HEADER    SIGNALING PROTEIN                       21-JUN-13   4BUO              
TITLE     HIGH RESOLUTION STRUCTURE OF THERMOSTABLE AGONIST-BOUND               
TITLE    2 NEUROTENSIN RECEPTOR 1 MUTANT WITHOUT LYSOZYME FUSION                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NEUROTENSIN RECEPTOR TYPE 1;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 50-272 AND 291-390;                               
COMPND   5 SYNONYM: NT-R-1, NTR1, HIGH-AFFINITY LEVOCABASTINE-INSENSITIVE       
COMPND   6  NEUROTENSIN RECEPTOR, NTRH;                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 OTHER_DETAILS: THERMOSTABLE MUTANT WITH INTRACELLULAR LOOP 3         
COMPND  10  DELETION B (E273-T290);                                             
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: NEUROTENSIN/NEUROMEDIN N;                                  
COMPND  13 CHAIN: C, D;                                                         
COMPND  14 FRAGMENT: C-TERMINUS, RESIDUES 8-13;                                 
COMPND  15 SYNONYM: NEUROTENSIN, NT;                                            
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 OTHER_DETAILS: RESIDUES 8-13 CORRESPOND TO NEUROTENSIN C- TERMINUS.  
COMPND  18  RESIDUES 4-7 ARE PART OF AN ARTIFICIAL LINKER AND DO NOT            
COMPND  19  CORRESPOND TO NEUROTENSIN SEQUENCE                                  
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: TUNER;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PEP-TM86VDIC3III;                         
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  13 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE  14 ORGANISM_TAXID: 10116;                                               
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    SIGNALING PROTEIN, G PROTEIN COUPLED RECEPTOR, MEMBRANE PROTEIN       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.EGLOFF,M.HILLENBRAND,K.M.SCHLINKMANN,A.BATYUK,P.MITTL,A.PLUECKTHUN  
REVDAT   3   26-FEB-14 4BUO    1       JRNL                                     
REVDAT   2   05-FEB-14 4BUO    1       JRNL                                     
REVDAT   1   29-JAN-14 4BUO    0                                                
JRNL        AUTH   P.EGLOFF,M.HILLENBRAND,C.KLENK,A.BATYUK,P.HEINE,S.BALADA,    
JRNL        AUTH 2 K.M.SCHLINKMANN,D.J.SCOTT,M.SCHUETZ,A.PLUECKTHUN             
JRNL        TITL   STRUCTURE OF SIGNALING-COMPETENT NEUROTENSIN RECEPTOR 1      
JRNL        TITL 2 OBTAINED BY DIRECTED EVOLUTION IN ESCHERICHIA COLI           
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 111  E655 2014              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   24453215                                                     
JRNL        DOI    10.1073/PNAS.1317903111                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.750                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.821                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.35                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.75                          
REMARK   3   NUMBER OF REFLECTIONS             : 31649                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.2490                          
REMARK   3   R VALUE            (WORKING SET) : 0.2478                          
REMARK   3   FREE R VALUE                     : 0.2728                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1581                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 19.8216 -  6.0625    1.00     2950   155  0.2321 0.2527        
REMARK   3     2  6.0625 -  4.8350    1.00     2805   148  0.2401 0.2657        
REMARK   3     3  4.8350 -  4.2306    1.00     2784   146  0.2048 0.2228        
REMARK   3     4  4.2306 -  3.8469    1.00     2788   147  0.2286 0.2591        
REMARK   3     5  3.8469 -  3.5729    1.00     2748   144  0.2561 0.2899        
REMARK   3     6  3.5729 -  3.3633    1.00     2754   145  0.2758 0.3257        
REMARK   3     7  3.3633 -  3.1956    1.00     2718   143  0.3071 0.3682        
REMARK   3     8  3.1956 -  3.0570    1.00     2730   144  0.3354 0.3521        
REMARK   3     9  3.0570 -  2.9397    1.00     2740   144  0.3969 0.4093        
REMARK   3    10  2.9397 -  2.8386    0.99     2677   143  0.4339 0.4554        
REMARK   3    11  2.8386 -  2.7500    0.88     2374   122  0.4691 0.4789        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.55             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.94            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 109.97                         
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           5160                                  
REMARK   3   ANGLE     :  0.653           7020                                  
REMARK   3   CHIRALITY :  0.047            845                                  
REMARK   3   PLANARITY :  0.003            854                                  
REMARK   3   DIHEDRAL  : 10.140           1774                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 2                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN A AND (RESSEQ 52:93 OR               
REMARK   3                          RESSEQ 97:270 OR RESSEQ 297:384))           
REMARK   3     SELECTION          : (CHAIN B AND (RESSEQ 49:91 OR               
REMARK   3                          RESSEQ 98:272 OR RESSEQ 291:386))           
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN C                                     
REMARK   3     SELECTION          : CHAIN D                                     
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: PHENIX AND REFMAC WERE USED.              
REMARK   4                                                                      
REMARK   4 4BUO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-JUN-13.                  
REMARK 100 THE PDBE ID CODE IS EBI-57351.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-AUG-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06DA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PILATUS                            
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32141                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.75                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NONE                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 13.1                               
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.85                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.9                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.45                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3ZEV                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.46                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 21.5% (V/V) PEG600, 2 M NACL, 50         
REMARK 280  MM GLYCINE PH 9.4                                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       31.65500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      106.06500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.70000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      106.06500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.65500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.70000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1600 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14680 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.3 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1600 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15400 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.9 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
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     PRO A    47                                                      
REMARK 465     GLY A    48                                                      
REMARK 465     SER A    49                                                      
REMARK 465     GLY A    50                                                      
REMARK 465     PRO A    51                                                      
REMARK 465     SER A    94                                                      
REMARK 465     LEU A    95                                                      
REMARK 465     GLN A    96                                                      
REMARK 465     ALA A   271                                                      
REMARK 465     ALA A   272                                                      
REMARK 465     PHE A   291                                                      
REMARK 465     ASN A   292                                                      
REMARK 465     MET A   293                                                      
REMARK 465     THR A   294                                                      
REMARK 465     ILE A   295                                                      
REMARK 465     GLU A   296                                                      
REMARK 465     ALA A   385                                                      
REMARK 465     CYS A   386                                                      
REMARK 465     LEU A   387                                                      
REMARK 465     CYS A   388                                                      
REMARK 465     PRO A   389                                                      
REMARK 465     GLY A   390                                                      
REMARK 465     THR A   391                                                      
REMARK 465     ARG A   392                                                      
REMARK 465     GLU A   393                                                      
REMARK 465     LEU A   394                                                      
REMARK 465     GLU A   395                                                      
REMARK 465     VAL A   396                                                      
REMARK 465     LEU A   397                                                      
REMARK 465     PHE A   398                                                      
REMARK 465     GLN A   399                                                      
REMARK 465     PRO B    47                                                      
REMARK 465     GLY B    48                                                      
REMARK 465     LYS B    92                                                      
REMARK 465     LYS B    93                                                      
REMARK 465     SER B    94                                                      
REMARK 465     LEU B    95                                                      
REMARK 465     GLN B    96                                                      
REMARK 465     SER B    97                                                      
REMARK 465     LEU B   387                                                      
REMARK 465     CYS B   388                                                      
REMARK 465     PRO B   389                                                      
REMARK 465     GLY B   390                                                      
REMARK 465     THR B   391                                                      
REMARK 465     ARG B   392                                                      
REMARK 465     GLU B   393                                                      
REMARK 465     LEU B   394                                                      
REMARK 465     GLU B   395                                                      
REMARK 465     VAL B   396                                                      
REMARK 465     LEU B   397                                                      
REMARK 465     PHE B   398                                                      
REMARK 465     GLN B   399                                                      
REMARK 465     GLY C     4                                                      
REMARK 465     PRO C     5                                                      
REMARK 465     GLY C     6                                                      
REMARK 465     GLY C     7                                                      
REMARK 465     GLY D     4                                                      
REMARK 465     PRO D     5                                                      
REMARK 465     GLY D     6                                                      
REMARK 465     GLY D     7                                                      
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     GLN A 270    CG   CD   OE1  NE2                                  
REMARK 470     ARG B  91    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    LEU A    98     OG1  THR A   101              2.20            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A 246      -76.07   -129.97                                   
REMARK 500    ASN B  52       44.42    -75.88                                   
REMARK 500    SER B  53       67.84   -115.36                                   
REMARK 500    ASP B  54       63.94    -69.89                                   
REMARK 500    TRP B 130      -81.75    -96.39                                   
REMARK 500    PHE B 175      -61.29    -95.55                                   
REMARK 500    LYS B 176       47.52   -107.17                                   
REMARK 500    LYS B 178     -105.79     47.36                                   
REMARK 500    LEU B 213       34.61    -86.50                                   
REMARK 500    PHE B 246      -76.28   -127.81                                   
REMARK 500    THR B 294     -155.89   -159.32                                   
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 GLY A1385                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY A1386                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY A1387                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY A1389                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY A1390                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY A1391                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY B1387                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY B1388                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY B1389                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3ZEV   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THERMOSTABLE AGONIST-BOUND NEUROTENSIN                 
REMARK 900  RECEPTOR 1 MUTANT WITHOUT LYSOZYME FUSION                           
REMARK 900 RELATED ID: 4BV0   RELATED DB: PDB                                   
REMARK 900  HIGH RESOLUTION STRUCTURE OF EVOLVED AGONIST-BOUND                  
REMARK 900  NEUROTENSIN RECEPTOR 1 MUTANT WITHOUT LYSOZYME FUSION               
REMARK 900 RELATED ID: 4BWB   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF EVOLVED AGONIST-BOUND NEUROTENSIN RECEPTOR             
REMARK 900  1 MUTANT WITHOUT LYSOZYME FUSION                                    
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 CHAINS C AND D -  THE SEQUENCE RRPYIL REPRESENTS NEUROTENSIN         
REMARK 999 RESIDUES 8-13 AND THE REST IS LINKER.                                
DBREF  4BUO A   50   272  UNP    P20789   NTR1_RAT        50    272             
DBREF  4BUO A  291   390  UNP    P20789   NTR1_RAT       291    390             
DBREF  4BUO B   50   272  UNP    P20789   NTR1_RAT        50    272             
DBREF  4BUO B  291   390  UNP    P20789   NTR1_RAT       291    390             
DBREF  4BUO C    8    13  UNP    P20068   NEUT_RAT       157    162             
DBREF  4BUO D    8    13  UNP    P20068   NEUT_RAT       157    162             
SEQADV 4BUO PRO A   47  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BUO GLY A   48  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BUO SER A   49  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BUO THR A  391  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BUO ARG A  392  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BUO GLU A  393  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BUO LEU A  394  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BUO GLU A  395  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BUO VAL A  396  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BUO LEU A  397  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BUO PHE A  398  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BUO GLN A  399  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BUO LEU A   86  UNP  P20789    ALA    86 ENGINEERED MUTATION            
SEQADV 4BUO ASP A  103  UNP  P20789    HIS   103 ENGINEERED MUTATION            
SEQADV 4BUO TYR A  105  UNP  P20789    HIS   105 ENGINEERED MUTATION            
SEQADV 4BUO VAL A  161  UNP  P20789    ALA   161 ENGINEERED MUTATION            
SEQADV 4BUO LEU A  167  UNP  P20789    ARG   167 ENGINEERED MUTATION            
SEQADV 4BUO LEU A  213  UNP  P20789    ARG   213 ENGINEERED MUTATION            
SEQADV 4BUO LEU A  234  UNP  P20789    VAL   234 ENGINEERED MUTATION            
SEQADV 4BUO ALA A  253  UNP  P20789    ILE   253 ENGINEERED MUTATION            
SEQADV 4BUO ARG A  305  UNP  P20789    HIS   305 ENGINEERED MUTATION            
SEQADV 4BUO VAL A  358  UNP  P20789    PHE   358 ENGINEERED MUTATION            
SEQADV 4BUO ALA A  362  UNP  P20789    SER   362 ENGINEERED MUTATION            
SEQADV 4BUO PRO B   47  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BUO GLY B   48  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BUO SER B   49  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BUO THR B  391  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BUO ARG B  392  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BUO GLU B  393  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BUO LEU B  394  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BUO GLU B  395  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BUO VAL B  396  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BUO LEU B  397  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BUO PHE B  398  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BUO GLN B  399  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BUO LEU B   86  UNP  P20789    ALA    86 ENGINEERED MUTATION            
