
ATOM    282  CD2 LEU A  57      11.906   5.751 -15.954  1.00188.46           C  
ANISOU  282  CD2 LEU A  57    31319  22337  17951  -4045  -1415    926       C  
ATOM    283  N   ILE A  58      16.539   4.730 -16.637  1.00185.28           N  
ANISOU  283  N   ILE A  58    28369  23834  18195  -6800  -3568   2224       N  
ATOM    284  CA  ILE A  58      17.141   3.453 -16.237  1.00183.19           C  
ANISOU  284  CA  ILE A  58    27120  24421  18064  -6755  -3724   2626       C  
ATOM    285  C   ILE A  58      18.554   3.686 -15.656  1.00194.20           C  
ANISOU  285  C   ILE A  58    28385  26236  19164  -7814  -4595   2983       C  
ATOM    286  O   ILE A  58      18.891   3.096 -14.628  1.00196.41           O  
ANISOU  286  O   ILE A  58    28605  26927  19093  -7930  -4891   3108       O  
ATOM    287  CB  ILE A  58      17.070   2.415 -17.403  1.00178.24           C  
ANISOU  287  CB  ILE A  58    25238  24293  18193  -6152  -3263   2960       C  
ATOM    288  CG1 ILE A  58      15.684   1.731 -17.422  1.00172.32           C  
ANISOU  288  CG1 ILE A  58    24535  23353  17584  -5149  -2544   2687       C  
ATOM    289  CG2 ILE A  58      18.193   1.362 -17.350  1.00179.27           C  
ANISOU  289  CG2 ILE A  58    24250  25316  18548  -6345  -3560   3549       C  
ATOM    290  CD1 ILE A  58      15.050   1.578 -18.787  1.00172.48           C  
ANISOU  290  CD1 ILE A  58    24090  23264  18182  -4612  -2035   2684       C  
ATOM    291  N   LEU A  59      19.339   4.587 -16.278  1.00194.75           N  
ANISOU  291  N   LEU A  59    28450  26197  19350  -8613  -5025   3171       N  
ATOM    292  CA  LEU A  59      20.692   4.943 -15.830  1.00196.36           C  
ANISOU  292  CA  LEU A  59    28040  26653  19915  -8612  -5340   3078       C  
ATOM    293  C   LEU A  59      20.692   5.940 -14.656  1.00201.14           C  
ANISOU  293  C   LEU A  59    29383  26672  20370  -8131  -5315   2216       C  
ATOM    294  O   LEU A  59      21.678   6.007 -13.918  1.00202.46           O  
ANISOU  294  O   LEU A  59    29103  27131  20693  -8019  -5578   2051       O  
ATOM    295  CB  LEU A  59      21.525   5.485 -17.002  1.00195.79           C  
ANISOU  295  CB  LEU A  59    27259  26648  20483  -8859  -5351   3327       C  
ATOM    296  CG  LEU A  59      22.000   4.447 -18.015  1.00196.58           C  
ANISOU  296  CG  LEU A  59    26071  27526  21096  -8702  -5160   4008       C  
ATOM    297  CD1 LEU A  59      21.816   4.945 -19.433  1.00195.58           C  
ANISOU  297  CD1 LEU A  59    25811  27227  21272  -8920  -4962   4261       C  
ATOM    298  CD2 LEU A  59      23.443   4.049 -17.760  1.00198.63           C  
ANISOU  298  CD2 LEU A  59    25303  28322  21845  -8404  -5240   4111       C  
ATOM    299  N   SER A  60      19.589   6.701 -14.487  1.00199.21           N  
ANISOU  299  N   SER A  60    30407  25655  19628  -8139  -5144   1814       N  
ATOM    300  CA  SER A  60      19.404   7.707 -13.434  1.00201.80           C  
ANISOU  300  CA  SER A  60    31441  25490  19744  -7700  -5081   1069       C  
ATOM    301  C   SER A  60      19.171   7.068 -12.059  1.00205.44           C  
ANISOU  301  C   SER A  60    31983  26277  19797  -7119  -5029    830       C  
ATOM    302  O   SER A  60      19.735   7.542 -11.069  1.00207.70           O  
ANISOU  302  O   SER A  60    32165  26681  20071  -6868  -5212    400       O  
ATOM    303  CB  SER A  60      18.252   8.647 -13.786  1.00204.44           C  
ANISOU  303  CB  SER A  60    32620  25015  20043  -7234  -4554    635       C  
ATOM    304  OG  SER A  60      18.321   9.866 -13.066  1.00212.41           O  
ANISOU  304  OG  SER A  60    33487  25795  21424  -6464  -4301   -119       O  
ATOM    305  N   SER A  61      18.343   6.000 -11.996  1.00201.17           N  
ANISOU  305  N   SER A  61    31915  25847  18672  -7305  -4955   1225       N  
ATOM    306  CA  SER A  61      18.032   5.282 -10.756  1.00201.91           C  
ANISOU  306  CA  SER A  61    32274  26224  18217  -6959  -4939   1155       C  
ATOM    307  C   SER A  61      18.992   4.111 -10.541  1.00203.03           C  
ANISOU  307  C   SER A  61    31276  27256  18610  -7044  -5251   1659       C  
ATOM    308  O   SER A  61      19.234   3.328 -11.463  1.00200.05           O  
ANISOU  308  O   SER A  61    30193  27303  18515  -7495  -5338   2307       O  
ATOM    309  CB  SER A  61      16.585   4.800 -10.755  1.00203.24           C  
ANISOU  309  CB  SER A  61    33189  26055  17977  -6524  -4352   1133       C  
ATOM    310  OG  SER A  61      16.202   4.304  -9.482  1.00210.87           O  
ANISOU  310  OG  SER A  61    34021  27347  18755  -5581  -4025    877       O  
ATOM    311  N   HIS A  62      19.544   4.011  -9.319  1.00202.80           N  
ANISOU  311  N   HIS A  62    31245  27539  18271  -6903  -5562   1487       N  
ATOM    312  CA  HIS A  62      20.500   2.977  -8.910  1.00202.55           C  
ANISOU  312  CA  HIS A  62    30298  28291  18370  -6930  -5895   1929       C  
ATOM    313  C   HIS A  62      19.896   1.569  -8.828  1.00203.59           C  
ANISOU  313  C   HIS A  62    30181  28837  18338  -6717  -5629   2430       C  
ATOM    314  O   HIS A  62      20.598   0.595  -9.107  1.00202.17           O  
ANISOU  314  O   HIS A  62    29009  29316  18491  -6830  -5788   3020       O  
ATOM    315  CB  HIS A  62      21.194   3.359  -7.590  1.00206.27           C  
ANISOU  315  CB  HIS A  62    30750  28925  18698  -6445  -6130   1410       C  
ATOM    316  CG  HIS A  62      20.274   3.946  -6.566  1.00210.95           C  
ANISOU  316  CG  HIS A  62    32173  29181  18798  -5763  -5781    748       C  
ATOM    317  ND1 HIS A  62      19.973   5.296  -6.559  1.00213.43           N  
ANISOU  317  ND1 HIS A  62    32883  28996  19215  -5542  -5586    102       N  
ATOM    318  CD2 HIS A  62      19.610   3.345  -5.552  1.00213.44           C  
ANISOU  318  CD2 HIS A  62    32848  29684  18565  -5232  -5550    701       C  
ATOM    319  CE1 HIS A  62      19.143   5.473  -5.544  1.00215.10           C  
ANISOU  319  CE1 HIS A  62    33731  29151  18845  -5037  -5318   -262       C  
ATOM    320  NE2 HIS A  62      18.895   4.328  -4.908  1.00215.41           N  
ANISOU  320  NE2 HIS A  62    33785  29594  18466  -4818  -5272     76       N  
ATOM    321  N   GLN A  63      18.610   1.461  -8.449  1.00201.29           N  
ANISOU  321  N   GLN A  63    30946  28190  17344  -6743  -5347   2347       N  
ATOM    322  CA  GLN A  63      17.915   0.175  -8.326  1.00199.97           C  
ANISOU  322  CA  GLN A  63    30684  28409  16887  -6776  -5121   2867       C  
ATOM    323  C   GLN A  63      17.440  -0.401  -9.676  1.00193.07           C  
ANISOU  323  C   GLN A  63    28835  27583  16942  -6184  -4467   3031       C  
ATOM    324  O   GLN A  63      17.200  -1.607  -9.765  1.00187.10           O  
ANISOU  324  O   GLN A  63    27253  27250  16585  -5557  -4059   3323       O  
ATOM    325  CB  GLN A  63      16.760   0.245  -7.302  1.00203.15           C  
ANISOU  325  CB  GLN A  63    32222  28347  16617  -6155  -4652   2417       C  
ATOM    326  CG  GLN A  63      15.672   1.278  -7.601  1.00212.93           C  
ANISOU  326  CG  GLN A  63    33967  28784  18155  -5129  -3859   1668       C  
ATOM    327  CD  GLN A  63      14.565   1.236  -6.578  1.00227.76           C  
ANISOU  327  CD  GLN A  63    35638  30745  20157  -3463  -2955   1192       C  
ATOM    328  OE1 GLN A  63      14.724   1.666  -5.430  1.00226.85           O  
ANISOU  328  OE1 GLN A  63    35858  30772  19562  -3259  -3096    891       O  
ATOM    329  NE2 GLN A  63      13.412   0.720  -6.975  1.00221.59           N  
ANISOU  329  NE2 GLN A  63    35803  29493  18899  -3741  -2571   1450       N  
ATOM    330  N   LEU A  64      17.316   0.450 -10.717  1.00187.14           N  
ANISOU  330  N   LEU A  64    28206  26369  16530  -6347  -4368   2832       N  
ATOM    331  CA  LEU A  64      16.861   0.032 -12.048  1.00178.10           C  
ANISOU  331  CA  LEU A  64    26235  25218  16217  -5781  -3778   2925       C  
ATOM    332  C   LEU A  64      17.995  -0.435 -12.966  1.00179.66           C  
ANISOU  332  C   LEU A  64    25205  26047  17010  -6120  -4061   3486       C  
ATOM    333  O   LEU A  64      17.815  -1.410 -13.697  1.00172.86           O  
ANISOU  333  O   LEU A  64    23461  25479  16739  -5531  -3614   3726       O  
ATOM    334  CB  LEU A  64      16.030   1.136 -12.740  1.00176.88           C  
ANISOU  334  CB  LEU A  64    26825  24259  16120  -5632  -3428   2459       C  
ATOM    335  CG  LEU A  64      14.734   1.616 -12.052  1.00183.06           C  
ANISOU  335  CG  LEU A  64    28764  24385  16407  -5053  -2934   1949       C  
ATOM    336  CD1 LEU A  64      14.128   2.790 -12.798  1.00183.36           C  
ANISOU  336  CD1 LEU A  64    29488  23673  16509  -4970  -2669   1592       C  
ATOM    337  CD2 LEU A  64      13.696   0.505 -11.953  1.00179.76           C  
ANISOU  337  CD2 LEU A  64    27861  24173  16267  -4104  -2230   2024       C  
ATOM    338  N   ARG A  65      19.149   0.264 -12.934  1.00182.17           N  
ANISOU  338  N   ARG A  65    25501  26564  17152  -7067  -4794   3721       N  
ATOM    339  CA  ARG A  65      20.339  -0.002 -13.760  1.00182.02           C  
ANISOU  339  CA  ARG A  65    24327  27198  17633  -7465  -5099   4348       C  
ATOM    340  C   ARG A  65      20.975  -1.393 -13.561  1.00183.93           C  
ANISOU  340  C   ARG A  65    23446  28320  18117  -7128  -5086   4961       C  
ATOM    341  O   ARG A  65      21.474  -1.973 -14.528  1.00180.57           O  
ANISOU  341  O   ARG A  65    22003  28329  18275  -6880  -4877   5408       O  
ATOM    342  CB  ARG A  65      21.408   1.102 -13.576  1.00189.44           C  
ANISOU  342  CB  ARG A  65    25509  28112  18358  -8455  -5858   4414       C  
ATOM    343  CG  ARG A  65      21.845   1.343 -12.129  1.00197.27           C  
ANISOU  343  CG  ARG A  65    26877  28818  19258  -7708  -5882   3661       C  
ATOM    344  CD  ARG A  65      23.152   2.097 -12.018  1.00202.30           C  
ANISOU  344  CD  ARG A  65    27065  29331  20470  -7369  -6004   3204       C  
ATOM    345  NE  ARG A  65      23.531   2.292 -10.617  1.00208.33           N  
ANISOU  345  NE  ARG A  65    28089  30000  21068  -6736  -6095   2566       N  
ATOM    346  CZ  ARG A  65      24.721   2.721 -10.209  1.00217.92           C  
ANISOU  346  CZ  ARG A  65    28751  31150  22900  -5951  -6023   1926       C  
ATOM    347  NH1 ARG A  65      25.674   2.999 -11.090  1.00208.31           N  
ANISOU  347  NH1 ARG A  65    26985  30218  21944  -6900  -6447   2472       N  
ATOM    348  NH2 ARG A  65      24.970   2.869  -8.915  1.00210.79           N  
ANISOU  348  NH2 ARG A  65    28316  30498  21278  -6400  -6653   1899       N  
ATOM    349  N   ARG A  66      20.976  -1.902 -12.313  1.00182.49           N  
ANISOU  349  N   ARG A  66    23506  28383  17450  -7088  -5293   5001       N  
ATOM    350  CA  ARG A  66      21.581  -3.183 -11.938  1.00181.93           C  
ANISOU  350  CA  ARG A  66    22502  29113  17510  -6771  -5319   5603       C  
ATOM    351  C   ARG A  66      20.853  -4.418 -12.484  1.00175.99           C  
ANISOU  351  C   ARG A  66    21228  28350  17290  -5705  -4498   5631       C  
ATOM    352  O   ARG A  66      21.518  -5.366 -12.910  1.00174.46           O  
ANISOU  352  O   ARG A  66    20044  28741  17503  -5396  -4389   6202       O  
ATOM    353  CB  ARG A  66      21.733  -3.277 -10.412  1.00188.44           C  
ANISOU  353  CB  ARG A  66    23863  30149  17588  -7063  -5799   5614       C  
ATOM    354  N   LYS A  67      19.502  -4.411 -12.454  1.00166.41           N  
ANISOU  354  N   LYS A  67    20697  26478  16055  -5151  -3932   5056       N  
ATOM    355  CA  LYS A  67      18.634  -5.514 -12.893  1.00158.66           C  
ANISOU  355  CA  LYS A  67    19382  25376  15524  -4248  -3205   5024       C  
ATOM    356  C   LYS A  67      18.716  -5.816 -14.407  1.00155.88           C  
ANISOU  356  C   LYS A  67    18344  25013  15870  -3936  -2842   5155       C  
ATOM    357  O   LYS A  67      18.767  -4.874 -15.203  1.00154.85           O  
ANISOU  357  O   LYS A  67    18354  24618  15865  -4251  -2910   4969       O  
ATOM    358  CB  LYS A  67      17.179  -5.268 -12.454  1.00158.70           C  
ANISOU  358  CB  LYS A  67    20262  24738  15298  -3849  -2759   4451       C  
ATOM    359  CG  LYS A  67      16.964  -5.445 -10.953  1.00178.36           C  
ANISOU  359  CG  LYS A  67    23321  27311  17137  -3840  -2898   4410       C  
ATOM    360  CD  LYS A  67      15.682  -4.789 -10.468  1.00188.50           C  
ANISOU  360  CD  LYS A  67    25619  27959  18042  -3573  -2533   3855       C  
ATOM    361  CE  LYS A  67      15.579  -4.838  -8.964  1.00204.99           C  
ANISOU  361  CE  LYS A  67    28374  30141  19370  -3598  -2699   3817       C  
ATOM    362  NZ  LYS A  67      14.423  -4.053  -8.463  1.00215.95           N  
ANISOU  362  NZ  LYS A  67    30846  30914  20292  -3315  -2328   3303       N  
ATOM    363  N   PRO A  68      18.726  -7.112 -14.826  1.00148.07           N  
ANISOU  363  N   PRO A  68    16696  24264  15300  -3309  -2450   5469       N  
ATOM    364  CA  PRO A  68      18.824  -7.423 -16.266  1.00143.41           C  
ANISOU  364  CA  PRO A  68    15576  23636  15278  -2983  -2105   5572       C  
ATOM    365  C   PRO A  68      17.542  -7.201 -17.068  1.00140.76           C  
ANISOU  365  C   PRO A  68    15649  22643  15191  -2645  -1632   5046       C  
ATOM    366  O   PRO A  68      17.622  -7.044 -18.285  1.00137.70           O  
ANISOU  366  O   PRO A  68    15008  22159  15151  -2552  -1462   5037       O  
ATOM    367  CB  PRO A  68      19.265  -8.895 -16.296  1.00144.95           C  
ANISOU  367  CB  PRO A  68    15117  24233  15723  -2416  -1865   6066       C  
ATOM    368  CG  PRO A  68      19.468  -9.304 -14.864  1.00153.57           C  
ANISOU  368  CG  PRO A  68    16310  25638  16403  -2496  -2129   6278       C  
ATOM    369  CD  PRO A  68      18.683  -8.351 -14.028  1.00149.93           C  
ANISOU  369  CD  PRO A  68    16713  24779  15476  -2866  -2303   5758       C  
ATOM    370  N   SER A  69      16.368  -7.203 -16.400  1.00135.22           N  
ANISOU  370  N   SER A  69    15537  21542  14299  -2437  -1412   4670       N  
ATOM    371  CA  SER A  69      15.057  -6.987 -17.026  1.00130.01           C  
ANISOU  371  CA  SER A  69    15218  20332  13848  -2116   -984   4250       C  
ATOM    372  C   SER A  69      14.957  -5.598 -17.661  1.00133.21           C  
ANISOU  372  C   SER A  69    15990  20414  14208  -2462  -1097   3946       C  
ATOM    373  O   SER A  69      14.434  -5.468 -18.768  1.00128.91           O  
ANISOU  373  O   SER A  69    15364  19612  14003  -2250   -828   3797       O  
ATOM    374  CB  SER A  69      13.935  -7.187 -16.009  1.00133.38           C  
ANISOU  374  CB  SER A  69    16138  20521  14020  -1853   -746   4040       C  
ATOM    375  OG  SER A  69      14.139  -6.440 -14.821  1.00146.00           O  
ANISOU  375  OG  SER A  69    18303  22145  15025  -2199  -1054   3935       O  
ATOM    376  N   TYR A  70      15.501  -4.576 -16.969  1.00134.42           N  
ANISOU  376  N   TYR A  70    16581  20571  13920  -3026  -1529   3877       N  
ATOM    377  CA  TYR A  70      15.522  -3.175 -17.394  1.00135.70           C  
ANISOU  377  CA  TYR A  70    17233  20367  13960  -3450  -1704   3614       C  
ATOM    378  C   TYR A  70      16.597  -2.889 -18.449  1.00140.25           C  
ANISOU  378  C   TYR A  70    17242  21209  14840  -3814  -1937   3917       C  
ATOM    379  O   TYR A  70      16.546  -1.845 -19.106  1.00140.38           O  
ANISOU  379  O   TYR A  70    17552  20893  14891  -4083  -1987   3745       O  
ATOM    380  CB  TYR A  70      15.630  -2.241 -16.179  1.00142.67           C  
ANISOU  380  CB  TYR A  70    18967  21051  14188  -3932  -2087   3397       C  
ATOM    381  CG  TYR A  70      14.359  -2.212 -15.357  1.00143.74           C  
ANISOU  381  CG  TYR A  70    19819  20793  14003  -3467  -1710   3037       C  
ATOM    382  CD1 TYR A  70      14.120  -3.168 -14.374  1.00146.03           C  
ANISOU  382  CD1 TYR A  70    20031  21346  14107  -3156  -1596   3164       C  
ATOM    383  CD2 TYR A  70      13.382  -1.249 -15.584  1.00144.20           C  
ANISOU  383  CD2 TYR A  70    20594  20242  13953  -3276  -1415   2634       C  
ATOM    384  CE1 TYR A  70      12.936  -3.167 -13.638  1.00146.94           C  
ANISOU  384  CE1 TYR A  70    20733  21158  13938  -2685  -1186   2915       C  
ATOM    385  CE2 TYR A  70      12.197  -1.235 -14.849  1.00145.52           C  
ANISOU  385  CE2 TYR A  70    21344  20114  13832  -2754   -989   2395       C  
ATOM    386  CZ  TYR A  70      11.980  -2.193 -13.873  1.00153.31           C  
ANISOU  386  CZ  TYR A  70    22211  21403  14637  -2471   -872   2544       C  
ATOM    387  OH  TYR A  70      10.818  -2.177 -13.140  1.00155.53           O  
ANISOU  387  OH  TYR A  70    23020  21447  14626  -1934   -408   2382       O  
ATOM    388  N   LEU A  71      17.543  -3.837 -18.639  1.00136.95           N  
ANISOU  388  N   LEU A  71    16002  21387  14645  -3751  -2020   4414       N  
ATOM    389  CA  LEU A  71      18.581  -3.758 -19.667  1.00137.49           C  
ANISOU  389  CA  LEU A  71    15396  21821  15023  -3945  -2129   4822       C  
ATOM    390  C   LEU A  71      17.937  -4.025 -21.028  1.00134.69           C  
ANISOU  390  C   LEU A  71    14880  21199  15095  -3405  -1618   4673       C  
ATOM    391  O   LEU A  71      18.446  -3.557 -22.044  1.00134.47           O  
ANISOU  391  O   LEU A  71    14576  21247  15272  -3554  -1622   4836       O  
ATOM    392  CB  LEU A  71      19.709  -4.778 -19.413  1.00140.43           C  
ANISOU  392  CB  LEU A  71    14947  22935  15477  -3868  -2270   5453       C  
ATOM    393  CG  LEU A  71      20.868  -4.343 -18.512  1.00152.74           C  
ANISOU  393  CG  LEU A  71    16326  25006  16702  -4605  -2931   5860       C  
ATOM    394  CD1 LEU A  71      21.663  -5.542 -18.043  1.00155.44           C  
ANISOU  394  CD1 LEU A  71    15925  26050  17086  -4317  -2970   6459       C  
ATOM    395  CD2 LEU A  71      21.809  -3.388 -19.233  1.00159.32           C  
ANISOU  395  CD2 LEU A  71    16840  26050  17643  -5247  -3264   6173       C  
ATOM    396  N   PHE A  72      16.814  -4.776 -21.035  1.00126.18           N  
ANISOU  396  N   PHE A  72    13982  19831  14132  -2816  -1205   4394       N  
ATOM    397  CA  PHE A  72      16.033  -5.115 -22.227  1.00120.89           C  
ANISOU  397  CA  PHE A  72    13248  18878  13807  -2333   -778   4215       C  
ATOM    398  C   PHE A  72      14.957  -4.062 -22.493  1.00121.05           C  
ANISOU  398  C   PHE A  72    13871  18351  13771  -2383   -672   3767       C  
ATOM    399  O   PHE A  72      14.565  -3.864 -23.644  1.00117.55           O  
ANISOU  399  O   PHE A  72    13383  17718  13564  -2196   -464   3668       O  
ATOM    400  CB  PHE A  72      15.432  -6.530 -22.111  1.00120.19           C  
ANISOU  400  CB  PHE A  72    13004  18781  13883  -1762   -457   4230       C  
ATOM    401  CG  PHE A  72      16.433  -7.618 -21.780  1.00124.44           C  
ANISOU  401  CG  PHE A  72    13024  19802  14456  -1601   -501   4693       C  
ATOM    402  CD1 PHE A  72      17.614  -7.749 -22.508  1.00130.05           C  
ANISOU  402  CD1 PHE A  72    13195  20920  15300  -1594   -540   5109       C  
ATOM    403  CD2 PHE A  72      16.190  -8.520 -20.753  1.00127.23           C  
ANISOU  403  CD2 PHE A  72    13413  20224  14707  -1396   -458   4773       C  
ATOM    404  CE1 PHE A  72      18.543  -8.747 -22.195  1.00133.90           C  
ANISOU  404  CE1 PHE A  72    13178  21885  15811  -1347   -530   5610       C  
ATOM    405  CE2 PHE A  72      17.121  -9.519 -20.443  1.00132.75           C  
ANISOU  405  CE2 PHE A  72    13645  21364  15431  -1187   -478   5249       C  
ATOM    406  CZ  PHE A  72      18.286  -9.631 -21.171  1.00133.21           C  
ANISOU  406  CZ  PHE A  72    13165  21828  15622  -1136   -504   5669       C  
ATOM    407  N   ILE A  73      14.499  -3.378 -21.426  1.00118.81           N  
ANISOU  407  N   ILE A  73    14187  17822  13134  -2594   -801   3523       N  
ATOM    408  CA  ILE A  73      13.525  -2.285 -21.485  1.00118.04           C  
ANISOU  408  CA  ILE A  73    14755  17193  12902  -2586   -675   3141       C  
ATOM    409  C   ILE A  73      14.251  -1.065 -22.073  1.00123.69           C  
ANISOU  409  C   ILE A  73    15637  17787  13573  -3099   -944   3165       C  
ATOM    410  O   ILE A  73      13.708  -0.388 -22.950  1.00121.60           O  
ANISOU  410  O   ILE A  73    15569  17186  13446  -2984   -761   3006       O  
ATOM    411  CB  ILE A  73      12.905  -2.026 -20.078  1.00123.80           C  
ANISOU  411  CB  ILE A  73    16136  17711  13189  -2565   -675   2916       C  
ATOM    412  CG1 ILE A  73      11.982  -3.201 -19.669  1.00121.46           C  
ANISOU  412  CG1 ILE A  73    15638  17500  13013  -2013   -319   2936       C  
ATOM    413  CG2 ILE A  73      12.154  -0.683 -20.014  1.00126.43           C  
ANISOU  413  CG2 ILE A  73    17292  17475  13269  -2585   -575   2567       C  
ATOM    414  CD1 ILE A  73      11.781  -3.424 -18.151  1.00132.81           C  
ANISOU  414  CD1 ILE A  73    17458  18989  14013  -1980   -348   2908       C  
ATOM    415  N   GLY A  74      15.485  -0.846 -21.610  1.00124.05           N  
ANISOU  415  N   GLY A  74    15543  18146  13443  -3676  -1393   3426       N  
ATOM    416  CA  GLY A  74      16.367   0.221 -22.070  1.00127.43           C  
ANISOU  416  CA  GLY A  74    16031  18546  13841  -4310  -1735   3572       C  
ATOM    417  C   GLY A  74      16.795   0.029 -23.511  1.00127.76           C  
ANISOU  417  C   GLY A  74    15411  18821  14313  -4166  -1558   3856       C  
ATOM    418  O   GLY A  74      16.784   0.988 -24.286  1.00127.85           O  
ANISOU  418  O   GLY A  74    15637  18546  14393  -4373  -1556   3809       O  
ATOM    419  N   SER A  75      17.145  -1.228 -23.881  1.00121.28           N  
ANISOU  419  N   SER A  75    13850  18483  13749  -3755  -1370   4154       N  
ATOM    420  CA  SER A  75      17.541  -1.629 -25.236  1.00118.87           C  
ANISOU  420  CA  SER A  75    12952  18425  13787  -3464  -1120   4429       C  
ATOM    421  C   SER A  75      16.379  -1.468 -26.203  1.00118.65           C  
ANISOU  421  C   SER A  75    13224  17939  13919  -3018   -741   4070       C  
ATOM    422  O   SER A  75      16.614  -1.188 -27.378  1.00117.91           O  
ANISOU  422  O   SER A  75    12928  17876  13997  -2956   -611   4202       O  
ATOM    423  CB  SER A  75      18.029  -3.072 -25.257  1.00120.76           C  
ANISOU  423  CB  SER A  75    12549  19158  14176  -3015   -952   4759       C  
ATOM    424  OG  SER A  75      18.356  -3.501 -26.569  1.00125.81           O  
ANISOU  424  OG  SER A  75    12753  19978  15071  -2632   -649   4988       O  
ATOM    425  N   LEU A  76      15.133  -1.655 -25.719  1.00112.90           N  
ANISOU  425  N   LEU A  76    12933  16842  13122  -2700   -564   3676       N  
ATOM    426  CA  LEU A  76      13.939  -1.457 -26.535  1.00109.72           C  
ANISOU  426  CA  LEU A  76    12780  16054  12854  -2312   -258   3389       C  
ATOM    427  C   LEU A  76      13.815   0.038 -26.821  1.00116.55           C  
ANISOU  427  C   LEU A  76    14132  16541  13611  -2630   -347   3261       C  
ATOM    428  O   LEU A  76      13.695   0.411 -27.986  1.00115.19           O  
ANISOU  428  O   LEU A  76    13889  16280  13598  -2519   -213   3295       O  
ATOM    429  CB  LEU A  76      12.669  -2.007 -25.850  1.00107.45           C  
ANISOU  429  CB  LEU A  76    12742  15554  12530  -1932    -58   3121       C  
ATOM    430  CG  LEU A  76      11.324  -1.665 -26.523  1.00109.67           C  
ANISOU  430  CG  LEU A  76    13264  15483  12923  -1582    209   2888       C  
ATOM    431  CD1 LEU A  76      11.086  -2.503 -27.768  1.00106.77           C  
ANISOU  431  CD1 LEU A  76    12502  15233  12833  -1260    368   2957       C  
ATOM    432  CD2 LEU A  76      10.171  -1.795 -25.550  1.00111.99           C  
ANISOU  432  CD2 LEU A  76    13860  15589  13101  -1335    370   2710       C  
ATOM    433  N   ALA A  77      13.912   0.885 -25.763  1.00116.80           N  
ANISOU  433  N   ALA A  77    14714  16331  13333  -3035   -586   3130       N  
ATOM    434  CA  ALA A  77      13.854   2.349 -25.843  1.00119.79           C  
ANISOU  434  CA  ALA A  77    15739  16234  13540  -3390   -702   2994       C  
ATOM    435  C   ALA A  77      14.977   2.913 -26.729  1.00125.60           C  
ANISOU  435  C   ALA A  77    16170  17139  14413  -3870   -912   3329       C  
ATOM    436  O   ALA A  77      14.766   3.926 -27.393  1.00126.34           O  
ANISOU  436  O   ALA A  77    16625  16853  14526  -3970   -860   3276       O  
ATOM    437  CB  ALA A  77      13.924   2.953 -24.450  1.00125.08           C  
ANISOU  437  CB  ALA A  77    17117  16632  13777  -3771   -970   2802       C  
ATOM    438  N   LEU A  78      16.154   2.237 -26.751  1.00122.85           N  
ANISOU  438  N   LEU A  78    15122  17388  14167  -4116  -1111   3736       N  
ATOM    439  CA  LEU A  78      17.325   2.581 -27.567  1.00125.32           C  
ANISOU  439  CA  LEU A  78    14941  18036  14637  -4526  -1268   4201       C  
ATOM    440  C   LEU A  78      17.019   2.275 -29.028  1.00126.42           C  
ANISOU  440  C   LEU A  78    14733  18244  15055  -3986   -859   4277       C  
ATOM    441  O   LEU A  78      17.310   3.095 -29.901  1.00127.91           O  
ANISOU  441  O   LEU A  78    14942  18334  15324  -4198   -846   4448       O  
ATOM    442  CB  LEU A  78      18.550   1.766 -27.112  1.00127.55           C  
ANISOU  442  CB  LEU A  78    14486  19031  14947  -4759  -1508   4680       C  
ATOM    443  CG  LEU A  78      19.915   2.310 -27.509  1.00137.30           C  
ANISOU  443  CG  LEU A  78    15220  20685  16263  -5405  -1810   5272       C  
ATOM    444  CD1 LEU A  78      20.896   2.174 -26.373  1.00142.90           C  
ANISOU  444  CD1 LEU A  78    15664  21839  16793  -6014  -2322   5605       C  
ATOM    445  CD2 LEU A  78      20.452   1.611 -28.740  1.00137.59           C  
ANISOU  445  CD2 LEU A  78    14443  21238  16597  -4935  -1446   5715       C  
ATOM    446  N   ALA A  79      16.434   1.087 -29.286  1.00118.79           N  
ANISOU  446  N   ALA A  79    13500  17429  14207  -3319   -546   4160       N  
ATOM    447  CA  ALA A  79      16.043   0.628 -30.618  1.00115.43           C  
ANISOU  447  CA  ALA A  79    12848  17045  13967  -2776   -191   4169       C  
ATOM    448  C   ALA A  79      14.863   1.447 -31.136  1.00117.74           C  
ANISOU  448  C   ALA A  79    13684  16803  14247  -2607    -47   3831       C  
ATOM    449  O   ALA A  79      14.719   1.605 -32.347  1.00116.48           O  
ANISOU  449  O   ALA A  79    13440  16634  14182  -2378    139   3903       O  
ATOM    450  CB  ALA A  79      15.685  -0.847 -30.576  1.00112.72           C  
ANISOU  450  CB  ALA A  79    12235  16896  13696  -2219     18   4094       C  
ATOM    451  N   ASP A  80      14.042   1.985 -30.213  1.00114.64           N  
ANISOU  451  N   ASP A  80    13860  15991  13707  -2680   -114   3503       N  
ATOM    452  CA  ASP A  80      12.875   2.810 -30.509  1.00114.05           C  
ANISOU  452  CA  ASP A  80    14320  15416  13597  -2453     51   3234       C  
ATOM    453  C   ASP A  80      13.264   4.252 -30.786  1.00121.15           C  
ANISOU  453  C   ASP A  80    15648  15970  14412  -2883    -72   3314       C  
ATOM    454  O   ASP A  80      12.755   4.814 -31.748  1.00120.42           O  
ANISOU  454  O   ASP A  80    15697  15665  14394  -2661    106   3315       O  
ATOM    455  CB  ASP A  80      11.835   2.739 -29.374  1.00115.83           C  
ANISOU  455  CB  ASP A  80    14975  15364  13671  -2237    120   2917       C  
ATOM    456  CG  ASP A  80      10.738   1.694 -29.525  1.00124.92           C  
ANISOU  456  CG  ASP A  80    15875  16628  14961  -1668    365   2803       C  
ATOM    457  OD1 ASP A  80      10.778   0.920 -30.514  1.00123.19           O  
ANISOU  457  OD1 ASP A  80    15211  16666  14931  -1450    444   2912       O  
ATOM    458  OD2 ASP A  80       9.832   1.657 -28.660  1.00131.75           O  
ANISOU  458  OD2 ASP A  80    17022  17315  15722  -1453    476   2625       O  
ATOM    459  N   PHE A  81      14.150   4.854 -29.954  1.00121.61           N  
ANISOU  459  N   PHE A  81    15945  15958  14302  -3530   -406   3401       N  
ATOM    460  CA  PHE A  81      14.621   6.239 -30.114  1.00126.43           C  
ANISOU  460  CA  PHE A  81    17050  16171  14817  -4091   -600   3498       C  
ATOM    461  C   PHE A  81      15.277   6.437 -31.474  1.00129.88           C  
ANISOU  461  C   PHE A  81    17005  16862  15481  -4178   -530   3894       C  
ATOM    462  O   PHE A  81      14.948   7.397 -32.173  1.00130.65           O  
ANISOU  462  O   PHE A  81    17491  16557  15593  -4172   -420   3900       O  
ATOM    463  CB  PHE A  81      15.596   6.634 -28.985  1.00133.84           C  
ANISOU  463  CB  PHE A  81    18231  17097  15525  -4890  -1078   3581       C  
ATOM    464  CG  PHE A  81      16.238   7.996 -29.133  1.00141.82           C  
ANISOU  464  CG  PHE A  81    19744  17700  16442  -5638  -1374   3739       C  
ATOM    465  CD1 PHE A  81      15.578   9.144 -28.707  1.00148.31           C  
ANISOU  465  CD1 PHE A  81    21665  17691  16995  -5734  -1382   3394       C  
ATOM    466  CD2 PHE A  81      17.510   8.128 -29.680  1.00147.27           C  
ANISOU  466  CD2 PHE A  81    19833  18822  17302  -6242  -1629   4275       C  
ATOM    467  CE1 PHE A  81      16.174  10.401 -28.840  1.00155.94           C  
ANISOU  467  CE1 PHE A  81    23204  18182  17864  -6478  -1679   3537       C  
ATOM    468  CE2 PHE A  81      18.103   9.385 -29.816  1.00156.81           C  
ANISOU  468  CE2 PHE A  81    21500  19636  18447  -7027  -1938   4472       C  
ATOM    469  CZ  PHE A  81      17.433  10.513 -29.392  1.00158.31           C  
ANISOU  469  CZ  PHE A  81    22867  18918  18367  -7173  -1984   4079       C  
ATOM    470  N   LEU A  82      16.209   5.531 -31.833  1.00125.39           N  
ANISOU  470  N   LEU A  82    15614  16964  15065  -4205   -554   4259       N  
ATOM    471  CA  LEU A  82      16.926   5.552 -33.102  1.00126.00           C  
ANISOU  471  CA  LEU A  82    15153  17400  15320  -4196   -421   4702       C  
ATOM    472  C   LEU A  82      15.974   5.334 -34.278  1.00125.21           C  
ANISOU  472  C   LEU A  82    15082  17194  15296  -3487    -25   4546       C  
ATOM    473  O   LEU A  82      16.087   6.048 -35.269  1.00126.18           O  
ANISOU  473  O   LEU A  82    15257  17221  15465  -3522     83   4752       O  
ATOM    474  CB  LEU A  82      18.069   4.530 -33.104  1.00127.01           C  
ANISOU  474  CB  LEU A  82    14427  18285  15545  -4229   -458   5142       C  
ATOM    475  CG  LEU A  82      19.352   4.920 -32.357  1.00138.10           C  
ANISOU  475  CG  LEU A  82    15558  19992  16920  -5062   -895   5574       C  
ATOM    476  CD1 LEU A  82      20.194   3.693 -32.050  1.00138.66           C  
ANISOU  476  CD1 LEU A  82    14818  20810  17055  -4894   -894   5936       C  
ATOM    477  CD2 LEU A  82      20.184   5.925 -33.153  1.00145.53           C  
ANISOU  477  CD2 LEU A  82    16336  20998  17960  -5604   -983   6081       C  
ATOM    478  N   ALA A  83      14.994   4.410 -34.142  1.00116.89           N  
ANISOU  478  N   ALA A  83    14036  16136  14239  -2898    152   4202       N  
ATOM    479  CA  ALA A  83      13.973   4.149 -35.167  1.00113.08           C  
ANISOU  479  CA  ALA A  83    13605  15562  13795  -2290    432   4040       C  
ATOM    480  C   ALA A  83      13.032   5.354 -35.347  1.00117.43           C  
ANISOU  480  C   ALA A  83    14772  15553  14294  -2246    485   3868       C  
ATOM    481  O   ALA A  83      12.686   5.685 -36.478  1.00116.96           O  
ANISOU  481  O   ALA A  83    14731  15451  14258  -1986    646   3961       O  
ATOM    482  CB  ALA A  83      13.168   2.911 -34.809  1.00109.59           C  
ANISOU  482  CB  ALA A  83    13042  15228  13371  -1831    519   3760       C  
ATOM    483  N   SER A  84      12.652   6.023 -34.236  1.00115.10           N  
ANISOU  483  N   SER A  84    15022  14824  13888  -2461    368   3643       N  
ATOM    484  CA  SER A  84      11.773   7.198 -34.220  1.00116.67           C  
ANISOU  484  CA  SER A  84    15913  14422  13996  -2348    467   3490       C  
ATOM    485  C   SER A  84      12.374   8.397 -34.953  1.00123.55           C  
ANISOU  485  C   SER A  84    17045  15029  14870  -2714    426   3758       C  
ATOM    486  O   SER A  84      11.631   9.219 -35.484  1.00124.28           O  
ANISOU  486  O   SER A  84    17558  14725  14937  -2440    600   3738       O  
ATOM    487  CB  SER A  84      11.421   7.589 -32.787  1.00122.64           C  
ANISOU  487  CB  SER A  84    17278  14766  14553  -2487    377   3204       C  
ATOM    488  OG  SER A  84      10.699   6.555 -32.140  1.00128.73           O  
ANISOU  488  OG  SER A  84    17833  15752  15325  -2087    474   2996       O  
ATOM    489  N   VAL A  85      13.710   8.500 -34.972  1.00122.04           N  
ANISOU  489  N   VAL A  85    16575  15079  14716  -3332    200   4069       N  
ATOM    490  CA  VAL A  85      14.411   9.587 -35.650  1.00126.27           C  
ANISOU  490  CA  VAL A  85    17276  15418  15284  -3793    133   4418       C  
ATOM    491  C   VAL A  85      14.794   9.167 -37.076  1.00127.58           C  
ANISOU  491  C   VAL A  85    16791  16094  15589  -3522    345   4787       C  
ATOM    492  O   VAL A  85      14.546   9.942 -37.994  1.00129.11           O  
ANISOU  492  O   VAL A  85    17213  16051  15793  -3409    498   4942       O  
ATOM    493  CB  VAL A  85      15.602  10.158 -34.827  1.00136.06           C  
ANISOU  493  CB  VAL A  85    18657  16575  16466  -4733   -280   4622       C  
ATOM    494  CG1 VAL A  85      16.275  11.328 -35.545  1.00141.67           C  
ANISOU  494  CG1 VAL A  85    19562  17032  17233  -5283   -363   5032       C  
ATOM    495  CG2 VAL A  85      15.148  10.589 -33.435  1.00137.89           C  
ANISOU  495  CG2 VAL A  85    19704  16236  16452  -4946   -482   4197       C  
ATOM    496  N   VAL A  86      15.355   7.945 -37.269  1.00120.17           N  
ANISOU  496  N   VAL A  86    15118  15823  14719  -3350    390   4928       N  
ATOM    497  CA  VAL A  86      15.774   7.449 -38.594  1.00118.68           C  
ANISOU  497  CA  VAL A  86    14389  16127  14579  -3014    639   5268       C  
ATOM    498  C   VAL A  86      14.560   7.223 -39.519  1.00116.74           C  
ANISOU  498  C   VAL A  86    14326  15763  14268  -2302    892   5023       C  
ATOM    499  O   VAL A  86      14.605   7.682 -40.661  1.00118.13           O  
ANISOU  499  O   VAL A  86    14504  15970  14411  -2154   1058   5273       O  
ATOM    500  CB  VAL A  86      16.738   6.221 -38.555  1.00122.24           C  
ANISOU  500  CB  VAL A  86    14102  17274  15071  -2938    676   5517       C  
ATOM    501  CG1 VAL A  86      17.149   5.784 -39.959  1.00122.45           C  
ANISOU  501  CG1 VAL A  86    13718  17744  15066  -2501   1004   5864       C  
ATOM    502  CG2 VAL A  86      17.990   6.533 -37.738  1.00126.90           C  
ANISOU  502  CG2 VAL A  86    14402  18084  15731  -3689    381   5895       C  
ATOM    503  N   PHE A  87      13.477   6.572 -39.031  1.00107.09           N  
ANISOU  503  N   PHE A  87    13248  14423  13017  -1906    896   4589       N  
ATOM    504  CA  PHE A  87      12.277   6.344 -39.852  1.00103.40           C  
ANISOU  504  CA  PHE A  87    12899  13895  12491  -1318   1049   4407       C  
ATOM    505  C   PHE A  87      11.530   7.648 -40.205  1.00108.49           C  
ANISOU  505  C   PHE A  87    14053  14061  13108  -1253   1108   4432       C  
ATOM    506  O   PHE A  87      11.291   7.880 -41.387  1.00108.57           O  
ANISOU  506  O   PHE A  87    14049  14149  13054   -978   1235   4605       O  
ATOM    507  CB  PHE A  87      11.324   5.294 -39.235  1.00100.66           C  
ANISOU  507  CB  PHE A  87    12495  13596  12154   -986   1013   4035       C  
ATOM    508  CG  PHE A  87      10.019   5.104 -39.977  1.00 99.88           C  
ANISOU  508  CG  PHE A  87    12481  13460  12007   -494   1080   3901       C  
ATOM    509  CD1 PHE A  87       9.975   4.391 -41.169  1.00101.72           C  
ANISOU  509  CD1 PHE A  87    12511  14002  12135   -197   1129   3965       C  
ATOM    510  CD2 PHE A  87       8.836   5.641 -39.486  1.00101.24           C  
ANISOU  510  CD2 PHE A  87    12949  13310  12207   -316   1088   3748       C  
ATOM    511  CE1 PHE A  87       8.774   4.232 -41.863  1.00101.64           C  
ANISOU  511  CE1 PHE A  87    12574  13993  12051    165   1098   3876       C  
ATOM    512  CE2 PHE A  87       7.635   5.475 -40.178  1.00103.20           C  
ANISOU  512  CE2 PHE A  87    13164  13619  12427    105   1109   3727       C  
ATOM    513  CZ  PHE A  87       7.613   4.771 -41.362  1.00100.59           C  
ANISOU  513  CZ  PHE A  87    12611  13612  11997    291   1069   3789       C  
ATOM    514  N   ALA A  88      11.176   8.487 -39.198  1.00105.72           N  
ANISOU  514  N   ALA A  88    14202  13203  12762  -1461   1037   4274       N  
ATOM    515  CA  ALA A  88      10.446   9.753 -39.389  1.00107.77           C  
ANISOU  515  CA  ALA A  88    15057  12915  12976  -1325   1142   4300       C  
ATOM    516  C   ALA A  88      11.187  10.779 -40.245  1.00114.52           C  
ANISOU  516  C   ALA A  88    16075  13607  13830  -1628   1176   4682       C  
ATOM    517  O   ALA A  88      10.545  11.585 -40.923  1.00116.04           O  
ANISOU  517  O   ALA A  88    16601  13505  13983  -1334   1326   4799       O  
ATOM    518  CB  ALA A  88      10.078  10.362 -38.048  1.00110.34           C  
ANISOU  518  CB  ALA A  88    15988  12697  13238  -1471   1092   4043       C  
ATOM    519  N   CYS A  89      12.532  10.754 -40.208  1.00111.84           N  
ANISOU  519  N   CYS A  89    15464  13489  13543  -2212   1043   4942       N  
ATOM    520  CA  CYS A  89      13.372  11.643 -41.001  1.00115.76           C  
ANISOU  520  CA  CYS A  89    15998  13917  14068  -2591   1069   5402       C  
ATOM    521  C   CYS A  89      13.253  11.226 -42.468  1.00116.58           C  
ANISOU  521  C   CYS A  89    15697  14475  14125  -2087   1306   5643       C  
ATOM    522  O   CYS A  89      12.738  12.000 -43.268  1.00117.99           O  
ANISOU  522  O   CYS A  89    16187  14396  14249  -1844   1449   5790       O  
ATOM    523  CB  CYS A  89      14.820  11.595 -40.519  1.00119.26           C  
ANISOU  523  CB  CYS A  89    16106  14613  14595  -3353    845   5697       C  
ATOM    524  SG  CYS A  89      15.693  13.181 -40.602  1.00131.69           S  
ANISOU  524  SG  CYS A  89    18141  15674  16220  -4215    683   6151       S  
ATOM    525  N   SER A  90      13.648   9.975 -42.790  1.00109.07           N  
ANISOU  525  N   SER A  90    14133  14160  13149  -1868   1356   5656       N  
ATOM    526  CA  SER A  90      13.638   9.403 -44.140  1.00107.83           C  
ANISOU  526  CA  SER A  90    13661  14456  12854  -1379   1573   5840       C  
ATOM    527  C   SER A  90      12.247   9.194 -44.763  1.00108.76           C  
ANISOU  527  C   SER A  90    13999  14493  12832   -749   1629   5572       C  
ATOM    528  O   SER A  90      12.146   9.235 -45.986  1.00109.49           O  
ANISOU  528  O   SER A  90    14060  14785  12755   -427   1773   5782       O  
ATOM    529  CB  SER A  90      14.430   8.101 -44.177  1.00109.69           C  
ANISOU  529  CB  SER A  90    13327  15292  13056  -1278   1628   5890       C  
ATOM    530  OG  SER A  90      13.937   7.168 -43.231  1.00114.50           O  
ANISOU  530  OG  SER A  90    13893  15905  13706  -1164   1488   5451       O  
ATOM    531  N   PHE A  91      11.191   8.961 -43.957  1.00102.34           N  
ANISOU  531  N   PHE A  91    13374  13443  12068   -576   1510   5168       N  
ATOM    532  CA  PHE A  91       9.830   8.758 -44.480  1.00100.38           C  
ANISOU  532  CA  PHE A  91    13229  13193  11719    -37   1512   5001       C  
ATOM    533  C   PHE A  91       9.196  10.073 -44.954  1.00106.34           C  
ANISOU  533  C   PHE A  91    14398  13558  12448    122   1606   5208       C  
ATOM    534  O   PHE A  91       8.597  10.099 -46.028  1.00106.60           O  
ANISOU  534  O   PHE A  91    14413  13762  12328    512   1647   5344       O  
ATOM    535  CB  PHE A  91       8.930   8.028 -43.464  1.00 98.92           C  
ANISOU  535  CB  PHE A  91    12999  12968  11617    100   1387   4610       C  
ATOM    536  CG  PHE A  91       7.735   7.322 -44.060  1.00 98.87           C  
ANISOU  536  CG  PHE A  91    12858  13194  11514    557   1311   4489       C  
ATOM    537  CD1 PHE A  91       7.893   6.158 -44.805  1.00100.62           C  
ANISOU  537  CD1 PHE A  91    12826  13825  11581    687   1238   4424       C  
ATOM    538  CD2 PHE A  91       6.447   7.797 -43.843  1.00101.72           C  
ANISOU  538  CD2 PHE A  91    13365  13365  11920    850   1302   4468       C  
ATOM    539  CE1 PHE A  91       6.789   5.501 -45.351  1.00101.11           C  
ANISOU  539  CE1 PHE A  91    12817  14074  11526    986   1073   4316       C  
ATOM    540  CE2 PHE A  91       5.342   7.139 -44.388  1.00104.21           C  
ANISOU  540  CE2 PHE A  91    13467  13967  12161   1181   1161   4438       C  
ATOM    541  CZ  PHE A  91       5.520   5.995 -45.139  1.00101.22           C  
ANISOU  541  CZ  PHE A  91    12870  13967  11622   1187   1005   4348       C  
ATOM    542  N   VAL A  92       9.347  11.158 -44.164  1.00104.79           N  
ANISOU  542  N   VAL A  92    14633  12817  12365   -178   1630   5242       N  
ATOM    543  CA  VAL A  92       8.847  12.499 -44.501  1.00108.44           C  
ANISOU  543  CA  VAL A  92    15617  12780  12805    -30   1761   5460       C  
ATOM    544  C   VAL A  92       9.699  13.078 -45.656  1.00114.81           C  
ANISOU  544  C   VAL A  92    16401  13673  13547   -206   1861   5914       C  
ATOM    545  O   VAL A  92       9.154  13.703 -46.566  1.00116.05           O  
ANISOU  545  O   VAL A  92    16745  13743  13605    150   1985   6161       O  
ATOM    546  CB  VAL A  92       8.798  13.427 -43.251  1.00115.16           C  
ANISOU  546  CB  VAL A  92    17096  12927  13734   -303   1761   5314       C  
ATOM    547  CG1 VAL A  92       8.533  14.885 -43.628  1.00120.42           C  
ANISOU  547  CG1 VAL A  92    18425  12968  14363   -209   1927   5586       C  
ATOM    548  CG2 VAL A  92       7.752  12.946 -42.254  1.00112.19           C  
ANISOU  548  CG2 VAL A  92    16766  12492  13368     51   1758   4945       C  
ATOM    549  N   ASN A  93      11.026  12.827 -45.620  1.00112.05           N  
ANISOU  549  N   ASN A  93    15766  13559  13250   -725   1821   6079       N  
ATOM    550  CA  ASN A  93      12.002  13.251 -46.623  1.00115.44           C  
ANISOU  550  CA  ASN A  93    16047  14180  13636   -944   1948   6585       C  
ATOM    551  C   ASN A  93      11.609  12.706 -47.988  1.00117.83           C  
ANISOU  551  C   ASN A  93    16097  14973  13699   -352   2091   6713       C  
ATOM    552  O   ASN A  93      11.304  13.494 -48.879  1.00120.77           O  
ANISOU  552  O   ASN A  93    16714  15208  13964   -137   2221   7016       O  
ATOM    553  CB  ASN A  93      13.405  12.754 -46.239  1.00117.78           C  
ANISOU  553  CB  ASN A  93    15881  14837  14033  -1502   1882   6755       C  
ATOM    554  CG  ASN A  93      14.557  13.401 -46.966  1.00154.75           C  
ANISOU  554  CG  ASN A  93    20397  19658  18743  -1905   2006   7383       C  
ATOM    555  OD1 ASN A  93      14.408  14.399 -47.684  1.00156.43           O  
ANISOU  555  OD1 ASN A  93    20946  19573  18919  -1885   2130   7702       O  
ATOM    556  ND2 ASN A  93      15.750  12.848 -46.777  1.00148.89           N  
ANISOU  556  ND2 ASN A  93    19093  19399  18078  -2276   1989   7639       N  
ATOM    557  N   PHE A  94      11.535  11.363 -48.114  1.00110.08           N  
ANISOU  557  N   PHE A  94    14717  14506  12601    -78   2047   6460       N  
ATOM    558  CA  PHE A  94      11.195  10.630 -49.334  1.00109.33           C  
ANISOU  558  CA  PHE A  94    14469  14875  12195    444   2119   6487       C  
ATOM    559  C   PHE A  94       9.769  10.852 -49.828  1.00115.83           C  
ANISOU  559  C   PHE A  94    15543  15588  12881    915   2024   6375       C  
ATOM    560  O   PHE A  94       9.587  11.058 -51.026  1.00118.50           O  
ANISOU  560  O   PHE A  94    15954  16119  12951   1225   2105   6632       O  
ATOM    561  CB  PHE A  94      11.469   9.125 -49.156  1.00107.01           C  
ANISOU  561  CB  PHE A  94    13833  15016  11812    562   2065   6191       C  
ATOM    562  CG  PHE A  94      11.357   8.257 -50.389  1.00108.06           C  
ANISOU  562  CG  PHE A  94    13925  15586  11546   1038   2139   6193       C  
ATOM    563  CD1 PHE A  94      10.118   7.798 -50.829  1.00109.10           C  
ANISOU  563  CD1 PHE A  94    14227  15754  11471   1402   1932   5915       C  
ATOM    564  CD2 PHE A  94      12.493   7.836 -51.067  1.00111.47           C  
ANISOU  564  CD2 PHE A  94    14162  16411  11780   1120   2404   6483       C  
ATOM    565  CE1 PHE A  94      10.018   6.969 -51.950  1.00110.86           C  
ANISOU  565  CE1 PHE A  94    14541  16327  11253   1778   1933   5870       C  
ATOM    566  CE2 PHE A  94      12.392   7.004 -52.187  1.00115.10           C  
ANISOU  566  CE2 PHE A  94    14735  17214  11783   1611   2496   6438       C  
ATOM    567  CZ  PHE A  94      11.155   6.580 -52.624  1.00111.90           C  
ANISOU  567  CZ  PHE A  94    14613  16770  11135   1906   2230   6098       C  
ATOM    568  N   HIS A  95       8.757  10.755 -48.951  1.00111.82           N  
ANISOU  568  N   HIS A  95    15119  14846  12522   1002   1858   6042       N  
ATOM    569  CA  HIS A  95       7.379  10.886 -49.415  1.00113.12           C  
ANISOU  569  CA  HIS A  95    15382  15028  12571   1467   1755   6028       C  
ATOM    570  C   HIS A  95       6.902  12.330 -49.526  1.00123.09           C  
ANISOU  570  C   HIS A  95    17029  15837  13901   1611   1893   6340       C  
ATOM    571  O   HIS A  95       6.629  12.758 -50.643  1.00125.67           O  
ANISOU  571  O   HIS A  95    17436  16295  14018   1903   1943   6659       O  
ATOM    572  CB  HIS A  95       6.415  10.027 -48.594  1.00110.42           C  
ANISOU  572  CB  HIS A  95    14860  14763  12332   1582   1544   5641       C  
ATOM    573  CG  HIS A  95       6.465   8.589 -48.997  1.00111.57           C  
ANISOU  573  CG  HIS A  95    14728  15373  12289   1622   1365   5404       C  
ATOM    574  ND1 HIS A  95       5.713   8.112 -50.054  1.00114.71           N  
ANISOU  574  ND1 HIS A  95    15091  16105  12389   1924   1175   5440       N  
ATOM    575  CD2 HIS A  95       7.227   7.581 -48.513  1.00110.56           C  
ANISOU  575  CD2 HIS A  95    14426  15386  12196   1397   1349   5157       C  
ATOM    576  CE1 HIS A  95       6.014   6.828 -50.158  1.00112.26           C  
ANISOU  576  CE1 HIS A  95    14672  16053  11929   1856   1048   5166       C  
ATOM    577  NE2 HIS A  95       6.925   6.464 -49.257  1.00110.05           N  
ANISOU  577  NE2 HIS A  95    14292  15670  11853   1585   1179   5004       N  
ATOM    578  N   VAL A  96       6.834  13.084 -48.409  1.00122.31           N  
ANISOU  578  N   VAL A  96    17240  15186  14047   1432   1967   6261       N  
ATOM    579  CA  VAL A  96       6.345  14.475 -48.377  1.00127.73           C  
ANISOU  579  CA  VAL A  96    18442  15303  14785   1623   2140   6524       C  
ATOM    580  C   VAL A  96       7.219  15.458 -49.199  1.00138.82           C  
ANISOU  580  C   VAL A  96    20126  16487  16132   1402   2304   6969       C  
ATOM    581  O   VAL A  96       6.667  16.240 -49.980  1.00142.35           O  
ANISOU  581  O   VAL A  96    20810  16805  16472   1785   2425   7313       O  
ATOM    582  CB  VAL A  96       6.114  14.999 -46.929  1.00132.20           C  
ANISOU  582  CB  VAL A  96    19430  15254  15546   1498   2200   6282       C  
ATOM    583  CG1 VAL A  96       5.395  16.346 -46.934  1.00137.27           C  
ANISOU  583  CG1 VAL A  96    20692  15279  16185   1884   2428   6539       C  
ATOM    584  CG2 VAL A  96       5.341  13.992 -46.084  1.00127.90           C  
ANISOU  584  CG2 VAL A  96    18559  14972  15063   1688   2075   5901       C  
ATOM    585  N   PHE A  97       8.557  15.437 -49.009  1.00137.32           N  
ANISOU  585  N   PHE A  97    19874  16277  16022    788   2310   7028       N  
ATOM    586  CA  PHE A  97       9.460  16.365 -49.700  1.00142.82           C  
ANISOU  586  CA  PHE A  97    20777  16781  16708    474   2463   7521       C  
ATOM    587  C   PHE A  97      10.184  15.776 -50.917  1.00148.99           C  
ANISOU  587  C   PHE A  97    21091  18236  17282    519   2544   7821       C  
ATOM    588  O   PHE A  97      11.124  16.403 -51.411  1.00152.59           O  
ANISOU  588  O   PHE A  97    21586  18638  17752    178   2690   8279       O  
ATOM    589  CB  PHE A  97      10.463  16.984 -48.713  1.00147.04           C  
ANISOU  589  CB  PHE A  97    21599  16800  17468   -299   2413   7540       C  
ATOM    590  CG  PHE A  97       9.803  17.790 -47.620  1.00150.33           C  
ANISOU  590  CG  PHE A  97    22716  16412  17989   -312   2392   7288       C  
ATOM    591  CD1 PHE A  97       9.174  18.997 -47.904  1.00158.37           C  
ANISOU  591  CD1 PHE A  97    24402  16798  18972    -12   2572   7526       C  
ATOM    592  CD2 PHE A  97       9.810  17.341 -46.305  1.00149.80           C  
ANISOU  592  CD2 PHE A  97    22697  16205  18015   -562   2228   6833       C  
ATOM    593  CE1 PHE A  97       8.551  19.732 -46.895  1.00161.72           C  
ANISOU  593  CE1 PHE A  97    25577  16437  19433     90   2623   7293       C  
ATOM    594  CE2 PHE A  97       9.194  18.082 -45.296  1.00154.92           C  
ANISOU  594  CE2 PHE A  97    24086  16096  18680   -497   2259   6594       C  
ATOM    595  CZ  PHE A  97       8.568  19.271 -45.598  1.00158.17           C  
ANISOU  595  CZ  PHE A  97    25202  15859  19037   -149   2474   6818       C  
ATOM    596  N   HIS A  98       9.729  14.607 -51.419  1.00144.10           N  
ANISOU  596  N   HIS A  98    20090  18218  16441    942   2460   7595       N  
ATOM    597  CA  HIS A  98      10.248  13.884 -52.592  1.00145.81           C  
ANISOU  597  CA  HIS A  98    19987  19072  16343   1141   2553   7786       C  
ATOM    598  C   HIS A  98      11.806  13.704 -52.589  1.00153.11           C  
ANISOU  598  C   HIS A  98    20606  20234  17334    677   2723   8062       C  
ATOM    599  O   HIS A  98      12.436  13.602 -53.642  1.00156.02           O  
ANISOU  599  O   HIS A  98    20822  21005  17454    821   2942   8447       O  
ATOM    600  CB  HIS A  98       9.717  14.515 -53.911  1.00151.16           C  
ANISOU  600  CB  HIS A  98    20882  19832  16721   1591   2662   8181       C  
ATOM    601  CG  HIS A  98      10.463  15.709 -54.452  1.00160.70           C  
ANISOU  601  CG  HIS A  98    22306  20787  17965   1367   2922   8782       C  
ATOM    602  ND1 HIS A  98      10.197  16.996 -54.006  1.00165.78           N  
ANISOU  602  ND1 HIS A  98    23409  20726  18853   1195   2967   8970       N  
ATOM    603  CD2 HIS A  98      11.367  15.779 -55.461  1.00166.24           C  
ANISOU  603  CD2 HIS A  98    22867  21846  18452   1349   3165   9258       C  
ATOM    604  CE1 HIS A  98      10.977  17.796 -54.719  1.00170.50           C  
ANISOU  604  CE1 HIS A  98    24118  21247  19417    987   3192   9547       C  
ATOM    605  NE2 HIS A  98      11.708  17.108 -55.599  1.00171.21           N  
ANISOU  605  NE2 HIS A  98    23806  22002  19245   1070   3330   9765       N  
ATOM    606  N   GLY A  99      12.379  13.596 -51.393  1.00149.18           N  
ANISOU  606  N   GLY A  99    19988  19552  17143    163   2620   7886       N  
ATOM    607  CA  GLY A  99      13.817  13.496 -51.162  1.00151.69           C  
ANISOU  607  CA  GLY A  99    19937  20102  17597   -359   2717   8205       C  
ATOM    608  C   GLY A  99      14.537  12.213 -51.518  1.00155.57           C  
ANISOU  608  C   GLY A  99    19905  21295  17911   -148   2847   8214       C  
ATOM    609  O   GLY A  99      14.101  11.116 -51.155  1.00150.55           O  
ANISOU  609  O   GLY A  99    19163  20838  17200    124   2725   7733       O  
ATOM    610  N   VAL A 100      15.692  12.373 -52.198  1.00157.95           N  
ANISOU  610  N   VAL A 100    19884  21978  18151   -278   3126   8818       N  
ATOM    611  CA  VAL A 100      16.615  11.311 -52.623  1.00158.87           C  
ANISOU  611  CA  VAL A 100    19500  22785  18079    -25   3383   9015       C  
ATOM    612  C   VAL A 100      18.056  11.773 -52.371  1.00168.18           C  
ANISOU  612  C   VAL A 100    20179  24203  19520   -630   3525   9696       C  
ATOM    613  O   VAL A 100      18.593  12.623 -53.096  1.00173.05           O  
ANISOU  613  O   VAL A 100    20742  24885  20125   -799   3742  10336       O  
ATOM    614  CB  VAL A 100      16.365  10.762 -54.055  1.00164.30           C  
ANISOU  614  CB  VAL A 100    20309  23881  18238    740   3669   9089       C  
ATOM    615  CG1 VAL A 100      15.166   9.837 -54.061  1.00159.12           C  
ANISOU  615  CG1 VAL A 100    19969  23150  17339   1220   3434   8380       C  
ATOM    616  CG2 VAL A 100      16.182  11.885 -55.077  1.00168.55           C  
ANISOU  616  CG2 VAL A 100    21127  24290  18626    815   3827   9555       C  
ATOM    617  N   ASP A 101      18.631  11.279 -51.261  1.00163.54           N  
ANISOU  617  N   ASP A 101    19222  23723  19194  -1028   3350   9586       N  
ATOM    618  CA  ASP A 101      19.957  11.666 -50.777  1.00168.51           C  
ANISOU  618  CA  ASP A 101    19300  24604  20120  -1738   3345  10220       C  
ATOM    619  C   ASP A 101      21.107  11.164 -51.665  1.00176.60           C  
ANISOU  619  C   ASP A 101    19666  26454  20981  -1419   3824  10944       C  
ATOM    620  O   ASP A 101      21.944  11.975 -52.055  1.00182.75           O  
ANISOU  620  O   ASP A 101    20138  27411  21885  -1850   3970  11715       O  
ATOM    621  CB  ASP A 101      20.148  11.258 -49.307  1.00167.70           C  
ANISOU  621  CB  ASP A 101    19021  24402  20294  -2225   2969   9881       C  
ATOM    622  CG  ASP A 101      19.272  12.019 -48.313  1.00176.22           C  
ANISOU  622  CG  ASP A 101    20747  24654  21554  -2686   2537   9349       C  
ATOM    623  OD1 ASP A 101      18.068  12.211 -48.600  1.00173.24           O  
ANISOU  623  OD1 ASP A 101    20946  23844  21035  -2254   2529   8894       O  
ATOM    624  OD2 ASP A 101      19.774  12.367 -47.225  1.00184.63           O  
ANISOU  624  OD2 ASP A 101    21748  25534  22869  -3438   2209   9393       O  
ATOM    625  N   SER A 102      21.137   9.850 -51.985  1.00169.65           N  
ANISOU  625  N   SER A 102    18608  26044  19805   -656   4087  10726       N  
ATOM    626  CA  SER A 102      22.101   9.155 -52.864  1.00173.28           C  
ANISOU  626  CA  SER A 102    18566  27283  19991    -77   4647  11317       C  
ATOM    627  C   SER A 102      21.584   7.739 -53.148  1.00170.91           C  
ANISOU  627  C   SER A 102    18542  27119  19278    829   4814  10714       C  
ATOM    628  O   SER A 102      20.539   7.345 -52.617  1.00164.64           O  
ANISOU  628  O   SER A 102    18212  25863  18482    880   4453   9917       O  
ATOM    629  CB  SER A 102      23.497   9.082 -52.241  1.00181.33           C  
ANISOU  629  CB  SER A 102    18704  28859  21336   -561   4716  12029       C  
ATOM    630  OG  SER A 102      24.124  10.347 -52.113  1.00189.09           O  
ANISOU  630  OG  SER A 102    20166  29119  22559  -1607   4452  11585       O  
ATOM    631  N   LYS A 103      22.303   6.983 -53.994  1.00169.31           N  
ANISOU  631  N   LYS A 103    18098  27525  18705   1548   5374  11119       N  
ATOM    632  CA  LYS A 103      21.947   5.607 -54.330  1.00165.79           C  
ANISOU  632  CA  LYS A 103    18021  27168  17805   2418   5574  10599       C  
ATOM    633  C   LYS A 103      22.508   4.657 -53.258  1.00165.63           C  
ANISOU  633  C   LYS A 103    17549  27358  18024   2395   5531  10522       C  
ATOM    634  O   LYS A 103      21.879   3.644 -52.945  1.00160.34           O  
ANISOU  634  O   LYS A 103    17283  26444  17196   2756   5393   9834       O  
ATOM    635  CB  LYS A 103      22.457   5.261 -55.734  1.00174.30           C  
ANISOU  635  CB  LYS A 103    19198  28733  18294   3275   6241  11059       C  
ATOM    636  CG  LYS A 103      21.949   3.945 -56.300  1.00180.11           C  
ANISOU  636  CG  LYS A 103    20749  29226  18459   3994   6292  10173       C  
ATOM    637  CD  LYS A 103      23.055   2.915 -56.290  1.00183.23           C  
ANISOU  637  CD  LYS A 103    21189  29581  18850   3957   6411   9669       C  
ATOM    638  CE  LYS A 103      22.558   1.514 -56.527  1.00184.62           C  
ANISOU  638  CE  LYS A 103    22013  29569  18564   4652   6461   9026       C  
ATOM    639  NZ  LYS A 103      23.200   0.561 -55.591  1.00186.14           N  
ANISOU  639  NZ  LYS A 103    21913  29767  19045   4597   6439   8799       N  
ATOM    640  N   ALA A 104      23.683   4.996 -52.697  1.00165.02           N  
ANISOU  640  N   ALA A 104    16624  27744  18331   1933   5618  11274       N  
ATOM    641  CA  ALA A 104      24.325   4.218 -51.644  1.00163.80           C  
ANISOU  641  CA  ALA A 104    15926  27878  18434   1850   5555  11352       C  
ATOM    642  C   ALA A 104      23.783   4.627 -50.273  1.00160.55           C  
ANISOU  642  C   ALA A 104    15570  26953  18477    963   4847  10853       C  
ATOM    643  O   ALA A 104      23.586   3.754 -49.426  1.00156.74           O  
ANISOU  643  O   ALA A 104    15111  26380  18061   1063   4665  10409       O  
ATOM    644  CB  ALA A 104      25.833   4.395 -51.699  1.00169.44           C  
ANISOU  644  CB  ALA A 104    16004  29041  19334   1544   5792  11905       C  
ATOM    645  N   VAL A 105      23.512   5.943 -50.068  1.00155.35           N  
ANISOU  645  N   VAL A 105    15023  25913  18089    143   4476  10917       N  
ATOM    646  CA  VAL A 105      22.965   6.506 -48.820  1.00150.34           C  
ANISOU  646  CA  VAL A 105    14597  24710  17815   -683   3840  10453       C  
ATOM    647  C   VAL A 105      21.557   5.951 -48.542  1.00145.63           C  
ANISOU  647  C   VAL A 105    14741  23523  17071   -335   3602   9448       C  
ATOM    648  O   VAL A 105      21.215   5.723 -47.380  1.00141.04           O  
ANISOU  648  O   VAL A 105    14225  22670  16694   -669   3222   9011       O  
ATOM    649  CB  VAL A 105      23.039   8.062 -48.779  1.00156.99           C  
ANISOU  649  CB  VAL A 105    15528  25210  18912  -1559   3572  10793       C  
ATOM    650  CG1 VAL A 105      22.195   8.658 -47.649  1.00152.40           C  
ANISOU  650  CG1 VAL A 105    15483  23867  18556  -2205   2986  10154       C  
ATOM    651  CG2 VAL A 105      24.487   8.536 -48.668  1.00164.92           C  
ANISOU  651  CG2 VAL A 105    15681  26809  20172  -2168   3636  11806       C  
ATOM    652  N   PHE A 106      20.768   5.695 -49.603  1.00140.42           N  
ANISOU  652  N   PHE A 106    14604  22717  16034    325   3815   9133       N  
ATOM    653  CA  PHE A 106      19.436   5.119 -49.454  1.00134.02           C  
ANISOU  653  CA  PHE A 106    14412  21437  15071    637   3576   8285       C  
ATOM    654  C   PHE A 106      19.509   3.723 -48.839  1.00134.74           C  
ANISOU  654  C   PHE A 106    14405  21672  15119    984   3588   7948       C  
ATOM    655  O   PHE A 106      18.725   3.432 -47.936  1.00129.96           O  
ANISOU  655  O   PHE A 106    14021  20693  14664    796   3229   7383       O  
ATOM    656  CB  PHE A 106      18.656   5.096 -50.778  1.00136.26           C  
ANISOU  656  CB  PHE A 106    15238  21619  14916   1220   3747   8100       C  
ATOM    657  CG  PHE A 106      17.268   4.523 -50.608  1.00132.75           C  
ANISOU  657  CG  PHE A 106    15344  20749  14344   1434   3426   7311       C  
ATOM    658  CD1 PHE A 106      16.265   5.259 -49.986  1.00132.63           C  
ANISOU  658  CD1 PHE A 106    15578  20238  14576   1025   3027   6968       C  
ATOM    659  CD2 PHE A 106      16.977   3.229 -51.023  1.00134.30           C  
ANISOU  659  CD2 PHE A 106    15819  21034  14175   2034   3526   6948       C  
ATOM    660  CE1 PHE A 106      14.992   4.716 -49.798  1.00129.39           C  
ANISOU  660  CE1 PHE A 106    15549  19529  14084   1209   2740   6350       C  
ATOM    661  CE2 PHE A 106      15.705   2.687 -50.830  1.00132.97           C  
ANISOU  661  CE2 PHE A 106    16098  20500  13925   2114   3171   6288       C  
ATOM    662  CZ  PHE A 106      14.723   3.434 -50.215  1.00127.65           C  
ANISOU  662  CZ  PHE A 106    15526  19436  13538   1696   2782   6030       C  
ATOM    663  N   LEU A 107      20.464   2.878 -49.298  1.00133.96           N  
ANISOU  663  N   LEU A 107    13978  22107  14813   1518   4035   8343       N  
ATOM    664  CA  LEU A 107      20.665   1.521 -48.770  1.00131.96           C  
ANISOU  664  CA  LEU A 107    13654  21988  14498   1930   4125   8117       C  
ATOM    665  C   LEU A 107      21.130   1.554 -47.306  1.00133.79           C  
ANISOU  665  C   LEU A 107    13367  22289  15177   1323   3814   8213       C  
ATOM    666  O   LEU A 107      20.967   0.570 -46.577  1.00130.63           O  
ANISOU  666  O   LEU A 107    13006  21820  14807   1500   3723   7872       O  
ATOM    667  CB  LEU A 107      21.633   0.707 -49.650  1.00137.72           C  
ANISOU  667  CB  LEU A 107    14200  23262  14865   2740   4762   8603       C  
ATOM    668  CG  LEU A 107      21.114   0.289 -51.037  1.00143.91           C  
ANISOU  668  CG  LEU A 107    15698  23930  15052   3493   5071   8354       C  
ATOM    669  CD1 LEU A 107      22.258  -0.067 -51.965  1.00151.83           C  
ANISOU  669  CD1 LEU A 107    16454  25534  15701   4224   5786   9049       C  
ATOM    670  CD2 LEU A 107      20.146  -0.879 -50.947  1.00142.22           C  
ANISOU  670  CD2 LEU A 107    16203  23259  14574   3869   4885   7543       C  
ATOM    671  N   LEU A 108      21.680   2.707 -46.884  1.00132.15           N  
ANISOU  671  N   LEU A 108    12740  22182  15290    571   3618   8676       N  
ATOM    672  CA  LEU A 108      22.112   2.959 -45.519  1.00131.46           C  
ANISOU  672  CA  LEU A 108    12244  22129  15575   -151   3228   8784       C  
ATOM    673  C   LEU A 108      20.923   3.393 -44.669  1.00128.32           C  
ANISOU  673  C   LEU A 108    12414  21029  15311   -600   2727   8056       C  
ATOM    674  O   LEU A 108      20.795   2.907 -43.550  1.00125.61           O  
ANISOU  674  O   LEU A 108    12029  20597  15101   -784   2464   7769       O  
ATOM    675  CB  LEU A 108      23.243   4.001 -45.472  1.00138.10           C  
ANISOU  675  CB  LEU A 108    12458  23359  16655   -836   3187   9626       C  
ATOM    676  CG  LEU A 108      23.881   4.255 -44.102  1.00144.71           C  
ANISOU  676  CG  LEU A 108    12832  24332  17821  -1662   2734   9853       C  
ATOM    677  CD1 LEU A 108      24.692   3.054 -43.633  1.00146.67           C  
ANISOU  677  CD1 LEU A 108    12451  25202  18074  -1264   2912  10162       C  
ATOM    678  CD2 LEU A 108      24.734   5.512 -44.118  1.00153.78           C  
ANISOU  678  CD2 LEU A 108    13571  25665  19194  -2541   2549  10587       C  
ATOM    679  N   LYS A 109      20.054   4.293 -45.198  1.00122.45           N  
ANISOU  679  N   LYS A 109    12197  19815  14514   -713   2633   7805       N  
ATOM    680  CA  LYS A 109      18.834   4.807 -44.541  1.00117.17           C  
ANISOU  680  CA  LYS A 109    12100  18483  13936  -1001   2255   7183       C  
ATOM    681  C   LYS A 109      17.898   3.660 -44.172  1.00113.77           C  
ANISOU  681  C   LYS A 109    11939  17882  13406   -546   2191   6544       C  
ATOM    682  O   LYS A 109      17.521   3.518 -43.009  1.00109.82           O  
ANISOU  682  O   LYS A 109    11517  17149  13059   -822   1908   6211       O  
ATOM    683  CB  LYS A 109      18.044   5.719 -45.495  1.00119.98           C  
ANISOU  683  CB  LYS A 109    12934  18483  14171   -900   2307   7108       C  
ATOM    684  CG  LYS A 109      18.631   7.071 -45.799  1.00139.28           C  