SEQADV 4BUO ASP B  103  UNP  P20789    HIS   103 ENGINEERED MUTATION            
SEQADV 4BUO TYR B  105  UNP  P20789    HIS   105 ENGINEERED MUTATION            
SEQADV 4BUO VAL B  161  UNP  P20789    ALA   161 ENGINEERED MUTATION            
SEQADV 4BUO LEU B  167  UNP  P20789    ARG   167 ENGINEERED MUTATION            
SEQADV 4BUO LEU B  213  UNP  P20789    ARG   213 ENGINEERED MUTATION            
SEQADV 4BUO LEU B  234  UNP  P20789    VAL   234 ENGINEERED MUTATION            
SEQADV 4BUO ALA B  253  UNP  P20789    ILE   253 ENGINEERED MUTATION            
SEQADV 4BUO ARG B  305  UNP  P20789    HIS   305 ENGINEERED MUTATION            
SEQADV 4BUO VAL B  358  UNP  P20789    PHE   358 ENGINEERED MUTATION            
SEQADV 4BUO ALA B  362  UNP  P20789    SER   362 ENGINEERED MUTATION            
SEQADV 4BUO GLY C    4  UNP  P20068              SEE REMARK 999                 
SEQADV 4BUO PRO C    5  UNP  P20068              SEE REMARK 999                 
SEQADV 4BUO GLY C    6  UNP  P20068              SEE REMARK 999                 
SEQADV 4BUO GLY C    7  UNP  P20068              SEE REMARK 999                 
SEQADV 4BUO GLY D    4  UNP  P20068              SEE REMARK 999                 
SEQADV 4BUO PRO D    5  UNP  P20068              SEE REMARK 999                 
SEQADV 4BUO GLY D    6  UNP  P20068              SEE REMARK 999                 
SEQADV 4BUO GLY D    7  UNP  P20068              SEE REMARK 999                 
SEQRES   1 A  335  PRO GLY SER GLY PRO ASN SER ASP LEU ASP VAL ASN THR          
SEQRES   2 A  335  ASP ILE TYR SER LYS VAL LEU VAL THR ALA ILE TYR LEU          
SEQRES   3 A  335  ALA LEU PHE VAL VAL GLY THR VAL GLY ASN SER VAL THR          
SEQRES   4 A  335  LEU PHE THR LEU ALA ARG LYS LYS SER LEU GLN SER LEU          
SEQRES   5 A  335  GLN SER THR VAL ASP TYR TYR LEU GLY SER LEU ALA LEU          
SEQRES   6 A  335  SER ASP LEU LEU ILE LEU LEU LEU ALA MET PRO VAL GLU          
SEQRES   7 A  335  LEU TYR ASN PHE ILE TRP VAL HIS HIS PRO TRP ALA PHE          
SEQRES   8 A  335  GLY ASP ALA GLY CYS ARG GLY TYR TYR PHE LEU ARG ASP          
SEQRES   9 A  335  ALA CYS THR TYR ALA THR ALA LEU ASN VAL VAL SER LEU          
SEQRES  10 A  335  SER VAL GLU LEU TYR LEU ALA ILE CYS HIS PRO PHE LYS          
SEQRES  11 A  335  ALA LYS THR LEU MET SER ARG SER ARG THR LYS LYS PHE          
SEQRES  12 A  335  ILE SER ALA ILE TRP LEU ALA SER ALA LEU LEU ALA ILE          
SEQRES  13 A  335  PRO MET LEU PHE THR MET GLY LEU GLN ASN LEU SER GLY          
SEQRES  14 A  335  ASP GLY THR HIS PRO GLY GLY LEU VAL CYS THR PRO ILE          
SEQRES  15 A  335  VAL ASP THR ALA THR LEU LYS VAL VAL ILE GLN VAL ASN          
SEQRES  16 A  335  THR PHE MET SER PHE LEU PHE PRO MET LEU VAL ALA SER          
SEQRES  17 A  335  ILE LEU ASN THR VAL ILE ALA ASN LYS LEU THR VAL MET          
SEQRES  18 A  335  VAL HIS GLN ALA ALA PHE ASN MET THR ILE GLU PRO GLY          
SEQRES  19 A  335  ARG VAL GLN ALA LEU ARG ARG GLY VAL LEU VAL LEU ARG          
SEQRES  20 A  335  ALA VAL VAL ILE ALA PHE VAL VAL CYS TRP LEU PRO TYR          
SEQRES  21 A  335  HIS VAL ARG ARG LEU MET PHE CYS TYR ILE SER ASP GLU          
SEQRES  22 A  335  GLN TRP THR THR PHE LEU PHE ASP PHE TYR HIS TYR PHE          
SEQRES  23 A  335  TYR MET LEU THR ASN ALA LEU VAL TYR VAL SER ALA ALA          
SEQRES  24 A  335  ILE ASN PRO ILE LEU TYR ASN LEU VAL SER ALA ASN PHE          
SEQRES  25 A  335  ARG GLN VAL PHE LEU SER THR LEU ALA CYS LEU CYS PRO          
SEQRES  26 A  335  GLY THR ARG GLU LEU GLU VAL LEU PHE GLN                      
SEQRES   1 B  335  PRO GLY SER GLY PRO ASN SER ASP LEU ASP VAL ASN THR          
SEQRES   2 B  335  ASP ILE TYR SER LYS VAL LEU VAL THR ALA ILE TYR LEU          
SEQRES   3 B  335  ALA LEU PHE VAL VAL GLY THR VAL GLY ASN SER VAL THR          
SEQRES   4 B  335  LEU PHE THR LEU ALA ARG LYS LYS SER LEU GLN SER LEU          
SEQRES   5 B  335  GLN SER THR VAL ASP TYR TYR LEU GLY SER LEU ALA LEU          
SEQRES   6 B  335  SER ASP LEU LEU ILE LEU LEU LEU ALA MET PRO VAL GLU          
SEQRES   7 B  335  LEU TYR ASN PHE ILE TRP VAL HIS HIS PRO TRP ALA PHE          
SEQRES   8 B  335  GLY ASP ALA GLY CYS ARG GLY TYR TYR PHE LEU ARG ASP          
SEQRES   9 B  335  ALA CYS THR TYR ALA THR ALA LEU ASN VAL VAL SER LEU          
SEQRES  10 B  335  SER VAL GLU LEU TYR LEU ALA ILE CYS HIS PRO PHE LYS          
SEQRES  11 B  335  ALA LYS THR LEU MET SER ARG SER ARG THR LYS LYS PHE          
SEQRES  12 B  335  ILE SER ALA ILE TRP LEU ALA SER ALA LEU LEU ALA ILE          
SEQRES  13 B  335  PRO MET LEU PHE THR MET GLY LEU GLN ASN LEU SER GLY          
SEQRES  14 B  335  ASP GLY THR HIS PRO GLY GLY LEU VAL CYS THR PRO ILE          
SEQRES  15 B  335  VAL ASP THR ALA THR LEU LYS VAL VAL ILE GLN VAL ASN          
SEQRES  16 B  335  THR PHE MET SER PHE LEU PHE PRO MET LEU VAL ALA SER          
SEQRES  17 B  335  ILE LEU ASN THR VAL ILE ALA ASN LYS LEU THR VAL MET          
SEQRES  18 B  335  VAL HIS GLN ALA ALA PHE ASN MET THR ILE GLU PRO GLY          
SEQRES  19 B  335  ARG VAL GLN ALA LEU ARG ARG GLY VAL LEU VAL LEU ARG          
SEQRES  20 B  335  ALA VAL VAL ILE ALA PHE VAL VAL CYS TRP LEU PRO TYR          
SEQRES  21 B  335  HIS VAL ARG ARG LEU MET PHE CYS TYR ILE SER ASP GLU          
SEQRES  22 B  335  GLN TRP THR THR PHE LEU PHE ASP PHE TYR HIS TYR PHE          
SEQRES  23 B  335  TYR MET LEU THR ASN ALA LEU VAL TYR VAL SER ALA ALA          
SEQRES  24 B  335  ILE ASN PRO ILE LEU TYR ASN LEU VAL SER ALA ASN PHE          
SEQRES  25 B  335  ARG GLN VAL PHE LEU SER THR LEU ALA CYS LEU CYS PRO          
SEQRES  26 B  335  GLY THR ARG GLU LEU GLU VAL LEU PHE GLN                      
SEQRES   1 C   10  GLY PRO GLY GLY ARG ARG PRO TYR ILE LEU                      
SEQRES   1 D   10  GLY PRO GLY GLY ARG ARG PRO TYR ILE LEU                      
HET    GLY  A1385       5                                                       
HET    GLY  A1386       5                                                       
HET    GLY  A1387       5                                                       
HET    GLY  A1388       5                                                       
HET    GLY  A1389       5                                                       
HET    GLY  A1390       5                                                       
HET    GLY  A1391       5                                                       
HET    GLY  A1392       5                                                       
HET    GLY  B1387       5                                                       
HET    GLY  B1388       5                                                       
HET    GLY  B1389       5                                                       
HETNAM     GLY GLYCINE                                                          
FORMUL   3  GLY    11(C2 H5 N O2)                                               
HELIX    1   1 ASP A   60  ARG A   91  1                                  32    
HELIX    2   2 LEU A   98  LEU A  119  1                                  22    
HELIX    3   3 LEU A  119  TRP A  130  1                                  12    
HELIX    4   4 PHE A  137  HIS A  173  1                                  37    
HELIX    5   5 HIS A  173  THR A  179  1                                   7    
HELIX    6   6 SER A  182  ILE A  202  1                                  21    
HELIX    7   7 PRO A  203  THR A  207  1                                   5    
HELIX    8   8 HIS A  219  GLY A  221  5                                   3    
HELIX    9   9 ASP A  230  PHE A  246  1                                  17    
HELIX   10  10 PHE A  246  GLN A  270  1                                  25    
HELIX   11  11 PRO A  297  ILE A  334  1                                  38    
HELIX   12  12 THR A  340  SER A  373  1                                  34    
HELIX   13  13 SER A  373  LEU A  384  1                                  12    
HELIX   14  14 ASP B   60  ALA B   90  1                                  31    
HELIX   15  15 GLN B   99  PHE B  128  1                                  30    
HELIX   16  16 PHE B  137  HIS B  173  1                                  37    
HELIX   17  17 SER B  182  ILE B  202  1                                  21    
HELIX   18  18 PRO B  203  THR B  207  1                                   5    
HELIX   19  19 HIS B  219  GLY B  221  5                                   3    
HELIX   20  20 ASP B  230  PHE B  246  1                                  17    
HELIX   21  21 PHE B  246  ALA B  272  1                                  27    
HELIX   22  22 GLU B  296  ILE B  334  1                                  39    
HELIX   23  23 THR B  340  ALA B  385  1                                  46    
SHEET    1  AA 2 MET A 208  ASN A 212  0                                        
SHEET    2  AA 2 LEU A 223  PRO A 227 -1  O  VAL A 224   N  GLN A 211           
SHEET    1  BA 2 MET B 208  ASN B 212  0                                        
SHEET    2  BA 2 LEU B 223  PRO B 227 -1  O  VAL B 224   N  GLN B 211           
SSBOND   1 CYS A  142    CYS A  225                          1555   1555  2.03  
SSBOND   2 CYS B  142    CYS B  225                          1555   1555  2.03  
CISPEP   1 HIS A  133    PRO A  134          0         0.43                     
CISPEP   2 GLY B   50    PRO B   51          0        -1.22                     
CISPEP   3 HIS B  133    PRO B  134          0        -0.33                     
SITE     1 AC1  1 PHE A 206                                                     
SITE     1 AC2  2 ASP A 103  TYR A 104                                          
SITE     1 AC3  3 GLU A 166  MET A 181  PHE B 243                               
SITE     1 AC4  2 LEU A 322  VAL A 326                                          
SITE     1 AC5  1 ALA A 140                                                     
SITE     1 AC6  1 PHE A 206                                                     
SITE     1 AC7  1 TRP B 194                                                     
SITE     1 AC8  4 GLN B  99  ARG B 305  SER B 373  ASN B 375                    
SITE     1 AC9  5 LEU A 247  PHE A 248  LEU B 180  MET B 181                    
SITE     2 AC9  5 PHE B 189                                                     
CRYST1   63.310   89.400  212.130  90.00  90.00  90.00 P 21 21 21    8          
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      0.015795  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011186  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004714        0.00000                         
MTRIX1   1 -0.897400 -0.096480  0.430500       26.98000    1                    
MTRIX2   1 -0.055670 -0.943200 -0.327400      -22.54000    1                    
MTRIX3   1  0.437700 -0.317800  0.841100      -10.70000    1                    
ATOM      1  N   ASN A  52       5.307 -37.589 -56.582  1.00152.42           N  
ANISOU    1  N   ASN A  52    25901  15492  16518   1039    117  -3869       N  
ATOM      2  CA  ASN A  52       6.520 -37.217 -55.862  1.00150.08           C  
ANISOU    2  CA  ASN A  52    25091  15374  16557   1090    200  -3519       C  
ATOM      3  C   ASN A  52       6.576 -37.809 -54.456  1.00150.52           C  
ANISOU    3  C   ASN A  52    25137  15051  17001   1133    132  -3445       C  
ATOM      4  O   ASN A  52       5.789 -37.445 -53.584  1.00148.44           O  
ANISOU    4  O   ASN A  52    24597  14797  17005    910    -49  -3189       O  
ATOM      5  CB  ASN A  52       6.672 -35.693 -55.811  1.00 94.83           C  
ANISOU    5  CB  ASN A  52    17755   8695   9583    743    -18  -3255       C  
ATOM      6  CG  ASN A  52       5.351 -34.979 -55.586  1.00 96.19           C  
ANISOU    6  CG  ASN A  52    18110   8676   9761    335   -418  -3304       C  
ATOM      7  OD1 ASN A  52       4.425 -35.528 -54.991  1.00 99.86           O  
ANISOU    7  OD1 ASN A  52    18852   8737  10355    262   -566  -3437       O  
ATOM      8  ND2 ASN A  52       5.256 -33.750 -56.075  1.00 93.61           N  
ANISOU    8  ND2 ASN A  52    17624   8637   9306     64   -602  -3186       N  
ATOM      9  N   SER A  53       7.514 -38.725 -54.242  1.00137.26           N  
ANISOU    9  N   SER A  53    23769  13037  15346   1432    285  -3669       N  
ATOM     10  CA  SER A  53       7.649 -39.380 -52.947  1.00137.72           C  
ANISOU   10  CA  SER A  53    23838  12719  15768   1533    251  -3593       C  
ATOM     11  C   SER A  53       8.830 -38.829 -52.154  1.00136.48           C  
ANISOU   11  C   SER A  53    23229  12775  15851   1814    496  -3321       C  
ATOM     12  O   SER A  53       9.338 -39.485 -51.244  1.00136.38           O  
ANISOU   12  O   SER A  53    23127  12530  16160   1887    463  -3174       O  
ATOM     13  CB  SER A  53       7.784 -40.894 -53.120  1.00107.32           C  
ANISOU   13  CB  SER A  53    20510   8403  11864   1771    316  -3938       C  
ATOM     14  OG  SER A  53       8.929 -41.221 -53.887  1.00110.41           O  
ANISOU   14  OG  SER A  53    20958   8935  12058   2199    684  -4110       O  
ATOM     15  N   ASP A  54       9.261 -37.621 -52.503  1.00 99.45           N  
ANISOU   15  N   ASP A  54    18263   8527  10997   1957    728  -3245       N  
ATOM     16  CA  ASP A  54      10.371 -36.976 -51.811  1.00 98.48           C  
ANISOU   16  CA  ASP A  54    17705   8645  11069   2220    964  -2999       C  
ATOM     17  C   ASP A  54       9.890 -36.168 -50.609  1.00 95.29           C  
ANISOU   17  C   ASP A  54    16877   8450  10880   1952    795  -2644       C  
ATOM     18  O   ASP A  54      10.642 -35.949 -49.659  1.00 94.43           O  
ANISOU   18  O   ASP A  54    16457   8397  11026   2097    878  -2416       O  
ATOM     19  CB  ASP A  54      11.159 -36.082 -52.770  1.00145.79           C  
ANISOU   19  CB  ASP A  54    23562  15028  16803   2458   1283  -3049       C  
ATOM     20  CG  ASP A  54      11.912 -36.874 -53.819  1.00149.19           C  
ANISOU   20  CG  ASP A  54    24388  15286  17011   2776   1508  -3398       C  
ATOM     21  OD1 ASP A  54      12.312 -38.020 -53.525  1.00151.11           O  
ANISOU   21  OD1 ASP A  54    24936  15092  17384   2931   1480  -3568       O  
ATOM     22  OD2 ASP A  54      12.105 -36.352 -54.937  1.00150.02           O  
ANISOU   22  OD2 ASP A  54    24509  15687  16804   2875   1720  -3502       O  
ATOM     23  N   LEU A  55       8.636 -35.730 -50.655  1.00 88.63           N  
ANISOU   23  N   LEU A  55    16025   7726   9926   1570    554  -2601       N  
ATOM     24  CA  LEU A  55       8.056 -34.956 -49.563  1.00 84.47           C  
ANISOU   24  CA  LEU A  55    15125   7389   9580   1307    390  -2290       C  
ATOM     25  C   LEU A  55       7.325 -35.860 -48.577  1.00 84.03           C  
ANISOU   25  C   LEU A  55    15145   6999   9782   1085    134  -2208       C  
ATOM     26  O   LEU A  55       6.609 -35.381 -47.697  1.00 82.38           O  
ANISOU   26  O   LEU A  55    14813   6869   9619    746    -93  -2073       O  
ATOM     27  CB  LEU A  55       7.097 -33.885 -50.097  1.00 67.54           C  
ANISOU   27  CB  LEU A  55    12902   5555   7206   1023    263  -2264       C  
ATOM     28  CG  LEU A  55       7.658 -32.771 -50.987  1.00 64.21           C  
ANISOU   28  CG  LEU A  55    12199   5575   6622   1129    465  -2157       C  
ATOM     29  CD1 LEU A  55       9.035 -32.339 -50.506  1.00 68.77           C  
ANISOU   29  CD1 LEU A  55    12945   6204   6980   1456    762  -2361       C  
ATOM     30  CD2 LEU A  55       7.709 -33.202 -52.446  1.00 61.77           C  
ANISOU   30  CD2 LEU A  55    11840   5506   6125    819    278  -2111       C  
ATOM     31  N   ASP A  56       7.507 -37.168 -48.728  1.00 68.95           N  
ANISOU   31  N   ASP A  56    13434   4719   8046   1281    177  -2280       N  
ATOM     32  CA  ASP A  56       6.854 -38.135 -47.854  1.00 70.49           C  
ANISOU   32  CA  ASP A  56    13747   4554   8482   1074    -57  -2203       C  
ATOM     33  C   ASP A  56       7.593 -38.293 -46.529  1.00 69.08           C  
ANISOU   33  C   ASP A  56    13347   4295   8604   1271     31  -1967       C  
ATOM     34  O   ASP A  56       8.816 -38.425 -46.501  1.00 69.15           O  
ANISOU   34  O   ASP A  56    13224   4411   8639   1631    275  -1947       O  
ATOM     35  CB  ASP A  56       6.728 -39.494 -48.548  1.00 96.84           C  
ANISOU   35  CB  ASP A  56    17607   7429  11759   1070   -156  -2508       C  
ATOM     36  CG  ASP A  56       5.773 -39.461 -49.724  1.00 97.09           C  
ANISOU   36  CG  ASP A  56    17870   7492  11528    760   -351  -2703       C  
ATOM     37  OD1 ASP A  56       5.827 -38.491 -50.506  1.00 99.59           O  
ANISOU   37  OD1 ASP A  56    18597   7606  11639    859   -326  -3020       O  
ATOM     38  OD2 ASP A  56       4.964 -40.401 -49.862  1.00 94.79           O  
ANISOU   38  OD2 ASP A  56    17354   7431  11232    426   -534  -2541       O  
ATOM     39  N   VAL A  57       6.837 -38.281 -45.436  1.00 68.39           N  
ANISOU   39  N   VAL A  57    13215   4028   8740   1033   -170  -1779       N  
ATOM     40  CA  VAL A  57       7.397 -38.472 -44.104  1.00 67.71           C  
ANISOU   40  CA  VAL A  57    12953   3846   8928   1190   -120  -1539       C  
ATOM     41  C   VAL A  57       7.139 -39.893 -43.614  1.00 73.27           C  
ANISOU   41  C   VAL A  57    13987   4034   9819   1094   -292  -1567       C  
ATOM     42  O   VAL A  57       5.990 -40.325 -43.515  1.00 75.10           O  
ANISOU   42  O   VAL A  57    14412   4094  10028    748   -514  -1631       O  
ATOM     43  CB  VAL A  57       6.803 -37.473 -43.098  1.00 61.08           C  
ANISOU   43  CB  VAL A  57    11681   3345   8182    988   -179  -1211       C  
ATOM     44  CG1 VAL A  57       7.222 -37.833 -41.687  1.00 60.97           C  
ANISOU   44  CG1 VAL A  57    11501   3244   8420   1159   -134   -963       C  
ATOM     45  CG2 VAL A  57       7.230 -36.055 -43.446  1.00 55.86           C  