ANISOU  684  CG  LYS A 109    15325  20858  16735  -1432   2305   7640       C  
ATOM    685  CD  LYS A 109      17.797   7.651 -46.903  1.00149.07           C  
ANISOU  685  CD  LYS A 109    17028  21832  17782  -1088   2440   7563       C  
ATOM    686  CE  LYS A 109      18.102   9.078 -47.184  1.00164.77           C  
ANISOU  686  CE  LYS A 109    19147  23569  19889  -1595   2418   8005       C  
ATOM    687  NZ  LYS A 109      17.222   9.591 -48.273  1.00174.77           N  
ANISOU  687  NZ  LYS A 109    20868  24595  20942  -1172   2560   7943       N  
ATOM    688  N   ILE A 110      17.510   2.867 -45.196  1.00109.08           N  
ANISOU  688  N   ILE A 110    11540  17385  12521    128   2443   6390       N  
ATOM    689  CA  ILE A 110      16.610   1.724 -45.112  1.00104.87           C  
ANISOU  689  CA  ILE A 110    11321  16679  11844    554   2382   5834       C  
ATOM    690  C   ILE A 110      17.191   0.651 -44.173  1.00109.34           C  
ANISOU  690  C   ILE A 110    11581  17450  12511    608   2392   5819       C  
ATOM    691  O   ILE A 110      16.478   0.186 -43.287  1.00105.25           O  
ANISOU  691  O   ILE A 110    11218  16668  12103    512   2148   5392       O  
ATOM    692  CB  ILE A 110      16.230   1.215 -46.539  1.00108.72           C  
ANISOU  692  CB  ILE A 110    12166  17220  11923   1177   2616   5745       C  
ATOM    693  CG1 ILE A 110      14.912   0.431 -46.523  1.00105.13           C  
ANISOU  693  CG1 ILE A 110    12176  16428  11341   1389   2375   5128       C  
ATOM    694  CG2 ILE A 110      17.358   0.438 -47.242  1.00113.76           C  
ANISOU  694  CG2 ILE A 110    12600  18320  12304   1692   3068   6134       C  
ATOM    695  CD1 ILE A 110      14.179   0.486 -47.799  1.00112.19           C  
ANISOU  695  CD1 ILE A 110    13510  17243  11873   1717   2382   4999       C  
ATOM    696  N   GLY A 111      18.493   0.371 -44.315  1.00110.44           N  
ANISOU  696  N   GLY A 111    11238  18087  12637    738   2678   6362       N  
ATOM    697  CA  GLY A 111      19.232  -0.588 -43.500  1.00111.08           C  
ANISOU  697  CA  GLY A 111    10936  18463  12807    849   2742   6509       C  
ATOM    698  C   GLY A 111      19.271  -0.209 -42.034  1.00113.58           C  
ANISOU  698  C   GLY A 111    11031  18687  13436    185   2339   6449       C  
ATOM    699  O   GLY A 111      19.229  -1.087 -41.169  1.00111.53           O  
ANISOU  699  O   GLY A 111    10713  18430  13235    271   2252   6264       O  
ATOM    700  N   SER A 112      19.336   1.112 -41.754  1.00111.33           N  
ANISOU  700  N   SER A 112    10707  18275  13317   -478   2090   6599       N  
ATOM    701  CA  SER A 112      19.336   1.685 -40.408  1.00110.67           C  
ANISOU  701  CA  SER A 112    10591  18012  13447  -1176   1671   6509       C  
ATOM    702  C   SER A 112      17.945   1.574 -39.779  1.00109.25           C  
ANISOU  702  C   SER A 112    10980  17265  13265  -1151   1449   5803       C  
ATOM    703  O   SER A 112      17.846   1.337 -38.574  1.00107.42           O  
ANISOU  703  O   SER A 112    10748  16950  13118  -1405   1210   5617       O  
ATOM    704  CB  SER A 112      19.795   3.139 -40.442  1.00118.21           C  
ANISOU  704  CB  SER A 112    11503  18896  14516  -1870   1491   6868       C  
ATOM    705  OG  SER A 112      19.969   3.671 -39.139  1.00128.01           O  
ANISOU  705  OG  SER A 112    12777  19972  15889  -2584   1064   6820       O  
ATOM    706  N   VAL A 113      16.873   1.727 -40.596  1.00103.17           N  
ANISOU  706  N   VAL A 113    10659  16161  12382   -829   1533   5467       N  
ATOM    707  CA  VAL A 113      15.481   1.589 -40.144  1.00 98.48           C  
ANISOU  707  CA  VAL A 113    10508  15118  11791   -736   1367   4900       C  
ATOM    708  C   VAL A 113      15.238   0.098 -39.841  1.00 99.63           C  
ANISOU  708  C   VAL A 113    10598  15363  11893   -344   1416   4657       C  
ATOM    709  O   VAL A 113      14.747  -0.239 -38.759  1.00 95.58           O  
ANISOU  709  O   VAL A 113    10155  14685  11474   -471   1240   4390       O  
ATOM    710  CB  VAL A 113      14.448   2.164 -41.163  1.00101.39           C  
ANISOU  710  CB  VAL A 113    11268  15203  12052   -508   1415   4727       C  
ATOM    711  CG1 VAL A 113      13.015   1.913 -40.705  1.00 97.77           C  
ANISOU  711  CG1 VAL A 113    11127  14403  11618   -373   1259   4255       C  
ATOM    712  CG2 VAL A 113      14.657   3.654 -41.396  1.00103.95           C  
ANISOU  712  CG2 VAL A 113    11724  15343  12428   -881   1382   4978       C  
ATOM    713  N   THR A 114      15.640  -0.782 -40.791  1.00 98.73           N  
ANISOU  713  N   THR A 114    10406  15499  11607    143   1681   4781       N  
ATOM    714  CA  THR A 114      15.526  -2.241 -40.718  1.00 98.10           C  
ANISOU  714  CA  THR A 114    10388  15450  11433    569   1778   4591       C  
ATOM    715  C   THR A 114      16.219  -2.789 -39.471  1.00102.29           C  
ANISOU  715  C   THR A 114    10571  16174  12120    421   1722   4730       C  
ATOM    716  O   THR A 114      15.682  -3.698 -38.855  1.00 98.99           O  
ANISOU  716  O   THR A 114    10297  15586  11729    542   1644   4442       O  
ATOM    717  CB  THR A 114      16.025  -2.900 -42.026  1.00112.50           C  
ANISOU  717  CB  THR A 114    12303  17476  12967   1144   2129   4760       C  
ATOM    718  OG1 THR A 114      15.427  -2.253 -43.149  1.00114.39           O  
ANISOU  718  OG1 THR A 114    12854  17578  13029   1222   2138   4676       O  
ATOM    719  CG2 THR A 114      15.704  -4.385 -42.101  1.00111.45           C  
ANISOU  719  CG2 THR A 114    12481  17195  12669   1602   2211   4473       C  
ATOM    720  N   MET A 115      17.386  -2.225 -39.088  1.00103.24           N  
ANISOU  720  N   MET A 115    10224  16661  12342    115   1727   5209       N  
ATOM    721  CA  MET A 115      18.137  -2.656 -37.903  1.00104.49           C  
ANISOU  721  CA  MET A 115     9987  17091  12622    -76   1620   5430       C  
ATOM    722  C   MET A 115      17.478  -2.213 -36.603  1.00106.71           C  
ANISOU  722  C   MET A 115    10453  17070  13021   -580   1244   5107       C  
ATOM    723  O   MET A 115      17.260  -3.049 -35.729  1.00104.99           O  
ANISOU  723  O   MET A 115    10242  16818  12829   -490   1174   4943       O  
ATOM    724  CB  MET A 115      19.607  -2.213 -37.965  1.00111.96           C  
ANISOU  724  CB  MET A 115    10308  18609  13624   -288   1696   6131       C  
ATOM    725  CG  MET A 115      20.481  -2.911 -36.948  1.00117.96           C  
ANISOU  725  CG  MET A 115    10575  19782  14462   -324   1634   6468       C  
ATOM    726  SD  MET A 115      22.036  -2.057 -36.612  1.00129.31           S  
ANISOU  726  SD  MET A 115    11206  21896  16031   -940   1470   7319       S  
ATOM    727  CE  MET A 115      21.445  -0.704 -35.592  1.00124.48           C  
ANISOU  727  CE  MET A 115    10998  20806  15492  -1929    870   6955       C  
ATOM    728  N   THR A 116      17.152  -0.916 -36.480  1.00103.77           N  
ANISOU  728  N   THR A 116    10290  16449  12688  -1062   1037   5027       N  
ATOM    729  CA  THR A 116      16.531  -0.344 -35.282  1.00102.51           C  
ANISOU  729  CA  THR A 116    10432  15952  12565  -1490    733   4724       C  
ATOM    730  C   THR A 116      15.186  -1.008 -34.929  1.00103.96           C  
ANISOU  730  C   THR A 116    10969  15791  12739  -1171    749   4225       C  
ATOM    731  O   THR A 116      14.935  -1.267 -33.750  1.00102.53           O  
ANISOU  731  O   THR A 116    10858  15533  12565  -1311    600   4070       O  
ATOM    732  CB  THR A 116      16.424   1.177 -35.392  1.00109.23           C  
ANISOU  732  CB  THR A 116    11577  16511  13415  -1962    582   4740       C  
ATOM    733  OG1 THR A 116      15.734   1.523 -36.593  1.00107.42           O  
ANISOU  733  OG1 THR A 116    11584  16074  13157  -1649    776   4631       O  
ATOM    734  CG2 THR A 116      17.774   1.855 -35.348  1.00111.12           C  
ANISOU  734  CG2 THR A 116    11454  17075  13691  -2500    441   5270       C  
ATOM    735  N   PHE A 117      14.349  -1.318 -35.943  1.00 99.61           N  
ANISOU  735  N   PHE A 117    10616  15077  12156   -767    910   4024       N  
ATOM    736  CA  PHE A 117      13.054  -1.967 -35.719  1.00 96.54           C  
ANISOU  736  CA  PHE A 117    10480  14419  11782   -529    890   3643       C  
ATOM    737  C   PHE A 117      13.169  -3.473 -35.461  1.00 98.87           C  
ANISOU  737  C   PHE A 117    10651  14835  12080   -240    960   3607       C  
ATOM    738  O   PHE A 117      12.337  -4.014 -34.728  1.00 97.10           O  
ANISOU  738  O   PHE A 117    10543  14438  11913   -220    882   3381       O  
ATOM    739  CB  PHE A 117      12.052  -1.661 -36.844  1.00 97.80           C  
ANISOU  739  CB  PHE A 117    10893  14374  11892   -309    938   3481       C  
ATOM    740  CG  PHE A 117      11.361  -0.321 -36.718  1.00 99.83           C  
ANISOU  740  CG  PHE A 117    11397  14360  12175   -502    864   3410       C  
ATOM    741  CD1 PHE A 117      10.594  -0.015 -35.597  1.00102.29           C  
ANISOU  741  CD1 PHE A 117    11883  14442  12539   -616    779   3226       C  
ATOM    742  CD2 PHE A 117      11.447   0.621 -37.734  1.00103.86           C  
ANISOU  742  CD2 PHE A 117    12011  14823  12627   -501    925   3550       C  
ATOM    743  CE1 PHE A 117       9.951   1.222 -35.484  1.00104.19           C  
ANISOU  743  CE1 PHE A 117    12440  14383  12764   -683    780   3176       C  
ATOM    744  CE2 PHE A 117      10.805   1.860 -37.620  1.00107.50           C  
ANISOU  744  CE2 PHE A 117    12768  14973  13102   -616    893   3509       C  
ATOM    745  CZ  PHE A 117      10.056   2.149 -36.499  1.00104.96           C  
ANISOU  745  CZ  PHE A 117    12660  14398  12824   -680    833   3315       C  
ATOM    746  N   THR A 118      14.189  -4.146 -36.045  1.00 96.35           N  
ANISOU  746  N   THR A 118    10115  14801  11692     15   1141   3868       N  
ATOM    747  CA  THR A 118      14.439  -5.576 -35.816  1.00 96.21           C  
ANISOU  747  CA  THR A 118    10051  14851  11652    355   1259   3881       C  
ATOM    748  C   THR A 118      14.977  -5.743 -34.381  1.00 99.33           C  
ANISOU  748  C   THR A 118    10171  15427  12142    120   1138   4035       C  
ATOM    749  O   THR A 118      14.602  -6.694 -33.691  1.00 97.83           O  
ANISOU  749  O   THR A 118    10057  15126  11987    243   1122   3909       O  
ATOM    750  CB  THR A 118      15.353  -6.166 -36.918  1.00107.57           C  
ANISOU  750  CB  THR A 118    11419  16519  12935    815   1566   4144       C  
ATOM    751  OG1 THR A 118      14.689  -6.061 -38.180  1.00105.59           O  
ANISOU  751  OG1 THR A 118    11539  16054  12528   1015   1626   3934       O  
ATOM    752  CG2 THR A 118      15.723  -7.633 -36.676  1.00108.54           C  
ANISOU  752  CG2 THR A 118    11576  16660  13005   1247   1746   4200       C  
ATOM    753  N   ALA A 119      15.810  -4.778 -33.929  1.00 96.69           N  
ANISOU  753  N   ALA A 119     9555  15352  11831   -274   1013   4316       N  
ATOM    754  CA  ALA A 119      16.386  -4.736 -32.587  1.00 97.24           C  
ANISOU  754  CA  ALA A 119     9389  15632  11927   -604    810   4489       C  
ATOM    755  C   ALA A 119      15.329  -4.476 -31.514  1.00 98.02           C  
ANISOU  755  C   ALA A 119     9834  15387  12023   -846    610   4111       C  
ATOM    756  O   ALA A 119      15.535  -4.882 -30.375  1.00 98.10           O  
ANISOU  756  O   ALA A 119     9759  15511  12006   -956    489   4165       O  
ATOM    757  CB  ALA A 119      17.474  -3.686 -32.514  1.00101.55           C  
ANISOU  757  CB  ALA A 119     9616  16502  12467  -1071    653   4885       C  
ATOM    758  N   SER A 120      14.201  -3.820 -31.869  1.00 92.48           N  
ANISOU  758  N   SER A 120     9508  14302  11327   -873    606   3779       N  
ATOM    759  CA  SER A 120      13.075  -3.571 -30.957  1.00 90.69           C  
ANISOU  759  CA  SER A 120     9608  13764  11085   -969    517   3468       C  
ATOM    760  C   SER A 120      12.399  -4.905 -30.643  1.00 91.60           C  
ANISOU  760  C   SER A 120     9714  13824  11267   -655    609   3348       C  
ATOM    761  O   SER A 120      12.124  -5.193 -29.483  1.00 90.47           O  
ANISOU  761  O   SER A 120     9619  13659  11095   -724    550   3299       O  
ATOM    762  CB  SER A 120      12.057  -2.627 -31.594  1.00 94.55           C  
ANISOU  762  CB  SER A 120    10415  13927  11581   -949    555   3254       C  
ATOM    763  OG  SER A 120      12.631  -1.394 -31.990  1.00109.36           O  
ANISOU  763  OG  SER A 120    12372  15774  13405  -1234    489   3375       O  
ATOM    764  N   VAL A 121      12.165  -5.718 -31.692  1.00 87.91           N  
ANISOU  764  N   VAL A 121     9236  13312  10855   -330    744   3315       N  
ATOM    765  CA  VAL A 121      11.563  -7.052 -31.654  1.00 87.62           C  
ANISOU  765  CA  VAL A 121     9269  13144  10879    -75    807   3216       C  
ATOM    766  C   VAL A 121      12.446  -7.984 -30.807  1.00 94.23           C  
ANISOU  766  C   VAL A 121     9912  14183  11708     14    846   3431       C  
ATOM    767  O   VAL A 121      11.949  -8.630 -29.881  1.00 93.36           O  
ANISOU  767  O   VAL A 121     9847  13984  11642     12    820   3385       O  
ATOM    768  CB  VAL A 121      11.343  -7.587 -33.101  1.00 92.33           C  
ANISOU  768  CB  VAL A 121    10022  13616  11443    198    897   3136       C  
ATOM    769  CG1 VAL A 121      10.886  -9.044 -33.108  1.00 92.66           C  
ANISOU  769  CG1 VAL A 121    10243  13451  11513    401    924   3046       C  
ATOM    770  CG2 VAL A 121      10.358  -6.708 -33.875  1.00 91.26           C  
ANISOU  770  CG2 VAL A 121    10046  13320  11307    113    819   2965       C  
ATOM    771  N   GLY A 122      13.744  -8.009 -31.124  1.00 94.12           N  
ANISOU  771  N   GLY A 122     9644  14480  11636    108    923   3728       N  
ATOM    772  CA  GLY A 122      14.758  -8.789 -30.423  1.00 96.42           C  
ANISOU  772  CA  GLY A 122     9656  15070  11910    245    973   4052       C  
ATOM    773  C   GLY A 122      14.898  -8.398 -28.964  1.00101.15           C  
ANISOU  773  C   GLY A 122    10131  15827  12474   -113    753   4126       C  
ATOM    774  O   GLY A 122      15.044  -9.279 -28.112  1.00102.43           O  
ANISOU  774  O   GLY A 122    10220  16067  12632     12    763   4249       O  
ATOM    775  N   SER A 123      14.820  -7.070 -28.659  1.00 96.69           N  
ANISOU  775  N   SER A 123     9631  15263  11845   -553    549   4042       N  
ATOM    776  CA  SER A 123      14.888  -6.519 -27.295  1.00 97.15           C  
ANISOU  776  CA  SER A 123     9750  15392  11770   -940    304   4041       C  
ATOM    777  C   SER A 123      13.777  -7.103 -26.432  1.00 98.60           C  
ANISOU  777  C   SER A 123    10198  15320  11945   -812    355   3802       C  
ATOM    778  O   SER A 123      14.017  -7.464 -25.280  1.00 99.73           O  
ANISOU  778  O   SER A 123    10301  15617  11974   -886    257   3916       O  
ATOM    779  CB  SER A 123      14.765  -4.998 -27.309  1.00100.76           C  
ANISOU  779  CB  SER A 123    10458  15699  12128  -1372    126   3898       C  
ATOM    780  OG  SER A 123      15.958  -4.367 -27.743  1.00111.48           O  
ANISOU  780  OG  SER A 123    11527  17360  13470  -1663     -9   4222       O  
ATOM    781  N   LEU A 124      12.570  -7.218 -27.011  1.00 92.09           N  
ANISOU  781  N   LEU A 124     9602  14154  11236   -627    502   3528       N  
ATOM    782  CA  LEU A 124      11.400  -7.775 -26.351  1.00 90.62           C  
ANISOU  782  CA  LEU A 124     9588  13754  11091   -511    582   3376       C  
ATOM    783  C   LEU A 124      11.496  -9.290 -26.209  1.00 94.75           C  
ANISOU  783  C   LEU A 124     9988  14297  11718   -249    683   3520       C  
ATOM    784  O   LEU A 124      10.978  -9.823 -25.224  1.00 94.74           O  
ANISOU  784  O   LEU A 124    10040  14252  11705   -229    710   3543       O  
ATOM    785  CB  LEU A 124      10.105  -7.366 -27.069  1.00 88.83           C  
ANISOU  785  CB  LEU A 124     9545  13234  10971   -444    664   3143       C  
ATOM    786  CG  LEU A 124       9.717  -5.886 -26.981  1.00 93.68           C  
ANISOU  786  CG  LEU A 124    10393  13732  11469   -610    630   3000       C  
ATOM    787  CD1 LEU A 124       8.461  -5.609 -27.770  1.00 92.62           C  
ANISOU  787  CD1 LEU A 124    10341  13389  11462   -460    728   2870       C  
ATOM    788  CD2 LEU A 124       9.523  -5.441 -25.540  1.00 97.99           C  
ANISOU  788  CD2 LEU A 124    11166  14262  11803   -724    609   2966       C  
ATOM    789  N   LEU A 125      12.166  -9.982 -27.178  1.00 90.94           N  
ANISOU  789  N   LEU A 125     9392  13853  11307    -14    773   3637       N  
ATOM    790  CA  LEU A 125      12.369 -11.438 -27.135  1.00 91.29           C  
ANISOU  790  CA  LEU A 125     9439  13831  11418    298    905   3782       C  
ATOM    791  C   LEU A 125      13.247 -11.792 -25.959  1.00 95.11           C  
ANISOU  791  C   LEU A 125     9696  14634  11808    314    869   4092       C  
ATOM    792  O   LEU A 125      12.963 -12.767 -25.270  1.00 95.41           O  
ANISOU  792  O   LEU A 125     9801  14568  11881    449    933   4176       O  
ATOM    793  CB  LEU A 125      12.963 -11.995 -28.448  1.00 92.56           C  
ANISOU  793  CB  LEU A 125     9645  13935  11587    632   1064   3839       C  
ATOM    794  CG  LEU A 125      13.333 -13.500 -28.484  1.00 99.66           C  
ANISOU  794  CG  LEU A 125    10674  14691  12500   1048   1253   4004       C  
ATOM    795  CD1 LEU A 125      12.133 -14.405 -28.173  1.00 99.40           C  
ANISOU  795  CD1 LEU A 125    10976  14211  12581    993   1226   3823       C  
ATOM    796  CD2 LEU A 125      13.929 -13.880 -29.814  1.00103.70           C  
ANISOU  796  CD2 LEU A 125    11342  15130  12931   1443   1460   4038       C  
ATOM    797  N   LEU A 126      14.293 -10.985 -25.717  1.00 92.10           N  
ANISOU  797  N   LEU A 126     9042  14649  11302    130    733   4296       N  
ATOM    798  CA  LEU A 126      15.193 -11.170 -24.587  1.00 94.46           C  
ANISOU  798  CA  LEU A 126     9074  15346  11470     59    605   4640       C  
ATOM    799  C   LEU A 126      14.470 -10.833 -23.278  1.00 96.34           C  
ANISOU  799  C   LEU A 126     9529  15512  11562   -217    452   4484       C  
ATOM    800  O   LEU A 126      14.691 -11.522 -22.286  1.00 97.55           O  
ANISOU  800  O   LEU A 126     9612  15823  11629   -134    430   4698       O  
ATOM    801  CB  LEU A 126      16.496 -10.362 -24.753  1.00 97.40           C  
ANISOU  801  CB  LEU A 126     9059  16198  11750   -167    430   4956       C  
ATOM    802  CG  LEU A 126      17.493 -10.835 -25.835  1.00104.51           C  
ANISOU  802  CG  LEU A 126     9618  17346  12746    218    650   5305       C  
ATOM    803  CD1 LEU A 126      18.599  -9.821 -26.034  1.00107.79           C  
ANISOU  803  CD1 LEU A 126     9607  18246  13104   -129    454   5642       C  
ATOM    804  CD2 LEU A 126      18.117 -12.180 -25.486  1.00109.96           C  
ANISOU  804  CD2 LEU A 126    10099  18231  13451    718    844   5698       C  
ATOM    805  N   ALA A 127      13.557  -9.829 -23.300  1.00 89.94           N  
ANISOU  805  N   ALA A 127     9018  14449  10708   -464    399   4136       N  
ATOM    806  CA  ALA A 127      12.729  -9.428 -22.155  1.00 89.50           C  
ANISOU  806  CA  ALA A 127     9260  14276  10471   -619    352   3969       C  
ATOM    807  C   ALA A 127      11.737 -10.545 -21.809  1.00 92.80           C  
ANISOU  807  C   ALA A 127     9749  14485  11027   -344    570   3964       C  
ATOM    808  O   ALA A 127      11.473 -10.780 -20.629  1.00 93.82           O  
ANISOU  808  O   ALA A 127     9977  14680  10992   -351    575   4041       O  
ATOM    809  CB  ALA A 127      11.981  -8.145 -22.470  1.00 88.89           C  
ANISOU  809  CB  ALA A 127     9495  13943  10335   -803    340   3649       C  
ATOM    810  N   ALA A 128      11.212 -11.244 -22.846  1.00 87.80           N  
ANISOU  810  N   ALA A 128     9093  13599  10670   -138    729   3898       N  
ATOM    811  CA  ALA A 128      10.298 -12.391 -22.742  1.00 87.27           C  
ANISOU  811  CA  ALA A 128     9095  13279  10786     32    886   3930       C  
ATOM    812  C   ALA A 128      11.043 -13.625 -22.202  1.00 93.15           C  
ANISOU  812  C   ALA A 128     9741  14122  11529    243    938   4239       C  
ATOM    813  O   ALA A 128      10.486 -14.356 -21.380  1.00 93.57           O  
ANISOU  813  O   ALA A 128     9859  14088  11607    292   1022   4362       O  
ATOM    814  CB  ALA A 128       9.689 -12.704 -24.103  1.00 86.53           C  
ANISOU  814  CB  ALA A 128     9081  12876  10922     98    939   3765       C  
ATOM    815  N   ILE A 129      12.300 -13.849 -22.673  1.00 90.71           N  
ANISOU  815  N   ILE A 129     9257  14016  11193    407    921   4423       N  
ATOM    816  CA  ILE A 129      13.188 -14.936 -22.243  1.00 93.18           C  
ANISOU  816  CA  ILE A 129     9436  14482  11486    707   1002   4795       C  
ATOM    817  C   ILE A 129      13.597 -14.685 -20.789  1.00 98.47           C  
ANISOU  817  C   ILE A 129     9959  15540  11917    559    847   5021       C  
ATOM    818  O   ILE A 129      13.619 -15.625 -19.989  1.00100.28           O  
ANISOU  818  O   ILE A 129    10195  15781  12125    743    927   5272       O  
ATOM    819  CB  ILE A 129      14.391 -15.118 -23.222  1.00 97.97           C  
ANISOU  819  CB  ILE A 129     9846  15266  12111    998   1083   4993       C  
ATOM    820  CG1 ILE A 129      13.954 -15.926 -24.471  1.00 98.14           C  
ANISOU  820  CG1 ILE A 129    10198  14795  12295   1293   1299   4817       C  
ATOM    821  CG2 ILE A 129      15.605 -15.784 -22.546  1.00102.82           C  
ANISOU  821  CG2 ILE A 129    10146  16291  12628   1287   1118   5506       C  
ATOM    822  CD1 ILE A 129      14.823 -15.737 -25.742  1.00105.29           C  
ANISOU  822  CD1 ILE A 129    11025  15809  13171   1563   1425   4872       C  
ATOM    823  N   ASP A 130      13.857 -13.407 -20.448  1.00 94.41           N  
ANISOU  823  N   ASP A 130     9390  15290  11192    203    613   4920       N  
ATOM    824  CA  ASP A 130      14.209 -12.953 -19.105  1.00 96.90           C  
ANISOU  824  CA  ASP A 130     9698  15943  11179    -36    386   5055       C  
ATOM    825  C   ASP A 130      13.107 -13.332 -18.111  1.00101.42           C  
ANISOU  825  C   ASP A 130    10556  16311  11669     10    515   4974       C  
ATOM    826  O   ASP A 130      13.406 -13.839 -17.026  1.00104.22           O  
ANISOU  826  O   ASP A 130    10880  16893  11825     71    468   5245       O  
ATOM    827  CB  ASP A 130      14.432 -11.432 -19.100  1.00 98.81           C  
ANISOU  827  CB  ASP A 130    10042  16299  11202   -482    113   4844       C  
ATOM    828  CG  ASP A 130      14.467 -10.807 -17.722  1.00112.73           C  
ANISOU  828  CG  ASP A 130    12055  18240  12538   -788   -136   4830       C  
ATOM    829  OD1 ASP A 130      15.510 -10.923 -17.046  1.00116.31           O  
ANISOU  829  OD1 ASP A 130    12285  19135  12773   -930   -409   5168       O  
ATOM    830  OD2 ASP A 130      13.448 -10.214 -17.316  1.00119.76           O  
ANISOU  830  OD2 ASP A 130    13380  18843  13281   -857    -52   4509       O  
ATOM    831  N   ARG A 131      11.841 -13.095 -18.497  1.00 95.21           N  
ANISOU  831  N   ARG A 131    10001  15143  11031     -1    688   4666       N  
ATOM    832  CA  ARG A 131      10.673 -13.387 -17.671  1.00 95.19           C  
ANISOU  832  CA  ARG A 131    10198  14978  10991     57    870   4648       C  
ATOM    833  C   ARG A 131      10.376 -14.878 -17.566  1.00 98.97           C  
ANISOU  833  C   ARG A 131    10600  15294  11711    297   1059   4912       C  
ATOM    834  O   ARG A 131       9.921 -15.312 -16.506  1.00 99.42           O  
ANISOU  834  O   ARG A 131    10733  15395  11647    355   1166   5094       O  
ATOM    835  CB  ARG A 131       9.445 -12.585 -18.136  1.00 93.67           C  
ANISOU  835  CB  ARG A 131    10179  14521  10890    -18    993   4338       C  
ATOM    836  CG  ARG A 131       9.433 -11.147 -17.604  1.00104.52           C  
ANISOU  836  CG  ARG A 131    11839  15982  11890   -195    892   4120       C  
ATOM    837  CD  ARG A 131       9.119 -11.109 -16.112  1.00115.52           C  
ANISOU  837  CD  ARG A 131    13489  17505  12897   -142    967   4220       C  
ATOM    838  NE  ARG A 131       9.794 -10.019 -15.407  1.00120.74           N  
ANISOU  838  NE  ARG A 131    14501  18312  13062   -372    718   4083       N  
ATOM    839  CZ  ARG A 131      11.028 -10.086 -14.920  1.00134.70           C  
ANISOU  839  CZ  ARG A 131    16203  20390  14586   -580    384   4243       C  
ATOM    840  NH1 ARG A 131      11.762 -11.176 -15.099  1.00118.53           N  
ANISOU  840  NH1 ARG A 131    13718  18558  12761   -486    325   4568       N  
ATOM    841  NH2 ARG A 131      11.549  -9.052 -14.275  1.00127.61           N  
ANISOU  841  NH2 ARG A 131    15699  19582  13206   -891     91   4106       N  
ATOM    842  N   TYR A 132      10.660 -15.663 -18.641  1.00 95.49           N  
ANISOU  842  N   TYR A 132    10078  14636  11567    448   1112   4944       N  
ATOM    843  CA  TYR A 132      10.469 -17.118 -18.648  1.00 97.39           C  
ANISOU  843  CA  TYR A 132    10379  14600  12022    667   1276   5178       C  
ATOM    844  C   TYR A 132      11.363 -17.754 -17.576  1.00102.89           C  
ANISOU  844  C   TYR A 132    10975  15594  12524    868   1275   5580       C  
ATOM    845  O   TYR A 132      10.863 -18.506 -16.738  1.00104.21           O  
ANISOU  845  O   TYR A 132    11230  15670  12696    932   1399   5802       O  
ATOM    846  CB  TYR A 132      10.743 -17.741 -20.045  1.00 99.21           C  
ANISOU  846  CB  TYR A 132    10700  14496  12497    832   1328   5092       C  
ATOM    847  CG  TYR A 132      10.753 -19.264 -20.047  1.00105.56           C  
ANISOU  847  CG  TYR A 132    11713  14935  13461   1087   1489   5335       C  
ATOM    848  CD1 TYR A 132       9.572 -19.987 -20.199  1.00107.47           C  
ANISOU  848  CD1 TYR A 132    12204  14698  13932    926   1547   5290       C  
ATOM    849  CD2 TYR A 132      11.937 -19.975 -19.859  1.00110.68           C  
ANISOU  849  CD2 TYR A 132    12311  15717  14026   1481   1579   5664       C  
ATOM    850  CE1 TYR A 132       9.571 -21.384 -20.162  1.00112.05           C  
ANISOU  850  CE1 TYR A 132    13081  14849  14644   1103   1673   5516       C  
ATOM    851  CE2 TYR A 132      11.943 -21.370 -19.803  1.00115.03           C  
ANISOU  851  CE2 TYR A 132    13149  15859  14697   1768   1763   5904       C  
ATOM    852  CZ  TYR A 132      10.760 -22.071 -19.968  1.00121.59           C  
ANISOU  852  CZ  TYR A 132    14332  16120  15746   1556   1802   5800       C  
ATOM    853  OH  TYR A 132      10.768 -23.446 -19.939  1.00125.67           O  
ANISOU  853  OH  TYR A 132    15240  16135  16375   1789   1962   6028       O  
ATOM    854  N   LEU A 133      12.675 -17.435 -17.606  1.00 98.98           N  
ANISOU  854  N   LEU A 133    10253  15495  11859    953   1126   5731       N  
ATOM    855  CA  LEU A 133      13.669 -17.944 -16.663  1.00101.96           C  
ANISOU  855  CA  LEU A 133    10439  16273  12030   1145   1065   6182       C  
ATOM    856  C   LEU A 133      13.330 -17.552 -15.226  1.00106.61           C  
ANISOU  856  C   LEU A 133    11107  17122  12278    944    950   6248       C  
ATOM    857  O   LEU A 133      13.453 -18.375 -14.318  1.00109.41           O  
ANISOU  857  O   LEU A 133    11459  17580  12529   1135   1018   6606       O  
ATOM    858  CB  LEU A 133      15.074 -17.432 -17.033  1.00103.25           C  
ANISOU  858  CB  LEU A 133    10236  16917  12078   1169    868   6368       C  
ATOM    859  CG  LEU A 133      15.653 -17.903 -18.363  1.00108.06           C  
ANISOU  859  CG  LEU A 133    10743  17378  12938   1512   1050   6428       C  
ATOM    860  CD1 LEU A 133      16.886 -17.106 -18.722  1.00109.93           C  
ANISOU  860  CD1 LEU A 133    10541  18165  13062   1430    852   6623       C  
ATOM    861  CD2 LEU A 133      15.978 -19.392 -18.343  1.00114.11           C  
ANISOU  861  CD2 LEU A 133    11579  17950  13826   2067   1333   6808       C  
ATOM    862  N   CYS A 134      12.881 -16.301 -15.038  1.00100.35           N  
ANISOU  862  N   CYS A 134    10454  16396  11279    600    805   5907       N  
ATOM    863  CA  CYS A 134      12.516 -15.716 -13.753  1.00101.46           C  
ANISOU  863  CA  CYS A 134    10818  16734  10997    427    716   5880       C  
ATOM    864  C   CYS A 134      11.346 -16.422 -13.076  1.00105.62           C  
ANISOU  864  C   CYS A 134    11534  17025  11574    587   1027   5974       C  
ATOM    865  O   CYS A 134      11.348 -16.579 -11.852  1.00108.39           O  
ANISOU  865  O   CYS A 134    12003  17608  11574    633   1025   6193       O  
ATOM    866  CB  CYS A 134      12.238 -14.229 -13.928  1.00100.01           C  
ANISOU  866  CB  CYS A 134    10864  16526  10608    102    565   5456       C  
ATOM    867  SG  CYS A 134      12.145 -13.307 -12.379  1.00107.64           S  
ANISOU  867  SG  CYS A 134    12275  17739  10884   -111    384   5380       S  
ATOM    868  N   LEU A 135      10.349 -16.838 -13.875  1.00 99.15           N  
ANISOU  868  N   LEU A 135    10731  15771  11170    638   1273   5847       N  
ATOM    869  CA  LEU A 135       9.129 -17.490 -13.406  1.00 99.31           C  
ANISOU  869  CA  LEU A 135    10843  15561  11328    708   1563   5991       C  
ATOM    870  C   LEU A 135       9.230 -19.018 -13.359  1.00105.31           C  
ANISOU  870  C   LEU A 135    11549  16107  12356    903   1699   6375       C  
ATOM    871  O   LEU A 135       8.748 -19.622 -12.397  1.00107.40           O  
ANISOU  871  O   LEU A 135    11871  16393  12544    983   1872   6686       O  
ATOM    872  CB  LEU A 135       7.942 -17.032 -14.272  1.00 96.27           C  
ANISOU  872  CB  LEU A 135    10471  14871  11237    570   1686   5706       C  
ATOM    873  CG  LEU A 135       7.083 -15.852 -13.770  1.00100.31           C  
ANISOU  873  CG  LEU A 135    11129  15501  11484    517   1797   5518       C  
ATOM    874  CD1 LEU A 135       7.919 -14.621 -13.408  1.00100.76           C  
ANISOU  874  CD1 LEU A 135    11399  15817  11068    433   1568   5268       C  
ATOM    875  CD2 LEU A 135       6.094 -15.445 -14.817  1.00 98.96           C  
ANISOU  875  CD2 LEU A 135    10869  15083  11647    423   1880   5307       C  
ATOM    876  N   ARG A 136       9.857 -19.638 -14.387  1.00101.05           N  
ANISOU  876  N   ARG A 136    10960  15336  12100   1013   1653   6371       N  
ATOM    877  CA  ARG A 136      10.035 -21.092 -14.483  1.00103.22           C  
ANISOU  877  CA  ARG A 136    11323  15284  12612   1250   1799   6701       C  
ATOM    878  C   ARG A 136      11.086 -21.595 -13.492  1.00110.33           C  
ANISOU  878  C   ARG A 136    12131  16549  13240   1543   1779   7140       C  
ATOM    879  O   ARG A 136      10.841 -22.582 -12.801  1.00112.59           O  
ANISOU  879  O   ARG A 136    12524  16691  13564   1691   1947   7506       O  
ATOM    880  CB  ARG A 136      10.341 -21.519 -15.936  1.00102.40           C  
ANISOU  880  CB  ARG A 136    11327  14769  12810   1346   1798   6518       C  
ATOM    881  CG  ARG A 136      10.601 -23.008 -16.158  1.00117.33           C  
ANISOU  881  CG  ARG A 136    13480  16200  14902   1648   1968   6810       C  
ATOM    882  CD  ARG A 136       9.386 -23.897 -16.032  1.00131.94           C  
ANISOU  882  CD  ARG A 136    15602  17511  17019   1435   2088   6909       C  
ATOM    883  NE  ARG A 136       9.774 -25.269 -15.706  1.00149.05           N  
ANISOU  883  NE  ARG A 136    18048  19326  19258   1750   2259   7314       N  
ATOM    884  CZ  ARG A 136       9.845 -25.754 -14.470  1.00170.54           C  
ANISOU  884  CZ  ARG A 136    20707  22238  21854   1884   2372   7756       C  
ATOM    885  NH1 ARG A 136       9.544 -24.987 -13.429  1.00158.83           N  
ANISOU  885  NH1 ARG A 136    18928  21296  20127   1728   2331   7826       N  
ATOM    886  NH2 ARG A 136      10.214 -27.010 -14.265  1.00164.54           N  
ANISOU  886  NH2 ARG A 136    20245  21098  21173   2208   2545   8137       N  
ATOM    887  N   TYR A 137      12.235 -20.905 -13.404  1.00107.93           N  
ANISOU  887  N   TYR A 137    11603  16743  12662   1591   1553   7154       N  
ATOM    888  CA  TYR A 137      13.315 -21.259 -12.479  1.00112.29           C  
ANISOU  888  CA  TYR A 137    11971  17773  12919   1829   1451   7624       C  
ATOM    889  C   TYR A 137      13.629 -20.036 -11.569  1.00117.14           C  
ANISOU  889  C   TYR A 137    12501  18974  13034   1524   1131   7538       C  
ATOM    890  O   TYR A 137      14.646 -19.368 -11.787  1.00117.54           O  
ANISOU  890  O   TYR A 137    12304  19432  12924   1419    840   7547       O  
ATOM    891  CB  TYR A 137      14.576 -21.767 -13.234  1.00115.54           C  
ANISOU  891  CB  TYR A 137    12151  18288  13461   2200   1449   7882       C  
ATOM    892  CG  TYR A 137      14.301 -22.609 -14.466  1.00117.00           C  
ANISOU  892  CG  TYR A 137    12580  17814  14061   2449   1723   7762       C  
ATOM    893  CD1 TYR A 137      14.042 -23.975 -14.360  1.00121.88           C  
ANISOU  893  CD1 TYR A 137    13499  17942  14868   2773   1997   8045       C  
ATOM    894  CD2 TYR A 137      14.333 -22.049 -15.742  1.00114.98           C  
ANISOU  894  CD2 TYR A 137    12329  17393  13967   2357   1695   7375       C  
ATOM    895  CE1 TYR A 137      13.794 -24.755 -15.491  1.00123.00           C  
ANISOU  895  CE1 TYR A 137    14021  17393  15320   2962   2207   7896       C  
ATOM    896  CE2 TYR A 137      14.088 -22.818 -16.880  1.00116.05           C  
ANISOU  896  CE2 TYR A 137    12797  16903  14393   2579   1916   7235       C  
ATOM    897  CZ  TYR A 137      13.822 -24.173 -16.750  1.00127.47           C  
ANISOU  897  CZ  TYR A 137    14619  17821  15992   2869   2158   7478       C  
ATOM    898  OH  TYR A 137      13.562 -24.927 -17.871  1.00129.37           O  
ANISOU  898  OH  TYR A 137    15338  17361  16454   3039   2334   7296       O  
ATOM    899  N   PRO A 138      12.763 -19.711 -10.564  1.00114.20           N  
ANISOU  899  N   PRO A 138    12372  18635  12386   1367   1181   7469       N  
ATOM    900  CA  PRO A 138      13.016 -18.522  -9.722  1.00115.30           C  
ANISOU  900  CA  PRO A 138    12625  19218  11966   1081    879   7317       C  
ATOM    901  C   PRO A 138      14.278 -18.538  -8.829  1.00123.94           C  
ANISOU  901  C   PRO A 138    13546  20934  12612   1080    517   7717       C  
ATOM    902  O   PRO A 138      14.952 -17.504  -8.871  1.00123.88           O  
ANISOU  902  O   PRO A 138    13496  21246  12328    745    127   7549       O  
ATOM    903  CB  PRO A 138      11.738 -18.380  -8.888  1.00117.60           C  
ANISOU  903  CB  PRO A 138    13269  19352  12062   1066   1139   7220       C  
ATOM    904  CG  PRO A 138      10.724 -19.243  -9.560  1.00120.01           C  
ANISOU  904  CG  PRO A 138    13539  19136  12926   1201   1519   7245       C  
ATOM    905  CD  PRO A 138      11.489 -20.358 -10.188  1.00116.06           C  
ANISOU  905  CD  PRO A 138    12823  18494  12782   1430   1526   7534       C  
ATOM    906  N   PRO A 139      14.656 -19.582  -8.019  1.00124.72           N  
ANISOU  906  N   PRO A 139    13539  21247  12601   1388    578   8264       N  
ATOM    907  CA  PRO A 139      15.888 -19.453  -7.212  1.00129.80           C  
ANISOU  907  CA  PRO A 139    13956  22581  12782   1331    148   8669       C  
ATOM    908  C   PRO A 139      17.189 -19.548  -8.020  1.00135.46           C  
ANISOU  908  C   PRO A 139    14123  23624  13723   1406    -72   8949       C  
ATOM    909  O   PRO A 139      18.233 -19.087  -7.552  1.00139.28           O  
ANISOU  909  O   PRO A 139    14329  24750  13842   1183   -541   9228       O  
ATOM    910  CB  PRO A 139      15.765 -20.585  -6.191  1.00135.39           C  
ANISOU  910  CB  PRO A 139    14718  23374  13351   1703    350   9196       C  
ATOM    911  CG  PRO A 139      14.975 -21.619  -6.880  1.00136.88           C  
ANISOU  911  CG  PRO A 139    14968  22907  14132   2033    862   9213       C  
ATOM    912  CD  PRO A 139      14.017 -20.899  -7.790  1.00126.92           C  
ANISOU  912  CD  PRO A 139    13897  21170  13155   1762    998   8585       C  
ATOM    913  N   SER A 140      17.118 -20.144  -9.228  1.00129.22           N  
ANISOU  913  N   SER A 140    13187  22409  13501   1712    261   8908       N  
ATOM    914  CA  SER A 140      18.248 -20.325 -10.140  1.00129.96           C  
ANISOU  914  CA  SER A 140    12790  22746  13845   1929    208   9193       C  
ATOM    915  C   SER A 140      18.294 -19.253 -11.241  1.00128.77           C  
ANISOU  915  C   SER A 140    12574  22501  13853   1576     81   8720       C  
ATOM    916  O   SER A 140      19.157 -19.328 -12.117  1.00129.17           O  
ANISOU  916  O   SER A 140    12222  22736  14121   1764     96   8936       O  
ATOM    917  CB  SER A 140      18.222 -21.726 -10.747  1.00134.41           C  
ANISOU  917  CB  SER A 140    13363  22867  14840   2581    692   9480       C  
ATOM    918  OG  SER A 140      18.315 -22.728  -9.747  1.00147.67           O  
ANISOU  918  OG  SER A 140    15078  24650  16379   2936    807  10004       O  
ATOM    919  N   TYR A 141      17.390 -18.247 -11.183  1.00120.98           N  
ANISOU  919  N   TYR A 141    11980  21251  12735   1117    -10   8128       N  
ATOM    920  CA  TYR A 141      17.331 -17.153 -12.156  1.00117.07           C  
ANISOU  920  CA  TYR A 141    11498  20624  12360    767   -128   7672       C  
ATOM    921  C   TYR A 141      18.591 -16.288 -12.111  1.00123.85           C  
ANISOU  921  C   TYR A 141    11961  22125  12973    388   -627   7896       C  
ATOM    922  O   TYR A 141      19.309 -16.218 -13.109  1.00123.44           O  
ANISOU  922  O   TYR A 141    11504  22211  13188    467   -615   8042       O  
ATOM    923  CB  TYR A 141      16.047 -16.303 -11.984  1.00114.90           C  
ANISOU  923  CB  TYR A 141    11764  19926  11965    449    -71   7066       C  
ATOM    924  CG  TYR A 141      16.088 -14.933 -12.640  1.00114.90           C  
ANISOU  924  CG  TYR A 141    11854  19881  11921     10   -299   6638       C  
ATOM    925  CD1 TYR A 141      15.954 -14.792 -14.020  1.00113.01           C  
ANISOU  925  CD1 TYR A 141    11499  19338  12100     74   -126   6413       C  
ATOM    926  CD2 TYR A 141      16.232 -13.777 -11.878  1.00118.17           C  
ANISOU  926  CD2 TYR A 141    12559  20503  11837   -471   -686   6453       C  
ATOM    927  CE1 TYR A 141      15.971 -13.535 -14.624  1.00111.95           C  
ANISOU  927  CE1 TYR A 141    11464  19141  11929   -313   -313   6057       C  
ATOM    928  CE2 TYR A 141      16.267 -12.516 -12.473  1.00117.73           C  
ANISOU  928  CE2 TYR A 141    12668  20325  11740   -884   -888   6076       C  
ATOM    929  CZ  TYR A 141      16.135 -12.400 -13.846  1.00121.29           C  
ANISOU  929  CZ  TYR A 141    12930  20503  12653   -794   -688   5900       C  
ATOM    930  OH  TYR A 141      16.167 -11.156 -14.427  1.00122.03           O  
ANISOU  930  OH  TYR A 141    13196  20464  12706  -1188   -871   5569       O  
ATOM    931  N   LYS A 142      18.873 -15.668 -10.946  1.00123.82           N  
ANISOU  931  N   LYS A 142    12084  22524  12436    -31  -1072   7966       N  
ATOM    932  CA  LYS A 142      20.007 -14.767 -10.713  1.00128.10           C  
ANISOU  932  CA  LYS A 142    12325  23684  12664   -576  -1679   8189       C  
ATOM    933  C   LYS A 142      21.367 -15.324 -11.179  1.00137.11           C  
ANISOU  933  C   LYS A 142    12619  25446  14030   -344  -1772   8914       C  
ATOM    934  O   LYS A 142      22.253 -14.538 -11.510  1.00139.48           O  
ANISOU  934  O   LYS A 142    12531  26181  14283   -793  -2176   9094       O  
ATOM    935  CB  LYS A 142      20.054 -14.321  -9.245  1.00134.84           C  
ANISOU  935  CB  LYS A 142    13552  24842  12839   -987  -2137   8212       C  
ATOM    936  CG  LYS A 142      19.056 -13.206  -8.941  1.00140.48           C  
ANISOU  936  CG  LYS A 142    15096  25062  13218  -1387  -2186   7493       C  
ATOM    937  CD  LYS A 142      19.011 -12.838  -7.462  1.00152.89           C  
ANISOU  937  CD  LYS A 142    17211  26850  14029  -1694  -2563   7472       C  
ATOM    938  CE  LYS A 142      18.336 -11.507  -7.210  1.00160.25           C  
ANISOU  938  CE  LYS A 142    19009  27351  14529  -2143  -2705   6805       C  
ATOM    939  NZ  LYS A 142      16.875 -11.540  -7.497  1.00162.76           N  
ANISOU  939  NZ  LYS A 142    19785  26991  15064  -1716  -2048   6325       N  
ATOM    940  N   ALA A 143      21.510 -16.665 -11.250  1.00135.48           N  
ANISOU  940  N   ALA A 143    12143  25254  14080    376  -1364   9355       N  
ATOM    941  CA  ALA A 143      22.721 -17.354 -11.712  1.00139.87           C  
ANISOU  941  CA  ALA A 143    11931  26355  14860    824  -1291  10104       C  
ATOM    942  C   ALA A 143      22.629 -17.697 -13.207  1.00140.53           C  
ANISOU  942  C   ALA A 143    11930  26006  15459   1298   -767   9965       C  
ATOM    943  O   ALA A 143      23.650 -17.666 -13.899  1.00142.78           O  
ANISOU  943  O   ALA A 143    11595  26753  15902   1468   -761  10431       O  
ATOM    944  CB  ALA A 143      22.953 -18.616 -10.893  1.00144.69           C  
ANISOU  944  CB  ALA A 143    12407  27178  15391   1412  -1117  10690       C  
ATOM    945  N   LEU A 144      21.408 -18.021 -13.700  1.00132.00           N  
ANISOU  945  N   LEU A 144    11467  24076  14611   1504   -337   9366       N  
ATOM    946  CA  LEU A 144      21.155 -18.346 -15.108  1.00128.71           C  
ANISOU  946  CA  LEU A 144    11148  23149  14607   1900    121   9133       C  
ATOM    947  C   LEU A 144      21.214 -17.091 -15.980  1.00131.20           C  
ANISOU  947  C   LEU A 144    11392  23481  14978   1409    -69   8762       C  
ATOM    948  O   LEU A 144      21.565 -17.186 -17.156  1.00130.45           O  
ANISOU  948  O   LEU A 144    11116  23314  15136   1712    196   8813       O  
ATOM    949  CB  LEU A 144      19.812 -19.063 -15.284  1.00124.28           C  
ANISOU  949  CB  LEU A 144    11258  21722  14243   2138    521   8657       C  
ATOM    950  N   LEU A 145      20.884 -15.919 -15.400  1.00127.50           N  
ANISOU  950  N   LEU A 145    11128  23080  14236    684   -504   8405       N  
ATOM    951  CA  LEU A 145      20.926 -14.621 -16.074  1.00125.83           C  
ANISOU  951  CA  LEU A 145    10929  22852  14031    142   -736   8065       C  
ATOM    952  C   LEU A 145      21.570 -13.551 -15.176  1.00135.10           C  
ANISOU  952  C   LEU A 145    11972  24564  14795   -609  -1389   8206       C  
ATOM    953  O   LEU A 145      21.014 -13.183 -14.135  1.00134.83           O  
ANISOU  953  O   LEU A 145    12418  24410  14400   -948  -1631   7928       O  
ATOM    954  CB  LEU A 145      19.534 -14.191 -16.555  1.00119.52           C  
ANISOU  954  CB  LEU A 145    10782  21284  13348     34   -519   7303       C  
ATOM    955  N   THR A 146      22.770 -13.089 -15.576  1.00136.69           N  
ANISOU  955  N   THR A 146    11535  25374  15028   -864  -1674   8687       N  
ATOM    956  CA  THR A 146      23.557 -12.065 -14.875  1.00142.43           C  
ANISOU  956  CA  THR A 146    12067  26656  15391  -1693  -2385   8917       C  
ATOM    957  C   THR A 146      23.675 -10.797 -15.736  1.00145.57           C  
ANISOU  957  C   THR A 146    12510  26918  15881  -2276  -2577   8651       C  
ATOM    958  O   THR A 146      23.363 -10.840 -16.931  1.00140.70           O  
ANISOU  958  O   THR A 146    11883  25949  15629  -1928  -2132   8445       O  
ATOM    959  CB  THR A 146      24.951 -12.610 -14.491  1.00160.59           C  
ANISOU  959  CB  THR A 146    13457  29914  17645  -1599  -2647   9883       C  
ATOM    960  OG1 THR A 146      25.622 -13.086 -15.659  1.00161.69           O  
ANISOU  960  OG1 THR A 146    12925  30304  18207  -1046  -2232  10352       O  
ATOM    961  CG2 THR A 146      24.892 -13.704 -13.432  1.00162.32           C  
ANISOU  961  CG2 THR A 146    13688  30311  17674  -1141  -2576  10187       C  
ATOM    962  N   ARG A 147      24.145  -9.676 -15.127  1.00147.03           N  
ANISOU  962  N   ARG A 147    12792  27366  15706  -3185  -3264   8674       N  
ATOM    963  CA  ARG A 147      24.353  -8.369 -15.772  1.00147.48           C  
ANISOU  963  CA  ARG A 147    12949  27297  15790  -3886  -3556   8484       C  
ATOM    964  C   ARG A 147      25.168  -8.514 -17.056  1.00151.73           C  
ANISOU  964  C   ARG A 147    12646  28220  16786  -3632  -3295   9009       C  
ATOM    965  O   ARG A 147      24.798  -7.935 -18.075  1.00147.41           O  
ANISOU  965  O   ARG A 147    12296  27247  16465  -3655  -3055   8666       O  
ATOM    966  CB  ARG A 147      25.055  -7.392 -14.804  1.00155.89           C  
ANISOU  966  CB  ARG A 147    14119  28743  16369  -4930  -4431   8665       C  
ATOM    967  CG  ARG A 147      25.125  -5.947 -15.295  1.00167.66           C  
ANISOU  967  CG  ARG A 147    15969  29922  17811  -5766  -4787   8374       C  
ATOM    968  CD  ARG A 147      26.449  -5.295 -14.933  1.00180.26           C  
ANISOU  968  CD  ARG A 147    17684  31190  19617  -5842  -5122   7885       C  
ATOM    969  NE  ARG A 147      27.189  -4.885 -16.129  1.00186.20           N  
ANISOU  969  NE  ARG A 147    18183  31532  21034  -5484  -4749   7531       N  
ATOM    970  CZ  ARG A 147      28.443  -5.237 -16.407  1.00194.98           C  
ANISOU  970  CZ  ARG A 147    19081  32252  22749  -4667  -4402   6995       C  
ATOM    971  NH1 ARG A 147      29.130  -6.002 -15.565  1.00185.97           N  
ANISOU  971  NH1 ARG A 147    17347  31916  21397  -4727  -4769   7709       N  
ATOM    972  NH2 ARG A 147      29.021  -4.824 -17.528  1.00184.35           N  
ANISOU  972  NH2 ARG A 147    16875  31577  21591  -5172  -4468   7830       N  
ATOM    973  N   GLY A 148      26.239  -9.306 -16.984  1.00153.66           N  
ANISOU  973  N   GLY A 148    11976  29274  17135  -3319  -3302   9863       N  
ATOM    974  CA  GLY A 148      27.142  -9.583 -18.095  1.00155.94           C  
ANISOU  974  CA  GLY A 148    11376  30070  17805  -2934  -2988  10525       C  
ATOM    975  C   GLY A 148      26.516 -10.430 -19.181  1.00153.44           C  
ANISOU  975  C   GLY A 148    11229  29238  17834  -1925  -2142  10248       C  
ATOM    976  O   GLY A 148      26.554 -10.051 -20.356  1.00151.41           O  
ANISOU  976  O   GLY A 148    10879  28834  17817  -1826  -1855  10186       O  
ATOM    977  N   ARG A 149      25.913 -11.574 -18.787  1.00146.62           N  
ANISOU  977  N   ARG A 149    10680  28063  16966  -1210  -1763  10075       N  
ATOM    978  CA  ARG A 149      25.243 -12.520 -19.686  1.00141.06           C  
ANISOU  978  CA  ARG A 149    10285  26781  16532   -296  -1022   9781       C  
ATOM    979  C   ARG A 149      24.147 -11.853 -20.512  1.00137.64           C  
ANISOU  979  C   ARG A 149    10549  25545  16204   -465   -847   8950       C  
ATOM    980  O   ARG A 149      23.996 -12.183 -21.689  1.00135.00           O  
ANISOU  980  O   ARG A 149    10254  24939  16099     61   -361   8857       O  
ATOM    981  CB  ARG A 149      24.673 -13.711 -18.905  1.00139.77           C  
ANISOU  981  CB  ARG A 149    10469  26337  16301    256   -790   9691       C  
ATOM    982  CG  ARG A 149      25.140 -15.054 -19.450  1.00151.30           C  
ANISOU  982  CG  ARG A 149    11620  27900  17967   1283   -195  10192       C  
ATOM    983  CD  ARG A 149      24.298 -16.211 -18.944  1.00156.89           C  
ANISOU  983  CD  ARG A 149    12902  28037  18672   1815    121   9932       C  
ATOM    984  NE  ARG A 149      24.579 -16.551 -17.546  1.00164.13           N  
ANISOU  984  NE  ARG A 149    13642  29375  19344   1693   -208  10312       N  
ATOM    985  CZ  ARG A 149      25.480 -17.447 -17.156  1.00176.53           C  
ANISOU  985  CZ  ARG A 149    14998  31126  20950   2190   -132  10668       C  
ATOM    986  NH1 ARG A 149      26.213 -18.097 -18.053  1.00164.79           N  
ANISOU  986  NH1 ARG A 149    12787  30208  19619   3029    393  11618       N  
ATOM    987  NH2 ARG A 149      25.659 -17.696 -15.866  1.00168.91           N  
ANISOU  987  NH2 ARG A 149    13658  30839  19680   2086   -439  11340       N  
ATOM    988  N   ALA A 150      23.407 -10.898 -19.901  1.00131.41           N  
ANISOU  988  N   ALA A 150    10332  24394  15206  -1167  -1238   8378       N  
ATOM    989  CA  ALA A 150      22.334 -10.134 -20.545  1.00125.56           C  
ANISOU  989  CA  ALA A 150    10242  22936  14530  -1364  -1122   7636       C  
ATOM    990  C   ALA A 150      22.883  -9.252 -21.661  1.00130.26           C  
ANISOU  990  C   ALA A 150    10543  23672  15277  -1627  -1142   7769       C  
ATOM    991  O   ALA A 150      22.297  -9.206 -22.743  1.00125.25           O  
ANISOU  991  O   ALA A 150    10161  22595  14833  -1325   -770   7425       O  
ATOM    992  CB  ALA A 150      21.610  -9.282 -19.516  1.00125.52           C  
ANISOU  992  CB  ALA A 150    10875  22613  14203  -1989  -1521   7140       C  
ATOM    993  N   LEU A 151      24.026  -8.581 -21.400  1.00133.35           N  
ANISOU  993  N   LEU A 151    10377  24716  15576  -2213  -1598   8323       N  
ATOM    994  CA  LEU A 151      24.724  -7.711 -22.347  1.00135.80           C  
ANISOU  994  CA  LEU A 151    10286  25284  16029  -2566  -1673   8618       C  
ATOM    995  C   LEU A 151      25.335  -8.522 -23.488  1.00141.55           C  
ANISOU  995  C   LEU A 151    10401  26347  17034  -1761  -1101   9124       C  
ATOM    996  O   LEU A 151      25.351  -8.046 -24.623  1.00140.04           O  
ANISOU  996  O   LEU A 151    10182  26032  16996  -1708   -863   9080       O  
ATOM    997  CB  LEU A 151      25.801  -6.875 -21.638  1.00143.36           C  
ANISOU  997  CB  LEU A 151    10773  26893  16805  -3489  -2380   9166       C  
ATOM    998  CG  LEU A 151      25.308  -5.832 -20.630  1.00148.54           C  
ANISOU  998  CG  LEU A 151    12183  27154  17100  -4390  -2992   8650       C  
ATOM    999  CD1 LEU A 151      26.413  -5.437 -19.689  1.00157.35           C  
ANISOU  999  CD1 LEU A 151    12837  28986  17962  -5209  -3738   9262       C  
ATOM   1000  CD2 LEU A 151      24.748  -4.600 -21.321  1.00148.44           C  
ANISOU 1000  CD2 LEU A 151    12764  26516  17120  -4843  -3023   8129       C  
ATOM   1001  N   VAL A 152      25.819  -9.750 -23.189  1.00141.50           N  
ANISOU 1001  N   VAL A 152     9973  26733  17056  -1079   -845   9607       N  
ATOM   1002  CA  VAL A 152      26.381 -10.689 -24.174  1.00143.69           C  
ANISOU 1002  CA  VAL A 152     9803  27269  17524   -133   -211  10092       C  
ATOM   1003  C   VAL A 152      25.248 -11.069 -25.148  1.00141.42           C  
ANISOU 1003  C   VAL A 152    10297  26108  17327    422    314   9352       C  
ATOM   1004  O   VAL A 152      25.437 -11.012 -26.365  1.00141.34           O  
ANISOU 1004  O   VAL A 152    10210  26072  17421    792    704   9433       O  
ATOM   1005  CB  VAL A 152      27.041 -11.932 -23.493  1.00152.33           C  
ANISOU 1005  CB  VAL A 152    10425  28866  18586    512    -53  10734       C  
ATOM   1006  CG1 VAL A 152      27.337 -13.047 -24.496  1.00153.57           C  
ANISOU 1006  CG1 VAL A 152    10463  29008  18880   1671    726  11046       C  
ATOM   1007  CG2 VAL A 152      28.315 -11.542 -22.749  1.00159.90           C  
ANISOU 1007  CG2 VAL A 152    10493  30782  19481    -10   -572  11553       C  
ATOM   1008  N   LEU A 153      24.057 -11.384 -24.591  1.00132.71           N  
ANISOU 1008  N   LEU A 153     9940  24325  16159    409    278   8657       N  
ATOM   1009  CA  LEU A 153      22.849 -11.722 -25.338  1.00126.65           C  
ANISOU 1009  CA  LEU A 153     9920  22737  15465    769    637   7952       C  
ATOM   1010  C   LEU A 153      22.349 -10.530 -26.141  1.00127.94           C  
ANISOU 1010  C   LEU A 153    10356  22593  15661    309    537   7520       C  
ATOM   1011  O   LEU A 153      21.830 -10.727 -27.239  1.00125.09           O  
ANISOU 1011  O   LEU A 153    10333  21821  15373    696    891   7216       O  
ATOM   1012  CB  LEU A 153      21.748 -12.216 -24.393  1.00122.93           C  
ANISOU 1012  CB  LEU A 153    10029  21749  14928    725    546   7454       C  
ATOM   1013  CG  LEU A 153      21.838 -13.671 -23.953  1.00129.47           C  
ANISOU 1013  CG  LEU A 153    10873  22551  15769   1394    832   7704       C  
ATOM   1014  CD1 LEU A 153      21.047 -13.897 -22.688  1.00127.68           C  
ANISOU 1014  CD1 LEU A 153    10999  22076  15436   1137    602   7426       C  
ATOM   1015  CD2 LEU A 153      21.348 -14.614 -25.045  1.00130.64           C  
ANISOU 1015  CD2 LEU A 153    11468  22137  16032   2101   1358   7466       C  
ATOM   1016  N   LEU A 154      22.513  -9.299 -25.599  1.00125.68           N  
ANISOU 1016  N   LEU A 154     9985  22480  15290   -519     42   7504       N  
ATOM   1017  CA  LEU A 154      22.128  -8.046 -26.258  1.00123.60           C  
ANISOU 1017  CA  LEU A 154     9991  21928  15044  -1008    -87   7165       C  
ATOM   1018  C   LEU A 154      22.972  -7.817 -27.514  1.00130.77           C  
ANISOU 1018  C   LEU A 154    10422  23190  16074   -807    171   7616       C  
ATOM   1019  O   LEU A 154      22.417  -7.591 -28.592  1.00127.43           O  
ANISOU 1019  O   LEU A 154    10328  22379  15710   -593    444   7289       O  
ATOM   1020  CB  LEU A 154      22.271  -6.846 -25.304  1.00125.66           C  
ANISOU 1020  CB  LEU A 154    10339  22270  15135  -1934   -687   7119       C  
ATOM   1021  CG  LEU A 154      21.174  -6.638 -24.275  1.00127.01           C  
ANISOU 1021  CG  LEU A 154    11215  21922  15119  -2183   -893   6512       C  
ATOM   1022  CD1 LEU A 154      21.596  -5.612 -23.249  1.00131.35           C  
ANISOU 1022  CD1 LEU A 154    11871  22632  15405  -3039  -1495   6578       C  
ATOM   1023  CD2 LEU A 154      19.866  -6.234 -24.931  1.00123.93           C  
ANISOU 1023  CD2 LEU A 154    11475  20818  14795  -2048   -657   5851       C  
ATOM   1024  N   GLY A 155      24.295  -7.909 -27.360  1.00133.55           N  
ANISOU 1024  N   GLY A 155     9975  24320  16448   -848     94   8414       N  
ATOM   1025  CA  GLY A 155      25.255  -7.760 -28.444  1.00137.76           C  
ANISOU 1025  CA  GLY A 155     9904  25351  17088   -604    384   9026       C  
ATOM   1026  C   GLY A 155      24.980  -8.713 -29.589  1.00140.40           C  
ANISOU 1026  C   GLY A 155    10472  25421  17451    400   1071   8909       C  
ATOM   1027  O   GLY A 155      24.857  -8.268 -30.730  1.00139.24           O  
ANISOU 1027  O   GLY A 155    10463  25117  17325    518   1319   8809       O  
ATOM   1028  N   ILE A 156      24.823 -10.027 -29.275  1.00137.00           N  
ANISOU 1028  N   ILE A 156    10198  24870  16986   1111   1362   8883       N  
ATOM   1029  CA  ILE A 156      24.520 -11.122 -30.219  1.00136.08           C  
ANISOU 1029  CA  ILE A 156    10498  24379  16829   2085   1985   8718       C  
ATOM   1030  C   ILE A 156      23.275 -10.785 -31.056  1.00132.74           C  
ANISOU 1030  C   ILE A 156    10889  23171  16375   2009   2043   7903       C  
ATOM   1031  O   ILE A 156      23.287 -10.935 -32.281  1.00132.24           O  
ANISOU 1031  O   ILE A 156    11032  22972  16241   2501   2447   7871       O  
ATOM   1032  CB  ILE A 156      24.410 -12.484 -29.452  1.00140.11           C  
ANISOU 1032  CB  ILE A 156    11181  24748  17305   2647   2143   8749       C  
ATOM   1033  CG1 ILE A 156      25.814 -13.027 -29.096  1.00148.29           C  
ANISOU 1033  CG1 ILE A 156    11357  26638  18347   3095   2317   9729       C  
ATOM   1034  CG2 ILE A 156      23.583 -13.541 -30.220  1.00138.66           C  
ANISOU 1034  CG2 ILE A 156    11835  23801  17047   3383   2605   8238       C  
ATOM   1035  CD1 ILE A 156      25.856 -14.012 -27.916  1.00157.54           C  
ANISOU 1035  CD1 ILE A 156    12505  27856  19496   3339   2247   9897       C  
ATOM   1036  N   MET A 157      22.229 -10.290 -30.376  1.00124.30           N  
ANISOU 1036  N   MET A 157    10257  21642  15330   1402   1638   7300       N  
ATOM   1037  CA  MET A 157      20.961  -9.859 -30.951  1.00118.90           C  
ANISOU 1037  CA  MET A 157    10250  20287  14639   1227   1597   6584       C  
ATOM   1038  C   MET A 157      21.175  -8.618 -31.839  1.00121.45           C  
ANISOU 1038  C   MET A 157    10446  20729  14968    884   1551   6644       C  
ATOM   1039  O   MET A 157      20.633  -8.579 -32.941  1.00119.49           O  
ANISOU 1039  O   MET A 157    10588  20142  14670   1149   1776   6347       O  
ATOM   1040  CB  MET A 157      19.948  -9.604 -29.818  1.00117.59           C  
ANISOU 1040  CB  MET A 157    10435  19753  14492    715   1215   6104       C  
ATOM   1041  CG  MET A 157      18.556  -9.222 -30.276  1.00116.94           C  
ANISOU 1041  CG  MET A 157    10972  19038  14422    575   1176   5444       C  
ATOM   1042  SD  MET A 157      18.317  -7.427 -30.346  1.00120.73           S  
ANISOU 1042  SD  MET A 157    11501  19473  14898   -156    850   5276       S  
ATOM   1043  CE  MET A 157      18.470  -6.986 -28.602  1.00118.61           C  
ANISOU 1043  CE  MET A 157    11150  19362  14554   -747    416   5326       C  
ATOM   1044  N   TRP A 158      21.976  -7.630 -31.372  1.00119.11           N  
ANISOU 1044  N   TRP A 158     9633  20908  14716    271   1235   7054       N  
ATOM   1045  CA  TRP A 158      22.296  -6.400 -32.113  1.00119.34           C  
ANISOU 1045  CA  TRP A 158     9505  21065  14772   -148   1157   7213       C  
ATOM   1046  C   TRP A 158      23.126  -6.666 -33.374  1.00125.16           C  
ANISOU 1046  C   TRP A 158     9873  22190  15491    429   1639   7721       C  
ATOM   1047  O   TRP A 158      22.931  -5.992 -34.383  1.00123.78           O  
ANISOU 1047  O   TRP A 158     9870  21869  15293    394   1764   7629       O  
ATOM   1048  CB  TRP A 158      23.022  -5.392 -31.213  1.00121.55           C  
ANISOU 1048  CB  TRP A 158     9359  21737  15086  -1015    648   7582       C  
ATOM   1049  CG  TRP A 158      22.101  -4.536 -30.401  1.00118.91           C  
ANISOU 1049  CG  TRP A 158     9610  20877  14694  -1678    210   6998       C  
ATOM   1050  CD1 TRP A 158      21.817  -4.669 -29.075  1.00121.25           C  
ANISOU 1050  CD1 TRP A 158    10092  21081  14897  -1977   -125   6796       C  
ATOM   1051  CD2 TRP A 158      21.349  -3.407 -30.861  1.00116.45           C  
ANISOU 1051  CD2 TRP A 158     9815  20057  14372  -2045    109   6575       C  
ATOM   1052  NE1 TRP A 158      20.929  -3.697 -28.681  1.00118.17           N  
ANISOU 1052  NE1 TRP A 158    10336  20144  14419  -2469   -392   6262       N  
ATOM   1053  CE2 TRP A 158      20.623  -2.907 -29.758  1.00118.52           C  
ANISOU 1053  CE2 TRP A 158    10588  19915  14527  -2510   -253   6125       C  
ATOM   1054  CE3 TRP A 158      21.214  -2.765 -32.105  1.00117.32           C  
ANISOU 1054  CE3 TRP A 158    10034  20015  14528  -1977    319   6561       C  
ATOM   1055  CZ2 TRP A 158      19.775  -1.796 -29.857  1.00115.89           C  
ANISOU 1055  CZ2 TRP A 158    10875  19015  14143  -2856   -380   5676       C  
ATOM   1056  CZ3 TRP A 158      20.386  -1.654 -32.199  1.00116.53           C  
ANISOU 1056  CZ3 TRP A 158    10508  19370  14399  -2375    147   6130       C  
ATOM   1057  CH2 TRP A 158      19.677  -1.182 -31.085  1.00115.65           C  
ANISOU 1057  CH2 TRP A 158    10904  18846  14193  -2784   -183   5698       C  
ATOM   1058  N   VAL A 159      24.055  -7.636 -33.302  1.00125.50           N  
ANISOU 1058  N   VAL A 159     9422  22741  15520   1010   1941   8295       N  
ATOM   1059  CA  VAL A 159      24.945  -8.049 -34.391  1.00130.09           C  
ANISOU 1059  CA  VAL A 159     9630  23763  16037   1733   2504   8881       C  
ATOM   1060  C   VAL A 159      24.143  -8.769 -35.484  1.00132.00           C  
ANISOU 1060  C   VAL A 159    10665  23400  16089   2492   2961   8345       C  
ATOM   1061  O   VAL A 159      24.293  -8.430 -36.659  1.00132.41           O  
ANISOU 1061  O   VAL A 159    10784  23495  16029   2754   3273   8448       O  
ATOM   1062  CB  VAL A 159      26.156  -8.865 -33.851  1.00139.82           C  
ANISOU 1062  CB  VAL A 159    10089  25737  17299   2174   2695   9710       C  
ATOM   1063  CG1 VAL A 159      26.852  -9.666 -34.948  1.00144.73           C  
ANISOU 1063  CG1 VAL A 159    10559  26652  17781   3257   3448  10204       C  
ATOM   1064  CG2 VAL A 159      27.151  -7.954 -33.143  1.00144.24           C  
ANISOU 1064  CG2 VAL A 159     9737  27056  18013   1356   2235  10421       C  
ATOM   1065  N   LEU A 160      23.263  -9.725 -35.090  1.00126.36           N  
ANISOU 1065  N   LEU A 160    10581  22109  15319   2773   2958   7778       N  
ATOM   1066  CA  LEU A 160      22.389 -10.456 -36.019  1.00124.52           C  
ANISOU 1066  CA  LEU A 160    11203  21222  14887   3341   3257   7212       C  
ATOM   1067  C   LEU A 160      21.351  -9.514 -36.632  1.00124.87           C  
ANISOU 1067  C   LEU A 160    11707  20824  14915   2856   3009   6640       C  
ATOM   1068  O   LEU A 160      20.909  -9.742 -37.760  1.00124.92           O  
ANISOU 1068  O   LEU A 160    12255  20501  14709   3254   3254   6359       O  
ATOM   1069  CB  LEU A 160      21.702 -11.653 -35.341  1.00122.42           C  
ANISOU 1069  CB  LEU A 160    11453  20452  14609   3595   3228   6814       C  
ATOM   1070  CG  LEU A 160      22.386 -13.011 -35.527  1.00132.35           C  
ANISOU 1070  CG  LEU A 160    12810  21765  15711   4547   3749   7162       C  
ATOM   1071  CD1 LEU A 160      22.085 -13.932 -34.365  1.00131.54           C  
ANISOU 1071  CD1 LEU A 160    12847  21425  15706   4569   3605   7054       C  
ATOM   1072  CD2 LEU A 160      21.979 -13.671 -36.843  1.00135.80           C  
ANISOU 1072  CD2 LEU A 160    14098  21667  15833   5217   4158   6810       C  
ATOM   1073  N   SER A 161      20.997  -8.438 -35.893  1.00118.42           N  
ANISOU 1073  N   SER A 161    10704  20007  14283   2026   2527   6500       N  
ATOM   1074  CA  SER A 161      20.081  -7.389 -36.333  1.00114.57           C  
ANISOU 1074  CA  SER A 161    10569  19154  13807   1555   2288   6061       C  
ATOM   1075  C   SER A 161      20.736  -6.653 -37.502  1.00120.92           C  
ANISOU 1075  C   SER A 161    11153  20266  14526   1649   2529   6436       C  
ATOM   1076  O   SER A 161      20.148  -6.588 -38.579  1.00119.50           O  
ANISOU 1076  O   SER A 161    11439  19786  14180   1904   2686   6146       O  
ATOM   1077  CB  SER A 161      19.792  -6.421 -35.187  1.00116.81           C  
ANISOU 1077  CB  SER A 161    10719  19402  14263    745   1798   5943       C  
ATOM   1078  OG  SER A 161      18.797  -5.471 -35.523  1.00125.69           O  
ANISOU 1078  OG  SER A 161    12257  20106  15394    388   1609   5508       O  
ATOM   1079  N   ALA A 162      21.990  -6.187 -37.310  1.00121.58           N  
ANISOU 1079  N   ALA A 162    10498  20994  14703   1467   2565   7144       N  
ATOM   1080  CA  ALA A 162      22.791  -5.481 -38.311  1.00125.17           C  
ANISOU 1080  CA  ALA A 162    10582  21865  15113   1514   2817   7677       C  
ATOM   1081  C   ALA A 162      23.096  -6.331 -39.541  1.00132.24           C  
ANISOU 1081  C   ALA A 162    11662  22851  15734   2479   3440   7839       C  
ATOM   1082  O   ALA A 162      23.073  -5.797 -40.647  1.00133.18           O  
ANISOU 1082  O   ALA A 162    11927  22969  15708   2607   3651   7897       O  
ATOM   1083  CB  ALA A 162      24.083  -4.974 -37.689  1.00131.00           C  
ANISOU 1083  CB  ALA A 162    10406  23333  16034   1071   2677   8486       C  
ATOM   1084  N   LEU A 163      23.366  -7.644 -39.357  1.00130.91           N  
ANISOU 1084  N   LEU A 163    11568  22718  15453   3186   3750   7906       N  
ATOM   1085  CA  LEU A 163      23.699  -8.574 -40.447  1.00135.15           C  
ANISOU 1085  CA  LEU A 163    12430  23268  15654   4208   4392   8045       C  
ATOM   1086  C   LEU A 163      22.569  -8.765 -41.454  1.00135.98           C  
ANISOU 1086  C   LEU A 163    13531  22677  15459   4446   4439   7313       C  