ANISOU   45  CG2 VAL A  57    10724   3165   7336   1042    -38  -1187       C  
ATOM     46  N   ASN A  58       8.213 -40.614 -43.308  1.00136.64           N  
ANISOU   46  N   ASN A  58    22069  11808  18039   1394   -201  -1505       N  
ATOM     47  CA  ASN A  58       8.109 -42.016 -42.917  1.00138.40           C  
ANISOU   47  CA  ASN A  58    22641  11495  18450   1347   -350  -1531       C  
ATOM     48  C   ASN A  58       7.821 -42.227 -41.434  1.00136.41           C  
ANISOU   48  C   ASN A  58    22202  11181  18447   1161   -485  -1178       C  
ATOM     49  O   ASN A  58       8.714 -42.573 -40.661  1.00137.58           O  
ANISOU   49  O   ASN A  58    22437  11036  18803   1361   -474  -1067       O  
ATOM     50  CB  ASN A  58       9.377 -42.775 -43.313  1.00144.13           C  
ANISOU   50  CB  ASN A  58    23619  11911  19233   1816   -177  -1711       C  
ATOM     51  CG  ASN A  58       9.660 -42.699 -44.799  1.00146.55           C  
ANISOU   51  CG  ASN A  58    24162  12249  19270   2000    -30  -2081       C  
ATOM     52  OD1 ASN A  58       8.743 -42.596 -45.614  1.00147.28           O  
ANISOU   52  OD1 ASN A  58    24521  12255  19184   1737   -165  -2294       O  
ATOM     53  ND2 ASN A  58      10.937 -42.750 -45.161  1.00147.77           N  
ANISOU   53  ND2 ASN A  58    24215  12543  19388   2450    249  -2152       N  
ATOM     54  N   THR A  59       6.568 -42.022 -41.044  1.00 76.11           N  
ANISOU   54  N   THR A  59    14317   3820  10782    785   -612  -1001       N  
ATOM     55  CA  THR A  59       6.129 -42.308 -39.684  1.00 75.27           C  
ANISOU   55  CA  THR A  59    14062   3661  10875    556   -743   -679       C  
ATOM     56  C   THR A  59       4.969 -43.296 -39.717  1.00 80.40           C  
ANISOU   56  C   THR A  59    15035   3900  11614    206   -980   -715       C  
ATOM     57  O   THR A  59       3.974 -43.073 -40.407  1.00 80.59           O  
ANISOU   57  O   THR A  59    15137   3968  11517   -102  -1111   -850       O  
ATOM     58  CB  THR A  59       5.699 -41.030 -38.940  1.00 69.74           C  
ANISOU   58  CB  THR A  59    12926   3460  10112    334   -747   -457       C  
ATOM     59  OG1 THR A  59       4.691 -40.348 -39.697  1.00 68.21           O  
ANISOU   59  OG1 THR A  59    12736   3438   9744     48   -840   -603       O  
ATOM     60  CG2 THR A  59       6.890 -40.104 -38.737  1.00 65.25           C  
ANISOU   60  CG2 THR A  59    12039   3269   9482    652   -536   -387       C  
ATOM     61  N   ASP A  60       5.103 -44.388 -38.970  1.00 84.95           N  
ANISOU   61  N   ASP A  60    15796   4074  12409    249  -1045   -584       N  
ATOM     62  CA  ASP A  60       4.110 -45.460 -38.983  1.00 90.88           C  
ANISOU   62  CA  ASP A  60    16889   4369  13272    -71  -1270   -608       C  
ATOM     63  C   ASP A  60       2.728 -45.005 -38.518  1.00 88.73           C  
ANISOU   63  C   ASP A  60    16423   4301  12990   -584  -1441   -443       C  
ATOM     64  O   ASP A  60       2.587 -43.967 -37.871  1.00 83.08           O  
ANISOU   64  O   ASP A  60    15302   4019  12245   -667  -1384   -224       O  
ATOM     65  CB  ASP A  60       4.592 -46.655 -38.153  1.00139.29           C  
ANISOU   65  CB  ASP A  60    23201  10070  19654     62  -1305   -422       C  
ATOM     66  CG  ASP A  60       5.129 -46.247 -36.792  1.00136.37           C  
ANISOU   66  CG  ASP A  60    22468   9948  19398     17  -1279    -21       C  
ATOM     67  OD1 ASP A  60       4.597 -45.286 -36.199  1.00134.98           O  
ANISOU   67  OD1 ASP A  60    22243   9736  19308   -374  -1428    204       O  
ATOM     68  OD2 ASP A  60       6.084 -46.895 -36.313  1.00135.53           O  
ANISOU   68  OD2 ASP A  60    22123  10081  19289    365  -1111     73       O  
ATOM     69  N   ILE A  61       1.714 -45.796 -38.855  1.00102.24           N  
ANISOU   69  N   ILE A  61    18426   5691  14728   -923  -1652   -556       N  
ATOM     70  CA  ILE A  61       0.329 -45.462 -38.541  1.00101.11           C  
ANISOU   70  CA  ILE A  61    18109   5722  14584  -1423  -1829   -427       C  
ATOM     71  C   ILE A  61       0.072 -45.462 -37.035  1.00 99.75           C  
ANISOU   71  C   ILE A  61    17670   5644  14585  -1615  -1845    -24       C  
ATOM     72  O   ILE A  61      -0.777 -44.717 -36.544  1.00 96.24           O  
ANISOU   72  O   ILE A  61    16874   5587  14104  -1871  -1862    147       O  
ATOM     73  CB  ILE A  61      -0.648 -46.435 -39.233  1.00100.25           C  
ANISOU   73  CB  ILE A  61    18397   5194  14501  -1761  -2077   -616       C  
ATOM     74  CG1 ILE A  61      -0.231 -46.664 -40.687  1.00102.74           C  
ANISOU   74  CG1 ILE A  61    19059   5349  14627  -1542  -2059  -1035       C  
ATOM     75  CG2 ILE A  61      -2.076 -45.911 -39.160  1.00 99.38           C  
ANISOU   75  CG2 ILE A  61    18052   5338  14370  -2263  -2254   -507       C  
ATOM     76  CD1 ILE A  61      -1.158 -47.584 -41.450  1.00109.03           C  
ANISOU   76  CD1 ILE A  61    20323   5586  15517  -1243  -2030  -1206       C  
ATOM     77  N   TYR A  62       0.812 -46.298 -36.311  1.00102.41           N  
ANISOU   77  N   TYR A  62    18184   5626  15103  -1476  -1836    127       N  
ATOM     78  CA  TYR A  62       0.673 -46.401 -34.859  1.00101.69           C  
ANISOU   78  CA  TYR A  62    17902   5572  15164  -1657  -1858    518       C  
ATOM     79  C   TYR A  62       0.879 -45.051 -34.179  1.00 96.22           C  
ANISOU   79  C   TYR A  62    16741   5430  14388  -1527  -1687    724       C  
ATOM     80  O   TYR A  62       0.028 -44.587 -33.415  1.00 94.26           O  
ANISOU   80  O   TYR A  62    16217   5444  14155  -1813  -1708    976       O  
ATOM     81  CB  TYR A  62       1.672 -47.414 -34.295  1.00160.56           C  
ANISOU   81  CB  TYR A  62    25664  12527  22813  -1469  -1878    632       C  
ATOM     82  CG  TYR A  62       1.457 -48.834 -34.762  1.00163.85           C  
ANISOU   82  CG  TYR A  62    26576  12342  23336  -1625  -2065    454       C  
ATOM     83  CD1 TYR A  62       0.217 -49.257 -35.221  1.00164.43           C  
ANISOU   83  CD1 TYR A  62    26746  12353  23378  -2072  -2251    339       C  
ATOM     84  CD2 TYR A  62       2.497 -49.755 -34.741  1.00166.46           C  
ANISOU   84  CD2 TYR A  62    27283  12159  23804  -1325  -2067    401       C  
ATOM     85  CE1 TYR A  62       0.019 -50.557 -35.648  1.00167.50           C  
ANISOU   85  CE1 TYR A  62    27607  12176  23859  -2240  -2442    169       C  
ATOM     86  CE2 TYR A  62       2.309 -51.056 -35.164  1.00169.55           C  
ANISOU   86  CE2 TYR A  62    28162  11966  24292  -1467  -2244    225       C  
ATOM     87  CZ  TYR A  62       1.068 -51.452 -35.617  1.00170.04           C  
ANISOU   87  CZ  TYR A  62    28327  11971  24311  -1936  -2436    105       C  
ATOM     88  OH  TYR A  62       0.876 -52.748 -36.041  1.00173.19           O  
ANISOU   88  OH  TYR A  62    29229  11774  24802  -2101  -2633    -79       O  
ATOM     89  N   SER A  63       2.016 -44.427 -34.469  1.00102.36           N  
ANISOU   89  N   SER A  63    17432   6385  15076  -1099  -1514    612       N  
ATOM     90  CA  SER A  63       2.354 -43.133 -33.890  1.00 99.34           C  
ANISOU   90  CA  SER A  63    16631   6507  14605   -961  -1362    776       C  
ATOM     91  C   SER A  63       1.346 -42.061 -34.293  1.00 97.10           C  
ANISOU   91  C   SER A  63    16067   6660  14166  -1207  -1367    724       C  
ATOM     92  O   SER A  63       1.016 -41.184 -33.499  1.00 94.19           O  
ANISOU   92  O   SER A  63    15365   6658  13765  -1316  -1318    936       O  
ATOM     93  CB  SER A  63       3.768 -42.714 -34.298  1.00 85.95           C  
ANISOU   93  CB  SER A  63    14909   4894  12854   -469  -1188    648       C  
ATOM     94  OG  SER A  63       3.905 -42.689 -35.708  1.00 87.58           O  
ANISOU   94  OG  SER A  63    15237   5123  12917   -355  -1146    308       O  
ATOM     95  N   LYS A  64       0.855 -42.141 -35.526  1.00 75.18           N  
ANISOU   95  N   LYS A  64    13442   3835  11287  -1286  -1432    437       N  
ATOM     96  CA  LYS A  64      -0.126 -41.178 -36.019  1.00 71.71           C  
ANISOU   96  CA  LYS A  64    12770   3770  10708  -1519  -1468    375       C  
ATOM     97  C   LYS A  64      -1.448 -41.276 -35.263  1.00 73.28           C  
ANISOU   97  C   LYS A  64    12811   4035  10999  -1957  -1597    603       C  
ATOM     98  O   LYS A  64      -2.012 -40.262 -34.851  1.00 69.41           O  
ANISOU   98  O   LYS A  64    11970   3955  10450  -2072  -1552    738       O  
ATOM     99  CB  LYS A  64      -0.362 -41.360 -37.521  1.00 81.90           C  
ANISOU   99  CB  LYS A  64    14315   4931  11872  -1544  -1552     32       C  
ATOM    100  CG  LYS A  64       0.818 -40.955 -38.389  1.00 81.14           C  
ANISOU  100  CG  LYS A  64    14292   4912  11626  -1131  -1387   -202       C  
ATOM    101  CD  LYS A  64       0.454 -41.004 -39.864  1.00 84.03           C  
ANISOU  101  CD  LYS A  64    14975   5105  11849  -1166  -1475   -545       C  
ATOM    102  CE  LYS A  64       1.599 -40.514 -40.735  1.00 81.86           C  
ANISOU  102  CE  LYS A  64    14600   5158  11345   -910  -1320   -729       C  
ATOM    103  NZ  LYS A  64       1.249 -40.542 -42.183  1.00 84.78           N  
ANISOU  103  NZ  LYS A  64    15297   5378  11537   -945  -1403  -1063       N  
ATOM    104  N   VAL A  65      -1.936 -42.499 -35.081  1.00 78.79           N  
ANISOU  104  N   VAL A  65    13770   4323  11843  -2196  -1751    647       N  
ATOM    105  CA  VAL A  65      -3.186 -42.724 -34.363  1.00 81.37           C  
ANISOU  105  CA  VAL A  65    13959   4683  12275  -2636  -1871    878       C  
ATOM    106  C   VAL A  65      -3.044 -42.351 -32.887  1.00 79.29           C  
ANISOU  106  C   VAL A  65    13415   4647  12066  -2624  -1748   1223       C  
ATOM    107  O   VAL A  65      -3.941 -41.742 -32.302  1.00 78.10           O  
ANISOU  107  O   VAL A  65    12955   4813  11905  -2877  -1741   1400       O  
ATOM    108  CB  VAL A  65      -3.659 -44.189 -34.491  1.00 88.94           C  
ANISOU  108  CB  VAL A  65    15293   5107  13394  -2897  -2065    867       C  
ATOM    109  CG1 VAL A  65      -4.904 -44.429 -33.650  1.00 91.98           C  
ANISOU  109  CG1 VAL A  65    15503   5546  13902  -3363  -2169   1149       C  
ATOM    110  CG2 VAL A  65      -3.927 -44.532 -35.946  1.00 91.69           C  
ANISOU  110  CG2 VAL A  65    15931   5241  13664  -2957  -2211    514       C  
ATOM    111  N   LEU A  66      -1.909 -42.714 -32.296  1.00 79.15           N  
ANISOU  111  N   LEU A  66    13503   4475  12097  -2319  -1651   1314       N  
ATOM    112  CA  LEU A  66      -1.628 -42.387 -30.901  1.00 77.65           C  
ANISOU  112  CA  LEU A  66    13088   4484  11932  -2278  -1545   1635       C  
ATOM    113  C   LEU A  66      -1.614 -40.877 -30.680  1.00 71.18           C  
ANISOU  113  C   LEU A  66    11873   4217  10955  -2182  -1405   1661       C  
ATOM    114  O   LEU A  66      -2.316 -40.354 -29.806  1.00 70.39           O  
ANISOU  114  O   LEU A  66    11508   4400  10836  -2383  -1367   1879       O  
ATOM    115  CB  LEU A  66      -0.288 -42.987 -30.474  1.00 79.03           C  
ANISOU  115  CB  LEU A  66    13457   4391  12180  -1925  -1489   1701       C  
ATOM    116  CG  LEU A  66       0.158 -42.711 -29.037  1.00 78.02           C  
ANISOU  116  CG  LEU A  66    13136   4445  12060  -1850  -1399   2031       C  
ATOM    117  CD1 LEU A  66      -0.793 -43.363 -28.044  1.00 82.10           C  
ANISOU  117  CD1 LEU A  66    13635   4899  12662  -2250  -1474   2324       C  
ATOM    118  CD2 LEU A  66       1.586 -43.187 -28.813  1.00 79.62           C  
ANISOU  118  CD2 LEU A  66    13527   4381  12341  -1468  -1368   2072       C  
ATOM    119  N   VAL A  67      -0.811 -40.186 -31.484  1.00 70.82           N  
ANISOU  119  N   VAL A  67    11799   4316  10794  -1876  -1322   1437       N  
ATOM    120  CA  VAL A  67      -0.697 -38.734 -31.413  1.00 66.24           C  
ANISOU  120  CA  VAL A  67    10881   4221  10065  -1768  -1199   1436       C  
ATOM    121  C   VAL A  67      -2.043 -38.062 -31.666  1.00 65.16           C  
ANISOU  121  C   VAL A  67    10533   4351   9871  -2082  -1255   1417       C  
ATOM    122  O   VAL A  67      -2.381 -37.086 -31.008  1.00 62.35           O  
ANISOU  122  O   VAL A  67     9873   4369   9446  -2125  -1175   1542       O  
ATOM    123  CB  VAL A  67       0.369 -38.199 -32.399  1.00 88.06           C  
ANISOU  123  CB  VAL A  67    13680   7060  12721  -1408  -1108   1193       C  
ATOM    124  CG1 VAL A  67       0.235 -36.697 -32.588  1.00 85.83           C  
ANISOU  124  CG1 VAL A  67    13069   7254  12288  -1346  -1007   1182       C  
ATOM    125  CG2 VAL A  67       1.764 -38.549 -31.906  1.00 89.70           C  
ANISOU  125  CG2 VAL A  67    14012   7076  12995  -1069  -1034   1246       C  
ATOM    126  N   THR A  68      -2.813 -38.597 -32.609  1.00 63.24           N  
ANISOU  126  N   THR A  68    10457   3908   9661  -2297  -1401   1259       N  
ATOM    127  CA  THR A  68      -4.146 -38.072 -32.888  1.00 63.36           C  
ANISOU  127  CA  THR A  68    10272   4151   9650  -2611  -1486   1252       C  
ATOM    128  C   THR A  68      -5.055 -38.207 -31.669  1.00 65.74           C  
ANISOU  128  C   THR A  68    10367   4562  10047  -2905  -1485   1552       C  
ATOM    129  O   THR A  68      -5.783 -37.276 -31.325  1.00 63.72           O  
ANISOU  129  O   THR A  68     9789   4681   9741  -3013  -1434   1640       O  
ATOM    130  CB  THR A  68      -4.796 -38.782 -34.091  1.00 67.27           C  
ANISOU  130  CB  THR A  68    11016   4373  10170  -2813  -1679   1035       C  
ATOM    131  OG1 THR A  68      -3.999 -38.564 -35.261  1.00 65.16           O  
ANISOU  131  OG1 THR A  68    10930   4055   9774  -2540  -1659    747       O  
ATOM    132  CG2 THR A  68      -6.200 -38.248 -34.336  1.00 68.00           C  
ANISOU  132  CG2 THR A  68    10865   4717  10255  -3150  -1790   1058       C  
ATOM    133  N   ALA A  69      -5.001 -39.365 -31.017  1.00 71.35           N  
ANISOU  133  N   ALA A  69    11272   4944  10895  -3023  -1532   1713       N  
ATOM    134  CA  ALA A  69      -5.807 -39.619 -29.826  1.00 74.30           C  
ANISOU  134  CA  ALA A  69    11481   5398  11352  -3313  -1516   2021       C  
ATOM    135  C   ALA A  69      -5.452 -38.657 -28.694  1.00 70.61           C  
ANISOU  135  C   ALA A  69    10738   5301  10788  -3150  -1328   2211       C  
ATOM    136  O   ALA A  69      -6.335 -38.033 -28.095  1.00 70.57           O  
ANISOU  136  O   ALA A  69    10443   5614  10759  -3338  -1265   2368       O  
ATOM    137  CB  ALA A  69      -5.643 -41.058 -29.373  1.00 79.16           C  
ANISOU  137  CB  ALA A  69    12405   5552  12123  -3440  -1604   2163       C  
ATOM    138  N   ILE A  70      -4.157 -38.541 -28.411  1.00 66.94           N  
ANISOU  138  N   ILE A  70    10365   4800  10268  -2797  -1239   2191       N  
ATOM    139  CA  ILE A  70      -3.671 -37.609 -27.395  1.00 63.59           C  
ANISOU  139  CA  ILE A  70     9715   4712   9735  -2622  -1082   2342       C  
ATOM    140  C   ILE A  70      -4.107 -36.186 -27.729  1.00 59.18           C  
ANISOU  140  C   ILE A  70     8850   4588   9048  -2602  -1009   2237       C  
ATOM    141  O   ILE A  70      -4.533 -35.428 -26.855  1.00 58.44           O  
ANISOU  141  O   ILE A  70     8507   4810   8889  -2672   -909   2394       O  
ATOM    142  CB  ILE A  70      -2.134 -37.660 -27.279  1.00 61.49           C  
ANISOU  142  CB  ILE A  70     9587   4338   9438  -2235  -1027   2301       C  
ATOM    143  CG1 ILE A  70      -1.677 -39.063 -26.872  1.00 66.28           C  
ANISOU  143  CG1 ILE A  70    10476   4529  10178  -2228  -1093   2453       C  
ATOM    144  CG2 ILE A  70      -1.631 -36.622 -26.286  1.00 57.86           C  
ANISOU  144  CG2 ILE A  70     8884   4256   8844  -2064   -890   2414       C  
ATOM    145  CD1 ILE A  70      -0.174 -39.207 -26.749  1.00 65.04           C  
ANISOU  145  CD1 ILE A  70    10434   4261  10017  -1838  -1050   2438       C  
ATOM    146  N   TYR A  71      -4.011 -35.843 -29.010  1.00 64.73           N  
ANISOU  146  N   TYR A  71     9591   5295   9710  -2502  -1059   1971       N  
ATOM    147  CA  TYR A  71      -4.408 -34.534 -29.511  1.00 62.93           C  
ANISOU  147  CA  TYR A  71     9108   5433   9370  -2477  -1018   1858       C  
ATOM    148  C   TYR A  71      -5.884 -34.247 -29.252  1.00 62.72           C  
ANISOU  148  C   TYR A  71     8847   5603   9381  -2798  -1048   1963       C  
ATOM    149  O   TYR A  71      -6.243 -33.145 -28.846  1.00 60.76           O  
ANISOU  149  O   TYR A  71     8324   5708   9055  -2779   -953   2013       O  
ATOM    150  CB  TYR A  71      -4.117 -34.429 -31.009  1.00 60.89           C  
ANISOU  150  CB  TYR A  71     8979   5098   9061  -2356  -1092   1567       C  
ATOM    151  CG  TYR A  71      -2.771 -33.826 -31.342  1.00 60.38           C  
ANISOU  151  CG  TYR A  71     8985   5054   8903  -1991   -998   1449       C  
ATOM    152  CD1 TYR A  71      -1.639 -34.151 -30.604  1.00 59.83           C  
ANISOU  152  CD1 TYR A  71     8950   4937   8848  -1796   -906   1585       C  
ATOM    153  CD2 TYR A  71      -2.633 -32.939 -32.402  1.00 60.64           C  
ANISOU  153  CD2 TYR A  71     9040   5169   8832  -1852  -1005   1216       C  
ATOM    154  CE1 TYR A  71      -0.410 -33.605 -30.908  1.00 59.61           C  
ANISOU  154  CE1 TYR A  71     8951   4947   8751  -1474   -825   1490       C  
ATOM    155  CE2 TYR A  71      -1.409 -32.388 -32.716  1.00 60.48           C  
ANISOU  155  CE2 TYR A  71     9061   5188   8733  -1535   -906   1124       C  
ATOM    156  CZ  TYR A  71      -0.300 -32.724 -31.966  1.00 59.99           C  
ANISOU  156  CZ  TYR A  71     9007   5084   8705  -1349   -816   1261       C  
ATOM    157  OH  TYR A  71       0.920 -32.175 -32.277  1.00 60.08           O  
ANISOU  157  OH  TYR A  71     9024   5152   8652  -1045   -722   1182       O  
ATOM    158  N   LEU A  72      -6.734 -35.241 -29.490  1.00 63.77           N  