ATOM   1087  O   LEU A 163      22.801  -8.649 -42.659  1.00138.77           O  
ANISOU 1087  O   LEU A 163    14095  23115  15517   4911   4829   7456       O  
ATOM   1088  CB  LEU A 163      24.167  -9.936 -39.907  1.00138.20           C  
ANISOU 1088  CB  LEU A 163    12798  23727  15983   4900   4687   8244       C  
ATOM   1089  CG  LEU A 163      25.599 -10.008 -39.387  1.00149.25           C  
ANISOU 1089  CG  LEU A 163    13161  26012  17536   5090   4906   9228       C  
ATOM   1090  CD1 LEU A 163      25.723 -11.065 -38.316  1.00150.09           C  
ANISOU 1090  CD1 LEU A 163    13215  26088  17724   5354   4872   9273       C  
ATOM   1091  CD2 LEU A 163      26.587 -10.282 -40.508  1.00158.75           C  
ANISOU 1091  CD2 LEU A 163    14133  27708  18478   6017   5654   9908       C  
ATOM   1092  N   VAL A 164      21.353  -9.050 -40.959  1.00126.48           N  
ANISOU 1092  N   VAL A 164    12909  20834  14315   4114   4031   6581       N  
ATOM   1093  CA  VAL A 164      20.170  -9.267 -41.792  1.00123.53           C  
ANISOU 1093  CA  VAL A 164    13434  19818  13684   4207   3944   5899       C  
ATOM   1094  C   VAL A 164      19.673  -7.936 -42.396  1.00125.63           C  
ANISOU 1094  C   VAL A 164    13684  20073  13975   3693   3708   5782       C  
ATOM   1095  O   VAL A 164      19.223  -7.920 -43.542  1.00126.77           O  
ANISOU 1095  O   VAL A 164    14377  19992  13799   3965   3827   5547       O  
ATOM   1096  CB  VAL A 164      19.067 -10.051 -41.022  1.00122.83           C  
ANISOU 1096  CB  VAL A 164    13851  19131  13687   3997   3588   5287       C  
ATOM   1097  CG1 VAL A 164      17.841 -10.314 -41.895  1.00121.11           C  
ANISOU 1097  CG1 VAL A 164    14504  18306  13207   4015   3426   4656       C  
ATOM   1098  CG2 VAL A 164      19.612 -11.369 -40.479  1.00125.65           C  
ANISOU 1098  CG2 VAL A 164    14275  19462  14004   4551   3863   5455       C  
ATOM   1099  N   SER A 165      19.814  -6.824 -41.650  1.00119.61           N  
ANISOU 1099  N   SER A 165    12345  19549  13552   2978   3387   5978       N  
ATOM   1100  CA  SER A 165      19.365  -5.489 -42.062  1.00117.47           C  
ANISOU 1100  CA  SER A 165    12074  19214  13347   2459   3156   5905       C  
ATOM   1101  C   SER A 165      20.215  -4.795 -43.131  1.00125.18           C  
ANISOU 1101  C   SER A 165    12775  20610  14180   2642   3501   6447       C  
ATOM   1102  O   SER A 165      19.649  -4.229 -44.070  1.00124.03           O  
ANISOU 1102  O   SER A 165    12999  20267  13860   2645   3499   6263       O  
ATOM   1103  CB  SER A 165      19.233  -4.583 -40.849  1.00118.67           C  
ANISOU 1103  CB  SER A 165    11867  19367  13854   1656   2709   5903       C  
ATOM   1104  OG  SER A 165      18.300  -5.144 -39.941  1.00124.96           O  
ANISOU 1104  OG  SER A 165    12966  19764  14749   1514   2424   5395       O  
ATOM   1105  N   TYR A 166      21.535  -4.909 -43.054  1.00126.10           N  
ANISOU 1105  N   TYR A 166    12186  21349  14378   2770   3782   7178       N  
ATOM   1106  CA  TYR A 166      22.427  -4.289 -44.032  1.00130.74           C  
ANISOU 1106  CA  TYR A 166    12346  22458  14873   2930   4156   7863       C  
ATOM   1107  C   TYR A 166      22.839  -5.156 -45.213  1.00139.51           C  
ANISOU 1107  C   TYR A 166    13727  23738  15544   3970   4816   8062       C  
ATOM   1108  O   TYR A 166      23.687  -4.752 -45.988  1.00144.95           O  
ANISOU 1108  O   TYR A 166    14002  24954  16117   4270   5250   8736       O  
ATOM   1109  CB  TYR A 166      23.681  -3.768 -43.354  1.00135.09           C  
ANISOU 1109  CB  TYR A 166    11915  23656  15755   2430   4068   8645       C  
ATOM   1110  CG  TYR A 166      23.454  -2.544 -42.523  1.00133.29           C  
ANISOU 1110  CG  TYR A 166    11557  23236  15850   1367   3458   8519       C  
ATOM   1111  CD1 TYR A 166      22.902  -2.638 -41.271  1.00131.11           C  
ANISOU 1111  CD1 TYR A 166    11370  22679  15768    893   2987   8114       C  
ATOM   1112  CD2 TYR A 166      23.805  -1.297 -42.985  1.00136.09           C  
ANISOU 1112  CD2 TYR A 166    11753  23671  16283    857   3380   8835       C  
ATOM   1113  CE1 TYR A 166      22.703  -1.521 -40.494  1.00129.81           C  
ANISOU 1113  CE1 TYR A 166    11222  22282  15820    -18   2466   7978       C  
ATOM   1114  CE2 TYR A 166      23.608  -0.173 -42.217  1.00135.22           C  
ANISOU 1114  CE2 TYR A 166    11668  23286  16423    -94   2837   8706       C  
ATOM   1115  CZ  TYR A 166      23.053  -0.295 -40.969  1.00138.03           C  
ANISOU 1115  CZ  TYR A 166    12190  23334  16921   -508   2389   8259       C  
ATOM   1116  OH  TYR A 166      22.847   0.815 -40.189  1.00137.38           O  
ANISOU 1116  OH  TYR A 166    12265  22926  17007  -1382   1890   8107       O  
ATOM   1117  N   LEU A 167      22.252  -6.331 -45.370  1.00134.51           N  
ANISOU 1117  N   LEU A 167    13861  22615  14634   4507   4891   7472       N  
ATOM   1118  CA  LEU A 167      22.641  -7.203 -46.474  1.00139.25           C  
ANISOU 1118  CA  LEU A 167    15042  23152  14716   5521   5468   7465       C  
ATOM   1119  C   LEU A 167      22.442  -6.532 -47.821  1.00146.41           C  
ANISOU 1119  C   LEU A 167    16358  24067  15206   5815   5738   7493       C  
ATOM   1120  O   LEU A 167      23.262  -6.695 -48.724  1.00152.18           O  
ANISOU 1120  O   LEU A 167    17117  25136  15568   6637   6384   7952       O  
ATOM   1121  CB  LEU A 167      21.819  -8.488 -46.467  1.00136.52           C  
ANISOU 1121  CB  LEU A 167    15566  22111  14195   5762   5299   6713       C  
ATOM   1122  CG  LEU A 167      21.963  -9.464 -45.307  1.00146.72           C  
ANISOU 1122  CG  LEU A 167    17384  23291  15071   6790   5863   6766       C  
ATOM   1123  CD1 LEU A 167      20.953 -10.596 -45.426  1.00151.10           C  
ANISOU 1123  CD1 LEU A 167    17112  24446  15852   7154   6236   7517       C  
ATOM   1124  CD2 LEU A 167      23.384 -10.001 -45.291  1.00145.53           C  
ANISOU 1124  CD2 LEU A 167    18127  22354  14813   6768   5545   5987       C  
ATOM   1125  N   PRO A 168      21.296  -5.764 -47.954  1.00140.22           N  
ANISOU 1125  N   PRO A 168    15869  22969  14439   5248   5321   7095       N  
ATOM   1126  CA  PRO A 168      21.144  -5.129 -49.270  1.00143.92           C  
ANISOU 1126  CA  PRO A 168    16691  23515  14477   5580   5607   7213       C  
ATOM   1127  C   PRO A 168      22.248  -4.125 -49.466  1.00153.98           C  
ANISOU 1127  C   PRO A 168    17121  25485  15901   5494   5949   8110       C  
ATOM   1128  O   PRO A 168      22.813  -3.982 -50.543  1.00159.23           O  
ANISOU 1128  O   PRO A 168    17937  26417  16146   6081   6460   8467       O  
ATOM   1129  CB  PRO A 168      19.822  -4.388 -49.153  1.00139.89           C  
ANISOU 1129  CB  PRO A 168    16658  22487  14009   4972   5010   6573       C  
ATOM   1130  CG  PRO A 168      19.802  -3.948 -47.743  1.00138.66           C  
ANISOU 1130  CG  PRO A 168    16021  22220  14443   4166   4497   6443       C  
ATOM   1131  CD  PRO A 168      20.171  -5.227 -47.065  1.00134.88           C  
ANISOU 1131  CD  PRO A 168    15236  21879  14131   4374   4627   6575       C  
ATOM   1132  N   LEU A 169      22.570  -3.423 -48.393  1.00150.00           N  
ANISOU 1132  N   LEU A 169    15761  25265  15966   4734   5651   8491       N  
ATOM   1133  CA  LEU A 169      23.580  -2.401 -48.486  1.00155.12           C  
ANISOU 1133  CA  LEU A 169    15510  26568  16859   4417   5839   9397       C  
ATOM   1134  C   LEU A 169      24.854  -3.042 -48.953  1.00168.33           C  
ANISOU 1134  C   LEU A 169    16707  28899  18352   5220   6536  10138       C  
ATOM   1135  O   LEU A 169      25.560  -2.482 -49.777  1.00168.97           O  
ANISOU 1135  O   LEU A 169    16797  29003  18402   4995   6675  10119       O  
ATOM   1136  CB  LEU A 169      23.797  -1.738 -47.136  1.00152.06           C  
ANISOU 1136  CB  LEU A 169    14479  26231  17066   3397   5264   9514       C  
ATOM   1137  CG  LEU A 169      24.926  -0.714 -47.108  1.00160.37           C  
ANISOU 1137  CG  LEU A 169    14798  27695  18440   2641   5146  10248       C  
ATOM   1138  CD1 LEU A 169      24.787   0.204 -45.908  1.00155.91           C  
ANISOU 1138  CD1 LEU A 169    14171  26769  18298   1589   4431   9937       C  
ATOM   1139  CD2 LEU A 169      26.276  -1.403 -47.100  1.00169.35           C  
ANISOU 1139  CD2 LEU A 169    15066  29567  19714   2726   5480  11076       C  
ATOM   1140  N   MET A 170      25.155  -4.220 -48.437  1.00167.08           N  
ANISOU 1140  N   MET A 170    16567  28722  18196   5644   6638  10006       N  
ATOM   1141  CA  MET A 170      26.369  -4.890 -48.859  1.00168.42           C  
ANISOU 1141  CA  MET A 170    16806  28795  18390   5765   6821   9671       C  
ATOM   1142  C   MET A 170      26.262  -5.345 -50.314  1.00172.85           C  
ANISOU 1142  C   MET A 170    18360  28822  18493   6144   7060   8882       C  
ATOM   1143  O   MET A 170      26.073  -4.531 -51.209  1.00173.56           O  
ANISOU 1143  O   MET A 170    18384  28933  18628   6080   7223   8712       O  
ATOM   1144  CB  MET A 170      26.733  -6.041 -47.915  1.00169.57           C  
ANISOU 1144  CB  MET A 170    16874  28834  18719   5905   6692   9480       C  
ATOM   1145  CG  MET A 170      27.140  -5.598 -46.520  1.00171.18           C  
ANISOU 1145  CG  MET A 170    16255  29313  19474   5059   6174   9781       C  
ATOM   1146  SD  MET A 170      27.887  -3.958 -46.473  1.00175.03           S  
ANISOU 1146  SD  MET A 170    16081  29966  20457   3859   5800   9824       S  
ATOM   1147  CE  MET A 170      28.918  -3.999 -47.934  1.00173.83           C  
ANISOU 1147  CE  MET A 170    15827  29882  20340   4224   6103   9642       C  
ATOM   1148  N   GLY A 171      26.363  -6.645 -50.544  1.00171.10           N  
ANISOU 1148  N   GLY A 171    18904  28350  17757   6749   7216   8724       N  
ATOM   1149  CA  GLY A 171      26.317  -7.190 -51.881  1.00172.66           C  
ANISOU 1149  CA  GLY A 171    20027  28142  17432   7134   7431   8131       C  
ATOM   1150  C   GLY A 171      24.965  -7.603 -52.407  1.00175.95           C  
ANISOU 1150  C   GLY A 171    21573  27928  17353   7493   7285   7434       C  
ATOM   1151  O   GLY A 171      24.875  -8.124 -53.515  1.00176.95           O  
ANISOU 1151  O   GLY A 171    22471  27729  17034   7706   7388   6933       O  
ATOM   1152  N   TRP A 172      23.912  -7.393 -51.631  1.00173.05           N  
ANISOU 1152  N   TRP A 172    21279  27545  16927   7833   7213   7654       N  
ATOM   1153  CA  TRP A 172      22.599  -7.801 -52.099  1.00173.78           C  
ANISOU 1153  CA  TRP A 172    22537  27044  16448   8304   7117   7067       C  
ATOM   1154  C   TRP A 172      21.761  -6.645 -52.608  1.00175.05           C  
ANISOU 1154  C   TRP A 172    22970  26995  16546   7694   6627   6717       C  
ATOM   1155  O   TRP A 172      21.496  -5.695 -51.888  1.00168.56           O  
ANISOU 1155  O   TRP A 172    22296  25740  16011   6961   5936   6144       O  
ATOM   1156  CB  TRP A 172      21.836  -8.545 -51.004  1.00167.72           C  
ANISOU 1156  CB  TRP A 172    21999  25761  15966   8011   6671   6511       C  
ATOM   1157  CG  TRP A 172      20.736  -9.398 -51.553  1.00169.24           C  
ANISOU 1157  CG  TRP A 172    23503  25157  15643   8254   6457   5681       C  
ATOM   1158  CD1 TRP A 172      20.066  -9.207 -52.720  1.00175.03           C  
ANISOU 1158  CD1 TRP A 172    25214  25567  15724   8503   6435   5291       C  
ATOM   1159  CD2 TRP A 172      20.169 -10.566 -50.952  1.00167.22           C  
ANISOU 1159  CD2 TRP A 172    23735  24327  15475   8185   6175   5168       C  
ATOM   1160  NE1 TRP A 172      19.124 -10.187 -52.891  1.00175.04           N  
ANISOU 1160  NE1 TRP A 172    26289  24817  15399   8534   6111   4561       N  
ATOM   1161  CE2 TRP A 172      19.163 -11.033 -51.816  1.00173.30           C  
ANISOU 1161  CE2 TRP A 172    25789  24414  15642   8341   5963   4481       C  
ATOM   1162  CE3 TRP A 172      20.414 -11.263 -49.767  1.00165.42           C  
ANISOU 1162  CE3 TRP A 172    23003  24095  15754   7986   6065   5249       C  
ATOM   1163  CZ2 TRP A 172      18.403 -12.160 -51.536  1.00172.36           C  
ANISOU 1163  CZ2 TRP A 172    26451  23586  15453   8254   5642   3895       C  
ATOM   1164  CZ3 TRP A 172      19.659 -12.384 -49.493  1.00165.99           C  
ANISOU 1164  CZ3 TRP A 172    23835  23479  15755   7970   5797   4673       C  
ATOM   1165  CH2 TRP A 172      18.666 -12.822 -50.373  1.00169.45           C  
ANISOU 1165  CH2 TRP A 172    25540  23219  15626   8082   5590   4014       C  
ATOM   1166  N   THR A 173      21.347  -6.748 -53.864  1.00176.04           N  
ANISOU 1166  N   THR A 173    23180  27405  16304   7967   6968   7029       N  
ATOM   1167  CA  THR A 173      20.509  -5.752 -54.513  1.00174.64           C  
ANISOU 1167  CA  THR A 173    23311  27114  15929   7637   6655   6856       C  
ATOM   1168  C   THR A 173      19.805  -6.471 -55.655  1.00181.77           C  
ANISOU 1168  C   THR A 173    25469  27461  16134   7870   6505   6077       C  
ATOM   1169  O   THR A 173      20.222  -7.555 -56.047  1.00182.78           O  
ANISOU 1169  O   THR A 173    25964  27362  16121   7885   6606   5657       O  
ATOM   1170  CB  THR A 173      21.316  -4.543 -55.002  1.00180.31           C  
ANISOU 1170  CB  THR A 173    23305  28261  16942   7125   6750   7342       C  
ATOM   1171  OG1 THR A 173      22.265  -4.967 -55.980  1.00181.45           O  
ANISOU 1171  OG1 THR A 173    23481  28398  17064   6987   6954   7127       O  
ATOM   1172  CG2 THR A 173      22.058  -3.906 -53.847  1.00175.88           C  
ANISOU 1172  CG2 THR A 173    21570  28206  17052   6709   6734   8119       C  
ATOM   1173  N   CYS A 174      18.734  -5.902 -56.187  1.00178.45           N  
ANISOU 1173  N   CYS A 174    25629  26770  15405   7742   6083   5746       N  
ATOM   1174  CA  CYS A 174      18.028  -6.591 -57.271  1.00182.89           C  
ANISOU 1174  CA  CYS A 174    27448  26896  15146   8105   5951   5171       C  
ATOM   1175  C   CYS A 174      18.625  -6.295 -58.653  1.00186.90           C  
ANISOU 1175  C   CYS A 174    27962  27496  15554   7598   5935   4983       C  
ATOM   1176  O   CYS A 174      18.464  -5.198 -59.194  1.00186.40           O  
ANISOU 1176  O   CYS A 174    27697  27709  15419   7490   5928   5318       O  
ATOM   1177  CB  CYS A 174      16.522  -6.333 -57.228  1.00178.94           C  
ANISOU 1177  CB  CYS A 174    27307  25974  14710   7369   5075   4566       C  
ATOM   1178  SG  CYS A 174      16.052  -4.583 -57.263  1.00178.32           S  
ANISOU 1178  SG  CYS A 174    26418  26222  15113   6647   4725   4905       S  
ATOM   1179  N   CYS A 175      19.353  -7.279 -59.203  1.00186.22           N  
ANISOU 1179  N   CYS A 175    28180  27278  15299   7664   6140   4652       N  
ATOM   1180  CA  CYS A 175      19.968  -7.150 -60.521  1.00188.06           C  
ANISOU 1180  CA  CYS A 175    28469  27649  15335   7350   6235   4509       C  
ATOM   1181  C   CYS A 175      19.166  -7.993 -61.558  1.00193.19           C  
ANISOU 1181  C   CYS A 175    30012  27873  15518   6942   5740   3667       C  
ATOM   1182  O   CYS A 175      18.235  -7.408 -62.122  1.00193.68           O  
ANISOU 1182  O   CYS A 175    30468  27911  15210   6841   5417   3624       O  
ATOM   1183  CB  CYS A 175      21.462  -7.482 -60.494  1.00188.18           C  
ANISOU 1183  CB  CYS A 175    27857  27905  15738   7242   6639   4642       C  
ATOM   1184  SG  CYS A 175      22.379  -6.704 -59.136  1.00188.39           S  
ANISOU 1184  SG  CYS A 175    26636  28338  16607   7046   6823   5329       S  
ATOM   1185  N   PRO A 176      19.379  -9.324 -61.799  1.00192.31           N  
ANISOU 1185  N   PRO A 176    30385  27483  15202   7055   5796   3172       N  
ATOM   1186  CA  PRO A 176      18.491 -10.023 -62.748  1.00194.62           C  
ANISOU 1186  CA  PRO A 176    31502  27474  14972   6749   5355   2512       C  
ATOM   1187  C   PRO A 176      17.189 -10.489 -62.086  1.00197.23           C  
ANISOU 1187  C   PRO A 176    32314  27346  15280   6554   4755   2125       C  
ATOM   1188  O   PRO A 176      16.218 -10.784 -62.783  1.00198.93           O  
ANISOU 1188  O   PRO A 176    33134  27382  15069   6218   4267   1687       O  
ATOM   1189  CB  PRO A 176      19.343 -11.191 -63.252  1.00197.26           C  
ANISOU 1189  CB  PRO A 176    31751  27771  15426   6506   5519   2059       C  
ATOM   1190  CG  PRO A 176      20.404 -11.392 -62.216  1.00198.30           C  
ANISOU 1190  CG  PRO A 176    31122  27981  16244   6586   5828   2307       C  
ATOM   1191  CD  PRO A 176      20.378 -10.257 -61.232  1.00192.87           C  
ANISOU 1191  CD  PRO A 176    30082  27506  15694   7103   6069   3073       C  
ATOM   1192  N   ARG A 177      17.177 -10.537 -60.737  1.00192.73           N  
ANISOU 1192  N   ARG A 177    31706  26602  14920   7114   4941   2425       N  
ATOM   1193  CA  ARG A 177      16.046 -10.931 -59.895  1.00191.99           C  
ANISOU 1193  CA  ARG A 177    32205  26020  14722   7188   4504   2180       C  
ATOM   1194  C   ARG A 177      15.048  -9.768 -59.796  1.00193.65           C  
ANISOU 1194  C   ARG A 177    32376  26345  14857   7045   4100   2394       C  
ATOM   1195  O   ARG A 177      15.490  -8.617 -59.711  1.00191.73           O  
ANISOU 1195  O   ARG A 177    31498  26577  14775   7311   4453   3012       O  
ATOM   1196  CB  ARG A 177      16.539 -11.312 -58.487  1.00189.81           C  
ANISOU 1196  CB  ARG A 177    31571  25643  14906   7584   4824   2439       C  
ATOM   1197  CG  ARG A 177      17.387 -12.580 -58.431  1.00197.22           C  
ANISOU 1197  CG  ARG A 177    32036  26468  16429   7000   4816   1985       C  
ATOM   1198  CD  ARG A 177      18.412 -12.532 -57.309  1.00200.66           C  
ANISOU 1198  CD  ARG A 177    31414  27158  17670   6910   5077   2335       C  
ATOM   1199  NE  ARG A 177      19.603 -11.763 -57.681  1.00204.77           N  
ANISOU 1199  NE  ARG A 177    30951  28229  18625   6532   5301   2638       N  
ATOM   1200  CZ  ARG A 177      19.857 -10.519 -57.283  1.00211.38           C  
ANISOU 1200  CZ  ARG A 177    30873  29410  20030   5927   5127   2953       C  
ATOM   1201  NH1 ARG A 177      19.009  -9.885 -56.482  1.00202.47           N  
ANISOU 1201  NH1 ARG A 177    30016  28326  18588   6727   5304   3497       N  
ATOM   1202  NH2 ARG A 177      20.963  -9.903 -57.676  1.00200.80           N  
ANISOU 1202  NH2 ARG A 177    29287  28582  18426   6682   5881   3665       N  
ATOM   1203  N   PRO A 178      13.714 -10.034 -59.784  1.00192.65           N  
ANISOU 1203  N   PRO A 178    33150  25763  14285   6944   3462   2000       N  
ATOM   1204  CA  PRO A 178      12.741  -8.925 -59.699  1.00192.24           C  
ANISOU 1204  CA  PRO A 178    33160  25821  14061   6981   3073   2231       C  
ATOM   1205  C   PRO A 178      12.815  -8.105 -58.410  1.00186.32           C  
ANISOU 1205  C   PRO A 178    30987  25389  14416   6448   3029   2581       C  
ATOM   1206  O   PRO A 178      13.106  -8.651 -57.342  1.00182.28           O  
ANISOU 1206  O   PRO A 178    30127  24723  14409   6366   3124   2538       O  
ATOM   1207  CB  PRO A 178      11.386  -9.621 -59.859  1.00195.51           C  
ANISOU 1207  CB  PRO A 178    34373  25704  14209   6324   2136   1579       C  
ATOM   1208  CG  PRO A 178      11.628 -11.029 -59.453  1.00198.64           C  
ANISOU 1208  CG  PRO A 178    34820  25722  14933   5936   2103   1115       C  
ATOM   1209  CD  PRO A 178      13.027 -11.338 -59.889  1.00195.46           C  
ANISOU 1209  CD  PRO A 178    34159  25576  14531   6395   2904   1281       C  
ATOM   1210  N   CYS A 179      12.564  -6.785 -58.531  1.00179.07           N  
ANISOU 1210  N   CYS A 179    29329  24888  13822   6114   2896   2934       N  
ATOM   1211  CA  CYS A 179      12.596  -5.809 -57.434  1.00170.86           C  
ANISOU 1211  CA  CYS A 179    27073  24116  13731   5602   2841   3272       C  
ATOM   1212  C   CYS A 179      11.240  -5.693 -56.731  1.00167.69           C  
ANISOU 1212  C   CYS A 179    26435  23483  13797   4803   2035   2938       C  
ATOM   1213  O   CYS A 179      10.201  -5.944 -57.349  1.00169.81           O  
ANISOU 1213  O   CYS A 179    27289  23564  13668   4568   1466   2610       O  
ATOM   1214  CB  CYS A 179      13.078  -4.447 -57.935  1.00171.42           C  
ANISOU 1214  CB  CYS A 179    26576  24676  13881   5697   3171   3858       C  
ATOM   1215  SG  CYS A 179      14.689  -4.478 -58.770  1.00182.15           S  
ANISOU 1215  SG  CYS A 179    28034  26442  14733   6634   4177   4424       S  
ATOM   1216  N   SER A 180      11.256  -5.295 -55.442  1.00156.06           N  
ANISOU 1216  N   SER A 180    24090  22062  13143   4390   1989   3069       N  
ATOM   1217  CA  SER A 180      10.052  -5.111 -54.626  1.00150.10           C  
ANISOU 1217  CA  SER A 180    22982  21150  12897   3712   1352   2855       C  
ATOM   1218  C   SER A 180       9.350  -3.799 -54.958  1.00150.39           C  
ANISOU 1218  C   SER A 180    22637  21422  13083   3438   1092   3098       C  
ATOM   1219  O   SER A 180      10.008  -2.766 -55.097  1.00149.43           O  
ANISOU 1219  O   SER A 180    22099  21574  13106   3577   1471   3523       O  
ATOM   1220  CB  SER A 180      10.382  -5.193 -53.140  1.00147.71           C  
ANISOU 1220  CB  SER A 180    22002  20805  13315   3464   1460   2907       C  
ATOM   1221  OG  SER A 180      11.429  -4.311 -52.770  1.00153.93           O  
ANISOU 1221  OG  SER A 180    22134  21913  14440   3579   1944   3373       O  
ATOM   1222  N   GLU A 181       8.014  -3.847 -55.097  1.00145.37           N  
ANISOU 1222  N   GLU A 181    22137  20685  12410   3047    444   2882       N  
ATOM   1223  CA  GLU A 181       7.192  -2.683 -55.440  1.00143.99           C  
ANISOU 1223  CA  GLU A 181    21634  20730  12344   2846    160   3134       C  
ATOM   1224  C   GLU A 181       6.914  -1.750 -54.243  1.00140.11           C  
ANISOU 1224  C   GLU A 181    20311  20279  12645   2528    170   3351       C  
ATOM   1225  O   GLU A 181       6.347  -0.667 -54.430  1.00139.62           O  
ANISOU 1225  O   GLU A 181    19961  20364  12723   2451     53   3622       O  
ATOM   1226  CB  GLU A 181       5.893  -3.116 -56.139  1.00149.27           C  
ANISOU 1226  CB  GLU A 181    22743  21365  12610   2587   -548   2910       C  
ATOM   1227  CG  GLU A 181       6.093  -3.494 -57.598  1.00166.32           C  
ANISOU 1227  CG  GLU A 181    25773  23554  13865   2927   -573   2810       C  
ATOM   1228  CD  GLU A 181       4.829  -3.658 -58.422  1.00191.19           C  
ANISOU 1228  CD  GLU A 181    29316  26766  16561   2618  -1338   2695       C  
ATOM   1229  OE1 GLU A 181       3.953  -4.461 -58.025  1.00186.91           O  
ANISOU 1229  OE1 GLU A 181    28869  26036  16113   2140  -1921   2420       O  
ATOM   1230  OE2 GLU A 181       4.724  -2.994 -59.480  1.00187.56           O  
ANISOU 1230  OE2 GLU A 181    29061  26568  15635   2829  -1374   2923       O  
ATOM   1231  N   LEU A 182       7.341  -2.152 -53.029  1.00130.72           N  
ANISOU 1231  N   LEU A 182    18800  18942  11925   2391    337   3248       N  
ATOM   1232  CA  LEU A 182       7.171  -1.356 -51.813  1.00124.78           C  
ANISOU 1232  CA  LEU A 182    17393  18174  11843   2114    376   3402       C  
ATOM   1233  C   LEU A 182       8.449  -0.587 -51.494  1.00124.90           C  
ANISOU 1233  C   LEU A 182    17098  18284  12075   2235    906   3717       C  
ATOM   1234  O   LEU A 182       8.375   0.586 -51.140  1.00122.64           O  
ANISOU 1234  O   LEU A 182    16475  18012  12111   2091    972   3973       O  
ATOM   1235  CB  LEU A 182       6.774  -2.230 -50.601  1.00121.79           C  
ANISOU 1235  CB  LEU A 182    16845  17597  11831   1829    176   3125       C  
ATOM   1236  CG  LEU A 182       5.529  -3.122 -50.705  1.00128.19           C  
ANISOU 1236  CG  LEU A 182    17883  18300  12525   1573   -386   2856       C  
ATOM   1237  CD1 LEU A 182       5.456  -4.066 -49.529  1.00125.61           C  
ANISOU 1237  CD1 LEU A 182    17429  17763  12534   1347   -450   2637       C  
ATOM   1238  CD2 LEU A 182       4.244  -2.302 -50.783  1.00131.24           C  
ANISOU 1238  CD2 LEU A 182    17944  18845  13075   1372   -759   3050       C  
ATOM   1239  N   PHE A 183       9.613  -1.254 -51.604  1.00121.52           N  
ANISOU 1239  N   PHE A 183    16795  17913  11466   2494   1278   3734       N  
ATOM   1240  CA  PHE A 183      10.919  -0.663 -51.313  1.00120.70           C  
ANISOU 1240  CA  PHE A 183    16315  17986  11560   2566   1755   4116       C  
ATOM   1241  C   PHE A 183      11.829  -0.641 -52.551  1.00129.54           C  
ANISOU 1241  C   PHE A 183    17684  19357  12177   3031   2171   4405       C  
ATOM   1242  O   PHE A 183      11.967  -1.666 -53.224  1.00132.45           O  
ANISOU 1242  O   PHE A 183    18560  19712  12053   3415   2258   4210       O  
ATOM   1243  CB  PHE A 183      11.623  -1.406 -50.161  1.00119.88           C  
ANISOU 1243  CB  PHE A 183    15938  17846  11765   2491   1898   4045       C  
ATOM   1244  CG  PHE A 183      10.853  -1.530 -48.868  1.00116.39           C  
ANISOU 1244  CG  PHE A 183    15266  17181  11777   2085   1562   3787       C  
ATOM   1245  CD1 PHE A 183      10.837  -0.490 -47.946  1.00116.24           C  
ANISOU 1245  CD1 PHE A 183    14833  17127  12205   1729   1529   3949       C  
ATOM   1246  CD2 PHE A 183      10.187  -2.707 -48.547  1.00117.31           C  
ANISOU 1246  CD2 PHE A 183    15630  17095  11846   2062   1302   3402       C  
ATOM   1247  CE1 PHE A 183      10.154  -0.617 -46.736  1.00113.49           C  
ANISOU 1247  CE1 PHE A 183    14319  16590  12213   1432   1285   3729       C  
ATOM   1248  CE2 PHE A 183       9.497  -2.831 -47.339  1.00116.40           C  
ANISOU 1248  CE2 PHE A 183    15265  16820  12143   1716   1045   3231       C  
ATOM   1249  CZ  PHE A 183       9.485  -1.784 -46.443  1.00111.74           C  
ANISOU 1249  CZ  PHE A 183    14257  16240  11958   1442   1062   3396       C  
ATOM   1250  N   PRO A 184      12.486   0.504 -52.847  1.00127.24           N  
ANISOU 1250  N   PRO A 184    17087  19275  11983   3012   2458   4892       N  
ATOM   1251  CA  PRO A 184      13.377   0.559 -54.020  1.00132.20           C  
ANISOU 1251  CA  PRO A 184    17891  20204  12135   3483   2917   5258       C  
ATOM   1252  C   PRO A 184      14.710  -0.148 -53.804  1.00137.31           C  
ANISOU 1252  C   PRO A 184    18328  21093  12750   3801   3413   5497       C  
ATOM   1253  O   PRO A 184      15.197  -0.211 -52.675  1.00134.18           O  
ANISOU 1253  O   PRO A 184    17436  20713  12831   3520   3430   5574       O  
ATOM   1254  CB  PRO A 184      13.596   2.063 -54.246  1.00134.85           C  
ANISOU 1254  CB  PRO A 184    17897  20655  12687   3254   3030   5757       C  
ATOM   1255  CG  PRO A 184      12.756   2.775 -53.233  1.00134.73           C  
ANISOU 1255  CG  PRO A 184    17650  20336  13205   2719   2625   5592       C  
ATOM   1256  CD  PRO A 184      12.429   1.803 -52.154  1.00126.38           C  
ANISOU 1256  CD  PRO A 184    16534  19100  12385   2565   2388   5148       C  
ATOM   1257  N   LEU A 185      15.296  -0.673 -54.903  1.00138.93           N  
ANISOU 1257  N   LEU A 185    18926  21510  12350   4432   3832   5649       N  
ATOM   1258  CA  LEU A 185      16.605  -1.350 -54.999  1.00142.83           C  
ANISOU 1258  CA  LEU A 185    19280  22319  12671   4962   4443   5998       C  
ATOM   1259  C   LEU A 185      16.710  -2.715 -54.272  1.00145.42           C  
ANISOU 1259  C   LEU A 185    19786  22448  13017   5161   4440   5626       C  
ATOM   1260  O   LEU A 185      17.723  -3.402 -54.440  1.00149.65           O  
ANISOU 1260  O   LEU A 185    20311  23221  13326   5746   4983   5905       O  
ATOM   1261  CB  LEU A 185      17.763  -0.426 -54.547  1.00143.81           C  
ANISOU 1261  CB  LEU A 185    18505  22870  13268   4723   4785   6742       C  
ATOM   1262  CG  LEU A 185      17.886   0.938 -55.235  1.00150.84           C  
ANISOU 1262  CG  LEU A 185    19185  23952  14174   4523   4880   7240       C  
ATOM   1263  CD1 LEU A 185      18.531   1.948 -54.312  1.00149.75           C  
ANISOU 1263  CD1 LEU A 185    18229  23960  14710   3859   4840   7733       C  
ATOM   1264  CD2 LEU A 185      18.650   0.838 -56.551  1.00160.66           C  
ANISOU 1264  CD2 LEU A 185    20632  25602  14810   5238   5504   7715       C  
ATOM   1265  N   ILE A 186      15.677  -3.116 -53.503  1.00136.22           N  
ANISOU 1265  N   ILE A 186    18788  20866  12103   4733   3877   5058       N  
ATOM   1266  CA  ILE A 186      15.654  -4.372 -52.743  1.00134.40           C  
ANISOU 1266  CA  ILE A 186    18749  20381  11938   4834   3814   4702       C  
ATOM   1267  C   ILE A 186      14.831  -5.467 -53.479  1.00140.45           C  
ANISOU 1267  C   ILE A 186    20550  20721  12093   5120   3590   4117       C  
ATOM   1268  O   ILE A 186      13.750  -5.162 -53.991  1.00139.40           O  
ANISOU 1268  O   ILE A 186    20777  20406  11784   4836   3122   3824       O  
ATOM   1269  CB  ILE A 186      15.190  -4.080 -51.281  1.00130.78           C  
ANISOU 1269  CB  ILE A 186    17719  19779  12191   4138   3387   4560       C  
ATOM   1270  CG1 ILE A 186      16.389  -3.657 -50.405  1.00130.46           C  
ANISOU 1270  CG1 ILE A 186    16841  20116  12610   4017   3695   5099       C  
ATOM   1271  CG2 ILE A 186      14.413  -5.236 -50.636  1.00129.35           C  
ANISOU 1271  CG2 ILE A 186    17928  19169  12050   4032   3035   4005       C  
ATOM   1272  CD1 ILE A 186      16.112  -2.502 -49.448  1.00131.27           C  
ANISOU 1272  CD1 ILE A 186    16367  20212  13296   3277   3353   5198       C  
ATOM   1273  N   PRO A 187      15.326  -6.733 -53.557  1.00140.40           N  
ANISOU 1273  N   PRO A 187    21068  20541  11737   5674   3900   3970       N  
ATOM   1274  CA  PRO A 187      14.556  -7.782 -54.253  1.00143.82           C  
ANISOU 1274  CA  PRO A 187    22629  20472  11545   5867   3635   3389       C  
ATOM   1275  C   PRO A 187      13.459  -8.417 -53.396  1.00143.79           C  
ANISOU 1275  C   PRO A 187    22779  19997  11858   5266   2981   2868       C  
ATOM   1276  O   PRO A 187      13.388  -8.159 -52.194  1.00137.86           O  
ANISOU 1276  O   PRO A 187    21282  19309  11787   4824   2829   2953       O  
ATOM   1277  CB  PRO A 187      15.626  -8.808 -54.628  1.00152.00           C  
ANISOU 1277  CB  PRO A 187    24193  21474  12088   6762   4319   3506       C  
ATOM   1278  CG  PRO A 187      16.662  -8.666 -53.580  1.00153.97           C  
ANISOU 1278  CG  PRO A 187    23461  22100  12939   6833   4724   4012       C  
ATOM   1279  CD  PRO A 187      16.592  -7.271 -53.014  1.00143.76           C  
ANISOU 1279  CD  PRO A 187    21122  21200  12300   6149   4488   4354       C  
ATOM   1280  N   ASN A 188      12.617  -9.264 -54.020  1.00143.94           N  
ANISOU 1280  N   ASN A 188    23798  19543  11350   5233   2586   2355       N  
ATOM   1281  CA  ASN A 188      11.527  -9.994 -53.362  1.00141.60           C  
ANISOU 1281  CA  ASN A 188    23746  18780  11273   4643   1941   1895       C  
ATOM   1282  C   ASN A 188      12.086 -11.106 -52.459  1.00144.52           C  
ANISOU 1282  C   ASN A 188    24223  18852  11836   4870   2208   1816       C  
ATOM   1283  O   ASN A 188      11.539 -11.361 -51.385  1.00139.46           O  
ANISOU 1283  O   ASN A 188    23213  18045  11729   4355   1860   1693       O  
ATOM   1284  CB  ASN A 188      10.580 -10.606 -54.412  1.00149.32           C  
ANISOU 1284  CB  ASN A 188    25837  19349  11551   4511   1422   1429       C  
ATOM   1285  CG  ASN A 188       9.589  -9.661 -55.067  1.00174.13           C  
ANISOU 1285  CG  ASN A 188    28827  22726  14607   4054    883   1446       C  
ATOM   1286  OD1 ASN A 188       8.467 -10.050 -55.407  1.00172.64           O  
ANISOU 1286  OD1 ASN A 188    29141  22272  14182   3571    190   1116       O  
ATOM   1287  ND2 ASN A 188       9.967  -8.411 -55.285  1.00163.05           N  
ANISOU 1287  ND2 ASN A 188    26745  21827  13379   4178   1163   1872       N  
ATOM   1288  N   ASP A 189      13.179 -11.758 -52.908  1.00145.80           N  
ANISOU 1288  N   ASP A 189    24890  18966  11540   5701   2867   1936       N  
ATOM   1289  CA  ASP A 189      13.852 -12.853 -52.209  1.00146.75           C  
ANISOU 1289  CA  ASP A 189    25206  18814  11737   6116   3240   1938       C  
ATOM   1290  C   ASP A 189      14.489 -12.434 -50.888  1.00143.50           C  
ANISOU 1290  C   ASP A 189    23585  18826  12114   5975   3455   2375       C  
ATOM   1291  O   ASP A 189      14.459 -13.218 -49.938  1.00141.69           O  
ANISOU 1291  O   ASP A 189    23333  18319  12182   5881   3392   2272       O  
ATOM   1292  CB  ASP A 189      14.870 -13.539 -53.130  1.00156.98           C  
ANISOU 1292  CB  ASP A 189    27344  20016  12286   7170   3972   2042       C  
ATOM   1293  CG  ASP A 189      14.270 -14.061 -54.424  1.00173.94           C  
ANISOU 1293  CG  ASP A 189    30899  21659  13533   7334   3746   1551       C  
ATOM   1294  OD1 ASP A 189      13.138 -14.599 -54.384  1.00174.53           O  
ANISOU 1294  OD1 ASP A 189    31608  21178  13529   6697   3021   1021       O  
ATOM   1295  OD2 ASP A 189      14.932 -13.934 -55.475  1.00184.97           O  
ANISOU 1295  OD2 ASP A 189    32613  23273  14395   7918   4219   1691       O  
ATOM   1296  N   TYR A 190      15.048 -11.207 -50.817  1.00136.45           N  
ANISOU 1296  N   TYR A 190    21736  18574  11535   5913   3671   2865       N  
ATOM   1297  CA  TYR A 190      15.648 -10.677 -49.590  1.00131.21           C  
ANISOU 1297  CA  TYR A 190    19952  18330  11572   5665   3784   3287       C  
ATOM   1298  C   TYR A 190      14.568 -10.318 -48.562  1.00129.07           C  
ANISOU 1298  C   TYR A 190    19266  17902  11871   4786   3125   3021       C  
ATOM   1299  O   TYR A 190      14.760 -10.574 -47.369  1.00125.72           O  
ANISOU 1299  O   TYR A 190    18368  17501  11901   4596   3095   3108       O  
ATOM   1300  CB  TYR A 190      16.569  -9.477 -49.878  1.00132.19           C  
ANISOU 1300  CB  TYR A 190    19284  19124  11817   5783   4164   3904       C  
ATOM   1301  CG  TYR A 190      16.892  -8.647 -48.651  1.00128.02           C  
ANISOU 1301  CG  TYR A 190    17666  18971  12004   5228   4035   4254       C  
ATOM   1302  CD1 TYR A 190      17.745  -9.126 -47.664  1.00129.84           C  
ANISOU 1302  CD1 TYR A 190    17389  19405  12537   5380   4278   4568       C  
ATOM   1303  CD2 TYR A 190      16.313  -7.395 -48.464  1.00124.22           C  
ANISOU 1303  CD2 TYR A 190    16736  18604  11856   4555   3647   4264       C  
ATOM   1304  CE1 TYR A 190      18.017  -8.381 -46.519  1.00125.84           C  
ANISOU 1304  CE1 TYR A 190    15981  19217  12616   4809   4083   4855       C  
ATOM   1305  CE2 TYR A 190      16.591  -6.634 -47.330  1.00121.03           C  
ANISOU 1305  CE2 TYR A 190    15505  18452  12031   4029   3504   4532       C  
ATOM   1306  CZ  TYR A 190      17.443  -7.132 -46.359  1.00127.18           C  
ANISOU 1306  CZ  TYR A 190    15817  19436  13068   4123   3694   4811       C  
ATOM   1307  OH  TYR A 190      17.728  -6.386 -45.242  1.00124.14           O  
ANISOU 1307  OH  TYR A 190    14697  19291  13180   3559   3496   5059       O  
ATOM   1308  N   LEU A 191      13.451  -9.705 -49.020  1.00124.05           N  
ANISOU 1308  N   LEU A 191    18785  17155  11194   4301   2627   2755       N  
ATOM   1309  CA  LEU A 191      12.327  -9.346 -48.153  1.00118.56           C  
ANISOU 1309  CA  LEU A 191    17725  16337  10983   3560   2051   2549       C  
ATOM   1310  C   LEU A 191      11.725 -10.603 -47.550  1.00123.03           C  
ANISOU 1310  C   LEU A 191    18728  16419  11599   3401   1778   2187       C  
ATOM   1311  O   LEU A 191      11.517 -10.642 -46.340  1.00118.64           O  
ANISOU 1311  O   LEU A 191    17676  15862  11541   3054   1636   2215       O  
ATOM   1312  CB  LEU A 191      11.248  -8.560 -48.908  1.00118.21           C  
ANISOU 1312  CB  LEU A 191    17808  16298  10810   3203   1616   2405       C  
ATOM   1313  CG  LEU A 191      11.424  -7.050 -49.006  1.00120.82           C  
ANISOU 1313  CG  LEU A 191    17498  17040  11369   3055   1698   2759       C  
ATOM   1314  CD1 LEU A 191      10.267  -6.433 -49.751  1.00121.55           C  
ANISOU 1314  CD1 LEU A 191    17778  17101  11304   2776   1260   2627       C  
ATOM   1315  CD2 LEU A 191      11.514  -6.405 -47.635  1.00117.69           C  
ANISOU 1315  CD2 LEU A 191    16314  16784  11619   2659   1660   2938       C  
ATOM   1316  N   LEU A 192      11.506 -11.651 -48.388  1.00124.83           N  
ANISOU 1316  N   LEU A 192    19948  16209  11272   3668   1727   1864       N  
ATOM   1317  CA  LEU A 192      10.996 -12.966 -47.987  1.00126.21           C  
ANISOU 1317  CA  LEU A 192    20741  15811  11401   3532   1479   1521       C  
ATOM   1318  C   LEU A 192      11.857 -13.511 -46.850  1.00128.13           C  
ANISOU 1318  C   LEU A 192    20608  16079  11996   3798   1870   1739       C  
ATOM   1319  O   LEU A 192      11.315 -13.942 -45.836  1.00125.61           O  
ANISOU 1319  O   LEU A 192    20097  15561  12070   3383   1591   1645       O  
ATOM   1320  CB  LEU A 192      11.003 -13.939 -49.189  1.00133.90           C  
ANISOU 1320  CB  LEU A 192    22987  16291  11596   3938   1514   1193       C  
ATOM   1321  CG  LEU A 192      10.739 -15.421 -48.896  1.00142.31           C  
ANISOU 1321  CG  LEU A 192    24923  16644  12505   3926   1373    858       C  
ATOM   1322  CD1 LEU A 192       9.251 -15.718 -48.825  1.00142.57           C  
ANISOU 1322  CD1 LEU A 192    25224  16315  12631   3047    541    519       C  
ATOM   1323  CD2 LEU A 192      11.402 -16.299 -49.930  1.00152.67           C  
ANISOU 1323  CD2 LEU A 192    27455  17532  13020   4695   1779    680       C  
ATOM   1324  N   SER A 193      13.193 -13.429 -47.008  1.00125.79           N  
ANISOU 1324  N   SER A 193    20122  16102  11569   4485   2515   2104       N  
ATOM   1325  CA  SER A 193      14.182 -13.868 -46.029  1.00124.96           C  
ANISOU 1325  CA  SER A 193    19568  16159  11752   4831   2932   2437       C  
ATOM   1326  C   SER A 193      14.051 -13.107 -44.703  1.00120.74           C  
ANISOU 1326  C   SER A 193    17990  15988  11898   4242   2702   2646       C  
ATOM   1327  O   SER A 193      13.999 -13.752 -43.653  1.00119.11           O  
ANISOU 1327  O   SER A 193    17653  15622  11981   4123   2636   2639       O  
ATOM   1328  CB  SER A 193      15.592 -13.739 -46.597  1.00133.08           C  
ANISOU 1328  CB  SER A 193    20455  17609  12501   5652   3646   2904       C  
ATOM   1329  OG  SER A 193      15.725 -14.460 -47.811  1.00148.77           O  
ANISOU 1329  OG  SER A 193    23516  19232  13780   6293   3926   2701       O  
ATOM   1330  N   TRP A 194      13.955 -11.754 -44.755  1.00112.14           N  
ANISOU 1330  N   TRP A 194    16257  15328  11022   3880   2573   2818       N  
ATOM   1331  CA  TRP A 194      13.808 -10.895 -43.571  1.00105.82           C  
ANISOU 1331  CA  TRP A 194    14612  14818  10778   3327   2352   2981       C  
ATOM   1332  C   TRP A 194      12.463 -11.099 -42.872  1.00106.81           C  
ANISOU 1332  C   TRP A 194    14820  14601  11164   2744   1833   2625       C  
ATOM   1333  O   TRP A 194      12.417 -11.084 -41.642  1.00102.63           O  
ANISOU 1333  O   TRP A 194    13842  14139  11015   2472   1742   2706       O  
ATOM   1334  CB  TRP A 194      14.011  -9.420 -43.932  1.00102.31           C  
ANISOU 1334  CB  TRP A 194    13661  14789  10421   3120   2361   3230       C  
ATOM   1335  CG  TRP A 194      13.902  -8.472 -42.771  1.00 98.11           C  
ANISOU 1335  CG  TRP A 194    12429  14474  10373   2573   2148   3372       C  
ATOM   1336  CD1 TRP A 194      14.904  -8.085 -41.933  1.00100.63           C  
ANISOU 1336  CD1 TRP A 194    12127  15166  10942   2509   2314   3765       C  
ATOM   1337  CD2 TRP A 194      12.733  -7.744 -42.363  1.00 93.89           C  
ANISOU 1337  CD2 TRP A 194    11799  13798  10075   2033   1734   3147       C  
ATOM   1338  NE1 TRP A 194      14.428  -7.181 -41.010  1.00 96.02           N  
ANISOU 1338  NE1 TRP A 194    11183  14607  10692   1939   2008   3730       N  
ATOM   1339  CE2 TRP A 194      13.104  -6.936 -41.265  1.00 95.10           C  
ANISOU 1339  CE2 TRP A 194    11379  14179  10575   1698   1700   3365       C  
ATOM   1340  CE3 TRP A 194      11.404  -7.693 -42.822  1.00 94.03           C  
ANISOU 1340  CE3 TRP A 194    12157  13545  10024   1815   1385   2824       C  
ATOM   1341  CZ2 TRP A 194      12.197  -6.083 -40.621  1.00 90.84           C  
ANISOU 1341  CZ2 TRP A 194    10691  13543  10281   1245   1406   3237       C  
ATOM   1342  CZ3 TRP A 194      10.505  -6.856 -42.176  1.00 91.71           C  
ANISOU 1342  CZ3 TRP A 194    11575  13241  10028   1380   1104   2773       C  
ATOM   1343  CH2 TRP A 194      10.902  -6.065 -41.089  1.00 89.86           C  
ANISOU 1343  CH2 TRP A 194    10862  13176  10104   1144   1152   2960       C  
ATOM   1344  N   LEU A 195      11.379 -11.271 -43.654  1.00105.90           N  
ANISOU 1344  N   LEU A 195    15246  14167  10826   2548   1488   2285       N  
ATOM   1345  CA  LEU A 195      10.023 -11.507 -43.152  1.00104.35           C  
ANISOU 1345  CA  LEU A 195    15097  13698  10851   1993    984   2028       C  
ATOM   1346  C   LEU A 195       9.962 -12.834 -42.422  1.00111.27           C  
ANISOU 1346  C   LEU A 195    16276  14195  11806   2002    963   1912       C  
ATOM   1347  O   LEU A 195       9.398 -12.896 -41.333  1.00108.37           O  
ANISOU 1347  O   LEU A 195    15541  13810  11823   1624    766   1931       O  
ATOM   1348  CB  LEU A 195       8.990 -11.496 -44.288  1.00106.83           C  
ANISOU 1348  CB  LEU A 195    15929  13814  10847   1790    592   1771       C  
ATOM   1349  CG  LEU A 195       8.594 -10.137 -44.842  1.00109.44           C  
ANISOU 1349  CG  LEU A 195    15907  14483  11193   1633    467   1886       C  
ATOM   1350  CD1 LEU A 195       7.919 -10.296 -46.175  1.00113.84           C  
ANISOU 1350  CD1 LEU A 195    17089  14885  11278   1601    161   1682       C  
ATOM   1351  CD2 LEU A 195       7.694  -9.382 -43.880  1.00107.13           C  
ANISOU 1351  CD2 LEU A 195    14973  14342  11387   1159    202   1975       C  
ATOM   1352  N   LEU A 196      10.570 -13.882 -43.013  1.00113.71           N  
ANISOU 1352  N   LEU A 196    17295  14184  11726   2487   1214   1820       N  
ATOM   1353  CA  LEU A 196      10.663 -15.224 -42.443  1.00116.66           C  
ANISOU 1353  CA  LEU A 196    18111  14108  12106   2614   1274   1732       C  
ATOM   1354  C   LEU A 196      11.518 -15.194 -41.172  1.00119.61           C  
ANISOU 1354  C   LEU A 196    17795  14795  12855   2785   1592   2080       C  
ATOM   1355  O   LEU A 196      11.219 -15.927 -40.228  1.00119.11           O  
ANISOU 1355  O   LEU A 196    17736  14491  13028   2606   1487   2065       O  
ATOM   1356  CB  LEU A 196      11.257 -16.196 -43.478  1.00123.49           C  
ANISOU 1356  CB  LEU A 196    19981  14556  12385   3241   1573   1585       C  
ATOM   1357  CG  LEU A 196      10.283 -17.143 -44.199  1.00133.20           C  
ANISOU 1357  CG  LEU A 196    22286  15079  13244   2968   1144   1140       C  
ATOM   1358  CD1 LEU A 196       9.231 -16.387 -45.020  1.00132.73           C  
ANISOU 1358  CD1 LEU A 196    22244  15128  13058   2430    615    950       C  
ATOM   1359  CD2 LEU A 196      11.036 -18.095 -45.108  1.00143.25           C  
ANISOU 1359  CD2 LEU A 196    24661  15890  13879   3712   1545    999       C  
ATOM   1360  N   PHE A 197      12.557 -14.321 -41.142  1.00115.60           N  
ANISOU 1360  N   PHE A 197    16678  14845  12398   3073   1937   2427       N  
ATOM   1361  CA  PHE A 197      13.448 -14.123 -39.994  1.00113.85           C  
ANISOU 1361  CA  PHE A 197    15730  15033  12494   3163   2168   2816       C  
ATOM   1362  C   PHE A 197      12.700 -13.414 -38.869  1.00112.58           C  
ANISOU 1362  C   PHE A 197    14989  15024  12763   2505   1801   2794       C  
ATOM   1363  O   PHE A 197      12.877 -13.769 -37.706  1.00111.24           O  
ANISOU 1363  O   PHE A 197    14526  14907  12832   2429   1809   2935       O  
ATOM   1364  CB  PHE A 197      14.701 -13.323 -40.398  1.00116.97           C  
ANISOU 1364  CB  PHE A 197    15638  16001  12804   3533   2556   3236       C  
ATOM   1365  CG  PHE A 197      15.625 -12.936 -39.263  1.00117.44           C  
ANISOU 1365  CG  PHE A 197    14869  16575  13178   3485   2682   3690       C  
ATOM   1366  CD1 PHE A 197      16.602 -13.815 -38.809  1.00124.10           C  
ANISOU 1366  CD1 PHE A 197    15615  17539  13997   4003   3034   4030       C  
ATOM   1367  CD2 PHE A 197      15.539 -11.679 -38.671  1.00115.90           C  
ANISOU 1367  CD2 PHE A 197    14037  16736  13265   2930   2438   3803       C  
ATOM   1368  CE1 PHE A 197      17.464 -13.452 -37.767  1.00124.54           C  
ANISOU 1368  CE1 PHE A 197    14869  18137  14315   3906   3077   4499       C  
ATOM   1369  CE2 PHE A 197      16.400 -11.319 -37.628  1.00118.52           C  
ANISOU 1369  CE2 PHE A 197    13682  17525  13824   2801   2472   4211       C  
ATOM   1370  CZ  PHE A 197      17.357 -12.207 -37.184  1.00119.98           C  
ANISOU 1370  CZ  PHE A 197    13699  17899  13989   3261   2762   4570       C  
ATOM   1371  N   ILE A 198      11.893 -12.398 -39.219  1.00106.31           N  
ANISOU 1371  N   ILE A 198    14055  14309  12028   2095   1519   2650       N  
ATOM   1372  CA  ILE A 198      11.089 -11.629 -38.275  1.00101.87           C  
ANISOU 1372  CA  ILE A 198    13039  13861  11807   1563   1228   2626       C  
ATOM   1373  C   ILE A 198       9.967 -12.508 -37.708  1.00106.16           C  
ANISOU 1373  C   ILE A 198    13816  14029  12492   1276    952   2422       C  
ATOM   1374  O   ILE A 198       9.753 -12.488 -36.496  1.00103.70           O  
ANISOU 1374  O   ILE A 198    13160  13794  12448   1059    898   2513       O  
ATOM   1375  CB  ILE A 198      10.625 -10.293 -38.928  1.00103.24           C  
ANISOU 1375  CB  ILE A 198    13048  14212  11966   1342   1088   2594       C  
ATOM   1376  CG1 ILE A 198      11.721  -9.201 -38.808  1.00102.75           C  
ANISOU 1376  CG1 ILE A 198    12520  14573  11948   1401   1310   2903       C  
ATOM   1377  CG2 ILE A 198       9.255  -9.798 -38.449  1.00101.87           C  
ANISOU 1377  CG2 ILE A 198    12730  13958  12018    891    748   2458       C  
ATOM   1378  CD1 ILE A 198      12.013  -8.581 -37.378  1.00106.86           C  
ANISOU 1378  CD1 ILE A 198    12530  15316  12758   1096   1264   3077       C  
ATOM   1379  N   ALA A 199       9.311 -13.329 -38.568  1.00106.32           N  
ANISOU 1379  N   ALA A 199    14456  13640  12301   1263    775   2178       N  
ATOM   1380  CA  ALA A 199       8.255 -14.271 -38.172  1.00107.81           C  
ANISOU 1380  CA  ALA A 199    14917  13436  12610    916    470   2033       C  
ATOM   1381  C   ALA A 199       8.825 -15.362 -37.256  1.00114.84           C  
ANISOU 1381  C   ALA A 199    15919  14123  13591   1117    677   2139       C  
ATOM   1382  O   ALA A 199       8.095 -15.908 -36.431  1.00114.71           O  
ANISOU 1382  O   ALA A 199    15853  13925  13808    791    494   2153       O  
ATOM   1383  CB  ALA A 199       7.606 -14.895 -39.396  1.00112.80           C  
ANISOU 1383  CB  ALA A 199    16278  13658  12921    816    193   1763       C  
ATOM   1384  N   PHE A 200      10.138 -15.651 -37.391  1.00114.01           N  
ANISOU 1384  N   PHE A 200    15914  14098  13308   1682   1084   2282       N  
ATOM   1385  CA  PHE A 200      10.884 -16.589 -36.553  1.00115.84           C  
ANISOU 1385  CA  PHE A 200    16182  14230  13602   2008   1352   2478       C  
ATOM   1386  C   PHE A 200      11.078 -15.945 -35.169  1.00115.99           C  
ANISOU 1386  C   PHE A 200    15407  14707  13956   1800   1357   2740       C  
ATOM   1387  O   PHE A 200      10.902 -16.627 -34.158  1.00115.68           O  
ANISOU 1387  O   PHE A 200    15326  14538  14090   1715   1338   2835       O  
ATOM   1388  CB  PHE A 200      12.230 -16.944 -37.214  1.00121.66           C  
ANISOU 1388  CB  PHE A 200    17169  15030  14027   2747   1821   2644       C  
ATOM   1389  CG  PHE A 200      13.226 -17.679 -36.351  1.00125.77           C  
ANISOU 1389  CG  PHE A 200    17532  15638  14616   3203   2169   2987       C  
ATOM   1390  CD1 PHE A 200      13.112 -19.050 -36.141  1.00133.53           C  
ANISOU 1390  CD1 PHE A 200    19163  16044  15529   3427   2251   2930       C  
ATOM   1391  CD2 PHE A 200      14.303 -17.009 -35.778  1.00126.93           C  
ANISOU 1391  CD2 PHE A 200    16906  16442  14880   3399   2396   3410       C  
ATOM   1392  CE1 PHE A 200      14.045 -19.735 -35.350  1.00136.87           C  
ANISOU 1392  CE1 PHE A 200    19432  16567  16007   3919   2598   3305       C  
ATOM   1393  CE2 PHE A 200      15.235 -17.693 -34.988  1.00132.47           C  
ANISOU 1393  CE2 PHE A 200    17397  17303  15632   3833   2688   3801       C  
ATOM   1394  CZ  PHE A 200      15.101 -19.052 -34.782  1.00134.36           C  
ANISOU 1394  CZ  PHE A 200    18261  16985  15805   4136   2812   3755       C  
ATOM   1395  N   LEU A 201      11.402 -14.624 -35.131  1.00109.89           N  
ANISOU 1395  N   LEU A 201    14081  14429  13242   1689   1363   2852       N  
ATOM   1396  CA  LEU A 201      11.568 -13.852 -33.890  1.00106.75           C  
ANISOU 1396  CA  LEU A 201    13058  14428  13074   1436   1316   3048       C  
ATOM   1397  C   LEU A 201      10.231 -13.705 -33.174  1.00108.10           C  
ANISOU 1397  C   LEU A 201    13163  14456  13455    966   1034   2899       C  
ATOM   1398  O   LEU A 201      10.201 -13.706 -31.944  1.00106.86           O  
ANISOU 1398  O   LEU A 201    12727  14432  13443    835   1024   3035       O  
ATOM   1399  CB  LEU A 201      12.153 -12.446 -34.135  1.00105.27           C  
ANISOU 1399  CB  LEU A 201    12453  14681  12862   1357   1344   3170       C  
ATOM   1400  CG  LEU A 201      13.436 -12.284 -34.953  1.00113.10           C  
ANISOU 1400  CG  LEU A 201    13357  15949  13666   1763   1630   3412       C  
ATOM   1401  CD1 LEU A 201      13.882 -10.842 -34.950  1.00112.01           C  
ANISOU 1401  CD1 LEU A 201    12766  16218  13574   1506   1578   3574       C  
ATOM   1402  CD2 LEU A 201      14.564 -13.174 -34.445  1.00119.33           C  
ANISOU 1402  CD2 LEU A 201    14007  16907  14425   2189   1903   3758       C  
ATOM   1403  N   PHE A 202       9.133 -13.558 -33.945  1.00104.08           N  
ANISOU 1403  N   PHE A 202    12883  13725  12938    733    811   2670       N  
ATOM   1404  CA  PHE A 202       7.778 -13.441 -33.408  1.00102.69           C  
ANISOU 1404  CA  PHE A 202    12579  13470  12967    325    567   2618       C  
ATOM   1405  C   PHE A 202       7.312 -14.774 -32.846  1.00108.50           C  
ANISOU 1405  C   PHE A 202    13547  13867  13810    225    503   2649       C  
ATOM   1406  O   PHE A 202       6.760 -14.789 -31.752  1.00107.35           O  
ANISOU 1406  O   PHE A 202    13121  13806  13863     24    475   2782       O  
ATOM   1407  CB  PHE A 202       6.793 -12.912 -34.457  1.00104.77           C  
ANISOU 1407  CB  PHE A 202    12943  13679  13188    114    323   2463       C  
ATOM   1408  CG  PHE A 202       6.649 -11.409 -34.471  1.00103.68           C  
ANISOU 1408  CG  PHE A 202    12441  13868  13083     58    336   2502       C  
ATOM   1409  CD1 PHE A 202       5.787 -10.767 -33.586  1.00105.56           C  
ANISOU 1409  CD1 PHE A 202    12342  14251  13515   -142    289   2596       C  
ATOM   1410  CD2 PHE A 202       7.348 -10.636 -35.389  1.00105.02           C  
ANISOU 1410  CD2 PHE A 202    12658  14174  13072    239    427   2472       C  
ATOM   1411  CE1 PHE A 202       5.642  -9.376 -33.611  1.00104.77           C  
ANISOU 1411  CE1 PHE A 202    12039  14358  13412   -139    333   2623       C  
ATOM   1412  CE2 PHE A 202       7.203  -9.247 -35.413  1.00106.08           C  
ANISOU 1412  CE2 PHE A 202    12540  14528  13238    169    437   2520       C  
ATOM   1413  CZ  PHE A 202       6.347  -8.627 -34.529  1.00103.10           C  
ANISOU 1413  CZ  PHE A 202    11912  14222  13039    -10    387   2577       C  
ATOM   1414  N   SER A 203       7.585 -15.896 -33.562  1.00107.95           N  
ANISOU 1414  N   SER A 203    14047  13389  13580    396    515   2546       N  
ATOM   1415  CA  SER A 203       7.252 -17.259 -33.118  1.00110.53           C  
ANISOU 1415  CA  SER A 203    14741  13273  13982    307    463   2580       C  
ATOM   1416  C   SER A 203       7.953 -17.559 -31.795  1.00111.68           C  
ANISOU 1416  C   SER A 203    14596  13588  14250    517    716   2843       C  
ATOM   1417  O   SER A 203       7.373 -18.208 -30.925  1.00111.56           O  
ANISOU 1417  O   SER A 203    14556  13414  14418    298    653   2970       O  
ATOM   1418  CB  SER A 203       7.652 -18.289 -34.170  1.00119.17           C  
ANISOU 1418  CB  SER A 203    16643  13846  14788    568    499   2399       C  
ATOM   1419  OG  SER A 203       6.895 -18.126 -35.358  1.00130.46           O  
ANISOU 1419  OG  SER A 203    18426  15087  16055    298    185   2149       O  
ATOM   1420  N   GLY A 204       9.174 -17.042 -31.657  1.00106.20           N  
ANISOU 1420  N   GLY A 204    13642  13261  13448    902    975   2970       N  
ATOM   1421  CA  GLY A 204       9.972 -17.141 -30.445  1.00105.18           C  
ANISOU 1421  CA  GLY A 204    13160  13422  13383   1090   1165   3262       C  
ATOM   1422  C   GLY A 204       9.297 -16.395 -29.316  1.00105.18           C  
ANISOU 1422  C   GLY A 204    12698  13711  13553    717   1034   3331       C  
ATOM   1423  O   GLY A 204       9.127 -16.953 -28.233  1.00105.72           O  
ANISOU 1423  O   GLY A 204    12689  13761  13721    668   1065   3508       O  
ATOM   1424  N   ILE A 205       8.849 -15.152 -29.588  1.00 98.32           N  
ANISOU 1424  N   ILE A 205    11590  13075  12693    490    914   3203       N  
ATOM   1425  CA  ILE A 205       8.142 -14.284 -28.639  1.00 95.96           C  
ANISOU 1425  CA  ILE A 205    10957  13013  12491    217    843   3240       C  
ATOM   1426  C   ILE A 205       6.821 -14.921 -28.174  1.00102.01           C  
ANISOU 1426  C   ILE A 205    11757  13560  13443    -37    746   3286       C  
ATOM   1427  O   ILE A 205       6.593 -15.024 -26.968  1.00101.42           O  
ANISOU 1427  O   ILE A 205    11505  13606  13423    -87    818   3461       O  
ATOM   1428  CB  ILE A 205       7.967 -12.841 -29.215  1.00 96.56           C  
ANISOU 1428  CB  ILE A 205    10887  13290  12511    112    777   3100       C  
ATOM   1429  CG1 ILE A 205       9.287 -12.047 -29.099  1.00 95.96           C  
ANISOU 1429  CG1 ILE A 205    10642  13533  12287    234    862   3182       C  
ATOM   1430  CG2 ILE A 205       6.805 -12.077 -28.541  1.00 95.72           C  
ANISOU 1430  CG2 ILE A 205    10599  13272  12498   -108    727   3103       C  
ATOM   1431  CD1 ILE A 205       9.522 -10.974 -30.139  1.00 98.31           C  
ANISOU 1431  CD1 ILE A 205    10929  13921  12503    218    834   3077       C  
ATOM   1432  N   ILE A 206       5.978 -15.366 -29.131  1.00101.01           N  
ANISOU 1432  N   ILE A 206    11857  13134  13390   -220    568   3168       N  
ATOM   1433  CA  ILE A 206       4.672 -15.984 -28.872  1.00103.13           C  
ANISOU 1433  CA  ILE A 206    12102  13219  13863   -564    409   3280       C  
ATOM   1434  C   ILE A 206       4.818 -17.271 -28.047  1.00110.56           C  
ANISOU 1434  C   ILE A 206    13215  13906  14888   -558    489   3468       C  
ATOM   1435  O   ILE A 206       4.092 -17.440 -27.067  1.00110.92           O  
ANISOU 1435  O   ILE A 206    13009  14044  15092   -736    519   3705       O  
ATOM   1436  CB  ILE A 206       3.827 -16.188 -30.173  1.00108.12           C  
ANISOU 1436  CB  ILE A 206    12964  13603  14513   -845    101   3135       C  
ATOM   1437  CG1 ILE A 206       3.778 -14.918 -31.078  1.00106.27           C  
ANISOU 1437  CG1 ILE A 206    12593  13622  14165   -785     40   2976       C  
ATOM   1438  CG2 ILE A 206       2.412 -16.715 -29.878  1.00111.66           C  
ANISOU 1438  CG2 ILE A 206    13247  13967  15211  -1306   -124   3355       C  
ATOM   1439  CD1 ILE A 206       3.418 -13.547 -30.428  1.00109.80           C  
ANISOU 1439  CD1 ILE A 206    12553  14496  14672   -735    170   3083       C  
ATOM   1440  N   TYR A 207       5.770 -18.151 -28.418  1.00109.37           N  
ANISOU 1440  N   TYR A 207    13494  13448  14612   -294    572   3407       N  
ATOM   1441  CA  TYR A 207       6.010 -19.400 -27.694  1.00112.37           C  
ANISOU 1441  CA  TYR A 207    14114  13529  15051   -211    682   3606       C  
ATOM   1442  C   TYR A 207       6.557 -19.154 -26.284  1.00114.72           C  
ANISOU 1442  C   TYR A 207    14021  14223  15345    -12    903   3866       C  
ATOM   1443  O   TYR A 207       6.100 -19.807 -25.346  1.00116.25           O  
ANISOU 1443  O   TYR A 207    14171  14332  15666   -135    943   4110       O  
ATOM   1444  CB  TYR A 207       6.924 -20.348 -28.490  1.00116.70           C  
ANISOU 1444  CB  TYR A 207    15286  13634  15422    147    781   3497       C  
ATOM   1445  CG  TYR A 207       7.200 -21.664 -27.796  1.00122.22           C  
ANISOU 1445  CG  TYR A 207    16320  13948  16169    301    925   3723       C  
ATOM   1446  CD1 TYR A 207       6.215 -22.643 -27.697  1.00128.03           C  
ANISOU 1446  CD1 TYR A 207    17406  14166  17073   -117    737   3786       C  
ATOM   1447  CD2 TYR A 207       8.450 -21.939 -27.250  1.00123.53           C  
ANISOU 1447  CD2 TYR A 207    16442  14276  16219    849   1235   3930       C  
ATOM   1448  CE1 TYR A 207       6.460 -23.856 -27.053  1.00133.02           C  
ANISOU 1448  CE1 TYR A 207    18403  14383  17755     21    882   4019       C  
ATOM   1449  CE2 TYR A 207       8.710 -23.149 -26.607  1.00128.51           C  
ANISOU 1449  CE2 TYR A 207    17394  14547  16887   1054   1393   4182       C  
ATOM   1450  CZ  TYR A 207       7.712 -24.106 -26.511  1.00140.03           C  
ANISOU 1450  CZ  TYR A 207    19273  15422  18512    648   1231   4210       C  
ATOM   1451  OH  TYR A 207       7.964 -25.303 -25.884  1.00145.34           O  
ANISOU 1451  OH  TYR A 207    20322  15677  19224    847   1399   4480       O  
ATOM   1452  N   THR A 208       7.509 -18.206 -26.133  1.00107.84           N  
ANISOU 1452  N   THR A 208    12879  13787  14309    245   1013   3839       N  
ATOM   1453  CA  THR A 208       8.117 -17.867 -24.842  1.00106.35           C  
ANISOU 1453  CA  THR A 208    12367  14006  14034    379   1140   4064       C  
ATOM   1454  C   THR A 208       7.122 -17.147 -23.918  1.00108.65           C  
ANISOU 1454  C   THR A 208    12373  14535  14375    108   1112   4119       C  
ATOM   1455  O   THR A 208       7.055 -17.507 -22.740  1.00109.84           O  
ANISOU 1455  O   THR A 208    12434  14795  14507    131   1209   4359       O  
ATOM   1456  CB  THR A 208       9.438 -17.110 -25.039  1.00110.65           C  
ANISOU 1456  CB  THR A 208    12735  14925  14382    631   1192   4058       C  
ATOM   1457  OG1 THR A 208      10.281 -17.898 -25.878  1.00111.70           O  
ANISOU 1457  OG1 THR A 208    13128  14847  14464    983   1307   4087       O  
ATOM   1458  CG2 THR A 208      10.166 -16.824 -23.731  1.00108.88           C  
ANISOU 1458  CG2 THR A 208    12219  15131  14019    702   1232   4312       C  
ATOM   1459  N   TYR A 209       6.340 -16.167 -24.441  1.00102.22           N  
ANISOU 1459  N   TYR A 209    11440  13801  13598    -86   1019   3935       N  
ATOM   1460  CA  TYR A 209       5.367 -15.439 -23.614  1.00100.77           C  
ANISOU 1460  CA  TYR A 209    11019  13842  13429   -222   1075   4022       C  
ATOM   1461  C   TYR A 209       4.148 -16.280 -23.220  1.00106.84           C  
ANISOU 1461  C   TYR A 209    11714  14454  14427   -426   1091   4268       C  
ATOM   1462  O   TYR A 209       3.618 -16.075 -22.127  1.00106.98           O  
ANISOU 1462  O   TYR A 209    11547  14686  14413   -411   1250   4483       O  
ATOM   1463  CB  TYR A 209       4.937 -14.094 -24.215  1.00 99.11           C  
ANISOU 1463  CB  TYR A 209    10705  13778  13175   -273   1027   3823       C  
ATOM   1464  CG  TYR A 209       4.239 -13.227 -23.189  1.00 99.95           C  
ANISOU 1464  CG  TYR A 209    10660  14130  13186   -242   1184   3925       C  
ATOM   1465  CD1 TYR A 209       4.946 -12.639 -22.146  1.00101.52           C  
ANISOU 1465  CD1 TYR A 209    10937  14538  13101   -117   1280   3921       C  
ATOM   1466  CD2 TYR A 209       2.857 -13.061 -23.217  1.00101.75           C  
ANISOU 1466  CD2 TYR A 209    10690  14391  13579   -323   1242   4071       C  
ATOM   1467  CE1 TYR A 209       4.301 -11.880 -21.171  1.00103.26           C  
ANISOU 1467  CE1 TYR A 209    11168  14919  13147    -27   1463   3990       C  
ATOM   1468  CE2 TYR A 209       2.203 -12.295 -22.253  1.00103.53           C  
ANISOU 1468  CE2 TYR A 209    10818  14841  13676   -171   1480   4209       C  
ATOM   1469  CZ  TYR A 209       2.927 -11.722 -21.222  1.00109.80           C  
ANISOU 1469  CZ  TYR A 209    11820  15764  14134     -1   1609   4138       C  
ATOM   1470  OH  TYR A 209       2.281 -10.978 -20.265  1.00111.29           O  
ANISOU 1470  OH  TYR A 209    12057  16114  14113    206   1878   4244       O  
ATOM   1471  N   ALA A 210       3.721 -17.239 -24.076  1.00105.71           N  
ANISOU 1471  N   ALA A 210    11749  13932  14482   -634    926   4265       N  
ATOM   1472  CA  ALA A 210       2.610 -18.153 -23.761  1.00109.27           C  
ANISOU 1472  CA  ALA A 210    12135  14199  15184   -947    874   4558       C  
ATOM   1473  C   ALA A 210       2.977 -18.988 -22.526  1.00113.96           C  
ANISOU 1473  C   ALA A 210    12778  14763  15759   -822   1069   4845       C  
ATOM   1474  O   ALA A 210       2.105 -19.340 -21.726  1.00115.94           O  
ANISOU 1474  O   ALA A 210    12815  15085  16152   -990   1159   5189       O  
ATOM   1475  CB  ALA A 210       2.321 -19.070 -24.941  1.00112.84           C  
ANISOU 1475  CB  ALA A 210    12941  14159  15774  -1243    588   4450       C  
ATOM   1476  N   HIS A 211       4.288 -19.269 -22.375  1.00108.70           N  
ANISOU 1476  N   HIS A 211    12347  14048  14907   -498   1152   4759       N  
ATOM   1477  CA  HIS A 211       4.873 -19.976 -21.249  1.00109.71           C  
ANISOU 1477  CA  HIS A 211    12524  14205  14956   -291   1328   5036       C  
ATOM   1478  C   HIS A 211       4.972 -19.035 -20.054  1.00109.44           C  
ANISOU 1478  C   HIS A 211    12191  14695  14695   -149   1481   5138       C  
ATOM   1479  O   HIS A 211       4.711 -19.478 -18.942  1.00111.28           O  
ANISOU 1479  O   HIS A 211    12356  15025  14901   -121   1631   5454       O  
ATOM   1480  CB  HIS A 211       6.244 -20.547 -21.628  1.00111.19           C  
ANISOU 1480  CB  HIS A 211    13012  14219  15014     55   1357   4967       C  
ATOM   1481  CG  HIS A 211       6.162 -21.858 -22.342  1.00118.58           C  
ANISOU 1481  CG  HIS A 211    14433  14520  16103     11   1308   4979       C  
ATOM   1482  ND1 HIS A 211       6.583 -23.031 -21.742  1.00124.07           N  
ANISOU 1482  ND1 HIS A 211    15394  14934  16815    210   1450   5266       N  
ATOM   1483  CD2 HIS A 211       5.674 -22.148 -23.571  1.00121.63           C  
ANISOU 1483  CD2 HIS A 211    15155  14471  16589   -221   1116   4739       C  
ATOM   1484  CE1 HIS A 211       6.361 -23.987 -22.629  1.00126.94           C  
ANISOU 1484  CE1 HIS A 211    16307  14641  17284    104   1360   5167       C  
ATOM   1485  NE2 HIS A 211       5.816 -23.502 -23.745  1.00126.06           N  
ANISOU 1485  NE2 HIS A 211    16271  14420  17205   -179   1135   4837       N  
ATOM   1486  N   VAL A 212       5.297 -17.733 -20.285  1.00100.92           N  
ANISOU 1486  N   VAL A 212    11002  13917  13426    -78   1442   4875       N  
ATOM   1487  CA  VAL A 212       5.401 -16.691 -19.244  1.00 99.31           C  
ANISOU 1487  CA  VAL A 212    10681  14127  12927     26   1547   4887       C  
ATOM   1488  C   VAL A 212       4.063 -16.523 -18.494  1.00104.45           C  
ANISOU 1488  C   VAL A 212    11175  14887  13623    -43   1736   5106       C  
ATOM   1489  O   VAL A 212       4.062 -16.496 -17.262  1.00105.27           O  
ANISOU 1489  O   VAL A 212    11287  15212  13498     90   1906   5310       O  
ATOM   1490  CB  VAL A 212       5.963 -15.343 -19.791  1.00100.08           C  
ANISOU 1490  CB  VAL A 212    10793  14397  12834     47   1437   4554       C  
ATOM   1491  CG1 VAL A 212       5.861 -14.220 -18.760  1.00100.17           C  
ANISOU 1491  CG1 VAL A 212    10847  14706  12508    100   1526   4521       C  
ATOM   1492  CG2 VAL A 212       7.405 -15.495 -20.257  1.00 99.16           C  
ANISOU 1492  CG2 VAL A 212    10731  14317  12629    154   1307   4482       C  
ATOM   1493  N   LEU A 213       2.935 -16.452 -19.238  1.00101.28           N  
ANISOU 1493  N   LEU A 213    10612  14371  13500   -233   1709   5117       N  
ATOM   1494  CA  LEU A 213       1.584 -16.328 -18.674  1.00103.57           C  
ANISOU 1494  CA  LEU A 213    10631  14828  13894   -279   1913   5435       C  
ATOM   1495  C   LEU A 213       1.132 -17.576 -17.911  1.00112.12           C  
ANISOU 1495  C   LEU A 213    11627  15831  15144   -392   2026   5884       C  
ATOM   1496  O   LEU A 213       0.352 -17.461 -16.959  1.00114.47           O  
ANISOU 1496  O   LEU A 213    11720  16387  15386   -298   2304   6230       O  
ATOM   1497  CB  LEU A 213       0.553 -15.978 -19.754  1.00103.40           C  
ANISOU 1497  CB  LEU A 213    10370  14769  14149   -486   1794   5417       C  
ATOM   1498  CG  LEU A 213       0.288 -14.495 -19.993  1.00106.13           C  
ANISOU 1498  CG  LEU A 213    10657  15343  14323   -280   1888   5220       C  
ATOM   1499  CD1 LEU A 213      -0.625 -14.305 -21.186  1.00106.86           C  
ANISOU 1499  CD1 LEU A 213    10491  15407  14704   -491   1708   5245       C  
ATOM   1500  CD2 LEU A 213      -0.320 -13.819 -18.763  1.00110.09           C  
ANISOU 1500  CD2 LEU A 213    11076  16166  14589     36   2283   5461       C  
ATOM   1501  N   TRP A 214       1.607 -18.760 -18.338  1.00109.97           N  
ANISOU 1501  N   TRP A 214    11549  15178  15056   -561   1847   5904       N  
ATOM   1502  CA  TRP A 214       1.289 -20.037 -17.705  1.00113.93           C  
ANISOU 1502  CA  TRP A 214    12067  15487  15733   -702   1924   6327       C  
ATOM   1503  C   TRP A 214       1.977 -20.161 -16.340  1.00117.30           C  
ANISOU 1503  C   TRP A 214    12582  16145  15843   -371   2161   6516       C  
ATOM   1504  O   TRP A 214       1.354 -20.652 -15.400  1.00120.46           O  
ANISOU 1504  O   TRP A 214    12845  16648  16277   -391   2376   6956       O  
ATOM   1505  CB  TRP A 214       1.643 -21.211 -18.633  1.00114.33           C  
ANISOU 1505  CB  TRP A 214    12463  14958  16019   -932   1670   6244       C  
ATOM   1506  CG  TRP A 214       1.221 -22.560 -18.126  1.00120.62           C  
ANISOU 1506  CG  TRP A 214    13364  15427  17040  -1161   1710   6683       C  
ATOM   1507  CD1 TRP A 214       0.039 -22.880 -17.524  1.00127.50           C  
ANISOU 1507  CD1 TRP A 214    13905  16411  18128  -1454   1815   7170       C  
ATOM   1508  CD2 TRP A 214       1.958 -23.785 -18.243  1.00122.84           C  
ANISOU 1508  CD2 TRP A 214    14131  15179  17364  -1117   1659   6719       C  
ATOM   1509  NE1 TRP A 214       0.011 -24.222 -17.219  1.00131.62           N  
ANISOU 1509  NE1 TRP A 214    14687  16491  18833  -1658   1805   7502       N  
ATOM   1510  CE2 TRP A 214       1.173 -24.804 -17.656  1.00132.20           C  
ANISOU 1510  CE2 TRP A 214    15309  16127  18795  -1436   1714   7214       C  
ATOM   1511  CE3 TRP A 214       3.211 -24.122 -18.784  1.00122.96           C  
ANISOU 1511  CE3 TRP A 214    14588  14904  17229   -795   1611   6431       C  
ATOM   1512  CZ2 TRP A 214       1.603 -26.136 -17.588  1.00135.50           C  
ANISOU 1512  CZ2 TRP A 214    16233  15949  19302  -1452   1706   7385       C  
ATOM   1513  CZ3 TRP A 214       3.636 -25.442 -18.717  1.00128.59           C  
ANISOU 1513  CZ3 TRP A 214    15778  15067  18014   -728   1646   6616       C  
ATOM   1514  CH2 TRP A 214       2.840 -26.430 -18.119  1.00134.32           C  
ANISOU 1514  CH2 TRP A 214    16571  15488  18974  -1058   1685   7066       C  
ATOM   1515  N   LYS A 215       3.237 -19.685 -16.224  1.00110.10           N  
ANISOU 1515  N   LYS A 215    11863  15363  14608    -91   2106   6234       N  
ATOM   1516  CA  LYS A 215       3.999 -19.713 -14.969  1.00110.70           C  
ANISOU 1516  CA  LYS A 215    12028  15720  14316    188   2238   6401       C  
ATOM   1517  C   LYS A 215       3.568 -18.581 -14.022  1.00113.91           C  
ANISOU 1517  C   LYS A 215    12370  16559  14353    337   2433   6401       C  
ATOM   1518  O   LYS A 215       3.705 -18.722 -12.806  1.00115.53           O  
ANISOU 1518  O   LYS A 215    12647  16998  14250    516   2599   6656       O  
ATOM   1519  CB  LYS A 215       5.529 -19.665 -15.201  1.00111.75           C  
ANISOU 1519  CB  LYS A 215    12324  15891  14244    379   2055   6193       C  
ATOM   1520  CG  LYS A 215       6.086 -20.411 -16.422  1.00127.43           C  
ANISOU 1520  CG  LYS A 215    14454  17462  16501    362   1902   6060       C  
ATOM   1521  CD  LYS A 215       5.986 -21.937 -16.375  1.00141.70           C  
ANISOU 1521  CD  LYS A 215    16461  18828  18552    365   1973   6381       C  
ATOM   1522  CE  LYS A 215       6.322 -22.518 -17.728  1.00150.60           C  
ANISOU 1522  CE  LYS A 215    17873  19459  19891    352   1844   6160       C  
ATOM   1523  NZ  LYS A 215       6.407 -24.000 -17.694  1.00162.70           N  
ANISOU 1523  NZ  LYS A 215    19766  20460  21592    414   1918   6439       N  
ATOM   1524  N   ALA A 216       3.065 -17.457 -14.579  1.00108.41           N  
ANISOU 1524  N   ALA A 216    11606  15944  13641    305   2427   6120       N  
ATOM   1525  CA  ALA A 216       2.577 -16.313 -13.799  1.00109.23           C  
ANISOU 1525  CA  ALA A 216    11772  16360  13371    514   2660   6087       C  
ATOM   1526  C   ALA A 216       1.253 -16.668 -13.144  1.00117.12           C  
ANISOU 1526  C   ALA A 216    12526  17486  14486    577   3021   6560       C  
ATOM   1527  O   ALA A 216       0.972 -16.202 -12.039  1.00119.29           O  
ANISOU 1527  O   ALA A 216    12929  18034  14361    862   3324   6711       O  
ATOM   1528  CB  ALA A 216       2.400 -15.098 -14.693  1.00107.28           C  
ANISOU 1528  CB  ALA A 216    11547  16090  13125    499   2576   5701       C  
ATOM   1529  N   HIS A 217       0.445 -17.503 -13.829  1.00114.84           N  
ANISOU 1529  N   HIS A 217    11907  17006  14721    293   2979   6822       N  
ATOM   1530  CA  HIS A 217      -0.834 -17.988 -13.329  1.00119.26           C  
ANISOU 1530  CA  HIS A 217    12105  17711  15498    243   3274   7392       C  
ATOM   1531  C   HIS A 217      -0.600 -18.921 -12.145  1.00125.42           C  
ANISOU 1531  C   HIS A 217    12981  18540  16135    331   3459   7793       C  
ATOM   1532  O   HIS A 217      -1.411 -18.933 -11.224  1.00129.23           O  
ANISOU 1532  O   HIS A 217    13279  19312  16509    504   3843   8250       O  
ATOM   1533  CB  HIS A 217      -1.626 -18.701 -14.433  1.00121.39           C  
ANISOU 1533  CB  HIS A 217    12037  17728  16359   -230   3045   7569       C  
ATOM   1534  CG  HIS A 217      -3.053 -18.962 -14.061  1.00130.28           C  
ANISOU 1534  CG  HIS A 217    12648  19106  17746   -347   3311   8212       C  
ATOM   1535  ND1 HIS A 217      -3.431 -20.130 -13.422  1.00136.75           N  
ANISOU 1535  ND1 HIS A 217    13327  19864  18769   -562   3416   8767       N  
ATOM   1536  CD2 HIS A 217      -4.147 -18.181 -14.227  1.00134.23           C  
ANISOU 1536  CD2 HIS A 217    12716  19954  18330   -247   3512   8441       C  
ATOM   1537  CE1 HIS A 217      -4.737 -20.028 -13.229  1.00140.90           C  
ANISOU 1537  CE1 HIS A 217    13292  20732  19511   -635   3662   9335       C  
ATOM   1538  NE2 HIS A 217      -5.212 -18.872 -13.695  1.00139.99           N  
ANISOU 1538  NE2 HIS A 217    12963  20896  19330   -418   3740   9177       N  
ATOM   1539  N   GLN A 218       0.526 -19.673 -12.164  1.00120.06           N  
ANISOU 1539  N   GLN A 218    12582  17608  15426    274   3220   7662       N  
ATOM   1540  CA  GLN A 218       0.949 -20.614 -11.117  1.00122.75           C  
ANISOU 1540  CA  GLN A 218    13060  17961  15618    385   3344   8033       C  
ATOM   1541  C   GLN A 218       1.234 -19.908  -9.775  1.00126.85           C  
ANISOU 1541  C   GLN A 218    13777  18925  15496    794   3600   8077       C  
ATOM   1542  O   GLN A 218       0.859 -20.430  -8.716  1.00130.79           O  
ANISOU 1542  O   GLN A 218    14248  19596  15851    932   3894   8559       O  
ATOM   1543  CB  GLN A 218       2.185 -21.419 -11.574  1.00122.51           C  
ANISOU 1543  CB  GLN A 218    13293  17586  15670    337   3039   7860       C  
ATOM   1544  CG  GLN A 218       1.888 -22.500 -12.622  1.00139.51           C  
ANISOU 1544  CG  GLN A 218    15446  19185  18375    -32   2850   7933       C  
ATOM   1545  CD  GLN A 218       3.121 -23.117 -13.261  1.00158.64           C  
ANISOU 1545  CD  GLN A 218    18201  21244  20830     51   2612   7695       C  
ATOM   1546  OE1 GLN A 218       4.256 -22.998 -12.777  1.00152.49           O  
ANISOU 1546  OE1 GLN A 218    17558  20665  19717    378   2597   7632       O  
ATOM   1547  NE2 GLN A 218       2.919 -23.807 -14.374  1.00152.57           N  
ANISOU 1547  NE2 GLN A 218    17585  19944  20442   -235   2421   7594       N  
ATOM   1548  N   HIS A 219       1.886 -18.721  -9.833  1.00119.11           N  
ANISOU 1548  N   HIS A 219    13048  18104  14106    958   3471   7585       N  
ATOM   1549  CA  HIS A 219       2.245 -17.903  -8.667  1.00120.32           C  
ANISOU 1549  CA  HIS A 219    13554  18604  13557   1279   3611   7505       C  
ATOM   1550  C   HIS A 219       1.071 -17.083  -8.124  1.00124.75           C  
ANISOU 1550  C   HIS A 219    14123  19397  13879   1556   4063   7637       C  
ATOM   1551  O   HIS A 219       1.053 -16.766  -6.931  1.00128.06           O  
ANISOU 1551  O   HIS A 219    14863  20080  13714   1874   4322   7764       O  
ATOM   1552  CB  HIS A 219       3.438 -16.979  -8.979  1.00118.17           C  
ANISOU 1552  CB  HIS A 219    13599  18352  12949   1245   3233   6952       C  
ATOM   1553  CG  HIS A 219       4.724 -17.688  -9.282  1.00120.32           C  
ANISOU 1553  CG  HIS A 219    13854  18542  13321   1109   2858   6918       C  
ATOM   1554  ND1 HIS A 219       5.813 -17.007  -9.800  1.00119.49           N  
ANISOU 1554  ND1 HIS A 219    13866  18469  13065   1000   2489   6522       N  
ATOM   1555  CD2 HIS A 219       5.059 -18.991  -9.127  1.00123.61           C  
ANISOU 1555  CD2 HIS A 219    14143  18855  13966   1108   2842   7288       C  
ATOM   1556  CE1 HIS A 219       6.767 -17.912  -9.946  1.00119.02           C  
ANISOU 1556  CE1 HIS A 219    13689  18386  13146    985   2288   6693       C  
ATOM   1557  NE2 HIS A 219       6.359 -19.120  -9.554  1.00121.83           N  
ANISOU 1557  NE2 HIS A 219    13941  18628  13722   1074   2498   7133       N  
ATOM   1558  N   VAL A 220       0.104 -16.724  -8.996  1.00118.48           N  
ANISOU 1558  N   VAL A 220    12999  18525  13492   1479   4170   7631       N  
ATOM   1559  CA  VAL A 220      -1.083 -15.953  -8.589  1.00120.79           C  
ANISOU 1559  CA  VAL A 220    13210  19070  13615   1828   4663   7847       C  
ATOM   1560  C   VAL A 220      -2.237 -16.890  -8.165  1.00126.35           C  
ANISOU 1560  C   VAL A 220    13394  19953  14661   1823   5046   8607       C  
ATOM   1561  O   VAL A 220      -3.299 -16.410  -7.766  1.00130.55           O  
ANISOU 1561  O   VAL A 220    13733  20777  15093   2162   5533   8957       O  
ATOM   1562  CB  VAL A 220      -1.542 -14.865  -9.615  1.00122.34           C  
ANISOU 1562  CB  VAL A 220    13322  19192  13969   1857   4632   7515       C  
ATOM   1563  CG1 VAL A 220      -0.425 -13.876  -9.941  1.00118.08           C  
ANISOU 1563  CG1 VAL A 220    13325  18479  13063   1842   4288   6827       C  
ATOM   1564  CG2 VAL A 220      -2.129 -15.476 -10.885  1.00120.36           C  
ANISOU 1564  CG2 VAL A 220    12475  18781  14474   1435   4410   7669       C  
ATOM   1565  N   ALA A 221      -2.018 -18.174  -8.414  1.00120.03           N  
ANISOU 1565  N   ALA A 221    12379  18965  14263   1450   4840   8898       N  
ATOM   1566  CA  ALA A 221      -2.998 -19.192  -8.146  1.00123.44           C  
ANISOU 1566  CA  ALA A 221    12340  19486  15076   1295   5106   9647       C  
ATOM   1567  C   ALA A 221      -3.076 -19.365  -6.674  1.00129.48           C  
ANISOU 1567  C   ALA A 221    13309  20551  15337   1680   5528  10064       C  
ATOM   1568  O   ALA A 221      -2.057 -19.451  -5.997  1.00128.49           O  
ANISOU 1568  O   ALA A 221    13677  20404  14740   1835   5391   9808       O  
ATOM   1569  CB  ALA A 221      -2.600 -20.499  -8.805  1.00122.83           C  
ANISOU 1569  CB  ALA A 221    12131  18959  15579    730   4689   9731       C  
ATOM   1570  N   SER A 222      -4.293 -19.413  -6.169  1.00129.23           N  
ANISOU 1570  N   SER A 222    12872  20865  15366   1865   6055  10739       N  
ATOM   1571  CA  SER A 222      -4.456 -19.596  -4.761  1.00134.12           C  
ANISOU 1571  CA  SER A 222    13571  21841  15547   2268   6588  11309       C  
ATOM   1572  C   SER A 222      -5.632 -20.469  -4.410  1.00141.65           C  
ANISOU 1572  C   SER A 222    13772  23129  16919   2260   7065  12136       C  
ATOM   1573  O   SER A 222      -6.665 -20.468  -5.064  1.00141.06           O  
ANISOU 1573  O   SER A 222    13408  23208  16982   2380   7180  12070       O  
ATOM   1574  CB  SER A 222      -4.491 -18.255  -4.046  1.00137.93           C  
ANISOU 1574  CB  SER A 222    14703  22587  15119   2933   6887  10943       C  
ATOM   1575  OG  SER A 222      -3.172 -17.770  -3.888  1.00140.77           O  
ANISOU 1575  OG  SER A 222    15707  22735  15045   2892   6425  10284       O  
ATOM   1576  N   ASN A1001      -5.416 -21.216  -3.347  1.00 72.39           N  
ANISOU 1576  N   ASN A1001     8857  10882   7767   -254    273     61       N  
ATOM   1577  CA  ASN A1001      -6.358 -22.127  -2.776  1.00 69.53           C  
ANISOU 1577  CA  ASN A1001     8521  10517   7379   -371    214   -128       C  
ATOM   1578  C   ASN A1001      -5.828 -22.202  -1.373  1.00 70.94           C  
ANISOU 1578  C   ASN A1001     8771  10527   7656   -395    271   -241       C  
ATOM   1579  O   ASN A1001      -4.791 -21.648  -1.086  1.00 70.70           O  
ANISOU 1579  O   ASN A1001     8804  10357   7702   -403    349   -269       O  
ATOM   1580  CB  ASN A1001      -6.350 -23.474  -3.482  1.00 70.57           C  
ANISOU 1580  CB  ASN A1001     8673  10704   7438   -470    167   -203       C  
ATOM   1581  CG  ASN A1001      -4.989 -24.105  -3.517  1.00107.38           C  
ANISOU 1581  CG  ASN A1001    13304  15438  12057   -561     93   -338       C  
ATOM   1582  OD1 ASN A1001      -4.093 -23.704  -2.791  1.00104.75           O  
ANISOU 1582  OD1 ASN A1001    12983  15050  11768   -574     91   -405       O  
ATOM   1583  ND2 ASN A1001      -4.825 -25.101  -4.367  1.00102.30           N  
ANISOU 1583  ND2 ASN A1001    12613  14923  11333   -626     45   -379       N  
ATOM   1584  N   ILE A1002      -6.530 -22.869  -0.491  1.00 65.80           N  
ANISOU 1584  N   ILE A1002     8099   9910   6991   -417    237   -317       N  
ATOM   1585  CA  ILE A1002      -6.107 -22.949   0.887  1.00 63.91           C  
ANISOU 1585  CA  ILE A1002     7905   9586   6791   -444    273   -426       C  
ATOM   1586  C   ILE A1002      -4.742 -23.595   1.115  1.00 65.84           C  
ANISOU 1586  C   ILE A1002     8198   9820   6999   -529    236   -530       C  
ATOM   1587  O   ILE A1002      -4.007 -23.178   1.983  1.00 65.35           O  
ANISOU 1587  O   ILE A1002     8174   9699   6957   -550    274   -619       O  
ATOM   1588  CB  ILE A1002      -7.178 -23.672   1.700  1.00 66.33           C  
ANISOU 1588  CB  ILE A1002     8167   9947   7087   -428    266   -438       C  
ATOM   1589  CG1 ILE A1002      -7.065 -23.318   3.165  1.00 66.23           C  
ANISOU 1589  CG1 ILE A1002     8194   9871   7099   -438    326   -533       C  
ATOM   1590  CG2 ILE A1002      -7.094 -25.166   1.485  1.00 66.24           C  
ANISOU 1590  CG2 ILE A1002     8117  10038   7014   -487    192   -457       C  
ATOM   1591  CD1 ILE A1002      -8.380 -23.433   3.884  1.00 72.37           C  
ANISOU 1591  CD1 ILE A1002     8933  10697   7868   -419    346   -539       C  
ATOM   1592  N   PHE A1003      -4.402 -24.617   0.353  1.00 61.77           N  
ANISOU 1592  N   PHE A1003     7663   9376   6430   -578    167   -532       N  
ATOM   1593  CA  PHE A1003      -3.130 -25.311   0.544  1.00 61.27           C  
ANISOU 1593  CA  PHE A1003     7630   9300   6350   -642    135   -617       C  
ATOM   1594  C   PHE A1003      -1.985 -24.331   0.332  1.00 66.26           C  
ANISOU 1594  C   PHE A1003     8306   9857   7012   -658    177   -656       C  
ATOM   1595  O   PHE A1003      -1.061 -24.287   1.142  1.00 65.66           O  
ANISOU 1595  O   PHE A1003     8254   9754   6942   -687    184   -749       O  
ATOM   1596  CB  PHE A1003      -2.993 -26.524  -0.393  1.00 62.55           C  
ANISOU 1596  CB  PHE A1003     7751   9533   6483   -693     79   -627       C  
ATOM   1597  CG  PHE A1003      -1.642 -27.205  -0.347  1.00 62.94           C  
ANISOU 1597  CG  PHE A1003     7820   9557   6540   -745     56   -705       C  
ATOM   1598  CD1 PHE A1003      -0.601 -26.779  -1.168  1.00 65.19           C  
ANISOU 1598  CD1 PHE A1003     8120   9829   6820   -778     61   -736       C  
ATOM   1599  CD2 PHE A1003      -1.422 -28.292   0.487  1.00 63.83           C  
ANISOU 1599  CD2 PHE A1003     7925   9659   6670   -754     39   -732       C  
ATOM   1600  CE1 PHE A1003       0.642 -27.410  -1.129  1.00 65.43           C  
ANISOU 1600  CE1 PHE A1003     8153   9842   6867   -821     41   -816       C  
ATOM   1601  CE2 PHE A1003      -0.185 -28.937   0.509  1.00 66.21           C  
ANISOU 1601  CE2 PHE A1003     8227   9940   6991   -781     20   -787       C  
ATOM   1602  CZ  PHE A1003       0.839 -28.491  -0.298  1.00 64.28           C  
ANISOU 1602  CZ  PHE A1003     7992   9689   6745   -816     16   -840       C  
ATOM   1603  N   GLU A1004      -2.073 -23.537  -0.745  1.00 63.72           N  
ANISOU 1603  N   GLU A1004     7985   9519   6706   -637    213   -578       N  
ATOM   1604  CA  GLU A1004      -1.092 -22.524  -1.089  1.00 64.52           C  
ANISOU 1604  CA  GLU A1004     8125   9527   6860   -655    284   -594       C  
ATOM   1605  C   GLU A1004      -1.153 -21.320  -0.143  1.00 68.75           C  
ANISOU 1605  C   GLU A1004     8688   9938   7497   -629    388   -636       C  
ATOM   1606  O   GLU A1004      -0.159 -20.612  -0.013  1.00 69.25           O  
ANISOU 1606  O   GLU A1004     8777   9910   7624   -674    459   -720       O  
ATOM   1607  CB  GLU A1004      -1.224 -22.127  -2.561  1.00 67.06           C  
ANISOU 1607  CB  GLU A1004     8435   9886   7159   -631    303   -463       C  
ATOM   1608  CG  GLU A1004      -0.717 -23.218  -3.494  1.00 82.67           C  
ANISOU 1608  CG  GLU A1004    10383  11986   9042   -695    225   -494       C  
ATOM   1609  CD  GLU A1004      -1.230 -23.143  -4.920  1.00116.37           C  
ANISOU 1609  CD  GLU A1004    14604  16388  13224   -668    213   -366       C  
ATOM   1610  OE1 GLU A1004      -0.707 -22.311  -5.698  1.00127.81           O  
ANISOU 1610  OE1 GLU A1004    16076  17813  14674   -659    279   -283       O  
ATOM   1611  OE2 GLU A1004      -2.145 -23.926  -5.265  1.00108.24           O  
ANISOU 1611  OE2 GLU A1004    13504  15504  12119   -661    144   -352       O  
ATOM   1612  N   MET A1005      -2.295 -21.119   0.553  1.00 64.77           N  
ANISOU 1612  N   MET A1005     8165   9431   7014   -570    406   -607       N  
ATOM   1613  CA  MET A1005      -2.493 -20.050   1.539  1.00 64.73           C  
ANISOU 1613  CA  MET A1005     8168   9315   7111   -552    515   -678       C  
ATOM   1614  C   MET A1005      -1.755 -20.419   2.823  1.00 66.11           C  
ANISOU 1614  C   MET A1005     8345   9536   7240   -621    493   -861       C  
ATOM   1615  O   MET A1005      -0.864 -19.685   3.242  1.00 65.25           O  
ANISOU 1615  O   MET A1005     8243   9361   7189   -673    567   -996       O  
ATOM   1616  CB  MET A1005      -3.995 -19.861   1.825  1.00 67.68           C  
ANISOU 1616  CB  MET A1005     8506   9699   7511   -466    535   -592       C  
ATOM   1617  CG  MET A1005      -4.297 -18.809   2.878  1.00 72.55           C  
ANISOU 1617  CG  MET A1005     9119  10203   8244   -449    661   -687       C  
ATOM   1618  SD  MET A1005      -5.899 -19.066   3.672  1.00 76.91           S  
ANISOU 1618  SD  MET A1005     9619  10823   8780   -382    654   -658       S  
ATOM   1619  CE  MET A1005      -6.381 -17.384   3.959  1.00 75.30           C  
ANISOU 1619  CE  MET A1005     9398  10419   8793   -315    848   -675       C  
ATOM   1620  N   LEU A1006      -2.140 -21.565   3.435  1.00 62.05           N  
ANISOU 1620  N   LEU A1006     7812   9147   6618   -619    399   -861       N  
ATOM   1621  CA  LEU A1006      -1.574 -22.120   4.667  1.00 61.65           C  
ANISOU 1621  CA  LEU A1006     7750   9192   6483   -657    360   -979       C  
ATOM   1622  C   LEU A1006      -0.123 -22.615   4.498  1.00 65.25           C  
ANISOU 1622  C   LEU A1006     8206   9691   6895   -712    303  -1049       C  
ATOM   1623  O   LEU A1006       0.578 -22.805   5.493  1.00 65.03           O  
ANISOU 1623  O   LEU A1006     8153   9757   6799   -737    280  -1157       O  
ATOM   1624  CB  LEU A1006      -2.493 -23.216   5.249  1.00 61.21           C  
ANISOU 1624  CB  LEU A1006     7675   9236   6344   -624    300   -906       C  
ATOM   1625  CG  LEU A1006      -3.706 -22.729   6.050  1.00 66.67           C  
ANISOU 1625  CG  LEU A1006     8349   9931   7051   -586    364   -908       C  
ATOM   1626  CD1 LEU A1006      -4.756 -23.794   6.150  1.00 66.97           C  
ANISOU 1626  CD1 LEU A1006     8367  10035   7043   -558    320   -803       C  
ATOM   1627  CD2 LEU A1006      -3.324 -22.324   7.454  1.00 69.58           C  
ANISOU 1627  CD2 LEU A1006     8702  10373   7363   -614    407  -1055       C  
ATOM   1628  N   ARG A1007       0.328 -22.799   3.239  1.00 61.30           N  
ANISOU 1628  N   ARG A1007     7721   9145   6424   -727    281   -990       N  
ATOM   1629  CA  ARG A1007       1.701 -23.184   2.908  1.00 60.80           C  
ANISOU 1629  CA  ARG A1007     7651   9107   6344   -779    241  -1060       C  
ATOM   1630  C   ARG A1007       2.609 -22.025   3.316  1.00 66.30           C  
ANISOU 1630  C   ARG A1007     8341   9754   7097   -832    325  -1213       C  
ATOM   1631  O   ARG A1007       3.725 -22.260   3.767  1.00 67.50           O  
ANISOU 1631  O   ARG A1007     8458   9981   7210   -874    292  -1332       O  
ATOM   1632  CB  ARG A1007       1.843 -23.457   1.398  1.00 60.00           C  
ANISOU 1632  CB  ARG A1007     7562   8971   6263   -792    226   -974       C  
ATOM   1633  CG  ARG A1007       3.092 -24.218   1.008  1.00 66.79           C  
ANISOU 1633  CG  ARG A1007     8404   9872   7102   -840    172  -1035       C  
ATOM   1634  CD  ARG A1007       3.833 -23.531  -0.111  1.00 79.47           C  
ANISOU 1634  CD  ARG A1007    10025  11415   8754   -887    229  -1049       C  
ATOM   1635  NE  ARG A1007       5.096 -24.204  -0.415  1.00100.40           N  
ANISOU 1635  NE  ARG A1007    12647  14105  11394   -938    188  -1133       N  
ATOM   1636  CZ  ARG A1007       5.228 -25.201  -1.287  1.00124.89           C  
ANISOU 1636  CZ  ARG A1007    15730  17250  14472   -951    138  -1101       C  
ATOM   1637  NH1 ARG A1007       4.168 -25.669  -1.938  1.00115.36           N  
ANISOU 1637  NH1 ARG A1007    14524  16072  13237   -928    118  -1001       N  
ATOM   1638  NH2 ARG A1007       6.416 -25.750  -1.501  1.00115.66           N  
ANISOU 1638  NH2 ARG A1007    14526  16104  13314   -992    114  -1190       N  
ATOM   1639  N   ILE A1008       2.115 -20.781   3.174  1.00 62.99           N  
ANISOU 1639  N   ILE A1008     7941   9209   6783   -827    444  -1215       N  
ATOM   1640  CA  ILE A1008       2.825 -19.556   3.539  1.00 64.08           C  
ANISOU 1640  CA  ILE A1008     8067   9258   7025   -889    569  -1379       C  
ATOM   1641  C   ILE A1008       2.729 -19.329   5.058  1.00 69.97           C  
ANISOU 1641  C   ILE A1008     8764  10095   7726   -909    586  -1549       C  
ATOM   1642  O   ILE A1008       3.750 -19.112   5.712  1.00 70.86           O  
ANISOU 1642  O   ILE A1008     8825  10286   7814   -981    597  -1745       O  
ATOM   1643  CB  ILE A1008       2.285 -18.350   2.722  1.00 67.83           C  
ANISOU 1643  CB  ILE A1008     8577   9531   7663   -862    717  -1284       C  
ATOM   1644  CG1 ILE A1008       2.447 -18.586   1.200  1.00 67.59           C  
ANISOU 1644  CG1 ILE A1008     8582   9467   7631   -843    696  -1109       C  
ATOM   1645  CG2 ILE A1008       2.925 -17.023   3.178  1.00 69.99           C  
ANISOU 1645  CG2 ILE A1008     8832   9666   8095   -936    891  -1473       C  
ATOM   1646  CD1 ILE A1008       1.469 -17.807   0.306  1.00 75.48           C  
ANISOU 1646  CD1 ILE A1008     9608  10348   8723   -758    788   -903       C  
ATOM   1647  N   ASP A1009       1.512 -19.394   5.608  1.00 66.86           N  
ANISOU 1647  N   ASP A1009     8374   9721   7308   -849    588  -1484       N  
ATOM   1648  CA  ASP A1009       1.261 -19.163   7.019  1.00 68.23           C  
ANISOU 1648  CA  ASP A1009     8499  10002   7423   -866    616  -1636       C  
ATOM   1649  C   ASP A1009       1.852 -20.240   7.939  1.00 74.27           C  
ANISOU 1649  C   ASP A1009     9217  11011   7989   -873    485  -1685       C  
ATOM   1650  O   ASP A1009       2.700 -19.898   8.762  1.00 75.74           O  
ANISOU 1650  O   ASP A1009     9337  11320   8120   -936    500  -1887       O  
ATOM   1651  CB  ASP A1009      -0.239 -18.952   7.271  1.00 70.13           C  
ANISOU 1651  CB  ASP A1009     8753  10193   7701   -796    663  -1542       C  
ATOM   1652  CG  ASP A1009      -0.731 -17.561   6.913  1.00 79.22           C  
ANISOU 1652  CG  ASP A1009     9913  11124   9063   -786    836  -1565       C  
ATOM   1653  OD1 ASP A1009       0.105 -16.712   6.523  1.00 81.08           O  
ANISOU 1653  OD1 ASP A1009    10150  11231   9428   -844    939  -1661       O  
ATOM   1654  OD2 ASP A1009      -1.946 -17.314   7.037  1.00 82.44           O  
ANISOU 1654  OD2 ASP A1009    10320  11480   9524   -718    883  -1484       O  
ATOM   1655  N   GLU A1010       1.404 -21.484   7.837  1.00 70.43           N  
ANISOU 1655  N   GLU A1010     8752  10603   7404   -808    370  -1504       N  
ATOM   1656  CA  GLU A1010       1.953 -22.555   8.666  1.00 70.42           C  
ANISOU 1656  CA  GLU A1010     8709  10815   7234   -787    261  -1490       C  
ATOM   1657  C   GLU A1010       3.403 -22.904   8.331  1.00 74.56           C  
ANISOU 1657  C   GLU A1010     9199  11398   7732   -815    193  -1541       C  
ATOM   1658  O   GLU A1010       4.198 -23.174   9.215  1.00 74.89           O  
ANISOU 1658  O   GLU A1010     9174  11644   7639   -802    124  -1589       O  
ATOM   1659  CB  GLU A1010       1.083 -23.808   8.625  1.00 70.95           C  
ANISOU 1659  CB  GLU A1010     8805  10902   7250   -714    198  -1280       C  
ATOM   1660  CG  GLU A1010      -0.303 -23.644   9.223  1.00 79.88           C  
ANISOU 1660  CG  GLU A1010     9941  12051   8358   -685    252  -1246       C  
ATOM   1661  CD  GLU A1010      -0.300 -23.199  10.668  1.00 99.42           C  
ANISOU 1661  CD  GLU A1010    12362  14741  10671   -679    252  -1315       C  
ATOM   1662  OE1 GLU A1010       0.544 -23.681  11.443  1.00 97.02           O  
ANISOU 1662  OE1 GLU A1010    12020  14609  10234   -658    175  -1288       O  
ATOM   1663  OE2 GLU A1010      -1.167 -22.382  11.035  1.00 94.66           O  
ANISOU 1663  OE2 GLU A1010    11748  14150  10068   -688    333  -1387       O  
ATOM   1664  N   GLY A1011       3.728 -22.925   7.042  1.00 70.20           N  
ANISOU 1664  N   GLY A1011     8684  10688   7300   -844    213  -1520       N  
ATOM   1665  CA  GLY A1011       5.067 -23.238   6.573  1.00 69.67           C  
ANISOU 1665  CA  GLY A1011     8586  10643   7241   -880    168  -1577       C  
ATOM   1666  C   GLY A1011       5.282 -24.699   6.223  1.00 72.61           C  
ANISOU 1666  C   GLY A1011     8950  11077   7560   -824     58  -1441       C  
ATOM   1667  O   GLY A1011       5.482 -25.514   7.102  1.00 73.37           O  
ANISOU 1667  O   GLY A1011     8982  11345   7550   -786    -14  -1450       O  
ATOM   1668  N   LEU A1012       5.262 -25.032   4.940  1.00 67.19           N  
ANISOU 1668  N   LEU A1012     8316  10262   6953   -817     52  -1320       N  
ATOM   1669  CA  LEU A1012       5.457 -26.409   4.498  1.00 66.07           C  
ANISOU 1669  CA  LEU A1012     8162  10130   6811   -780    -20  -1214       C  
ATOM   1670  C   LEU A1012       6.861 -26.927   4.770  1.00 70.21           C  
ANISOU 1670  C   LEU A1012     8614  10754   7310   -776    -77  -1287       C  
ATOM   1671  O   LEU A1012       7.828 -26.214   4.584  1.00 70.68           O  
ANISOU 1671  O   LEU A1012     8641  10828   7385   -836    -55  -1432       O  
ATOM   1672  CB  LEU A1012       5.137 -26.528   3.015  1.00 64.95           C  
ANISOU 1672  CB  LEU A1012     8065   9861   6754   -807      2  -1147       C  
ATOM   1673  CG  LEU A1012       5.326 -27.875   2.327  1.00 68.47           C  
ANISOU 1673  CG  LEU A1012     8490  10293   7234   -793    -42  -1080       C  
ATOM   1674  CD1 LEU A1012       4.346 -28.910   2.830  1.00 68.49           C  
ANISOU 1674  CD1 LEU A1012     8487  10313   7224   -733    -61   -965       C  
ATOM   1675  CD2 LEU A1012       5.152 -27.691   0.836  1.00 70.10           C  
ANISOU 1675  CD2 LEU A1012     8720  10427   7488   -841    -14  -1063       C  
ATOM   1676  N   ARG A1013       6.954 -28.182   5.196  1.00 65.31           N  
ANISOU 1676  N   ARG A1013     7957  10193   6664   -702   -137  -1178       N  
ATOM   1677  CA  ARG A1013       8.217 -28.832   5.529  1.00 64.65           C  
ANISOU 1677  CA  ARG A1013     7787  10218   6559   -660   -198  -1200       C  
ATOM   1678  C   ARG A1013       8.032 -30.342   5.440  1.00 66.21           C  
ANISOU 1678  C   ARG A1013     7974  10369   6813   -577   -219  -1030       C  
ATOM   1679  O   ARG A1013       7.205 -30.898   6.160  1.00 65.66           O  
ANISOU 1679  O   ARG A1013     7920  10323   6706   -512   -215   -894       O  
ATOM   1680  CB  ARG A1013       8.608 -28.435   6.957  1.00 65.35           C  
ANISOU 1680  CB  ARG A1013     7802  10528   6498   -624   -237  -1259       C  
ATOM   1681  CG  ARG A1013      10.089 -28.426   7.218  1.00 78.25           C  
ANISOU 1681  CG  ARG A1013     9323  12317   8093   -617   -292  -1373       C  
ATOM   1682  CD  ARG A1013      10.674 -27.071   6.907  1.00 84.81           C  
ANISOU 1682  CD  ARG A1013    10138  13138   8947   -740   -242  -1610       C  
ATOM   1683  NE  ARG A1013      11.157 -26.994   5.534  1.00 83.55           N  
ANISOU 1683  NE  ARG A1013    10014  12803   8929   -807   -202  -1651       N  
ATOM   1684  CZ  ARG A1013      11.549 -25.871   4.952  1.00 96.39           C  
ANISOU 1684  CZ  ARG A1013    11653  14349  10623   -919   -124  -1813       C  
ATOM   1685  NH1 ARG A1013      11.511 -24.723   5.617  1.00 83.70           N  
ANISOU 1685  NH1 ARG A1013    10024  12794   8982   -983    -68  -1968       N  
ATOM   1686  NH2 ARG A1013      11.973 -25.881   3.699  1.00 88.20           N  
ANISOU 1686  NH2 ARG A1013    10645  13174   9692   -974    -84  -1824       N  
ATOM   1687  N   LEU A1014       8.789 -31.014   4.570  1.00 61.44           N  
ANISOU 1687  N   LEU A1014     7340   9690   6315   -583   -223  -1044       N  
ATOM   1688  CA  LEU A1014       8.615 -32.462   4.403  1.00 60.76           C  
ANISOU 1688  CA  LEU A1014     7236   9517   6334   -514   -210   -904       C  
ATOM   1689  C   LEU A1014       9.456 -33.306   5.378  1.00 63.99           C  
ANISOU 1689  C   LEU A1014     7552  10040   6721   -384   -256   -798       C  
ATOM   1690  O   LEU A1014       9.323 -34.534   5.416  1.00 64.68           O  
ANISOU 1690  O   LEU A1014     7619  10039   6918   -306   -224   -652       O  
ATOM   1691  CB  LEU A1014       8.848 -32.873   2.946  1.00 60.07           C  
ANISOU 1691  CB  LEU A1014     7154   9282   6389   -586   -170   -975       C  
ATOM   1692  CG  LEU A1014       7.945 -32.206   1.918  1.00 63.47           C  
ANISOU 1692  CG  LEU A1014     7659   9633   6822   -692   -127  -1035       C  
ATOM   1693  CD1 LEU A1014       8.440 -32.456   0.527  1.00 64.06           C  
ANISOU 1693  CD1 LEU A1014     7717   9637   6987   -769    -97  -1133       C  
ATOM   1694  CD2 LEU A1014       6.525 -32.668   2.049  1.00 65.00           C  
ANISOU 1694  CD2 LEU A1014     7895   9770   7033   -680    -94   -930       C  
ATOM   1695  N   LYS A1015      10.282 -32.632   6.182  1.00 58.54           N  
ANISOU 1695  N   LYS A1015     6795   9554   5894   -359   -320   -870       N  
ATOM   1696  CA  LYS A1015      11.148 -33.197   7.213  1.00 59.13           C  
ANISOU 1696  CA  LYS A1015     6755   9824   5890   -225   -385   -776       C  
ATOM   1697  C   LYS A1015      10.418 -32.870   8.551  1.00 63.21           C  
ANISOU 1697  C   LYS A1015     7278  10524   6213   -175   -406   -689       C  
ATOM   1698  O   LYS A1015       9.648 -31.907   8.580  1.00 61.52           O  
ANISOU 1698  O   LYS A1015     7135  10299   5940   -270   -378   -791       O  
ATOM   1699  CB  LYS A1015      12.546 -32.502   7.173  1.00 61.24           C  
ANISOU 1699  CB  LYS A1015     6918  10248   6102   -259   -446   -971       C  
ATOM   1700  CG  LYS A1015      13.358 -32.487   5.829  1.00 60.64           C  
ANISOU 1700  CG  LYS A1015     6832  10023   6187   -344   -418  -1114       C  
ATOM   1701  CD  LYS A1015      12.765 -31.713   4.530  1.00 60.75           C  
ANISOU 1701  CD  LYS A1015     6966   9832   6284   -507   -340  -1244       C  
ATOM   1702  CE  LYS A1015      12.213 -30.286   4.641  1.00 37.76           C  
ANISOU 1702  CE  LYS A1015     4122   6941   3282   -612   -311  -1362       C  
ATOM   1703  NZ  LYS A1015      11.877 -29.693   3.323  1.00 11.04           N  
ANISOU 1703  NZ  LYS A1015      489   3014    692   -535    184   -906       N  
ATOM   1704  N   ILE A1016      10.611 -33.666   9.631  1.00 61.62           N  
ANISOU 1704  N   ILE A1016     7001  10493   5920    -23   -442   -491       N  
ATOM   1705  CA  ILE A1016       9.961 -33.402  10.933  1.00 62.62           C  
ANISOU 1705  CA  ILE A1016     7122  10836   5834     26   -457   -404       C  
ATOM   1706  C   ILE A1016      10.535 -32.123  11.544  1.00 68.89           C  
ANISOU 1706  C   ILE A1016     7840  11905   6428    -44   -521   -643       C  
ATOM   1707  O   ILE A1016      11.750 -32.023  11.717  1.00 70.66           O  
ANISOU 1707  O   ILE A1016     7939  12317   6593    -13   -593   -732       O  
ATOM   1708  CB  ILE A1016      10.055 -34.609  11.925  1.00 67.56           C  
ANISOU 1708  CB  ILE A1016     7677  11595   6397    221   -469    -96       C  
ATOM   1709  CG1 ILE A1016       9.233 -35.814  11.423  1.00 67.57           C  
ANISOU 1709  CG1 ILE A1016     7764  11286   6625    265   -361    125       C  
ATOM   1710  CG2 ILE A1016       9.660 -34.213  13.380  1.00 68.82           C  
ANISOU 1710  CG2 ILE A1016     7795  12084   6269    272   -503    -32       C  
ATOM   1711  CD1 ILE A1016       9.395 -37.085  12.236  1.00 76.42           C  
ANISOU 1711  CD1 ILE A1016     8820  12463   7753    465   -335    458       C  
ATOM   1712  N   TYR A1017       9.672 -31.157  11.873  1.00 65.27           N  
ANISOU 1712  N   TYR A1017     7444  11473   5883   -140   -482   -761       N  
ATOM   1713  CA  TYR A1017      10.116 -29.904  12.470  1.00 66.39           C  
ANISOU 1713  CA  TYR A1017     7509  11849   5866   -227   -508  -1022       C  
ATOM   1714  C   TYR A1017       9.503 -29.653  13.855  1.00 72.74           C  
ANISOU 1714  C   TYR A1017     8275  12930   6432   -194   -513   -995       C  
ATOM   1715  O   TYR A1017       8.828 -30.524  14.396  1.00 72.40           O  
ANISOU 1715  O   TYR A1017     8261  12915   6334    -85   -505   -738       O  
ATOM   1716  CB  TYR A1017       9.889 -28.729  11.502  1.00 66.19           C  
ANISOU 1716  CB  TYR A1017     7568  11598   5985   -396   -434  -1260       C  
ATOM   1717  CG  TYR A1017       8.449 -28.333  11.253  1.00 67.29           C  
ANISOU 1717  CG  TYR A1017     7842  11535   6191   -451   -345  -1227       C  
ATOM   1718  CD1 TYR A1017       7.715 -28.913  10.221  1.00 67.41           C  
ANISOU 1718  CD1 TYR A1017     7967  11266   6379   -449   -303  -1085       C  
ATOM   1719  CD2 TYR A1017       7.855 -27.302  11.974  1.00 69.19           C  
ANISOU 1719  CD2 TYR A1017     8081  11872   6334   -518   -297  -1372       C  
ATOM   1720  CE1 TYR A1017       6.412 -28.498   9.934  1.00 66.60           C  
ANISOU 1720  CE1 TYR A1017     7966  11003   6337   -497   -229  -1067       C  
ATOM   1721  CE2 TYR A1017       6.556 -26.872  11.692  1.00 69.34           C  
ANISOU 1721  CE2 TYR A1017     8210  11699   6436   -561   -211  -1349       C  
ATOM   1722  CZ  TYR A1017       5.837 -27.477  10.675  1.00 74.81           C  
ANISOU 1722  CZ  TYR A1017     9006  12132   7287   -544   -185  -1187       C  
ATOM   1723  OH  TYR A1017       4.555 -27.053  10.415  1.00 74.96           O  
ANISOU 1723  OH  TYR A1017     9109  11998   7375   -577   -111  -1163       O  
ATOM   1724  N   LYS A1018       9.797 -28.486  14.445  1.00 71.62           N  
ANISOU 1724  N   LYS A1018     8056  13005   6153   -292   -516  -1271       N  
ATOM   1725  CA  LYS A1018       9.276 -28.049  15.738  1.00 73.66           C  
ANISOU 1725  CA  LYS A1018     8258  13558   6173   -294   -508  -1325       C  
ATOM   1726  C   LYS A1018       8.496 -26.749  15.525  1.00 80.37           C  
ANISOU 1726  C   LYS A1018     9184  14246   7108   -456   -397  -1575       C  
ATOM   1727  O   LYS A1018       9.016 -25.819  14.897  1.00 80.41           O  
ANISOU 1727  O   LYS A1018     9179  14133   7240   -578   -357  -1826       O  
ATOM   1728  CB  LYS A1018      10.413 -27.839  16.751  1.00 77.46           C  
ANISOU 1728  CB  LYS A1018     8533  14504   6396   -267   -604  -1467       C  
ATOM   1729  CG  LYS A1018      10.657 -29.032  17.660  1.00 84.56           C  
ANISOU 1729  CG  LYS A1018     9340  15707   7083    -68   -696  -1156       C  
ATOM   1730  CD  LYS A1018      11.500 -28.634  18.865  1.00 93.53           C  
ANISOU 1730  CD  LYS A1018    10254  17392   7890    -51   -787  -1320       C  
ATOM   1731  CE  LYS A1018      11.789 -29.787  19.792  1.00101.19           C  
ANISOU 1731  CE  LYS A1018    11115  18707   8624    171   -881   -975       C  
ATOM   1732  NZ  LYS A1018      12.636 -29.368  20.938  1.00110.50           N  
ANISOU 1732  NZ  LYS A1018    12054  20484   9449    187   -984  -1150       N  
ATOM   1733  N   ASP A1019       7.243 -26.685  16.011  1.00 77.87           N  
ANISOU 1733  N   ASP A1019     8939  13901   6746   -453   -332  -1496       N  
ATOM   1734  CA  ASP A1019       6.429 -25.479  15.852  1.00 77.30           C  
ANISOU 1734  CA  ASP A1019     8930  13666   6774   -583   -215  -1711       C  
ATOM   1735  C   ASP A1019       6.802 -24.455  16.924  1.00 82.60           C  
ANISOU 1735  C   ASP A1019     9463  14658   7263   -674   -191  -2027       C  
ATOM   1736  O   ASP A1019       7.573 -24.787  17.826  1.00 83.47           O  
ANISOU 1736  O   ASP A1019     9430  15155   7131   -624   -282  -2047       O  
ATOM   1737  CB  ASP A1019       4.927 -25.821  15.893  1.00 78.73           C  
ANISOU 1737  CB  ASP A1019     9229  13685   6999   -546   -149  -1518       C  
ATOM   1738  CG  ASP A1019       4.363 -26.102  17.273  1.00 93.97           C  
ANISOU 1738  CG  ASP A1019    11104  15923   8677   -492   -148  -1445       C  
ATOM   1739  OD1 ASP A1019       4.990 -26.882  18.024  1.00 96.68           O  
ANISOU 1739  OD1 ASP A1019    11356  16566   8814   -391   -236  -1309       O  
ATOM   1740  OD2 ASP A1019       3.291 -25.547  17.598  1.00101.41           O  
ANISOU 1740  OD2 ASP A1019    12087  16816   9627   -541    -55  -1511       O  
ATOM   1741  N   THR A1020       6.247 -23.219  16.832  1.00 79.06           N  
ANISOU 1741  N   THR A1020     9045  14060   6936   -803    -61  -2276       N  
ATOM   1742  CA  THR A1020       6.472 -22.116  17.785  1.00 80.64           C  
ANISOU 1742  CA  THR A1020     9112  14511   7015   -921      6  -2637       C  
ATOM   1743  C   THR A1020       6.301 -22.560  19.235  1.00 85.69           C  
ANISOU 1743  C   THR A1020     9640  15608   7311   -862    -53  -2605       C  
ATOM   1744  O   THR A1020       7.114 -22.197  20.077  1.00 87.62           O  
ANISOU 1744  O   THR A1020     9709  16235   7346   -913    -88  -2846       O  
ATOM   1745  CB  THR A1020       5.596 -20.896  17.456  1.00 87.09           C  
ANISOU 1745  CB  THR A1020    10002  15029   8059  -1036    184  -2831       C  
ATOM   1746  OG1 THR A1020       4.370 -21.316  16.846  1.00 84.22           O  
ANISOU 1746  OG1 THR A1020     9799  14369   7834   -961    215  -2556       O  
ATOM   1747  CG2 THR A1020       6.305 -19.897  16.566  1.00 84.88           C  
ANISOU 1747  CG2 THR A1020     9720  14499   8031  -1156    275  -3064       C  
ATOM   1748  N   GLU A1021       5.282 -23.394  19.503  1.00 81.17           N  
ANISOU 1748  N   GLU A1021     9156  15014   6670   -753    -62  -2300       N  
ATOM   1749  CA  GLU A1021       4.971 -23.949  20.820  1.00 82.85           C  
ANISOU 1749  CA  GLU A1021     9287  15637   6556   -676   -104  -2188       C  
ATOM   1750  C   GLU A1021       6.010 -24.963  21.323  1.00 86.73           C  
ANISOU 1750  C   GLU A1021     9661  16490   6801   -542   -259  -1997       C  
ATOM   1751  O   GLU A1021       6.036 -25.269  22.516  1.00 88.55           O  
ANISOU 1751  O   GLU A1021     9777  17160   6707   -482   -303  -1946       O  
ATOM   1752  CB  GLU A1021       3.557 -24.546  20.829  1.00 83.51           C  
ANISOU 1752  CB  GLU A1021     9509  15534   6688   -605    -44  -1907       C  
ATOM   1753  CG  GLU A1021       2.444 -23.514  20.903  1.00 98.88           C  
ANISOU 1753  CG  GLU A1021    11504  17312   8753   -716    108  -2114       C  
ATOM   1754  CD  GLU A1021       2.271 -22.874  22.267  1.00137.59           C  
ANISOU 1754  CD  GLU A1021    16272  22615  13392   -786    163  -2366       C  
ATOM   1755  OE1 GLU A1021       1.484 -23.413  23.079  1.00139.90           O  
ANISOU 1755  OE1 GLU A1021    16567  23094  13495   -724    178  -2196       O  
ATOM   1756  OE2 GLU A1021       2.926 -21.837  22.528  1.00139.45           O  
ANISOU 1756  OE2 GLU A1021    16390  22985  13610   -912    202  -2747       O  
ATOM   1757  N   GLY A1022       6.848 -25.465  20.416  1.00 81.53           N  
ANISOU 1757  N   GLY A1022     9025  15659   6294   -490   -335  -1886       N  
ATOM   1758  CA  GLY A1022       7.929 -26.393  20.733  1.00 82.77           C  
ANISOU 1758  CA  GLY A1022     9064  16110   6276   -352   -477  -1705       C  
ATOM   1759  C   GLY A1022       7.683 -27.866  20.474  1.00 85.90           C  
ANISOU 1759  C   GLY A1022     9548  16369   6721   -166   -520  -1241       C  
ATOM   1760  O   GLY A1022       8.571 -28.685  20.723  1.00 86.86           O  
ANISOU 1760  O   GLY A1022     9568  16708   6726    -27   -625  -1056       O  
ATOM   1761  N   TYR A1023       6.491 -28.226  19.990  1.00 80.73           N  
ANISOU 1761  N   TYR A1023     9066  15360   6249   -158   -430  -1055       N  
ATOM   1762  CA  TYR A1023       6.167 -29.629  19.743  1.00 80.05           C  
ANISOU 1762  CA  TYR A1023     9060  15109   6247     -3   -436   -640       C  
ATOM   1763  C   TYR A1023       6.527 -30.036  18.319  1.00 81.74           C  
ANISOU 1763  C   TYR A1023     9362  14915   6781     -6   -440   -589       C  
ATOM   1764  O   TYR A1023       6.606 -29.178  17.436  1.00 79.30           O  
ANISOU 1764  O   TYR A1023     9101  14381   6648   -138   -412   -836       O  
ATOM   1765  CB  TYR A1023       4.686 -29.941  20.048  1.00 80.75           C  
ANISOU 1765  CB  TYR A1023     9263  15068   6350      5   -328   -464       C  
ATOM   1766  CG  TYR A1023       4.053 -29.177  21.197  1.00 83.89           C  
ANISOU 1766  CG  TYR A1023     9606  15770   6497    -58   -281   -622       C  
ATOM   1767  CD1 TYR A1023       4.415 -29.437  22.516  1.00 88.76           C  
ANISOU 1767  CD1 TYR A1023    10084  16884   6755     29   -333   -537       C  
ATOM   1768  CD2 TYR A1023       3.030 -28.264  20.969  1.00 83.48           C  
ANISOU 1768  CD2 TYR A1023     9636  15518   6565   -194   -175   -830       C  
ATOM   1769  CE1 TYR A1023       3.816 -28.758  23.577  1.00 91.19           C  
ANISOU 1769  CE1 TYR A1023    10333  17498   6818    -39   -280   -700       C  
ATOM   1770  CE2 TYR A1023       2.411 -27.594  22.024  1.00 86.10           C  
ANISOU 1770  CE2 TYR A1023     9913  16116   6686   -255   -113   -986       C  
ATOM   1771  CZ  TYR A1023       2.815 -27.835  23.326  1.00 97.19           C  
ANISOU 1771  CZ  TYR A1023    11176  18026   7724   -187   -164   -938       C  
ATOM   1772  OH  TYR A1023       2.207 -27.173  24.368  1.00101.19           O  
ANISOU 1772  OH  TYR A1023    11617  18821   8007   -259    -95  -1118       O  
ATOM   1773  N   TYR A1024       6.750 -31.350  18.098  1.00 78.90           N  
ANISOU 1773  N   TYR A1024     9017  14461   6501    142   -462   -263       N  
ATOM   1774  CA  TYR A1024       7.104 -31.903  16.788  1.00 76.77           C  
ANISOU 1774  CA  TYR A1024     8815  13828   6528    147   -457   -206       C  
ATOM   1775  C   TYR A1024       5.933 -31.871  15.816  1.00 75.98           C  
ANISOU 1775  C   TYR A1024     8875  13319   6674     53   -354   -209       C  
ATOM   1776  O   TYR A1024       4.823 -32.273  16.162  1.00 75.35           O  
ANISOU 1776  O   TYR A1024     8862  13173   6593     74   -279    -50       O  
ATOM   1777  CB  TYR A1024       7.722 -33.305  16.906  1.00 80.01           C  
ANISOU 1777  CB  TYR A1024     9171  14261   6970    334   -490    122       C  
ATOM   1778  CG  TYR A1024       9.048 -33.349  17.643  1.00 84.76           C  
ANISOU 1778  CG  TYR A1024     9588  15265   7351    442   -611    124       C  
ATOM   1779  CD1 TYR A1024      10.195 -32.775  17.096  1.00 86.12           C  
ANISOU 1779  CD1 TYR A1024     9677  15482   7564    380   -687   -129       C  
ATOM   1780  CD2 TYR A1024       9.172 -34.025  18.854  1.00 88.48           C  
ANISOU 1780  CD2 TYR A1024     9959  16082   7579    617   -645    399       C  
ATOM   1781  CE1 TYR A1024      11.420 -32.830  17.760  1.00 88.42           C  
ANISOU 1781  CE1 TYR A1024     9775  16167   7652    479   -804   -143       C  
ATOM   1782  CE2 TYR A1024      10.396 -34.098  19.520  1.00 91.87           C  
ANISOU 1782  CE2 TYR A1024    10194  16924   7787    734   -768    415       C  
ATOM   1783  CZ  TYR A1024      11.517 -33.501  18.968  1.00 98.92           C  
ANISOU 1783  CZ  TYR A1024    10994  17865   8724    662   -852    132       C  
ATOM   1784  OH  TYR A1024      12.721 -33.564  19.627  1.00105.04           O  
ANISOU 1784  OH  TYR A1024    11556  19077   9278    775   -979    129       O  
ATOM   1785  N   THR A1025       6.194 -31.358  14.605  1.00 69.53           N  
ANISOU 1785  N   THR A1025     8108  12256   6055    -53   -350   -396       N  
ATOM   1786  CA  THR A1025       5.224 -31.113  13.533  1.00 66.54           C  
ANISOU 1786  CA  THR A1025     7856  11536   5890   -152   -271   -446       C  
ATOM   1787  C   THR A1025       5.761 -31.562  12.158  1.00 68.18           C  
ANISOU 1787  C   THR A1025     8095  11484   6327   -172   -277   -452       C  
ATOM   1788  O   THR A1025       6.969 -31.703  11.989  1.00 68.73           O  
ANISOU 1788  O   THR A1025     8089  11628   6397   -142   -339   -495       O  
ATOM   1789  CB  THR A1025       4.955 -29.598  13.500  1.00 72.74           C  
ANISOU 1789  CB  THR A1025     8657  12340   6642   -284   -244   -728       C  
ATOM   1790  OG1 THR A1025       5.077 -29.042  14.811  1.00 75.92           O  
ANISOU 1790  OG1 THR A1025     8973  13070   6803   -279   -262   -821       O  
ATOM   1791  CG2 THR A1025       3.617 -29.256  12.938  1.00 69.33           C  
ANISOU 1791  CG2 THR A1025     8333  11671   6340   -350   -158   -732       C  
ATOM   1792  N   ILE A1026       4.869 -31.747  11.172  1.00 62.34           N  
ANISOU 1792  N   ILE A1026     7451  10467   5769   -230   -211   -428       N  
ATOM   1793  CA  ILE A1026       5.227 -32.127   9.801  1.00 61.01           C  
ANISOU 1793  CA  ILE A1026     7309  10071   5801   -270   -203   -459       C  
ATOM   1794  C   ILE A1026       4.294 -31.458   8.782  1.00 65.87           C  
ANISOU 1794  C   ILE A1026     8009  10498   6522   -381   -151   -564       C  
ATOM   1795  O   ILE A1026       3.097 -31.325   9.041  1.00 65.85           O  
ANISOU 1795  O   ILE A1026     8051  10464   6506   -394   -102   -519       O  
ATOM   1796  CB  ILE A1026       5.298 -33.672   9.632  1.00 64.20           C  
ANISOU 1796  CB  ILE A1026     7699  10358   6337   -179   -173   -248       C  
ATOM   1797  CG1 ILE A1026       5.903 -34.086   8.274  1.00 62.95           C  
ANISOU 1797  CG1 ILE A1026     7538  10007   6372   -224   -166   -321       C  
ATOM   1798  CG2 ILE A1026       3.943 -34.341   9.874  1.00 65.60           C  
ANISOU 1798  CG2 ILE A1026     7931  10426   6569   -165    -86    -90       C  
ATOM   1799  CD1 ILE A1026       7.293 -34.526   8.343  1.00 67.00           C  
ANISOU 1799  CD1 ILE A1026     7963  10595   6899   -148   -219   -308       C  
ATOM   1800  N   GLY A1027       4.853 -31.045   7.648  1.00 63.27           N  
ANISOU 1800  N   GLY A1027     7689  10064   6286   -452   -159   -691       N  
ATOM   1801  CA  GLY A1027       4.113 -30.417   6.556  1.00 62.97           C  
ANISOU 1801  CA  GLY A1027     7714   9876   6334   -539   -116   -765       C  
ATOM   1802  C   GLY A1027       3.436 -29.106   6.901  1.00 69.32           C  
ANISOU 1802  C   GLY A1027     8551  10712   7074   -581    -85   -851       C  
ATOM   1803  O   GLY A1027       4.074 -28.192   7.437  1.00 69.65           O  
ANISOU 1803  O   GLY A1027     8565  10854   7043   -603    -92   -977       O  
ATOM   1804  N   ILE A1028       2.124 -29.010   6.597  1.00 66.84           N  
ANISOU 1804  N   ILE A1028     8282  10311   6801   -595    -39   -798       N  
ATOM   1805  CA  ILE A1028       1.353 -27.794   6.867  1.00 66.82           C  
ANISOU 1805  CA  ILE A1028     8305  10309   6773   -620      8   -865       C  
ATOM   1806  C   ILE A1028       0.711 -27.896   8.263  1.00 70.19           C  
ANISOU 1806  C   ILE A1028     8717  10859   7093   -577     25   -823       C  
ATOM   1807  O   ILE A1028      -0.474 -28.225   8.429  1.00 69.37           O  
ANISOU 1807  O   ILE A1028     8630  10725   7001   -560     61   -734       O  
ATOM   1808  CB  ILE A1028       0.377 -27.391   5.716  1.00 69.26           C  
ANISOU 1808  CB  ILE A1028     8652  10487   7178   -649     47   -843       C  
ATOM   1809  CG1 ILE A1028       1.141 -27.278   4.361  1.00 68.53           C  
ANISOU 1809  CG1 ILE A1028     8565  10318   7153   -693     34   -881       C  
ATOM   1810  CG2 ILE A1028      -0.340 -26.071   6.064  1.00 71.05           C  
ANISOU 1810  CG2 ILE A1028     8894  10698   7406   -654    111   -900       C  
ATOM   1811  CD1 ILE A1028       0.394 -26.697   3.197  1.00 71.61           C  
ANISOU 1811  CD1 ILE A1028     8977  10633   7600   -712     67   -853       C  
ATOM   1812  N   GLY A1029       1.564 -27.656   9.250  1.00 66.83           N  
ANISOU 1812  N   GLY A1029     8245  10597   6550   -564     -2   -894       N  
ATOM   1813  CA  GLY A1029       1.225 -27.646  10.666  1.00 67.58           C  
ANISOU 1813  CA  GLY A1029     8306  10878   6495   -528      8   -881       C  
ATOM   1814  C   GLY A1029       0.683 -28.912  11.294  1.00 70.54           C  
ANISOU 1814  C   GLY A1029     8678  11308   6814   -453      6   -674       C  
ATOM   1815  O   GLY A1029       0.135 -28.828  12.397  1.00 71.61           O  
ANISOU 1815  O   GLY A1029     8796  11592   6822   -429     34   -649       O  
ATOM   1816  N   HIS A1030       0.859 -30.093  10.652  1.00 65.12           N  
ANISOU 1816  N   HIS A1030     8003  10510   6229   -417    -11   -531       N  
ATOM   1817  CA  HIS A1030       0.357 -31.344  11.225  1.00 65.25           C  
ANISOU 1817  CA  HIS A1030     8017  10538   6238   -345     20   -321       C  
ATOM   1818  C   HIS A1030       1.143 -31.746  12.458  1.00 71.22           C  
ANISOU 1818  C   HIS A1030     8710  11530   6820   -254    -19   -225       C  
ATOM   1819  O   HIS A1030       2.217 -32.338  12.344  1.00 72.59           O  
ANISOU 1819  O   HIS A1030     8841  11733   7008   -197    -70   -168       O  
ATOM   1820  CB  HIS A1030       0.287 -32.490  10.205  1.00 65.35           C  
ANISOU 1820  CB  HIS A1030     8045  10342   6442   -343     44   -221       C  
ATOM   1821  CG  HIS A1030      -0.322 -33.737  10.774  1.00 69.85           C  
ANISOU 1821  CG  HIS A1030     8612  10877   7051   -282    116    -10       C  
ATOM   1822  ND1 HIS A1030      -1.685 -33.970  10.710  1.00 71.52           N  
ANISOU 1822  ND1 HIS A1030     8851  10993   7331   -321    200     31       N  
ATOM   1823  CD2 HIS A1030       0.266 -34.769  11.423  1.00 73.25           C  
ANISOU 1823  CD2 HIS A1030     9007  11354   7471   -180    127    177       C  
ATOM   1824  CE1 HIS A1030      -1.879 -35.135  11.305  1.00 72.32           C  
ANISOU 1824  CE1 HIS A1030     8940  11067   7472   -257    272    231       C  
ATOM   1825  NE2 HIS A1030      -0.736 -35.651  11.756  1.00 73.76           N  
ANISOU 1825  NE2 HIS A1030     9088  11327   7611   -162    235    342       N  
ATOM   1826  N   LEU A1031       0.620 -31.389  13.637  1.00 67.98           N  
ANISOU 1826  N   LEU A1031     8282  11313   6235   -237      5   -211       N  
ATOM   1827  CA  LEU A1031       1.238 -31.707  14.921  1.00 69.28           C  
ANISOU 1827  CA  LEU A1031     8370  11773   6179   -145    -32   -110       C  
ATOM   1828  C   LEU A1031       1.154 -33.216  15.123  1.00 73.85           C  
ANISOU 1828  C   LEU A1031     8951  12294   6814    -32      6    197       C  
ATOM   1829  O   LEU A1031       0.071 -33.795  15.033  1.00 73.61           O  
ANISOU 1829  O   LEU A1031     8975  12105   6889    -40    100    322       O  
ATOM   1830  CB  LEU A1031       0.543 -30.926  16.057  1.00 70.20           C  
ANISOU 1830  CB  LEU A1031     8466  12113   6094   -172      5   -192       C  
ATOM   1831  CG  LEU A1031       0.699 -31.458  17.479  1.00 76.91           C  
ANISOU 1831  CG  LEU A1031     9244  13290   6686    -71     -2    -21       C  
ATOM   1832  CD1 LEU A1031       1.930 -30.909  18.137  1.00 78.15           C  
ANISOU 1832  CD1 LEU A1031     9287  13781   6624    -53   -100   -159       C  
ATOM   1833  CD2 LEU A1031      -0.513 -31.126  18.304  1.00 80.18           C  
ANISOU 1833  CD2 LEU A1031     9676  13800   6989   -104     86    -25       C  
ATOM   1834  N   LEU A1032       2.308 -33.848  15.328  1.00 71.56           N  
ANISOU 1834  N   LEU A1032     8593  12111   6484     71    -56    312       N  
ATOM   1835  CA  LEU A1032       2.414 -35.295  15.500  1.00 72.81           C  
ANISOU 1835  CA  LEU A1032     8740  12190   6732    199     -5    622       C  
ATOM   1836  C   LEU A1032       2.162 -35.703  16.948  1.00 79.45           C  
ANISOU 1836  C   LEU A1032     9538  13305   7344    314     25    858       C  
ATOM   1837  O   LEU A1032       1.243 -36.474  17.223  1.00 79.26           O  
ANISOU 1837  O   LEU A1032     9559  13165   7390    345    142   1068       O  
ATOM   1838  CB  LEU A1032       3.789 -35.793  15.015  1.00 72.99           C  
ANISOU 1838  CB  LEU A1032     8699  12194   6841    275    -76    652       C  
ATOM   1839  CG  LEU A1032       4.105 -35.545  13.550  1.00 75.02           C  
ANISOU 1839  CG  LEU A1032     8994  12189   7323    169    -92    447       C  
ATOM   1840  CD1 LEU A1032       5.562 -35.232  13.364  1.00 75.57           C  
ANISOU 1840  CD1 LEU A1032     8978  12392   7344    197   -201    332       C  
ATOM   1841  CD2 LEU A1032       3.670 -36.711  12.694  1.00 76.00           C  
ANISOU 1841  CD2 LEU A1032     9163  11980   7734    173     12    575       C  
ATOM   1842  N   THR A1033       2.975 -35.177  17.867  1.00 78.53           N  
ANISOU 1842  N   THR A1033     9323  13570   6946    370    -74    814       N  
ATOM   1843  CA  THR A1033       2.871 -35.440  19.296  1.00 81.93           C  
ANISOU 1843  CA  THR A1033     9686  14355   7088    482    -66   1021       C  
ATOM   1844  C   THR A1033       3.312 -34.217  20.090  1.00 88.79           C  
ANISOU 1844  C   THR A1033    10461  15634   7641    427   -164    761       C  
ATOM   1845  O   THR A1033       4.135 -33.433  19.612  1.00 88.53           O  
ANISOU 1845  O   THR A1033    10383  15636   7618    355   -253    490       O  
ATOM   1846  CB  THR A1033       3.621 -36.742  19.689  1.00 93.43           C  
ANISOU 1846  CB  THR A1033    11075  15879   8546    690    -66   1395       C  
ATOM   1847  OG1 THR A1033       3.302 -37.078  21.043  1.00 98.14           O  
ANISOU 1847  OG1 THR A1033    11622  16802   8867    804    -31   1651       O  
ATOM   1848  CG2 THR A1033       5.145 -36.650  19.512  1.00 91.20           C  
ANISOU 1848  CG2 THR A1033    10676  15765   8213    764   -207   1326       C  
ATOM   1849  N   LYS A1034       2.770 -34.050  21.300  1.00 87.66           N  
ANISOU 1849  N   LYS A1034    10279  15805   7221    451   -132    827       N  
ATOM   1850  CA  LYS A1034       3.182 -32.959  22.176  1.00 88.78           C  
ANISOU 1850  CA  LYS A1034    10306  16384   7044    395   -209    564       C  
ATOM   1851  C   LYS A1034       4.519 -33.355  22.824  1.00 95.23           C  
ANISOU 1851  C   LYS A1034    10960  17600   7624    545   -334    689       C  
ATOM   1852  O   LYS A1034       5.358 -32.489  23.068  1.00 96.26           O  
ANISOU 1852  O   LYS A1034    10969  18022   7582    487   -433    401       O  
ATOM   1853  CB  LYS A1034       2.100 -32.643  23.227  1.00 92.20           C  
ANISOU 1853  CB  LYS A1034    10744  17034   7256    357   -122    568       C  
ATOM   1854  CG  LYS A1034       0.949 -31.801  22.675  1.00 96.20           C  
ANISOU 1854  CG  LYS A1034    11361  17243   7949    185    -26    317       C  
ATOM   1855  CD  LYS A1034       0.255 -30.996  23.764  1.00104.17           C  
ANISOU 1855  CD  LYS A1034    12320  18563   8697    110     30    147       C  
ATOM   1856  CE  LYS A1034      -0.664 -29.931  23.211  1.00106.94           C  
ANISOU 1856  CE  LYS A1034    12746  18648   9237    -56    111   -160       C  
ATOM   1857  NZ  LYS A1034      -1.097 -28.971  24.266  1.00112.83           N  
ANISOU 1857  NZ  LYS A1034    13413  19720   9738   -143    163   -409       N  
ATOM   1858  N   SER A1035       4.723 -34.684  23.026  1.00 92.30           N  
ANISOU 1858  N   SER A1035    10580  17212   7277    740   -317   1117       N  
ATOM   1859  CA  SER A1035       5.890 -35.365  23.608  1.00 94.48           C  
ANISOU 1859  CA  SER A1035    10703  17826   7370    943   -417   1361       C  
ATOM   1860  C   SER A1035       7.266 -34.799  23.198  1.00 97.60           C  
ANISOU 1860  C   SER A1035    10972  18367   7743    920   -568   1092       C  
ATOM   1861  O   SER A1035       7.442 -34.429  22.032  1.00 94.83           O  
ANISOU 1861  O   SER A1035    10696  17654   7680    798   -568    861       O  
ATOM   1862  CB  SER A1035       5.830 -36.857  23.288  1.00 98.20           C  
ANISOU 1862  CB  SER A1035    11234  17994   8085   1122   -331   1816       C  
ATOM   1863  OG  SER A1035       7.050 -37.537  23.541  1.00107.48           O  
ANISOU 1863  OG  SER A1035    12267  19386   9185   1328   -424   2048       O  
ATOM   1864  N   PRO A1036       8.265 -34.780  24.125  1.00 96.24           N  
ANISOU 1864  N   PRO A1036    10597  18737   7232   1042   -694   1133       N  
ATOM   1865  CA  PRO A1036       9.605 -34.276  23.764  1.00 95.82           C  
ANISOU 1865  CA  PRO A1036    10401  18845   7161   1018   -833    868       C  
ATOM   1866  C   PRO A1036      10.495 -35.303  23.042  1.00 98.12           C  
ANISOU 1866  C   PRO A1036    10668  18914   7698   1184   -869   1120       C  
ATOM   1867  O   PRO A1036      11.661 -35.010  22.746  1.00 97.93           O  
ANISOU 1867  O   PRO A1036    10512  19029   7667   1185   -982    935       O  
ATOM   1868  CB  PRO A1036      10.208 -33.854  25.118  1.00101.20           C  
ANISOU 1868  CB  PRO A1036    10852  20245   7354   1077   -949    799       C  
ATOM   1869  CG  PRO A1036       9.185 -34.219  26.170  1.00107.53           C  
ANISOU 1869  CG  PRO A1036    11687  21255   7914   1148   -866   1071       C  
ATOM   1870  CD  PRO A1036       8.227 -35.174  25.545  1.00101.36           C  
ANISOU 1870  CD  PRO A1036    11121  19915   7477   1202   -716   1410       C  
ATOM   1871  N   SER A1037       9.942 -36.501  22.752  1.00 92.92           N  
ANISOU 1871  N   SER A1037    10129  17902   7276   1315   -756   1522       N  
ATOM   1872  CA  SER A1037      10.632 -37.590  22.066  1.00 92.16           C  
ANISOU 1872  CA  SER A1037    10020  17531   7465   1476   -746   1782       C  
ATOM   1873  C   SER A1037      10.426 -37.503  20.559  1.00 90.97           C  
ANISOU 1873  C   SER A1037    10023  16802   7738   1313   -677   1568       C  
ATOM   1874  O   SER A1037       9.285 -37.466  20.098  1.00 88.93           O  
ANISOU 1874  O   SER A1037     9936  16197   7658   1189   -555   1533       O  
ATOM   1875  CB  SER A1037      10.145 -38.938  22.590  1.00 97.61           C  
ANISOU 1875  CB  SER A1037    10743  18138   8207   1698   -629   2321       C  
ATOM   1876  OG  SER A1037      10.521 -40.014  21.745  1.00105.52           O  
ANISOU 1876  OG  SER A1037    11777  18722   9594   1814   -556   2543       O  
ATOM   1877  N   LEU A1038      11.531 -37.479  19.793  1.00 85.61           N  
ANISOU 1877  N   LEU A1038     9270  16049   7210   1317   -753   1424       N  
ATOM   1878  CA  LEU A1038      11.499 -37.444  18.326  1.00 81.60           C  
ANISOU 1878  CA  LEU A1038     8882  15042   7079   1176   -694   1228       C  
ATOM   1879  C   LEU A1038      11.075 -38.814  17.779  1.00 84.55           C  
ANISOU 1879  C   LEU A1038     9348  14984   7791   1287   -552   1559       C  
ATOM   1880  O   LEU A1038      10.413 -38.869  16.745  1.00 81.21           O  
ANISOU 1880  O   LEU A1038     9068  14137   7650   1146   -453   1443       O  
ATOM   1881  CB  LEU A1038      12.866 -37.022  17.753  1.00 81.18           C  
ANISOU 1881  CB  LEU A1038     8704  15078   7062   1150   -809    979       C  
ATOM   1882  CG  LEU A1038      12.992 -36.941  16.228  1.00 82.62           C  
ANISOU 1882  CG  LEU A1038     8988  14805   7599   1006   -756    766       C  
ATOM   1883  CD1 LEU A1038      12.452 -35.635  15.699  1.00 80.26           C  
ANISOU 1883  CD1 LEU A1038     8795  14409   7292    752   -744    386       C  
ATOM   1884  CD2 LEU A1038      14.427 -37.124  15.790  1.00 85.63           C  
ANISOU 1884  CD2 LEU A1038     9221  15255   8058   1076   -840    693       C  
ATOM   1885  N   ASN A1039      11.446 -39.910  18.484  1.00 83.41           N  
ANISOU 1885  N   ASN A1039     9109  14961   7621   1539   -532   1970       N  
ATOM   1886  CA  ASN A1039      11.101 -41.288  18.120  1.00 83.24           C  
ANISOU 1886  CA  ASN A1039     9151  14536   7939   1666   -366   2314       C  
ATOM   1887  C   ASN A1039       9.608 -41.552  18.265  1.00 84.63           C  
ANISOU 1887  C   ASN A1039     9488  14478   8191   1588   -205   2433       C  
ATOM   1888  O   ASN A1039       9.065 -42.389  17.544  1.00 82.97           O  
ANISOU 1888  O   ASN A1039     9373  13816   8337   1568    -42   2532       O  
ATOM   1889  CB  ASN A1039      11.924 -42.285  18.922  1.00 87.27           C  
ANISOU 1889  CB  ASN A1039     9504  15262   8392   1973   -379   2740       C  
ATOM   1890  CG  ASN A1039      13.401 -42.206  18.628  1.00111.16           C  
ANISOU 1890  CG  ASN A1039    12358  18457  11419   2063   -518   2636       C  
ATOM   1891  OD1 ASN A1039      13.836 -42.103  17.470  1.00100.18           O  
ANISOU 1891  OD1 ASN A1039    10994  16775  10296   1948   -515   2378       O  
ATOM   1892  ND2 ASN A1039      14.209 -42.258  19.676  1.00108.70           N  