ANISOU  158  N   LEU A  72     9086   5504   9640  -3090  -1181   1993       N  
ATOM    159  CA  LEU A  72      -8.170 -35.082 -29.278  1.00 65.54           C  
ANISOU  159  CA  LEU A  72     9065   5911   9927  -3420  -1218   2111       C  
ATOM    160  C   LEU A  72      -8.520 -34.997 -27.796  1.00 66.36           C  
ANISOU  160  C   LEU A  72     8974   6208  10034  -3513  -1070   2401       C  
ATOM    161  O   LEU A  72      -9.422 -34.251 -27.407  1.00 66.29           O  
ANISOU  161  O   LEU A  72     8653   6532  10002  -3624   -996   2486       O  
ATOM    162  CB  LEU A  72      -8.948 -36.218 -29.944  1.00 68.20           C  
ANISOU  162  CB  LEU A  72     9576   5931  10406  -3738  -1416   2082       C  
ATOM    163  CG  LEU A  72      -8.839 -36.297 -31.468  1.00 67.67           C  
ANISOU  163  CG  LEU A  72     9691   5709  10312  -3704  -1581   1784       C  
ATOM    164  CD1 LEU A  72      -9.758 -37.376 -32.024  1.00 73.76           C  
ANISOU  164  CD1 LEU A  72    10639   6165  11221  -4059  -1795   1766       C  
ATOM    165  CD2 LEU A  72      -9.140 -34.947 -32.103  1.00 64.19           C  
ANISOU  165  CD2 LEU A  72     8980   5643   9766  -3639  -1575   1663       C  
ATOM    166  N   ALA A  73      -7.807 -35.763 -26.973  1.00 65.65           N  
ANISOU  166  N   ALA A  73     9070   5910   9963  -3456  -1024   2554       N  
ATOM    167  CA  ALA A  73      -7.992 -35.701 -25.526  1.00 67.33           C  
ANISOU  167  CA  ALA A  73     9142   6298  10143  -3531   -880   2836       C  
ATOM    168  C   ALA A  73      -7.650 -34.308 -25.003  1.00 62.83           C  
ANISOU  168  C   ALA A  73     8345   6122   9404  -3288   -714   2823       C  
ATOM    169  O   ALA A  73      -8.434 -33.690 -24.275  1.00 63.60           O  
ANISOU  169  O   ALA A  73     8184   6533   9448  -3390   -592   2958       O  
ATOM    170  CB  ALA A  73      -7.142 -36.753 -24.836  1.00 71.12           C  
ANISOU  170  CB  ALA A  73     9901   6457  10666  -3487   -890   2997       C  
ATOM    171  N   LEU A  74      -6.476 -33.815 -25.389  1.00 66.95           N  
ANISOU  171  N   LEU A  74     8968   6626   9843  -2967   -706   2655       N  
ATOM    172  CA  LEU A  74      -6.043 -32.477 -25.004  1.00 64.55           C  
ANISOU  172  CA  LEU A  74     8486   6656   9383  -2736   -576   2616       C  
ATOM    173  C   LEU A  74      -6.959 -31.419 -25.608  1.00 63.88           C  
ANISOU  173  C   LEU A  74     8142   6859   9270  -2789   -563   2495       C  
ATOM    174  O   LEU A  74      -7.070 -30.309 -25.086  1.00 62.39           O  
ANISOU  174  O   LEU A  74     7751   6981   8971  -2689   -442   2512       O  
ATOM    175  CB  LEU A  74      -4.601 -32.231 -25.448  1.00 50.53           C  
ANISOU  175  CB  LEU A  74     6868   4781   7550  -2411   -591   2461       C  
ATOM    176  CG  LEU A  74      -3.525 -33.110 -24.809  1.00 51.92           C  
ANISOU  176  CG  LEU A  74     7266   4713   7748  -2284   -597   2582       C  
ATOM    177  CD1 LEU A  74      -2.185 -32.880 -25.488  1.00 48.49           C  
ANISOU  177  CD1 LEU A  74     6947   4195   7283  -1968   -614   2405       C  
ATOM    178  CD2 LEU A  74      -3.428 -32.840 -23.317  1.00 53.00           C  
ANISOU  178  CD2 LEU A  74     7310   5043   7786  -2283   -486   2819       C  
ATOM    179  N   PHE A  75      -7.615 -31.773 -26.708  1.00 53.79           N  
ANISOU  179  N   PHE A  75     6882   5464   8090  -2942   -700   2371       N  
ATOM    180  CA  PHE A  75      -8.545 -30.871 -27.375  1.00 52.91           C  
ANISOU  180  CA  PHE A  75     6529   5603   7973  -3006   -724   2269       C  
ATOM    181  C   PHE A  75      -9.810 -30.693 -26.553  1.00 56.27           C  
ANISOU  181  C   PHE A  75     6671   6270   8440  -3234   -640   2461       C  
ATOM    182  O   PHE A  75     -10.214 -29.569 -26.266  1.00 54.79           O  
ANISOU  182  O   PHE A  75     6234   6404   8181  -3149   -532   2461       O  
ATOM    183  CB  PHE A  75      -8.904 -31.391 -28.766  1.00 57.08           C  
ANISOU  183  CB  PHE A  75     7172   5932   8582  -3124   -921   2091       C  
ATOM    184  CG  PHE A  75      -9.889 -30.528 -29.501  1.00 56.58           C  
ANISOU  184  CG  PHE A  75     6864   6118   8514  -3186   -979   1995       C  
ATOM    185  CD1 PHE A  75      -9.476 -29.372 -30.142  1.00 52.28           C  
ANISOU  185  CD1 PHE A  75     6280   5726   7857  -2945   -969   1824       C  
ATOM    186  CD2 PHE A  75     -11.229 -30.874 -29.556  1.00 60.80           C  
ANISOU  186  CD2 PHE A  75     7200   6735   9166  -3489  -1052   2091       C  
ATOM    187  CE1 PHE A  75     -10.381 -28.577 -30.821  1.00 52.19           C  
ANISOU  187  CE1 PHE A  75     6052   5931   7844  -2989  -1038   1751       C  
ATOM    188  CE2 PHE A  75     -12.138 -30.083 -30.232  1.00 60.78           C  
ANISOU  188  CE2 PHE A  75     6953   6967   9171  -3531  -1122   2016       C  
ATOM    189  CZ  PHE A  75     -11.713 -28.933 -30.865  1.00 56.45           C  
ANISOU  189  CZ  PHE A  75     6386   6556   8506  -3272  -1119   1846       C  
ATOM    190  N   VAL A  76     -10.442 -31.802 -26.182  1.00 80.50           N  
ANISOU  190  N   VAL A  76     9778   9182  11629  -3521   -683   2627       N  
ATOM    191  CA  VAL A  76     -11.665 -31.725 -25.389  1.00 81.43           C  
ANISOU  191  CA  VAL A  76     9607   9541  11791  -3758   -585   2832       C  
ATOM    192  C   VAL A  76     -11.394 -31.167 -23.989  1.00 80.25           C  
ANISOU  192  C   VAL A  76     9357   9634  11502  -3624   -356   2989       C  
ATOM    193  O   VAL A  76     -12.073 -30.234 -23.548  1.00 79.93           O  
ANISOU  193  O   VAL A  76     9029   9937  11404  -3597   -220   3022       O  
ATOM    194  CB  VAL A  76     -12.423 -33.078 -25.324  1.00 76.58           C  
ANISOU  194  CB  VAL A  76     9059   8696  11341  -4134   -685   2999       C  
ATOM    195  CG1 VAL A  76     -13.102 -33.368 -26.655  1.00 78.26           C  
ANISOU  195  CG1 VAL A  76     9267   8782  11683  -4324   -909   2849       C  
ATOM    196  CG2 VAL A  76     -11.491 -34.215 -24.939  1.00 77.68           C  
ANISOU  196  CG2 VAL A  76     9556   8465  11493  -4117   -718   3082       C  
ATOM    197  N   VAL A  77     -10.388 -31.715 -23.311  1.00 63.90           N  
ANISOU  197  N   VAL A  77     7530   7382   9367  -3523   -320   3076       N  
ATOM    198  CA  VAL A  77     -10.036 -31.259 -21.968  1.00 63.72           C  
ANISOU  198  CA  VAL A  77     7459   7566   9188  -3410   -129   3230       C  
ATOM    199  C   VAL A  77      -9.640 -29.784 -21.976  1.00 59.06           C  
ANISOU  199  C   VAL A  77     6745   7248   8447  -3117    -37   3070       C  
ATOM    200  O   VAL A  77     -10.091 -29.000 -21.136  1.00 59.45           O  
ANISOU  200  O   VAL A  77     6603   7601   8384  -3081    132   3142       O  
ATOM    201  CB  VAL A  77      -8.893 -32.102 -21.361  1.00 64.29           C  
ANISOU  201  CB  VAL A  77     7833   7372   9222  -3335   -150   3347       C  
ATOM    202  CG1 VAL A  77      -8.436 -31.512 -20.035  1.00 63.90           C  
ANISOU  202  CG1 VAL A  77     7749   7553   8976  -3198     22   3483       C  
ATOM    203  CG2 VAL A  77      -9.339 -33.545 -21.180  1.00 69.61           C  
ANISOU  203  CG2 VAL A  77     8641   7765  10041  -3636   -230   3540       C  
ATOM    204  N   GLY A  78      -8.810 -29.410 -22.944  1.00 67.84           N  
ANISOU  204  N   GLY A  78     7975   8245   9555  -2912   -145   2850       N  
ATOM    205  CA  GLY A  78      -8.342 -28.043 -23.063  1.00 65.83           C  
ANISOU  205  CA  GLY A  78     7639   8203   9172  -2646    -84   2697       C  
ATOM    206  C   GLY A  78      -9.442 -27.050 -23.385  1.00 66.16           C  
ANISOU  206  C   GLY A  78     7392   8523   9221  -2668    -37   2623       C  
ATOM    207  O   GLY A  78      -9.584 -26.035 -22.705  1.00 65.57           O  
ANISOU  207  O   GLY A  78     7176   8708   9028  -2539    102   2624       O  
ATOM    208  N   THR A  79     -10.216 -27.337 -24.428  1.00 64.36           N  
ANISOU  208  N   THR A  79     7086   8236   9133  -2825   -165   2555       N  
ATOM    209  CA  THR A  79     -11.289 -26.443 -24.856  1.00 64.97           C  
ANISOU  209  CA  THR A  79     6876   8568   9243  -2839   -153   2491       C  
ATOM    210  C   THR A  79     -12.359 -26.287 -23.785  1.00 66.29           C  
ANISOU  210  C   THR A  79     6775   9005   9409  -2963     24   2674       C  
ATOM    211  O   THR A  79     -12.736 -25.165 -23.442  1.00 66.22           O  
ANISOU  211  O   THR A  79     6567   9269   9326  -2816    150   2640       O  
ATOM    212  CB  THR A  79     -11.948 -26.910 -26.170  1.00 66.38           C  
ANISOU  212  CB  THR A  79     7026   8625   9570  -3012   -357   2399       C  
ATOM    213  OG1 THR A  79     -12.226 -28.314 -26.096  1.00 67.52           O  
ANISOU  213  OG1 THR A  79     7267   8553   9835  -3295   -433   2527       O  
ATOM    214  CG2 THR A  79     -11.030 -26.637 -27.353  1.00 66.43           C  
ANISOU  214  CG2 THR A  79     7251   8454   9536  -2838   -499   2179       C  
ATOM    215  N   VAL A  80     -12.845 -27.409 -23.259  1.00 67.08           N  
ANISOU  215  N   VAL A  80     6878   9023   9587  -3227     42   2870       N  
ATOM    216  CA  VAL A  80     -13.842 -27.365 -22.194  1.00 69.68           C  
ANISOU  216  CA  VAL A  80     6951   9619   9906  -3363    236   3067       C  
ATOM    217  C   VAL A  80     -13.300 -26.600 -20.989  1.00 68.28           C  
ANISOU  217  C   VAL A  80     6802   9625   9516  -3144    449   3105       C  
ATOM    218  O   VAL A  80     -13.949 -25.683 -20.485  1.00 68.84           O  
ANISOU  218  O   VAL A  80     6637  10002   9515  -3051    618   3106       O  
ATOM    219  CB  VAL A  80     -14.297 -28.775 -21.764  1.00 74.11           C  
ANISOU  219  CB  VAL A  80     7553  10032  10574  -3703    220   3298       C  
ATOM    220  CG1 VAL A  80     -15.119 -28.706 -20.485  1.00 76.35           C  
ANISOU  220  CG1 VAL A  80     7607  10608  10796  -3816    467   3524       C  
ATOM    221  CG2 VAL A  80     -15.094 -29.438 -22.878  1.00 75.49           C  
ANISOU  221  CG2 VAL A  80     7646  10076  10963  -3964     14   3268       C  
ATOM    222  N   GLY A  81     -12.096 -26.964 -20.554  1.00 68.88           N  
ANISOU  222  N   GLY A  81     7174   9508   9490  -3049    429   3124       N  
ATOM    223  CA  GLY A  81     -11.466 -26.326 -19.412  1.00 67.75           C  
ANISOU  223  CA  GLY A  81     7110   9502   9132  -2863    588   3164       C  
ATOM    224  C   GLY A  81     -11.327 -24.819 -19.539  1.00 64.13           C  
ANISOU  224  C   GLY A  81     6567   9245   8554  -2583    652   2974       C  
ATOM    225  O   GLY A  81     -11.745 -24.074 -18.653  1.00 64.82           O  
ANISOU  225  O   GLY A  81     6574   9571   8484  -2487    836   3010       O  
ATOM    226  N   ASN A  82     -10.746 -24.369 -20.647  1.00 67.24           N  
ANISOU  226  N   ASN A  82     7006   9532   9011  -2449    500   2771       N  
ATOM    227  CA  ASN A  82     -10.507 -22.944 -20.861  1.00 66.47           C  
ANISOU  227  CA  ASN A  82     6853   9588   8814  -2194    537   2596       C  
ATOM    228  C   ASN A  82     -11.778 -22.133 -21.117  1.00 68.16           C  
ANISOU  228  C   ASN A  82     6759  10054   9085  -2186    619   2556       C  
ATOM    229  O   ASN A  82     -11.915 -21.013 -20.621  1.00 68.67           O  
ANISOU  229  O   ASN A  82     6736  10323   9033  -2007    753   2495       O  
ATOM    230  CB  ASN A  82      -9.499 -22.729 -21.994  1.00 55.47           C  
ANISOU  230  CB  ASN A  82     5624   8000   7452  -2054    358   2413       C  
ATOM    231  CG  ASN A  82      -8.103 -23.190 -21.626  1.00 53.81           C  
ANISOU  231  CG  ASN A  82     5685   7598   7163  -1977    311   2434       C  
ATOM    232  OD1 ASN A  82      -7.364 -22.481 -20.942  1.00 52.84           O  
ANISOU  232  OD1 ASN A  82     5637   7551   6887  -1815    375   2414       O  
ATOM    233  ND2 ASN A  82      -7.734 -24.382 -22.079  1.00 53.79           N  
ANISOU  233  ND2 ASN A  82     5830   7339   7267  -2090    190   2474       N  
ATOM    234  N   SER A  83     -12.702 -22.694 -21.892  1.00 88.65           N  
ANISOU  234  N   SER A  83     9191  12630  11863  -2379    530   2591       N  
ATOM    235  CA  SER A  83     -13.967 -22.016 -22.163  1.00 90.48           C  
ANISOU  235  CA  SER A  83     9092  13106  12181  -2382    585   2574       C  
ATOM    236  C   SER A  83     -14.773 -21.848 -20.877  1.00 92.34           C  
ANISOU  236  C   SER A  83     9134  13616  12336  -2401    848   2719       C  
ATOM    237  O   SER A  83     -15.264 -20.753 -20.573  1.00 93.51           O  
ANISOU  237  O   SER A  83     9095  14000  12437  -2223    981   2655       O  
ATOM    238  CB  SER A  83     -14.782 -22.783 -23.206  1.00100.54           C  
ANISOU  238  CB  SER A  83    10227  14306  13668  -2629    416   2610       C  
ATOM    239  OG  SER A  83     -15.043 -24.107 -22.775  1.00100.93           O  
ANISOU  239  OG  SER A  83    10370  14200  13778  -2900    394   2778       O  
ATOM    240  N   VAL A  84     -14.892 -22.940 -20.125  1.00 73.22           N  
ANISOU  240  N   VAL A  84     6771  11159   9890  -2607    929   2916       N  
ATOM    241  CA  VAL A  84     -15.573 -22.921 -18.834  1.00 76.73           C  
ANISOU  241  CA  VAL A  84     7057  11870  10224  -2641   1199   3071       C  
ATOM    242  C   VAL A  84     -14.871 -21.965 -17.874  1.00 74.70           C  
ANISOU  242  C   VAL A  84     6934  11730   9719  -2361   1354   2980       C  
ATOM    243  O   VAL A  84     -15.518 -21.291 -17.073  1.00 76.70           O  
ANISOU  243  O   VAL A  84     7009  12258   9876  -2258   1575   2988       O  
ATOM    244  CB  VAL A  84     -15.681 -24.341 -18.221  1.00 79.97           C  
ANISOU  244  CB  VAL A  84     7542  12204  10640  -2933   1248   3325       C  
ATOM    245  CG1 VAL A  84     -16.039 -24.278 -16.749  1.00 79.24           C  
ANISOU  245  CG1 VAL A  84     7833  11847  10427  -2899   1161   3344       C  
ATOM    246  CG2 VAL A  84     -16.710 -25.165 -18.980  1.00 82.06           C  
ANISOU  246  CG2 VAL A  84     7615  12784  10782  -2976   1547   3490       C  
ATOM    247  N   THR A  85     -13.548 -21.895 -17.972  1.00 63.21           N  
ANISOU  247  N   THR A  85     5790  10067   8160  -2239   1235   2889       N  
ATOM    248  CA  THR A  85     -12.776 -20.945 -17.180  1.00 61.13           C  
ANISOU  248  CA  THR A  85     5674   9884   7667  -1992   1333   2787       C  
ATOM    249  C   THR A  85     -13.206 -19.516 -17.500  1.00 61.59           C  
ANISOU  249  C   THR A  85     5573  10095   7732  -1761   1374   2595       C  
ATOM    250  O   THR A  85     -13.493 -18.728 -16.597  1.00 63.17           O  
ANISOU  250  O   THR A  85     5725  10501   7775  -1608   1567   2556       O  
ATOM    251  CB  THR A  85     -11.265 -21.095 -17.433  1.00 52.66           C  
ANISOU  251  CB  THR A  85     4924   8558   6528  -1908   1159   2718       C  
ATOM    252  OG1 THR A  85     -10.841 -22.405 -17.036  1.00 54.67           O  
ANISOU  252  OG1 THR A  85     5334   8652   6787  -2097   1115   2904       O  
ATOM    253  CG2 THR A  85     -10.486 -20.055 -16.648  1.00 50.80           C  
ANISOU  253  CG2 THR A  85     4835   8413   6054  -1686   1241   2622       C  
ATOM    254  N   LEU A  86     -13.260 -19.196 -18.791  1.00 75.57           N  
ANISOU  254  N   LEU A  86     7275  11760   9681  -1736   1190   2477       N  
ATOM    255  CA  LEU A  86     -13.694 -17.877 -19.243  1.00 76.43           C  
ANISOU  255  CA  LEU A  86     7237  11982   9821  -1520   1195   2310       C  
ATOM    256  C   LEU A  86     -15.092 -17.533 -18.740  1.00 79.12           C  
ANISOU  256  C   LEU A  86     7247  12614  10202  -1505   1401   2368       C  
ATOM    257  O   LEU A  86     -15.314 -16.446 -18.204  1.00 80.47           O  
ANISOU  257  O   LEU A  86     7366  12942  10267  -1279   1549   2271       O  
ATOM    258  CB  LEU A  86     -13.658 -17.787 -20.770  1.00 62.21           C  
ANISOU  258  CB  LEU A  86     5414  10022   8201  -1535    949   2209       C  
ATOM    259  CG  LEU A  86     -12.286 -17.627 -21.427  1.00 59.86           C  
ANISOU  259  CG  LEU A  86     5404   9495   7847  -1425    778   2076       C  
ATOM    260  CD1 LEU A  86     -12.431 -17.503 -22.934  1.00 59.27           C  
ANISOU  260  CD1 LEU A  86     5297   9296   7928  -1450    559   1985       C  
ATOM    261  CD2 LEU A  86     -11.563 -16.417 -20.858  1.00 60.09           C  
ANISOU  261  CD2 LEU A  86     5532   9587   7712  -1169    857   1948       C  
ATOM    262  N   PHE A  87     -16.030 -18.461 -18.910  1.00125.26           N  
ANISOU  262  N   PHE A  87    12865  18526  16201  -1745   1413   2527       N  
ATOM    263  CA  PHE A  87     -17.402 -18.236 -18.462  1.00127.85           C  
ANISOU  263  CA  PHE A  87    12824  19154  16600  -1748   1610   2604       C  
ATOM    264  C   PHE A  87     -17.486 -18.089 -16.944  1.00129.32           C  
ANISOU  264  C   PHE A  87    13008  19560  16568  -1678   1924   2678       C  
ATOM    265  O   PHE A  87     -18.363 -17.398 -16.426  1.00131.20           O  
ANISOU  265  O   PHE A  87    13044  20039  16767  -1487   2122   2624       O  
ATOM    266  CB  PHE A  87     -18.323 -19.359 -18.945  1.00158.71           C  
ANISOU  266  CB  PHE A  87    16487  23084  20732  -2064   1535   2775       C  
ATOM    267  CG  PHE A  87     -18.580 -19.337 -20.425  1.00158.72           C  
ANISOU  267  CG  PHE A  87    16415  22948  20944  -2110   1249   2687       C  
ATOM    268  CD1 PHE A  87     -18.324 -18.197 -21.169  1.00158.31           C  
ANISOU  268  CD1 PHE A  87    16438  22827  20884  -1855   1122   2484       C  
ATOM    269  CD2 PHE A  87     -19.080 -20.455 -21.072  1.00159.31           C  
ANISOU  269  CD2 PHE A  87    16361  22956  21213  -2422   1100   2810       C  
ATOM    270  CE1 PHE A  87     -18.560 -18.173 -22.530  1.00158.38           C  
ANISOU  270  CE1 PHE A  87    16397  22721  21057  -1902    859   2411       C  
ATOM    271  CE2 PHE A  87     -19.318 -20.437 -22.433  1.00159.43           C  