ANISOU 1892  ND2 ASN A1039    11856  18648  10796   2271   -644   2833       N  
ATOM   1893  N   ALA A1040       8.947 -40.816  19.180  1.00 81.00           N  
ANISOU 1893  N   ALA A1040     9045  14331   7399   1531   -242   2391       N  
ATOM   1894  CA  ALA A1040       7.504 -40.860  19.396  1.00 80.07           C  
ANISOU 1894  CA  ALA A1040     9067  14053   7304   1436   -104   2452       C  
ATOM   1895  C   ALA A1040       6.852 -40.169  18.212  1.00 81.05           C  
ANISOU 1895  C   ALA A1040     9321  13838   7635   1181    -77   2070       C  
ATOM   1896  O   ALA A1040       5.901 -40.706  17.653  1.00 80.55           O  
ANISOU 1896  O   ALA A1040     9370  13400   7835   1110     73   2120       O  
ATOM   1897  CB  ALA A1040       7.139 -40.133  20.678  1.00 82.19           C  
ANISOU 1897  CB  ALA A1040     9292  14799   7139   1438   -167   2456       C  
ATOM   1898  N   ALA A1041       7.391 -38.994  17.809  1.00 75.58           N  
ANISOU 1898  N   ALA A1041     8601  13285   6832   1046   -214   1693       N  
ATOM   1899  CA  ALA A1041       6.923 -38.218  16.663  1.00 72.08           C  
ANISOU 1899  CA  ALA A1041     8263  12565   6558    823   -203   1342       C  
ATOM   1900  C   ALA A1041       7.120 -39.013  15.366  1.00 76.05           C  
ANISOU 1900  C   ALA A1041     8810  12644   7442    804   -129   1344       C  
ATOM   1901  O   ALA A1041       6.198 -39.068  14.548  1.00 74.54           O  
ANISOU 1901  O   ALA A1041     8728  12139   7456    672    -33   1247       O  
ATOM   1902  CB  ALA A1041       7.661 -36.894  16.595  1.00 71.61           C  
ANISOU 1902  CB  ALA A1041     8142  12752   6313    717   -345    991       C  
ATOM   1903  N   LYS A1042       8.300 -39.677  15.214  1.00 73.54           N  
ANISOU 1903  N   LYS A1042     8390  12336   7217    943   -166   1457       N  
ATOM   1904  CA  LYS A1042       8.671 -40.524  14.070  1.00 72.31           C  
ANISOU 1904  CA  LYS A1042     8243  11809   7423    945    -89   1460       C  
ATOM   1905  C   LYS A1042       7.720 -41.712  13.945  1.00 75.83           C  
ANISOU 1905  C   LYS A1042     8762  11915   8137    980    107   1703       C  
ATOM   1906  O   LYS A1042       7.424 -42.128  12.829  1.00 73.37           O  
ANISOU 1906  O   LYS A1042     8503  11250   8125    875    205   1583       O  
ATOM   1907  CB  LYS A1042      10.130 -41.008  14.177  1.00 76.56           C  
ANISOU 1907  CB  LYS A1042     8633  12475   7982   1120   -163   1567       C  
ATOM   1908  CG  LYS A1042      11.156 -39.985  13.707  1.00 88.00           C  
ANISOU 1908  CG  LYS A1042    10013  14101   9322   1028   -315   1236       C  
ATOM   1909  CD  LYS A1042      12.572 -40.550  13.652  1.00 99.54           C  
ANISOU 1909  CD  LYS A1042    11319  15648  10855   1192   -374   1322       C  
ATOM   1910  CE  LYS A1042      13.523 -39.589  12.974  1.00106.94           C  
ANISOU 1910  CE  LYS A1042    12198  16685  11747   1065   -491    960       C  
ATOM   1911  NZ  LYS A1042      14.935 -40.045  13.065  1.00118.58           N  
ANISOU 1911  NZ  LYS A1042    13493  18313  13250   1231   -565   1031       N  
ATOM   1912  N   SER A1043       7.232 -42.237  15.096  1.00 74.85           N  
ANISOU 1912  N   SER A1043     8630  11913   7897   1118    174   2031       N  
ATOM   1913  CA  SER A1043       6.260 -43.330  15.179  1.00 75.66           C  
ANISOU 1913  CA  SER A1043     8796  11714   8237   1151    385   2286       C  
ATOM   1914  C   SER A1043       4.892 -42.817  14.734  1.00 77.53           C  
ANISOU 1914  C   SER A1043     9155  11795   8507    931    449   2069       C  
ATOM   1915  O   SER A1043       4.211 -43.504  13.975  1.00 76.50           O  
ANISOU 1915  O   SER A1043     9077  11301   8687    846    605   2045       O  
ATOM   1916  CB  SER A1043       6.180 -43.880  16.602  1.00 81.40           C  
ANISOU 1916  CB  SER A1043     9475  12674   8779   1361    431   2705       C  
ATOM   1917  OG  SER A1043       5.079 -44.760  16.766  1.00 89.33           O  
ANISOU 1917  OG  SER A1043    10555  13400   9987   1361    651   2929       O  
ATOM   1918  N   GLU A1044       4.507 -41.602  15.196  1.00 73.27           N  
ANISOU 1918  N   GLU A1044     8645  11540   7655    839    333   1895       N  
ATOM   1919  CA  GLU A1044       3.241 -40.935  14.868  1.00 71.20           C  
ANISOU 1919  CA  GLU A1044     8481  11188   7385    650    371   1687       C  
ATOM   1920  C   GLU A1044       3.155 -40.636  13.379  1.00 72.30           C  
ANISOU 1920  C   GLU A1044     8663  11064   7745    479    363   1377       C  
ATOM   1921  O   GLU A1044       2.076 -40.725  12.792  1.00 70.71           O  
ANISOU 1921  O   GLU A1044     8525  10649   7692    351    459   1283       O  
ATOM   1922  CB  GLU A1044       3.061 -39.634  15.684  1.00 72.10           C  
ANISOU 1922  CB  GLU A1044     8593  11670   7131    604    248   1549       C  
ATOM   1923  CG  GLU A1044       2.717 -39.827  17.153  1.00 84.30           C  
ANISOU 1923  CG  GLU A1044    10110  13497   8423    725    281   1817       C  
ATOM   1924  CD  GLU A1044       1.702 -40.910  17.460  1.00109.45           C  
ANISOU 1924  CD  GLU A1044    13346  16470  11771    766    479   2104       C  
ATOM   1925  OE1 GLU A1044       0.528 -40.770  17.044  1.00 99.83           O  
ANISOU 1925  OE1 GLU A1044    12206  15052  10672    621    571   1981       O  
ATOM   1926  OE2 GLU A1044       2.090 -41.909  18.106  1.00110.87           O  
ANISOU 1926  OE2 GLU A1044    13477  16679  11969    949    550   2458       O  
ATOM   1927  N   LEU A1045       4.301 -40.287  12.779  1.00 68.04           N  
ANISOU 1927  N   LEU A1045     8075  10566   7211    480    250   1221       N  
ATOM   1928  CA  LEU A1045       4.442 -39.990  11.362  1.00 66.23           C  
ANISOU 1928  CA  LEU A1045     7870  10137   7156    335    233    942       C  
ATOM   1929  C   LEU A1045       4.176 -41.256  10.539  1.00 72.40           C  
ANISOU 1929  C   LEU A1045     8654  10564   8291    319    391   1003       C  
ATOM   1930  O   LEU A1045       3.338 -41.228   9.632  1.00 70.52           O  
ANISOU 1930  O   LEU A1045     8463  10140   8192    168    455    832       O  
ATOM   1931  CB  LEU A1045       5.853 -39.427  11.102  1.00 65.80           C  
ANISOU 1931  CB  LEU A1045     7747  10238   7016    361     92    804       C  
ATOM   1932  CG  LEU A1045       6.158 -38.918   9.700  1.00 68.18           C  
ANISOU 1932  CG  LEU A1045     8069  10398   7438    213     60    512       C  
ATOM   1933  CD1 LEU A1045       5.399 -37.651   9.392  1.00 66.10           C  
ANISOU 1933  CD1 LEU A1045     7879  10190   7045     61     16    295       C  
ATOM   1934  CD2 LEU A1045       7.620 -38.661   9.545  1.00 70.98           C  
ANISOU 1934  CD2 LEU A1045     8339  10880   7751    263    -44    428       C  
ATOM   1935  N   ASP A1046       4.847 -42.376  10.903  1.00 72.09           N  
ANISOU 1935  N   ASP A1046     8550  10442   8399    481    465   1249       N  
ATOM   1936  CA  ASP A1046       4.687 -43.685  10.263  1.00 73.08           C  
ANISOU 1936  CA  ASP A1046     8658  10209   8899    484    651   1322       C  
ATOM   1937  C   ASP A1046       3.234 -44.188  10.419  1.00 74.85           C  
ANISOU 1937  C   ASP A1046     8941  10254   9244    407    821   1396       C  
ATOM   1938  O   ASP A1046       2.725 -44.862   9.526  1.00 75.16           O  
ANISOU 1938  O   ASP A1046     8980  10002   9574    296    964   1280       O  
ATOM   1939  CB  ASP A1046       5.701 -44.708  10.837  1.00 78.52           C  
ANISOU 1939  CB  ASP A1046     9258  10864   9711    710    706   1623       C  
ATOM   1940  CG  ASP A1046       7.194 -44.379  10.683  1.00 93.32           C  
ANISOU 1940  CG  ASP A1046    11045  12909  11505    800    553   1560       C  
ATOM   1941  OD1 ASP A1046       7.519 -43.313  10.113  1.00 92.25           O  
ANISOU 1941  OD1 ASP A1046    10922  12913  11216    675    407   1267       O  
ATOM   1942  OD2 ASP A1046       8.036 -45.187  11.150  1.00101.52           O  
ANISOU 1942  OD2 ASP A1046    11993  13942  12639   1002    588   1815       O  
ATOM   1943  N   LYS A1047       2.563 -43.812  11.530  1.00 69.01           N  
ANISOU 1943  N   LYS A1047     8240   9709   8271    451    807   1556       N  
ATOM   1944  CA  LYS A1047       1.174 -44.158  11.836  1.00 68.05           C  
ANISOU 1944  CA  LYS A1047     8170   9468   8219    381    960   1632       C  
ATOM   1945  C   LYS A1047       0.200 -43.395  10.935  1.00 67.29           C  
ANISOU 1945  C   LYS A1047     8120   9332   8115    164    928   1302       C  
ATOM   1946  O   LYS A1047      -0.761 -43.986  10.444  1.00 66.13           O  
ANISOU 1946  O   LYS A1047     7978   8958   8188     54   1081   1243       O  
ATOM   1947  CB  LYS A1047       0.858 -43.857  13.317  1.00 71.94           C  
ANISOU 1947  CB  LYS A1047     8679  10237   8417    496    936   1884       C  
ATOM   1948  CG  LYS A1047       1.229 -44.971  14.288  1.00 85.76           C  
ANISOU 1948  CG  LYS A1047    10388  11962  10236    707   1063   2305       C  
ATOM   1949  CD  LYS A1047       1.044 -44.547  15.742  1.00 94.53           C  
ANISOU 1949  CD  LYS A1047    11500  13434  10983    821   1009   2536       C  
ATOM   1950  CE  LYS A1047       1.685 -45.542  16.682  1.00113.28           C  
ANISOU 1950  CE  LYS A1047    13813  15861  13369   1070   1094   2980       C  
ATOM   1951  NZ  LYS A1047       1.571 -45.133  18.107  1.00125.47           N  
ANISOU 1951  NZ  LYS A1047    15340  17820  14513   1186   1034   3208       N  
ATOM   1952  N   ALA A1048       0.444 -42.078  10.740  1.00 61.80           N  
ANISOU 1952  N   ALA A1048     7446   8866   7170    106    740   1094       N  
ATOM   1953  CA  ALA A1048      -0.379 -41.163   9.933  1.00 58.71           C  
ANISOU 1953  CA  ALA A1048     7092   8485   6730    -66    687    813       C  
ATOM   1954  C   ALA A1048      -0.172 -41.291   8.421  1.00 59.02           C  
ANISOU 1954  C   ALA A1048     7108   8354   6963   -187    688    569       C  
ATOM   1955  O   ALA A1048      -1.056 -40.895   7.669  1.00 56.58           O  
ANISOU 1955  O   ALA A1048     6811   8014   6673   -324    692    381       O  
ATOM   1956  CB  ALA A1048      -0.152 -39.719  10.371  1.00 58.08           C  
ANISOU 1956  CB  ALA A1048     7038   8692   6339    -66    518    712       C  
ATOM   1957  N   ILE A1049       0.983 -41.819   7.973  1.00 56.05           N  
ANISOU 1957  N   ILE A1049     6687   7894   6714   -134    681    568       N  
ATOM   1958  CA  ILE A1049       1.277 -41.985   6.543  1.00 55.05           C  
ANISOU 1958  CA  ILE A1049     6528   7629   6760   -251    690    328       C  
ATOM   1959  C   ILE A1049       1.080 -43.460   6.111  1.00 60.59           C  
ANISOU 1959  C   ILE A1049     7176   8034   7813   -273    893    358       C  
ATOM   1960  O   ILE A1049       0.764 -43.724   4.953  1.00 59.31           O  
ANISOU 1960  O   ILE A1049     6977   7750   7807   -416    952    129       O  
ATOM   1961  CB  ILE A1049       2.666 -41.367   6.153  1.00 57.13           C  
ANISOU 1961  CB  ILE A1049     6771   8011   6923   -215    546    229       C  
ATOM   1962  CG1 ILE A1049       2.569 -39.832   6.034  1.00 55.62           C  
ANISOU 1962  CG1 ILE A1049     6628   8039   6464   -281    392     78       C  
ATOM   1963  CG2 ILE A1049       3.189 -41.901   4.825  1.00 57.26           C  
ANISOU 1963  CG2 ILE A1049     6736   7865   7157   -300    595     39       C  
ATOM   1964  CD1 ILE A1049       2.641 -39.035   7.309  1.00 66.27           C  
ANISOU 1964  CD1 ILE A1049     8006   9615   7560   -191    303    197       C  
ATOM   1965  N   GLY A1050       1.213 -44.386   7.049  1.00 60.52           N  
ANISOU 1965  N   GLY A1050     7153   7918   7923   -135   1012    636       N  
ATOM   1966  CA  GLY A1050       1.021 -45.802   6.775  1.00 63.63           C  
ANISOU 1966  CA  GLY A1050     7494   7992   8691   -144   1243    691       C  
ATOM   1967  C   GLY A1050       2.199 -46.458   6.091  1.00 72.36           C  
ANISOU 1967  C   GLY A1050     8529   8944  10020   -103   1281    632       C  
ATOM   1968  O   GLY A1050       2.057 -47.560   5.550  1.00 74.83           O  
ANISOU 1968  O   GLY A1050     8783   8965  10682   -155   1484    578       O  
ATOM   1969  N   ARG A1051       3.373 -45.784   6.110  1.00 69.01           N  
ANISOU 1969  N   ARG A1051     8098   8711   9411    -17   1101    623       N  
ATOM   1970  CA  ARG A1051       4.629 -46.289   5.548  1.00 69.92           C  
ANISOU 1970  CA  ARG A1051     8138   8723   9706     42   1114    574       C  
ATOM   1971  C   ARG A1051       5.829 -45.873   6.412  1.00 75.06           C  
ANISOU 1971  C   ARG A1051     8768   9598  10153    242    960    773       C  
ATOM   1972  O   ARG A1051       5.730 -44.901   7.169  1.00 73.68           O  
ANISOU 1972  O   ARG A1051     8641   9702   9651    278    806    837       O  
ATOM   1973  CB  ARG A1051       4.806 -45.894   4.062  1.00 68.26           C  
ANISOU 1973  CB  ARG A1051     7904   8504   9526   -146   1067    194       C  
ATOM   1974  CG  ARG A1051       5.290 -44.470   3.811  1.00 74.17           C  
ANISOU 1974  CG  ARG A1051     8693   9546   9943   -186    836     50       C  
ATOM   1975  CD  ARG A1051       5.795 -44.282   2.398  1.00 81.55           C  
ANISOU 1975  CD  ARG A1051     9586  10461  10937   -325    814   -258       C  
ATOM   1976  NE  ARG A1051       6.093 -42.877   2.123  1.00 89.11           N  
ANISOU 1976  NE  ARG A1051    10591  11673  11595   -378    625   -384       N  
ATOM   1977  CZ  ARG A1051       7.313 -42.349   2.088  1.00106.00           C  
ANISOU 1977  CZ  ARG A1051    12707  13935  13634   -322    513   -414       C  
ATOM   1978  NH1 ARG A1051       8.381 -43.110   2.303  1.00 98.65           N  
ANISOU 1978  NH1 ARG A1051    11698  12920  12865   -198    553   -326       N  
ATOM   1979  NH2 ARG A1051       7.477 -41.060   1.829  1.00 89.82           N  
ANISOU 1979  NH2 ARG A1051    10703  12085  11341   -387    375   -534       N  
ATOM   1980  N   ASN A1052       6.954 -46.609   6.299  1.00 73.58           N  
ANISOU 1980  N   ASN A1052     8493   9299  10165    368   1007    853       N  
ATOM   1981  CA  ASN A1052       8.175 -46.309   7.039  1.00 74.38           C  
ANISOU 1981  CA  ASN A1052     8540   9630  10092    562    863   1024       C  
ATOM   1982  C   ASN A1052       8.842 -45.107   6.383  1.00 76.23           C  
ANISOU 1982  C   ASN A1052     8776  10087  10101    455    665    732       C  
ATOM   1983  O   ASN A1052       9.641 -45.249   5.454  1.00 75.74           O  
ANISOU 1983  O   ASN A1052     8655   9940  10182    410    668    545       O  
ATOM   1984  CB  ASN A1052       9.093 -47.527   7.095  1.00 80.51           C  
ANISOU 1984  CB  ASN A1052     9208  10198  11185    742    994   1213       C  
ATOM   1985  CG  ASN A1052       8.512 -48.683   7.871  1.00118.01           C  
ANISOU 1985  CG  ASN A1052    13954  14724  16162    877   1207   1560       C  
ATOM   1986  OD1 ASN A1052       8.058 -48.541   9.018  1.00112.14           O  
ANISOU 1986  OD1 ASN A1052    13249  14146  15214    986   1181   1837       O  
ATOM   1987  ND2 ASN A1052       8.523 -49.860   7.260  1.00116.85           N  
ANISOU 1987  ND2 ASN A1052    13753  14191  16452    870   1440   1547       N  
ATOM   1988  N   THR A1053       8.444 -43.912   6.841  1.00 71.06           N  
ANISOU 1988  N   THR A1053     8189   9701   9109    401    515    682       N  
ATOM   1989  CA  THR A1053       8.879 -42.613   6.321  1.00 68.49           C  
ANISOU 1989  CA  THR A1053     7883   9580   8560    285    349    419       C  
ATOM   1990  C   THR A1053      10.300 -42.258   6.723  1.00 73.10           C  
ANISOU 1990  C   THR A1053     8376  10382   9017    408    217    441       C  
ATOM   1991  O   THR A1053      11.046 -41.712   5.910  1.00 72.45           O  
ANISOU 1991  O   THR A1053     8267  10338   8924    322    150    210       O  
ATOM   1992  CB  THR A1053       7.907 -41.519   6.772  1.00 73.10           C  
ANISOU 1992  CB  THR A1053     8560  10341   8873    199    270    375       C  
ATOM   1993  OG1 THR A1053       7.890 -41.504   8.195  1.00 76.98           O  
ANISOU 1993  OG1 THR A1053     9039  11027   9184    352    230    628       O  
ATOM   1994  CG2 THR A1053       6.501 -41.726   6.244  1.00 68.00           C  
ANISOU 1994  CG2 THR A1053     7987   9514   8334     60    381    306       C  
ATOM   1995  N   ASN A1054      10.663 -42.553   7.981  1.00 70.93           N  
ANISOU 1995  N   ASN A1054     8043  10274   8634    607    181    720       N  
ATOM   1996  CA  ASN A1054      11.959 -42.254   8.594  1.00 71.69           C  
ANISOU 1996  CA  ASN A1054     8022  10648   8570    749     45    773       C  
ATOM   1997  C   ASN A1054      12.221 -40.737   8.677  1.00 73.13           C  
ANISOU 1997  C   ASN A1054     8219  11123   8445    632   -120    530       C  
ATOM   1998  O   ASN A1054      13.347 -40.279   8.453  1.00 72.75           O  
ANISOU 1998  O   ASN A1054     8083  11218   8341    634   -216    383       O  
ATOM   1999  CB  ASN A1054      13.128 -43.024   7.945  1.00 72.30           C  
ANISOU 1999  CB  ASN A1054     7985  10586   8899    830     83    755       C  
ATOM   2000  CG  ASN A1054      14.214 -43.392   8.931  1.00 95.37           C  
ANISOU 2000  CG  ASN A1054    10757  13738  11741   1080      8    999       C  
ATOM   2001  OD1 ASN A1054      14.633 -42.592   9.780  1.00 84.41           O  
ANISOU 2001  OD1 ASN A1054     9315  12722  10035   1132   -149   1009       O  
ATOM   2002  ND2 ASN A1054      14.693 -44.623   8.848  1.00 92.60           N  
ANISOU 2002  ND2 ASN A1054    10320  13181  11682   1243    125   1198       N  
ATOM   2003  N   GLY A1055      11.170 -39.989   9.027  1.00 67.74           N  
ANISOU 2003  N   GLY A1055     7638  10515   7585    533   -135    488       N  
ATOM   2004  CA  GLY A1055      11.229 -38.543   9.217  1.00 65.94           C  
ANISOU 2004  CA  GLY A1055     7431  10530   7095    422   -254    271       C  
ATOM   2005  C   GLY A1055      10.945 -37.691   7.998  1.00 65.69           C  
ANISOU 2005  C   GLY A1055     7483  10359   7116    212   -245    -22       C  
ATOM   2006  O   GLY A1055      10.790 -36.472   8.123  1.00 64.16           O  
ANISOU 2006  O   GLY A1055     7324  10309   6745    112   -306   -187       O  
ATOM   2007  N   VAL A1056      10.916 -38.312   6.809  1.00 60.13           N  
ANISOU 2007  N   VAL A1056     6801   9388   6658    147   -161    -90       N  
ATOM   2008  CA  VAL A1056      10.672 -37.598   5.560  1.00 57.18           C  
ANISOU 2008  CA  VAL A1056     6495   8906   6326    -39   -148   -340       C  
ATOM   2009  C   VAL A1056       9.438 -38.125   4.871  1.00 60.84           C  
ANISOU 2009  C   VAL A1056     7037   9143   6935   -123    -38   -332       C  
ATOM   2010  O   VAL A1056       9.293 -39.333   4.672  1.00 61.08           O  
ANISOU 2010  O   VAL A1056     7040   8989   7177    -76     63   -233       O  
ATOM   2011  CB  VAL A1056      11.874 -37.576   4.573  1.00 60.17           C  
ANISOU 2011  CB  VAL A1056     6806   9247   6809    -84   -161   -515       C  
ATOM   2012  CG1 VAL A1056      11.797 -36.364   3.650  1.00 57.81           C  
ANISOU 2012  CG1 VAL A1056     6570   8962   6433   -259   -182   -752       C  
ATOM   2013  CG2 VAL A1056      13.216 -37.605   5.298  1.00 61.57           C  
ANISOU 2013  CG2 VAL A1056     6855   9620   6918     46   -246   -476       C  
ATOM   2014  N   ILE A1057       8.567 -37.203   4.470  1.00 56.70           N  
ANISOU 2014  N   ILE A1057     6597   8631   6313   -250    -48   -450       N  
ATOM   2015  CA  ILE A1057       7.374 -37.518   3.694  1.00 56.29           C  
ANISOU 2015  CA  ILE A1057     6602   8418   6367   -350     38   -487       C  
ATOM   2016  C   ILE A1057       7.461 -36.855   2.306  1.00 59.88           C  
ANISOU 2016  C   ILE A1057     7076   8849   6825   -496     29   -706       C  
ATOM   2017  O   ILE A1057       8.265 -35.940   2.099  1.00 59.14           O  
ANISOU 2017  O   ILE A1057     6979   8858   6632   -525    -37   -811       O  
ATOM   2018  CB  ILE A1057       6.046 -37.237   4.441  1.00 59.23           C  
ANISOU 2018  CB  ILE A1057     7040   8826   6639   -349     53   -386       C  
ATOM   2019  CG1 ILE A1057       5.914 -35.756   4.859  1.00 58.78           C  
ANISOU 2019  CG1 ILE A1057     7029   8947   6360   -383    -33   -459       C  
ATOM   2020  CG2 ILE A1057       5.908 -38.175   5.633  1.00 61.90           C  
ANISOU 2020  CG2 ILE A1057     7352   9157   7008   -211     99   -146       C  
ATOM   2021  CD1 ILE A1057       4.503 -35.267   4.965  1.00 64.23           C  
ANISOU 2021  CD1 ILE A1057     7784   9631   6990   -437     -5   -451       C  
ATOM   2022  N   THR A1058       6.667 -37.357   1.354  1.00 55.85           N  
ANISOU 2022  N   THR A1058     6574   8217   6429   -588    106   -775       N  
ATOM   2023  CA  THR A1058       6.590 -36.860  -0.013  1.00 54.32           C  
ANISOU 2023  CA  THR A1058     6387   8033   6220   -721    108   -956       C  
ATOM   2024  C   THR A1058       5.680 -35.611  -0.014  1.00 57.41           C  
ANISOU 2024  C   THR A1058     6851   8527   6436   -768     61   -961       C  
ATOM   2025  O   THR A1058       4.937 -35.422   0.952  1.00 56.56           O  
ANISOU 2025  O   THR A1058     6780   8446   6266   -715     51   -848       O  
ATOM   2026  CB  THR A1058       6.167 -38.041  -0.911  1.00 60.99           C  
ANISOU 2026  CB  THR A1058     7177   8741   7256   -792    215  -1038       C  
ATOM   2027  OG1 THR A1058       6.799 -37.953  -2.176  1.00 66.68           O  
ANISOU 2027  OG1 THR A1058     7858   9480   7997   -889    224  -1219       O  
ATOM   2028  CG2 THR A1058       4.676 -38.183  -1.069  1.00 54.96           C  
ANISOU 2028  CG2 THR A1058     6432   7961   6491   -856    261  -1036       C  
ATOM   2029  N   LYS A1059       5.740 -34.755  -1.058  1.00 54.90           N  
ANISOU 2029  N   LYS A1059     6549   8267   6042   -857     42  -1076       N  
ATOM   2030  CA  LYS A1059       4.875 -33.558  -1.102  1.00 55.14           C  
ANISOU 2030  CA  LYS A1059     6641   8374   5936   -881     14  -1056       C  
ATOM   2031  C   LYS A1059       3.379 -33.888  -1.167  1.00 60.76           C  
ANISOU 2031  C   LYS A1059     7354   9077   6656   -900     45  -1012       C  
ATOM   2032  O   LYS A1059       2.580 -33.262  -0.462  1.00 59.82           O  
ANISOU 2032  O   LYS A1059     7276   8990   6462   -863     30   -933       O  
ATOM   2033  CB  LYS A1059       5.253 -32.587  -2.231  1.00 57.63           C  
ANISOU 2033  CB  LYS A1059     6970   8749   6178   -955      6  -1145       C  
ATOM   2034  CG  LYS A1059       4.777 -31.153  -1.953  1.00 72.44           C  
ANISOU 2034  CG  LYS A1059     8909  10674   7942   -941    -12  -1095       C  
ATOM   2035  CD  LYS A1059       3.829 -30.598  -3.012  1.00 81.61           C  
ANISOU 2035  CD  LYS A1059    10079  11888   9041   -986      5  -1081       C  
ATOM   2036  CE  LYS A1059       3.611 -29.119  -2.794  1.00 90.19           C  
ANISOU 2036  CE  LYS A1059    11223  12984  10061   -960     13  -1025       C  
ATOM   2037  NZ  LYS A1059       3.570 -28.364  -4.074  1.00101.78           N  
ANISOU 2037  NZ  LYS A1059    12696  14504  11473   -999     40  -1012       N  
ATOM   2038  N   ASP A1060       3.007 -34.877  -1.991  1.00 59.30           N  
ANISOU 2038  N   ASP A1060     7111   8853   6570   -965     98  -1085       N  
ATOM   2039  CA  ASP A1060       1.606 -35.270  -2.130  1.00 60.47           C  
ANISOU 2039  CA  ASP A1060     7232   9007   6737  -1001    137  -1079       C  
ATOM   2040  C   ASP A1060       1.076 -36.018  -0.889  1.00 63.99           C  
ANISOU 2040  C   ASP A1060     7687   9357   7271   -936    182   -962       C  
ATOM   2041  O   ASP A1060      -0.140 -36.212  -0.769  1.00 63.30           O  
ANISOU 2041  O   ASP A1060     7584   9275   7194   -959    217   -943       O  
ATOM   2042  CB  ASP A1060       1.373 -36.045  -3.437  1.00 63.67           C  
ANISOU 2042  CB  ASP A1060     7550   9431   7212  -1113    189  -1238       C  
ATOM   2043  CG  ASP A1060       1.743 -35.286  -4.705  1.00 76.14           C  
ANISOU 2043  CG  ASP A1060     9114  11150   8665  -1178    149  -1332       C  
ATOM   2044  OD1 ASP A1060       2.087 -34.076  -4.604  1.00 75.98           O  
ANISOU 2044  OD1 ASP A1060     9160  11186   8521  -1134     91  -1259       O  
ATOM   2045  OD2 ASP A1060       1.698 -35.901  -5.797  1.00 83.40           O  
ANISOU 2045  OD2 ASP A1060     9948  12125   9614  -1276    189  -1483       O  
ATOM   2046  N   GLU A1061       1.993 -36.405   0.032  1.00 60.04           N  
ANISOU 2046  N   GLU A1061     7201   8789   6822   -849    184   -873       N  
ATOM   2047  CA  GLU A1061       1.675 -37.041   1.307  1.00 60.51           C  
ANISOU 2047  CA  GLU A1061     7271   8784   6934   -763    227   -716       C  
ATOM   2048  C   GLU A1061       1.292 -35.921   2.234  1.00 64.96           C  
ANISOU 2048  C   GLU A1061     7897   9465   7320   -710    161   -634       C  
ATOM   2049  O   GLU A1061       0.316 -36.046   2.967  1.00 65.10           O  
ANISOU 2049  O   GLU A1061     7930   9482   7323   -687    197   -544       O  
ATOM   2050  CB  GLU A1061       2.884 -37.787   1.887  1.00 62.55           C  
ANISOU 2050  CB  GLU A1061     7505   8976   7286   -670    241   -634       C  
ATOM   2051  CG  GLU A1061       2.740 -39.298   1.851  1.00 71.15           C  
ANISOU 2051  CG  GLU A1061     8538   9881   8616   -663    372   -592       C  
ATOM   2052  CD  GLU A1061       4.022 -40.108   1.762  1.00 82.20           C  
ANISOU 2052  CD  GLU A1061     9882  11182  10169   -599    406   -577       C  
ATOM   2053  OE1 GLU A1061       5.112 -39.565   2.056  1.00 56.85           O  
ANISOU 2053  OE1 GLU A1061     6672   8072   6855   -529    312   -556       O  
ATOM   2054  OE2 GLU A1061       3.929 -41.300   1.390  1.00 80.96           O  
ANISOU 2054  OE2 GLU A1061     9667  10841  10254   -623    538   -601       O  
ATOM   2055  N   ALA A1062       2.051 -34.808   2.181  1.00 61.99           N  
ANISOU 2055  N   ALA A1062     7551   9184   6821   -701     81   -683       N  
ATOM   2056  CA  ALA A1062       1.794 -33.611   2.984  1.00 61.68           C  
ANISOU 2056  CA  ALA A1062     7559   9247   6630   -668     36   -653       C  
ATOM   2057  C   ALA A1062       0.484 -32.968   2.538  1.00 63.90           C  
ANISOU 2057  C   ALA A1062     7860   9544   6876   -717     50   -676       C  
ATOM   2058  O   ALA A1062      -0.250 -32.451   3.379  1.00 64.58           O  
ANISOU 2058  O   ALA A1062     7971   9674   6892   -684     55   -622       O  
ATOM   2059  CB  ALA A1062       2.945 -32.623   2.854  1.00 62.07           C  
ANISOU 2059  CB  ALA A1062     7617   9361   6604   -673    -21   -738       C  
ATOM   2060  N   GLU A1063       0.176 -33.032   1.230  1.00 57.26           N  
ANISOU 2060  N   GLU A1063     6993   8688   6074   -790     59   -755       N  
ATOM   2061  CA  GLU A1063      -1.075 -32.504   0.719  1.00 56.01           C  
ANISOU 2061  CA  GLU A1063     6827   8577   5877   -821     66   -763       C  
ATOM   2062  C   GLU A1063      -2.225 -33.419   1.156  1.00 58.28           C  
ANISOU 2062  C   GLU A1063     7079   8832   6231   -827    122   -720       C  
ATOM   2063  O   GLU A1063      -3.279 -32.906   1.525  1.00 57.98           O  
ANISOU 2063  O   GLU A1063     7046   8838   6147   -810    128   -682       O  
ATOM   2064  CB  GLU A1063      -1.024 -32.326  -0.805  1.00 57.38           C  
ANISOU 2064  CB  GLU A1063     6963   8801   6038   -891     52   -852       C  
ATOM   2065  CG  GLU A1063      -2.133 -31.433  -1.347  1.00 69.09           C  
ANISOU 2065  CG  GLU A1063     8433  10377   7442   -891     39   -829       C  
ATOM   2066  CD  GLU A1063      -1.828 -30.650  -2.612  1.00 99.86           C  
ANISOU 2066  CD  GLU A1063    12320  14360  11264   -916     15   -854       C  
ATOM   2067  OE1 GLU A1063      -0.892 -31.035  -3.352  1.00101.63           O  
ANISOU 2067  OE1 GLU A1063    12528  14587  11499   -968     13   -930       O  
ATOM   2068  OE2 GLU A1063      -2.538 -29.650  -2.868  1.00 95.83           O  
ANISOU 2068  OE2 GLU A1063    11811  13912  10686   -877      7   -787       O  
ATOM   2069  N   LYS A1064      -2.006 -34.765   1.158  1.00 53.94           N  
ANISOU 2069  N   LYS A1064     6491   8191   5813   -850    180   -727       N  
ATOM   2070  CA  LYS A1064      -3.004 -35.766   1.576  1.00 53.85           C  
ANISOU 2070  CA  LYS A1064     6440   8112   5907   -868    268   -690       C  
ATOM   2071  C   LYS A1064      -3.352 -35.544   3.037  1.00 58.63           C  
ANISOU 2071  C   LYS A1064     7096   8725   6454   -785    281   -545       C  
ATOM   2072  O   LYS A1064      -4.522 -35.335   3.363  1.00 59.21           O  
ANISOU 2072  O   LYS A1064     7161   8833   6503   -794    309   -522       O  
ATOM   2073  CB  LYS A1064      -2.505 -37.207   1.345  1.00 55.89           C  
ANISOU 2073  CB  LYS A1064     6649   8229   6356   -899    357   -717       C  
ATOM   2074  CG  LYS A1064      -3.615 -38.258   1.278  1.00 59.17           C  
ANISOU 2074  CG  LYS A1064     6997   8558   6926   -969    479   -748       C  
ATOM   2075  CD  LYS A1064      -3.262 -39.368   0.303  1.00 71.70           C  
ANISOU 2075  CD  LYS A1064     8501  10039   8704  -1060    565   -897       C  
ATOM   2076  CE  LYS A1064      -4.368 -40.365   0.077  1.00 88.79           C  
ANISOU 2076  CE  LYS A1064    10576  12121  11041  -1162    703   -988       C  
ATOM   2077  NZ  LYS A1064      -4.395 -41.408   1.136  1.00105.68           N  
ANISOU 2077  NZ  LYS A1064    12730  14052  13372  -1109    847   -834       N  
ATOM   2078  N   LEU A1065      -2.323 -35.512   3.892  1.00 55.33           N  
ANISOU 2078  N   LEU A1065     6718   8309   5994   -704    255   -458       N  
ATOM   2079  CA  LEU A1065      -2.421 -35.273   5.329  1.00 56.08           C  
ANISOU 2079  CA  LEU A1065     6851   8466   5992   -620    257   -327       C  
ATOM   2080  C   LEU A1065      -3.011 -33.887   5.641  1.00 57.97           C  
ANISOU 2080  C   LEU A1065     7122   8819   6084   -619    210   -366       C  
ATOM   2081  O   LEU A1065      -3.656 -33.740   6.677  1.00 58.49           O  
ANISOU 2081  O   LEU A1065     7201   8938   6083   -583    242   -292       O  
ATOM   2082  CB  LEU A1065      -1.021 -35.431   5.955  1.00 57.07           C  
ANISOU 2082  CB  LEU A1065     6983   8625   6076   -538    215   -260       C  
ATOM   2083  CG  LEU A1065      -0.880 -35.545   7.474  1.00 63.38           C  
ANISOU 2083  CG  LEU A1065     7792   9524   6765   -437    221   -101       C  
ATOM   2084  CD1 LEU A1065      -1.558 -36.805   8.017  1.00 64.85           C  
ANISOU 2084  CD1 LEU A1065     7963   9611   7064   -404    339     66       C  
ATOM   2085  CD2 LEU A1065       0.591 -35.559   7.859  1.00 66.63           C  
ANISOU 2085  CD2 LEU A1065     8180  10019   7116   -359    153    -71       C  
ATOM   2086  N   PHE A1066      -2.813 -32.891   4.737  1.00 51.89           N  
ANISOU 2086  N   PHE A1066     6361   8078   5278   -656    153   -477       N  
ATOM   2087  CA  PHE A1066      -3.329 -31.531   4.891  1.00 50.64           C  
ANISOU 2087  CA  PHE A1066     6227   7987   5029   -648    132   -514       C  
ATOM   2088  C   PHE A1066      -4.832 -31.504   4.757  1.00 56.44           C  
ANISOU 2088  C   PHE A1066     6933   8725   5787   -667    175   -501       C  
ATOM   2089  O   PHE A1066      -5.514 -30.991   5.647  1.00 57.56           O  
ANISOU 2089  O   PHE A1066     7085   8911   5876   -636    202   -472       O  
ATOM   2090  CB  PHE A1066      -2.704 -30.580   3.872  1.00 51.41           C  
ANISOU 2090  CB  PHE A1066     6336   8087   5112   -674     87   -600       C  
ATOM   2091  CG  PHE A1066      -3.322 -29.205   3.842  1.00 52.73           C  
ANISOU 2091  CG  PHE A1066     6520   8279   5237   -660     96   -622       C  
ATOM   2092  CD1 PHE A1066      -3.129 -28.313   4.892  1.00 56.34           C  
ANISOU 2092  CD1 PHE A1066     7004   8767   5636   -629    111   -645       C  
ATOM   2093  CD2 PHE A1066      -4.079 -28.791   2.757  1.00 54.63           C  
ANISOU 2093  CD2 PHE A1066     6735   8523   5500   -675     96   -623       C  
ATOM   2094  CE1 PHE A1066      -3.681 -27.031   4.854  1.00 57.19           C  
ANISOU 2094  CE1 PHE A1066     7120   8861   5747   -614    146   -673       C  
ATOM   2095  CE2 PHE A1066      -4.637 -27.514   2.724  1.00 57.99           C  
ANISOU 2095  CE2 PHE A1066     7168   8951   5914   -639    119   -612       C  
ATOM   2096  CZ  PHE A1066      -4.417 -26.634   3.765  1.00 56.26           C  
ANISOU 2096  CZ  PHE A1066     6984   8715   5676   -610    153   -641       C  
ATOM   2097  N   ASN A1067      -5.350 -32.045   3.638  1.00 53.04           N  
ANISOU 2097  N   ASN A1067     6450   8271   5432   -723    183   -542       N  
ATOM   2098  CA  ASN A1067      -6.782 -32.123   3.342  1.00 52.76           C  
ANISOU 2098  CA  ASN A1067     6356   8268   5424   -750    217   -552       C  
ATOM   2099  C   ASN A1067      -7.492 -32.998   4.372  1.00 56.95           C  
ANISOU 2099  C   ASN A1067     6874   8762   6003   -750    298   -488       C  
ATOM   2100  O   ASN A1067      -8.698 -32.877   4.553  1.00 55.92           O  
ANISOU 2100  O   ASN A1067     6701   8667   5878   -758    336   -487       O  
ATOM   2101  CB  ASN A1067      -6.999 -32.648   1.929  1.00 52.78           C  
ANISOU 2101  CB  ASN A1067     6282   8294   5479   -823    206   -639       C  
ATOM   2102  CG  ASN A1067      -6.457 -31.764   0.834  1.00 67.63           C  
ANISOU 2102  CG  ASN A1067     8165  10239   7291   -822    137   -679       C  
ATOM   2103  OD1 ASN A1067      -6.367 -30.532   0.954  1.00 54.13           O  
ANISOU 2103  OD1 ASN A1067     6498   8554   5514   -764    109   -638       O  
ATOM   2104  ND2 ASN A1067      -6.092 -32.389  -0.271  1.00 61.72           N  
ANISOU 2104  ND2 ASN A1067     7365   9516   6571   -890    127   -763       N  
ATOM   2105  N   GLN A1068      -6.726 -33.862   5.061  1.00 55.35           N  
ANISOU 2105  N   GLN A1068     6702   8491   5836   -731    333   -418       N  
ATOM   2106  CA  GLN A1068      -7.212 -34.711   6.137  1.00 56.75           C  
ANISOU 2106  CA  GLN A1068     6879   8629   6054   -713    426   -310       C  
ATOM   2107  C   GLN A1068      -7.519 -33.804   7.325  1.00 62.44           C  
ANISOU 2107  C   GLN A1068     7640   9451   6633   -652    419   -254       C  
ATOM   2108  O   GLN A1068      -8.580 -33.935   7.952  1.00 63.00           O  
ANISOU 2108  O   GLN A1068     7692   9540   6705   -658    491   -214       O  
ATOM   2109  CB  GLN A1068      -6.163 -35.769   6.506  1.00 58.64           C  
ANISOU 2109  CB  GLN A1068     7136   8780   6363   -679    461   -217       C  
ATOM   2110  CG  GLN A1068      -6.192 -36.989   5.586  1.00 76.56           C  
ANISOU 2110  CG  GLN A1068     9348  10909   8833   -752    536   -272       C  
ATOM   2111  CD  GLN A1068      -5.212 -38.073   5.970  1.00103.32           C  
ANISOU 2111  CD  GLN A1068    12745  14179  12334   -701    595   -159       C  
ATOM   2112  OE1 GLN A1068      -4.552 -38.032   7.018  1.00101.20           O  
ANISOU 2112  OE1 GLN A1068    12518  13955  11978   -598    578     -8       O  
ATOM   2113  NE2 GLN A1068      -5.103 -39.084   5.123  1.00 97.43           N  
ANISOU 2113  NE2 GLN A1068    11942  13289  11787   -769    674   -236       N  
ATOM   2114  N   ASP A1069      -6.613 -32.838   7.581  1.00 58.76           N  
ANISOU 2114  N   ASP A1069     7218   9055   6053   -608    342   -281       N  
ATOM   2115  CA  ASP A1069      -6.751 -31.854   8.652  1.00 58.99           C  
ANISOU 2115  CA  ASP A1069     7273   9194   5948   -565    339   -281       C  
ATOM   2116  C   ASP A1069      -7.768 -30.759   8.305  1.00 61.62           C  
ANISOU 2116  C   ASP A1069     7586   9543   6282   -580    344   -365       C  
ATOM   2117  O   ASP A1069      -8.435 -30.259   9.218  1.00 62.34           O  
ANISOU 2117  O   ASP A1069     7676   9700   6312   -561    389   -365       O  
ATOM   2118  CB  ASP A1069      -5.388 -31.242   9.018  1.00 60.79           C  
ANISOU 2118  CB  ASP A1069     7530   9493   6075   -530    271   -318       C  
ATOM   2119  CG  ASP A1069      -4.411 -32.172   9.717  1.00 72.24           C  
ANISOU 2119  CG  ASP A1069     8981  10985   7483   -480    263   -210       C  
ATOM   2120  OD1 ASP A1069      -4.858 -33.212  10.265  1.00 74.18           O  
ANISOU 2120  OD1 ASP A1069     9217  11210   7758   -456    331    -71       O  
ATOM   2121  OD2 ASP A1069      -3.204 -31.854   9.730  1.00 77.15           O  
ANISOU 2121  OD2 ASP A1069     9604  11660   8048   -460    197   -254       O  
ATOM   2122  N   VAL A1070      -7.893 -30.392   7.002  1.00 55.27           N  
ANISOU 2122  N   VAL A1070     6761   8694   5544   -606    304   -428       N  
ATOM   2123  CA  VAL A1070      -8.851 -29.377   6.548  1.00 54.49           C  
ANISOU 2123  CA  VAL A1070     6630   8614   5460   -595    309   -471       C  
ATOM   2124  C   VAL A1070     -10.295 -29.899   6.730  1.00 61.35           C  
ANISOU 2124  C   VAL A1070     7433   9503   6373   -612    369   -448       C  
ATOM   2125  O   VAL A1070     -11.124 -29.202   7.328  1.00 61.72           O  
ANISOU 2125  O   VAL A1070     7462   9587   6401   -582    411   -456       O  
ATOM   2126  CB  VAL A1070      -8.536 -28.844   5.124  1.00 56.40           C  
ANISOU 2126  CB  VAL A1070     6858   8838   5733   -601    250   -508       C  
ATOM   2127  CG1 VAL A1070      -9.676 -28.003   4.566  1.00 56.50           C  
ANISOU 2127  CG1 VAL A1070     6813   8885   5770   -568    259   -505       C  
ATOM   2128  CG2 VAL A1070      -7.264 -28.024   5.137  1.00 55.59           C  
ANISOU 2128  CG2 VAL A1070     6817   8710   5596   -585    220   -542       C  
ATOM   2129  N   ASP A1071     -10.563 -31.149   6.276  1.00 58.63           N  
ANISOU 2129  N   ASP A1071     7047   9128   6103   -668    391   -436       N  
ATOM   2130  CA  ASP A1071     -11.850 -31.834   6.414  1.00 59.64           C  
ANISOU 2130  CA  ASP A1071     7099   9266   6295   -708    466   -434       C  
ATOM   2131  C   ASP A1071     -12.266 -31.899   7.877  1.00 64.54           C  
ANISOU 2131  C   ASP A1071     7748   9901   6872   -683    548   -366       C  
ATOM   2132  O   ASP A1071     -13.428 -31.649   8.201  1.00 64.48           O  
ANISOU 2132  O   ASP A1071     7688   9937   6874   -685    601   -382       O  
ATOM   2133  CB  ASP A1071     -11.755 -33.261   5.850  1.00 62.50           C  
ANISOU 2133  CB  ASP A1071     7421   9558   6770   -787    507   -450       C  
ATOM   2134  CG  ASP A1071     -12.146 -33.394   4.396  1.00 77.71           C  
ANISOU 2134  CG  ASP A1071     9250  11531   8745   -847    466   -561       C  
ATOM   2135  OD1 ASP A1071     -12.753 -32.442   3.856  1.00 79.83           O  
ANISOU 2135  OD1 ASP A1071     9469  11904   8958   -816    410   -593       O  
ATOM   2136  OD2 ASP A1071     -11.866 -34.461   3.801  1.00 83.75           O  
ANISOU 2136  OD2 ASP A1071     9976  12239   9606   -923    498   -617       O  
ATOM   2137  N   ALA A1072     -11.294 -32.228   8.751  1.00 61.74           N  
ANISOU 2137  N   ALA A1072     7468   9535   6456   -655    557   -290       N  
ATOM   2138  CA  ALA A1072     -11.432 -32.314  10.200  1.00 62.44           C  
ANISOU 2138  CA  ALA A1072     7586   9684   6454   -623    626   -207       C  
ATOM   2139  C   ALA A1072     -11.701 -30.930  10.810  1.00 65.44           C  
ANISOU 2139  C   ALA A1072     7973  10162   6728   -586    614   -277       C  
ATOM   2140  O   ALA A1072     -12.468 -30.834  11.770  1.00 66.06           O  
ANISOU 2140  O   ALA A1072     8036  10307   6755   -581    692   -259       O  
ATOM   2141  CB  ALA A1072     -10.168 -32.912  10.795  1.00 63.57           C  
ANISOU 2141  CB  ALA A1072     7784   9832   6535   -585    612   -105       C  
ATOM   2142  N   ALA A1073     -11.068 -29.867  10.255  1.00 60.29           N  
ANISOU 2142  N   ALA A1073     7341   9508   6059   -564    536   -364       N  
ATOM   2143  CA  ALA A1073     -11.248 -28.484  10.704  1.00 59.61           C  
ANISOU 2143  CA  ALA A1073     7255   9470   5923   -534    547   -455       C  
ATOM   2144  C   ALA A1073     -12.659 -28.024  10.354  1.00 62.13           C  
ANISOU 2144  C   ALA A1073     7506   9773   6326   -527    592   -487       C  
ATOM   2145  O   ALA A1073     -13.358 -27.516  11.233  1.00 62.89           O  
ANISOU 2145  O   ALA A1073     7579   9923   6391   -514    665   -523       O  
ATOM   2146  CB  ALA A1073     -10.214 -27.569  10.056  1.00 59.62           C  
ANISOU 2146  CB  ALA A1073     7289   9432   5933   -520    479   -528       C  
ATOM   2147  N   VAL A1074     -13.094 -28.265   9.093  1.00 56.28           N  
ANISOU 2147  N   VAL A1074     6717   8984   5682   -537    552   -477       N  
ATOM   2148  CA  VAL A1074     -14.425 -27.923   8.576  1.00 55.88           C  
ANISOU 2148  CA  VAL A1074     6573   8953   5707   -520    575   -496       C  
ATOM   2149  C   VAL A1074     -15.536 -28.567   9.427  1.00 57.60           C  
ANISOU 2149  C   VAL A1074     6740   9215   5932   -552    669   -484       C  
ATOM   2150  O   VAL A1074     -16.491 -27.884   9.794  1.00 56.54           O  
ANISOU 2150  O   VAL A1074     6549   9116   5819   -519    722   -520       O  
ATOM   2151  CB  VAL A1074     -14.538 -28.260   7.063  1.00 59.85           C  
ANISOU 2151  CB  VAL A1074     7016   9456   6268   -536    502   -492       C  
ATOM   2152  CG1 VAL A1074     -15.988 -28.230   6.568  1.00 60.79           C  
ANISOU 2152  CG1 VAL A1074     7004   9647   6445   -526    519   -508       C  
ATOM   2153  CG2 VAL A1074     -13.674 -27.321   6.236  1.00 59.00           C  
ANISOU 2153  CG2 VAL A1074     6948   9318   6153   -489    432   -491       C  
ATOM   2154  N   ARG A1075     -15.379 -29.859   9.767  1.00 53.75           N  
ANISOU 2154  N   ARG A1075     6270   8713   5441   -611    706   -429       N  
ATOM   2155  CA  ARG A1075     -16.324 -30.618  10.589  1.00 54.26           C  
ANISOU 2155  CA  ARG A1075     6295   8800   5522   -652    819   -395       C  
ATOM   2156  C   ARG A1075     -16.435 -30.029  12.000  1.00 58.19           C  
ANISOU 2156  C   ARG A1075     6828   9372   5909   -619    888   -388       C  
ATOM   2157  O   ARG A1075     -17.537 -29.997  12.561  1.00 58.30           O  
ANISOU 2157  O   ARG A1075     6783   9433   5937   -633    980   -406       O  
ATOM   2158  CB  ARG A1075     -15.946 -32.111  10.647  1.00 53.20           C  
ANISOU 2158  CB  ARG A1075     6183   8597   5433   -712    867   -311       C  
ATOM   2159  CG  ARG A1075     -16.328 -32.904   9.406  1.00 55.99           C  
ANISOU 2159  CG  ARG A1075     6454   8893   5925   -782    858   -366       C  
ATOM   2160  CD  ARG A1075     -15.949 -34.360   9.562  1.00 63.52           C  
ANISOU 2160  CD  ARG A1075     7428   9738   6968   -842    945   -292       C  
ATOM   2161  NE  ARG A1075     -16.062 -35.102   8.304  1.00 72.96           N  
ANISOU 2161  NE  ARG A1075     8543  10877   8300   -923    937   -388       N  
ATOM   2162  CZ  ARG A1075     -16.989 -36.024   8.043  1.00 89.13           C  
ANISOU 2162  CZ  ARG A1075    10489  12885  10492  -1022   1047   -450       C  
ATOM   2163  NH1 ARG A1075     -17.897 -36.342   8.959  1.00 79.34           N  
ANISOU 2163  NH1 ARG A1075     9223  11637   9284  -1047   1180   -404       N  
ATOM   2164  NH2 ARG A1075     -17.007 -36.641   6.870  1.00 74.17           N  
ANISOU 2164  NH2 ARG A1075     8507  10966   8708  -1107   1037   -577       N  
ATOM   2165  N   GLY A1076     -15.302 -29.553  12.532  1.00 54.21           N  
ANISOU 2165  N   GLY A1076     6404   8899   5292   -585    847   -385       N  
ATOM   2166  CA  GLY A1076     -15.201 -28.928  13.852  1.00 54.94           C  
ANISOU 2166  CA  GLY A1076     6521   9106   5249   -564    902   -416       C  
ATOM   2167  C   GLY A1076     -16.011 -27.649  13.961  1.00 58.47           C  
ANISOU 2167  C   GLY A1076     6914   9570   5734   -539    941   -544       C  
ATOM   2168  O   GLY A1076     -16.751 -27.462  14.937  1.00 59.01           O  
ANISOU 2168  O   GLY A1076     6948   9723   5751   -547   1039   -578       O  
ATOM   2169  N   ILE A1077     -15.885 -26.778  12.923  1.00 52.71           N  
ANISOU 2169  N   ILE A1077     6169   8753   5105   -502    876   -606       N  
ATOM   2170  CA  ILE A1077     -16.592 -25.505  12.738  1.00 51.98           C  
ANISOU 2170  CA  ILE A1077     6018   8628   5105   -452    914   -700       C  
ATOM   2171  C   ILE A1077     -18.102 -25.789  12.646  1.00 59.14           C  
ANISOU 2171  C   ILE A1077     6822   9557   6093   -450    974   -686       C  
ATOM   2172  O   ILE A1077     -18.884 -25.119  13.321  1.00 60.43           O  
ANISOU 2172  O   ILE A1077     6932   9752   6278   -428   1066   -760       O  
ATOM   2173  CB  ILE A1077     -16.058 -24.775  11.465  1.00 53.04           C  
ANISOU 2173  CB  ILE A1077     6161   8657   5334   -403    831   -699       C  
ATOM   2174  CG1 ILE A1077     -14.550 -24.443  11.578  1.00 51.67           C  
ANISOU 2174  CG1 ILE A1077     6078   8460   5094   -417    786   -736       C  
ATOM   2175  CG2 ILE A1077     -16.876 -23.522  11.144  1.00 53.78           C  
ANISOU 2175  CG2 ILE A1077     6182   8694   5559   -325    884   -746       C  
ATOM   2176  CD1 ILE A1077     -13.812 -24.337  10.260  1.00 47.88           C  
ANISOU 2176  CD1 ILE A1077     5626   7894   4673   -399    693   -690       C  
ATOM   2177  N   LEU A1078     -18.502 -26.795  11.821  1.00 56.74           N  
ANISOU 2177  N   LEU A1078     6476   9243   5839   -481    932   -615       N  
ATOM   2178  CA  LEU A1078     -19.900 -27.214  11.640  1.00 57.71           C  
ANISOU 2178  CA  LEU A1078     6479   9406   6041   -498    985   -620       C  
ATOM   2179  C   LEU A1078     -20.479 -27.726  12.944  1.00 65.22           C  
ANISOU 2179  C   LEU A1078     7427  10418   6936   -550   1112   -622       C  
ATOM   2180  O   LEU A1078     -21.605 -27.369  13.282  1.00 65.86           O  
ANISOU 2180  O   LEU A1078     7415  10543   7066   -539   1191   -676       O  
ATOM   2181  CB  LEU A1078     -20.048 -28.296  10.556  1.00 57.14           C  
ANISOU 2181  CB  LEU A1078     6358   9327   6027   -552    927   -583       C  
ATOM   2182  CG  LEU A1078     -19.670 -27.959   9.107  1.00 60.57           C  
ANISOU 2182  CG  LEU A1078     6765   9750   6500   -512    804   -580       C  
ATOM   2183  CD1 LEU A1078     -20.266 -28.978   8.154  1.00 60.33           C  
ANISOU 2183  CD1 LEU A1078     6625   9771   6526   -581    779   -600       C  
ATOM   2184  CD2 LEU A1078     -20.076 -26.534   8.710  1.00 63.23           C  
ANISOU 2184  CD2 LEU A1078     7045  10098   6880   -398    780   -592       C  
ATOM   2185  N   ARG A1079     -19.690 -28.529  13.698  1.00 63.63           N  
ANISOU 2185  N   ARG A1079     7320  10230   6626   -597   1136   -549       N  
ATOM   2186  CA  ARG A1079     -20.082 -29.069  15.004  1.00 64.94           C  
ANISOU 2186  CA  ARG A1079     7496  10477   6703   -639   1263   -508       C  
ATOM   2187  C   ARG A1079     -19.725 -28.094  16.145  1.00 71.68           C  
ANISOU 2187  C   ARG A1079     8387  11433   7415   -607   1303   -580       C  
ATOM   2188  O   ARG A1079     -19.454 -28.516  17.269  1.00 72.63           O  
ANISOU 2188  O   ARG A1079     8550  11664   7384   -631   1370   -523       O  
ATOM   2189  CB  ARG A1079     -19.503 -30.477  15.226  1.00 62.96           C  
ANISOU 2189  CB  ARG A1079     7308  10198   6415   -688   1288   -361       C  
ATOM   2190  CG  ARG A1079     -20.074 -31.520  14.282  1.00 65.76           C  
ANISOU 2190  CG  ARG A1079     7599  10453   6933   -749   1305   -335       C  
ATOM   2191  CD  ARG A1079     -19.103 -32.648  14.043  1.00 67.47           C  
ANISOU 2191  CD  ARG A1079     7887  10581   7168   -774   1289   -217       C  
ATOM   2192  NE  ARG A1079     -19.604 -33.573  13.028  1.00 78.50           N  
ANISOU 2192  NE  ARG A1079     9207  11876   8743   -850   1313   -246       N  
ATOM   2193  CZ  ARG A1079     -19.032 -34.732  12.715  1.00106.17           C  
ANISOU 2193  CZ  ARG A1079    12741  15265  12334   -893   1344   -169       C  
ATOM   2194  NH1 ARG A1079     -17.925 -35.125  13.338  1.00100.15           N  
ANISOU 2194  NH1 ARG A1079    12085  14477  11490   -848   1346    -23       N  
ATOM   2195  NH2 ARG A1079     -19.563 -35.509  11.780  1.00 98.70           N  
ANISOU 2195  NH2 ARG A1079    11702  14238  11561   -981   1382   -247       N  
ATOM   2196  N   ASN A1080     -19.743 -26.780  15.837  1.00 69.52           N  
ANISOU 2196  N   ASN A1080     8086  11132   7198   -554   1272   -707       N  
ATOM   2197  CA  ASN A1080     -19.518 -25.663  16.760  1.00 70.67           C  
ANISOU 2197  CA  ASN A1080     8237  11349   7264   -536   1329   -840       C  
ATOM   2198  C   ASN A1080     -20.663 -24.670  16.530  1.00 74.91           C  
ANISOU 2198  C   ASN A1080     8669  11836   7958   -490   1396   -952       C  
ATOM   2199  O   ASN A1080     -20.809 -24.135  15.423  1.00 73.50           O  
ANISOU 2199  O   ASN A1080     8454  11541   7931   -428   1333   -950       O  
ATOM   2200  CB  ASN A1080     -18.151 -25.001  16.532  1.00 71.99           C  
ANISOU 2200  CB  ASN A1080     8477  11484   7391   -514   1243   -892       C  
ATOM   2201  CG  ASN A1080     -17.824 -23.925  17.531  1.00 93.82           C  
ANISOU 2201  CG  ASN A1080    11235  14337  10076   -521   1317  -1068       C  
ATOM   2202  OD1 ASN A1080     -18.377 -22.819  17.504  1.00 86.46           O  
ANISOU 2202  OD1 ASN A1080    10243  13338   9270   -491   1389  -1205       O  
ATOM   2203  ND2 ASN A1080     -16.909 -24.228  18.432  1.00 87.56           N  
ANISOU 2203  ND2 ASN A1080    10489  13703   9075   -559   1307  -1075       N  
ATOM   2204  N   ALA A1081     -21.491 -24.469  17.574  1.00 72.54           N  
ANISOU 2204  N   ALA A1081     8311  11634   7617   -513   1528  -1033       N  
ATOM   2205  CA  ALA A1081     -22.685 -23.623  17.565  1.00 72.98           C  
ANISOU 2205  CA  ALA A1081     8249  11657   7822   -469   1619  -1141       C  
ATOM   2206  C   ALA A1081     -22.424 -22.160  17.228  1.00 76.29           C  
ANISOU 2206  C   ALA A1081     8648  11963   8377   -392   1627  -1265       C  
ATOM   2207  O   ALA A1081     -23.268 -21.537  16.585  1.00 76.39           O  
ANISOU 2207  O   ALA A1081     8564  11884   8577   -311   1648  -1276       O  
ATOM   2208  CB  ALA A1081     -23.407 -23.733  18.893  1.00 75.40           C  
ANISOU 2208  CB  ALA A1081     8511  12112   8028   -524   1771  -1219       C  
ATOM   2209  N   LYS A1082     -21.272 -21.613  17.662  1.00 72.17           N  
ANISOU 2209  N   LYS A1082     8204  11447   7770   -413   1622  -1354       N  
ATOM   2210  CA  LYS A1082     -20.904 -20.212  17.416  1.00 71.92           C  
ANISOU 2210  CA  LYS A1082     8158  11278   7890   -358   1664  -1489       C  
ATOM   2211  C   LYS A1082     -20.213 -20.028  16.059  1.00 72.15           C  
ANISOU 2211  C   LYS A1082     8236  11149   8029   -296   1540  -1374       C  
ATOM   2212  O   LYS A1082     -20.381 -18.987  15.424  1.00 72.07           O  
ANISOU 2212  O   LYS A1082     8184  10979   8220   -210   1577  -1396       O  
ATOM   2213  CB  LYS A1082     -20.027 -19.636  18.563  1.00 75.56           C  
ANISOU 2213  CB  LYS A1082     8652  11837   8219   -432   1741  -1690       C  
ATOM   2214  CG  LYS A1082     -20.577 -19.820  19.988  1.00 92.87           C  
ANISOU 2214  CG  LYS A1082    10796  14243  10246   -504   1865  -1813       C  
ATOM   2215  CD  LYS A1082     -21.794 -18.931  20.301  1.00105.99           C  
ANISOU 2215  CD  LYS A1082    12338  15845  12090   -469   2029  -1964       C  
ATOM   2216  CE  LYS A1082     -22.651 -19.503  21.408  1.00115.73           C  
ANISOU 2216  CE  LYS A1082    13517  17288  13166   -532   2130  -2000       C  
ATOM   2217  NZ  LYS A1082     -23.976 -18.830  21.500  1.00123.48           N  
ANISOU 2217  NZ  LYS A1082    14370  18195  14351   -484   2272  -2106       N  
ATOM   2218  N   LEU A1083     -19.451 -21.035  15.617  1.00 65.70           N  
ANISOU 2218  N   LEU A1083     7501  10373   7088   -334   1408  -1242       N  
ATOM   2219  CA  LEU A1083     -18.715 -20.970  14.361  1.00 64.01           C  
ANISOU 2219  CA  LEU A1083     7336  10039   6945   -291   1291  -1141       C  
ATOM   2220  C   LEU A1083     -19.543 -21.273  13.110  1.00 67.95           C  
ANISOU 2220  C   LEU A1083     7767  10489   7559   -221   1221   -996       C  
ATOM   2221  O   LEU A1083     -19.368 -20.584  12.106  1.00 67.31           O  
ANISOU 2221  O   LEU A1083     7676  10297   7602   -141   1185   -943       O  
ATOM   2222  CB  LEU A1083     -17.475 -21.873  14.409  1.00 62.58           C  
ANISOU 2222  CB  LEU A1083     7259   9926   6594   -360   1187  -1083       C  
ATOM   2223  CG  LEU A1083     -16.268 -21.325  15.152  1.00 67.56           C  
ANISOU 2223  CG  LEU A1083     7947  10594   7128   -407   1208  -1219       C  
ATOM   2224  CD1 LEU A1083     -15.247 -22.415  15.388  1.00 67.06           C  
ANISOU 2224  CD1 LEU A1083     7958  10645   6875   -461   1110  -1139       C  
ATOM   2225  CD2 LEU A1083     -15.624 -20.174  14.395  1.00 69.77           C  
ANISOU 2225  CD2 LEU A1083     8242  10703   7565   -366   1214  -1280       C  
ATOM   2226  N   LYS A1084     -20.406 -22.312  13.150  1.00 64.82           N  
ANISOU 2226  N   LYS A1084     7319  10191   7119   -254   1208   -933       N  
ATOM   2227  CA  LYS A1084     -21.212 -22.748  12.004  1.00 64.73           C  
ANISOU 2227  CA  LYS A1084     7217  10190   7189   -211   1137   -831       C  
ATOM   2228  C   LYS A1084     -21.989 -21.588  11.313  1.00 72.52           C  
ANISOU 2228  C   LYS A1084     8092  11113   8349    -77   1161   -817       C  
ATOM   2229  O   LYS A1084     -21.834 -21.466  10.091  1.00 72.46           O  
ANISOU 2229  O   LYS A1084     8061  11085   8385    -13   1065   -714       O  
ATOM   2230  CB  LYS A1084     -22.134 -23.924  12.375  1.00 66.57           C  
ANISOU 2230  CB  LYS A1084     7387  10532   7375   -285   1167   -817       C  
ATOM   2231  CG  LYS A1084     -22.698 -24.690  11.181  1.00 69.03           C  
ANISOU 2231  CG  LYS A1084     7608  10888   7734   -289   1080   -745       C  
ATOM   2232  CD  LYS A1084     -24.156 -24.329  10.911  1.00 71.41           C  
ANISOU 2232  CD  LYS A1084     7733  11254   8146   -224   1119   -769       C  
ATOM   2233  CE  LYS A1084     -24.717 -25.055   9.717  1.00 72.81           C  
ANISOU 2233  CE  LYS A1084     7791  11527   8348   -236   1027   -730       C  
ATOM   2234  NZ  LYS A1084     -26.087 -24.579   9.380  1.00 76.12           N  
ANISOU 2234  NZ  LYS A1084     8014  12042   8867   -151   1047   -750       N  
ATOM   2235  N   PRO A1085     -22.758 -20.706  12.020  1.00 71.20           N  
ANISOU 2235  N   PRO A1085     7851  10917   8284    -23   1290   -907       N  
ATOM   2236  CA  PRO A1085     -23.456 -19.607  11.314  1.00 72.60           C  
ANISOU 2236  CA  PRO A1085     7916  11016   8654    131   1321   -859       C  
ATOM   2237  C   PRO A1085     -22.537 -18.663  10.533  1.00 77.99           C  
ANISOU 2237  C   PRO A1085     8660  11546   9425    214   1298   -789       C  
ATOM   2238  O   PRO A1085     -22.923 -18.162   9.474  1.00 76.98           O  
ANISOU 2238  O   PRO A1085     8451  11391   9406    347   1260   -653       O  
ATOM   2239  CB  PRO A1085     -24.178 -18.869  12.443  1.00 75.81           C  
ANISOU 2239  CB  PRO A1085     8259  11391   9156    148   1492  -1005       C  
ATOM   2240  CG  PRO A1085     -23.437 -19.247  13.687  1.00 79.53           C  
ANISOU 2240  CG  PRO A1085     8845  11907   9468      6   1546  -1141       C  
ATOM   2241  CD  PRO A1085     -23.065 -20.668  13.463  1.00 73.39           C  
ANISOU 2241  CD  PRO A1085     8131  11243   8511    -91   1423  -1049       C  
ATOM   2242  N   VAL A1086     -21.316 -18.440  11.064  1.00 76.86           N  
ANISOU 2242  N   VAL A1086     8652  11323   9228    137   1325   -878       N  
ATOM   2243  CA  VAL A1086     -20.271 -17.601  10.474  1.00 77.82           C  
ANISOU 2243  CA  VAL A1086     8849  11288   9430    179   1326   -843       C  
ATOM   2244  C   VAL A1086     -19.787 -18.276   9.197  1.00 84.48           C  
ANISOU 2244  C   VAL A1086     9726  12185  10189    187   1162   -675       C  
ATOM   2245  O   VAL A1086     -19.764 -17.628   8.153  1.00 85.77           O  
ANISOU 2245  O   VAL A1086     9859  12275  10456    301   1144   -539       O  
ATOM   2246  CB  VAL A1086     -19.124 -17.310  11.480  1.00 81.50           C  
ANISOU 2246  CB  VAL A1086     9425  11703   9838     68   1396  -1025       C  
ATOM   2247  CG1 VAL A1086     -17.983 -16.535  10.832  1.00 81.16           C  
ANISOU 2247  CG1 VAL A1086     9455  11497   9883     89   1403  -1003       C  
ATOM   2248  CG2 VAL A1086     -19.649 -16.560  12.700  1.00 83.07           C  
ANISOU 2248  CG2 VAL A1086     9568  11872  10121     54   1573  -1222       C  
ATOM   2249  N   TYR A1087     -19.477 -19.590   9.268  1.00 81.32           N  
ANISOU 2249  N   TYR A1087     9373  11918   9606     74   1055   -676       N  
ATOM   2250  CA  TYR A1087     -19.036 -20.410   8.137  1.00 80.61           C  
ANISOU 2250  CA  TYR A1087     9304  11898   9428     54    910   -559       C  
ATOM   2251  C   TYR A1087     -20.075 -20.433   7.012  1.00 84.89           C  
ANISOU 2251  C   TYR A1087     9705  12533  10017    155    849   -433       C  
ATOM   2252  O   TYR A1087     -19.698 -20.364   5.841  1.00 84.47           O  
ANISOU 2252  O   TYR A1087     9647  12502   9948    202    763   -318       O  
ATOM   2253  CB  TYR A1087     -18.734 -21.839   8.606  1.00 81.53           C  
ANISOU 2253  CB  TYR A1087     9472  12118   9388    -82    852   -601       C  
ATOM   2254  CG  TYR A1087     -17.961 -22.679   7.609  1.00 83.71           C  
ANISOU 2254  CG  TYR A1087     9792  12430   9584   -130    727   -530       C  
ATOM   2255  CD1 TYR A1087     -16.594 -22.490   7.417  1.00 85.39           C  
ANISOU 2255  CD1 TYR A1087    10118  12567   9761   -156    693   -531       C  
ATOM   2256  CD2 TYR A1087     -18.586 -23.701   6.898  1.00 84.45           C  
ANISOU 2256  CD2 TYR A1087     9803  12641   9643   -163    657   -490       C  
ATOM   2257  CE1 TYR A1087     -15.874 -23.273   6.514  1.00 85.53           C  
ANISOU 2257  CE1 TYR A1087    10168  12617   9712   -203    589   -481       C  
ATOM   2258  CE2 TYR A1087     -17.873 -24.495   5.996  1.00 84.53           C  
ANISOU 2258  CE2 TYR A1087     9842  12685   9590   -219    559   -458       C  
ATOM   2259  CZ  TYR A1087     -16.517 -24.277   5.810  1.00 92.11           C  
ANISOU 2259  CZ  TYR A1087    10919  13561  10516   -235    525   -448       C  
ATOM   2260  OH  TYR A1087     -15.807 -25.046   4.922  1.00 94.06           O  
ANISOU 2260  OH  TYR A1087    11189  13841  10710   -291    440   -429       O  
ATOM   2261  N   ASP A1088     -21.377 -20.500   7.372  1.00 82.15           N  
ANISOU 2261  N   ASP A1088     9230  12264   9718    190    895   -457       N  
ATOM   2262  CA  ASP A1088     -22.505 -20.515   6.434  1.00 83.10           C  
ANISOU 2262  CA  ASP A1088     9179  12521   9875    290    839   -359       C  
ATOM   2263  C   ASP A1088     -22.571 -19.273   5.559  1.00 87.31           C  
ANISOU 2263  C   ASP A1088     9656  12990  10526    473    848   -207       C  
ATOM   2264  O   ASP A1088     -22.975 -19.371   4.400  1.00 87.25           O  
ANISOU 2264  O   ASP A1088     9538  13132  10482    554    749    -77       O  
ATOM   2265  CB  ASP A1088     -23.833 -20.640   7.192  1.00 86.40           C  
ANISOU 2265  CB  ASP A1088     9469  13011  10349    296    918   -439       C  
ATOM   2266  CG  ASP A1088     -24.110 -21.979   7.836  1.00 98.13           C  
ANISOU 2266  CG  ASP A1088    10960  14597  11730    134    917   -543       C  
ATOM   2267  OD1 ASP A1088     -23.332 -22.934   7.589  1.00 97.87           O  
ANISOU 2267  OD1 ASP A1088    11014  14585  11586     23    844   -545       O  
ATOM   2268  OD2 ASP A1088     -25.112 -22.078   8.580  1.00104.17           O  
ANISOU 2268  OD2 ASP A1088    11635  15408  12537    122   1003   -618       O  
ATOM   2269  N   SER A1089     -22.217 -18.106   6.122  1.00 84.30           N  
ANISOU 2269  N   SER A1089     9338  12399  10292    537    979   -226       N  
ATOM   2270  CA  SER A1089     -22.267 -16.830   5.419  1.00 85.75           C  
ANISOU 2270  CA  SER A1089     9478  12463  10641    721   1036    -66       C  
ATOM   2271  C   SER A1089     -21.029 -16.544   4.556  1.00 89.35           C  
ANISOU 2271  C   SER A1089    10048  12836  11067    727    992     46       C  
ATOM   2272  O   SER A1089     -21.158 -15.864   3.534  1.00 90.66           O  
ANISOU 2272  O   SER A1089    10152  12997  11300    883    984    252       O  
ATOM   2273  CB  SER A1089     -22.540 -15.686   6.395  1.00 90.39           C  
ANISOU 2273  CB  SER A1089    10059  12837  11448    784   1233   -156       C  
ATOM   2274  OG  SER A1089     -21.519 -15.532   7.366  1.00 96.95           O  
ANISOU 2274  OG  SER A1089    11040  13520  12276    649   1320   -340       O  
ATOM   2275  N   LEU A1090     -19.844 -17.074   4.947  1.00 83.69           N  
ANISOU 2275  N   LEU A1090     9485  12070  10242    565    965    -74       N  
ATOM   2276  CA  LEU A1090     -18.576 -16.852   4.233  1.00 82.55           C  
ANISOU 2276  CA  LEU A1090     9452  11842  10069    545    934     -3       C  
ATOM   2277  C   LEU A1090     -18.460 -17.607   2.899  1.00 85.41           C  
ANISOU 2277  C   LEU A1090     9779  12404  10271    550    769    138       C  
ATOM   2278  O   LEU A1090     -18.965 -18.722   2.762  1.00 83.92           O  
ANISOU 2278  O   LEU A1090     9525  12415   9944    480    661     95       O  
ATOM   2279  CB  LEU A1090     -17.344 -17.141   5.123  1.00 81.03           C  
ANISOU 2279  CB  LEU A1090     9413  11555   9819    379    959   -190       C  
ATOM   2280  CG  LEU A1090     -17.218 -16.387   6.461  1.00 86.48           C  
ANISOU 2280  CG  LEU A1090    10141  12085  10633    342   1123   -376       C  
ATOM   2281  CD1 LEU A1090     -16.118 -16.979   7.313  1.00 85.33           C  
ANISOU 2281  CD1 LEU A1090    10111  11960  10353    175   1101   -553       C  
ATOM   2282  CD2 LEU A1090     -16.981 -14.889   6.266  1.00 90.66           C  
ANISOU 2282  CD2 LEU A1090    10672  12371  11403    447   1286   -335       C  
ATOM   2283  N   ASP A1091     -17.786 -16.973   1.923  1.00 82.61           N  
ANISOU 2283  N   ASP A1091     9459  11989   9940    624    769    295       N  
ATOM   2284  CA  ASP A1091     -17.524 -17.475   0.568  1.00 82.43           C  
ANISOU 2284  CA  ASP A1091     9403  12156   9759    636    634    435       C  
ATOM   2285  C   ASP A1091     -16.228 -18.285   0.528  1.00 84.34           C  
ANISOU 2285  C   ASP A1091     9779  12391   9875    464    568    320       C  
ATOM   2286  O   ASP A1091     -15.407 -18.149   1.429  1.00 82.41           O  
ANISOU 2286  O   ASP A1091     9656  11971   9686    373    639    182       O  
ATOM   2287  CB  ASP A1091     -17.423 -16.299  -0.412  1.00 86.45           C  
ANISOU 2287  CB  ASP A1091     9885  12599  10363    815    693    688       C  
ATOM   2288  CG  ASP A1091     -16.492 -15.203   0.068  1.00100.07           C  
ANISOU 2288  CG  ASP A1091    11742  13995  12285    820    865    673       C  
ATOM   2289  OD1 ASP A1091     -16.929 -14.379   0.895  1.00102.04           O  
ANISOU 2289  OD1 ASP A1091    11977  14053  12739    883   1013    626       O  
ATOM   2290  OD2 ASP A1091     -15.321 -15.183  -0.374  1.00106.29           O  
ANISOU 2290  OD2 ASP A1091    12637  14719  13030    750    861    684       O  
ATOM   2291  N   ALA A1092     -16.025 -19.077  -0.552  1.00 81.17           N  
ANISOU 2291  N   ALA A1092     9340  12195   9305    425    437    372       N  
ATOM   2292  CA  ALA A1092     -14.878 -19.971  -0.802  1.00 79.67           C  
ANISOU 2292  CA  ALA A1092     9247  12031   8993    272    365    273       C  
ATOM   2293  C   ALA A1092     -13.475 -19.418  -0.412  1.00 83.32           C  
ANISOU 2293  C   ALA A1092     9870  12261   9527    217    444    226       C  
ATOM   2294  O   ALA A1092     -12.561 -20.209  -0.147  1.00 81.59           O  
ANISOU 2294  O   ALA A1092     9733  12031   9236     82    401     96       O  