ANISOU  271  CE2 PHE A  87    16332  22849  21393  -2472    826   2720       C  
ATOM    272  CZ  PHE A  87     -19.057 -19.294 -23.163  1.00158.94           C  
ANISOU  272  CZ  PHE A  87    16347  22737  21303  -2207    709   2523       C  
ATOM    273  N   THR A  88     -16.569 -18.744 -16.239  1.00113.60           N  
ANISOU  273  N   THR A  88    11253  17484  14427  -1820   1968   2801       N  
ATOM    274  CA  THR A  88     -16.500 -18.655 -14.786  1.00115.02           C  
ANISOU  274  CA  THR A  88    11477  17865  14360  -1778   2253   2885       C  
ATOM    275  C   THR A  88     -16.032 -17.269 -14.365  1.00115.12           C  
ANISOU  275  C   THR A  88    11677  17914  14151  -1456   2330   2679       C  
ATOM    276  O   THR A  88     -16.593 -16.661 -13.453  1.00117.26           O  
ANISOU  276  O   THR A  88    11865  18428  14263  -1315   2593   2659       O  
ATOM    277  CB  THR A  88     -15.541 -19.710 -14.204  1.00 88.54           C  
ANISOU  277  CB  THR A  88     8371  14386  10887  -2005   2243   3077       C  
ATOM    278  OG1 THR A  88     -16.060 -21.022 -14.455  1.00 86.25           O  
ANISOU  278  OG1 THR A  88     8395  13782  10596  -1981   1984   2992       O  
ATOM    279  CG2 THR A  88     -15.374 -19.516 -12.705  1.00 89.55           C  
ANISOU  279  CG2 THR A  88     8300  14526  11202  -2344   2240   3314       C  
ATOM    280  N   LEU A  89     -15.003 -16.771 -15.043  1.00 91.78           N  
ANISOU  280  N   LEU A  89     8977  14714  11179  -1343   2106   2525       N  
ATOM    281  CA  LEU A  89     -14.463 -15.448 -14.749  1.00 92.01           C  
ANISOU  281  CA  LEU A  89     9195  14747  11018  -1063   2143   2326       C  
ATOM    282  C   LEU A  89     -15.414 -14.349 -15.214  1.00 93.81           C  
ANISOU  282  C   LEU A  89     9200  15097  11347   -830   2201   2167       C  
ATOM    283  O   LEU A  89     -15.313 -13.201 -14.777  1.00 95.23           O  
ANISOU  283  O   LEU A  89     9456  15362  11364   -592   2333   2024       O  
ATOM    284  CB  LEU A  89     -13.092 -15.278 -15.405  1.00117.23           C  
ANISOU  284  CB  LEU A  89    12700  17659  14181  -1028   1888   2227       C  
ATOM    285  CG  LEU A  89     -12.065 -16.348 -15.028  1.00115.45           C  
ANISOU  285  CG  LEU A  89    12727  17310  13826  -1189   1832   2366       C  
ATOM    286  CD1 LEU A  89     -10.800 -16.203 -15.853  1.00113.07           C  
ANISOU  286  CD1 LEU A  89    12697  16772  13490  -1107   1606   2252       C  
ATOM    287  CD2 LEU A  89     -11.751 -16.295 -13.542  1.00116.90           C  
ANISOU  287  CD2 LEU A  89    12995  17687  13732  -1181   2069   2450       C  
ATOM    288  N   ALA A  90     -16.336 -14.707 -16.102  1.00107.23           N  
ANISOU  288  N   ALA A  90    10634  16795  13314   -899   2090   2193       N  
ATOM    289  CA  ALA A  90     -17.322 -13.758 -16.605  1.00109.04           C  
ANISOU  289  CA  ALA A  90    10609  17151  13671   -686   2131   2077       C  
ATOM    290  C   ALA A  90     -18.392 -13.450 -15.561  1.00112.05           C  
ANISOU  290  C   ALA A  90    10687  17858  14028   -642   2447   2162       C  
ATOM    291  O   ALA A  90     -18.778 -12.300 -15.378  1.00114.03           O  
ANISOU  291  O   ALA A  90    10763  18252  14309   -390   2567   2052       O  
ATOM    292  CB  ALA A  90     -17.961 -14.284 -17.882  1.00121.02           C  
ANISOU  292  CB  ALA A  90    11945  18568  15469   -786   1884   2089       C  
ATOM    293  N   ARG A  91     -18.869 -14.483 -14.877  1.00223.80           N  
ANISOU  293  N   ARG A  91    24780  32126  28128   -884   2588   2365       N  
ATOM    294  CA  ARG A  91     -19.922 -14.321 -13.881  1.00226.74           C  
ANISOU  294  CA  ARG A  91    24862  32831  28456   -880   2919   2479       C  
ATOM    295  C   ARG A  91     -19.344 -14.193 -12.473  1.00228.15           C  
ANISOU  295  C   ARG A  91    25232  33142  28314   -649   3187   2375       C  
ATOM    296  O   ARG A  91     -19.987 -14.580 -11.496  1.00230.73           O  
ANISOU  296  O   ARG A  91    25335  33733  28599   -466   3462   2342       O  
ATOM    297  CB  ARG A  91     -20.875 -15.515 -13.935  1.00182.45           C  
ANISOU  297  CB  ARG A  91    19151  27284  22887  -1249   2971   2752       C  
ATOM    298  CG  ARG A  91     -20.165 -16.840 -13.674  1.00184.49           C  
ANISOU  298  CG  ARG A  91    19183  27892  23024  -1281   3349   2901       C  
ATOM    299  CD  ARG A  91     -21.111 -18.024 -13.593  1.00184.79           C  
ANISOU  299  CD  ARG A  91    19238  27934  23041  -1660   3386   3181       C  
ATOM    300  NE  ARG A  91     -20.362 -19.261 -13.384  1.00185.20           N  
ANISOU  300  NE  ARG A  91    19038  27914  23414  -1946   3191   3324       N  
ATOM    301  CZ  ARG A  91     -19.781 -19.955 -14.358  1.00185.37           C  
ANISOU  301  CZ  ARG A  91    19067  27872  23492  -2310   3150   3567       C  
ATOM    302  NH1 ARG A  91     -19.862 -19.535 -15.611  1.00186.24           N  
ANISOU  302  NH1 ARG A  91    19417  27987  23358  -2425   3294   3709       N  
ATOM    303  NH2 ARG A  91     -19.120 -21.071 -14.083  1.00184.82           N  
ANISOU  303  NH2 ARG A  91    18781  27723  23718  -2566   2952   3669       N  
ATOM    304  N   LYS A  92     -18.128 -13.662 -12.381  1.00176.89           N  
ANISOU  304  N   LYS A  92    19153  26463  21594   -653   3100   2320       N  
ATOM    305  CA  LYS A  92     -17.438 -13.510 -11.101  1.00178.14           C  
ANISOU  305  CA  LYS A  92    19560  26721  21406   -491   3315   2235       C  
ATOM    306  C   LYS A  92     -18.257 -12.699 -10.098  1.00180.54           C  
ANISOU  306  C   LYS A  92    19798  27155  21644   -130   3492   2013       C  
ATOM    307  O   LYS A  92     -18.649 -13.208  -9.048  1.00180.36           O  
ANISOU  307  O   LYS A  92    19723  27011  21795     52   3336   1855       O  
ATOM    308  CB  LYS A  92     -16.070 -12.856 -11.311  1.00144.02           C  
ATOM    309  CG  LYS A  92     -15.194 -12.823 -10.068  1.00144.02           C  
ATOM    310  CD  LYS A  92     -14.836 -14.227  -9.610  1.00144.02           C  
ATOM    311  CE  LYS A  92     -13.916 -14.193  -8.404  1.00144.02           C  
ATOM    312  NZ  LYS A  92     -13.519 -15.561  -7.978  1.00144.02           N  
ATOM    313  N   LYS A  93     -18.508 -11.435 -10.426  1.00168.44           N  
ANISOU  313  N   LYS A  93    18284  25863  19850    -22   3820   2006       N  
ATOM    314  CA  LYS A  93     -19.306 -10.564  -9.570  1.00171.06           C  
ANISOU  314  CA  LYS A  93    18576  26325  20091    340   4031   1789       C  
ATOM    315  C   LYS A  93     -20.320  -9.767 -10.383  1.00170.51           C  
ANISOU  315  C   LYS A  93    18919  26004  19863    548   3862   1532       C  
ATOM    316  O   LYS A  93     -20.852 -10.255 -11.381  1.00171.17           O  
ANISOU  316  O   LYS A  93    18973  25988  20076    799   3783   1342       O  
ATOM    317  CB  LYS A  93     -18.406  -9.615  -8.775  1.00124.00           C  
ATOM    318  CG  LYS A  93     -17.501 -10.312  -7.772  1.00124.00           C  
ATOM    319  CD  LYS A  93     -16.641  -9.315  -7.015  1.00124.00           C  
ATOM    320  CE  LYS A  93     -15.740 -10.018  -6.014  1.00124.00           C  
ATOM    321  NZ  LYS A  93     -14.890  -9.057  -5.259  1.00124.00           N  
ATOM    322  N   SER A  97      -8.970  -6.718  -4.116  1.00147.24           N  
ANISOU  322  N   SER A  97    18928  22195  14824    449   3028    889       N  
ATOM    323  CA  SER A  97      -9.643  -7.133  -5.340  1.00146.31           C  
ANISOU  323  CA  SER A  97    18472  21990  15132    456   2957    938       C  
ATOM    324  C   SER A  97      -8.635  -7.409  -6.451  1.00142.70           C  
ANISOU  324  C   SER A  97    18070  21258  14891    333   2585    969       C  
ATOM    325  O   SER A  97      -8.956  -7.300  -7.634  1.00141.58           O  
ANISOU  325  O   SER A  97    17731  20995  15069    370   2475    947       O  
ATOM    326  CB  SER A  97     -10.642  -6.067  -5.792  1.00117.06           C  
ANISOU  326  CB  SER A  97    14636  18295  11544    743   3103    718       C  
ATOM    327  OG  SER A  97      -9.985  -4.851  -6.105  1.00119.72           O  
ANISOU  327  OG  SER A  97    15301  18571  11617    931   3123    462       O  
ATOM    328  N   LEU A  98      -7.414  -7.763  -6.062  1.00269.85           N  
ANISOU  328  N   LEU A  98    34438  37278  30814    192   2395   1026       N  
ATOM    329  CA  LEU A  98      -6.368  -8.077  -7.029  1.00266.30           C  
ANISOU  329  CA  LEU A  98    34021  36602  30561     66   2067   1087       C  
ATOM    330  C   LEU A  98      -6.659  -9.384  -7.755  1.00264.20           C  
ANISOU  330  C   LEU A  98    33518  36339  30528   -118   2033   1338       C  
ATOM    331  O   LEU A  98      -6.194  -9.597  -8.874  1.00261.76           O  
ANISOU  331  O   LEU A  98    33127  35855  30477   -180   1821   1374       O  
ATOM    332  CB  LEU A  98      -4.996  -8.145  -6.354  1.00141.19           C  
ANISOU  332  CB  LEU A  98    18500  20681  14464    -24   1866   1084       C  
ATOM    333  CG  LEU A  98      -4.260  -6.821  -6.125  1.00138.98           C  
ANISOU  333  CG  LEU A  98    18310  20158  14339    -29   1555    988       C  
ATOM    334  CD1 LEU A  98      -4.866  -6.037  -4.970  1.00140.39           C  
ANISOU  334  CD1 LEU A  98    18502  20235  14603    168   1568    738       C  
ATOM    335  CD2 LEU A  98      -2.777  -7.065  -5.896  1.00139.02           C  
ANISOU  335  CD2 LEU A  98    18598  20111  14110   -133   1343   1006       C  
ATOM    336  N   GLN A  99      -7.427 -10.258  -7.111  1.00158.89           N  
ANISOU  336  N   GLN A  99    20088  23196  17089   -212   2244   1511       N  
ATOM    337  CA  GLN A  99      -7.826 -11.518  -7.725  1.00157.37           C  
ANISOU  337  CA  GLN A  99    19673  23002  17121   -396   2235   1749       C  
ATOM    338  C   GLN A  99      -8.635 -11.229  -8.985  1.00157.15           C  
ANISOU  338  C   GLN A  99    19346  22921  17444   -340   2230   1698       C  
ATOM    339  O   GLN A  99      -8.456 -11.875 -10.018  1.00155.38           O  
ANISOU  339  O   GLN A  99    18980  22593  17467   -478   2106   1828       O  
ATOM    340  CB  GLN A  99      -8.640 -12.359  -6.740  1.00141.75           C  
ANISOU  340  CB  GLN A  99    17634  21259  14965   -506   2497   1941       C  
ATOM    341  CG  GLN A  99      -8.886 -13.786  -7.197  1.00140.23           C  
ANISOU  341  CG  GLN A  99    17294  21028  14958   -743   2448   2217       C  
ATOM    342  CD  GLN A  99      -9.596 -14.617  -6.149  1.00142.10           C  
ANISOU  342  CD  GLN A  99    17301  21502  15187   -833   2745   2378       C  
ATOM    343  OE1 GLN A  99      -8.960 -15.253  -5.309  1.00144.19           O  
ANISOU  343  OE1 GLN A  99    17479  21982  15326   -695   3007   2278       O  
ATOM    344  NE2 GLN A  99     -10.923 -14.619  -6.195  1.00141.52           N  
ANISOU  344  NE2 GLN A  99    17129  21389  15254  -1065   2709   2631       N  
ATOM    345  N   SER A 100      -9.508 -10.229  -8.895  1.00126.59           N  
ANISOU  345  N   SER A 100    15393  19116  13587   -131   2358   1506       N  
ATOM    346  CA  SER A 100     -10.296  -9.789 -10.040  1.00126.65           C  
ANISOU  346  CA  SER A 100    15132  19074  13915    -53   2326   1447       C  
ATOM    347  C   SER A 100      -9.399  -9.372 -11.203  1.00124.43           C  
ANISOU  347  C   SER A 100    14944  18529  13804    -45   2021   1359       C  
ATOM    348  O   SER A 100      -9.802  -9.450 -12.362  1.00123.25           O  
ANISOU  348  O   SER A 100    14607  18291  13929    -87   1906   1393       O  
ATOM    349  CB  SER A 100     -11.218  -8.634  -9.646  1.00134.17           C  
ANISOU  349  CB  SER A 100    15984  20162  14832    199   2542   1270       C  
ATOM    350  OG  SER A 100     -12.114  -9.020  -8.617  1.00136.35           O  
ANISOU  350  OG  SER A 100    16171  20707  14930    202   2855   1347       O  
ATOM    351  N   THR A 101      -8.184  -8.932 -10.889  1.00131.76           N  
ANISOU  351  N   THR A 101    16164  19342  14557     -2   1887   1251       N  
ATOM    352  CA  THR A 101      -7.214  -8.593 -11.922  1.00129.75           C  
ANISOU  352  CA  THR A 101    16003  18856  14442     -7   1612   1181       C  
ATOM    353  C   THR A 101      -6.541  -9.853 -12.458  1.00126.65           C  
ANISOU  353  C   THR A 101    15584  18368  14169   -210   1450   1367       C  
ATOM    354  O   THR A 101      -6.332  -9.981 -13.663  1.00125.01           O  
ANISOU  354  O   THR A 101    15284  18021  14194   -243   1294   1373       O  
ATOM    355  CB  THR A 101      -6.143  -7.607 -11.414  1.00 79.62           C  
ANISOU  355  CB  THR A 101     9959  12415   7876     68   1505   1027       C  
ATOM    356  OG1 THR A 101      -5.371  -8.226 -10.378  1.00 78.69           O  
ANISOU  356  OG1 THR A 101    10024  12328   7546    -69   1453   1141       O  
ATOM    357  CG2 THR A 101      -6.794  -6.340 -10.875  1.00 83.50           C  
ANISOU  357  CG2 THR A 101    10527  13000   8200    272   1693    840       C  
ATOM    358  N   VAL A 102      -6.217 -10.791 -11.570  1.00112.45           N  
ANISOU  358  N   VAL A 102    13880  16640  12203   -339   1490   1520       N  
ATOM    359  CA  VAL A 102      -5.594 -12.040 -12.005  1.00109.80           C  
ANISOU  359  CA  VAL A 102    13521  16208  11989   -516   1358   1709       C  
ATOM    360  C   VAL A 102      -6.623 -12.915 -12.713  1.00109.52           C  
ANISOU  360  C   VAL A 102    13218  16190  12204   -595   1424   1805       C  
ATOM    361  O   VAL A 102      -6.274 -13.887 -13.380  1.00107.35           O  
ANISOU  361  O   VAL A 102    12899  15777  12112   -706   1284   1898       O  
ATOM    362  CB  VAL A 102      -4.913 -12.813 -10.847  1.00 86.17           C  
ANISOU  362  CB  VAL A 102    10692  13281   8768   -636   1380   1879       C  
ATOM    363  CG1 VAL A 102      -4.157 -11.857  -9.936  1.00 87.22           C  
ANISOU  363  CG1 VAL A 102    11075  13470   8596   -550   1372   1764       C  
ATOM    364  CG2 VAL A 102      -5.920 -13.638 -10.062  1.00 87.83           C  
ANISOU  364  CG2 VAL A 102    10772  13661   8939   -739   1604   2047       C  
ATOM    365  N   ASP A 103      -7.894 -12.555 -12.564  1.00 82.21           N  
ANISOU  365  N   ASP A 103     9579  12904   8751   -539   1637   1781       N  
ATOM    366  CA  ASP A 103      -8.957 -13.175 -13.341  1.00 82.17           C  
ANISOU  366  CA  ASP A 103     9291  12926   9002   -609   1676   1852       C  
ATOM    367  C   ASP A 103      -8.861 -12.720 -14.791  1.00 81.18           C  
ANISOU  367  C   ASP A 103     9089  12652   9104   -526   1501   1719       C  
ATOM    368  O   ASP A 103      -9.159 -13.482 -15.711  1.00 79.96           O  
ANISOU  368  O   ASP A 103     8784  12426   9170   -632   1411   1785       O  
ATOM    369  CB  ASP A 103     -10.331 -12.819 -12.769  1.00122.56           C  
ANISOU  369  CB  ASP A 103    14196  18291  14080   -555   1951   1864       C  
ATOM    370  CG  ASP A 103     -10.685 -13.642 -11.545  1.00123.61           C  
ANISOU  370  CG  ASP A 103    14364  18590  14011   -684   2143   2042       C  
ATOM    371  OD1 ASP A 103      -9.770 -14.247 -10.949  1.00121.99           O  
ANISOU  371  OD1 ASP A 103    14305  18288  13758   -849   2040   2193       O  
ATOM    372  OD2 ASP A 103     -11.879 -13.682 -11.179  1.00126.20           O  
ANISOU  372  OD2 ASP A 103    14575  19149  14225   -611   2403   2035       O  
ATOM    373  N   TYR A 104      -8.450 -11.471 -14.991  1.00 87.22           N  
ANISOU  373  N   TYR A 104     9975  13362   9804   -348   1446   1535       N  
ATOM    374  CA  TYR A 104      -8.234 -10.963 -16.338  1.00 86.46           C  
ANISOU  374  CA  TYR A 104     9846  13112   9894   -277   1267   1425       C  
ATOM    375  C   TYR A 104      -7.085 -11.731 -16.984  1.00 83.28           C  
ANISOU  375  C   TYR A 104     9555  12520   9568   -400   1052   1483       C  
ATOM    376  O   TYR A 104      -7.259 -12.338 -18.046  1.00 81.98           O  
ANISOU  376  O   TYR A 104     9292  12259   9601   -449    934   1493       O  
ATOM    377  CB  TYR A 104      -7.948  -9.459 -16.321  1.00 93.61           C  
ANISOU  377  CB  TYR A 104    10882  13977  10708    -73   1249   1229       C  
ATOM    378  CG  TYR A 104      -9.155  -8.603 -15.997  1.00 96.71           C  
ANISOU  378  CG  TYR A 104    11142  14518  11087    105   1441   1134       C  
ATOM    379  CD1 TYR A 104     -10.430  -8.979 -16.404  1.00 97.43           C  
ANISOU  379  CD1 TYR A 104    10965  14657  11396    157   1461   1138       C  
ATOM    380  CD2 TYR A 104      -9.019  -7.420 -15.284  1.00 98.89           C  
ANISOU  380  CD2 TYR A 104    11563  14882  11128    235   1594   1034       C  
ATOM    381  CE1 TYR A 104     -11.532  -8.200 -16.111  1.00100.10           C  
ANISOU  381  CE1 TYR A 104    11156  15136  11741    347   1639   1058       C  
ATOM    382  CE2 TYR A 104     -10.115  -6.635 -14.986  1.00101.67           C  
ANISOU  382  CE2 TYR A 104    11795  15365  11470    430   1788    935       C  
ATOM    383  CZ  TYR A 104     -11.368  -7.030 -15.402  1.00102.22           C  
ANISOU  383  CZ  TYR A 104    11571  15487  11780    494   1813    953       C  
ATOM    384  OH  TYR A 104     -12.465  -6.254 -15.109  1.00104.88           O  
ANISOU  384  OH  TYR A 104    11762  15962  12127    714   2008    862       O  
ATOM    385  N   TYR A 105      -5.927 -11.716 -16.324  1.00 68.88           N  
ANISOU  385  N   TYR A 105     7937  10652   7582   -443   1002   1523       N  
ATOM    386  CA  TYR A 105      -4.753 -12.460 -16.777  1.00 65.75           C  
ANISOU  386  CA  TYR A 105     7635  10090   7256   -537    816   1587       C  
ATOM    387  C   TYR A 105      -5.106 -13.904 -17.115  1.00 64.27           C  
ANISOU  387  C   TYR A 105     7340   9863   7214   -694    809   1746       C  
ATOM    388  O   TYR A 105      -4.912 -14.345 -18.251  1.00 62.28           O  
ANISOU  388  O   TYR A 105     7064   9470   7128   -737    676   1747       O  
ATOM    389  CB  TYR A 105      -3.645 -12.424 -15.721  1.00 59.65           C  