ATOM   2295  CB  ALA A1092     -14.875 -20.412  -2.260  1.00 80.94           C  
ANISOU 2295  CB  ALA A1092     9323  12431   8998    284    252    375       C  
ATOM   2296  N   VAL A1093     -13.317 -18.075  -0.382  1.00 80.41           N  
ANISOU 2296  N   VAL A1093     9532  11706   9313    323    569    325       N  
ATOM   2297  CA  VAL A1093     -12.069 -17.384  -0.028  1.00 78.89           C  
ANISOU 2297  CA  VAL A1093     9466  11287   9221    271    673    263       C  
ATOM   2298  C   VAL A1093     -12.069 -17.065   1.475  1.00 80.71           C  
ANISOU 2298  C   VAL A1093     9739  11360   9567    219    776     71       C  
ATOM   2299  O   VAL A1093     -11.143 -17.466   2.176  1.00 78.57           O  
ANISOU 2299  O   VAL A1093     9550  11052   9251     90    769   -100       O  
ATOM   2300  CB  VAL A1093     -11.830 -16.111  -0.897  1.00 83.90           C  
ANISOU 2300  CB  VAL A1093    10105  11790   9983    400    783    472       C  
ATOM   2301  CG1 VAL A1093     -10.433 -15.539  -0.669  1.00 83.20           C  
ANISOU 2301  CG1 VAL A1093    10139  11484   9990    313    890    382       C  
ATOM   2302  CG2 VAL A1093     -12.058 -16.394  -2.382  1.00 84.22           C  
ANISOU 2302  CG2 VAL A1093    10072  12055   9872    476    677    688       C  
ATOM   2303  N   ARG A1094     -13.116 -16.356   1.961  1.00 77.85           N  
ANISOU 2303  N   ARG A1094     9307  10930   9343    323    872     98       N  
ATOM   2304  CA  ARG A1094     -13.283 -15.940   3.363  1.00 77.40           C  
ANISOU 2304  CA  ARG A1094     9264  10747   9397    283    990    -91       C  
ATOM   2305  C   ARG A1094     -13.490 -17.125   4.316  1.00 78.67           C  
ANISOU 2305  C   ARG A1094     9429  11060   9402    165    902   -254       C  
ATOM   2306  O   ARG A1094     -13.185 -17.014   5.506  1.00 77.79           O  
ANISOU 2306  O   ARG A1094     9356  10895   9305     86    972   -439       O  
ATOM   2307  CB  ARG A1094     -14.401 -14.893   3.508  1.00 79.38           C  
ANISOU 2307  CB  ARG A1094     9423  10887   9850    436   1124    -10       C  
ATOM   2308  CG  ARG A1094     -14.087 -13.561   2.832  1.00 90.49           C  
ANISOU 2308  CG  ARG A1094    10839  12071  11472    555   1273    145       C  
ATOM   2309  CD  ARG A1094     -15.147 -12.521   3.123  1.00100.18           C  
ANISOU 2309  CD  ARG A1094    11971  13152  12939    711   1432    209       C  
ATOM   2310  NE  ARG A1094     -15.833 -12.061   1.914  1.00107.25           N  
ANISOU 2310  NE  ARG A1094    12776  14085  13891    917   1424    532       N  
ATOM   2311  CZ  ARG A1094     -15.568 -10.926   1.275  1.00122.84           C  
ANISOU 2311  CZ  ARG A1094    14755  15846  16071   1047   1575    728       C  
ATOM   2312  NH1 ARG A1094     -14.626 -10.107   1.726  1.00111.06           N  
ANISOU 2312  NH1 ARG A1094    13357  14062  14777    975   1761    601       N  
ATOM   2313  NH2 ARG A1094     -16.247 -10.596   0.186  1.00111.93           N  
ANISOU 2313  NH2 ARG A1094    13276  14551  14701   1252   1551   1053       N  
ATOM   2314  N   ARG A1095     -13.991 -18.262   3.778  1.00 73.62           N  
ANISOU 2314  N   ARG A1095     8740  10619   8611    151    759   -187       N  
ATOM   2315  CA  ARG A1095     -14.188 -19.520   4.500  1.00 71.40           C  
ANISOU 2315  CA  ARG A1095     8461  10471   8196     43    686   -298       C  
ATOM   2316  C   ARG A1095     -12.809 -20.100   4.812  1.00 71.03           C  
ANISOU 2316  C   ARG A1095     8524  10410   8055    -80    644   -396       C  
ATOM   2317  O   ARG A1095     -12.601 -20.602   5.918  1.00 70.44           O  
ANISOU 2317  O   ARG A1095     8483  10362   7918   -158    655   -517       O  
ATOM   2318  CB  ARG A1095     -15.025 -20.522   3.675  1.00 71.14           C  
ANISOU 2318  CB  ARG A1095     8333  10630   8068     51    570   -213       C  
ATOM   2319  CG  ARG A1095     -16.495 -20.570   4.082  1.00 82.92           C  
ANISOU 2319  CG  ARG A1095     9705  12200   9600    106    600   -214       C  
ATOM   2320  CD  ARG A1095     -17.272 -21.683   3.395  1.00 97.67           C  
ANISOU 2320  CD  ARG A1095    11464  14273  11371     77    496   -188       C  
ATOM   2321  NE  ARG A1095     -17.944 -21.230   2.173  1.00111.57           N  
ANISOU 2321  NE  ARG A1095    13099  16155  13138    200    446    -43       N  
ATOM   2322  CZ  ARG A1095     -17.706 -21.707   0.952  1.00128.37           C  
ANISOU 2322  CZ  ARG A1095    15183  18435  15158    188    341     20       C  
ATOM   2323  NH1 ARG A1095     -16.812 -22.674   0.769  1.00111.30           N  
ANISOU 2323  NH1 ARG A1095    13096  16290  12903     52    283    -62       N  
ATOM   2324  NH2 ARG A1095     -18.366 -21.225  -0.095  1.00119.22           N  
ANISOU 2324  NH2 ARG A1095    13892  17429  13978    316    296    166       N  
ATOM   2325  N   ALA A1096     -11.859 -19.977   3.852  1.00 64.32           N  
ANISOU 2325  N   ALA A1096     7721   9527   7190    -87    602   -335       N  
ATOM   2326  CA  ALA A1096     -10.486 -20.449   3.999  1.00 62.26           C  
ANISOU 2326  CA  ALA A1096     7548   9251   6855   -190    562   -421       C  
ATOM   2327  C   ALA A1096      -9.741 -19.661   5.069  1.00 65.75           C  
ANISOU 2327  C   ALA A1096     8045   9579   7358   -230    663   -568       C  
ATOM   2328  O   ALA A1096      -8.931 -20.245   5.794  1.00 64.80           O  
ANISOU 2328  O   ALA A1096     7968   9508   7145   -316    629   -679       O  
ATOM   2329  CB  ALA A1096      -9.752 -20.361   2.675  1.00 62.77           C  
ANISOU 2329  CB  ALA A1096     7634   9310   6905   -183    515   -325       C  
ATOM   2330  N   ALA A1097     -10.040 -18.343   5.190  1.00 62.74           N  
ANISOU 2330  N   ALA A1097     7647   9054   7137   -164    797   -575       N  
ATOM   2331  CA  ALA A1097      -9.446 -17.443   6.186  1.00 62.40           C  
ANISOU 2331  CA  ALA A1097     7630   8896   7184   -212    926   -758       C  
ATOM   2332  C   ALA A1097      -9.851 -17.863   7.597  1.00 65.48           C  
ANISOU 2332  C   ALA A1097     7997   9395   7486   -265    937   -908       C  
ATOM   2333  O   ALA A1097      -9.031 -17.791   8.506  1.00 65.68           O  
ANISOU 2333  O   ALA A1097     8044   9455   7455   -352    964  -1084       O  
ATOM   2334  CB  ALA A1097      -9.854 -16.002   5.916  1.00 64.56           C  
ANISOU 2334  CB  ALA A1097     7874   8966   7690   -121   1091   -720       C  
ATOM   2335  N   LEU A1098     -11.093 -18.347   7.769  1.00 61.44           N  
ANISOU 2335  N   LEU A1098     7431   8968   6945   -216    912   -838       N  
ATOM   2336  CA  LEU A1098     -11.604 -18.839   9.049  1.00 61.37           C  
ANISOU 2336  CA  LEU A1098     7397   9081   6839   -261    928   -946       C  
ATOM   2337  C   LEU A1098     -10.941 -20.170   9.406  1.00 63.96           C  
ANISOU 2337  C   LEU A1098     7769   9564   6968   -342    810   -946       C  
ATOM   2338  O   LEU A1098     -10.591 -20.372  10.566  1.00 63.87           O  
ANISOU 2338  O   LEU A1098     7765   9653   6849   -402    831  -1066       O  
ATOM   2339  CB  LEU A1098     -13.135 -18.980   8.995  1.00 62.02           C  
ANISOU 2339  CB  LEU A1098     7400   9198   6966   -186    946   -860       C  
ATOM   2340  CG  LEU A1098     -13.877 -19.289  10.300  1.00 67.20           C  
ANISOU 2340  CG  LEU A1098     8017   9961   7554   -222   1002   -965       C  
ATOM   2341  CD1 LEU A1098     -13.813 -18.119  11.276  1.00 68.66           C  
ANISOU 2341  CD1 LEU A1098     8182  10074   7830   -235   1158  -1158       C  
ATOM   2342  CD2 LEU A1098     -15.325 -19.652  10.013  1.00 70.07           C  
ANISOU 2342  CD2 LEU A1098     8295  10374   7955   -157    994   -863       C  
ATOM   2343  N   ILE A1099     -10.744 -21.062   8.404  1.00 59.52           N  
ANISOU 2343  N   ILE A1099     7225   9028   6360   -340    695   -813       N  
ATOM   2344  CA  ILE A1099     -10.078 -22.364   8.576  1.00 58.38           C  
ANISOU 2344  CA  ILE A1099     7117   8990   6075   -403    597   -790       C  
ATOM   2345  C   ILE A1099      -8.606 -22.118   8.962  1.00 62.89           C  
ANISOU 2345  C   ILE A1099     7738   9564   6591   -456    587   -895       C  
ATOM   2346  O   ILE A1099      -8.053 -22.834   9.798  1.00 62.07           O  
ANISOU 2346  O   ILE A1099     7649   9577   6360   -496    552   -928       O  
ATOM   2347  CB  ILE A1099     -10.264 -23.296   7.333  1.00 60.24           C  
ANISOU 2347  CB  ILE A1099     7341   9238   6309   -397    502   -660       C  
ATOM   2348  CG1 ILE A1099     -11.765 -23.584   7.067  1.00 60.40           C  
ANISOU 2348  CG1 ILE A1099     7282   9301   6368   -358    513   -592       C  
ATOM   2349  CG2 ILE A1099      -9.484 -24.616   7.491  1.00 60.25           C  
ANISOU 2349  CG2 ILE A1099     7377   9303   6211   -457    429   -643       C  
ATOM   2350  CD1 ILE A1099     -12.119 -23.955   5.628  1.00 64.12           C  
ANISOU 2350  CD1 ILE A1099     7702   9798   6861   -338    441   -499       C  
ATOM   2351  N   ASN A1100      -8.015 -21.049   8.409  1.00 60.93           N  
ANISOU 2351  N   ASN A1100     7507   9196   6449   -450    632   -944       N  
ATOM   2352  CA  ASN A1100      -6.657 -20.618   8.704  1.00 61.81           C  
ANISOU 2352  CA  ASN A1100     7645   9299   6540   -509    644  -1076       C  
ATOM   2353  C   ASN A1100      -6.562 -20.304  10.199  1.00 68.99           C  
ANISOU 2353  C   ASN A1100     8524  10317   7372   -553    708  -1253       C  
ATOM   2354  O   ASN A1100      -5.580 -20.694  10.834  1.00 69.87           O  
ANISOU 2354  O   ASN A1100     8635  10560   7353   -605    660  -1337       O  
ATOM   2355  CB  ASN A1100      -6.321 -19.377   7.871  1.00 64.20           C  
ANISOU 2355  CB  ASN A1100     7959   9419   7014   -494    730  -1094       C  
ATOM   2356  CG  ASN A1100      -4.869 -18.949   7.845  1.00 92.94           C  
ANISOU 2356  CG  ASN A1100    11622  13026  10665   -566    747  -1222       C  
ATOM   2357  OD1 ASN A1100      -4.129 -19.013   8.840  1.00 85.17           O  
ANISOU 2357  OD1 ASN A1100    10620  12153   9588   -634    745  -1389       O  
ATOM   2358  ND2 ASN A1100      -4.442 -18.458   6.691  1.00 87.98           N  
ANISOU 2358  ND2 ASN A1100    11021  12261  10146   -552    772  -1148       N  
ATOM   2359  N   MET A1101      -7.599 -19.632  10.762  1.00 66.35           N  
ANISOU 2359  N   MET A1101     8151   9954   7107   -528    815  -1309       N  
ATOM   2360  CA  MET A1101      -7.670 -19.262  12.180  1.00 67.19           C  
ANISOU 2360  CA  MET A1101     8212  10184   7135   -575    895  -1500       C  
ATOM   2361  C   MET A1101      -7.842 -20.489  13.069  1.00 69.52           C  
ANISOU 2361  C   MET A1101     8500  10707   7207   -585    816  -1440       C  
ATOM   2362  O   MET A1101      -7.224 -20.560  14.135  1.00 69.58           O  
ANISOU 2362  O   MET A1101     8480  10903   7055   -636    816  -1569       O  
ATOM   2363  CB  MET A1101      -8.805 -18.265  12.433  1.00 70.95           C  
ANISOU 2363  CB  MET A1101     8641  10549   7768   -539   1043  -1568       C  
ATOM   2364  CG  MET A1101      -8.501 -16.875  11.968  1.00 76.23           C  
ANISOU 2364  CG  MET A1101     9301  10995   8667   -537   1176  -1673       C  
ATOM   2365  SD  MET A1101      -9.934 -15.808  12.220  1.00 83.09           S  
ANISOU 2365  SD  MET A1101    10103  11711   9756   -465   1359  -1716       S  
ATOM   2366  CE  MET A1101      -9.518 -15.059  13.791  1.00 81.83           C  
ANISOU 2366  CE  MET A1101     9879  11654   9561   -585   1506  -2087       C  
ATOM   2367  N   VAL A1102      -8.689 -21.453  12.629  1.00 64.23           N  
ANISOU 2367  N   VAL A1102     7846  10033   6527   -538    758  -1244       N  
ATOM   2368  CA  VAL A1102      -8.971 -22.711  13.337  1.00 63.15           C  
ANISOU 2368  CA  VAL A1102     7708  10063   6224   -540    709  -1141       C  
ATOM   2369  C   VAL A1102      -7.700 -23.581  13.343  1.00 67.60           C  
ANISOU 2369  C   VAL A1102     8303  10720   6664   -556    603  -1085       C  
ATOM   2370  O   VAL A1102      -7.438 -24.289  14.319  1.00 68.49           O  
ANISOU 2370  O   VAL A1102     8402  11017   6603   -560    583  -1052       O  
ATOM   2371  CB  VAL A1102     -10.227 -23.429  12.769  1.00 65.05           C  
ANISOU 2371  CB  VAL A1102     7940  10242   6534   -500    702   -979       C  
ATOM   2372  CG1 VAL A1102     -10.423 -24.808  13.388  1.00 64.70           C  
ANISOU 2372  CG1 VAL A1102     7901  10324   6358   -510    675   -854       C  
ATOM   2373  CG2 VAL A1102     -11.484 -22.580  12.961  1.00 65.34           C  
ANISOU 2373  CG2 VAL A1102     7924  10226   6677   -473    809  -1040       C  
ATOM   2374  N   PHE A1103      -6.875 -23.464  12.287  1.00 62.99           N  
ANISOU 2374  N   PHE A1103     7749  10019   6164   -559    544  -1073       N  
ATOM   2375  CA  PHE A1103      -5.610 -24.182  12.207  1.00 62.46           C  
ANISOU 2375  CA  PHE A1103     7700  10023   6009   -571    451  -1039       C  
ATOM   2376  C   PHE A1103      -4.664 -23.657  13.256  1.00 70.43           C  
ANISOU 2376  C   PHE A1103     8670  11205   6886   -607    460  -1208       C  
ATOM   2377  O   PHE A1103      -4.044 -24.446  13.967  1.00 71.04           O  
ANISOU 2377  O   PHE A1103     8726  11468   6798   -594    400  -1158       O  
ATOM   2378  CB  PHE A1103      -5.000 -24.064  10.809  1.00 62.65           C  
ANISOU 2378  CB  PHE A1103     7757   9888   6159   -575    404  -1012       C  
ATOM   2379  CG  PHE A1103      -5.117 -25.343  10.020  1.00 62.75           C  
ANISOU 2379  CG  PHE A1103     7790   9860   6191   -555    333   -844       C  
ATOM   2380  CD1 PHE A1103      -6.343 -25.756   9.511  1.00 64.90           C  
ANISOU 2380  CD1 PHE A1103     8056  10069   6535   -537    351   -745       C  
ATOM   2381  CD2 PHE A1103      -4.007 -26.147   9.805  1.00 64.52           C  
ANISOU 2381  CD2 PHE A1103     8024  10116   6376   -560    258   -805       C  
ATOM   2382  CE1 PHE A1103      -6.457 -26.952   8.804  1.00 65.11           C  
ANISOU 2382  CE1 PHE A1103     8083  10061   6594   -540    305   -633       C  
ATOM   2383  CE2 PHE A1103      -4.120 -27.335   9.080  1.00 66.78           C  
ANISOU 2383  CE2 PHE A1103     8318  10343   6710   -551    218   -678       C  
ATOM   2384  CZ  PHE A1103      -5.343 -27.724   8.576  1.00 64.09           C  
ANISOU 2384  CZ  PHE A1103     7970   9938   6445   -549    247   -605       C  
ATOM   2385  N   GLN A1104      -4.637 -22.325  13.411  1.00 70.02           N  
ANISOU 2385  N   GLN A1104     8592  11104   6909   -649    549  -1408       N  
ATOM   2386  CA  GLN A1104      -3.799 -21.594  14.355  1.00 72.40           C  
ANISOU 2386  CA  GLN A1104     8831  11567   7112   -711    585  -1642       C  
ATOM   2387  C   GLN A1104      -4.131 -21.852  15.840  1.00 79.09           C  
ANISOU 2387  C   GLN A1104     9617  12695   7738   -717    605  -1698       C  
ATOM   2388  O   GLN A1104      -3.237 -22.265  16.579  1.00 79.15           O  
ANISOU 2388  O   GLN A1104     9575  12954   7545   -727    538  -1733       O  
ATOM   2389  CB  GLN A1104      -3.843 -20.087  14.029  1.00 74.65           C  
ANISOU 2389  CB  GLN A1104     9102  11667   7596   -762    716  -1846       C  
ATOM   2390  CG  GLN A1104      -2.676 -19.270  14.590  1.00 92.65           C  
ANISOU 2390  CG  GLN A1104    11311  14050   9840   -854    760  -2127       C  
ATOM   2391  CD  GLN A1104      -2.458 -17.951  13.877  1.00112.31           C  
ANISOU 2391  CD  GLN A1104    13806  16274  12591   -902    894  -2276       C  
ATOM   2392  OE1 GLN A1104      -3.207 -17.548  12.974  1.00108.98           O  
ANISOU 2392  OE1 GLN A1104    13438  15595  12373   -850    957  -2152       O  
ATOM   2393  NE2 GLN A1104      -1.411 -17.245  14.265  1.00103.34           N  
ANISOU 2393  NE2 GLN A1104    12603  15204  11458  -1000    948  -2540       N  
ATOM   2394  N   MET A1105      -5.394 -21.617  16.277  1.00 77.57           N  
ANISOU 2394  N   MET A1105     9418  12485   7571   -707    697  -1699       N  
ATOM   2395  CA  MET A1105      -5.761 -21.731  17.697  1.00 79.76           C  
ANISOU 2395  CA  MET A1105     9631  13041   7633   -724    739  -1772       C  
ATOM   2396  C   MET A1105      -6.950 -22.666  18.043  1.00 85.10           C  
ANISOU 2396  C   MET A1105    10332  13760   8244   -670    750  -1558       C  
ATOM   2397  O   MET A1105      -7.404 -22.651  19.192  1.00 86.70           O  
ANISOU 2397  O   MET A1105    10481  14181   8279   -687    811  -1619       O  
ATOM   2398  CB  MET A1105      -6.011 -20.328  18.295  1.00 83.70           C  
ANISOU 2398  CB  MET A1105    10061  13549   8194   -800    886  -2086       C  
ATOM   2399  CG  MET A1105      -6.971 -19.466  17.489  1.00 86.85           C  
ANISOU 2399  CG  MET A1105    10488  13621   8889   -784    998  -2107       C  
ATOM   2400  SD  MET A1105      -6.273 -17.836  17.136  1.00 91.99           S  
ANISOU 2400  SD  MET A1105    11101  14076   9774   -861   1129  -2411       S  
ATOM   2401  CE  MET A1105      -7.281 -17.354  15.784  1.00 87.57           C  
ANISOU 2401  CE  MET A1105    10605  13125   9542   -774   1194  -2237       C  
ATOM   2402  N   GLY A1106      -7.421 -23.468  17.086  1.00 80.39           N  
ANISOU 2402  N   GLY A1106     9800  12974   7770   -617    703  -1329       N  
ATOM   2403  CA  GLY A1106      -8.514 -24.414  17.315  1.00 80.22           C  
ANISOU 2403  CA  GLY A1106     9794  12967   7721   -580    727  -1136       C  
ATOM   2404  C   GLY A1106      -9.899 -23.807  17.396  1.00 84.99           C  
ANISOU 2404  C   GLY A1106    10373  13482   8438   -587    841  -1200       C  
ATOM   2405  O   GLY A1106     -10.039 -22.607  17.643  1.00 85.05           O  
ANISOU 2405  O   GLY A1106    10341  13468   8507   -618    923  -1413       O  
ATOM   2406  N   GLU A1107     -10.937 -24.656  17.214  1.00 82.71           N  
ANISOU 2406  N   GLU A1107    10096  13138   8192   -560    860  -1025       N  
ATOM   2407  CA  GLU A1107     -12.368 -24.293  17.215  1.00 83.50           C  
ANISOU 2407  CA  GLU A1107    10159  13160   8406   -556    959  -1053       C  
ATOM   2408  C   GLU A1107     -12.805 -23.511  18.452  1.00 90.47           C  
ANISOU 2408  C   GLU A1107    10982  14204   9190   -589   1076  -1235       C  
ATOM   2409  O   GLU A1107     -13.483 -22.493  18.310  1.00 90.08           O  
ANISOU 2409  O   GLU A1107    10890  14045   9290   -588   1163  -1377       O  
ATOM   2410  CB  GLU A1107     -13.275 -25.526  17.033  1.00 84.63           C  
ANISOU 2410  CB  GLU A1107    10308  13276   8572   -542    967   -850       C  
ATOM   2411  CG  GLU A1107     -13.072 -26.287  15.734  1.00 96.42           C  
ANISOU 2411  CG  GLU A1107    11837  14603  10195   -525    877   -711       C  
ATOM   2412  CD  GLU A1107     -12.059 -27.420  15.769  1.00129.44           C  
ANISOU 2412  CD  GLU A1107    16067  18829  14284   -521    806   -567       C  
ATOM   2413  OE1 GLU A1107     -11.241 -27.478  16.717  1.00130.38           O  
ANISOU 2413  OE1 GLU A1107    16194  19121  14222   -516    795   -569       O  
ATOM   2414  OE2 GLU A1107     -12.081 -28.255  14.835  1.00128.91           O  
ANISOU 2414  OE2 GLU A1107    16016  18634  14329   -521    764   -457       O  
ATOM   2415  N   THR A1108     -12.406 -23.981  19.659  1.00 89.81           N  
ANISOU 2415  N   THR A1108    10883  14390   8850   -612   1086  -1228       N  
ATOM   2416  CA  THR A1108     -12.742 -23.368  20.955  1.00 92.09           C  
ANISOU 2416  CA  THR A1108    11102  14905   8985   -656   1196  -1411       C  
ATOM   2417  C   THR A1108     -12.168 -21.955  21.070  1.00 97.41           C  
ANISOU 2417  C   THR A1108    11728  15569   9714   -704   1240  -1719       C  
ATOM   2418  O   THR A1108     -12.780 -21.099  21.712  1.00 99.08           O  
ANISOU 2418  O   THR A1108    11872  15828   9947   -744   1370  -1930       O  
ATOM   2419  CB  THR A1108     -12.291 -24.262  22.128  1.00101.26           C  
ANISOU 2419  CB  THR A1108    12251  16399   9824   -658   1178  -1299       C  
ATOM   2420  OG1 THR A1108     -12.406 -25.643  21.770  1.00100.78           O  
ANISOU 2420  OG1 THR A1108    12250  16278   9765   -606   1126   -987       O  
ATOM   2421  CG2 THR A1108     -13.075 -23.990  23.406  1.00100.76           C  
ANISOU 2421  CG2 THR A1108    12116  16578   9590   -699   1310  -1410       C  
ATOM   2422  N   GLY A1109     -11.013 -21.736  20.440  1.00 92.66           N  
ANISOU 2422  N   GLY A1109    11156  14893   9157   -706   1150  -1751       N  
ATOM   2423  CA  GLY A1109     -10.321 -20.454  20.423  1.00 92.89           C  
ANISOU 2423  CA  GLY A1109    11143  14877   9274   -762   1200  -2038       C  
ATOM   2424  C   GLY A1109     -11.012 -19.413  19.568  1.00 95.37           C  
ANISOU 2424  C   GLY A1109    11458  14863   9916   -744   1299  -2122       C  
ATOM   2425  O   GLY A1109     -11.384 -18.346  20.073  1.00 96.60           O  
ANISOU 2425  O   GLY A1109    11546  14997  10162   -787   1446  -2368       O  
ATOM   2426  N   VAL A1110     -11.194 -19.731  18.263  1.00 88.95           N  
ANISOU 2426  N   VAL A1110    10712  13802   9282   -676   1226  -1912       N  
ATOM   2427  CA  VAL A1110     -11.831 -18.873  17.249  1.00 87.88           C  
ANISOU 2427  CA  VAL A1110    10577  13366   9448   -624   1294  -1908       C  
ATOM   2428  C   VAL A1110     -13.256 -18.492  17.657  1.00 93.81           C  
ANISOU 2428  C   VAL A1110    11265  14085  10293   -596   1422  -1949       C  
ATOM   2429  O   VAL A1110     -13.641 -17.331  17.499  1.00 95.10           O  
ANISOU 2429  O   VAL A1110    11383  14073  10677   -577   1552  -2086       O  
ATOM   2430  CB  VAL A1110     -11.764 -19.472  15.819  1.00 89.21           C  
ANISOU 2430  CB  VAL A1110    10813  13364   9720   -557   1173  -1659       C  
ATOM   2431  CG1 VAL A1110     -12.212 -18.458  14.769  1.00 88.86           C  
ANISOU 2431  CG1 VAL A1110    10758  13049   9956   -492   1240  -1645       C  
ATOM   2432  CG2 VAL A1110     -10.361 -19.965  15.501  1.00 88.07           C  
ANISOU 2432  CG2 VAL A1110    10723  13270   9469   -588   1052  -1623       C  
ATOM   2433  N   ALA A1111     -14.011 -19.456  18.234  1.00 90.09           N  
ANISOU 2433  N   ALA A1111    10784  13779   9666   -593   1403  -1836       N  
ATOM   2434  CA  ALA A1111     -15.380 -19.270  18.723  1.00 90.65           C  
ANISOU 2434  CA  ALA A1111    10786  13862   9794   -576   1521  -1872       C  
ATOM   2435  C   ALA A1111     -15.489 -18.102  19.719  1.00 96.65           C  
ANISOU 2435  C   ALA A1111    11467  14675  10581   -630   1690  -2180       C  
ATOM   2436  O   ALA A1111     -16.549 -17.478  19.820  1.00 97.95           O  
ANISOU 2436  O   ALA A1111    11562  14742  10911   -599   1818  -2256       O  
ATOM   2437  CB  ALA A1111     -15.878 -20.553  19.368  1.00 91.25           C  
ANISOU 2437  CB  ALA A1111    10869  14144   9656   -593   1487  -1722       C  
ATOM   2438  N   GLY A1112     -14.388 -17.817  20.416  1.00 93.11           N  
ANISOU 2438  N   GLY A1112    11013  14387   9979   -713   1693  -2367       N  
ATOM   2439  CA  GLY A1112     -14.287 -16.746  21.398  1.00 94.96           C  
ANISOU 2439  CA  GLY A1112    11157  14710  10214   -795   1855  -2713       C  
ATOM   2440  C   GLY A1112     -14.361 -15.348  20.820  1.00 98.84           C  
ANISOU 2440  C   GLY A1112    11612  14884  11058   -778   1997  -2888       C  
ATOM   2441  O   GLY A1112     -14.781 -14.419  21.518  1.00100.07           O  
ANISOU 2441  O   GLY A1112    11676  15031  11315   -825   2182  -3162       O  
ATOM   2442  N   PHE A1113     -13.970 -15.184  19.536  1.00 93.95           N  
ANISOU 2442  N   PHE A1113    11059  13997  10639   -709   1929  -2728       N  
ATOM   2443  CA  PHE A1113     -13.976 -13.893  18.833  1.00 94.60           C  
ANISOU 2443  CA  PHE A1113    11119  13745  11080   -670   2069  -2823       C  
ATOM   2444  C   PHE A1113     -15.408 -13.438  18.447  1.00 98.86           C  
ANISOU 2444  C   PHE A1113    11608  14080  11876   -554   2178  -2730       C  
ATOM   2445  O   PHE A1113     -15.633 -13.031  17.307  1.00 97.69           O  
ANISOU 2445  O   PHE A1113    11479  13665  11972   -443   2181  -2554       O  
ATOM   2446  CB  PHE A1113     -13.058 -13.948  17.592  1.00 94.72           C  
ANISOU 2446  CB  PHE A1113    11222  13583  11184   -632   1957  -2648       C  
ATOM   2447  CG  PHE A1113     -11.579 -14.148  17.837  1.00 96.02           C  
ANISOU 2447  CG  PHE A1113    11418  13894  11172   -737   1877  -2767       C  
ATOM   2448  CD1 PHE A1113     -11.021 -15.419  17.823  1.00 97.45           C  
ANISOU 2448  CD1 PHE A1113    11659  14295  11073   -745   1675  -2594       C  
ATOM   2449  CD2 PHE A1113     -10.730 -13.058  18.001  1.00 99.81           C  
ANISOU 2449  CD2 PHE A1113    11858  14270  11797   -823   2012  -3047       C  
ATOM   2450  CE1 PHE A1113      -9.646 -15.602  18.010  1.00 98.19           C  
ANISOU 2450  CE1 PHE A1113    11765  14531  11012   -825   1594  -2691       C  
ATOM   2451  CE2 PHE A1113      -9.354 -13.242  18.188  1.00102.32           C  
ANISOU 2451  CE2 PHE A1113    12184  14741  11952   -921   1932  -3167       C  
ATOM   2452  CZ  PHE A1113      -8.822 -14.513  18.193  1.00 98.61           C  
ANISOU 2452  CZ  PHE A1113    11768  14514  11186   -914   1715  -2982       C  
ATOM   2453  N   THR A1114     -16.354 -13.465  19.419  1.00 96.86           N  
ANISOU 2453  N   THR A1114    11275  13967  11559   -576   2276  -2852       N  
ATOM   2454  CA  THR A1114     -17.785 -13.130  19.266  1.00 97.45           C  
ANISOU 2454  CA  THR A1114    11276  13909  11843   -473   2381  -2792       C  
ATOM   2455  C   THR A1114     -18.036 -11.776  18.593  1.00102.38           C  
ANISOU 2455  C   THR A1114    11850  14170  12879   -378   2552  -2838       C  
ATOM   2456  O   THR A1114     -18.928 -11.675  17.751  1.00101.58           O  
ANISOU 2456  O   THR A1114    11722  13905  12970   -230   2546  -2617       O  
ATOM   2457  CB  THR A1114     -18.539 -13.231  20.607  1.00106.47           C  
ANISOU 2457  CB  THR A1114    12331  15281  12842   -546   2494  -2995       C  
ATOM   2458  OG1 THR A1114     -18.023 -12.260  21.516  1.00109.69           O  
ANISOU 2458  OG1 THR A1114    12672  15717  13287   -658   2672  -3372       O  
ATOM   2459  CG2 THR A1114     -18.492 -14.637  21.224  1.00102.35           C  
ANISOU 2459  CG2 THR A1114    11855  15102  11931   -609   2344  -2874       C  
ATOM   2460  N   ASN A1115     -17.245 -10.754  18.960  1.00100.70           N  
ANISOU 2460  N   ASN A1115    11613  13841  12805   -460   2711  -3119       N  
ATOM   2461  CA  ASN A1115     -17.307  -9.394  18.418  1.00102.25           C  
ANISOU 2461  CA  ASN A1115    11765  13660  13426   -386   2919  -3186       C  
ATOM   2462  C   ASN A1115     -17.064  -9.383  16.902  1.00104.14           C  
ANISOU 2462  C   ASN A1115    12082  13668  13819   -247   2814  -2838       C  
ATOM   2463  O   ASN A1115     -17.890  -8.863  16.150  1.00103.55           O  
ANISOU 2463  O   ASN A1115    11965  13363  14018    -81   2886  -2648       O  
ATOM   2464  CB  ASN A1115     -16.309  -8.465  19.151  1.00105.14           C  
ANISOU 2464  CB  ASN A1115    12093  13979  13876   -545   3104  -3590       C  
ATOM   2465  CG  ASN A1115     -15.064  -9.148  19.700  1.00117.66           C  
ANISOU 2465  CG  ASN A1115    13731  15877  15098   -708   2956  -3723       C  
ATOM   2466  OD1 ASN A1115     -14.210  -9.665  18.968  1.00 98.19           O  
ANISOU 2466  OD1 ASN A1115    11362  13418  12527   -701   2784  -3532       O  
ATOM   2467  ND2 ASN A1115     -14.938  -9.159  21.016  1.00113.25           N  
ANISOU 2467  ND2 ASN A1115    13095  15605  14330   -855   3023  -4055       N  
ATOM   2468  N   SER A1116     -15.949  -9.998  16.466  1.00 99.69           N  
ANISOU 2468  N   SER A1116    11622  13196  13059   -308   2641  -2746       N  
ATOM   2469  CA  SER A1116     -15.544 -10.091  15.061  1.00 98.44           C  
ANISOU 2469  CA  SER A1116    11543  12875  12985   -205   2529  -2438       C  
ATOM   2470  C   SER A1116     -16.421 -11.067  14.271  1.00101.30           C  
ANISOU 2470  C   SER A1116    11920  13341  13229    -77   2335  -2093       C  
ATOM   2471  O   SER A1116     -16.760 -10.783  13.120  1.00100.99           O  
ANISOU 2471  O   SER A1116    11878  13131  13362     71   2319  -1835       O  
ATOM   2472  CB  SER A1116     -14.076 -10.492  14.955  1.00 99.97           C  
ANISOU 2472  CB  SER A1116    11827  13163  12993   -327   2413  -2490       C  
ATOM   2473  OG  SER A1116     -13.228  -9.536  15.569  1.00108.99           O  
ANISOU 2473  OG  SER A1116    12938  14209  14265   -451   2597  -2824       O  
ATOM   2474  N   LEU A1117     -16.787 -12.206  14.895  1.00 96.82           N  
ANISOU 2474  N   LEU A1117    11355  13062  12369   -137   2200  -2092       N  
ATOM   2475  CA  LEU A1117     -17.622 -13.265  14.322  1.00 95.37           C  
ANISOU 2475  CA  LEU A1117    11170  13011  12058    -58   2031  -1827       C  
ATOM   2476  C   LEU A1117     -19.015 -12.743  13.950  1.00101.23           C  
ANISOU 2476  C   LEU A1117    11801  13635  13028     97   2121  -1719       C  
ATOM   2477  O   LEU A1117     -19.583 -13.167  12.939  1.00 99.54           O  
ANISOU 2477  O   LEU A1117    11566  13434  12822    210   2003  -1461       O  
ATOM   2478  CB  LEU A1117     -17.719 -14.431  15.319  1.00 94.65           C  
ANISOU 2478  CB  LEU A1117    11092  13219  11653   -171   1940  -1898       C  
ATOM   2479  CG  LEU A1117     -16.838 -15.674  15.082  1.00 97.54           C  
ANISOU 2479  CG  LEU A1117    11557  13753  11750   -241   1739  -1775       C  
ATOM   2480  CD1 LEU A1117     -15.367 -15.328  14.899  1.00 97.47           C  
ANISOU 2480  CD1 LEU A1117    11622  13685  11725   -305   1717  -1856       C  
ATOM   2481  CD2 LEU A1117     -16.974 -16.657  16.230  1.00100.23           C  
ANISOU 2481  CD2 LEU A1117    11900  14364  11819   -336   1704  -1840       C  
ATOM   2482  N   ARG A1118     -19.540 -11.798  14.756  1.00101.22           N  
ANISOU 2482  N   ARG A1118    11713  13531  13215    102   2334  -1931       N  
ATOM   2483  CA  ARG A1118     -20.825 -11.131  14.541  1.00103.49           C  
ANISOU 2483  CA  ARG A1118    11875  13684  13763    257   2458  -1863       C  
ATOM   2484  C   ARG A1118     -20.732 -10.227  13.303  1.00108.71           C  
ANISOU 2484  C   ARG A1118    12526  14064  14713    427   2508  -1647       C  
ATOM   2485  O   ARG A1118     -21.692 -10.146  12.538  1.00109.36           O  
ANISOU 2485  O   ARG A1118    12524  14116  14914    600   2480  -1415       O  
ATOM   2486  CB  ARG A1118     -21.179 -10.262  15.756  1.00107.69           C  
ANISOU 2486  CB  ARG A1118    12322  14148  14447    201   2703  -2189       C  
ATOM   2487  CG  ARG A1118     -22.424 -10.676  16.551  1.00120.85           C  
ANISOU 2487  CG  ARG A1118    13886  15991  16039    198   2738  -2265       C  
ATOM   2488  CD  ARG A1118     -23.019  -9.521  17.372  1.00132.18           C  
ANISOU 2488  CD  ARG A1118    15200  17273  17749    211   3018  -2536       C  
ATOM   2489  NE  ARG A1118     -22.032  -8.827  18.214  1.00137.62           N  
ANISOU 2489  NE  ARG A1118    15916  17908  18466     57   3176  -2877       N  
ATOM   2490  CZ  ARG A1118     -21.493  -7.642  17.931  1.00147.39           C  
ANISOU 2490  CZ  ARG A1118    17144  18834  20024     86   3358  -2976       C  
ATOM   2491  NH1 ARG A1118     -21.840  -6.991  16.826  1.00130.26           N  
ANISOU 2491  NH1 ARG A1118    14948  16369  18175    284   3407  -2721       N  
ATOM   2492  NH2 ARG A1118     -20.595  -7.104  18.745  1.00134.30           N  
ANISOU 2492  NH2 ARG A1118    15493  17168  18367    -83   3498  -3328       N  
ATOM   2493  N   MET A1119     -19.585  -9.537  13.125  1.00105.19           N  
ANISOU 2493  N   MET A1119    12156  13431  14380    378   2591  -1722       N  
ATOM   2494  CA  MET A1119     -19.335  -8.630  12.000  1.00105.96           C  
ANISOU 2494  CA  MET A1119    12259  13244  14756    526   2671  -1511       C  
ATOM   2495  C   MET A1119     -19.104  -9.393  10.695  1.00107.63           C  
ANISOU 2495  C   MET A1119    12532  13566  14798    601   2435  -1173       C  
ATOM   2496  O   MET A1119     -19.515  -8.925   9.633  1.00107.96           O  
ANISOU 2496  O   MET A1119    12528  13486  15007    788   2447   -893       O  
ATOM   2497  CB  MET A1119     -18.159  -7.701  12.309  1.00109.50           C  
ANISOU 2497  CB  MET A1119    12764  13463  15380    418   2857  -1734       C  
ATOM   2498  CG  MET A1119     -18.501  -6.611  13.294  1.00116.10           C  
ANISOU 2498  CG  MET A1119    13505  14103  16504    389   3151  -2043       C  
ATOM   2499  SD  MET A1119     -17.067  -6.122  14.273  1.00121.30           S  
ANISOU 2499  SD  MET A1119    14211  14719  17158    133   3299  -2491       S  
ATOM   2500  CE  MET A1119     -17.717  -4.680  15.094  1.00121.87           C  
ANISOU 2500  CE  MET A1119    14140  14491  17672    147   3687  -2804       C  
ATOM   2501  N   LEU A1120     -18.459 -10.573  10.787  1.00101.90           N  
ANISOU 2501  N   LEU A1120    11896  13083  13739    461   2230  -1199       N  
ATOM   2502  CA  LEU A1120     -18.163 -11.488   9.674  1.00 99.57           C  
ANISOU 2502  CA  LEU A1120    11657  12932  13244    488   2001   -943       C  
ATOM   2503  C   LEU A1120     -19.458 -12.056   9.098  1.00103.54           C  
ANISOU 2503  C   LEU A1120    12055  13593  13692    618   1885   -732       C  
ATOM   2504  O   LEU A1120     -19.548 -12.296   7.892  1.00102.68           O  
ANISOU 2504  O   LEU A1120    11932  13539  13543    720   1763   -477       O  
ATOM   2505  CB  LEU A1120     -17.280 -12.639  10.192  1.00 97.10           C  
ANISOU 2505  CB  LEU A1120    11443  12832  12618    299   1847  -1073       C  
ATOM   2506  CG  LEU A1120     -15.813 -12.700   9.763  1.00 99.87           C  
ANISOU 2506  CG  LEU A1120    11909  13138  12900    212   1791  -1080       C  
ATOM   2507  CD1 LEU A1120     -15.118 -11.354   9.891  1.00101.56           C  
ANISOU 2507  CD1 LEU A1120    12137  13078  13374    203   2004  -1210       C  
ATOM   2508  CD2 LEU A1120     -15.073 -13.717  10.591  1.00 99.57           C  
ANISOU 2508  CD2 LEU A1120    11937  13311  12585     42   1679  -1243       C  
ATOM   2509  N   GLN A1121     -20.454 -12.277   9.971  1.00100.95           N  
ANISOU 2509  N   GLN A1121    11641  13363  13353    606   1928   -856       N  
ATOM   2510  CA  GLN A1121     -21.771 -12.778   9.601  1.00101.44           C  
ANISOU 2510  CA  GLN A1121    11577  13585  13382    712   1844   -711       C  
ATOM   2511  C   GLN A1121     -22.612 -11.638   9.001  1.00108.83           C  
ANISOU 2511  C   GLN A1121    12383  14352  14614    940   1968   -546       C  
ATOM   2512  O   GLN A1121     -23.405 -11.877   8.089  1.00108.96           O  
ANISOU 2512  O   GLN A1121    12293  14494  14612   1081   1861   -319       O  
ATOM   2513  CB  GLN A1121     -22.466 -13.372  10.832  1.00102.59           C  
ANISOU 2513  CB  GLN A1121    11678  13881  13421    605   1873   -917       C  
ATOM   2514  CG  GLN A1121     -23.492 -14.446  10.494  1.00115.72           C  
ANISOU 2514  CG  GLN A1121    13248  15783  14937    624   1729   -806       C  
ATOM   2515  CD  GLN A1121     -24.135 -15.031  11.726  1.00133.05           C  
ANISOU 2515  CD  GLN A1121    15408  18113  17033    511   1782   -995       C  
ATOM   2516  OE1 GLN A1121     -23.465 -15.454  12.679  1.00127.46           O  
ANISOU 2516  OE1 GLN A1121    14800  17459  16171    353   1800  -1160       O  
ATOM   2517  NE2 GLN A1121     -25.457 -15.081  11.727  1.00125.95           N  
ANISOU 2517  NE2 GLN A1121    14355  17295  16207    594   1808   -965       N  
ATOM   2518  N   GLN A1122     -22.418 -10.401   9.507  1.00107.74           N  
ANISOU 2518  N   GLN A1122    12243  13938  14757    976   2201   -664       N  
ATOM   2519  CA  GLN A1122     -23.129  -9.196   9.065  1.00110.46           C  
ANISOU 2519  CA  GLN A1122    12468  14059  15443   1201   2371   -512       C  
ATOM   2520  C   GLN A1122     -22.464  -8.498   7.871  1.00115.12           C  
ANISOU 2520  C   GLN A1122    13103  14465  16174   1334   2393   -243       C  
ATOM   2521  O   GLN A1122     -22.936  -7.440   7.442  1.00117.30           O  
ANISOU 2521  O   GLN A1122    13289  14524  16755   1540   2554    -71       O  
ATOM   2522  CB  GLN A1122     -23.319  -8.214  10.235  1.00113.86           C  
ANISOU 2522  CB  GLN A1122    12856  14259  16145   1170   2647   -794       C  
ATOM   2523  CG  GLN A1122     -24.378  -8.648  11.232  1.00130.30           C  
ANISOU 2523  CG  GLN A1122    14836  16511  18160   1122   2665   -983       C  
ATOM   2524  CD  GLN A1122     -24.727  -7.518  12.157  1.00158.66           C  
ANISOU 2524  CD  GLN A1122    18349  19861  22073   1140   2959  -1224       C  
ATOM   2525  OE1 GLN A1122     -25.619  -6.714  11.875  1.00159.72           O  
ANISOU 2525  OE1 GLN A1122    18345  19834  22507   1343   3096  -1107       O  
ATOM   2526  NE2 GLN A1122     -24.029  -7.427  13.280  1.00150.83           N  
ANISOU 2526  NE2 GLN A1122    17429  18853  21027    931   3068  -1573       N  
ATOM   2527  N   LYS A1123     -21.370  -9.091   7.341  1.00109.86           N  
ANISOU 2527  N   LYS A1123    12571  13880  15291   1223   2246   -194       N  
ATOM   2528  CA  LYS A1123     -20.584  -8.615   6.192  1.00110.33           C  
ANISOU 2528  CA  LYS A1123    12694  13810  15416   1309   2246     54       C  
ATOM   2529  C   LYS A1123     -19.950  -7.216   6.405  1.00117.92           C  
ANISOU 2529  C   LYS A1123    13695  14368  16741   1338   2535     -8       C  
ATOM   2530  O   LYS A1123     -19.556  -6.565   5.432  1.00118.66           O  
ANISOU 2530  O   LYS A1123    13809  14297  16978   1465   2600    250       O  
ATOM   2531  CB  LYS A1123     -21.405  -8.681   4.881  1.00113.30           C  
ANISOU 2531  CB  LYS A1123    12953  14337  15760   1542   2125    441       C  
ATOM   2532  CG  LYS A1123     -21.458 -10.066   4.237  1.00117.28           C  
ANISOU 2532  CG  LYS A1123    13457  15218  15886   1473   1832    519       C  
ATOM   2533  CD  LYS A1123     -22.565 -10.960   4.778  1.00121.49           C  
ANISOU 2533  CD  LYS A1123    13879  16008  16273   1434   1721    401       C  
ATOM   2534  CE  LYS A1123     -22.439 -12.365   4.255  1.00122.33           C  
ANISOU 2534  CE  LYS A1123    14002  16437  16039   1318   1470    415       C  
ATOM   2535  NZ  LYS A1123     -23.665 -13.154   4.529  1.00127.92           N  
ANISOU 2535  NZ  LYS A1123    14567  17393  16642   1314   1379    356       N  
ATOM   2536  N   ARG A1124     -19.810  -6.780   7.679  1.00116.42           N  
ANISOU 2536  N   ARG A1124    13512  14028  16692   1206   2719   -361       N  
ATOM   2537  CA  ARG A1124     -19.186  -5.505   8.054  1.00118.99           C  
ANISOU 2537  CA  ARG A1124    13863  13973  17376   1183   3020   -515       C  
ATOM   2538  C   ARG A1124     -17.679  -5.771   8.069  1.00122.05           C  
ANISOU 2538  C   ARG A1124    14399  14361  17614    976   2972   -661       C  
ATOM   2539  O   ARG A1124     -17.082  -5.943   9.135  1.00121.21           O  
ANISOU 2539  O   ARG A1124    14334  14301  17420    764   3006  -1025       O  
ATOM   2540  CB  ARG A1124     -19.673  -5.024   9.442  1.00121.35           C  
ANISOU 2540  CB  ARG A1124    14086  14174  17849   1100   3225   -885       C  
ATOM   2541  CG  ARG A1124     -21.183  -4.866   9.605  1.00134.36           C  
ANISOU 2541  CG  ARG A1124    15574  15851  19625   1278   3269   -799       C  
ATOM   2542  CD  ARG A1124     -21.496  -4.291  10.972  1.00147.95           C  
ANISOU 2542  CD  ARG A1124    17226  17451  21536   1175   3507  -1200       C  
ATOM   2543  NE  ARG A1124     -22.889  -4.501  11.373  1.00159.90           N  
ANISOU 2543  NE  ARG A1124    18598  19100  23059   1277   3497  -1198       N  
ATOM   2544  CZ  ARG A1124     -23.436  -3.988  12.473  1.00175.51           C  
ANISOU 2544  CZ  ARG A1124    20480  20989  25217   1228   3710  -1509       C  
ATOM   2545  NH1 ARG A1124     -22.719  -3.220  13.285  1.00165.95           N  
ANISOU 2545  NH1 ARG A1124    19295  19563  24195   1075   3952  -1862       N  
ATOM   2546  NH2 ARG A1124     -24.707  -4.229  12.763  1.00159.51           N  
ANISOU 2546  NH2 ARG A1124    18320  19100  23188   1324   3690  -1489       N  
ATOM   2547  N   TRP A1125     -17.084  -5.868   6.870  1.00118.47           N  
ANISOU 2547  N   TRP A1125    14014  13901  17099   1042   2876   -372       N  
ATOM   2548  CA  TRP A1125     -15.682  -6.210   6.657  1.00116.94           C  
ANISOU 2548  CA  TRP A1125    13951  13734  16746    871   2802   -452       C  
ATOM   2549  C   TRP A1125     -14.694  -5.259   7.293  1.00122.41           C  
ANISOU 2549  C   TRP A1125    14685  14131  17693    729   3061   -746       C  
ATOM   2550  O   TRP A1125     -13.806  -5.710   8.012  1.00120.40           O  
ANISOU 2550  O   TRP A1125    14491  13996  17260    511   3004  -1047       O  
ATOM   2551  CB  TRP A1125     -15.382  -6.375   5.165  1.00115.77           C  
ANISOU 2551  CB  TRP A1125    13846  13626  16516    994   2681    -62       C  
ATOM   2552  CG  TRP A1125     -16.262  -7.354   4.442  1.00115.87           C  
ANISOU 2552  CG  TRP A1125    13801  13969  16256   1111   2419    197       C  
ATOM   2553  CD1 TRP A1125     -16.822  -7.185   3.212  1.00120.22           C  
ANISOU 2553  CD1 TRP A1125    14287  14571  16819   1330   2366    590       C  
ATOM   2554  CD2 TRP A1125     -16.670  -8.658   4.894  1.00113.43           C  
ANISOU 2554  CD2 TRP A1125    13479  13998  15620   1009   2184     73       C  
ATOM   2555  NE1 TRP A1125     -17.546  -8.302   2.862  1.00118.25           N  
ANISOU 2555  NE1 TRP A1125    13975  14687  16267   1356   2108    683       N  
ATOM   2556  CE2 TRP A1125     -17.475  -9.219   3.879  1.00117.55           C  
ANISOU 2556  CE2 TRP A1125    13922  14754  15987   1158   2004    371       C  
ATOM   2557  CE3 TRP A1125     -16.438  -9.408   6.063  1.00113.27           C  
ANISOU 2557  CE3 TRP A1125    13498  14116  15423    807   2119   -252       C  
ATOM   2558  CZ2 TRP A1125     -18.039 -10.495   3.989  1.00114.97           C  
ANISOU 2558  CZ2 TRP A1125    13556  14757  15370   1095   1780    326       C  
ATOM   2559  CZ3 TRP A1125     -17.007 -10.666   6.177  1.00112.87           C  
ANISOU 2559  CZ3 TRP A1125    13420  14378  15088    765   1902   -253       C  
ATOM   2560  CH2 TRP A1125     -17.810 -11.191   5.155  1.00113.52           C  
ANISOU 2560  CH2 TRP A1125    13424  14652  15057    900   1745     19       C  
ATOM   2561  N   ASP A1126     -14.851  -3.953   7.039  1.00122.62           N  
ANISOU 2561  N   ASP A1126    14667  13780  18144    854   3353   -662       N  
ATOM   2562  CA  ASP A1126     -13.983  -2.892   7.555  1.00124.74           C  
ANISOU 2562  CA  ASP A1126    14953  13709  18735    726   3657   -946       C  
ATOM   2563  C   ASP A1126     -14.039  -2.804   9.081  1.00128.48           C  
ANISOU 2563  C   ASP A1126    15370  14223  19223    538   3762  -1442       C  
ATOM   2564  O   ASP A1126     -13.004  -2.592   9.715  1.00128.13           O  
ANISOU 2564  O   ASP A1126    15355  14137  19189    322   3857  -1792       O  
ATOM   2565  CB  ASP A1126     -14.354  -1.546   6.916  1.00130.50           C  
ANISOU 2565  CB  ASP A1126    15629  14003  19953    935   3968   -701       C  
ATOM   2566  CG  ASP A1126     -14.580  -1.637   5.421  1.00141.39           C  
ANISOU 2566  CG  ASP A1126    17030  15406  21284   1169   3855   -157       C  
ATOM   2567  OD1 ASP A1126     -15.709  -1.991   5.012  1.00141.81           O  
ANISOU 2567  OD1 ASP A1126    17007  15638  21238   1369   3712    119       O  
ATOM   2568  OD2 ASP A1126     -13.625  -1.373   4.660  1.00147.75           O  
ANISOU 2568  OD2 ASP A1126    17921  16082  22136   1146   3907    -16       O  
ATOM   2569  N   GLU A1127     -15.242  -2.991   9.662  1.00124.86           N  
ANISOU 2569  N   GLU A1127    14818  13879  18743    616   3739  -1478       N  
ATOM   2570  CA  GLU A1127     -15.482  -2.973  11.108  1.00124.91           C  
ANISOU 2570  CA  GLU A1127    14756  13980  18725    457   3829  -1922       C  
ATOM   2571  C   GLU A1127     -14.853  -4.193  11.789  1.00124.44           C  
ANISOU 2571  C   GLU A1127    14760  14334  18188    244   3567  -2136       C  
ATOM   2572  O   GLU A1127     -14.383  -4.078  12.920  1.00124.49           O  
ANISOU 2572  O   GLU A1127    14738  14418  18143     46   3656  -2551       O  
ATOM   2573  CB  GLU A1127     -16.986  -2.893  11.411  1.00127.50           C  
ANISOU 2573  CB  GLU A1127    14965  14329  19152    618   3868  -1851       C  
ATOM   2574  CG  GLU A1127     -17.580  -1.518  11.169  1.00142.79           C  
ANISOU 2574  CG  GLU A1127    16804  15827  21622    799   4205  -1769       C  
ATOM   2575  CD  GLU A1127     -19.091  -1.508  11.078  1.00165.82           C  
ANISOU 2575  CD  GLU A1127    19598  18775  24630   1024   4197  -1564       C  
ATOM   2576  OE1 GLU A1127     -19.749  -1.358  12.133  1.00163.96           O  
ANISOU 2576  OE1 GLU A1127    19266  18570  24460    967   4312  -1863       O  
ATOM   2577  OE2 GLU A1127     -19.620  -1.652   9.953  1.00159.01           O  
ANISOU 2577  OE2 GLU A1127    18722  17931  23762   1255   4074  -1112       O  
ATOM   2578  N   ALA A1128     -14.842  -5.351  11.097  1.00117.10           N  
ANISOU 2578  N   ALA A1128    13902  13674  16915    288   3255  -1853       N  
ATOM   2579  CA  ALA A1128     -14.240  -6.595  11.581  1.00113.66           C  
ANISOU 2579  CA  ALA A1128    13533  13609  16045    120   3002  -1976       C  
ATOM   2580  C   ALA A1128     -12.712  -6.515  11.463  1.00116.73           C  
ANISOU 2580  C   ALA A1128    14002  13964  16384    -36   3001  -2112       C  
ATOM   2581  O   ALA A1128     -12.005  -7.011  12.341  1.00115.44           O  
ANISOU 2581  O   ALA A1128    13852  14026  15984   -218   2928  -2392       O  
ATOM   2582  CB  ALA A1128     -14.762  -7.774  10.778  1.00111.82           C  
ANISOU 2582  CB  ALA A1128    13335  13616  15535    226   2713  -1631       C  
ATOM   2583  N   ALA A1129     -12.214  -5.870  10.381  1.00113.46           N  
ANISOU 2583  N   ALA A1129    13633  13281  16195     43   3091  -1906       N  
ATOM   2584  CA  ALA A1129     -10.790  -5.677  10.088  1.00112.60           C  
ANISOU 2584  CA  ALA A1129    13595  13095  16095    -88   3119  -2003       C  
ATOM   2585  C   ALA A1129     -10.076  -4.862  11.163  1.00117.33           C  
ANISOU 2585  C   ALA A1129    14140  13582  16860   -283   3356  -2472       C  
ATOM   2586  O   ALA A1129      -8.903  -5.117  11.443  1.00116.43           O  
ANISOU 2586  O   ALA A1129    14054  13591  16591   -458   3301  -2685       O  
ATOM   2587  CB  ALA A1129     -10.619  -5.011   8.731  1.00114.37           C  
ANISOU 2587  CB  ALA A1129    13860  13024  16570     58   3219  -1663       C  
ATOM   2588  N   VAL A1130     -10.778  -3.879  11.753  1.00115.37           N  
ANISOU 2588  N   VAL A1130    13795  13107  16932   -255   3626  -2649       N  
ATOM   2589  CA  VAL A1130     -10.233  -3.031  12.813  1.00116.95           C  
ANISOU 2589  CA  VAL A1130    13915  13201  17321   -449   3886  -3143       C  
ATOM   2590  C   VAL A1130     -10.424  -3.690  14.187  1.00118.60           C  
ANISOU 2590  C   VAL A1130    14060  13802  17201   -593   3775  -3482       C  
ATOM   2591  O   VAL A1130      -9.571  -3.521  15.059  1.00119.37           O  
ANISOU 2591  O   VAL A1130    14107  14026  17222   -805   3843  -3896       O  
ATOM   2592  CB  VAL A1130     -10.726  -1.555  12.769  1.00124.56           C  
ANISOU 2592  CB  VAL A1130    14798  13688  18843   -372   4283  -3213       C  
ATOM   2593  CG1 VAL A1130     -10.181  -0.826  11.544  1.00125.45           C  
ANISOU 2593  CG1 VAL A1130    14974  13416  19277   -278   4435  -2936       C  
ATOM   2594  CG2 VAL A1130     -12.250  -1.450  12.829  1.00125.19           C  
ANISOU 2594  CG2 VAL A1130    14812  13713  19040   -170   4319  -3031       C  
ATOM   2595  N   ASN A1131     -11.525  -4.458  14.364  1.00112.15           N  
ANISOU 2595  N   ASN A1131    13237  13200  16176   -482   3605  -3303       N  
ATOM   2596  CA  ASN A1131     -11.842  -5.164  15.610  1.00110.65           C  
ANISOU 2596  CA  ASN A1131    12992  13392  15656   -592   3498  -3551       C  
ATOM   2597  C   ASN A1131     -10.888  -6.331  15.826  1.00110.10           C  
ANISOU 2597  C   ASN A1131    12990  13707  15137   -713   3218  -3565       C  
ATOM   2598  O   ASN A1131     -10.480  -6.579  16.962  1.00110.16           O  
ANISOU 2598  O   ASN A1131    12940  14006  14910   -875   3200  -3894       O  
ATOM   2599  CB  ASN A1131     -13.293  -5.648  15.621  1.00110.39           C  
ANISOU 2599  CB  ASN A1131    12935  13446  15563   -433   3414  -3323       C  
ATOM   2600  CG  ASN A1131     -13.777  -6.066  16.987  1.00130.74           C  
ANISOU 2600  CG  ASN A1131    15434  16342  17899   -542   3402  -3608       C  
ATOM   2601  OD1 ASN A1131     -13.574  -7.202  17.428  1.00120.26           O  
ANISOU 2601  OD1 ASN A1131    14145  15387  16162   -610   3172  -3587       O  
ATOM   2602  ND2 ASN A1131     -14.425  -5.151  17.690  1.00125.57           N  
ANISOU 2602  ND2 ASN A1131    14664  15543  17502   -557   3667  -3875       N  
ATOM   2603  N   LEU A1132     -10.527  -7.038  14.741  1.00102.82           N  
ANISOU 2603  N   LEU A1132    12177  12798  14094   -629   3006  -3210       N  
ATOM   2604  CA  LEU A1132      -9.589  -8.156  14.802  1.00 99.94           C  
ANISOU 2604  CA  LEU A1132    11875  12750  13346   -720   2749  -3185       C  
ATOM   2605  C   LEU A1132      -8.179  -7.639  15.073  1.00105.37           C  
ANISOU 2605  C   LEU A1132    12542  13424  14068   -894   2838  -3493       C  
ATOM   2606  O   LEU A1132      -7.393  -8.338  15.707  1.00104.04           O  
ANISOU 2606  O   LEU A1132    12365  13583  13582  -1014   2690  -3646       O  
ATOM   2607  CB  LEU A1132      -9.616  -8.977  13.506  1.00 97.17           C  
ANISOU 2607  CB  LEU A1132    11631  12389  12901   -588   2531  -2751       C  
ATOM   2608  CG  LEU A1132     -10.729 -10.001  13.351  1.00 99.41           C  
ANISOU 2608  CG  LEU A1132    11930  12847  12993   -469   2347  -2481       C  
ATOM   2609  CD1 LEU A1132     -11.015 -10.267  11.899  1.00 97.74           C  
ANISOU 2609  CD1 LEU A1132    11780  12511  12844   -316   2241  -2088       C  
ATOM   2610  CD2 LEU A1132     -10.399 -11.298  14.070  1.00100.11           C  
ANISOU 2610  CD2 LEU A1132    12041  13316  12681   -559   2133  -2524       C  
ATOM   2611  N   ALA A1133      -7.872  -6.399  14.618  1.00104.78           N  
ANISOU 2611  N   ALA A1133    12448  12972  14391   -904   3095  -3585       N  
ATOM   2612  CA  ALA A1133      -6.581  -5.726  14.809  1.00106.47           C  
ANISOU 2612  CA  ALA A1133    12624  13111  14719  -1080   3237  -3909       C  
ATOM   2613  C   ALA A1133      -6.364  -5.359  16.291  1.00113.35           C  
ANISOU 2613  C   ALA A1133    13357  14196  15514  -1272   3363  -4430       C  
ATOM   2614  O   ALA A1133      -5.226  -5.128  16.716  1.00113.95           O  
ANISOU 2614  O   ALA A1133    13374  14384  15538  -1452   3406  -4757       O  
ATOM   2615  CB  ALA A1133      -6.507  -4.481  13.935  1.00109.10           C  
ANISOU 2615  CB  ALA A1133    12969  12946  15539  -1026   3519  -3840       C  
ATOM   2616  N   LYS A1134      -7.464  -5.336  17.070  1.00111.01           N  
ANISOU 2616  N   LYS A1134    12998  13989  15192  -1237   3418  -4513       N  
ATOM   2617  CA  LYS A1134      -7.492  -5.049  18.505  1.00113.17           C  
ANISOU 2617  CA  LYS A1134    13131  14511  15357  -1402   3534  -4987       C  
ATOM   2618  C   LYS A1134      -7.446  -6.358  19.342  1.00114.78           C  
ANISOU 2618  C   LYS A1134    13332  15267  15014  -1440   3245  -4974       C  
ATOM   2619  O   LYS A1134      -7.750  -6.329  20.537  1.00116.37           O  
ANISOU 2619  O   LYS A1134    13423  15744  15048  -1536   3301  -5278       O  
ATOM   2620  CB  LYS A1134      -8.762  -4.245  18.861  1.00118.11           C  
ANISOU 2620  CB  LYS A1134    13683  14905  16288  -1335   3783  -5079       C  
ATOM   2621  CG  LYS A1134      -8.837  -2.830  18.298  1.00136.77           C  
ANISOU 2621  CG  LYS A1134    16015  16723  19228  -1308   4132  -5156       C  
ATOM   2622  CD  LYS A1134     -10.115  -2.160  18.784  1.00151.62           C  
ANISOU 2622  CD  LYS A1134    17806  18427  21377  -1236   4363  -5260       C  
ATOM   2623  CE  LYS A1134     -10.577  -1.026  17.908  1.00166.74           C  
ANISOU 2623  CE  LYS A1134    19724  19764  23866  -1089   4650  -5094       C  
ATOM   2624  NZ  LYS A1134     -11.952  -0.589  18.273  1.00177.09           N  
ANISOU 2624  NZ  LYS A1134    20952  20934  25400   -969   4818  -5099       N  
ATOM   2625  N   SER A1135      -7.082  -7.499  18.720  1.00107.13           N  
ANISOU 2625  N   SER A1135    12476  14455  13774  -1360   2954  -4619       N  
ATOM   2626  CA  SER A1135      -7.029  -8.788  19.418  1.00104.65           C  
ANISOU 2626  CA  SER A1135    12167  14617  12978  -1370   2695  -4543       C  
ATOM   2627  C   SER A1135      -5.621  -9.208  19.825  1.00107.21           C  
ANISOU 2627  C   SER A1135    12451  15265  13017  -1503   2562  -4721       C  
ATOM   2628  O   SER A1135      -4.638  -8.665  19.316  1.00106.80           O  
ANISOU 2628  O   SER A1135    12395  15050  13133  -1574   2626  -4837       O  
ATOM   2629  CB  SER A1135      -7.690  -9.887  18.587  1.00104.25           C  
ANISOU 2629  CB  SER A1135    12246  14550  12813  -1192   2473  -4045       C  
ATOM   2630  OG  SER A1135      -6.880 -10.313  17.504  1.00107.02           O  
ANISOU 2630  OG  SER A1135    12696  14803  13164  -1150   2328  -3802       O  
ATOM   2631  N   ARG A1136      -5.538 -10.187  20.746  1.00103.09           N  
ANISOU 2631  N   ARG A1136    11894  15210  12065  -1527   2383  -4727       N  
ATOM   2632  CA  ARG A1136      -4.283 -10.769  21.222  1.00102.89           C  
ANISOU 2632  CA  ARG A1136    11814  15571  11708  -1617   2220  -4842       C  
ATOM   2633  C   ARG A1136      -3.634 -11.587  20.102  1.00103.22           C  
ANISOU 2633  C   ARG A1136    11983  15517  11719  -1523   2013  -4476       C  
ATOM   2634  O   ARG A1136      -2.409 -11.628  20.027  1.00103.51           O  
ANISOU 2634  O   ARG A1136    11982  15672  11676  -1600   1947  -4595       O  
ATOM   2635  CB  ARG A1136      -4.491 -11.619  22.492  1.00104.87           C  
ANISOU 2635  CB  ARG A1136    11991  16346  11508  -1634   2095  -4878       C  
ATOM   2636  CG  ARG A1136      -5.561 -12.704  22.366  1.00119.11           C  
ANISOU 2636  CG  ARG A1136    13904  18182  13171  -1477   1959  -4458       C  
ATOM   2637  CD  ARG A1136      -5.645 -13.612  23.574  1.00137.65           C  
ANISOU 2637  CD  ARG A1136    16188  21046  15068  -1485   1841  -4443       C  
ATOM   2638  NE  ARG A1136      -4.377 -14.289  23.860  1.00151.86           N  
ANISOU 2638  NE  ARG A1136    17945  23199  16556  -1511   1659  -4433       N  
ATOM   2639  CZ  ARG A1136      -4.261 -15.384  24.604  1.00170.82           C  
ANISOU 2639  CZ  ARG A1136    20324  26022  18556  -1462   1499  -4259       C  
ATOM   2640  NH1 ARG A1136      -5.338 -15.950  25.141  1.00162.96           N  
ANISOU 2640  NH1 ARG A1136    19356  25143  17420  -1398   1505  -4083       N  
ATOM   2641  NH2 ARG A1136      -3.071 -15.932  24.808  1.00157.18           N  
ANISOU 2641  NH2 ARG A1136    18545  24601  16577  -1468   1340  -4241       N  
ATOM   2642  N   TRP A1137      -4.463 -12.197  19.215  1.00 96.08           N  
ANISOU 2642  N   TRP A1137    11215  14401  10892  -1364   1923  -4060       N  
ATOM   2643  CA  TRP A1137      -4.060 -12.991  18.045  1.00 92.56           C  
ANISOU 2643  CA  TRP A1137    10890  13834  10443  -1266   1745  -3701       C  
ATOM   2644  C   TRP A1137      -3.203 -12.153  17.086  1.00 96.36           C  
ANISOU 2644  C   TRP A1137    11393  14008  11211  -1311   1841  -3774       C  
ATOM   2645  O   TRP A1137      -2.247 -12.667  16.502  1.00 94.54           O  
ANISOU 2645  O   TRP A1137    11203  13816  10903  -1313   1706  -3666       O  
ATOM   2646  CB  TRP A1137      -5.312 -13.553  17.353  1.00 89.01           C  
ANISOU 2646  CB  TRP A1137    10544  13212  10064  -1112   1689  -3328       C  
ATOM   2647  CG  TRP A1137      -5.112 -14.097  15.970  1.00 87.65           C  
ANISOU 2647  CG  TRP A1137    10485  12844   9972  -1017   1563  -2995       C  
ATOM   2648  CD1 TRP A1137      -4.382 -15.191  15.614  1.00 88.69           C  
ANISOU 2648  CD1 TRP A1137    10667  13125   9907   -996   1362  -2815       C  
ATOM   2649  CD2 TRP A1137      -5.749 -13.633  14.772  1.00 86.37           C  
ANISOU 2649  CD2 TRP A1137    10389  12330  10097   -919   1631  -2789       C  
ATOM   2650  NE1 TRP A1137      -4.489 -15.413  14.261  1.00 86.44           N  
ANISOU 2650  NE1 TRP A1137    10474  12603   9767   -911   1308  -2546       N  
ATOM   2651  CE2 TRP A1137      -5.322 -14.469  13.719  1.00 88.27           C  
ANISOU 2651  CE2 TRP A1137    10716  12546  10279   -860   1462  -2516       C  
ATOM   2652  CE3 TRP A1137      -6.622 -12.571  14.480  1.00 88.81           C  
ANISOU 2652  CE3 TRP A1137    10682  12352  10711   -868   1825  -2806       C  
ATOM   2653  CZ2 TRP A1137      -5.737 -14.278  12.397  1.00 86.55           C  
ANISOU 2653  CZ2 TRP A1137    10562  12066  10258   -761   1472  -2269       C  
ATOM   2654  CZ3 TRP A1137      -7.028 -12.381  13.169  1.00 89.19           C  
ANISOU 2654  CZ3 TRP A1137    10796  12130  10965   -750   1831  -2527       C  
ATOM   2655  CH2 TRP A1137      -6.591 -13.228  12.147  1.00 87.78           C  
ANISOU 2655  CH2 TRP A1137    10696  11972  10684   -701   1651  -2266       C  
ATOM   2656  N   TYR A1138      -3.541 -10.857  16.956  1.00 94.72           N  
ANISOU 2656  N   TYR A1138    11152  13491  11347  -1349   2094  -3961       N  
ATOM   2657  CA  TYR A1138      -2.818  -9.874  16.156  1.00 95.15           C  
ANISOU 2657  CA  TYR A1138    11214  13215  11724  -1403   2254  -4056       C  
ATOM   2658  C   TYR A1138      -1.548  -9.452  16.910  1.00 99.74           C  
ANISOU 2658  C   TYR A1138    11669  13999  12229  -1595   2312  -4485       C  
ATOM   2659  O   TYR A1138      -0.520  -9.230  16.279  1.00 99.07           O  
ANISOU 2659  O   TYR A1138    11595  13804  12243  -1652   2323  -4519       O  
ATOM   2660  CB  TYR A1138      -3.719  -8.657  15.849  1.00 98.32           C  
ANISOU 2660  CB  TYR A1138    11611  13207  12541  -1360   2530  -4088       C  
ATOM   2661  CG  TYR A1138      -3.035  -7.567  15.052  1.00102.24           C  
ANISOU 2661  CG  TYR A1138    12114  13323  13410  -1409   2741  -4167       C  
ATOM   2662  CD1 TYR A1138      -3.056  -7.582  13.659  1.00101.67           C  
ANISOU 2662  CD1 TYR A1138    12158  12967  13504  -1283   2716  -3793       C  
ATOM   2663  CD2 TYR A1138      -2.367  -6.524  15.684  1.00107.53           C  
ANISOU 2663  CD2 TYR A1138    12664  13925  14266  -1588   2980  -4620       C  
ATOM   2664  CE1 TYR A1138      -2.410  -6.591  12.918  1.00104.01           C  
ANISOU 2664  CE1 TYR A1138    12465  12914  14140  -1325   2927  -3834       C  
ATOM   2665  CE2 TYR A1138      -1.705  -5.538  14.955  1.00110.18           C  
ANISOU 2665  CE2 TYR A1138    13005  13890  14967  -1644   3200  -4691       C  
ATOM   2666  CZ  TYR A1138      -1.733  -5.573  13.570  1.00114.53           C  
ANISOU 2666  CZ  TYR A1138    13687  14151  15679  -1505   3176  -4278       C  
ATOM   2667  OH  TYR A1138      -1.100  -4.587  12.852  1.00116.45           O  
ANISOU 2667  OH  TYR A1138    13938  14021  16287  -1555   3414  -4320       O  
ATOM   2668  N   ASN A1139      -1.626  -9.319  18.252  1.00 97.25           N  
ANISOU 2668  N   ASN A1139    11221  13997  11733  -1701   2357  -4826       N  
ATOM   2669  CA  ASN A1139      -0.489  -8.932  19.092  1.00 98.72           C  
ANISOU 2669  CA  ASN A1139    11250  14458  11802  -1894   2406  -5276       C  
ATOM   2670  C   ASN A1139       0.561 -10.043  19.220  1.00101.05           C  
ANISOU 2670  C   ASN A1139    11529  15151  11713  -1895   2127  -5186       C  
ATOM   2671  O   ASN A1139       1.726  -9.733  19.480  1.00102.57           O  
ANISOU 2671  O   ASN A1139    11607  15503  11863  -2035   2145  -5489       O  
ATOM   2672  CB  ASN A1139      -0.952  -8.444  20.472  1.00100.56           C  
ANISOU 2672  CB  ASN A1139    11328  14942  11937  -2006   2543  -5676       C  
ATOM   2673  CG  ASN A1139      -1.334  -6.975  20.566  1.00120.64           C  
ANISOU 2673  CG  ASN A1139    13798  17124  14915  -2106   2898  -6017       C  
ATOM   2674  OD1 ASN A1139      -1.580  -6.453  21.657  1.00113.59           O  
ANISOU 2674  OD1 ASN A1139    12759  16420  13981  -2229   3045  -6417       O  
ATOM   2675  ND2 ASN A1139      -1.402  -6.267  19.444  1.00112.59           N  
ANISOU 2675  ND2 ASN A1139    12870  15581  14327  -2054   3060  -5870       N  
ATOM   2676  N   GLN A1140       0.162 -11.326  19.021  1.00 94.03           N  
ANISOU 2676  N   GLN A1140    10745  14413  10570  -1740   1882  -4776       N  
ATOM   2677  CA  GLN A1140       1.079 -12.469  19.107  1.00 92.09           C  
ANISOU 2677  CA  GLN A1140    10490  14513   9988  -1709   1625  -4634       C  
ATOM   2678  C   GLN A1140       1.649 -12.860  17.743  1.00 92.34           C  
ANISOU 2678  C   GLN A1140    10643  14284  10156  -1637   1529  -4345       C  
ATOM   2679  O   GLN A1140       2.831 -13.183  17.652  1.00 91.24           O  
ANISOU 2679  O   GLN A1140    10454  14314   9900  -1682   1422  -4405       O  
ATOM   2680  CB  GLN A1140       0.468 -13.680  19.855  1.00 92.59           C  
ANISOU 2680  CB  GLN A1140    10565  14933   9681  -1602   1439  -4400       C  
ATOM   2681  CG  GLN A1140      -0.787 -14.311  19.243  1.00109.08           C  
ANISOU 2681  CG  GLN A1140    12809  16793  11842  -1444   1392  -3989       C  
ATOM   2682  CD  GLN A1140      -1.615 -15.131  20.219  1.00129.67           C  
ANISOU 2682  CD  GLN A1140    15401  19712  14155  -1381   1312  -3867       C  
ATOM   2683  OE1 GLN A1140      -1.329 -15.219  21.422  1.00126.68           O  
ANISOU 2683  OE1 GLN A1140    14896  19745  13491  -1445   1294  -4073       O  
ATOM   2684  NE2 GLN A1140      -2.676 -15.755  19.715  1.00119.37           N  
ANISOU 2684  NE2 GLN A1140    14215  18233  12906  -1256   1270  -3528       N  
ATOM   2685  N   THR A1141       0.825 -12.824  16.690  1.00 87.84           N  
ANISOU 2685  N   THR A1141    10219  13334   9823  -1527   1567  -4042       N  
ATOM   2686  CA  THR A1141       1.250 -13.169  15.329  1.00 86.17           C  
ANISOU 2686  CA  THR A1141    10123  12883   9736  -1458   1490  -3761       C  
ATOM   2687  C   THR A1141       0.789 -12.070  14.356  1.00 91.88           C  
ANISOU 2687  C   THR A1141    10913  13137  10859  -1446   1704  -3719       C  
ATOM   2688  O   THR A1141      -0.113 -12.334  13.557  1.00 90.74           O  
ANISOU 2688  O   THR A1141    10877  12796  10805  -1314   1676  -3394       O  
ATOM   2689  CB  THR A1141       0.724 -14.563  14.918  1.00 89.11           C  
ANISOU 2689  CB  THR A1141    10600  13341   9919  -1307   1270  -3352       C  
ATOM   2690  OG1 THR A1141      -0.692 -14.616  15.112  1.00 86.49           O  
ANISOU 2690  OG1 THR A1141    10310  12937   9616  -1223   1311  -3214       O  
ATOM   2691  CG2 THR A1141       1.416 -15.706  15.654  1.00 87.47           C  
ANISOU 2691  CG2 THR A1141    10334  13544   9356  -1298   1065  -3329       C  
ATOM   2692  N   PRO A1142       1.359 -10.833  14.405  1.00 90.17           N  
ANISOU 2692  N   PRO A1142    10625  12740  10896  -1576   1930  -4034       N  
ATOM   2693  CA  PRO A1142       0.884  -9.770  13.493  1.00 90.28           C  
ANISOU 2693  CA  PRO A1142    10702  12284  11315  -1542   2160  -3950       C  
ATOM   2694  C   PRO A1142       1.040 -10.094  12.012  1.00 90.50           C  
ANISOU 2694  C   PRO A1142    10860  12091  11435  -1437   2087  -3574       C  
ATOM   2695  O   PRO A1142       0.123  -9.837  11.230  1.00 88.51           O  
ANISOU 2695  O   PRO A1142    10691  11576  11364  -1310   2152  -3300       O  
ATOM   2696  CB  PRO A1142       1.693  -8.538  13.918  1.00 95.01           C  
ANISOU 2696  CB  PRO A1142    11183  12770  12146  -1728   2415  -4391       C  
ATOM   2697  CG  PRO A1142       2.883  -9.080  14.611  1.00 99.76           C  
ANISOU 2697  CG  PRO A1142    11679  13773  12453  -1852   2266  -4641       C  
ATOM   2698  CD  PRO A1142       2.435 -10.337  15.286  1.00 93.78           C  
ANISOU 2698  CD  PRO A1142    10927  13412  11294  -1760   2002  -4482       C  
ATOM   2699  N   ASN A1143       2.190 -10.698  11.656  1.00 86.08           N  
ANISOU 2699  N   ASN A1143    10304  11674  10727  -1485   1944  -3564       N  
ATOM   2700  CA  ASN A1143       2.581 -11.136  10.313  1.00 83.71           C  
ANISOU 2700  CA  ASN A1143    10108  11241  10457  -1415   1855  -3259       C  
ATOM   2701  C   ASN A1143       1.456 -11.952   9.635  1.00 84.07           C  
ANISOU 2701  C   ASN A1143    10261  11266  10418  -1238   1710  -2852       C  
ATOM   2702  O   ASN A1143       0.991 -11.596   8.545  1.00 82.90           O  
ANISOU 2702  O   ASN A1143    10189  10859  10451  -1148   1782  -2603       O  
ATOM   2703  CB  ASN A1143       3.916 -11.932  10.369  1.00 82.12           C  
ANISOU 2703  CB  ASN A1143     9865  11304  10032  -1490   1680  -3347       C  
ATOM   2704  CG  ASN A1143       4.307 -12.529  11.724  1.00 88.70           C  
ANISOU 2704  CG  ASN A1143    10581  12551  10568  -1551   1546  -3584       C  
ATOM   2705  OD1 ASN A1143       3.665 -13.445  12.269  1.00 71.76           O  
ANISOU 2705  OD1 ASN A1143     8448  10631   8187  -1464   1386  -3446       O  
ATOM   2706  ND2 ASN A1143       5.396 -12.030  12.287  1.00 79.13           N  
ANISOU 2706  ND2 ASN A1143     9244  11467   9356  -1704   1614  -3941       N  
ATOM   2707  N   ARG A1144       0.982 -12.985  10.325  1.00 78.38           N  
ANISOU 2707  N   ARG A1144     9529  10827   9424  -1190   1525  -2797       N  
ATOM   2708  CA  ARG A1144      -0.094 -13.836   9.834  1.00 75.84           C  
ANISOU 2708  CA  ARG A1144     9282  10537   8998  -1049   1383  -2470       C  
ATOM   2709  C   ARG A1144      -1.462 -13.185   9.962  1.00 79.50           C  
ANISOU 2709  C   ARG A1144     9751  10831   9625   -969   1515  -2401       C  
ATOM   2710  O   ARG A1144      -2.268 -13.281   9.058  1.00 78.34           O  
ANISOU 2710  O   ARG A1144     9665  10557   9544   -851   1487  -2117       O  
ATOM   2711  CB  ARG A1144      -0.105 -15.181  10.569  1.00 75.42           C  
ANISOU 2711  CB  ARG A1144     9203  10827   8626  -1040   1180  -2459       C  
ATOM   2712  CG  ARG A1144       1.270 -15.814  10.841  1.00 82.14           C  
ANISOU 2712  CG  ARG A1144    10122  11719   9369   -919   1031  -2143       C  
ATOM   2713  CD  ARG A1144       1.220 -17.211  11.502  1.00 85.11           C  
ANISOU 2713  CD  ARG A1144    10482  12384   9473   -915    847  -2100       C  
ATOM   2714  NE  ARG A1144      -0.172 -17.714  11.569  1.00 83.23           N  
ANISOU 2714  NE  ARG A1144    10290  12180   9155   -819    749  -1850       N  
ATOM   2715  CZ  ARG A1144      -0.616 -18.856  11.037  1.00 91.22           C  
ANISOU 2715  CZ  ARG A1144    11318  13327  10012   -785    600  -1701       C  
ATOM   2716  NH1 ARG A1144       0.193 -19.672  10.393  1.00 75.18           N  
ANISOU 2716  NH1 ARG A1144     9264  11420   7882   -820    517  -1754       N  
ATOM   2717  NH2 ARG A1144      -1.882 -19.192  11.151  1.00 79.36           N  
ANISOU 2717  NH2 ARG A1144     9848  11829   8475   -716    545  -1503       N  
ATOM   2718  N   ALA A1145      -1.726 -12.529  11.089  1.00 77.13           N  
ANISOU 2718  N   ALA A1145     9372  10553   9382  -1032   1656  -2672       N  
ATOM   2719  CA  ALA A1145      -3.009 -11.868  11.345  1.00 77.61           C  
ANISOU 2719  CA  ALA A1145     9415  10462   9610   -963   1800  -2655       C  
ATOM   2720  C   ALA A1145      -3.396 -10.860  10.273  1.00 81.04           C  
ANISOU 2720  C   ALA A1145     9888  10520  10382   -881   1978  -2495       C  
ATOM   2721  O   ALA A1145      -4.496 -10.975   9.737  1.00 80.25           O  
ANISOU 2721  O   ALA A1145     9819  10338  10335   -741   1957  -2233       O  
ATOM   2722  CB  ALA A1145      -3.020 -11.219  12.717  1.00 80.53           C  
ANISOU 2722  CB  ALA A1145     9679  10930   9990  -1075   1942  -3032       C  
ATOM   2723  N   LYS A1146      -2.490  -9.913   9.926  1.00 77.84           N  
ANISOU 2723  N   LYS A1146     9474   9900  10201   -963   2151  -2633       N  
ATOM   2724  CA  LYS A1146      -2.713  -8.897   8.889  1.00 78.37           C  
ANISOU 2724  CA  LYS A1146     9578   9592  10607   -882   2350  -2456       C  
ATOM   2725  C   LYS A1146      -3.261  -9.544   7.600  1.00 79.19           C  
ANISOU 2725  C   LYS A1146     9767   9688  10635   -717   2195  -2016       C  
ATOM   2726  O   LYS A1146      -4.318  -9.121   7.122  1.00 79.34           O  
ANISOU 2726  O   LYS A1146     9789   9547  10810   -570   2273  -1793       O  
ATOM   2727  CB  LYS A1146      -1.414  -8.129   8.581  1.00 82.47           C  
ANISOU 2727  CB  LYS A1146    10090   9934  11311  -1012   2513  -2632       C  
ATOM   2728  CG  LYS A1146      -0.973  -7.134   9.646  1.00100.09           C  
ANISOU 2728  CG  LYS A1146    12216  12083  13731  -1175   2751  -3082       C  
ATOM   2729  CD  LYS A1146       0.313  -6.420   9.223  1.00111.25           C  
ANISOU 2729  CD  LYS A1146    13617  13310  15344  -1310   2918  -3245       C  
ATOM   2730  CE  LYS A1146       0.903  -5.541  10.301  1.00122.58           C  
ANISOU 2730  CE  LYS A1146    14922  14717  16937  -1510   3142  -3755       C  
ATOM   2731  NZ  LYS A1146       1.728  -6.314  11.266  1.00127.86           N  
ANISOU 2731  NZ  LYS A1146    15506  15823  17250  -1653   2944  -4058       N  
ATOM   2732  N   ARG A1147      -2.566 -10.605   7.088  1.00 72.17           N  
ANISOU 2732  N   ARG A1147     8927   8999   9496   -741   1975  -1909       N  
ATOM   2733  CA  ARG A1147      -2.923 -11.378   5.889  1.00 69.40           C  
ANISOU 2733  CA  ARG A1147     8639   8705   9025   -621   1809  -1553       C  
ATOM   2734  C   ARG A1147      -4.315 -11.997   6.026  1.00 71.86           C  
ANISOU 2734  C   ARG A1147     8936   9142   9227   -500   1695  -1387       C  
ATOM   2735  O   ARG A1147      -5.156 -11.787   5.147  1.00 71.73           O  
ANISOU 2735  O   ARG A1147     8926   9033   9294   -360   1711  -1118       O  
ATOM   2736  CB  ARG A1147      -1.882 -12.478   5.591  1.00 66.65           C  
ANISOU 2736  CB  ARG A1147     8324   8568   8431   -698   1607  -1557       C  
ATOM   2737  CG  ARG A1147      -0.461 -11.973   5.318  1.00 74.85           C  
ANISOU 2737  CG  ARG A1147     9369   9509   9562   -818   1701  -1706       C  
ATOM   2738  CD  ARG A1147       0.468 -13.065   4.803  1.00 70.97           C  
ANISOU 2738  CD  ARG A1147     8906   9207   8851   -862   1504  -1657       C  
ATOM   2739  NE  ARG A1147       0.866 -14.012   5.849  1.00 72.01           N  
ANISOU 2739  NE  ARG A1147     8996   9611   8752   -930   1345  -1840       N  
ATOM   2740  CZ  ARG A1147       2.032 -13.991   6.494  1.00 86.10           C  
ANISOU 2740  CZ  ARG A1147    10728  11498  10486  -1055   1344  -2103       C  
ATOM   2741  NH1 ARG A1147       2.944 -13.068   6.205  1.00 69.10           N  
ANISOU 2741  NH1 ARG A1147     8559   9183   8515  -1148   1505  -2248       N  
ATOM   2742  NH2 ARG A1147       2.296 -14.895   7.428  1.00 75.62           N  
ANISOU 2742  NH2 ARG A1147     9355  10448   8930  -1083   1190  -2213       N  
ATOM   2743  N   VAL A1148      -4.568 -12.734   7.137  1.00 67.23           N  
ANISOU 2743  N   VAL A1148     8317   8777   8450   -551   1589  -1543       N  
ATOM   2744  CA  VAL A1148      -5.864 -13.373   7.418  1.00 66.38           C  
ANISOU 2744  CA  VAL A1148     8188   8798   8237   -460   1495  -1424       C  
ATOM   2745  C   VAL A1148      -6.995 -12.322   7.434  1.00 71.86           C  
ANISOU 2745  C   VAL A1148     8836   9290   9178   -354   1676  -1372       C  
ATOM   2746  O   VAL A1148      -8.002 -12.512   6.753  1.00 71.19           O  
ANISOU 2746  O   VAL A1148     8740   9205   9104   -221   1626  -1125       O  
ATOM   2747  CB  VAL A1148      -5.842 -14.272   8.690  1.00 69.59           C  
ANISOU 2747  CB  VAL A1148     8568   9467   8406   -541   1385  -1600       C  
ATOM   2748  CG1 VAL A1148      -7.219 -14.860   8.992  1.00 69.03           C  
ANISOU 2748  CG1 VAL A1148     8470   9502   8256   -458   1324  -1484       C  
ATOM   2749  CG2 VAL A1148      -4.816 -15.390   8.562  1.00 67.69           C  
ANISOU 2749  CG2 VAL A1148     8364   9415   7941   -607   1204  -1590       C  
ATOM   2750  N   ILE A1149      -6.786 -11.197   8.152  1.00 70.51           N  
ANISOU 2750  N   ILE A1149     8625   8947   9218   -412   1894  -1610       N  
ATOM   2751  CA  ILE A1149      -7.717 -10.064   8.260  1.00 72.78           C  
ANISOU 2751  CA  ILE A1149     8859   8994   9800   -319   2113  -1602       C  
ATOM   2752  C   ILE A1149      -8.030  -9.459   6.873  1.00 81.04           C  
ANISOU 2752  C   ILE A1149     9928   9811  11051   -161   2186  -1269       C  
ATOM   2753  O   ILE A1149      -9.183  -9.105   6.608  1.00 81.59           O  
ANISOU 2753  O   ILE A1149     9953   9798  11251     -6   2243  -1088       O  
ATOM   2754  CB  ILE A1149      -7.189  -9.024   9.298  1.00 77.23           C  
ANISOU 2754  CB  ILE A1149     9369   9417  10557   -451   2349  -1982       C  
ATOM   2755  CG1 ILE A1149      -7.331  -9.571  10.735  1.00 76.70           C  
ANISOU 2755  CG1 ILE A1149     9248   9629  10267   -561   2283  -2268       C  
ATOM   2756  CG2 ILE A1149      -7.858  -7.650   9.163  1.00 80.01           C  
ANISOU 2756  CG2 ILE A1149     9672   9417  11311   -358   2637  -1967       C  
ATOM   2757  CD1 ILE A1149      -6.345  -9.013  11.763  1.00 81.90           C  
ANISOU 2757  CD1 ILE A1149     9847  10322  10948   -749   2414  -2690       C  
ATOM   2758  N   THR A1150      -7.012  -9.390   5.987  1.00 79.98           N  
ANISOU 2758  N   THR A1150     9856   9608  10926   -193   2177  -1174       N  
ATOM   2759  CA  THR A1150      -7.129  -8.870   4.617  1.00 81.86           C  
ANISOU 2759  CA  THR A1150    10119   9671  11312    -51   2241   -838       C  
ATOM   2760  C   THR A1150      -8.041  -9.753   3.759  1.00 86.98           C  
ANISOU 2760  C   THR A1150    10760  10533  11755     93   2026   -518       C  
ATOM   2761  O   THR A1150      -8.923  -9.229   3.077  1.00 88.46           O  
ANISOU 2761  O   THR A1150    10907  10626  12077    271   2092   -251       O  
ATOM   2762  CB  THR A1150      -5.742  -8.668   3.999  1.00 89.59           C  
ANISOU 2762  CB  THR A1150    11162  10560  12317   -150   2285   -856       C  
ATOM   2763  OG1 THR A1150      -4.997  -7.785   4.838  1.00 93.46           O  
ANISOU 2763  OG1 THR A1150    11633  10856  13024   -291   2505  -1187       O  
ATOM   2764  CG2 THR A1150      -5.804  -8.111   2.582  1.00 88.12           C  
ANISOU 2764  CG2 THR A1150    11004  10212  12266     -6   2366   -491       C  
ATOM   2765  N   THR A1151      -7.848 -11.088   3.826  1.00 81.94           N  
ANISOU 2765  N   THR A1151    10145  10187  10801     18   1780   -553       N  
ATOM   2766  CA  THR A1151      -8.649 -12.084   3.103  1.00 80.64           C  
ANISOU 2766  CA  THR A1151     9958  10256  10426    111   1573   -323       C  
ATOM   2767  C   THR A1151     -10.131 -11.994   3.545  1.00 84.65           C  
ANISOU 2767  C   THR A1151    10380  10797  10987    228   1589   -273       C  
ATOM   2768  O   THR A1151     -11.027 -12.245   2.740  1.00 83.93           O  
ANISOU 2768  O   THR A1151    10234  10815  10842    362   1504    -31       O  
ATOM   2769  CB  THR A1151      -7.983 -13.467   3.243  1.00 89.53           C  
ANISOU 2769  CB  THR A1151    11125  11626  11264    -19   1359   -428       C  
ATOM   2770  OG1 THR A1151      -6.664 -13.388   2.690  1.00 90.22           O  
ANISOU 2770  OG1 THR A1151    11276  11661  11342   -102   1368   -449       O  
ATOM   2771  CG2 THR A1151      -8.751 -14.582   2.541  1.00 87.50           C  
ANISOU 2771  CG2 THR A1151    10835  11607  10805     42   1163   -248       C  
ATOM   2772  N   PHE A1152     -10.375 -11.558   4.792  1.00 82.30           N  
ANISOU 2772  N   PHE A1152    10055  10414  10801    177   1711   -511       N  
ATOM   2773  CA  PHE A1152     -11.720 -11.357   5.321  1.00 83.16           C  
ANISOU 2773  CA  PHE A1152    10076  10529  10991    276   1760   -501       C  
ATOM   2774  C   PHE A1152     -12.362 -10.081   4.786  1.00 91.22           C  
ANISOU 2774  C   PHE A1152    11040  11298  12322    454   1957   -316       C  
ATOM   2775  O   PHE A1152     -13.579 -10.062   4.609  1.00 91.86           O  
ANISOU 2775  O   PHE A1152    11032  11432  12437    599   1940   -163       O  
ATOM   2776  CB  PHE A1152     -11.721 -11.324   6.856  1.00 84.71           C  
ANISOU 2776  CB  PHE A1152    10256  10743  11186    151   1835   -835       C  
ATOM   2777  CG  PHE A1152     -11.761 -12.669   7.538  1.00 83.97           C  
ANISOU 2777  CG  PHE A1152    10175  10941  10790     48   1644   -940       C  
ATOM   2778  CD1 PHE A1152     -12.796 -13.565   7.289  1.00 85.93           C  
ANISOU 2778  CD1 PHE A1152    10379  11372  10898    117   1501   -788       C  
ATOM   2779  CD2 PHE A1152     -10.796 -13.019   8.473  1.00 85.34           C  
ANISOU 2779  CD2 PHE A1152    10389  11209  10828   -115   1623  -1191       C  
ATOM   2780  CE1 PHE A1152     -12.838 -14.805   7.929  1.00 85.28           C  
ANISOU 2780  CE1 PHE A1152    10310  11522  10569     22   1358   -869       C  
ATOM   2781  CE2 PHE A1152     -10.842 -14.256   9.117  1.00 86.69           C  
ANISOU 2781  CE2 PHE A1152    10569  11637  10731   -189   1465  -1245       C  
ATOM   2782  CZ  PHE A1152     -11.868 -15.137   8.848  1.00 83.94           C  
ANISOU 2782  CZ  PHE A1152    10192  11428  10274   -121   1345  -1079       C  
ATOM   2783  N   ARG A1153     -11.572  -9.009   4.552  1.00 90.19           N  
ANISOU 2783  N   ARG A1153    10948  10887  12434    447   2158   -328       N  
ATOM   2784  CA  ARG A1153     -12.142  -7.745   4.073  1.00 93.20           C  
ANISOU 2784  CA  ARG A1153    11274  10984  13154    629   2383   -129       C  
ATOM   2785  C   ARG A1153     -12.207  -7.644   2.537  1.00 97.71           C  
ANISOU 2785  C   ARG A1153    11849  11570  13706    798   2330    287       C  
ATOM   2786  O   ARG A1153     -13.234  -7.201   2.015  1.00 98.95           O  
ANISOU 2786  O   ARG A1153    11919  11697  13981   1010   2373    556       O  
ATOM   2787  CB  ARG A1153     -11.468  -6.504   4.706  1.00 96.23           C  
ANISOU 2787  CB  ARG A1153    11672  11011  13882    549   2689   -362       C  
ATOM   2788  CG  ARG A1153     -10.002  -6.228   4.342  1.00107.73           C  
ANISOU 2788  CG  ARG A1153    13219  12338  15377    416   2761   -433       C  
ATOM   2789  CD  ARG A1153      -9.842  -5.050   3.388  1.00123.36           C  
ANISOU 2789  CD  ARG A1153    15205  13978  17688    553   3001   -165       C  
ATOM   2790  NE  ARG A1153     -10.468  -3.819   3.883  1.00140.65           N  
ANISOU 2790  NE  ARG A1153    17321  15827  20293    644   3309   -218       N  
ATOM   2791  CZ  ARG A1153      -9.862  -2.917   4.650  1.00159.75           C  
ANISOU 2791  CZ  ARG A1153    19733  17954  23013    508   3586   -542       C  
ATOM   2792  NH1 ARG A1153      -8.601  -3.094   5.027  1.00148.88           N  
ANISOU 2792  NH1 ARG A1153    18412  16609  21548    275   3581   -843       N  
ATOM   2793  NH2 ARG A1153     -10.513  -1.832   5.049  1.00148.63           N  
ANISOU 2793  NH2 ARG A1153    18245  16224  22002    600   3877   -586       N  
ATOM   2794  N   THR A1154     -11.142  -8.060   1.824  1.00 93.04           N  
ANISOU 2794  N   THR A1154    11343  11052  12955    711   2235    342       N  
ATOM   2795  CA  THR A1154     -11.084  -7.989   0.360  1.00 93.62           C  
ANISOU 2795  CA  THR A1154    11421  11180  12972    850   2187    720       C  
ATOM   2796  C   THR A1154     -11.877  -9.092  -0.341  1.00 96.50           C  
ANISOU 2796  C   THR A1154    11724  11926  13016    930   1912    907       C  
ATOM   2797  O   THR A1154     -12.594  -8.810  -1.302  1.00 97.94           O  
ANISOU 2797  O   THR A1154    11829  12181  13202   1130   1899   1242       O  
ATOM   2798  CB  THR A1154      -9.631  -7.940  -0.163  1.00100.56           C  
ANISOU 2798  CB  THR A1154    12406  11984  13819    721   2218    695       C  
ATOM   2799  OG1 THR A1154      -8.869  -9.022   0.379  1.00 95.93           O  
ANISOU 2799  OG1 THR A1154    11876  11595  12980    510   2038    411       O  
ATOM   2800  CG2 THR A1154      -8.945  -6.605   0.101  1.00102.06           C  
ANISOU 2800  CG2 THR A1154    12631  11763  14384    692   2539    616       C  
ATOM   2801  N   GLY A1155     -11.722 -10.328   0.127  1.00 90.51           N  
ANISOU 2801  N   GLY A1155    10987  11412  11990    774   1706    694       N  
ATOM   2802  CA  GLY A1155     -12.328 -11.505  -0.486  1.00 89.09           C  
ANISOU 2802  CA  GLY A1155    10750  11589  11513    798   1457    800       C  
ATOM   2803  C   GLY A1155     -11.446 -12.035  -1.605  1.00 92.78           C  
ANISOU 2803  C   GLY A1155    11268  12201  11782    747   1341    915       C  
ATOM   2804  O   GLY A1155     -11.887 -12.859  -2.410  1.00 91.64           O  
ANISOU 2804  O   GLY A1155    11061  12350  11408    781   1161   1038       O  
ATOM   2805  N   THR A1156     -10.181 -11.550  -1.655  1.00 90.24           N  
ANISOU 2805  N   THR A1156    11051  11682  11555    653   1456    851       N  
ATOM   2806  CA  THR A1156      -9.163 -11.906  -2.646  1.00 89.93           C  
ANISOU 2806  CA  THR A1156    11071  11734  11365    587   1388    931       C  
ATOM   2807  C   THR A1156      -7.959 -12.585  -1.991  1.00 92.92           C  
ANISOU 2807  C   THR A1156    11541  12107  11658    365   1333    623       C  
ATOM   2808  O   THR A1156      -7.716 -12.416  -0.794  1.00 91.71           O  
ANISOU 2808  O   THR A1156    11415  11818  11613    270   1406    370       O  
ATOM   2809  CB  THR A1156      -8.703 -10.666  -3.441  1.00100.98           C  
ANISOU 2809  CB  THR A1156    12500  12905  12964    690   1594   1174       C  
ATOM   2810  OG1 THR A1156      -8.037  -9.753  -2.568  1.00102.18           O  
ANISOU 2810  OG1 THR A1156    12715  12709  13402    610   1819    982       O  
ATOM   2811  CG2 THR A1156      -9.840  -9.968  -4.185  1.00102.24           C  
ANISOU 2811  CG2 THR A1156    12558  13085  13203    944   1652   1538       C  
ATOM   2812  N   TRP A1157      -7.185 -13.318  -2.800  1.00 90.08           N  
ANISOU 2812  N   TRP A1157    11214  11908  11103    287   1213    648       N  
ATOM   2813  CA  TRP A1157      -5.980 -14.036  -2.383  1.00 88.74           C  
ANISOU 2813  CA  TRP A1157    11116  11762  10839     98   1146    399       C  
ATOM   2814  C   TRP A1157      -4.713 -13.175  -2.502  1.00 95.70           C  
ANISOU 2814  C   TRP A1157    12070  12414  11878     25   1316    349       C  
ATOM   2815  O   TRP A1157      -3.611 -13.661  -2.218  1.00 93.66           O  
ANISOU 2815  O   TRP A1157    11858  12174  11555   -125   1273    147       O  
ATOM   2816  CB  TRP A1157      -5.813 -15.279  -3.247  1.00 85.80           C  
ANISOU 2816  CB  TRP A1157    10727  11672  10202     51    947    439       C  
ATOM   2817  CG  TRP A1157      -6.878 -16.312  -3.065  1.00 85.48           C  
ANISOU 2817  CG  TRP A1157    10611  11858  10009     72    786    419       C  
ATOM   2818  CD1 TRP A1157      -7.868 -16.626  -3.945  1.00 88.83           C  
ANISOU 2818  CD1 TRP A1157    10941  12499  10311    174    695    601       C  
ATOM   2819  CD2 TRP A1157      -6.984 -17.250  -1.988  1.00 83.51           C  
ANISOU 2819  CD2 TRP A1157    10365  11664   9700    -25    698    199       C  
ATOM   2820  NE1 TRP A1157      -8.574 -17.715  -3.493  1.00 87.14           N  
ANISOU 2820  NE1 TRP A1157    10671  12453   9985    130    564    482       N  
ATOM   2821  CE2 TRP A1157      -8.057 -18.114  -2.288  1.00 87.18           C  
ANISOU 2821  CE2 TRP A1157    10743  12349  10033     13    571    253       C  
ATOM   2822  CE3 TRP A1157      -6.260 -17.458  -0.801  1.00 83.76           C  
ANISOU 2822  CE3 TRP A1157    10455  11601   9767   -140    718    -34       C  
ATOM   2823  CZ2 TRP A1157      -8.449 -19.151  -1.432  1.00 85.38           C  
ANISOU 2823  CZ2 TRP A1157    10497  12205   9737    -59    487     97       C  
ATOM   2824  CZ3 TRP A1157      -6.651 -18.483   0.047  1.00 84.03           C  
ANISOU 2824  CZ3 TRP A1157    10470  11749   9708   -194    620   -162       C  
ATOM   2825  CH2 TRP A1157      -7.729 -19.319  -0.271  1.00 84.50           C  
ANISOU 2825  CH2 TRP A1157    10457  11986   9665   -155    516    -90       C  
ATOM   2826  N   ASP A1158      -4.882 -11.902  -2.917  1.00 96.58           N  
ANISOU 2826  N   ASP A1158    12181  12304  12211    137   1519    537       N  
ATOM   2827  CA  ASP A1158      -3.842 -10.887  -3.129  1.00 98.48           C  
ANISOU 2827  CA  ASP A1158    12479  12278  12660     87   1736    531       C  
ATOM   2828  C   ASP A1158      -2.850 -10.745  -1.966  1.00101.38           C  
ANISOU 2828  C   ASP A1158    12882  12500  13139    -98   1815    158       C  
ATOM   2829  O   ASP A1158      -1.672 -10.469  -2.191  1.00100.96           O  
ANISOU 2829  O   ASP A1158    12871  12345  13144   -209   1904     69       O  
ATOM   2830  CB  ASP A1158      -4.491  -9.530  -3.473  1.00103.73           C  
ANISOU 2830  CB  ASP A1158    13121  12690  13603    262   1970    790       C  
ATOM   2831  CG  ASP A1158      -5.271  -9.512  -4.788  1.00119.07           C  
ANISOU 2831  CG  ASP A1158    15016  14796  15428    459   1913   1205       C  
ATOM   2832  OD1 ASP A1158      -5.793 -10.582  -5.194  1.00118.27           O  
ANISOU 2832  OD1 ASP A1158    14868  15033  15037    480   1673   1253       O  
ATOM   2833  OD2 ASP A1158      -5.362  -8.433  -5.408  1.00129.89           O  
ANISOU 2833  OD2 ASP A1158    16385  15969  16999    594   2117   1479       O  
ATOM   2834  N   ALA A1159      -3.341 -10.950  -0.721  1.00 96.89           N  
ANISOU 2834  N   ALA A1159    12281  11952  12581   -133   1781    -66       N  
ATOM   2835  CA  ALA A1159      -2.562 -10.903   0.523  1.00 95.84           C  
ANISOU 2835  CA  ALA A1159    12151  11764  12499   -300   1827   -437       C  
ATOM   2836  C   ALA A1159      -1.517 -12.016   0.582  1.00 96.50           C  
ANISOU 2836  C   ALA A1159    12259  12063  12345   -439   1642   -593       C  
ATOM   2837  O   ALA A1159      -0.547 -11.905   1.323  1.00 95.56           O  
ANISOU 2837  O   ALA A1159    12136  11915  12257   -579   1687   -869       O  
ATOM   2838  CB  ALA A1159      -3.485 -11.015   1.727  1.00 96.38           C  
ANISOU 2838  CB  ALA A1159    12170  11879  12570   -283   1806   -589       C  
ATOM   2839  N   TYR A1160      -1.734 -13.104  -0.187  1.00 91.54           N  
ANISOU 2839  N   TYR A1160    11638  11660  11482   -398   1438   -428       N  
ATOM   2840  CA  TYR A1160      -0.857 -14.271  -0.253  1.00 89.92           C  
ANISOU 2840  CA  TYR A1160    11447  11653  11064   -504   1261   -539       C  
ATOM   2841  C   TYR A1160      -0.198 -14.400  -1.637  1.00 97.49           C  
ANISOU 2841  C   TYR A1160    12435  12641  11964   -508   1246   -375       C  
ATOM   2842  O   TYR A1160       0.329 -15.467  -1.977  1.00 95.56           O  
ANISOU 2842  O   TYR A1160    12194  12576  11539   -567   1092   -412       O  
ATOM   2843  CB  TYR A1160      -1.642 -15.551   0.100  1.00 88.59           C  
ANISOU 2843  CB  TYR A1160    11253  11719  10690   -477   1055   -532       C  
ATOM   2844  CG  TYR A1160      -2.133 -15.570   1.532  1.00 89.33           C  
ANISOU 2844  CG  TYR A1160    11318  11824  10800   -494   1061   -710       C  
ATOM   2845  CD1 TYR A1160      -3.332 -14.951   1.891  1.00 92.21           C  
ANISOU 2845  CD1 TYR A1160    11652  12110  11274   -398   1144   -646       C  
ATOM   2846  CD2 TYR A1160      -1.402 -16.204   2.532  1.00 89.00           C  
ANISOU 2846  CD2 TYR A1160    11269  11891  10655   -599    987   -936       C  
ATOM   2847  CE1 TYR A1160      -3.779 -14.943   3.212  1.00 92.77           C  
ANISOU 2847  CE1 TYR A1160    11692  12206  11352   -423   1164   -823       C  
ATOM   2848  CE2 TYR A1160      -1.846 -16.211   3.855  1.00 90.09           C  
ANISOU 2848  CE2 TYR A1160    11374  12079  10777   -616    997  -1091       C  
ATOM   2849  CZ  TYR A1160      -3.041 -15.590   4.185  1.00 98.21           C  
ANISOU 2849  CZ  TYR A1160    12378  13026  11912   -535   1087  -1043       C  
ATOM   2850  OH  TYR A1160      -3.488 -15.601   5.477  1.00 98.92           O  
ANISOU 2850  OH  TYR A1160    12430  13182  11973   -558   1106  -1205       O  
ATOM   2851  N   ALA A 235      -0.225 -13.314  -2.434  1.00144.33           N  
ANISOU 2851  N   ALA A 235    19299  22993  12547   3833   5917   7683       N  
ATOM   2852  CA  ALA A 235       0.353 -13.291  -3.766  1.00138.16           C  
ANISOU 2852  CA  ALA A 235    18163  21933  12398   3313   5361   7307       C  
ATOM   2853  C   ALA A 235       1.888 -13.246  -3.727  1.00142.54           C  
ANISOU 2853  C   ALA A 235    19089  22407  12664   2907   4667   6880       C  
ATOM   2854  O   ALA A 235       2.478 -12.257  -3.272  1.00144.16           O  
ANISOU 2854  O   ALA A 235    20051  22563  12162   2936   4470   6443       O  
ATOM   2855  CB  ALA A 235      -0.219 -12.136  -4.571  1.00137.39           C  
ANISOU 2855  CB  ALA A 235    18158  21640  12404   3464   5505   6971       C  
ATOM   2856  N   ARG A 236       2.533 -14.328  -4.244  1.00137.86           N  
ANISOU 2856  N   ARG A 236    17961  21790  12629   2518   4289   7041       N  
ATOM   2857  CA  ARG A 236       3.995 -14.458  -4.311  1.00136.77           C  
ANISOU 2857  CA  ARG A 236    17958  21664  12345   2163   3658   6797       C  
ATOM   2858  C   ARG A 236       4.553 -13.884  -5.603  1.00136.20           C  
ANISOU 2858  C   ARG A 236    17749  21347  12653   1819   3247   6333       C  
ATOM   2859  O   ARG A 236       4.026 -14.160  -6.682  1.00131.76           O  
ANISOU 2859  O   ARG A 236    16702  20586  12775   1729   3326   6355       O  
ATOM   2860  CB  ARG A 236       4.485 -15.913  -4.052  1.00138.78           C  
ANISOU 2860  CB  ARG A 236    17806  22039  12884   2066   3539   7274       C  
ATOM   2861  CG  ARG A 236       3.831 -16.991  -4.924  1.00149.90           C  
ANISOU 2861  CG  ARG A 236    18552  23227  15177   1961   3710   7607       C  
ATOM   2862  CD  ARG A 236       4.503 -18.338  -4.752  1.00164.09           C  
ANISOU 2862  CD  ARG A 236    20110  25025  17212   1873   3544   8001       C  
ATOM   2863  NE  ARG A 236       4.024 -19.327  -5.719  1.00173.22           N  
ANISOU 2863  NE  ARG A 236    20795  25839  19181   1688   3603   8217       N  
ATOM   2864  CZ  ARG A 236       4.675 -20.442  -6.037  1.00187.13           C  
ANISOU 2864  CZ  ARG A 236    22398  27412  21291   1585   3412   8427       C  
ATOM   2865  NH1 ARG A 236       5.852 -20.716  -5.483  1.00173.35           N  
ANISOU 2865  NH1 ARG A 236    20800  25866  19199   1685   3163   8511       N  
ATOM   2866  NH2 ARG A 236       4.163 -21.285  -6.924  1.00173.60           N  
ANISOU 2866  NH2 ARG A 236    20411  25299  20251   1387   3455   8573       N  
ATOM   2867  N   MET A 237       5.641 -13.086  -5.474  1.00134.18           N  
ANISOU 2867  N   MET A 237    17935  21125  11922   1588   2776   5946       N  
ATOM   2868  CA  MET A 237       6.372 -12.394  -6.541  1.00130.85           C  
ANISOU 2868  CA  MET A 237    17470  20529  11719   1232   2344   5526       C  
ATOM   2869  C   MET A 237       5.534 -11.348  -7.298  1.00133.22           C  
ANISOU 2869  C   MET A 237    17924  20532  12163   1327   2578   5188       C  
ATOM   2870  O   MET A 237       5.874 -11.031  -8.439  1.00128.71           O  
ANISOU 2870  O   MET A 237    17122  19787  11995   1075   2331   4947       O  
ATOM   2871  CB  MET A 237       7.016 -13.412  -7.531  1.00128.70           C  
ANISOU 2871  CB  MET A 237    16512  20239  12148   1007   2087   5698       C  
ATOM   2872  CG  MET A 237       8.344 -13.944  -7.077  1.00134.44           C  
ANISOU 2872  CG  MET A 237    17161  21257  12663    835   1657   5887       C  
ATOM   2873  SD  MET A 237       9.123 -14.856  -8.428  1.00134.15           S  
ANISOU 2873  SD  MET A 237    16452  21129  13390    692   1435   6011       S  
ATOM   2874  CE  MET A 237      10.832 -14.802  -7.916  1.00133.95           C  
ANISOU 2874  CE  MET A 237    16394  21559  12943    470    860   6162       C  
ATOM   2875  N   ARG A 238       4.507 -10.770  -6.646  1.00134.01           N  
ANISOU 2875  N   ARG A 238    18442  20593  11881   1732   3065   5194       N  
ATOM   2876  CA  ARG A 238       3.553  -9.803  -7.206  1.00134.05           C  
ANISOU 2876  CA  ARG A 238    18603  20358  11973   1981   3410   4989       C  
ATOM   2877  C   ARG A 238       4.168  -8.703  -8.113  1.00136.16           C  
ANISOU 2877  C   ARG A 238    19144  20336  12256   1674   3026   4477       C  
ATOM   2878  O   ARG A 238       3.627  -8.445  -9.193  1.00132.39           O  
ANISOU 2878  O   ARG A 238    18325  19691  12287   1700   3136   4414       O  
ATOM   2879  CB  ARG A 238       2.662  -9.158  -6.115  1.00140.81           C  
ANISOU 2879  CB  ARG A 238    20109  21237  12156   2545   3974   5047       C  
ATOM   2880  CG  ARG A 238       3.360  -8.336  -5.025  1.00156.55           C  
ANISOU 2880  CG  ARG A 238    23153  23173  13156   2547   3779   4710       C  
ATOM   2881  CD  ARG A 238       2.326  -7.569  -4.209  1.00173.07           C  
ANISOU 2881  CD  ARG A 238    25967  25178  14615   3227   4448   4717       C  
ATOM   2882  NE  ARG A 238       2.727  -6.186  -3.927  1.00185.72           N  
ANISOU 2882  NE  ARG A 238    28713  26398  15452   3217   4283   4152       N  
ATOM   2883  CZ  ARG A 238       2.500  -5.148  -4.730  1.00195.98           C  
ANISOU 2883  CZ  ARG A 238    30289  27306  16869   3258   4324   3810       C  
ATOM   2884  NH1 ARG A 238       1.896  -5.322  -5.900  1.00176.28           N  
ANISOU 2884  NH1 ARG A 238    26952  24807  15218   3308   4495   3975       N  
ATOM   2885  NH2 ARG A 238       2.891  -3.930  -4.377  1.00185.05           N  
ANISOU 2885  NH2 ARG A 238    30072  25503  14735   3218   4160   3307       N  
ATOM   2886  N   LEU A 239       5.280  -8.077  -7.690  1.00135.07           N  
ANISOU 2886  N   LEU A 239    19594  20159  11569   1346   2553   4161       N  
ATOM   2887  CA  LEU A 239       5.933  -7.009  -8.452  1.00133.59           C  
ANISOU 2887  CA  LEU A 239    19707  19696  11355    981   2161   3728       C  
ATOM   2888  C   LEU A 239       6.730  -7.532  -9.642  1.00131.62           C  
ANISOU 2888  C   LEU A 239    18712  19519  11779    559   1752   3769       C  
ATOM   2889  O   LEU A 239       6.847  -6.834 -10.651  1.00128.49           O  
ANISOU 2889  O   LEU A 239    18289  18892  11639    386   1624   3524       O  
ATOM   2890  CB  LEU A 239       6.781  -6.111  -7.546  1.00139.27           C  
ANISOU 2890  CB  LEU A 239    21368  20332  11218    699   1766   3416       C  
ATOM   2891  CG  LEU A 239       6.000  -5.302  -6.498  1.00150.67           C  
ANISOU 2891  CG  LEU A 239    23826  21554  11868   1166   2194   3247       C  
ATOM   2892  CD1 LEU A 239       6.900  -4.867  -5.359  1.00157.27           C  
ANISOU 2892  CD1 LEU A 239    25557  22410  11789    837   1731   3043       C  
ATOM   2893  CD2 LEU A 239       5.290  -4.101  -7.128  1.00153.46           C  
ANISOU 2893  CD2 LEU A 239    24655  21429  12225   1426   2507   2930       C  
ATOM   2894  N   ASP A 240       7.269  -8.761  -9.529  1.00126.68           N  
ANISOU 2894  N   ASP A 240    17521  19197  11415    451   1591   4102       N  
ATOM   2895  CA  ASP A 240       7.997  -9.433 -10.608  1.00121.73           C  
ANISOU 2895  CA  ASP A 240    16213  18644  11395    189   1305   4206       C  
ATOM   2896  C   ASP A 240       6.986  -9.990 -11.617  1.00121.00           C  
ANISOU 2896  C   ASP A 240    15611  18383  11980    410   1659   4309       C  
ATOM   2897  O   ASP A 240       7.279 -10.037 -12.810  1.00116.43           O  
ANISOU 2897  O   ASP A 240    14689  17700  11850    247   1504   4220       O  
ATOM   2898  CB  ASP A 240       8.879 -10.561 -10.045  1.00124.70           C  
ANISOU 2898  CB  ASP A 240    16261  19369  11750    106   1075   4568       C  
ATOM   2899  CG  ASP A 240      10.377 -10.323 -10.164  1.00134.85           C  
ANISOU 2899  CG  ASP A 240    17462  20889  12887   -317    497   4564       C  
ATOM   2900  OD1 ASP A 240      10.819  -9.172  -9.955  1.00137.61           O  
ANISOU 2900  OD1 ASP A 240    18297  21192  12796   -634    189   4283       O  
ATOM   2901  OD2 ASP A 240      11.109 -11.291 -10.428  1.00139.29           O  
ANISOU 2901  OD2 ASP A 240    17489  21683  13752   -330    356   4883       O  
ATOM   2902  N   VAL A 241       5.784 -10.391 -11.128  1.00119.18           N  
ANISOU 2902  N   VAL A 241    15340  18152  11792    763   2124   4531       N  
ATOM   2903  CA  VAL A 241       4.667 -10.918 -11.926  1.00116.40           C  
ANISOU 2903  CA  VAL A 241    14504  17689  12033    913   2434   4712       C  
ATOM   2904  C   VAL A 241       3.983  -9.759 -12.675  1.00118.46           C  
ANISOU 2904  C   VAL A 241    14908  17745  12356   1011   2574   4445       C  
ATOM   2905  O   VAL A 241       3.661  -9.926 -13.853  1.00114.53           O  
ANISOU 2905  O   VAL A 241    14009  17133  12374    915   2528   4432       O  
ATOM   2906  CB  VAL A 241       3.670 -11.810 -11.111  1.00123.17           C  
ANISOU 2906  CB  VAL A 241    15164  18690  12945   1188   2853   5167       C  
ATOM   2907  CG1 VAL A 241       2.492 -12.272 -11.972  1.00121.79           C  
ANISOU 2907  CG1 VAL A 241    14460  18428  13389   1222   3087   5397       C  
ATOM   2908  CG2 VAL A 241       4.374 -13.022 -10.496  1.00123.61           C  
ANISOU 2908  CG2 VAL A 241    15070  18899  12998   1096   2708   5463       C  
ATOM   2909  N   GLU A 242       3.811  -8.576 -12.020  1.00118.13           N  
ANISOU 2909  N   GLU A 242    15508  17625  11751   1208   2724   4226       N  
ATOM   2910  CA  GLU A 242       3.220  -7.398 -12.677  1.00117.96           C  
ANISOU 2910  CA  GLU A 242    15720  17365  11736   1369   2886   3988       C  
ATOM   2911  C   GLU A 242       4.134  -6.858 -13.802  1.00117.90           C  
ANISOU 2911  C   GLU A 242    15699  17172  11925    969   2438   3659       C  
ATOM   2912  O   GLU A 242       3.649  -6.182 -14.712  1.00116.39           O  
ANISOU 2912  O   GLU A 242    15468  16798  11955   1048   2525   3540       O  
ATOM   2913  CB  GLU A 242       2.789  -6.301 -11.671  1.00124.98           C  
ANISOU 2913  CB  GLU A 242    17435  18127  11926   1759   3220   3843       C  
ATOM   2914  CG  GLU A 242       3.877  -5.344 -11.184  1.00140.59           C  
ANISOU 2914  CG  GLU A 242    20257  19894  13267   1479   2843   3419       C  
ATOM   2915  CD  GLU A 242       4.260  -4.196 -12.107  1.00166.47           C  
ANISOU 2915  CD  GLU A 242    23849  22819  16583   1249   2603   3047       C  
ATOM   2916  OE1 GLU A 242       3.353  -3.590 -12.722  1.00164.10           O  
ANISOU 2916  OE1 GLU A 242    23552  22329  16471   1596   2951   3034       O  
ATOM   2917  OE2 GLU A 242       5.473  -3.898 -12.211  1.00161.26           O  
ANISOU 2917  OE2 GLU A 242    23401  22100  15769    717   2064   2823       O  
ATOM   2918  N   LEU A 243       5.453  -7.152 -13.723  1.00112.62           N  
ANISOU 2918  N   LEU A 243    15029  16597  11166    565   1979   3579       N  
ATOM   2919  CA  LEU A 243       6.438  -6.769 -14.732  1.00109.29           C  
ANISOU 2919  CA  LEU A 243    14498  16094  10934    179   1569   3378       C  
ATOM   2920  C   LEU A 243       6.172  -7.581 -16.003  1.00106.77           C  
ANISOU 2920  C   LEU A 243    13503  15785  11282    178   1591   3512       C  
ATOM   2921  O   LEU A 243       6.338  -7.055 -17.104  1.00103.96           O  
ANISOU 2921  O   LEU A 243    13065  15288  11148     54   1470   3349       O  
ATOM   2922  CB  LEU A 243       7.869  -7.034 -14.226  1.00110.78           C  
ANISOU 2922  CB  LEU A 243    14715  16507  10871   -201   1114   3414       C  
ATOM   2923  CG  LEU A 243       8.886  -5.899 -14.404  1.00117.27           C  
ANISOU 2923  CG  LEU A 243    15923  17234  11402   -635    694   3162       C  
ATOM   2924  CD1 LEU A 243      10.020  -6.028 -13.411  1.00121.16           C  
ANISOU 2924  CD1 LEU A 243    16578  18011  11447   -978    275   3265       C  
ATOM   2925  CD2 LEU A 243       9.431  -5.837 -15.832  1.00115.86           C  
ANISOU 2925  CD2 LEU A 243    15282  17035  11706   -849    513   3147       C  
ATOM   2926  N   ALA A 244       5.740  -8.857 -15.844  1.00101.46           N  
ANISOU 2926  N   ALA A 244    12415  15243  10892    303   1738   3812       N  
ATOM   2927  CA  ALA A 244       5.406  -9.743 -16.961  1.00 97.89           C  
ANISOU 2927  CA  ALA A 244    11454  14731  11007    271   1735   3933       C  
ATOM   2928  C   ALA A 244       4.100  -9.295 -17.620  1.00101.45           C  
ANISOU 2928  C   ALA A 244    11790  15061  11697    434   1977   3932       C  
ATOM   2929  O   ALA A 244       3.953  -9.448 -18.833  1.00 98.44           O  
ANISOU 2929  O   ALA A 244    11148  14576  11677    330   1863   3882       O  
ATOM   2930  CB  ALA A 244       5.298 -11.183 -16.487  1.00 99.24           C  
ANISOU 2930  CB  ALA A 244    11350  14997  11360    312   1806   4265       C  
ATOM   2931  N   LYS A 245       3.170  -8.710 -16.818  1.00101.18           N  
ANISOU 2931  N   LYS A 245    11964  15065  11415    728   2320   4016       N  
ATOM   2932  CA  LYS A 245       1.884  -8.166 -17.274  1.00101.99           C  
ANISOU 2932  CA  LYS A 245    11926  15139  11687    983   2611   4117       C  
ATOM   2933  C   LYS A 245       2.127  -6.965 -18.189  1.00104.63           C  
ANISOU 2933  C   LYS A 245    12498  15273  11983    956   2489   3797       C  
ATOM   2934  O   LYS A 245       1.511  -6.876 -19.254  1.00103.27           O  
ANISOU 2934  O   LYS A 245    12005  15073  12158    965   2482   3851       O  
ATOM   2935  CB  LYS A 245       1.010  -7.735 -16.082  1.00109.24           C  
ANISOU 2935  CB  LYS A 245    13093  16167  12245   1419   3080   4312       C  
ATOM   2936  CG  LYS A 245       0.234  -8.859 -15.418  1.00124.91           C  
ANISOU 2936  CG  LYS A 245    14661  18394  14404   1523   3331   4788       C  
ATOM   2937  CD  LYS A 245      -0.691  -8.308 -14.342  1.00139.03           C  
ANISOU 2937  CD  LYS A 245    16683  20330  15812   2054   3882   5026       C  
ATOM   2938  CE  LYS A 245      -1.448  -9.397 -13.629  1.00152.45           C  
ANISOU 2938  CE  LYS A 245    17938  22313  17674   2148   4164   5574       C  
ATOM   2939  NZ  LYS A 245      -2.374  -8.842 -12.607  1.00166.76           N  
ANISOU 2939  NZ  LYS A 245    19954  24319  19090   2755   4782   5869       N  
ATOM   2940  N   THR A 246       3.044  -6.055 -17.772  1.00101.74           N  
ANISOU 2940  N   THR A 246    12711  14765  11182    873   2354   3491       N  
ATOM   2941  CA  THR A 246       3.452  -4.851 -18.506  1.00100.85           C  
ANISOU 2941  CA  THR A 246    12935  14408  10976    779   2211   3193       C  
ATOM   2942  C   THR A 246       3.857  -5.253 -19.919  1.00 99.04           C  
ANISOU 2942  C   THR A 246    12245  14187  11198    509   1928   3167       C  
ATOM   2943  O   THR A 246       3.269  -4.765 -20.886  1.00 97.47           O  
ANISOU 2943  O   THR A 246    11927  13896  11210    612   1990   3154       O  
ATOM   2944  CB  THR A 246       4.595  -4.119 -17.757  1.00114.91           C  
ANISOU 2944  CB  THR A 246    15362  16059  12239    530   1969   2927       C  
ATOM   2945  OG1 THR A 246       4.332  -4.109 -16.353  1.00120.50           O  
ANISOU 2945  OG1 THR A 246    16497  16808  12481    749   2182   2970       O  
ATOM   2946  CG2 THR A 246       4.811  -2.692 -18.254  1.00115.44           C  
ANISOU 2946  CG2 THR A 246    15960  15784  12120    462   1901   2649       C  
ATOM   2947  N   LEU A 247       4.805  -6.210 -20.014  1.00 92.90           N  
ANISOU 2947  N   LEU A 247    11214  13539  10545    230   1655   3202       N  
ATOM   2948  CA  LEU A 247       5.343  -6.774 -21.249  1.00 89.27           C  
ANISOU 2948  CA  LEU A 247    10394  13090  10433     34   1423   3192       C  
ATOM   2949  C   LEU A 247       4.247  -7.312 -22.174  1.00 90.79           C  
ANISOU 2949  C   LEU A 247    10221  13258  11019    142   1518   3317       C  
ATOM   2950  O   LEU A 247       4.312  -7.063 -23.370  1.00 88.70           O  
ANISOU 2950  O   LEU A 247     9864  12914  10922     74   1396   3222       O  
ATOM   2951  CB  LEU A 247       6.388  -7.864 -20.927  1.00 88.81           C  
ANISOU 2951  CB  LEU A 247    10159  13191  10395   -123   1238   3304       C  
ATOM   2952  CG  LEU A 247       7.027  -8.599 -22.109  1.00 91.28           C  
ANISOU 2952  CG  LEU A 247    10180  13502  11001   -214   1074   3324       C  
ATOM   2953  CD1 LEU A 247       8.176  -7.802 -22.706  1.00 91.35           C  
ANISOU 2953  CD1 LEU A 247    10254  13553  10904   -394    873   3209       C  
ATOM   2954  CD2 LEU A 247       7.494  -9.974 -21.699  1.00 93.59           C  
ANISOU 2954  CD2 LEU A 247    10291  13890  11378   -182   1052   3533       C  
ATOM   2955  N   GLY A 248       3.256  -8.009 -21.613  1.00 87.96           N  
ANISOU 2955  N   GLY A 248     9657  12986  10776    276   1712   3563       N  
ATOM   2956  CA  GLY A 248       2.137  -8.571 -22.365  1.00 87.68           C  
ANISOU 2956  CA  GLY A 248     9235  12971  11108    277   1739   3762       C  
ATOM   2957  C   GLY A 248       1.412  -7.551 -23.211  1.00 91.17           C  
ANISOU 2957  C   GLY A 248     9640  13389  11611    408   1792   3727       C  
ATOM   2958  O   GLY A 248       1.137  -7.803 -24.388  1.00 89.61           O  
ANISOU 2958  O   GLY A 248     9222  13164  11663    271   1601   3731       O  
ATOM   2959  N   LEU A 249       1.142  -6.376 -22.611  1.00 89.19           N  
ANISOU 2959  N   LEU A 249     9684  13121  11083    695   2049   3687       N  
ATOM   2960  CA  LEU A 249       0.502  -5.233 -23.260  1.00 89.84           C  
ANISOU 2960  CA  LEU A 249     9830  13146  11159    928   2173   3678       C  
ATOM   2961  C   LEU A 249       1.424  -4.646 -24.332  1.00 90.20           C  
ANISOU 2961  C   LEU A 249    10072  13007  11191    724   1900   3381       C  
ATOM   2962  O   LEU A 249       0.963  -4.335 -25.429  1.00 89.29           O  
ANISOU 2962  O   LEU A 249     9779  12893  11254    755   1831   3423       O  
ATOM   2963  CB  LEU A 249       0.150  -4.159 -22.221  1.00 93.40           C  
ANISOU 2963  CB  LEU A 249    10737  13521  11230   1338   2559   3676       C  
ATOM   2964  CG  LEU A 249      -1.081  -4.427 -21.374  1.00101.63           C  
ANISOU 2964  CG  LEU A 249    11536  14799  12280   1720   2969   4077       C  
ATOM   2965  CD1 LEU A 249      -0.947  -3.769 -20.024  1.00104.98           C  
ANISOU 2965  CD1 LEU A 249    12591  15109  12188   2054   3306   3983       C  
ATOM   2966  CD2 LEU A 249      -2.353  -3.965 -22.084  1.00106.39           C  
ANISOU 2966  CD2 LEU A 249    11746  15563  13115   2046   3174   4409       C  
ATOM   2967  N   VAL A 250       2.727  -4.528 -24.017  1.00 85.06           N  
ANISOU 2967  N   VAL A 250     9742  12248  10329    503   1735   3142       N  
ATOM   2968  CA  VAL A 250       3.756  -4.031 -24.928  1.00 82.96           C  
ANISOU 2968  CA  VAL A 250     9611  11864  10045    275   1492   2937       C  
ATOM   2969  C   VAL A 250       3.831  -4.962 -26.149  1.00 86.43           C  
ANISOU 2969  C   VAL A 250     9658  12388  10794    136   1290   2983       C  
ATOM   2970  O   VAL A 250       3.931  -4.475 -27.276  1.00 86.37           O  
ANISOU 2970  O   VAL A 250     9647  12320  10848    111   1196   2918       O  
ATOM   2971  CB  VAL A 250       5.113  -3.854 -24.199  1.00 86.44           C  
ANISOU 2971  CB  VAL A 250    10353  12279  10213     19   1332   2795       C  
ATOM   2972  CG1 VAL A 250       6.249  -3.572 -25.176  1.00 84.69           C  
ANISOU 2972  CG1 VAL A 250    10101  12041  10036   -250   1083   2708       C  
ATOM   2973  CG2 VAL A 250       5.026  -2.749 -23.150  1.00 89.40           C  
ANISOU 2973  CG2 VAL A 250    11305  12469  10193    110   1473   2682       C  
ATOM   2974  N   LEU A 251       3.703  -6.287 -25.921  1.00 82.58           N  
ANISOU 2974  N   LEU A 251     8911  12001  10465     66   1240   3104       N  
ATOM   2975  CA  LEU A 251       3.705  -7.316 -26.961  1.00 81.29           C  
ANISOU 2975  CA  LEU A 251     8529  11827  10531    -61   1053   3126       C  
ATOM   2976  C   LEU A 251       2.422  -7.265 -27.771  1.00 86.15           C  
ANISOU 2976  C   LEU A 251     8927  12467  11337    -27   1020   3248       C  
ATOM   2977  O   LEU A 251       2.468  -7.534 -28.968  1.00 84.97           O  
ANISOU 2977  O   LEU A 251     8751  12266  11269   -129    821   3183       O  
ATOM   2978  CB  LEU A 251       3.892  -8.732 -26.379  1.00 81.67           C  
ANISOU 2978  CB  LEU A 251     8477  11884  10670   -147   1020   3236       C  
ATOM   2979  CG  LEU A 251       5.210  -9.057 -25.667  1.00 86.12           C  
ANISOU 2979  CG  LEU A 251     9160  12490  11070   -171   1008   3203       C  
ATOM   2980  CD1 LEU A 251       5.176 -10.439 -25.113  1.00 87.21           C  
ANISOU 2980  CD1 LEU A 251     9215  12606  11316   -188   1019   3365       C  
ATOM   2981  CD2 LEU A 251       6.415  -8.906 -26.581  1.00 87.78           C  
ANISOU 2981  CD2 LEU A 251     9433  12697  11224   -208    882   3085       C  
ATOM   2982  N   ALA A 252       1.280  -6.925 -27.124  1.00 85.33           N  
ANISOU 2982  N   ALA A 252     8664  12480  11278    137   1218   3466       N  
ATOM   2983  CA  ALA A 252      -0.028  -6.819 -27.781  1.00 87.36           C  
ANISOU 2983  CA  ALA A 252     8592  12873  11730    184   1189   3709       C  
ATOM   2984  C   ALA A 252      -0.027  -5.678 -28.796  1.00 92.00           C  
ANISOU 2984  C   ALA A 252     9289  13422  12244    314   1153   3609       C  
ATOM   2985  O   ALA A 252      -0.357  -5.922 -29.955  1.00 92.10           O  
ANISOU 2985  O   ALA A 252     9147  13473  12372    176    903   3642       O  
ATOM   2986  CB  ALA A 252      -1.129  -6.622 -26.753  1.00 91.11           C  
ANISOU 2986  CB  ALA A 252     8834  13546  12239    432   1502   4049       C  
ATOM   2987  N   VAL A 253       0.421  -4.462 -28.381  1.00 88.79           N  
ANISOU 2987  N   VAL A 253     9228  12898  11612    542   1370   3474       N  
ATOM   2988  CA  VAL A 253       0.543  -3.262 -29.226  1.00 88.80           C  
ANISOU 2988  CA  VAL A 253     9432  12789  11518    677   1379   3388       C  
ATOM   2989  C   VAL A 253       1.432  -3.587 -30.435  1.00 90.63           C  
ANISOU 2989  C   VAL A 253     9706  12961  11769    413   1079   3200       C  
ATOM   2990  O   VAL A 253       1.010  -3.362 -31.572  1.00 90.73           O  
ANISOU 2990  O   VAL A 253     9607  13026  11841    436    948   3265       O  
ATOM   2991  CB  VAL A 253       1.064  -2.032 -28.427  1.00 93.65           C  
ANISOU 2991  CB  VAL A 253    10563  13171  11849    859   1622   3236       C  
ATOM   2992  CG1 VAL A 253       1.269  -0.817 -29.332  1.00 93.95           C  
ANISOU 2992  CG1 VAL A 253    10868  13024  11804    949   1620   3164       C  
ATOM   2993  CG2 VAL A 253       0.128  -1.683 -27.277  1.00 96.71           C  
ANISOU 2993  CG2 VAL A 253    11015  13594  12136   1236   1991   3422       C  
ATOM   2994  N   LEU A 254       2.633  -4.163 -30.173  1.00 85.28           N  
ANISOU 2994  N   LEU A 254     9168  12215  11020    205    988   3018       N  
ATOM   2995  CA  LEU A 254       3.623  -4.607 -31.161  1.00 83.69           C  
ANISOU 2995  CA  LEU A 254     9016  11984  10798     41    795   2886       C  
ATOM   2996  C   LEU A 254       2.957  -5.519 -32.203  1.00 90.60           C  
ANISOU 2996  C   LEU A 254     9717  12907  11800    -29    585   2936       C  
ATOM   2997  O   LEU A 254       3.106  -5.286 -33.400  1.00 90.44           O  
ANISOU 2997  O   LEU A 254     9771  12875  11718    -26    465   2884       O  
ATOM   2998  CB  LEU A 254       4.749  -5.382 -30.437  1.00 82.33           C  
ANISOU 2998  CB  LEU A 254     8893  11818  10571    -84    784   2818       C  
ATOM   2999  CG  LEU A 254       6.212  -5.269 -30.911  1.00 85.58           C  
ANISOU 2999  CG  LEU A 254     9401  12247  10867   -167    732   2750       C  
ATOM   3000  CD1 LEU A 254       6.421  -5.799 -32.313  1.00 85.26           C  
ANISOU 3000  CD1 LEU A 254     9351  12203  10840   -123    637   2721       C  
ATOM   3001  CD2 LEU A 254       6.770  -3.879 -30.724  1.00 88.65           C  
ANISOU 3001  CD2 LEU A 254     9975  12593  11116   -238    777   2727       C  
ATOM   3002  N   LEU A 255       2.205  -6.533 -31.741  1.00 90.03           N  
ANISOU 3002  N   LEU A 255     9453  12876  11878   -125    522   3054       N  
ATOM   3003  CA  LEU A 255       1.488  -7.483 -32.589  1.00 92.49           C  
ANISOU 3003  CA  LEU A 255     9659  13185  12297   -313    246   3116       C  
ATOM   3004  C   LEU A 255       0.444  -6.775 -33.440  1.00 98.64           C  
ANISOU 3004  C   LEU A 255    10251  14116  13111   -274    125   3275       C  
ATOM   3005  O   LEU A 255       0.394  -7.019 -34.646  1.00 99.27           O  
ANISOU 3005  O   LEU A 255    10435  14169  13115   -391   -140   3206       O  
ATOM   3006  CB  LEU A 255       0.825  -8.577 -31.727  1.00 94.57           C  
ANISOU 3006  CB  LEU A 255     9730  13459  12744   -484    213   3291       C  
ATOM   3007  CG  LEU A 255       1.470  -9.968 -31.748  1.00100.16           C  
ANISOU 3007  CG  LEU A 255    10672  13936  13449   -662     87   3169       C  
ATOM   3008  CD1 LEU A 255       2.798  -9.998 -30.981  1.00 97.94           C  
ANISOU 3008  CD1 LEU A 255    10567  13599  13047   -491    313   3042       C  
ATOM   3009  CD2 LEU A 255       0.523 -11.004 -31.175  1.00106.23           C  
ANISOU 3009  CD2 LEU A 255    11244  14685  14432   -920    -21   3409       C  
ATOM   3010  N   ILE A 256      -0.360  -5.875 -32.816  1.00 96.48           N  
ANISOU 3010  N   ILE A 256     9742  14006  12909    -58    340   3504       N  
ATOM   3011  CA  ILE A 256      -1.418  -5.091 -33.469  1.00 98.82           C  
ANISOU 3011  CA  ILE A 256     9786  14508  13252     89    298   3762       C  
ATOM   3012  C   ILE A 256      -0.832  -4.252 -34.614  1.00102.42           C  
ANISOU 3012  C   ILE A 256    10511  14877  13526    190    234   3596       C  
ATOM   3013  O   ILE A 256      -1.192  -4.470 -35.769  1.00103.40           O  
ANISOU 3013  O   ILE A 256    10579  15091  13617     61    -70   3642       O  
ATOM   3014  CB  ILE A 256      -2.228  -4.218 -32.447  1.00103.50           C  
ANISOU 3014  CB  ILE A 256    10171  15251  13903    462    679   4054       C  
ATOM   3015  CG1 ILE A 256      -2.971  -5.078 -31.406  1.00105.53           C  
ANISOU 3015  CG1 ILE A 256    10074  15679  14343    381    760   4327       C  
ATOM   3016  CG2 ILE A 256      -3.212  -3.269 -33.158  1.00107.11           C  
ANISOU 3016  CG2 ILE A 256    10381  15927  14389    739    703   4370       C  
ATOM   3017  CD1 ILE A 256      -3.224  -4.357 -30.050  1.00112.53           C  
ANISOU 3017  CD1 ILE A 256    11006  16596  15153    810   1261   4466       C  
ATOM   3018  N   CYS A 257       0.088  -3.329 -34.283  1.00 97.79           N  
ANISOU 3018  N   CYS A 257    10242  14113  12801    372    491   3422       N  
ATOM   3019  CA  CYS A 257       0.726  -2.385 -35.200  1.00 97.58           C  
ANISOU 3019  CA  CYS A 257    10478  13984  12614    468    503   3321       C  
ATOM   3020  C   CYS A 257       1.481  -3.032 -36.365  1.00100.58           C  
ANISOU 3020  C   CYS A 257    11005  14339  12874    279    257   3148       C  
ATOM   3021  O   CYS A 257       1.358  -2.555 -37.493  1.00101.59           O  
ANISOU 3021  O   CYS A 257    11191  14516  12894    346    150   3197       O  
ATOM   3022  CB  CYS A 257       1.626  -1.425 -34.430  1.00 96.94           C  
ANISOU 3022  CB  CYS A 257    10727  13684  12422    562    776   3191       C  
ATOM   3023  SG  CYS A 257       0.764  -0.446 -33.173  1.00103.25           S  
ANISOU 3023  SG  CYS A 257    11600  14408  13222    905   1133   3353       S  
ATOM   3024  N   TRP A 258       2.260  -4.090 -36.096  1.00 95.29           N  
ANISOU 3024  N   TRP A 258    10430  13589  12188    106    205   2973       N  
ATOM   3025  CA  TRP A 258       3.098  -4.751 -37.097  1.00 94.79           C  
ANISOU 3025  CA  TRP A 258    10594  13465  11956     40     74   2812       C  
ATOM   3026  C   TRP A 258       2.394  -5.754 -38.014  1.00 99.80           C  
ANISOU 3026  C   TRP A 258    11281  14104  12533   -112   -261   2790       C  
ATOM   3027  O   TRP A 258       2.890  -5.972 -39.118  1.00 99.74           O  
ANISOU 3027  O   TRP A 258    11559  14046  12292    -76   -356   2673       O  
ATOM   3028  CB  TRP A 258       4.300  -5.409 -36.425  1.00 92.14           C  
ANISOU 3028  CB  TRP A 258    10366  13041  11600     11    211   2689       C  
ATOM   3029  CG  TRP A 258       5.369  -4.414 -36.116  1.00 92.13           C  
ANISOU 3029  CG  TRP A 258    10415  13054  11536     72    424   2703       C  
ATOM   3030  CD1 TRP A 258       5.380  -3.506 -35.097  1.00 94.58           C  
ANISOU 3030  CD1 TRP A 258    10696  13337  11902     53    562   2750       C  
ATOM   3031  CD2 TRP A 258       6.537  -4.154 -36.899  1.00 92.34           C  
ANISOU 3031  CD2 TRP A 258    10560  13119  11404    130    502   2708       C  
ATOM   3032  NE1 TRP A 258       6.503  -2.718 -35.177  1.00 94.04           N  
ANISOU 3032  NE1 TRP A 258    10736  13260  11736      1    653   2770       N  
ATOM   3033  CE2 TRP A 258       7.234  -3.096 -36.276  1.00 96.10           C  
ANISOU 3033  CE2 TRP A 258    11019  13603  11892     51    634   2786       C  
ATOM   3034  CE3 TRP A 258       7.074  -4.727 -38.066  1.00 94.96           C  
ANISOU 3034  CE3 TRP A 258    11047  13480  11555    251    487   2678       C  
ATOM   3035  CZ2 TRP A 258       8.448  -2.603 -36.774  1.00 96.27           C  
ANISOU 3035  CZ2 TRP A 258    11057  13711  11810     24    726   2896       C  
ATOM   3036  CZ3 TRP A 258       8.268  -4.229 -38.567  1.00 97.09           C  
ANISOU 3036  CZ3 TRP A 258    11333  13858  11698    335    656   2790       C  
ATOM   3037  CH2 TRP A 258       8.943  -3.181 -37.924  1.00 97.35           C  
ANISOU 3037  CH2 TRP A 258    11233  13948  11806    191    761   2928       C  
ATOM   3038  N   PHE A 259       1.262  -6.355 -37.587  1.00 97.91           N  
ANISOU 3038  N   PHE A 259    10802  13925  12474   -301   -449   2924       N  
ATOM   3039  CA  PHE A 259       0.539  -7.330 -38.414  1.00100.93           C  
ANISOU 3039  CA  PHE A 259    11270  14285  12796   -582   -866   2925       C  
ATOM   3040  C   PHE A 259       0.139  -6.784 -39.800  1.00105.55           C  
ANISOU 3040  C   PHE A 259    11941  14999  13165   -562  -1114   2969       C  
ATOM   3041  O   PHE A 259       0.424  -7.482 -40.775  1.00107.10           O  
ANISOU 3041  O   PHE A 259    12558  15046  13090   -676  -1355   2777       O  
ATOM   3042  CB  PHE A 259      -0.673  -7.943 -37.688  1.00105.41           C  
ANISOU 3042  CB  PHE A 259    11454  14960  13635   -862  -1049   3177       C  
ATOM   3043  CG  PHE A 259      -1.262  -9.151 -38.385  1.00111.51           C  
ANISOU 3043  CG  PHE A 259    12405  15615  14347  -1302  -1542   3157       C  
ATOM   3044  CD1 PHE A 259      -0.751 -10.425 -38.157  1.00114.43           C  
ANISOU 3044  CD1 PHE A 259    13172  15629  14679  -1491  -1606   2947       C  
ATOM   3045  CD2 PHE A 259      -2.331  -9.015 -39.266  1.00119.00           C  
ANISOU 3045  CD2 PHE A 259    13167  16790  15257  -1544  -1968   3371       C  
ATOM   3046  CE1 PHE A 259      -1.295 -11.540 -38.803  1.00122.21           C  
ANISOU 3046  CE1 PHE A 259    14469  16396  15568  -1948  -2093   2901       C  
ATOM   3047  CE2 PHE A 259      -2.870 -10.130 -39.916  1.00124.82           C  
ANISOU 3047  CE2 PHE A 259    14152  17381  15894  -2058  -2512   3343       C  
ATOM   3048  CZ  PHE A 259      -2.351 -11.385 -39.678  1.00124.70           C  
ANISOU 3048  CZ  PHE A 259    14632  16923  15823  -2274  -2573   3085       C  
ATOM   3049  N   PRO A 260      -0.479  -5.576 -39.951  1.00101.18           N  
ANISOU 3049  N   PRO A 260    11078  14694  12671   -379  -1047   3219       N  
ATOM   3050  CA  PRO A 260      -0.824  -5.108 -41.305  1.00102.96           C  
ANISOU 3050  CA  PRO A 260    11397  15063  12660   -347  -1301   3293       C  
ATOM   3051  C   PRO A 260       0.386  -4.778 -42.179  1.00103.50           C  
ANISOU 3051  C   PRO A 260    11933  14984  12408   -139  -1146   3057       C  
ATOM   3052  O   PRO A 260       0.329  -5.027 -43.382  1.00105.96           O  
ANISOU 3052  O   PRO A 260    12536  15316  12408   -195  -1422   2992       O  
ATOM   3053  CB  PRO A 260      -1.685  -3.872 -41.042  1.00105.60           C  
ANISOU 3053  CB  PRO A 260    11284  15669  13172    -99  -1156   3666       C  
ATOM   3054  CG  PRO A 260      -1.235  -3.374 -39.729  1.00107.02           C  
ANISOU 3054  CG  PRO A 260    11396  15721  13547    113   -694   3639       C  
ATOM   3055  CD  PRO A 260      -0.917  -4.597 -38.933  1.00101.42           C  
ANISOU 3055  CD  PRO A 260    10735  14861  12939   -144   -726   3459       C  
ATOM   3056  N   VAL A 261       1.476  -4.244 -41.576  1.00 94.82           N  
ANISOU 3056  N   VAL A 261    10905  13762  11359     74   -724   2964       N  
ATOM   3057  CA  VAL A 261       2.713  -3.854 -42.269  1.00 93.01           C  
ANISOU 3057  CA  VAL A 261    10997  13460  10882    268   -509   2851       C  
ATOM   3058  C   VAL A 261       3.446  -5.054 -42.875  1.00 97.23           C  
ANISOU 3058  C   VAL A 261    11949  13850  11145    247   -580   2612       C  
ATOM   3059  O   VAL A 261       3.856  -4.994 -44.033  1.00 98.53           O  
ANISOU 3059  O   VAL A 261    12437  14030  10969    392   -595   2567       O  
ATOM   3060  CB  VAL A 261       3.669  -2.985 -41.411  1.00 93.59           C  
ANISOU 3060  CB  VAL A 261    10990  13472  11098    392   -112   2885       C  
ATOM   3061  CG1 VAL A 261       4.489  -2.061 -42.299  1.00 93.71           C  
ANISOU 3061  CG1 VAL A 261    11176  13516  10915    559     60   2966       C  
ATOM   3062  CG2 VAL A 261       2.914  -2.175 -40.364  1.00 92.59           C  
ANISOU 3062  CG2 VAL A 261    10586  13355  11237    411     -9   3038       C  
ATOM   3063  N   LEU A 262       3.604  -6.134 -42.094  1.00 93.13           N  
ANISOU 3063  N   LEU A 262    11471  13172  10743    119   -587   2479       N  
ATOM   3064  CA  LEU A 262       4.278  -7.363 -42.526  1.00 94.77           C  
ANISOU 3064  CA  LEU A 262    12154  13159  10696    168   -600   2260       C  
ATOM   3065  C   LEU A 262       3.454  -8.132 -43.565  1.00102.73           C  
ANISOU 3065  C   LEU A 262    13571  14045  11415    -31  -1049   2133       C  
ATOM   3066  O   LEU A 262       4.032  -8.726 -44.476  1.00105.11           O  
ANISOU 3066  O   LEU A 262    14452  14173  11313    133  -1039   1949       O  
ATOM   3067  CB  LEU A 262       4.617  -8.269 -41.320  1.00 93.42           C  
ANISOU 3067  CB  LEU A 262    11920  12824  10751    100   -478   2202       C  
ATOM   3068  CG  LEU A 262       5.511  -7.671 -40.212  1.00 94.74           C  
ANISOU 3068  CG  LEU A 262    11744  13110  11143    234   -106   2317       C  
ATOM   3069  CD1 LEU A 262       5.331  -8.409 -38.907  1.00 93.73           C  
ANISOU 3069  CD1 LEU A 262    11452  12889  11274     87    -96   2322       C  
ATOM   3070  CD2 LEU A 262       6.977  -7.649 -40.609  1.00 97.80           C  
ANISOU 3070  CD2 LEU A 262    12290  13541  11326    545    216   2334       C  
ATOM   3071  N   ALA A 263       2.110  -8.112 -43.429  1.00100.53           N  
ANISOU 3071  N   ALA A 263    13006  13875  11315   -382  -1444   2265       N  
ATOM   3072  CA  ALA A 263       1.174  -8.791 -44.330  1.00105.34           C  
ANISOU 3072  CA  ALA A 263    13922  14422  11680   -727  -2001   2212       C  
ATOM   3073  C   ALA A 263       1.254  -8.255 -45.763  1.00112.11           C  
ANISOU 3073  C   ALA A 263    15118  15396  12082   -565  -2133   2182       C  
ATOM   3074  O   ALA A 263       1.217  -9.048 -46.706  1.00116.17           O  
ANISOU 3074  O   ALA A 263    16284  15697  12157   -687  -2446   1966       O  
ATOM   3075  CB  ALA A 263      -0.246  -8.677 -43.800  1.00107.35           C  
ANISOU 3075  CB  ALA A 263    13586  14918  12286  -1118  -2353   2513       C  
ATOM   3076  N   LEU A 264       1.390  -6.917 -45.920  1.00106.67           N  
ANISOU 3076  N   LEU A 264    14070  14999  11459   -283  -1883   2396       N  
ATOM   3077  CA  LEU A 264       1.514  -6.246 -47.221  1.00108.92           C  
ANISOU 3077  CA  LEU A 264    14613  15436  11335    -75  -1935   2441       C  
ATOM   3078  C   LEU A 264       2.849  -6.596 -47.863  1.00112.86           C  
ANISOU 3078  C   LEU A 264    15721  15736  11423    278  -1596   2208       C  
ATOM   3079  O   LEU A 264       2.929  -6.714 -49.088  1.00116.56           O  
ANISOU 3079  O   LEU A 264    16712  16199  11376    387  -1744   2119       O  
ATOM   3080  CB  LEU A 264       1.387  -4.721 -47.080  1.00106.74           C  
ANISOU 3080  CB  LEU A 264    13824  15448  11285    156  -1686   2764       C  
ATOM   3081  CG  LEU A 264       0.003  -4.182 -46.722  1.00112.81           C  
ANISOU 3081  CG  LEU A 264    14013  16491  12359    -20  -1962   3095       C  
ATOM   3082  CD1 LEU A 264       0.116  -2.882 -45.971  1.00109.87           C  
ANISOU 3082  CD1 LEU A 264    13220  16203  12320    269  -1527   3333       C  
ATOM   3083  CD2 LEU A 264      -0.855  -3.993 -47.956  1.00120.26           C  
ANISOU 3083  CD2 LEU A 264    15026  17692  12976   -115  -2437   3269       C  
ATOM   3084  N   MET A 265       3.890  -6.784 -47.026  1.00105.38           N  
ANISOU 3084  N   MET A 265    14698  14661  10679    478  -1136   2150       N  
ATOM   3085  CA  MET A 265       5.230  -7.174 -47.464  1.00105.73           C  
ANISOU 3085  CA  MET A 265    15189  14583  10400    879   -728   2034       C  
ATOM   3086  C   MET A 265       5.226  -8.632 -47.920  1.00114.29           C  
ANISOU 3086  C   MET A 265    17031  15298  11096    859   -923   1716       C  
ATOM   3087  O   MET A 265       6.002  -8.992 -48.803  1.00117.00           O  
ANISOU 3087  O   MET A 265    17975  15533  10945   1243   -698   1605       O  
ATOM   3088  CB  MET A 265       6.253  -6.976 -46.343  1.00103.71           C  
ANISOU 3088  CB  MET A 265    14531  14366  10510   1038   -255   2147       C  
ATOM   3089  CG  MET A 265       6.556  -5.540 -46.032  1.00104.04           C  
ANISOU 3089  CG  MET A 265    14046  14672  10811   1084    -16   2428       C  
ATOM   3090  SD  MET A 265       7.647  -5.476 -44.601  1.00104.26           S  
ANISOU 3090  SD  MET A 265    13655  14727  11230   1107    372   2540       S  
ATOM   3091  CE  MET A 265       7.421  -3.837 -44.105  1.00 98.29           C  
ANISOU 3091  CE  MET A 265    12439  14124  10783    950    425   2780       C  
ATOM   3092  N   ALA A 266       4.359  -9.466 -47.310  1.00111.99           N  
ANISOU 3092  N   ALA A 266    16752  14790  11010    426  -1316   1596       N  
ATOM   3093  CA  ALA A 266       4.193 -10.878 -47.654  1.00116.92           C  
ANISOU 3093  CA  ALA A 266    18173  14955  11298    278  -1592   1289       C  
ATOM   3094  C   ALA A 266       3.437 -10.998 -48.980  1.00127.04           C  
ANISOU 3094  C   ALA A 266    20039  16190  12041     59  -2125   1158       C  
ATOM   3095  O   ALA A 266       3.824 -11.801 -49.831  1.00131.69           O  
ANISOU 3095  O   ALA A 266    21573  16422  12041    239  -2150    874       O  
ATOM   3096  CB  ALA A 266       3.442 -11.604 -46.547  1.00116.86           C  
ANISOU 3096  CB  ALA A 266    17905  14764  11731   -206  -1874   1290       C  
ATOM   3097  N   HIS A 267       2.385 -10.161 -49.164  1.00123.86           N  
ANISOU 3097  N   HIS A 267    19099  16163  11800   -280  -2528   1391       N  
ATOM   3098  CA  HIS A 267       1.548 -10.083 -50.368  1.00129.57           C  
ANISOU 3098  CA  HIS A 267    20188  16987  12057   -548  -3113   1374       C  
ATOM   3099  C   HIS A 267       2.373  -9.616 -51.569  1.00136.51           C  
ANISOU 3099  C   HIS A 267    21601  17935  12331     -8  -2814   1304       C  
ATOM   3100  O   HIS A 267       2.084 -10.003 -52.701  1.00142.34           O  