ANISOU  389  CB  TYR A 105     7078   9302   6284   -549    760   1619       C  
ATOM    390  CG  TYR A 105      -3.046 -11.055 -15.501  1.00 60.67           C  
ANISOU  390  CG  TYR A 105     7348   9415   6291   -427    704   1458       C  
ATOM    391  CD1 TYR A 105      -2.205 -10.488 -16.447  1.00 59.08           C  
ANISOU  391  CD1 TYR A 105     7192   9073   6184   -396    532   1381       C  
ATOM    392  CD2 TYR A 105      -3.312 -10.335 -14.344  1.00 63.33           C  
ANISOU  392  CD2 TYR A 105     7785   9870   6408   -352    825   1383       C  
ATOM    393  CE1 TYR A 105      -1.653  -9.237 -16.254  1.00 60.17           C  
ANISOU  393  CE1 TYR A 105     7466   9178   6221   -313    468   1245       C  
ATOM    394  CE2 TYR A 105      -2.761  -9.082 -14.139  1.00 64.51           C  
ANISOU  394  CE2 TYR A 105     8091   9974   6447   -254    756   1226       C  
ATOM    395  CZ  TYR A 105      -1.932  -8.538 -15.097  1.00 62.97           C  
ANISOU  395  CZ  TYR A 105     7934   9627   6368   -246    570   1164       C  
ATOM    396  OH  TYR A 105      -1.381  -7.292 -14.898  1.00 64.28           O  
ANISOU  396  OH  TYR A 105     8261   9730   6433   -176    490   1019       O  
ATOM    397  N   LEU A 106      -5.639 -14.623 -16.129  1.00 56.17           N  
ANISOU  397  N   LEU A 106     6269   8958   6116   -786    954   1878       N  
ATOM    398  CA  LEU A 106      -6.121 -15.987 -16.325  1.00 55.41           C  
ANISOU  398  CA  LEU A 106     6082   8820   6151   -961    958   2044       C  
ATOM    399  C   LEU A 106      -7.022 -16.048 -17.550  1.00 55.67           C  
ANISOU  399  C   LEU A 106     5907   8832   6413   -994    931   2003       C  
ATOM    400  O   LEU A 106      -6.807 -16.869 -18.448  1.00 54.39           O  
ANISOU  400  O   LEU A 106     5724   8533   6408  -1117    826   2069       O  
ATOM    401  CB  LEU A 106      -6.878 -16.475 -15.086  1.00 55.58           C  
ANISOU  401  CB  LEU A 106     6074   9006   6036  -1057   1148   2199       C  
ATOM    402  CG  LEU A 106      -6.110 -17.340 -14.084  1.00 54.99           C  
ANISOU  402  CG  LEU A 106     6198   8905   5789  -1136   1133   2352       C  
ATOM    403  CD1 LEU A 106      -4.774 -16.709 -13.728  1.00 54.12           C  
ANISOU  403  CD1 LEU A 106     6295   8729   5536  -1017   1005   2259       C  
ATOM    404  CD2 LEU A 106      -6.946 -17.553 -12.837  1.00 57.35           C  
ANISOU  404  CD2 LEU A 106     6473   9421   5896  -1194   1359   2470       C  
ATOM    405  N   GLY A 107      -8.003 -15.149 -17.594  1.00 51.20           N  
ANISOU  405  N   GLY A 107     5197   8396   5862   -880   1017   1893       N  
ATOM    406  CA  GLY A 107      -8.898 -15.050 -18.730  1.00 51.75           C  
ANISOU  406  CA  GLY A 107     5059   8463   6140   -896    969   1854       C  
ATOM    407  C   GLY A 107      -8.109 -14.971 -20.018  1.00 49.89           C  
ANISOU  407  C   GLY A 107     4906   8038   6010   -856    759   1750       C  
ATOM    408  O   GLY A 107      -8.309 -15.788 -20.923  1.00 49.18           O  
ANISOU  408  O   GLY A 107     4734   7866   6087   -952    652   1766       O  
ATOM    409  N   SER A 108      -7.186 -14.013 -20.078  1.00 60.64           N  
ANISOU  409  N   SER A 108     6441   9335   7264   -727    699   1647       N  
ATOM    410  CA  SER A 108      -6.318 -13.849 -21.238  1.00 58.74           C  
ANISOU  410  CA  SER A 108     6291   8931   7097   -689    521   1561       C  
ATOM    411  C   SER A 108      -5.677 -15.183 -21.596  1.00 56.10           C  
ANISOU  411  C   SER A 108     6042   8444   6830   -820    421   1649       C  
ATOM    412  O   SER A 108      -5.772 -15.639 -22.742  1.00 54.87           O  
ANISOU  412  O   SER A 108     5881   8173   6795   -851    301   1611       O  
ATOM    413  CB  SER A 108      -5.243 -12.792 -20.965  1.00 55.67           C  
ANISOU  413  CB  SER A 108     6067   8513   6573   -555    487   1461       C  
ATOM    414  OG  SER A 108      -4.347 -12.671 -22.056  1.00 53.59           O  
ANISOU  414  OG  SER A 108     5889   8105   6370   -539    332   1406       O  
ATOM    415  N   LEU A 109      -5.067 -15.821 -20.598  1.00 39.04           N  
ANISOU  415  N   LEU A 109     3972   6280   4581   -888    470   1765       N  
ATOM    416  CA  LEU A 109      -4.414 -17.109 -20.791  1.00 37.22           C  
ANISOU  416  CA  LEU A 109     3833   5891   4416   -992    385   1863       C  
ATOM    417  C   LEU A 109      -5.366 -18.089 -21.454  1.00 37.80           C  
ANISOU  417  C   LEU A 109     3795   5916   4651  -1145    373   1926       C  
ATOM    418  O   LEU A 109      -5.028 -18.702 -22.471  1.00 36.70           O  
ANISOU  418  O   LEU A 109     3713   5606   4623  -1197    257   1915       O  
ATOM    419  CB  LEU A 109      -3.918 -17.665 -19.454  1.00 33.38           C  
ANISOU  419  CB  LEU A 109     3464   5425   3796  -1029    438   1998       C  
ATOM    420  CG  LEU A 109      -2.697 -16.973 -18.847  1.00 32.31           C  
ANISOU  420  CG  LEU A 109     3469   5306   3503   -914    400   1956       C  
ATOM    421  CD1 LEU A 109      -2.345 -17.592 -17.499  1.00 34.96           C  
ANISOU  421  CD1 LEU A 109     3905   5697   3683   -965    454   2105       C  
ATOM    422  CD2 LEU A 109      -1.522 -17.061 -19.804  1.00 30.20           C  
ANISOU  422  CD2 LEU A 109     3281   4879   3315   -860    249   1906       C  
ATOM    423  N   ALA A 110      -6.572 -18.188 -20.901  1.00 34.10           N  
ANISOU  423  N   ALA A 110     3167   5599   4190  -1219    494   1990       N  
ATOM    424  CA  ALA A 110      -7.576 -19.102 -21.424  1.00 36.32           C  
ANISOU  424  CA  ALA A 110     3315   5857   4631  -1396    479   2066       C  
ATOM    425  C   ALA A 110      -7.787 -18.828 -22.905  1.00 34.55           C  
ANISOU  425  C   ALA A 110     3015   5572   4543  -1378    346   1939       C  
ATOM    426  O   ALA A 110      -7.749 -19.749 -23.728  1.00 35.23           O  
ANISOU  426  O   ALA A 110     3105   5524   4757  -1515    238   1958       O  
ATOM    427  CB  ALA A 110      -8.885 -18.952 -20.654  1.00 39.46           C  
ANISOU  427  CB  ALA A 110     3515   6473   5006  -1465    654   2162       C  
ATOM    428  N   LEU A 111      -7.972 -17.551 -23.236  1.00 39.40           N  
ANISOU  428  N   LEU A 111     3580   6273   5118  -1213    344   1809       N  
ATOM    429  CA  LEU A 111      -8.152 -17.142 -24.621  1.00 39.31           C  
ANISOU  429  CA  LEU A 111     3520   6210   5206  -1179    207   1695       C  
ATOM    430  C   LEU A 111      -6.982 -17.658 -25.449  1.00 36.93           C  
ANISOU  430  C   LEU A 111     3420   5699   4912  -1174     69   1636       C  
ATOM    431  O   LEU A 111      -7.178 -18.364 -26.447  1.00 36.75           O  
ANISOU  431  O   LEU A 111     3406   5571   4987  -1256    -54   1600       O  
ATOM    432  CB  LEU A 111      -8.253 -15.617 -24.724  1.00 65.46           C  
ANISOU  432  CB  LEU A 111     6770   9638   8465   -989    234   1585       C  
ATOM    433  CG  LEU A 111      -8.555 -15.043 -26.110  1.00 65.42           C  
ANISOU  433  CG  LEU A 111     6728   9589   8540   -936     87   1480       C  
ATOM    434  CD1 LEU A 111      -9.884 -15.570 -26.630  1.00 66.92           C  
ANISOU  434  CD1 LEU A 111     6719   9828   8879  -1073     24   1524       C  
ATOM    435  CD2 LEU A 111      -8.553 -13.524 -26.079  1.00 66.70           C  
ANISOU  435  CD2 LEU A 111     6866   9834   8644   -736    115   1388       C  
ATOM    436  N   SER A 112      -5.769 -17.354 -24.988  1.00 54.85           N  
ANISOU  436  N   SER A 112     5849   7918   7072  -1077     89   1627       N  
ATOM    437  CA  SER A 112      -4.551 -17.711 -25.707  1.00 52.76           C  
ANISOU  437  CA  SER A 112     5755   7481   6810  -1043    -12   1579       C  
ATOM    438  C   SER A 112      -4.464 -19.217 -25.918  1.00 52.72           C  
ANISOU  438  C   SER A 112     5826   7310   6896  -1179    -64   1647       C  
ATOM    439  O   SER A 112      -3.834 -19.683 -26.867  1.00 52.01           O  
ANISOU  439  O   SER A 112     5841   7069   6849  -1171   -159   1578       O  
ATOM    440  CB  SER A 112      -3.313 -17.216 -24.957  1.00 88.56           C  
ANISOU  440  CB  SER A 112    10406  12019  11221   -930     23   1588       C  
ATOM    441  OG  SER A 112      -3.139 -17.929 -23.746  1.00 86.86           O  
ANISOU  441  OG  SER A 112    10322  11658  11022   -889    -57   1558       O  
ATOM    442  N   ASP A 113      -5.099 -19.975 -25.029  1.00 58.87           N  
ANISOU  442  N   ASP A 113     6564   8108   7696  -1304      4   1782       N  
ATOM    443  CA  ASP A 113      -5.163 -21.417 -25.194  1.00 59.34           C  
ANISOU  443  CA  ASP A 113     6709   7986   7854  -1452    -49   1862       C  
ATOM    444  C   ASP A 113      -6.231 -21.776 -26.221  1.00 60.76           C  
ANISOU  444  C   ASP A 113     6795   8129   8161  -1603   -133   1826       C  
ATOM    445  O   ASP A 113      -5.943 -22.464 -27.205  1.00 61.04           O  
ANISOU  445  O   ASP A 113     6951   7968   8274  -1670   -244   1782       O  
ATOM    446  CB  ASP A 113      -5.434 -22.102 -23.853  1.00102.14           C  
ANISOU  446  CB  ASP A 113    12133  13434  13241  -1549     49   2045       C  
ATOM    447  CG  ASP A 113      -4.307 -21.892 -22.855  1.00100.99           C  
ANISOU  447  CG  ASP A 113    12113  13291  12967  -1421     89   2094       C  
ATOM    448  OD1 ASP A 113      -3.165 -21.632 -23.294  1.00 99.64           O  
ANISOU  448  OD1 ASP A 113    11983  13144  12732  -1261     61   1984       O  
ATOM    449  OD2 ASP A 113      -4.565 -21.987 -21.635  1.00101.56           O  
ANISOU  449  OD2 ASP A 113    12242  13346  13002  -1493    140   2253       O  
ATOM    450  N   LEU A 114      -7.446 -21.274 -26.007  1.00 65.73           N  
ANISOU  450  N   LEU A 114     7210   8952   8811  -1649    -84   1841       N  
ATOM    451  CA  LEU A 114      -8.593 -21.630 -26.842  1.00 67.29           C  
ANISOU  451  CA  LEU A 114     7276   9156   9136  -1802   -179   1822       C  
ATOM    452  C   LEU A 114      -8.303 -21.449 -28.326  1.00 66.81           C  
ANISOU  452  C   LEU A 114     7294   9001   9089  -1739   -333   1659       C  
ATOM    453  O   LEU A 114      -8.511 -22.371 -29.121  1.00 67.82           O  
ANISOU  453  O   LEU A 114     7446   9016   9306  -1883   -466   1626       O  
ATOM    454  CB  LEU A 114      -9.831 -20.829 -26.433  1.00 71.31           C  
ANISOU  454  CB  LEU A 114     7504   9922   9666  -1816    -88   1869       C  
ATOM    455  CG  LEU A 114     -10.613 -21.368 -25.233  1.00 72.70           C  
ANISOU  455  CG  LEU A 114     7549  10205   9869  -1972     50   2049       C  
ATOM    456  CD1 LEU A 114     -11.815 -20.487 -24.943  1.00 74.57           C  
ANISOU  456  CD1 LEU A 114     7482  10714  10134  -1954    152   2077       C  
ATOM    457  CD2 LEU A 114     -11.051 -22.803 -25.491  1.00 73.52           C  
ANISOU  457  CD2 LEU A 114     7696  10134  10101  -2234    -48   2142       C  
ATOM    458  N   LEU A 115      -7.802 -20.266 -28.676  1.00 40.95           N  
ANISOU  458  N   LEU A 115     4070   5773   5715  -1537   -320   1560       N  
ATOM    459  CA  LEU A 115      -7.353 -19.974 -30.031  1.00 40.40           C  
ANISOU  459  CA  LEU A 115     4092   5631   5629  -1470   -448   1418       C  
ATOM    460  C   LEU A 115      -6.519 -21.123 -30.588  1.00 40.17           C  
ANISOU  460  C   LEU A 115     4290   5364   5610  -1510   -524   1369       C  
ATOM    461  O   LEU A 115      -6.904 -21.749 -31.582  1.00 41.21           O  
ANISOU  461  O   LEU A 115     4484   5399   5776  -1590   -654   1286       O  
ATOM    462  CB  LEU A 115      -6.551 -18.669 -30.056  1.00 49.04           C  
ANISOU  462  CB  LEU A 115     5210   6810   6613  -1261   -405   1347       C  
ATOM    463  CG  LEU A 115      -7.316 -17.377 -29.762  1.00 49.97           C  
ANISOU  463  CG  LEU A 115     5136   7126   6723  -1184   -366   1345       C  
ATOM    464  CD1 LEU A 115      -6.377 -16.179 -29.818  1.00 48.48           C  
ANISOU  464  CD1 LEU A 115     5021   6970   6429   -995   -342   1274       C  
ATOM    465  CD2 LEU A 115      -8.463 -17.208 -30.744  1.00 51.62           C  
ANISOU  465  CD2 LEU A 115     5210   7383   7018  -1263   -492   1314       C  
ATOM    466  N   ILE A 116      -5.406 -21.423 -29.918  1.00 51.00           N  
ANISOU  466  N   ILE A 116     5790   6641   6946  -1445   -449   1417       N  
ATOM    467  CA  ILE A 116      -4.500 -22.477 -30.367  1.00 51.35           C  
ANISOU  467  CA  ILE A 116     6049   6452   7009  -1442   -499   1376       C  
ATOM    468  C   ILE A 116      -5.236 -23.806 -30.507  1.00 53.38           C  
ANISOU  468  C   ILE A 116     6354   6548   7381  -1653   -578   1416       C  
ATOM    469  O   ILE A 116      -4.991 -24.568 -31.442  1.00 54.69           O  
ANISOU  469  O   ILE A 116     6676   6532   7573  -1692   -680   1314       O  
ATOM    470  CB  ILE A 116      -3.305 -22.653 -29.402  1.00 79.44           C  
ANISOU  470  CB  ILE A 116     9701   9956  10525  -1323   -409   1451       C  
ATOM    471  CG1 ILE A 116      -2.456 -21.382 -29.345  1.00 77.56           C  
ANISOU  471  CG1 ILE A 116     9438   9852  10179  -1136   -357   1400       C  
ATOM    472  CG2 ILE A 116      -2.444 -23.841 -29.816  1.00 80.55           C  
ANISOU  472  CG2 ILE A 116    10050   9842  10713  -1305   -454   1421       C  
ATOM    473  CD1 ILE A 116      -1.178 -21.550 -28.539  1.00 76.66           C  
ANISOU  473  CD1 ILE A 116     9406   9695  10026  -1019   -300   1467       C  
ATOM    474  N   LEU A 117      -6.160 -24.068 -29.587  1.00 40.64           N  
ANISOU  474  N   LEU A 117     4614   5000   5828  -1797   -528   1563       N  
ATOM    475  CA  LEU A 117      -6.914 -25.315 -29.603  1.00 42.58           C  
ANISOU  475  CA  LEU A 117     4893   5091   6193  -2033   -602   1633       C  
ATOM    476  C   LEU A 117      -7.947 -25.341 -30.722  1.00 44.15           C  
ANISOU  476  C   LEU A 117     5027   5291   6455  -2182   -752   1540       C  
ATOM    477  O   LEU A 117      -8.239 -26.400 -31.277  1.00 45.82           O  
ANISOU  477  O   LEU A 117     5394   5282   6731  -2317   -877   1488       O  
ATOM    478  CB  LEU A 117      -7.596 -25.543 -28.253  1.00 47.61           C  
ANISOU  478  CB  LEU A 117     5381   5840   6868  -2165   -495   1833       C  
ATOM    479  CG  LEU A 117      -6.650 -25.899 -27.106  1.00 47.22           C  
ANISOU  479  CG  LEU A 117     5445   5733   6763  -2080   -387   1956       C  
ATOM    480  CD1 LEU A 117      -7.362 -25.800 -25.771  1.00 49.40           C  
ANISOU  480  CD1 LEU A 117     5552   6197   7021  -2183   -255   2142       C  
ATOM    481  CD2 LEU A 117      -6.084 -27.294 -27.313  1.00 48.64           C  
ANISOU  481  CD2 LEU A 117     5870   5591   7021  -2143   -466   1983       C  
ATOM    482  N   LEU A 118      -8.487 -24.174 -31.061  1.00 49.42           N  
ANISOU  482  N   LEU A 118     5476   6199   7102  -2153   -750   1518       N  
ATOM    483  CA  LEU A 118      -9.578 -24.106 -32.031  1.00 50.98           C  
ANISOU  483  CA  LEU A 118     5572   6437   7360  -2295   -909   1454       C  
ATOM    484  C   LEU A 118      -9.105 -23.856 -33.460  1.00 51.06           C  
ANISOU  484  C   LEU A 118     5763   6347   7290  -2203  -1040   1266       C  
ATOM    485  O   LEU A 118      -9.795 -24.207 -34.418  1.00 52.73           O  
ANISOU  485  O   LEU A 118     6037   6459   7539  -2356  -1210   1193       O  
ATOM    486  CB  LEU A 118     -10.610 -23.051 -31.615  1.00 38.76           C  
ANISOU  486  CB  LEU A 118     3707   5187   5835  -2277   -863   1514       C  
ATOM    487  CG  LEU A 118     -11.428 -23.376 -30.362  1.00 41.97           C  
ANISOU  487  CG  LEU A 118     3890   5733   6326  -2411   -739   1698       C  
ATOM    488  CD1 LEU A 118     -12.442 -22.278 -30.067  1.00 42.81           C  
ANISOU  488  CD1 LEU A 118     3680   6135   6450  -2344   -684   1729       C  
ATOM    489  CD2 LEU A 118     -12.120 -24.722 -30.509  1.00 46.25           C  
ANISOU  489  CD2 LEU A 118     4431   6139   7004  -2717   -846   1780       C  
ATOM    490  N   LEU A 119      -7.925 -23.263 -33.601  1.00 56.22           N  
ANISOU  490  N   LEU A 119     6504   7032   7823  -1966   -962   1193       N  
ATOM    491  CA  LEU A 119      -7.414 -22.905 -34.917  1.00 56.36           C  
ANISOU  491  CA  LEU A 119     6673   7000   7741  -1868  -1057   1030       C  
ATOM    492  C   LEU A 119      -6.169 -23.702 -35.290  1.00 56.74           C  
ANISOU  492  C   LEU A 119     7010   6814   7732  -1785  -1039    935       C  
ATOM    493  O   LEU A 119      -6.120 -24.334 -36.346  1.00 58.50           O  
ANISOU  493  O   LEU A 119     7413   6893   7921  -1836  -1157    808       O  
ATOM    494  CB  LEU A 119      -7.120 -21.404 -34.978  1.00 46.29           C  
ANISOU  494  CB  LEU A 119     5295   5923   6370  -1674   -997   1009       C  
ATOM    495  CG  LEU A 119      -8.293 -20.495 -34.604  1.00 46.49           C  
ANISOU  495  CG  LEU A 119     5041   6175   6447  -1701  -1011   1081       C  
ATOM    496  CD1 LEU A 119      -7.886 -19.032 -34.659  1.00 44.86           C  
ANISOU  496  CD1 LEU A 119     4789   6109   6146  -1496   -962   1048       C  
ATOM    497  CD2 LEU A 119      -9.490 -20.756 -35.511  1.00 48.56           C  
ANISOU  497  CD2 LEU A 119     5226   6451   6775  -1881  -1204   1054       C  
ATOM    498  N   ALA A 120      -5.167 -23.672 -34.417  1.00 49.49           N  
ANISOU  498  N   ALA A 120     6139   5864   6801  -1649   -896    995       N  
ATOM    499  CA  ALA A 120      -3.882 -24.304 -34.701  1.00 50.09           C  
ANISOU  499  CA  ALA A 120     6450   5754   6830  -1514   -857    913       C  
ATOM    500  C   ALA A 120      -3.962 -25.829 -34.736  1.00 52.38           C  
ANISOU  500  C   ALA A 120     6932   5764   7207  -1628   -915    902       C  
ATOM    501  O   ALA A 120      -3.357 -26.464 -35.598  1.00 54.23           O  
ANISOU  501  O   ALA A 120     7390   5815   7401  -1556   -942    769       O  
ATOM    502  CB  ALA A 120      -2.832 -23.846 -33.698  1.00 32.39           C  