ANISOU 3100  O   HIS A 267    23096  18555  12431   -100  -3208   1124       O  
ATOM   3101  CB  HIS A 267       0.386  -9.103 -50.141  1.00129.04           C  
ANISOU 3101  CB  HIS A 267    19219  17420  12390   -866  -3449   1779       C  
ATOM   3102  CG  HIS A 267      -0.906  -9.513 -50.781  1.00138.92           C  
ANISOU 3102  CG  HIS A 267    20601  18761  13422  -1484  -4290   1845       C  
ATOM   3103  ND1 HIS A 267      -1.001  -9.736 -52.145  1.00147.05           N  
ANISOU 3103  ND1 HIS A 267    22412  19730  13731  -1543  -4694   1672       N  
ATOM   3104  CD2 HIS A 267      -2.128  -9.686 -50.225  1.00142.24           C  
ANISOU 3104  CD2 HIS A 267    20420  19381  14245  -2067  -4795   2123       C  
ATOM   3105  CE1 HIS A 267      -2.264 -10.063 -52.367  1.00151.80           C  
ANISOU 3105  CE1 HIS A 267    22874  20484  14321  -2228  -5496   1834       C  
ATOM   3106  NE2 HIS A 267      -2.980 -10.045 -51.242  1.00149.59           N  
ANISOU 3106  NE2 HIS A 267    21717  20387  14731  -2562  -5572   2141       N  
ATOM   3107  N   SER A 268       3.396  -8.780 -51.306  1.00129.51           N  
ANISOU 3107  N   SER A 268    20329  17250  11629    522  -2133   1475       N  
ATOM   3108  CA  SER A 268       4.332  -8.207 -52.272  1.00131.33           C  
ANISOU 3108  CA  SER A 268    20876  17621  11401   1085  -1700   1533       C  
ATOM   3109  C   SER A 268       5.111  -9.268 -53.061  1.00141.81           C  
ANISOU 3109  C   SER A 268    23275  18569  12036   1462  -1511   1207       C  
ATOM   3110  O   SER A 268       5.350  -9.079 -54.256  1.00146.32           O  
ANISOU 3110  O   SER A 268    24412  19209  11973   1771  -1463   1181       O  
ATOM   3111  CB  SER A 268       5.296  -7.262 -51.554  1.00129.42           C  
ANISOU 3111  CB  SER A 268    19934  17623  11617   1431  -1045   1823       C  
ATOM   3112  OG  SER A 268       6.449  -6.927 -52.312  1.00141.23           O  
ANISOU 3112  OG  SER A 268    21701  19230  12728   1992   -513   1929       O  
ATOM   3113  N   LEU A 269       5.499 -10.371 -52.393  1.00138.65           N  
ANISOU 3113  N   LEU A 269    23194  17760  11728   1490  -1371    981       N  
ATOM   3114  CA  LEU A 269       6.304 -11.462 -52.960  1.00144.00           C  
ANISOU 3114  CA  LEU A 269    24936  17992  11787   1958  -1080    686       C  
ATOM   3115  C   LEU A 269       5.510 -12.506 -53.754  1.00156.67           C  
ANISOU 3115  C   LEU A 269    27669  19097  12761   1605  -1724    272       C  
ATOM   3116  O   LEU A 269       6.088 -13.178 -54.613  1.00162.21           O  
ANISOU 3116  O   LEU A 269    29463  19445  12723   2070  -1511     15       O  
ATOM   3117  CB  LEU A 269       7.139 -12.156 -51.864  1.00141.18           C  
ANISOU 3117  CB  LEU A 269    24430  17406  11808   2218   -594    687       C  
ATOM   3118  CG  LEU A 269       7.342 -11.401 -50.547  1.00137.58           C  
ANISOU 3118  CG  LEU A 269    22771  17320  12185   2087   -358   1020       C  
ATOM   3119  CD1 LEU A 269       7.479 -12.350 -49.390  1.00136.07           C  
ANISOU 3119  CD1 LEU A 269    22528  16806  12366   1982   -291    934       C  
ATOM   3120  CD2 LEU A 269       8.508 -10.435 -50.623  1.00137.02           C  
ANISOU 3120  CD2 LEU A 269    22180  17694  12187   2621    296   1380       C  
ATOM   3121  N   ALA A 270       4.207 -12.658 -53.459  1.00154.91           N  
ANISOU 3121  N   ALA A 270    27215  18840  12804    787  -2502    235       N  
ATOM   3122  CA  ALA A 270       3.342 -13.634 -54.125  1.00163.39           C  
ANISOU 3122  CA  ALA A 270    29288  19452  13341    242  -3265   -111       C  
ATOM   3123  C   ALA A 270       2.674 -13.099 -55.396  1.00173.61           C  
ANISOU 3123  C   ALA A 270    30899  21019  14046     39  -3805    -97       C  
ATOM   3124  O   ALA A 270       2.631 -13.815 -56.400  1.00181.41           O  
ANISOU 3124  O   ALA A 270    33135  21596  14199     26  -4112   -451       O  
ATOM   3125  CB  ALA A 270       2.293 -14.156 -53.154  1.00163.26           C  
ANISOU 3125  CB  ALA A 270    28819  19297  13914   -595  -3856    -70       C  
ATOM   3126  N   THR A 271       2.140 -11.858 -55.350  1.00166.90           N  
ANISOU 3126  N   THR A 271    28993  20832  13589   -104  -3929    314       N  
ATOM   3127  CA  THR A 271       1.445 -11.214 -56.476  1.00171.63           C  
ANISOU 3127  CA  THR A 271    29699  21801  13711   -285  -4446    441       C  
ATOM   3128  C   THR A 271       1.912  -9.772 -56.720  1.00171.33           C  
ANISOU 3128  C   THR A 271    28926  22350  13823    265  -3914    837       C  
ATOM   3129  O   THR A 271       2.552  -9.171 -55.853  1.00163.45           O  
ANISOU 3129  O   THR A 271    27147  21518  13438    598  -3279   1057       O  
ATOM   3130  CB  THR A 271      -0.088 -11.270 -56.283  1.00183.67           C  
ANISOU 3130  CB  THR A 271    30724  23536  15526  -1220  -5407    626       C  
ATOM   3131  OG1 THR A 271      -0.427 -10.827 -54.967  1.00176.27           O  
ANISOU 3131  OG1 THR A 271    28555  22870  15549  -1396  -5239    965       O  
ATOM   3132  CG2 THR A 271      -0.674 -12.654 -56.545  1.00191.10           C  
ANISOU 3132  CG2 THR A 271    32677  23898  16036  -1905  -6161    244       C  
ATOM   3133  N   THR A 272       1.584  -9.224 -57.908  1.00173.56           N  
ANISOU 3133  N   THR A 272    29507  22923  13514    321  -4211    938       N  
ATOM   3134  CA  THR A 272       1.900  -7.845 -58.295  1.00170.84           C  
ANISOU 3134  CA  THR A 272    28567  23105  13239    782  -3797   1349       C  
ATOM   3135  C   THR A 272       0.838  -6.926 -57.696  1.00172.02           C  
ANISOU 3135  C   THR A 272    27548  23721  14092    366  -4153   1794       C  
ATOM   3136  O   THR A 272      -0.354  -7.242 -57.766  1.00175.47           O  
ANISOU 3136  O   THR A 272    27880  24259  14531   -266  -4953   1844       O  
ATOM   3137  CB  THR A 272       1.986  -7.694 -59.826  1.00186.64           C  
ANISOU 3137  CB  THR A 272    31438  25214  14261   1057  -3950   1297       C  
ATOM   3138  OG1 THR A 272       0.784  -8.181 -60.425  1.00193.40           O  
ANISOU 3138  OG1 THR A 272    32725  26068  14689    384  -4955   1180       O  
ATOM   3139  CG2 THR A 272       3.199  -8.399 -60.423  1.00189.04           C  
ANISOU 3139  CG2 THR A 272    32854  25119  13852   1707  -3361    951       C  
ATOM   3140  N   LEU A 273       1.264  -5.806 -57.091  1.00162.69           N  
ANISOU 3140  N   LEU A 273    25509  22811  13495    715  -3562   2146       N  
ATOM   3141  CA  LEU A 273       0.344  -4.865 -56.448  1.00159.57           C  
ANISOU 3141  CA  LEU A 273    24070  22800  13760    478  -3748   2583       C  
ATOM   3142  C   LEU A 273       0.327  -3.502 -57.126  1.00164.18           C  
ANISOU 3142  C   LEU A 273    24345  23791  14247    841  -3562   3007       C  
ATOM   3143  O   LEU A 273       1.386  -2.919 -57.376  1.00161.78           O  
ANISOU 3143  O   LEU A 273    24163  23468  13839   1346  -2921   3070       O  
ATOM   3144  CB  LEU A 273       0.655  -4.720 -54.945  1.00152.26           C  
ANISOU 3144  CB  LEU A 273    22436  21757  13658    489  -3289   2633       C  
ATOM   3145  CG  LEU A 273       0.674  -6.005 -54.105  1.00156.16           C  
ANISOU 3145  CG  LEU A 273    23126  21857  14350    155  -3409   2286       C  
ATOM   3146  CD1 LEU A 273       1.459  -5.801 -52.830  1.00149.16           C  
ANISOU 3146  CD1 LEU A 273    21749  20849  14077    371  -2771   2305       C  
ATOM   3147  CD2 LEU A 273      -0.740  -6.504 -53.800  1.00161.80           C  
ANISOU 3147  CD2 LEU A 273    23529  22670  15277   -520  -4173   2381       C  
ATOM   3148  N   SER A 274      -0.886  -2.997 -57.417  1.00164.10           N  
ANISOU 3148  N   SER A 274    23898  24169  14282    578  -4125   3361       N  
ATOM   3149  CA  SER A 274      -1.101  -1.697 -58.054  1.00165.14           C  
ANISOU 3149  CA  SER A 274    23712  24696  14339    911  -4024   3834       C  
ATOM   3150  C   SER A 274      -0.877  -0.545 -57.064  1.00162.44           C  
ANISOU 3150  C   SER A 274    22585  24388  14747   1203  -3414   4166       C  
ATOM   3151  O   SER A 274      -0.779  -0.782 -55.856  1.00157.07           O  
ANISOU 3151  O   SER A 274    21532  23505  14641   1074  -3199   4052       O  
ATOM   3152  CB  SER A 274      -2.502  -1.624 -58.659  1.00175.17           C  
ANISOU 3152  CB  SER A 274    24751  26404  15404    546  -4858   4155       C  
ATOM   3153  OG  SER A 274      -2.623  -2.471 -59.790  1.00190.96           O  
ANISOU 3153  OG  SER A 274    27627  28374  16557    301  -5438   3874       O  
ATOM   3154  N   ASP A 275      -0.810   0.702 -57.585  1.00159.51           N  
ANISOU 3154  N   ASP A 275    22040  24239  14330   1590  -3154   4579       N  
ATOM   3155  CA  ASP A 275      -0.604   1.950 -56.833  1.00154.70           C  
ANISOU 3155  CA  ASP A 275    20872  23592  14315   1888  -2596   4921       C  
ATOM   3156  C   ASP A 275      -1.566   2.135 -55.648  1.00154.93           C  
ANISOU 3156  C   ASP A 275    20174  23679  15013   1714  -2712   5108       C  
ATOM   3157  O   ASP A 275      -1.208   2.798 -54.673  1.00149.76           O  
ANISOU 3157  O   ASP A 275    19221  22810  14870   1880  -2209   5180       O  
ATOM   3158  CB  ASP A 275      -0.676   3.165 -57.779  1.00160.15           C  
ANISOU 3158  CB  ASP A 275    21578  24521  14751   2273  -2472   5389       C  
ATOM   3159  CG  ASP A 275       0.421   3.238 -58.831  1.00173.25           C  
ANISOU 3159  CG  ASP A 275    23878  26130  15818   2556  -2155   5314       C  
ATOM   3160  OD1 ASP A 275       0.832   2.168 -59.343  1.00176.05           O  
ANISOU 3160  OD1 ASP A 275    24816  26414  15660   2458  -2312   4919       O  
ATOM   3161  OD2 ASP A 275       0.854   4.365 -59.161  1.00179.09           O  
ANISOU 3161  OD2 ASP A 275    24576  26888  16583   2899  -1732   5679       O  
ATOM   3162  N   GLN A 276      -2.775   1.544 -55.739  1.00154.57           N  
ANISOU 3162  N   GLN A 276    19868  23931  14931   1366  -3380   5214       N  
ATOM   3163  CA  GLN A 276      -3.812   1.575 -54.703  1.00153.26           C  
ANISOU 3163  CA  GLN A 276    18964  23925  15344   1203  -3530   5473       C  
ATOM   3164  C   GLN A 276      -3.380   0.826 -53.435  1.00150.22           C  
ANISOU 3164  C   GLN A 276    18517  23179  15382    980  -3285   5088       C  
ATOM   3165  O   GLN A 276      -3.722   1.254 -52.331  1.00146.90           O  
ANISOU 3165  O   GLN A 276    17573  22737  15506   1083  -3006   5274       O  
ATOM   3166  CB  GLN A 276      -5.167   1.065 -55.244  1.00161.62           C  
ANISOU 3166  CB  GLN A 276    19719  25476  16214    811  -4368   5769       C  
ATOM   3167  CG  GLN A 276      -5.120  -0.299 -55.955  1.00180.71           C  
ANISOU 3167  CG  GLN A 276    22765  27818  18078    263  -5005   5337       C  
ATOM   3168  CD  GLN A 276      -6.296  -0.568 -56.873  1.00205.18           C  
ANISOU 3168  CD  GLN A 276    25737  31430  20791   -133  -5903   5673       C  
ATOM   3169  OE1 GLN A 276      -7.375   0.028 -56.763  1.00202.89           O  
ANISOU 3169  OE1 GLN A 276    24655  31653  20781   -103  -6144   6297       O  
ATOM   3170  NE2 GLN A 276      -6.111  -1.498 -57.799  1.00200.50           N  
ANISOU 3170  NE2 GLN A 276    25954  30716  19512   -509  -6432   5287       N  
ATOM   3171  N   VAL A 277      -2.608  -0.272 -53.599  1.00145.00           N  
ANISOU 3171  N   VAL A 277    18442  22221  14431    739  -3351   4571       N  
ATOM   3172  CA  VAL A 277      -2.071  -1.082 -52.494  1.00139.75           C  
ANISOU 3172  CA  VAL A 277    17805  21200  14093    555  -3118   4200       C  
ATOM   3173  C   VAL A 277      -0.835  -0.362 -51.930  1.00136.55           C  
ANISOU 3173  C   VAL A 277    17458  20517  13909    939  -2364   4112       C  
ATOM   3174  O   VAL A 277      -0.676  -0.289 -50.709  1.00131.67           O  
ANISOU 3174  O   VAL A 277    16524  19735  13770    926  -2061   4073       O  
ATOM   3175  CB  VAL A 277      -1.753  -2.550 -52.907  1.00146.00           C  
ANISOU 3175  CB  VAL A 277    19259  21746  14467    203  -3469   3725       C  
ATOM   3176  CG1 VAL A 277      -1.398  -3.399 -51.691  1.00141.63           C  
ANISOU 3176  CG1 VAL A 277    18643  20864  14306      9  -3276   3439       C  
ATOM   3177  CG2 VAL A 277      -2.913  -3.186 -53.669  1.00152.92           C  
ANISOU 3177  CG2 VAL A 277    20220  22873  15008   -271  -4314   3819       C  
ATOM   3178  N   LYS A 278       0.017   0.186 -52.833  1.00133.06           N  
ANISOU 3178  N   LYS A 278    17412  20049  13094   1249  -2090   4126       N  
ATOM   3179  CA  LYS A 278       1.240   0.943 -52.530  1.00128.78           C  
ANISOU 3179  CA  LYS A 278    16930  19304  12698   1544  -1440   4140       C  
ATOM   3180  C   LYS A 278       0.955   2.143 -51.616  1.00129.22           C  
ANISOU 3180  C   LYS A 278    16506  19314  13279   1674  -1143   4444       C  
ATOM   3181  O   LYS A 278       1.744   2.416 -50.708  1.00124.76           O  
ANISOU 3181  O   LYS A 278    15879  18499  13025   1685   -732   4356       O  
ATOM   3182  CB  LYS A 278       1.919   1.428 -53.823  1.00134.35           C  
ANISOU 3182  CB  LYS A 278    18058  20099  12889   1838  -1272   4261       C  
ATOM   3183  CG  LYS A 278       2.623   0.350 -54.644  1.00151.45           C  
ANISOU 3183  CG  LYS A 278    20860  22209  14477   1870  -1317   3931       C  
ATOM   3184  CD  LYS A 278       3.471   0.992 -55.745  1.00163.53           C  
ANISOU 3184  CD  LYS A 278    22735  23842  15559   2251   -966   4130       C  
ATOM   3185  CE  LYS A 278       3.990   0.017 -56.774  1.00176.13           C  
ANISOU 3185  CE  LYS A 278    25065  25426  16432   2407  -1009   3862       C  
ATOM   3186  NZ  LYS A 278       2.928  -0.430 -57.713  1.00189.58           N  
ANISOU 3186  NZ  LYS A 278    27146  27284  17601   2249  -1680   3783       N  
ATOM   3187  N   LYS A 279      -0.174   2.849 -51.861  1.00128.27           N  
ANISOU 3187  N   LYS A 279    16087  19431  13220   1788  -1357   4821       N  
ATOM   3188  CA  LYS A 279      -0.630   3.995 -51.070  1.00126.92           C  
ANISOU 3188  CA  LYS A 279    15557  19189  13476   2016  -1069   5144       C  
ATOM   3189  C   LYS A 279      -0.958   3.551 -49.644  1.00127.05           C  
ANISOU 3189  C   LYS A 279    15251  19082  13942   1850  -1008   5000       C  
ATOM   3190  O   LYS A 279      -0.481   4.173 -48.696  1.00124.04           O  
ANISOU 3190  O   LYS A 279    14872  18402  13854   1953   -585   4970       O  
ATOM   3191  CB  LYS A 279      -1.874   4.638 -51.703  1.00134.45           C  
ANISOU 3191  CB  LYS A 279    16227  20503  14356   2239  -1342   5632       C  
ATOM   3192  CG  LYS A 279      -1.582   5.646 -52.798  1.00151.50           C  
ANISOU 3192  CG  LYS A 279    18652  22704  16207   2562  -1199   5928       C  
ATOM   3193  CD  LYS A 279      -2.795   6.537 -53.027  1.00165.46           C  
ANISOU 3193  CD  LYS A 279    20052  24758  18058   2902  -1306   6501       C  
ATOM   3194  CE  LYS A 279      -2.996   6.885 -54.477  1.00180.93           C  
ANISOU 3194  CE  LYS A 279    22182  27035  19529   3071  -1563   6807       C  
ATOM   3195  NZ  LYS A 279      -4.310   7.539 -54.703  1.00195.60           N  
ANISOU 3195  NZ  LYS A 279    23571  29290  21456   3384  -1769   7420       N  
ATOM   3196  N   ALA A 280      -1.746   2.457 -49.505  1.00123.84           N  
ANISOU 3196  N   ALA A 280    14612  18889  13551   1554  -1452   4917       N  
ATOM   3197  CA  ALA A 280      -2.180   1.865 -48.234  1.00121.00           C  
ANISOU 3197  CA  ALA A 280    13912  18482  13581   1366  -1448   4832       C  
ATOM   3198  C   ALA A 280      -1.014   1.440 -47.332  1.00118.25           C  
ANISOU 3198  C   ALA A 280    13803  17755  13373   1249  -1105   4421       C  
ATOM   3199  O   ALA A 280      -1.096   1.604 -46.113  1.00115.18           O  
ANISOU 3199  O   ALA A 280    13205  17230  13327   1279   -852   4418       O  
ATOM   3200  CB  ALA A 280      -3.096   0.680 -48.501  1.00124.96           C  
ANISOU 3200  CB  ALA A 280    14211  19267  14003    965  -2055   4836       C  
ATOM   3201  N   PHE A 281       0.071   0.918 -47.939  1.00112.93           N  
ANISOU 3201  N   PHE A 281    13568  16942  12400   1162  -1079   4120       N  
ATOM   3202  CA  PHE A 281       1.278   0.476 -47.246  1.00108.37           C  
ANISOU 3202  CA  PHE A 281    13181  16088  11908   1084   -770   3809       C  
ATOM   3203  C   PHE A 281       1.957   1.612 -46.482  1.00108.43           C  
ANISOU 3203  C   PHE A 281    13147  15891  12160   1239   -304   3905       C  
ATOM   3204  O   PHE A 281       2.459   1.381 -45.380  1.00104.99           O  
ANISOU 3204  O   PHE A 281    12654  15281  11955   1125   -117   3747       O  
ATOM   3205  CB  PHE A 281       2.255  -0.191 -48.228  1.00111.27           C  
ANISOU 3205  CB  PHE A 281    14008  16418  11850   1093   -776   3589       C  
ATOM   3206  CG  PHE A 281       3.566  -0.630 -47.614  1.00110.20           C  
ANISOU 3206  CG  PHE A 281    14001  16084  11785   1087   -429   3376       C  
ATOM   3207  CD1 PHE A 281       3.628  -1.752 -46.792  1.00111.75           C  
ANISOU 3207  CD1 PHE A 281    14176  16157  12126    900   -499   3132       C  
ATOM   3208  CD2 PHE A 281       4.739   0.075 -47.861  1.00111.86           C  
ANISOU 3208  CD2 PHE A 281    14313  16265  11925   1258    -40   3486       C  
ATOM   3209  CE1 PHE A 281       4.839  -2.153 -46.221  1.00110.12           C  
ANISOU 3209  CE1 PHE A 281    14036  15826  11980    938   -181   3006       C  
ATOM   3210  CE2 PHE A 281       5.949  -0.330 -47.290  1.00112.47           C  
ANISOU 3210  CE2 PHE A 281    14399  16256  12079   1242    253   3387       C  
ATOM   3211  CZ  PHE A 281       5.989  -1.440 -46.476  1.00108.68           C  
ANISOU 3211  CZ  PHE A 281    13887  15680  11729   1110    182   3149       C  
ATOM   3212  N   ALA A 282       1.969   2.829 -47.066  1.00106.01           N  
ANISOU 3212  N   ALA A 282    12920  15581  11780   1469   -149   4175       N  
ATOM   3213  CA  ALA A 282       2.562   4.027 -46.468  1.00104.52           C  
ANISOU 3213  CA  ALA A 282    12819  15118  11778   1562    241   4292       C  
ATOM   3214  C   ALA A 282       1.860   4.427 -45.165  1.00107.65           C  
ANISOU 3214  C   ALA A 282    13041  15357  12503   1615    358   4329       C  
ATOM   3215  O   ALA A 282       2.527   4.875 -44.233  1.00105.38           O  
ANISOU 3215  O   ALA A 282    12896  14777  12368   1528    614   4235       O  
ATOM   3216  CB  ALA A 282       2.531   5.179 -47.458  1.00108.19           C  
ANISOU 3216  CB  ALA A 282    13451  15583  12075   1803    342   4613       C  
ATOM   3217  N   PHE A 283       0.528   4.239 -45.095  1.00106.37           N  
ANISOU 3217  N   PHE A 283    12575  15417  12424   1750    165   4496       N  
ATOM   3218  CA  PHE A 283      -0.272   4.560 -43.913  1.00106.77           C  
ANISOU 3218  CA  PHE A 283    12428  15393  12746   1910    329   4605       C  
ATOM   3219  C   PHE A 283      -0.174   3.483 -42.822  1.00109.56           C  
ANISOU 3219  C   PHE A 283    12624  15738  13265   1644    284   4336       C  
ATOM   3220  O   PHE A 283      -0.445   3.769 -41.652  1.00109.15           O  
ANISOU 3220  O   PHE A 283    12537  15539  13395   1755    521   4348       O  
ATOM   3221  CB  PHE A 283      -1.727   4.872 -44.297  1.00112.72           C  
ANISOU 3221  CB  PHE A 283    12818  16473  13536   2222    195   5031       C  
ATOM   3222  CG  PHE A 283      -1.874   5.986 -45.311  1.00117.65           C  
ANISOU 3222  CG  PHE A 283    13600  17104  13997   2550    265   5354       C  
ATOM   3223  CD1 PHE A 283      -1.635   7.310 -44.956  1.00121.78           C  
ANISOU 3223  CD1 PHE A 283    14471  17227  14573   2874    690   5486       C  
ATOM   3224  CD2 PHE A 283      -2.274   5.715 -46.612  1.00122.74           C  
ANISOU 3224  CD2 PHE A 283    14110  18122  14402   2527   -109   5536       C  
ATOM   3225  CE1 PHE A 283      -1.769   8.339 -45.894  1.00126.19           C  
ANISOU 3225  CE1 PHE A 283    15209  17752  14987   3191    775   5820       C  
ATOM   3226  CE2 PHE A 283      -2.410   6.745 -47.550  1.00128.93           C  
ANISOU 3226  CE2 PHE A 283    15038  18934  15016   2856    -38   5874       C  
ATOM   3227  CZ  PHE A 283      -2.159   8.049 -47.184  1.00127.73           C  
ANISOU 3227  CZ  PHE A 283    15195  18376  14959   3200    421   6030       C  
ATOM   3228  N   CYS A 284       0.229   2.254 -43.206  1.00105.50           N  
ANISOU 3228  N   CYS A 284    12088  15348  12649   1331      8   4099       N  
ATOM   3229  CA  CYS A 284       0.451   1.133 -42.290  1.00103.25           C  
ANISOU 3229  CA  CYS A 284    11711  15025  12494   1070    -43   3851       C  
ATOM   3230  C   CYS A 284       1.825   1.289 -41.657  1.00104.28           C  
ANISOU 3230  C   CYS A 284    12111  14879  12630    976    230   3618       C  
ATOM   3231  O   CYS A 284       2.006   0.945 -40.491  1.00102.15           O  
ANISOU 3231  O   CYS A 284    11790  14507  12513    876    339   3495       O  
ATOM   3232  CB  CYS A 284       0.329  -0.200 -43.021  1.00104.58           C  
ANISOU 3232  CB  CYS A 284    11870  15354  12512    808   -438   3711       C  
ATOM   3233  SG  CYS A 284      -1.358  -0.611 -43.524  1.00113.22           S  
ANISOU 3233  SG  CYS A 284    12556  16824  13638    715   -902   4023       S  
ATOM   3234  N   SER A 285       2.788   1.822 -42.437  1.00101.03           N  
ANISOU 3234  N   SER A 285    11954  14392  12042    994    328   3614       N  
ATOM   3235  CA  SER A 285       4.168   2.096 -42.038  1.00 99.24           C  
ANISOU 3235  CA  SER A 285    11910  13988  11810    857    547   3514       C  
ATOM   3236  C   SER A 285       4.224   3.135 -40.907  1.00104.09           C  
ANISOU 3236  C   SER A 285    12645  14325  12580    849    767   3553       C  
ATOM   3237  O   SER A 285       5.145   3.106 -40.090  1.00102.85           O  
ANISOU 3237  O   SER A 285    12566  14043  12469    630    856   3441       O  
ATOM   3238  CB  SER A 285       4.976   2.568 -43.241  1.00103.51           C  
ANISOU 3238  CB  SER A 285    12626  14569  12132    904    612   3633       C  
ATOM   3239  OG  SER A 285       4.952   1.596 -44.274  1.00111.31           O  
ANISOU 3239  OG  SER A 285    13639  15770  12884    955    431   3561       O  
ATOM   3240  N   MET A 286       3.207   4.016 -40.841  1.00103.05           N  
ANISOU 3240  N   MET A 286    12558  14101  12497   1110    847   3727       N  
ATOM   3241  CA  MET A 286       3.037   5.051 -39.816  1.00104.22           C  
ANISOU 3241  CA  MET A 286    12973  13908  12719   1215   1090   3759       C  
ATOM   3242  C   MET A 286       2.747   4.428 -38.436  1.00106.94           C  
ANISOU 3242  C   MET A 286    13219  14240  13173   1166   1131   3599       C  
ATOM   3243  O   MET A 286       3.006   5.076 -37.422  1.00107.36           O  
ANISOU 3243  O   MET A 286    13605  13978  13209   1144   1311   3519       O  
ATOM   3244  CB  MET A 286       1.887   6.006 -40.197  1.00110.01           C  
ANISOU 3244  CB  MET A 286    13760  14590  13450   1655   1214   4047       C  
ATOM   3245  CG  MET A 286       2.059   6.681 -41.549  1.00115.58           C  
ANISOU 3245  CG  MET A 286    14577  15313  14026   1753   1184   4257       C  
ATOM   3246  SD  MET A 286       3.039   8.194 -41.493  1.00121.97           S  
ANISOU 3246  SD  MET A 286    16006  15568  14770   1659   1437   4319       S  
ATOM   3247  CE  MET A 286       1.772   9.371 -41.092  1.00123.01           C  
ANISOU 3247  CE  MET A 286    16424  15391  14924   2240   1726   4567       C  
ATOM   3248  N   LEU A 287       2.192   3.186 -38.403  1.00101.98           N  
ANISOU 3248  N   LEU A 287    12193  13927  12629   1130    952   3562       N  
ATOM   3249  CA  LEU A 287       1.848   2.449 -37.177  1.00100.40           C  
ANISOU 3249  CA  LEU A 287    11836  13771  12540   1084    986   3469       C  
ATOM   3250  C   LEU A 287       3.053   2.044 -36.362  1.00101.13           C  
ANISOU 3250  C   LEU A 287    12084  13738  12603    773    996   3229       C  
ATOM   3251  O   LEU A 287       2.953   2.012 -35.138  1.00100.62           O  
ANISOU 3251  O   LEU A 287    12100  13575  12557    777   1119   3161       O  
ATOM   3252  CB  LEU A 287       1.008   1.206 -37.472  1.00100.31           C  
ANISOU 3252  CB  LEU A 287    11384  14095  12633   1032    744   3538       C  
ATOM   3253  CG  LEU A 287      -0.403   1.440 -37.950  1.00108.51           C  
ANISOU 3253  CG  LEU A 287    12109  15376  13744   1294    685   3869       C  
ATOM   3254  CD1 LEU A 287      -0.902   0.241 -38.711  1.00109.47           C  
ANISOU 3254  CD1 LEU A 287    11903  15798  13892   1049    285   3911       C  
ATOM   3255  CD2 LEU A 287      -1.329   1.773 -36.793  1.00113.29           C  
ANISOU 3255  CD2 LEU A 287    12569  16004  14473   1591    962   4073       C  
ATOM   3256  N   CYS A 288       4.180   1.710 -37.027  1.00 96.07           N  
ANISOU 3256  N   CYS A 288    11464  13145  11892    540    881   3146       N  
ATOM   3257  CA  CYS A 288       5.433   1.335 -36.365  1.00 94.48           C  
ANISOU 3257  CA  CYS A 288    11316  12917  11666    256    875   3018       C  
ATOM   3258  C   CYS A 288       5.891   2.494 -35.488  1.00100.34           C  
ANISOU 3258  C   CYS A 288    12416  13365  12345    132    995   3003       C  
ATOM   3259  O   CYS A 288       6.299   2.279 -34.346  1.00 99.58           O  
ANISOU 3259  O   CYS A 288    12392  13218  12225    -40    992   2901       O  
ATOM   3260  CB  CYS A 288       6.497   0.955 -37.389  1.00 94.24           C  
ANISOU 3260  CB  CYS A 288    11215  13038  11556    144    808   3049       C  
ATOM   3261  SG  CYS A 288       6.031  -0.426 -38.461  1.00 97.62           S  
ANISOU 3261  SG  CYS A 288    11460  13693  11939    283    646   2999       S  
ATOM   3262  N   LEU A 289       5.752   3.726 -36.018  1.00 99.45           N  
ANISOU 3262  N   LEU A 289    12590  13024  12173    221   1086   3110       N  
ATOM   3263  CA  LEU A 289       6.055   4.990 -35.354  1.00102.17           C  
ANISOU 3263  CA  LEU A 289    13449  12955  12415    104   1187   3094       C  
ATOM   3264  C   LEU A 289       5.123   5.180 -34.134  1.00108.38           C  
ANISOU 3264  C   LEU A 289    14484  13543  13153    357   1352   2996       C  
ATOM   3265  O   LEU A 289       5.599   5.586 -33.073  1.00109.62           O  
ANISOU 3265  O   LEU A 289    15049  13434  13169    147   1362   2862       O  
ATOM   3266  CB  LEU A 289       5.881   6.135 -36.372  1.00104.57           C  
ANISOU 3266  CB  LEU A 289    14004  13045  12682    245   1277   3273       C  
ATOM   3267  CG  LEU A 289       6.488   7.493 -36.042  1.00112.79           C  
ANISOU 3267  CG  LEU A 289    15664  13584  13608      1   1331   3294       C  
ATOM   3268  CD1 LEU A 289       7.957   7.545 -36.425  1.00113.30           C  
ANISOU 3268  CD1 LEU A 289    15637  13739  13674   -542   1155   3393       C  
ATOM   3269  CD2 LEU A 289       5.774   8.578 -36.796  1.00118.12           C  
ANISOU 3269  CD2 LEU A 289    16652  13975  14252    359   1511   3476       C  
ATOM   3270  N   ILE A 290       3.818   4.845 -34.280  1.00105.60           N  
ANISOU 3270  N   ILE A 290    13871  13362  12891    793   1470   3099       N  
ATOM   3271  CA  ILE A 290       2.796   4.937 -33.223  1.00107.77           C  
ANISOU 3271  CA  ILE A 290    14260  13557  13130   1151   1705   3114       C  
ATOM   3272  C   ILE A 290       3.098   3.925 -32.107  1.00111.90           C  
ANISOU 3272  C   ILE A 290    14636  14232  13648    942   1638   2958       C  
ATOM   3273  O   ILE A 290       2.986   4.264 -30.928  1.00113.73           O  
ANISOU 3273  O   ILE A 290    15254  14246  13712   1032   1807   2865       O  
ATOM   3274  CB  ILE A 290       1.355   4.777 -33.803  1.00111.98           C  
ANISOU 3274  CB  ILE A 290    14374  14368  13805   1629   1812   3399       C  
ATOM   3275  CG1 ILE A 290       1.014   5.918 -34.788  1.00115.21           C  
ANISOU 3275  CG1 ILE A 290    14989  14606  14177   1918   1917   3602       C  
ATOM   3276  CG2 ILE A 290       0.293   4.687 -32.694  1.00114.86           C  
ANISOU 3276  CG2 ILE A 290    14697  14782  14162   2032   2100   3516       C  
ATOM   3277  CD1 ILE A 290      -0.039   5.561 -35.865  1.00122.85           C  
ANISOU 3277  CD1 ILE A 290    15383  16004  15291   2184   1816   3919       C  
ATOM   3278  N   ASN A 291       3.487   2.693 -32.492  1.00106.44           N  
ANISOU 3278  N   ASN A 291    13460  13884  13100    695   1407   2935       N  
ATOM   3279  CA  ASN A 291       3.846   1.581 -31.606  1.00104.69           C  
ANISOU 3279  CA  ASN A 291    13044  13832  12902    499   1322   2834       C  
ATOM   3280  C   ASN A 291       5.001   1.973 -30.675  1.00109.95           C  
ANISOU 3280  C   ASN A 291    14102  14301  13373    178   1270   2674       C  
ATOM   3281  O   ASN A 291       4.892   1.789 -29.464  1.00110.28           O  
ANISOU 3281  O   ASN A 291    14302  14303  13295    194   1345   2604       O  
ATOM   3282  CB  ASN A 291       4.208   0.352 -32.447  1.00101.86           C  
ANISOU 3282  CB  ASN A 291    12246  13765  12693    324   1098   2843       C  
ATOM   3283  CG  ASN A 291       5.013  -0.689 -31.728  1.00118.28           C  
ANISOU 3283  CG  ASN A 291    14204  15962  14775     90   1000   2756       C  
ATOM   3284  OD1 ASN A 291       4.519  -1.378 -30.825  1.00109.30           O  
ANISOU 3284  OD1 ASN A 291    12953  14898  13679    146   1052   2767       O  
ATOM   3285  ND2 ASN A 291       6.279  -0.806 -32.114  1.00108.11           N  
ANISOU 3285  ND2 ASN A 291    12912  14724  13440   -145    883   2728       N  
ATOM   3286  N   SER A 292       6.077   2.554 -31.248  1.00107.37           N  
ANISOU 3286  N   SER A 292    13929  13874  12994   -131   1129   2662       N  
ATOM   3287  CA  SER A 292       7.276   3.023 -30.546  1.00109.10           C  
ANISOU 3287  CA  SER A 292    14467  13949  13038   -568    979   2590       C  
ATOM   3288  C   SER A 292       7.004   4.220 -29.628  1.00116.39           C  
ANISOU 3288  C   SER A 292    16126  14401  13696   -554   1086   2466       C  
ATOM   3289  O   SER A 292       7.819   4.521 -28.756  1.00118.08           O  
ANISOU 3289  O   SER A 292    16692  14474  13698   -948    916   2372       O  
ATOM   3290  CB  SER A 292       8.361   3.380 -31.554  1.00114.27           C  
ANISOU 3290  CB  SER A 292    15012  14662  13743   -889    825   2719       C  
ATOM   3291  OG  SER A 292       8.825   2.210 -32.207  1.00124.39           O  
ANISOU 3291  OG  SER A 292    15730  16357  15176   -883    754   2816       O  
ATOM   3292  N   MET A 293       5.875   4.910 -29.852  1.00114.31           N  
ANISOU 3292  N   MET A 293    16126  13891  13415    -91   1360   2490       N  
ATOM   3293  CA  MET A 293       5.409   6.066 -29.091  1.00118.58           C  
ANISOU 3293  CA  MET A 293    17471  13912  13672    118   1576   2386       C  
ATOM   3294  C   MET A 293       4.517   5.582 -27.935  1.00122.64           C  
ANISOU 3294  C   MET A 293    18036  14501  14061    518   1823   2339       C  
ATOM   3295  O   MET A 293       4.620   6.108 -26.829  1.00125.97           O  
ANISOU 3295  O   MET A 293    19149  14580  14133    504   1898   2169       O  
ATOM   3296  CB  MET A 293       4.664   7.036 -30.042  1.00122.91           C  
ANISOU 3296  CB  MET A 293    18220  14202  14279    521   1804   2531       C  
ATOM   3297  CG  MET A 293       3.948   8.184 -29.363  1.00132.07           C  
ANISOU 3297  CG  MET A 293    20232  14799  15149    956   2147   2474       C  
ATOM   3298  SD  MET A 293       2.156   8.012 -29.525  1.00137.05           S  
ANISOU 3298  SD  MET A 293    20482  15678  15913   1891   2617   2760       S  
ATOM   3299  CE  MET A 293       1.617   8.950 -28.115  1.00140.34           C  
ANISOU 3299  CE  MET A 293    21951  15505  15865   2386   3059   2626       C  
ATOM   3300  N   VAL A 294       3.669   4.567 -28.191  1.00116.18           N  
ANISOU 3300  N   VAL A 294    16518  14127  13500    835   1930   2507       N  
ATOM   3301  CA  VAL A 294       2.731   3.986 -27.223  1.00116.94           C  
ANISOU 3301  CA  VAL A 294    16486  14395  13549   1223   2190   2579       C  
ATOM   3302  C   VAL A 294       3.452   3.147 -26.139  1.00120.18           C  
ANISOU 3302  C   VAL A 294    16883  14953  13829    878   2018   2438       C  
ATOM   3303  O   VAL A 294       3.118   3.278 -24.960  1.00122.22           O  
ANISOU 3303  O   VAL A 294    17545  15092  13801   1093   2231   2381       O  
ATOM   3304  CB  VAL A 294       1.599   3.207 -27.956  1.00119.06           C  
ANISOU 3304  CB  VAL A 294    15972  15098  14169   1554   2285   2879       C  
ATOM   3305  CG1 VAL A 294       0.857   2.244 -27.031  1.00119.07           C  
ANISOU 3305  CG1 VAL A 294    15619  15407  14216   1755   2450   3023       C  
ATOM   3306  CG2 VAL A 294       0.617   4.170 -28.614  1.00121.93           C  
ANISOU 3306  CG2 VAL A 294    16428  15339  14561   2067   2557   3097       C  
ATOM   3307  N   ASN A 295       4.430   2.305 -26.539  1.00114.15           N  
ANISOU 3307  N   ASN A 295    15682  14452  13238    408   1668   2414       N  
ATOM   3308  CA  ASN A 295       5.201   1.428 -25.644  1.00113.43           C  
ANISOU 3308  CA  ASN A 295    15477  14562  13059     95   1479   2354       C  
ATOM   3309  C   ASN A 295       5.807   2.147 -24.401  1.00122.44           C  
ANISOU 3309  C   ASN A 295    17360  15415  13748   -121   1413   2166       C  
ATOM   3310  O   ASN A 295       5.566   1.643 -23.303  1.00123.32           O  
ANISOU 3310  O   ASN A 295    17551  15627  13677     -2   1509   2156       O  
ATOM   3311  CB  ASN A 295       6.275   0.635 -26.405  1.00110.87           C  
ANISOU 3311  CB  ASN A 295    14650  14519  12958   -299   1160   2405       C  
ATOM   3312  CG  ASN A 295       5.759  -0.399 -27.393  1.00131.80           C  
ANISOU 3312  CG  ASN A 295    16678  17445  15957   -131   1174   2542       C  
ATOM   3313  OD1 ASN A 295       6.522  -0.933 -28.201  1.00127.39           O  
ANISOU 3313  OD1 ASN A 295    15817  17049  15538   -325    995   2580       O  
ATOM   3314  ND2 ASN A 295       4.465  -0.716 -27.373  1.00121.85           N  
ANISOU 3314  ND2 ASN A 295    15230  16248  14820    222   1380   2647       N  
ATOM   3315  N   PRO A 296       6.512   3.316 -24.488  1.00122.53           N  
ANISOU 3315  N   PRO A 296    17978  15044  13534   -443   1249   2028       N  
ATOM   3316  CA  PRO A 296       7.023   3.954 -23.257  1.00127.08           C  
ANISOU 3316  CA  PRO A 296    19362  15308  13616   -712   1120   1829       C  
ATOM   3317  C   PRO A 296       5.943   4.573 -22.368  1.00134.85           C  
ANISOU 3317  C   PRO A 296    21088  15919  14229   -154   1540   1706       C  
ATOM   3318  O   PRO A 296       6.231   4.892 -21.217  1.00138.38           O  
ANISOU 3318  O   PRO A 296    22245  16137  14195   -293   1470   1523       O  
ATOM   3319  CB  PRO A 296       8.001   5.019 -23.773  1.00131.52           C  
ANISOU 3319  CB  PRO A 296    20344  15534  14094  -1269    802   1767       C  
ATOM   3320  CG  PRO A 296       8.182   4.735 -25.226  1.00131.97           C  
ANISOU 3320  CG  PRO A 296    19672  15854  14616  -1294    766   1969       C  
ATOM   3321  CD  PRO A 296       6.918   4.094 -25.672  1.00124.22           C  
ANISOU 3321  CD  PRO A 296    18222  15078  13899   -639   1136   2064       C  
ATOM   3322  N   VAL A 297       4.712   4.743 -22.893  1.00131.24           N  
ANISOU 3322  N   VAL A 297    20478  15428  13960    498   1979   1841       N  
ATOM   3323  CA  VAL A 297       3.569   5.268 -22.135  1.00135.83           C  
ANISOU 3323  CA  VAL A 297    21634  15746  14228   1198   2498   1840       C  
ATOM   3324  C   VAL A 297       3.015   4.124 -21.248  1.00139.30           C  
ANISOU 3324  C   VAL A 297    21619  16640  14669   1473   2692   1987       C  
ATOM   3325  O   VAL A 297       2.586   4.381 -20.118  1.00143.48           O  
ANISOU 3325  O   VAL A 297    22767  16997  14751   1837   2998   1923       O  
ATOM   3326  CB  VAL A 297       2.488   5.933 -23.043  1.00140.73           C  
ANISOU 3326  CB  VAL A 297    22186  16227  15056   1816   2897   2038       C  
ATOM   3327  CG1 VAL A 297       1.336   6.514 -22.223  1.00146.30           C  
ANISOU 3327  CG1 VAL A 297    23489  16688  15411   2646   3511   2113       C  
ATOM   3328  CG2 VAL A 297       3.100   7.018 -23.927  1.00141.58           C  
ANISOU 3328  CG2 VAL A 297    22746  15878  15169   1511   2697   1925       C  
ATOM   3329  N   ILE A 298       3.076   2.863 -21.750  1.00130.81           N  
ANISOU 3329  N   ILE A 298    19541  16103  14056   1285   2513   2184       N  
ATOM   3330  CA  ILE A 298       2.660   1.646 -21.034  1.00129.54           C  
ANISOU 3330  CA  ILE A 298    18871  16372  13978   1426   2628   2369       C  
ATOM   3331  C   ILE A 298       3.570   1.457 -19.805  1.00136.95           C  
ANISOU 3331  C   ILE A 298    20282  17273  14480   1083   2408   2177       C  
ATOM   3332  O   ILE A 298       3.064   1.211 -18.708  1.00139.44           O  
ANISOU 3332  O   ILE A 298    20827  17656  14498   1409   2690   2236       O  
ATOM   3333  CB  ILE A 298       2.647   0.396 -21.970  1.00126.83           C  
ANISOU 3333  CB  ILE A 298    17510  16476  14202   1217   2418   2582       C  
ATOM   3334  CG1 ILE A 298       1.703   0.605 -23.174  1.00126.04           C  
ANISOU 3334  CG1 ILE A 298    16982  16441  14468   1513   2568   2785       C  
ATOM   3335  CG2 ILE A 298       2.284  -0.889 -21.201  1.00126.66           C  
ANISOU 3335  CG2 ILE A 298    17031  16823  14272   1287   2507   2789       C  
ATOM   3336  CD1 ILE A 298       2.009  -0.250 -24.381  1.00127.64           C  
ANISOU 3336  CD1 ILE A 298    16496  16894  15105   1178   2237   2856       C  
ATOM   3337  N   TYR A 299       4.903   1.617 -19.993  1.00133.91           N  
ANISOU 3337  N   TYR A 299    20032  16816  14033    434   1909   1997       N  
ATOM   3338  CA  TYR A 299       5.910   1.529 -18.931  1.00136.93           C  
ANISOU 3338  CA  TYR A 299    20828  17206  13992     -8   1575   1856       C  
ATOM   3339  C   TYR A 299       5.764   2.686 -17.939  1.00148.53           C  
ANISOU 3339  C   TYR A 299    23483  18163  14788    114   1702   1592       C  
ATOM   3340  O   TYR A 299       6.050   2.515 -16.755  1.00151.43           O  
ANISOU 3340  O   TYR A 299    24291  18560  14687     19   1614   1507       O  
ATOM   3341  CB  TYR A 299       7.327   1.537 -19.520  1.00136.96           C  
ANISOU 3341  CB  TYR A 299    20594  17308  14137   -729   1015   1834       C  
ATOM   3342  CG  TYR A 299       7.734   0.257 -20.223  1.00134.18           C  
ANISOU 3342  CG  TYR A 299    19228  17460  14293   -850    869   2078       C  
ATOM   3343  CD1 TYR A 299       8.089  -0.876 -19.496  1.00135.61           C  
ANISOU 3343  CD1 TYR A 299    19046  18022  14459   -913    767   2223       C  
ATOM   3344  CD2 TYR A 299       7.855   0.210 -21.608  1.00131.53           C  
ANISOU 3344  CD2 TYR A 299    18395  17185  14396   -900    826   2163       C  
ATOM   3345  CE1 TYR A 299       8.497  -2.047 -20.137  1.00132.61           C  
ANISOU 3345  CE1 TYR A 299    17864  18016  14505   -971    665   2442       C  
ATOM   3346  CE2 TYR A 299       8.266  -0.954 -22.259  1.00128.56           C  
ANISOU 3346  CE2 TYR A 299    17245  17199  14405   -964    718   2357       C  
ATOM   3347  CZ  TYR A 299       8.588  -2.080 -21.518  1.00135.68           C  
ANISOU 3347  CZ  TYR A 299    17839  18419  15295   -988    648   2490       C  
ATOM   3348  OH  TYR A 299       8.991  -3.230 -22.154  1.00133.31           O  
ANISOU 3348  OH  TYR A 299    16894  18418  15340   -987    584   2678       O  
ATOM   3349  N   ALA A 300       5.310   3.857 -18.423  1.00148.66           N  
ANISOU 3349  N   ALA A 300    24083  17683  14718    353   1917   1467       N  
ATOM   3350  CA  ALA A 300       5.093   5.052 -17.608  1.00156.37           C  
ANISOU 3350  CA  ALA A 300    26355  18030  15029    556   2101   1192       C  
ATOM   3351  C   ALA A 300       3.817   4.962 -16.760  1.00165.17           C  
ANISOU 3351  C   ALA A 300    27762  19143  15853   1446   2774   1285       C  
ATOM   3352  O   ALA A 300       3.605   5.818 -15.900  1.00171.84           O  
ANISOU 3352  O   ALA A 300    29774  19478  16038   1728   3001   1056       O  
ATOM   3353  CB  ALA A 300       5.049   6.289 -18.493  1.00159.06           C  
ANISOU 3353  CB  ALA A 300    27210  17809  15415    555   2138   1080       C  
ATOM   3354  N   LEU A 301       2.973   3.934 -16.994  1.00158.89           N  
ANISOU 3354  N   LEU A 301    25950  18901  15519   1880   3097   1646       N  
ATOM   3355  CA  LEU A 301       1.721   3.745 -16.259  1.00162.71           C  
ANISOU 3355  CA  LEU A 301    26484  19519  15819   2722   3765   1877       C  
ATOM   3356  C   LEU A 301       1.652   2.452 -15.438  1.00166.19           C  
ANISOU 3356  C   LEU A 301    26351  20508  16286   2709   3784   2095       C  
ATOM   3357  O   LEU A 301       1.123   2.484 -14.325  1.00170.65           O  
ANISOU 3357  O   LEU A 301    27421  21061  16359   3201   4199   2145       O  
ATOM   3358  CB  LEU A 301       0.505   3.849 -17.195  1.00161.71           C  
ANISOU 3358  CB  LEU A 301    25725  19542  16176   3352   4232   2235       C  
ATOM   3359  CG  LEU A 301       0.020   5.262 -17.511  1.00171.49           C  
ANISOU 3359  CG  LEU A 301    27795  20198  17164   3865   4593   2141       C  
ATOM   3360  CD1 LEU A 301      -0.579   5.328 -18.897  1.00168.38           C  
ANISOU 3360  CD1 LEU A 301    26590  19992  17395   4044   4663   2438       C  
ATOM   3361  CD2 LEU A 301      -0.986   5.754 -16.473  1.00181.65           C  
ANISOU 3361  CD2 LEU A 301    29810  21306  17901   4811   5339   2258       C  
ATOM   3362  N   ARG A 302       2.152   1.320 -15.979  1.00157.47           N  
ANISOU 3362  N   ARG A 302    24251  19858  15724   2209   3387   2246       N  
ATOM   3363  CA  ARG A 302       2.093   0.044 -15.261  1.00156.50           C  
ANISOU 3363  CA  ARG A 302    23583  20209  15670   2189   3405   2490       C  
ATOM   3364  C   ARG A 302       3.266  -0.170 -14.313  1.00163.23           C  
ANISOU 3364  C   ARG A 302    24893  21067  16060   1683   2968   2273       C  
ATOM   3365  O   ARG A 302       3.031  -0.391 -13.123  1.00167.00           O  
ANISOU 3365  O   ARG A 302    25756  21629  16068   1947   3193   2326       O  
ATOM   3366  CB  ARG A 302       1.919  -1.157 -16.208  1.00150.27           C  
ANISOU 3366  CB  ARG A 302    21600  19856  15640   1998   3263   2798       C  
ATOM   3367  CG  ARG A 302       1.591  -2.456 -15.458  1.00160.61           C  
ANISOU 3367  CG  ARG A 302    22391  21587  17048   2084   3397   3126       C  
ATOM   3368  CD  ARG A 302       0.889  -3.482 -16.319  1.00168.04           C  
ANISOU 3368  CD  ARG A 302    22316  22851  18682   2084   3441   3495       C  
ATOM   3369  NE  ARG A 302      -0.440  -3.026 -16.721  1.00179.66           N  
ANISOU 3369  NE  ARG A 302    23565  24366  20331   2608   3894   3765       N  
ATOM   3370  CZ  ARG A 302      -1.582  -3.596 -16.353  1.00194.48           C  
ANISOU 3370  CZ  ARG A 302    24949  26570  22374   2986   4306   4242       C  
ATOM   3371  NH1 ARG A 302      -1.574  -4.681 -15.587  1.00181.29           N  
ANISOU 3371  NH1 ARG A 302    22997  25159  20727   2879   4328   4476       N  
ATOM   3372  NH2 ARG A 302      -2.740  -3.097 -16.761  1.00182.43           N  
ANISOU 3372  NH2 ARG A 302    23162  25145  21010   3470   4699   4552       N  
ATOM   3373  N   SER A 303       4.511  -0.142 -14.839  1.00157.78           N  
ANISOU 3373  N   SER A 303    24100  20352  15499    977   2355   2097       N  
ATOM   3374  CA  SER A 303       5.739  -0.369 -14.072  1.00159.57           C  
ANISOU 3374  CA  SER A 303    24591  20685  15353    405   1838   1982       C  
ATOM   3375  C   SER A 303       5.763   0.452 -12.781  1.00171.78           C  
ANISOU 3375  C   SER A 303    27341  21899  16028    498   1892   1724       C  
ATOM   3376  O   SER A 303       5.872   1.681 -12.831  1.00175.61           O  
ANISOU 3376  O   SER A 303    28725  21853  16144    416   1837   1415       O  
ATOM   3377  CB  SER A 303       6.972  -0.106 -14.932  1.00160.68           C  
ANISOU 3377  CB  SER A 303    24520  20803  15729   -302   1244   1881       C  
ATOM   3378  OG  SER A 303       8.176  -0.378 -14.233  1.00171.34           O  
ANISOU 3378  OG  SER A 303    25963  22369  16769   -874    710   1882       O  
ATOM   3379  N   GLU A 304       5.571  -0.238 -11.633  1.00170.89           N  
ANISOU 3379  N   GLU A 304    27308  22059  15562    722   2045   1862       N  
ATOM   3380  CA  GLU A 304       5.537   0.376 -10.305  1.00178.45           C  
ANISOU 3380  CA  GLU A 304    29445  22753  15604    881   2133   1639       C  
ATOM   3381  C   GLU A 304       6.891   0.962  -9.921  1.00185.98           C  
ANISOU 3381  C   GLU A 304    31094  23519  16051     53   1371   1336       C  
ATOM   3382  O   GLU A 304       6.923   2.046  -9.346  1.00192.26           O  
ANISOU 3382  O   GLU A 304    33143  23780  16128     29   1335    983       O  
ATOM   3383  CB  GLU A 304       5.024  -0.600  -9.230  1.00181.47           C  
ANISOU 3383  CB  GLU A 304    29643  23548  15758   1316   2483   1930       C  
ATOM   3384  CG  GLU A 304       4.468   0.110  -8.005  1.00200.26           C  
ANISOU 3384  CG  GLU A 304    33270  25613  17206   1845   2897   1748       C  
ATOM   3385  CD  GLU A 304       4.035  -0.784  -6.861  1.00221.32           C  
ANISOU 3385  CD  GLU A 304    35849  28697  19547   2265   3244   2055       C  
ATOM   3386  OE1 GLU A 304       2.954  -1.405  -6.966  1.00214.77           O  
ANISOU 3386  OE1 GLU A 304    34334  28150  19121   2885   3875   2461       O  
ATOM   3387  OE2 GLU A 304       4.775  -0.858  -5.853  1.00218.89           O  
ANISOU 3387  OE2 GLU A 304    36149  28452  18566   1944   2864   1928       O  
ATOM   3388  N   GLU A 305       7.999   0.269 -10.262  1.00179.03           N  
ANISOU 3388  N   GLU A 305    29427  23063  15534   -620    764   1506       N  
ATOM   3389  CA  GLU A 305       9.357   0.743  -9.982  1.00182.89           C  
ANISOU 3389  CA  GLU A 305    30332  23518  15640  -1501    -33   1356       C  
ATOM   3390  C   GLU A 305       9.694   2.009 -10.773  1.00189.09           C  
ANISOU 3390  C   GLU A 305    31648  23752  16445  -1923   -285   1072       C  
ATOM   3391  O   GLU A 305      10.417   2.862 -10.262  1.00195.21           O  
ANISOU 3391  O   GLU A 305    33351  24202  16618  -2532   -803    822       O  
ATOM   3392  CB  GLU A 305      10.400  -0.357 -10.212  1.00180.35           C  
ANISOU 3392  CB  GLU A 305    28898  23867  15758  -1984   -519   1731       C  
ATOM   3393  CG  GLU A 305      10.599  -1.247  -8.998  1.00192.28           C  
ANISOU 3393  CG  GLU A 305    30370  25822  16865  -1915   -608   1941       C  
ATOM   3394  CD  GLU A 305      11.879  -2.057  -9.000  1.00207.02           C  
ANISOU 3394  CD  GLU A 305    31421  28299  18938  -2486  -1222   2301       C  
ATOM   3395  OE1 GLU A 305      11.966  -3.034  -9.778  1.00191.39           O  
ANISOU 3395  OE1 GLU A 305    28360  26675  17683  -2324  -1086   2628       O  
ATOM   3396  OE2 GLU A 305      12.794  -1.722  -8.214  1.00203.41           O  
ANISOU 3396  OE2 GLU A 305    31432  27967  17888  -3082  -1842   2282       O  
ATOM   3397  N   ILE A 306       9.143   2.140 -11.998  1.00181.34           N  
ANISOU 3397  N   ILE A 306    30133  22646  16122  -1620     65   1124       N  
ATOM   3398  CA  ILE A 306       9.313   3.314 -12.859  1.00182.80           C  
ANISOU 3398  CA  ILE A 306    30764  22296  16397  -1903    -63    910       C  
ATOM   3399  C   ILE A 306       8.440   4.476 -12.343  1.00194.04           C  
ANISOU 3399  C   ILE A 306    33567  22965  17195  -1413    366    551       C  
ATOM   3400  O   ILE A 306       8.928   5.607 -12.259  1.00199.28           O  
ANISOU 3400  O   ILE A 306    35255  23037  17424  -1890     27    254       O  
ATOM   3401  CB  ILE A 306       9.103   2.954 -14.361  1.00178.25           C  
ANISOU 3401  CB  ILE A 306    29090  21925  16711  -1753    123   1137       C  
ATOM   3402  CG1 ILE A 306      10.407   2.372 -14.954  1.00175.66           C  
ANISOU 3402  CG1 ILE A 306    27850  22094  16798  -2475   -474   1392       C  
ATOM   3403  CG2 ILE A 306       8.586   4.142 -15.197  1.00179.86           C  
ANISOU 3403  CG2 ILE A 306    29825  21514  16998  -1567    370    946       C  
ATOM   3404  CD1 ILE A 306      10.248   1.535 -16.222  1.00176.66           C  
ANISOU 3404  CD1 ILE A 306    26793  22595  17733  -2238   -271   1670       C  
ATOM   3405  N   ARG A 307       7.170   4.187 -11.969  1.00190.79           N  
ANISOU 3405  N   ARG A 307    33204  22571  16717   -464   1117    618       N  
ATOM   3406  CA  ARG A 307       6.229   5.175 -11.426  1.00197.35           C  
ANISOU 3406  CA  ARG A 307    35290  22757  16936    227   1684    365       C  
ATOM   3407  C   ARG A 307       6.651   5.679 -10.040  1.00209.85           C  
ANISOU 3407  C   ARG A 307    37900  24168  17665      1   1395     30       C  
ATOM   3408  O   ARG A 307       6.381   6.835  -9.719  1.00211.03           O  
ANISOU 3408  O   ARG A 307    37895  24329  17957    176   1408   -320       O  
ATOM   3409  CB  ARG A 307       4.789   4.642 -11.406  1.00194.62           C  
ANISOU 3409  CB  ARG A 307    34432  22676  16840   1305   2562    664       C  
ATOM   3410  CG  ARG A 307       4.128   4.631 -12.777  1.00194.88           C  
ANISOU 3410  CG  ARG A 307    33557  22798  17690   1629   2871    903       C  
ATOM   3411  CD  ARG A 307       2.654   4.985 -12.710  1.00202.60           C  
ANISOU 3411  CD  ARG A 307    34740  23636  18602   2723   3756   1078       C  
ATOM   3412  NE  ARG A 307       2.430   6.432 -12.680  1.00210.69           N  
ANISOU 3412  NE  ARG A 307    36560  24112  19381   2856   3817    731       N  
ATOM   3413  CZ  ARG A 307       1.253   7.017 -12.893  1.00217.10           C  
ANISOU 3413  CZ  ARG A 307    36184  25394  20909   3164   3980    732       C  
ATOM   3414  NH1 ARG A 307       0.179   6.285 -13.165  1.00205.69           N  
ANISOU 3414  NH1 ARG A 307    35062  23838  19251   4362   5023   1350       N  
ATOM   3415  NH2 ARG A 307       1.144   8.337 -12.846  1.00208.45           N  
ANISOU 3415  NH2 ARG A 307    36197  23590  19414   3434   4160    447       N  
ATOM   3416  N   SER A 308       7.318   4.820  -9.230  1.00208.76           N  
ANISOU 3416  N   SER A 308    37837  24364  17120   -412   1014    138       N  
ATOM   3417  CA  SER A 308       7.834   5.183  -7.904  1.00211.84           C  
ANISOU 3417  CA  SER A 308    37948  25283  17259   -630    577   -148       C  
ATOM   3418  C   SER A 308       9.086   6.048  -8.059  1.00216.04           C  
ANISOU 3418  C   SER A 308    37832  26048  18205  -1388   -233   -428       C  
ATOM   3419  O   SER A 308       9.317   6.937  -7.237  1.00217.58           O  
ANISOU 3419  O   SER A 308    37831  26478  18363  -1352   -419   -831       O  
ATOM   3420  CB  SER A 308       8.161   3.941  -7.079  1.00215.00           C  
ANISOU 3420  CB  SER A 308    37943  26309  17438   -715    420    140       C  
ATOM   3421  OG  SER A 308       7.007   3.150  -6.843  1.00219.97           O  
ANISOU 3421  OG  SER A 308    37925  27338  18316    122   1160    426       O  
ATOM   3422  N   SER A 309       9.892   5.784  -9.114  1.00212.86           N  
ANISOU 3422  N   SER A 309    37604  25339  17936  -2166   -683   -199       N  
ATOM   3423  CA  SER A 309      11.108   6.541  -9.430  1.00213.40           C  
ANISOU 3423  CA  SER A 309    37241  25486  18354  -2890  -1388   -350       C  
ATOM   3424  C   SER A 309      10.766   7.862 -10.126  1.00216.75           C  
ANISOU 3424  C   SER A 309    37407  25580  19366  -2573  -1147   -656       C  
ATOM   3425  O   SER A 309      11.556   8.803 -10.056  1.00217.76           O  
ANISOU 3425  O   SER A 309    37222  25733  19784  -2880  -1547   -936       O  
ATOM   3426  CB  SER A 309      12.062   5.712 -10.287  1.00213.57           C  
ANISOU 3426  CB  SER A 309    36683  25775  18689  -3700  -1898    100       C  
ATOM   3427  OG  SER A 309      11.580   5.521 -11.607  1.00217.54           O  
ANISOU 3427  OG  SER A 309    36792  26119  19745  -3543  -1540    312       O  
ATOM   3428  N   ALA A 310       9.579   7.934 -10.773  1.00213.63           N  
ANISOU 3428  N   ALA A 310    37670  24621  18880  -2058   -495   -581       N  
ATOM   3429  CA  ALA A 310       9.066   9.120 -11.469  1.00213.55           C  
ANISOU 3429  CA  ALA A 310    37772  24136  19232  -1758   -214   -787       C  
ATOM   3430  C   ALA A 310       8.871  10.313 -10.518  1.00219.29           C  
ANISOU 3430  C   ALA A 310    37851  25205  20263  -1359   -180  -1283       C  
ATOM   3431  O   ALA A 310       8.851  11.459 -10.971  1.00219.41           O  
ANISOU 3431  O   ALA A 310    37854  24871  20639  -1360   -186  -1510       O  
ATOM   3432  CB  ALA A 310       7.758   8.789 -12.172  1.00212.29           C  
ANISOU 3432  CB  ALA A 310    37906  23657  19098  -1000    567   -554       C  
ATOM   3433  N   HIS A 311       8.743  10.039  -9.202  1.00219.40           N  
ANISOU 3433  N   HIS A 311    37887  25636  19839  -1159   -154  -1448       N  
ATOM   3434  CA  HIS A 311       8.573  11.049  -8.154  1.00222.17           C  
ANISOU 3434  CA  HIS A 311    37923  26260  20233   -919   -137  -1948       C  
ATOM   3435  C   HIS A 311       9.928  11.615  -7.669  1.00226.55           C  
ANISOU 3435  C   HIS A 311    37796  27205  21078  -1411   -788  -2281       C  
ATOM   3436  O   HIS A 311       9.968  12.748  -7.183  1.00228.58           O  
ANISOU 3436  O   HIS A 311    37813  27488  21551  -1329   -825  -2756       O  
ATOM   3437  CB  HIS A 311       7.778  10.483  -6.957  1.00223.94           C  
ANISOU 3437  CB  HIS A 311    37973  27043  20069   -434    230  -1961       C  
ATOM   3438  CG  HIS A 311       6.494   9.792  -7.317  1.00224.53           C  
ANISOU 3438  CG  HIS A 311    37951  27145  20217    148    883  -1595       C  
ATOM   3439  ND1 HIS A 311       5.448  10.471  -7.918  1.00224.87           N  
ANISOU 3439  ND1 HIS A 311    37872  26917  20652    594   1339  -1622       N  
ATOM   3440  CD2 HIS A 311       6.113   8.511  -7.099  1.00224.70           C  
ANISOU 3440  CD2 HIS A 311    37915  27461  19997    359   1141  -1200       C  
ATOM   3441  CE1 HIS A 311       4.483   9.578  -8.075  1.00222.97           C  
ANISOU 3441  CE1 HIS A 311    37715  26713  20290   1085   1881  -1237       C  
ATOM   3442  NE2 HIS A 311       4.837   8.385  -7.598  1.00223.09           N  
ANISOU 3442  NE2 HIS A 311    37746  27059  19958    968   1801   -979       N  
ATOM   3443  N   HIS A 312      11.025  10.825  -7.797  1.00223.16           N  
ANISOU 3443  N   HIS A 312    37580  26814  20395  -2016  -1311  -2027       N  
ATOM   3444  CA  HIS A 312      12.375  11.183  -7.343  1.00224.52           C  
ANISOU 3444  CA  HIS A 312    37301  27291  20716  -2485  -1935  -2268       C  
ATOM   3445  C   HIS A 312      13.382  11.569  -8.439  1.00225.84           C  
ANISOU 3445  C   HIS A 312    36986  27260  21561  -2983  -2301  -2163       C  
ATOM   3446  O   HIS A 312      14.090  12.563  -8.275  1.00227.60           O  
ANISOU 3446  O   HIS A 312    36849  27467  22162  -3137  -2552  -2544       O  
ATOM   3447  CB  HIS A 312      12.983  10.055  -6.483  1.00225.56           C  
ANISOU 3447  CB  HIS A 312    37153  28089  20461  -2584  -2239  -2076       C  
ATOM   3448  CG  HIS A 312      12.303   9.818  -5.169  1.00229.60           C  
ANISOU 3448  CG  HIS A 312    37427  29204  20608  -1993  -1915  -2261       C  
ATOM   3449  ND1 HIS A 312      12.225  10.808  -4.205  1.00233.67           N  
ANISOU 3449  ND1 HIS A 312    37528  30061  21194  -1710  -1857  -2832       N  
ATOM   3450  CD2 HIS A 312      11.756   8.681  -4.675  1.00230.39           C  
ANISOU 3450  CD2 HIS A 312    37550  29678  20308  -1712  -1661  -1927       C  
ATOM   3451  CE1 HIS A 312      11.597  10.259  -3.179  1.00234.42           C  
ANISOU 3451  CE1 HIS A 312    37669  30630  20772  -1371  -1597  -2807       C  
ATOM   3452  NE2 HIS A 312      11.299   8.978  -3.415  1.00232.78           N  
ANISOU 3452  NE2 HIS A 312    37693  30462  20291  -1336  -1458  -2256       N  
ATOM   3453  N   CYS A 313      13.495  10.751  -9.507  1.00220.38           N  
ANISOU 3453  N   CYS A 313    36749  26238  20747  -3475  -2415  -1627       N  
ATOM   3454  CA  CYS A 313      14.470  10.909 -10.595  1.00218.77           C  
ANISOU 3454  CA  CYS A 313    36254  25858  21011  -4148  -2809  -1390       C  
ATOM   3455  C   CYS A 313      14.385  12.244 -11.348  1.00221.26           C  
ANISOU 3455  C   CYS A 313    36392  25717  21959  -4037  -2629  -1638       C  
ATOM   3456  O   CYS A 313      15.418  12.897 -11.510  1.00221.81           O  
ANISOU 3456  O   CYS A 313    36029  25787  22462  -4430  -2984  -1771       O  
ATOM   3457  CB  CYS A 313      14.414   9.728 -11.561  1.00216.03           C  
ANISOU 3457  CB  CYS A 313    35977  25522  20583  -4527  -2833   -778       C  
ATOM   3458  SG  CYS A 313      14.806   8.131 -10.799  1.00218.19           S  
ANISOU 3458  SG  CYS A 313    35715  26603  20583  -4538  -3040   -433       S  
ATOM   3459  N   LEU A 314      13.182  12.637 -11.826  1.00218.10           N  
ANISOU 3459  N   LEU A 314    36785  24712  21371  -3708  -2154  -1645       N  
ATOM   3460  CA  LEU A 314      12.954  13.861 -12.614  1.00218.27           C  
ANISOU 3460  CA  LEU A 314    36894  24174  21865  -3641  -1978  -1793       C  
ATOM   3461  C   LEU A 314      13.414  15.158 -11.922  1.00223.56           C  
ANISOU 3461  C   LEU A 314    36921  24963  23058  -3480  -2080  -2358       C  
ATOM   3462  O   LEU A 314      14.016  16.007 -12.578  1.00223.69           O  
ANISOU 3462  O   LEU A 314    36740  24658  23593  -3802  -2234  -2406       O  
ATOM   3463  CB  LEU A 314      11.483  13.958 -13.048  1.00217.24           C  
ANISOU 3463  CB  LEU A 314    37316  23637  21589  -2984  -1339  -1724       C  
ATOM   3464  CG  LEU A 314      11.235  14.565 -14.434  1.00219.30           C  
ANISOU 3464  CG  LEU A 314    37365  23515  22446  -2914  -1130  -1527       C  
ATOM   3465  CD1 LEU A 314      10.198  13.763 -15.206  1.00217.04           C  
ANISOU 3465  CD1 LEU A 314    37550  23033  21883  -2541   -661  -1153       C  
ATOM   3466  CD2 LEU A 314      10.790  16.011 -14.325  1.00223.03           C  
ANISOU 3466  CD2 LEU A 314    37540  23763  23438  -2480   -912  -1906       C  
ATOM   3467  N   ALA A 315      13.154  15.294 -10.601  1.00223.30           N  
ANISOU 3467  N   ALA A 315    37067  25169  22610  -3207  -2061  -2762       N  
ATOM   3468  CA  ALA A 315      13.553  16.457  -9.814  1.00245.63           C  
ANISOU 3468  CA  ALA A 315    37278  29110  26940  -2359  -1852  -3430       C  
ATOM   3469  C   ALA A 315      15.012  16.345  -9.388  1.00262.08           C  
ANISOU 3469  C   ALA A 315    37206  32293  30081  -2002  -1986  -3683       C  
ATOM   3470  O   ALA A 315      15.914  16.718 -10.139  1.00236.02           O  
ANISOU 3470  O   ALA A 315    36510  27454  25713  -3642  -2783  -3443       O  
ATOM   3471  CB  ALA A 315      12.661  16.593  -8.588  1.00247.87           C  
ANISOU 3471  CB  ALA A 315    37507  29787  26887  -1881  -1602  -3788       C  
TER    3472      ALA A 315                                                      
HETATM 3473  C1  E3R A1201      10.606   1.424 -43.407  1.00115.65           C  
HETATM 3474  C2  E3R A1201       9.397   0.759 -43.149  1.00114.87           C  
HETATM 3475  C3  E3R A1201       8.324   1.049 -44.015  1.00114.37           C  
HETATM 3476  C4  E3R A1201       8.461   1.943 -45.087  1.00113.78           C  
HETATM 3477  C5  E3R A1201       9.705   2.555 -45.395  1.00115.25           C  
HETATM 3478  N1  E3R A1201      14.312  -5.619 -45.255  1.00115.52           N  
HETATM 3479  C10 E3R A1201       9.492   2.953 -47.868  1.00114.79           C  
HETATM 3480  C11 E3R A1201       9.535   4.095 -48.940  1.00114.10           C  
HETATM 3481  C12 E3R A1201      10.858   4.932 -48.892  1.00114.73           C  
HETATM 3482  C13 E3R A1201      11.263   5.346 -47.456  1.00115.44           C  
HETATM 3483  C14 E3R A1201       9.425   3.481 -50.331  1.00113.45           C  
HETATM 3484  C15 E3R A1201      13.547   4.465 -45.428  1.00115.76           C  
HETATM 3485  C16 E3R A1201      11.494   5.295 -44.283  1.00114.27           C  
HETATM 3486  C17 E3R A1201       9.270  -0.106 -42.001  1.00113.35           C  
HETATM 3487  C18 E3R A1201      10.472  -1.064 -41.823  1.00112.19           C  
HETATM 3488  C19 E3R A1201       7.971  -0.923 -42.010  1.00113.05           C  
HETATM 3489  C20 E3R A1201       9.203   0.750 -40.725  1.00113.15           C  
HETATM 3490  C21 E3R A1201      10.592  -2.117 -42.931  1.00111.62           C  
HETATM 3491  C22 E3R A1201      12.046  -2.570 -43.013  1.00111.46           C  
HETATM 3492  C23 E3R A1201      12.352  -2.986 -44.444  1.00112.14           C  
HETATM 3493  C24 E3R A1201      12.112  -4.486 -44.590  1.00113.18           C  
HETATM 3494  C25 E3R A1201      13.354  -5.125 -44.963  1.00114.70           C  
HETATM 3495  C6  E3R A1201      10.757   2.307 -44.472  1.00115.64           C  
HETATM 3496  C7  E3R A1201       9.852   3.520 -46.460  1.00115.57           C  
HETATM 3497  C8  E3R A1201      11.316   4.052 -46.607  1.00115.82           C  
HETATM 3498  C9  E3R A1201      12.052   4.189 -45.217  1.00115.36           C  
HETATM 3499  O1  E3R A1201      11.983   2.916 -44.620  1.00115.42           O  
HETATM 3500  O2  E3R A1201       8.051   3.256 -50.658  1.00113.54           O  
HETATM 3501  O3  E3R A1201       7.386   2.191 -45.888  1.00112.29           O  
CONECT 1178 1215                                                                
CONECT 1215 1178                                                                
CONECT 3473 3474 3495                                                           
CONECT 3474 3473 3475 3486                                                      
CONECT 3475 3474 3476                                                           
CONECT 3476 3475 3477 3501                                                      
CONECT 3477 3476 3495 3496                                                      
CONECT 3478 3494                                                                
CONECT 3479 3480 3496                                                           
CONECT 3480 3479 3481 3483                                                      
CONECT 3481 3480 3482                                                           
CONECT 3482 3481 3497                                                           
CONECT 3483 3480 3500                                                           
CONECT 3484 3498                                                                
CONECT 3485 3498                                                                
CONECT 3486 3474 3487 3488 3489                                                 
CONECT 3487 3486 3490                                                           
CONECT 3488 3486                                                                
CONECT 3489 3486                                                                
CONECT 3490 3487 3491                                                           
CONECT 3491 3490 3492                                                           
CONECT 3492 3491 3493                                                           
CONECT 3493 3492 3494                                                           
CONECT 3494 3478 3493                                                           
CONECT 3495 3473 3477 3499                                                      
CONECT 3496 3477 3479 3497                                                      
CONECT 3497 3482 3496 3498                                                      
CONECT 3498 3484 3485 3497 3499                                                 
CONECT 3499 3495 3498                                                           
CONECT 3500 3483                                                                
CONECT 3501 3476                                                                
MASTER      346    0    1   22    3    0    4    6 3500    1   31   39          
END