ANISOU  502  CB  ALA A 120     4172   3583   4552  -1329   -708    991       C  
ATOM    503  N   MET A 121      -4.709 -26.410 -33.802  1.00 59.11           N  
ANISOU  503  N   MET A 121     7706   6577   8176  -1805   -926   1041       N  
ATOM    504  CA  MET A 121      -4.791 -27.868 -33.688  1.00 61.19           C  
ANISOU  504  CA  MET A 121     8164   6547   8539  -1930   -986   1056       C  
ATOM    505  C   MET A 121      -5.369 -28.627 -34.897  1.00 63.78           C  
ANISOU  505  C   MET A 121     8659   6694   8882  -2088  -1160    905       C  
ATOM    506  O   MET A 121      -4.774 -29.605 -35.335  1.00 65.72           O  
ANISOU  506  O   MET A 121     9174   6677   9120  -2029  -1190    790       O  
ATOM    507  CB  MET A 121      -5.487 -28.295 -32.388  1.00 57.23           C  
ANISOU  507  CB  MET A 121     7545   6049   8151  -2103   -950   1268       C  
ATOM    508  CG  MET A 121      -5.922 -29.754 -32.389  1.00 59.45           C  
ANISOU  508  CG  MET A 121     8036   6002   8548  -2265  -1032   1301       C  
ATOM    509  SD  MET A 121      -6.175 -30.450 -30.747  1.00 59.30           S  
ANISOU  509  SD  MET A 121     7899   5983   8648  -2479   -977   1582       S  
ATOM    510  CE  MET A 121      -4.487 -30.712 -30.216  1.00 57.37           C  
ANISOU  510  CE  MET A 121     7681   5785   8332  -2205   -806   1692       C  
ATOM    511  N   PRO A 122      -6.529 -28.199 -35.431  1.00 59.82           N  
ANISOU  511  N   PRO A 122     8002   6328   8401  -2283  -1282    902       N  
ATOM    512  CA  PRO A 122      -7.059 -28.925 -36.596  1.00 62.37           C  
ANISOU  512  CA  PRO A 122     8499   6472   8728  -2458  -1477    759       C  
ATOM    513  C   PRO A 122      -6.099 -28.881 -37.781  1.00 63.44           C  
ANISOU  513  C   PRO A 122     8862   6542   8702  -2278  -1502    538       C  
ATOM    514  O   PRO A 122      -5.777 -29.926 -38.363  1.00 65.91           O  
ANISOU  514  O   PRO A 122     9442   6611   8992  -2347  -1616    389       O  
ATOM    515  CB  PRO A 122      -8.334 -28.147 -36.940  1.00 43.27           C  
ANISOU  515  CB  PRO A 122     5806   4284   6350  -2660  -1595    819       C  
ATOM    516  CG  PRO A 122      -8.742 -27.514 -35.658  1.00 39.90           C  
ANISOU  516  CG  PRO A 122     5114   4165   5883  -2490  -1448    913       C  
ATOM    517  CD  PRO A 122      -7.459 -27.152 -34.973  1.00 37.96           C  
ANISOU  517  CD  PRO A 122     4905   3869   5650  -2344  -1259   1016       C  
ATOM    518  N   VAL A 123      -5.646 -27.675 -38.116  1.00 54.52           N  
ANISOU  518  N   VAL A 123     7636   5625   7455  -2057  -1392    517       N  
ATOM    519  CA  VAL A 123      -4.702 -27.456 -39.208  1.00 55.63           C  
ANISOU  519  CA  VAL A 123     7972   5738   7428  -1873  -1375    334       C  
ATOM    520  C   VAL A 123      -3.422 -28.273 -39.041  1.00 57.06           C  
ANISOU  520  C   VAL A 123     8396   5680   7606  -1697  -1260    269       C  
ATOM    521  O   VAL A 123      -2.971 -28.935 -39.980  1.00 59.74           O  
ANISOU  521  O   VAL A 123     9004   5833   7863  -1653  -1301     90       O  
ATOM    522  CB  VAL A 123      -4.335 -25.959 -39.345  1.00 43.58           C  
ANISOU  522  CB  VAL A 123     6270   4497   5792  -1696  -1279    360       C  
ATOM    523  CG1 VAL A 123      -3.201 -25.779 -40.336  1.00 44.86           C  
ANISOU  523  CG1 VAL A 123     6628   4630   5788  -1486  -1204    209       C  
ATOM    524  CG2 VAL A 123      -5.555 -25.141 -39.765  1.00 42.89           C  
ANISOU  524  CG2 VAL A 123     5991   4617   5688  -1831  -1416    385       C  
ATOM    525  N   GLU A 124      -2.844 -28.232 -37.845  1.00 49.30           N  
ANISOU  525  N   GLU A 124     7320   4706   6708  -1589  -1120    414       N  
ATOM    526  CA  GLU A 124      -1.616 -28.971 -37.583  1.00 50.62           C  
ANISOU  526  CA  GLU A 124     7674   4664   6898  -1398  -1012    386       C  
ATOM    527  C   GLU A 124      -1.831 -30.478 -37.645  1.00 53.12           C  
ANISOU  527  C   GLU A 124     8235   4629   7321  -1523  -1107    344       C  
ATOM    528  O   GLU A 124      -0.993 -31.210 -38.160  1.00 55.62           O  
ANISOU  528  O   GLU A 124     8811   4715   7607  -1384  -1084    199       O  
ATOM    529  CB  GLU A 124      -1.022 -28.597 -36.228  1.00 73.82           C  
ANISOU  529  CB  GLU A 124    10439   7710   9898  -1275   -872    574       C  
ATOM    530  CG  GLU A 124       0.149 -29.477 -35.845  1.00 75.25           C  
ANISOU  530  CG  GLU A 124    10780   7685  10128  -1071   -778    577       C  
ATOM    531  CD  GLU A 124       0.729 -29.151 -34.490  1.00 73.00           C  
ANISOU  531  CD  GLU A 124    10340   7480   9916  -1004   -688    788       C  
ATOM    532  OE1 GLU A 124       0.328 -28.134 -33.883  1.00 70.20           O  
ANISOU  532  OE1 GLU A 124     9757   7390   9526  -1041   -654    893       O  
ATOM    533  OE2 GLU A 124       1.594 -29.923 -34.036  1.00 74.13           O  
ANISOU  533  OE2 GLU A 124    10604   7414  10146   -908   -658    848       O  
ATOM    534  N   LEU A 125      -2.952 -30.938 -37.106  1.00 66.30           N  
ANISOU  534  N   LEU A 125     9822   6253   9116  -1785  -1208    472       N  
ATOM    535  CA  LEU A 125      -3.268 -32.355 -37.125  1.00 68.51           C  
ANISOU  535  CA  LEU A 125    10331   6184   9516  -1950  -1316    462       C  
ATOM    536  C   LEU A 125      -3.296 -32.809 -38.578  1.00 71.38           C  
ANISOU  536  C   LEU A 125    10971   6352   9799  -2015  -1458    215       C  
ATOM    537  O   LEU A 125      -2.486 -33.647 -38.993  1.00 73.84           O  
ANISOU  537  O   LEU A 125    11582   6315  10158  -2014  -1505    117       O  
ATOM    538  CB  LEU A 125      -4.609 -32.603 -36.438  1.00 67.59           C  
ANISOU  538  CB  LEU A 125    10035   6107   9538  -2262  -1401    657       C  
ATOM    539  CG  LEU A 125      -4.923 -34.036 -36.029  1.00 69.60           C  
ANISOU  539  CG  LEU A 125    10499   6000   9944  -2466  -1504    711       C  
ATOM    540  CD1 LEU A 125      -3.694 -34.665 -35.400  1.00 70.26           C  
ANISOU  540  CD1 LEU A 125    10772   5842  10081  -2242  -1392    757       C  
ATOM    541  CD2 LEU A 125      -6.086 -34.050 -35.058  1.00 68.62           C  
ANISOU  541  CD2 LEU A 125    10139   5987   9948  -2773  -1550    941       C  
ATOM    542  N   TYR A 126      -4.183 -32.200 -39.360  1.00 61.77           N  
ANISOU  542  N   TYR A 126     9668   5350   8450  -2064  -1530    113       N  
ATOM    543  CA  TYR A 126      -4.321 -32.551 -40.770  1.00 64.51           C  
ANISOU  543  CA  TYR A 126    10278   5555   8676  -2131  -1676   -125       C  
ATOM    544  C   TYR A 126      -3.014 -32.443 -41.554  1.00 64.24           C  
ANISOU  544  C   TYR A 126    10468   5465   8474  -1820  -1545   -320       C  
ATOM    545  O   TYR A 126      -2.456 -33.453 -41.981  1.00 67.26           O  
ANISOU  545  O   TYR A 126    11180   5540   8833  -1760  -1563   -490       O  
ATOM    546  CB  TYR A 126      -5.393 -31.689 -41.444  1.00 59.19           C  
ANISOU  546  CB  TYR A 126     9422   5145   7921  -2314  -1827   -137       C  
ATOM    547  CG  TYR A 126      -5.508 -31.911 -42.940  1.00 61.66           C  
ANISOU  547  CG  TYR A 126    10004   5358   8068  -2382  -1992   -380       C  
ATOM    548  CD1 TYR A 126      -6.241 -32.975 -43.451  1.00 64.39           C  
ANISOU  548  CD1 TYR A 126    10559   5442   8466  -2654  -2213   -470       C  
ATOM    549  CD2 TYR A 126      -4.890 -31.050 -43.840  1.00 61.96           C  
ANISOU  549  CD2 TYR A 126    10098   5561   7882  -2190  -1935   -516       C  
ATOM    550  CE1 TYR A 126      -6.349 -33.180 -44.814  1.00 67.26           C  
ANISOU  550  CE1 TYR A 126    11192   5712   8651  -2725  -2380   -703       C  
ATOM    551  CE2 TYR A 126      -4.992 -31.247 -45.203  1.00 64.16           C  
ANISOU  551  CE2 TYR A 126    10644   5761   7975  -2253  -2085   -737       C  
ATOM    552  CZ  TYR A 126      -5.723 -32.313 -45.684  1.00 66.05           C  
ANISOU  552  CZ  TYR A 126    11099   5740   8258  -2517  -2311   -837       C  
ATOM    553  OH  TYR A 126      -5.826 -32.513 -47.040  1.00 69.09           O  
ANISOU  553  OH  TYR A 126    11774   6045   8433  -2589  -2475  -1069       O  
ATOM    554  N   ASN A 127      -2.527 -31.219 -41.733  1.00 48.80           N  
ANISOU  554  N   ASN A 127     8332   3803   6405  -1621  -1405   -294       N  
ATOM    555  CA  ASN A 127      -1.424 -30.965 -42.659  1.00 49.71           C  
ANISOU  555  CA  ASN A 127     8613   3936   6336  -1355  -1277   -469       C  
ATOM    556  C   ASN A 127      -0.018 -31.253 -42.137  1.00 50.24           C  
ANISOU  556  C   ASN A 127     8712   3925   6449  -1052  -1059   -442       C  
ATOM    557  O   ASN A 127       0.926 -31.362 -42.920  1.00 52.18           O  
ANISOU  557  O   ASN A 127     9095   4171   6559   -821   -932   -586       O  
ATOM    558  CB  ASN A 127      -1.490 -29.531 -43.187  1.00 45.86           C  
ANISOU  558  CB  ASN A 127     7941   3798   5685  -1317  -1257   -462       C  
ATOM    559  CG  ASN A 127      -1.719 -29.474 -44.682  1.00 48.00           C  
ANISOU  559  CG  ASN A 127     8428   4065   5745  -1383  -1382   -670       C  
ATOM    560  OD1 ASN A 127      -1.270 -30.346 -45.426  1.00 50.80           O  
ANISOU  560  OD1 ASN A 127     9104   4191   6005  -1318  -1380   -870       O  
ATOM    561  ND2 ASN A 127      -2.421 -28.444 -45.131  1.00 46.56           N  
ANISOU  561  ND2 ASN A 127     8082   4132   5478  -1504  -1494   -626       N  
ATOM    562  N   PHE A 128       0.127 -31.367 -40.823  1.00 37.41           N  
ANISOU  562  N   PHE A 128     6956   2247   5012  -1052  -1013   -249       N  
ATOM    563  CA  PHE A 128       1.445 -31.596 -40.239  1.00 36.09           C  
ANISOU  563  CA  PHE A 128     6786   2020   4904   -769   -832   -193       C  
ATOM    564  C   PHE A 128       1.579 -32.982 -39.617  1.00 40.14           C  
ANISOU  564  C   PHE A 128     7486   2172   5594   -770   -862   -153       C  
ATOM    565  O   PHE A 128       2.689 -33.428 -39.329  1.00 40.66           O  
ANISOU  565  O   PHE A 128     7633   2107   5709   -511   -737   -157       O  
ATOM    566  CB  PHE A 128       1.784 -30.516 -39.207  1.00 43.08           C  
ANISOU  566  CB  PHE A 128     7337   3208   5823   -702   -728     19       C  
ATOM    567  CG  PHE A 128       2.064 -29.169 -39.806  1.00 42.13           C  
ANISOU  567  CG  PHE A 128     7065   3405   5538   -627   -663    -19       C  
ATOM    568  CD1 PHE A 128       2.909 -29.044 -40.896  1.00 44.81           C  
ANISOU  568  CD1 PHE A 128     7550   3758   5717   -458   -581   -201       C  
ATOM    569  CD2 PHE A 128       1.480 -28.028 -39.280  1.00 38.67           C  
ANISOU  569  CD2 PHE A 128     6351   3243   5098   -723   -676    127       C  
ATOM    570  CE1 PHE A 128       3.169 -27.804 -41.451  1.00 44.09           C  
ANISOU  570  CE1 PHE A 128     7330   3950   5471   -406   -523   -215       C  
ATOM    571  CE2 PHE A 128       1.735 -26.785 -39.830  1.00 37.74           C  
ANISOU  571  CE2 PHE A 128     6117   3385   4838   -658   -628    101       C  
ATOM    572  CZ  PHE A 128       2.581 -26.673 -40.918  1.00 40.46           C  
ANISOU  572  CZ  PHE A 128     6607   3740   5028   -511   -556    -60       C  
ATOM    573  N   ILE A 129       0.460 -33.670 -39.409  1.00 58.67           N  
ANISOU  573  N   ILE A 129     9892   4357   8043  -1061  -1032   -102       N  
ATOM    574  CA  ILE A 129       0.545 -35.015 -38.851  1.00 60.00           C  
ANISOU  574  CA  ILE A 129    10259   4153   8385  -1106  -1084    -47       C  
ATOM    575  C   ILE A 129       0.031 -36.096 -39.807  1.00 63.12           C  
ANISOU  575  C   ILE A 129    11028   4195   8761  -1215  -1225   -275       C  
ATOM    576  O   ILE A 129       0.646 -37.156 -39.941  1.00 65.49           O  
ANISOU  576  O   ILE A 129    11607   4163   9113  -1043  -1191   -375       O  
ATOM    577  CB  ILE A 129      -0.129 -35.096 -37.462  1.00 62.23           C  
ANISOU  577  CB  ILE A 129    10350   4473   8824  -1368  -1159    220       C  
ATOM    578  CG1 ILE A 129       0.896 -34.788 -36.368  1.00 60.03           C  
ANISOU  578  CG1 ILE A 129     9848   4360   8602  -1192  -1011    443       C  
ATOM    579  CG2 ILE A 129      -0.748 -36.463 -37.225  1.00 64.14           C  
ANISOU  579  CG2 ILE A 129    10849   4302   9219  -1556  -1294    241       C  
ATOM    580  CD1 ILE A 129       0.306 -34.155 -35.141  1.00 57.51           C  
ANISOU  580  CD1 ILE A 129     9236   4457   8158  -1081   -902    478       C  
ATOM    581  N   TRP A 130      -1.075 -35.818 -40.488  1.00 61.17           N  
ANISOU  581  N   TRP A 130    10790   4014   8438  -1491  -1392   -361       N  
ATOM    582  CA  TRP A 130      -1.724 -36.826 -41.327  1.00 65.58           C  
ANISOU  582  CA  TRP A 130    11706   4243   8969  -1652  -1567   -576       C  
ATOM    583  C   TRP A 130      -1.344 -36.777 -42.806  1.00 66.73           C  
ANISOU  583  C   TRP A 130    12079   4394   8878  -1464  -1526   -873       C  
ATOM    584  O   TRP A 130      -1.214 -37.816 -43.450  1.00 69.26           O  
ANISOU  584  O   TRP A 130    12700   4447   9168  -1230  -1441  -1047       O  
ATOM    585  CB  TRP A 130      -3.244 -36.765 -41.158  1.00 70.09           C  
ANISOU  585  CB  TRP A 130    12177   4862   9591  -2079  -1802   -507       C  
ATOM    586  CG  TRP A 130      -3.710 -37.461 -39.921  1.00 71.85           C  
ANISOU  586  CG  TRP A 130    12287   4967  10046  -2305  -1859   -252       C  
ATOM    587  CD1 TRP A 130      -4.258 -36.888 -38.811  1.00 69.42           C  
ANISOU  587  CD1 TRP A 130    11603   4946   9825  -2455  -1837      8       C  
ATOM    588  CD2 TRP A 130      -3.643 -38.868 -39.658  1.00 76.93           C  
ANISOU  588  CD2 TRP A 130    13208   5167  10854  -2405  -1939   -228       C  
ATOM    589  NE1 TRP A 130      -4.547 -37.853 -37.877  1.00 72.64           N  
ANISOU  589  NE1 TRP A 130    12029   5141  10429  -2652  -1888    202       N  
ATOM    590  CE2 TRP A 130      -4.179 -39.075 -38.371  1.00 77.22           C  
ANISOU  590  CE2 TRP A 130    13008   5263  11067  -2633  -1960     70       C  
ATOM    591  CE3 TRP A 130      -3.188 -39.971 -40.387  1.00 81.64           C  
ANISOU  591  CE3 TRP A 130    14243   5313  11463  -2318  -1990   -431       C  
ATOM    592  CZ2 TRP A 130      -4.274 -40.344 -37.801  1.00 81.99           C  
ANISOU  592  CZ2 TRP A 130    13798   5493  11859  -2796  -2039    192       C  
ATOM    593  CZ3 TRP A 130      -3.282 -41.226 -39.817  1.00 86.37           C  
ANISOU  593  CZ3 TRP A 130    15035   5516  12263  -2467  -2078   -322       C  
ATOM    594  CH2 TRP A 130      -3.821 -41.402 -38.538  1.00 86.52           C  
ANISOU  594  CH2 TRP A 130    14809   5607  12456  -2713  -2106     -3       C  
ATOM    595  N   VAL A 131      -1.177 -35.576 -43.344  1.00 57.74           N  
ANISOU  595  N   VAL A 131    10804   3565   7568  -1559  -1582   -927       N  
ATOM    596  CA  VAL A 131      -0.772 -35.425 -44.739  1.00 58.40           C  
ANISOU  596  CA  VAL A 131    11097   3698   7394  -1408  -1545  -1189       C  
ATOM    597  C   VAL A 131       0.197 -34.251 -44.894  1.00 52.77           C  
ANISOU  597  C   VAL A 131    10169   3322   6561  -1106  -1304  -1146       C  
ATOM    598  O   VAL A 131      -0.196 -33.082 -44.876  1.00 48.63           O  
ANISOU  598  O   VAL A 131     9343   3143   5991  -1169  -1303  -1015       O  
ATOM    599  CB  VAL A 131      -1.994 -35.313 -45.687  1.00 71.09           C  
ANISOU  599  CB  VAL A 131    12760   5394   8858  -1711  -1791  -1298       C  
ATOM    600  CG1 VAL A 131      -3.047 -34.380 -45.102  1.00 68.25           C  
ANISOU  600  CG1 VAL A 131    11989   5358   8584  -1939  -1887  -1059       C  
ATOM    601  CG2 VAL A 131      -1.567 -34.856 -47.076  1.00 71.77           C  
ANISOU  601  CG2 VAL A 131    13015   5616   8640  -1546  -1732  -1526       C  
ATOM    602  N   HIS A 132       1.476 -34.585 -45.032  1.00 60.15           N  
ANISOU  602  N   HIS A 132    11256   4143   7457   -775  -1101  -1252       N  
ATOM    603  CA  HIS A 132       2.547 -33.599 -44.981  1.00 56.52           C  
ANISOU  603  CA  HIS A 132    10577   3975   6923   -487   -860  -1185       C  
ATOM    604  C   HIS A 132       2.651 -32.784 -46.267  1.00 56.50           C  
ANISOU  604  C   HIS A 132    10620   4215   6634   -439   -819  -1340       C  
ATOM    605  O   HIS A 132       3.251 -31.707 -46.285  1.00 55.50           O  
ANISOU  605  O   HIS A 132    10253   4404   6430   -314   -677  -1245       O  
ATOM    606  CB  HIS A 132       3.872 -34.297 -44.667  1.00 73.43           C  
ANISOU  606  CB  HIS A 132    12827   5925   9149   -144   -656  -1221       C  
ATOM    607  CG  HIS A 132       3.761 -35.336 -43.593  1.00 72.66           C  
ANISOU  607  CG  HIS A 132    12702   5583   9322   -167   -696  -1050       C  
ATOM    608  ND1 HIS A 132       3.928 -35.048 -42.255  1.00 72.70           N  
ANISOU  608  ND1 HIS A 132    12704   5465   9454    137   -531   -994       N  
ATOM    609  CD2 HIS A 132       3.483 -36.660 -43.660  1.00 71.86           C  
ANISOU  609  CD2 HIS A 132    12571   5346   9388   -458   -882   -908       C  
ATOM    610  CE1 HIS A 132       3.765 -36.150 -41.546  1.00 71.96           C  
ANISOU  610  CE1 HIS A 132    12602   5158   9583     33   -624   -822       C  
ATOM    611  NE2 HIS A 132       3.495 -37.143 -42.374  1.00 71.46           N  
ANISOU  611  NE2 HIS A 132    12523   5085   9544   -333   -827   -766       N  
ATOM    612  N   HIS A 133       2.056 -33.303 -47.336  1.00 56.33           N  
ANISOU  612  N   HIS A 133    10924   4034   6447   -552   -952  -1574       N  
ATOM    613  CA  HIS A 133       2.038 -32.616 -48.620  1.00 56.84           C  
ANISOU  613  CA  HIS A 133    11075   4312   6210   -547   -949  -1721       C  
ATOM    614  C   HIS A 133       0.859 -33.093 -49.460  1.00 60.59           C  
ANISOU  614  C   HIS A 133    11828   4628   6566   -834  -1229  -1894       C  
ATOM    615  O   HIS A 133       0.539 -34.281 -49.463  1.00 65.04           O  
ANISOU  615  O   HIS A 133    12662   4833   7217   -922  -1344  -2014       O  
ATOM    616  CB  HIS A 133       3.352 -32.840 -49.374  1.00 54.68           C  
ANISOU  616  CB  HIS A 133    10986   4031   5759   -198   -684  -1900       C  
ATOM    617  CG  HIS A 133       3.547 -34.248 -49.842  1.00 61.01           C  
ANISOU  617  CG  HIS A 133    12203   4432   6548    -87   -672  -2149       C  
ATOM    618  ND1 HIS A 133       3.828 -35.285 -48.980  1.00 65.93           N  
ANISOU  618  ND1 HIS A 133    13177   4989   6885     36   -604  -2436       N  
ATOM    619  CD2 HIS A 133       3.498 -34.792 -51.082  1.00 63.75           C  
ANISOU  619  CD2 HIS A 133    12690   4407   7124    -75   -720  -2156       C  
ATOM    620  CE1 HIS A 133       3.942 -36.408 -49.667  1.00 71.41           C  
ANISOU  620  CE1 HIS A 133    14215   5278   7638    129   -608  -2627       C  
ATOM    621  NE2 HIS A 133       3.749 -36.135 -50.945  1.00 70.19           N  
ANISOU  621  NE2 HIS A 133    13941   4923   7804     62   -685  -2455       N  
ATOM    622  N   PRO A 134       0.207 -32.167 -50.181  1.00 66.46           N  
ANISOU  622  N   PRO A 134    12515   5629   7110   -988  -1355  -1904       N  
ATOM    623  CA  PRO A 134       0.553 -30.743 -50.223  1.00 61.95           C  
ANISOU  623  CA  PRO A 134    11653   5454   6431   -898  -1237  -1761       C  
ATOM    624  C   PRO A 134      -0.147 -29.940 -49.131  1.00 57.57           C  
ANISOU  624  C   PRO A 134    10683   5097   6094  -1051  -1318  -1476       C  
ATOM    625  O   PRO A 134      -1.080 -30.436 -48.499  1.00 58.32           O  
ANISOU  625  O   PRO A 134    10712   5068   6381  -1281  -1502  -1396       O  
ATOM    626  CB  PRO A 134       0.029 -30.315 -51.591  1.00 56.58           C  
ANISOU  626  CB  PRO A 134    11163   4891   5443  -1030  -1395  -1911       C  
ATOM    627  CG  PRO A 134      -1.180 -31.170 -51.790  1.00 61.45           C  
ANISOU  627  CG  PRO A 134    11971   5262   6115  -1329  -1702  -2008       C  
ATOM    628  CD  PRO A 134      -0.876 -32.497 -51.126  1.00 63.35           C  
ANISOU  628  CD  PRO A 134    12376   5129   6564  -1264  -1642  -2071       C  
ATOM    629  N   TRP A 135       0.311 -28.711 -48.916  1.00 60.00           N  
ANISOU  629  N   TRP A 135    10720   5709   6366   -924  -1172  -1327       N  
ATOM    630  CA  TRP A 135      -0.357 -27.791 -48.007  1.00 57.17           C  
ANISOU  630  CA  TRP A 135     9989   5565   6168  -1045  -1237  -1081       C  
ATOM    631  C   TRP A 135      -1.695 -27.397 -48.618  1.00 55.98           C  
ANISOU  631  C   TRP A 135     9814   5513   5943  -1314  -1513  -1081       C  
ATOM    632  O   TRP A 135      -1.788 -27.171 -49.824  1.00 56.19           O  
ANISOU  632  O   TRP A 135     9992   5637   5722  -1328  -1579  -1195       O  
ATOM    633  CB  TRP A 135       0.511 -26.556 -47.762  1.00 56.27           C  
ANISOU  633  CB  TRP A 135     9647   5730   6003   -848  -1031   -953       C  
ATOM    634  CG  TRP A 135      -0.122 -25.531 -46.861  1.00 53.00           C  
ANISOU  634  CG  TRP A 135     8882   5533   5722   -946  -1088   -726       C  
ATOM    635  CD1 TRP A 135      -0.726 -24.369 -47.241  1.00 50.62           C  
ANISOU  635  CD1 TRP A 135     8448   5467   5318  -1025  -1183   -656       C  
ATOM    636  CD2 TRP A 135      -0.207 -25.577 -45.429  1.00 50.67           C  
ANISOU  636  CD2 TRP A 135     8343   5234   5676   -961  -1049   -544       C  
ATOM    637  NE1 TRP A 135      -1.182 -23.689 -46.135  1.00 47.31           N  
ANISOU  637  NE1 TRP A 135     7718   5182   5078  -1074  -1197   -456       N  
ATOM    638  CE2 TRP A 135      -0.877 -24.410 -45.012  1.00 47.16           C  
ANISOU  638  CE2 TRP A 135     7628   5029   5263  -1042  -1112   -388       C  
ATOM    639  CE3 TRP A 135       0.219 -26.492 -44.462  1.00 50.90           C  
ANISOU  639  CE3 TRP A 135     8369   5077   5896   -907   -970   -495       C  
ATOM    640  CZ2 TRP A 135      -1.130 -24.135 -43.668  1.00 44.08           C  
ANISOU  640  CZ2 TRP A 135     6974   4706   5069  -1070  -1083   -203       C  
ATOM    641  CZ3 TRP A 135      -0.034 -26.217 -43.130  1.00 47.62           C  
ANISOU  641  CZ3 TRP A 135     7689   4738   5668   -951   -954   -293       C  
ATOM    642  CH2 TRP A 135      -0.704 -25.050 -42.745  1.00 44.34           C  
ANISOU  642  CH2 TRP A 135     7014   4571   5261  -1032  -1003   -158       C  
ATOM    643  N   ALA A 136      -2.731 -27.319 -47.790  1.00 44.57           N  
ANISOU  643  N   ALA A 136     8168   4055   4711  -1527  -1672   -941       N  
ATOM    644  CA  ALA A 136      -4.089 -27.150 -48.295  1.00 47.98           C  
ANISOU  644  CA  ALA A 136     8570   4542   5119  -1804  -1961   -943       C  
ATOM    645  C   ALA A 136      -4.780 -25.875 -47.813  1.00 45.57           C  
ANISOU  645  C   ALA A 136     7933   4557   4826  -1838  -2013   -762       C  
ATOM    646  O   ALA A 136      -5.961 -25.670 -48.092  1.00 48.35           O  
ANISOU  646  O   ALA A 136     8261   5017   5092  -1999  -2236   -770       O  
ATOM    647  CB  ALA A 136      -4.932 -28.371 -47.942  1.00 55.46           C  
ANISOU  647  CB  ALA A 136     9506   5274   6292  -2045  -2121   -907       C  
ATOM    648  N   PHE A 137      -4.056 -25.019 -47.101  1.00 64.39           N  
ANISOU  648  N   PHE A 137    10066   7083   7318  -1682  -1820   -600       N  
ATOM    649  CA  PHE A 137      -4.668 -23.819 -46.535  1.00 62.08           C  
ANISOU  649  CA  PHE A 137     9466   7061   7061  -1695  -1856   -430       C  
ATOM    650  C   PHE A 137      -4.168 -22.523 -47.166  1.00 61.13           C  
ANISOU  650  C   PHE A 137     9401   7117   6709  -1539  -1784   -457       C  
ATOM    651  O   PHE A 137      -4.498 -21.432 -46.702  1.00 61.95           O  
ANISOU  651  O   PHE A 137     9747   7156   6635  -1407  -1662   -591       O  
ATOM    652  CB  PHE A 137      -4.481 -23.785 -45.017  1.00 56.63           C  
ANISOU  652  CB  PHE A 137     8494   6430   6590  -1630  -1706   -245       C  
ATOM    653  CG  PHE A 137      -5.040 -24.987 -44.317  1.00 57.06           C  
ANISOU  653  CG  PHE A 137     8518   6304   6856  -1775  -1744   -202       C  
ATOM    654  CD1 PHE A 137      -6.394 -25.080 -44.045  1.00 56.49           C  
ANISOU  654  CD1 PHE A 137     8267   6274   6922  -2008  -1926   -113       C  
ATOM    655  CD2 PHE A 137      -4.212 -26.028 -43.934  1.00 58.01           C  
ANISOU  655  CD2 PHE A 137     8785   6213   7041  -1679  -1600   -237       C  
ATOM    656  CE1 PHE A 137      -6.912 -26.187 -43.403  1.00 56.80           C  
ANISOU  656  CE1 PHE A 137     8278   6150   7151  -2166  -1955    -53       C  
ATOM    657  CE2 PHE A 137      -4.724 -27.138 -43.291  1.00 58.16           C  
ANISOU  657  CE2 PHE A 137     8797   6050   7251  -1823  -1643   -178       C  
ATOM    658  CZ  PHE A 137      -6.075 -27.217 -43.025  1.00 57.54           C  
ANISOU  658  CZ  PHE A 137     8546   6018   7299  -2079  -1816    -84       C  
ATOM    659  N   GLY A 138      -3.376 -22.645 -48.225  1.00 66.55           N  
ANISOU  659  N   GLY A 138     9867   8022   7395  -1553  -1855   -326       N  
ATOM    660  CA  GLY A 138      -2.916 -21.485 -48.964  1.00 65.24           C  
ANISOU  660  CA  GLY A 138     9748   8020   7020  -1429  -1804   -319       C  
ATOM    661  C   GLY A 138      -1.890 -20.635 -48.237  1.00 64.27           C  
ANISOU  661  C   GLY A 138     9588   7940   6890  -1213  -1525   -270       C  
ATOM    662  O   GLY A 138      -1.464 -20.959 -47.126  1.00 64.44           O  
ANISOU  662  O   GLY A 138     9531   7878   7076  -1149  -1382   -234       O  
ATOM    663  N   ASP A 139      -1.505 -19.534 -48.875  1.00 60.94           N  
ANISOU  663  N   ASP A 139     9224   7655   6275  -1114  -1459   -258       N  
ATOM    664  CA  ASP A 139      -0.462 -18.654 -48.363  1.00 59.91           C  
ANISOU  664  CA  ASP A 139     9034   7596   6133   -933  -1212   -194       C  
ATOM    665  C   ASP A 139      -0.878 -17.979 -47.058  1.00 56.74           C  
ANISOU  665  C   ASP A 139     8335   7275   5949   -918  -1186    -18       C  
ATOM    666  O   ASP A 139      -0.123 -17.972 -46.082  1.00 56.05           O  
ANISOU  666  O   ASP A 139     8150   7176   5969   -813  -1010     38       O  
ATOM    667  CB  ASP A 139      -0.116 -17.597 -49.413  1.00 64.68           C  
ANISOU  667  CB  ASP A 139     9751   8343   6484   -875  -1175   -190       C  
ATOM    668  CG  ASP A 139       1.283 -17.049 -49.249  1.00 64.61           C  
ANISOU  668  CG  ASP A 139     9721   8396   6434   -707   -908   -151       C  
ATOM    669  OD1 ASP A 139       2.224 -17.648 -49.811  1.00 66.67           O  
ANISOU  669  OD1 ASP A 139    10179   8666   6487   -632   -786   -251       O  
ATOM    670  OD2 ASP A 139       1.444 -16.018 -48.564  1.00 62.51           O  
ANISOU  670  OD2 ASP A 139     9238   8178   6337   -653   -821    -19       O  
ATOM    671  N   ALA A 140      -2.083 -17.414 -47.049  1.00 45.00           N  
ANISOU  671  N   ALA A 140     6707   5870   4520  -1018  -1368     65       N  
ATOM    672  CA  ALA A 140      -2.604 -16.715 -45.878  1.00 42.15           C  
ANISOU  672  CA  ALA A 140     6076   5584   4354  -1006  -1358    211       C  
ATOM    673  C   ALA A 140      -2.743 -17.652 -44.682  1.00 42.53           C  
ANISOU  673  C   ALA A 140     6028   5525   4605  -1042  -1303    221       C  
ATOM    674  O   ALA A 140      -2.499 -17.261 -43.539  1.00 40.53           O  
ANISOU  674  O   ALA A 140     5607   5308   4483   -982  -1196    321       O  
ATOM    675  CB  ALA A 140      -3.942 -16.066 -46.202  1.00 26.75           C  
ANISOU  675  CB  ALA A 140     3998   3734   2430  -1093  -1570    281       C  
ATOM    676  N   GLY A 141      -3.135 -18.892 -44.953  1.00 47.34           N  
ANISOU  676  N   GLY A 141     6763   5994   5230  -1151  -1386    120       N  
ATOM    677  CA  GLY A 141      -3.230 -19.896 -43.911  1.00 47.98           C  
ANISOU  677  CA  GLY A 141     6798   5943   5489  -1197  -1336    134       C  
ATOM    678  C   GLY A 141      -1.854 -20.256 -43.392  1.00 48.42           C  
ANISOU  678  C   GLY A 141     6928   5918   5550  -1041  -1121    120       C  
ATOM    679  O   GLY A 141      -1.650 -20.397 -42.183  1.00 47.15           O  
ANISOU  679  O   GLY A 141     6641   5736   5537  -1009  -1026    212       O  
ATOM    680  N   CYS A 142      -0.906 -20.392 -44.316  1.00 47.84           N  
ANISOU  680  N   CYS A 142     7056   5814   5309   -939  -1042     10       N  
ATOM    681  CA  CYS A 142       0.472 -20.732 -43.978  1.00 49.08           C  
ANISOU  681  CA  CYS A 142     7269   5913   5466   -768   -835     -7       C  
ATOM    682  C   CYS A 142       1.109 -19.699 -43.052  1.00 46.04           C  
ANISOU  682  C   CYS A 142     6675   5675   5145   -666   -710    141       C  
ATOM    683  O   CYS A 142       1.673 -20.050 -42.015  1.00 45.54           O  
ANISOU  683  O   CYS A 142     6529   5565   5208   -601   -610    207       O  
ATOM    684  CB  CYS A 142       1.308 -20.879 -45.250  1.00 46.44           C  
ANISOU  684  CB  CYS A 142     7162   5567   4916   -670   -759   -147       C  
ATOM    685  SG  CYS A 142       3.067 -21.184 -44.959  1.00 48.47           S  
ANISOU  685  SG  CYS A 142     7454   5785   5180   -435   -490   -165       S  
ATOM    686  N   ARG A 143       1.017 -18.427 -43.429  1.00 56.45           N  
ANISOU  686  N   ARG A 143     7922   7158   6367   -659   -731    195       N  
ATOM    687  CA  ARG A 143       1.597 -17.348 -42.632  1.00 53.33           C  
ANISOU  687  CA  ARG A 143     7356   6888   6018   -581   -634    323       C  
ATOM    688  C   ARG A 143       0.825 -17.133 -41.328  1.00 50.44           C  
ANISOU  688  C   ARG A 143     6799   6540   5825   -638   -682    430       C  
ATOM    689  O   ARG A 143       1.417 -16.992 -40.250  1.00 48.76           O  
ANISOU  689  O   ARG A 143     6480   6347   5699   -576   -583    512       O  
ATOM    690  CB  ARG A 143       1.632 -16.051 -43.445  1.00 61.55           C  
ANISOU  690  CB  ARG A 143     8401   8070   6914   -576   -665    356       C  
ATOM    691  CG  ARG A 143       2.453 -16.140 -44.725  1.00 64.13           C  
ANISOU  691  CG  ARG A 143     8909   8416   7040   -516   -584    272       C  
ATOM    692  CD  ARG A 143       2.243 -14.914 -45.605  1.00 62.55           C  
ANISOU  692  CD  ARG A 143     8731   8346   6688   -541   -643    325       C  
ATOM    693  NE  ARG A 143       3.507 -14.292 -45.993  1.00 62.75           N  
ANISOU  693  NE  ARG A 143     8805   8456   6582   -456   -476    347       N  
ATOM    694  CZ  ARG A 143       4.211 -14.631 -47.068  1.00 65.29           C  
ANISOU  694  CZ  ARG A 143     9310   8793   6705   -423   -404    254       C  
ATOM    695  NH1 ARG A 143       3.779 -15.593 -47.873  1.00 67.82           N  
ANISOU  695  NH1 ARG A 143     9811   9032   6925   -471   -502    117       N  
ATOM    696  NH2 ARG A 143       5.350 -14.008 -47.337  1.00 65.17           N  
ANISOU  696  NH2 ARG A 143     9299   8879   6582   -350   -231    297       N  
ATOM    697  N   GLY A 144      -0.501 -17.123 -41.438  1.00 44.74           N  
ANISOU  697  N   GLY A 144     6031   5822   5145   -758   -833    430       N  
ATOM    698  CA  GLY A 144      -1.370 -16.887 -40.300  1.00 42.67           C  
ANISOU  698  CA  GLY A 144     5576   5604   5030   -814   -868    528       C  
ATOM    699  C   GLY A 144      -1.241 -17.932 -39.208  1.00 43.09           C  
ANISOU  699  C   GLY A 144     5600   5557   5215   -834   -799    561       C  
ATOM    700  O   GLY A 144      -1.384 -17.620 -38.025  1.00 41.15           O  
ANISOU  700  O   GLY A 144     5209   5366   5059   -825   -748    658       O  
ATOM    701  N   TYR A 145      -0.974 -19.172 -39.606  1.00 45.76           N  
ANISOU  701  N   TYR A 145     6094   5738   5554   -860   -801    479       N  
ATOM    702  CA  TYR A 145      -0.772 -20.260 -38.653  1.00 46.27           C  
ANISOU  702  CA  TYR A 145     6164   5672   5742   -878   -746    519       C  
ATOM    703  C   TYR A 145       0.388 -19.965 -37.704  1.00 44.76           C  
ANISOU  703  C   TYR A 145     5914   5518   5574   -737   -598    601       C  
ATOM    704  O   TYR A 145       0.204 -19.870 -36.485  1.00 42.80           O  
ANISOU  704  O   TYR A 145     5541   5305   5413   -754   -565    711       O  
ATOM    705  CB  TYR A 145      -0.526 -21.575 -39.400  1.00 47.71           C  
ANISOU  705  CB  TYR A 145     6568   5648   5909   -901   -775    398       C  
ATOM    706  CG  TYR A 145      -0.147 -22.737 -38.509  1.00 48.47           C  
ANISOU  706  CG  TYR A 145     6714   5573   6126   -881   -710    440       C  
ATOM    707  CD1 TYR A 145      -1.119 -23.476 -37.848  1.00 48.24           C  
ANISOU  707  CD1 TYR A 145     6643   5456   6230  -1040   -781    511       C  
ATOM    708  CD2 TYR A 145       1.182 -23.100 -38.336  1.00 49.64           C  
ANISOU  708  CD2 TYR A 145     6946   5651   6262   -704   -581    423       C  
ATOM    709  CE1 TYR A 145      -0.777 -24.538 -37.034  1.00 48.88           C  
ANISOU  709  CE1 TYR A 145     6788   5365   6417  -1027   -732    569       C  
ATOM    710  CE2 TYR A 145       1.534 -24.157 -37.523  1.00 50.33           C  
ANISOU  710  CE2 TYR A 145     7083   5571   6467   -670   -538    476       C  
ATOM    711  CZ  TYR A 145       0.552 -24.875 -36.875  1.00 49.83           C  
ANISOU  711  CZ  TYR A 145     7004   5404   6524   -834   -617    551       C  
ATOM    712  OH  TYR A 145       0.900 -25.933 -36.066  1.00 50.52           O  
ANISOU  712  OH  TYR A 145     7160   5311   6724   -805   -584    622       O  
ATOM    713  N   TYR A 146       1.581 -19.823 -38.274  1.00 58.54           N  
ANISOU  713  N   TYR A 146     7743   7270   7232   -603   -512    550       N  
ATOM    714  CA  TYR A 146       2.786 -19.568 -37.493  1.00 57.38           C  
ANISOU  714  CA  TYR A 146     7530   7165   7109   -474   -390    627       C  
ATOM    715  C   TYR A 146       2.724 -18.233 -36.757  1.00 53.65           C  
ANISOU  715  C   TYR A 146     6893   6863   6629   -476   -382    727       C  
ATOM    716  O   TYR A 146       3.200 -18.119 -35.620  1.00 51.86           O  
ANISOU  716  O   TYR A 146     6579   6668   6458   -438   -330    822       O  
ATOM    717  CB  TYR A 146       4.029 -19.644 -38.384  1.00 40.13           C  
ANISOU  717  CB  TYR A 146     5442   4973   4831   -338   -293    553       C  
ATOM    718  CG  TYR A 146       4.357 -21.047 -38.842  1.00 44.22           C  
ANISOU  718  CG  TYR A 146     6134   5299   5370   -285   -266    452       C  
ATOM    719  CD1 TYR A 146       3.794 -21.574 -39.998  1.00 47.16           C  
ANISOU  719  CD1 TYR A 146     6683   5583   5651   -335   -327    308       C  
ATOM    720  CD2 TYR A 146       5.227 -21.849 -38.112  1.00 45.03           C  
ANISOU  720  CD2 TYR A 146     6238   5294   5578   -181   -193    500       C  
ATOM    721  CE1 TYR A 146       4.092 -22.859 -40.413  1.00 50.63           C  
ANISOU  721  CE1 TYR A 146     7314   5820   6103   -282   -305    195       C  
ATOM    722  CE2 TYR A 146       5.531 -23.133 -38.520  1.00 48.63           C  
ANISOU  722  CE2 TYR A 146     6870   5543   6062   -112   -169    402       C  
ATOM    723  CZ  TYR A 146       4.961 -23.635 -39.670  1.00 51.36           C  
ANISOU  723  CZ  TYR A 146     7408   5790   6315   -162   -221    241       C  
ATOM    724  OH  TYR A 146       5.262 -24.914 -40.080  1.00 54.69           O  
ANISOU  724  OH  TYR A 146     8038   5981   6759    -88   -200    123       O  
ATOM    725  N   PHE A 147       2.131 -17.229 -37.401  1.00 44.08           N  
ANISOU  725  N   PHE A 147     5656   5749   5345   -518   -446    704       N  
ATOM    726  CA  PHE A 147       1.935 -15.936 -36.752  1.00 41.12           C  
ANISOU  726  CA  PHE A 147     5152   5505   4968   -515   -451    782       C  
ATOM    727  C   PHE A 147       1.107 -16.084 -35.479  1.00 39.81           C  
ANISOU  727  C   PHE A 147     4875   5351   4902   -572   -464    854       C  
ATOM    728  O   PHE A 147       1.477 -15.564 -34.425  1.00 38.12           O  
ANISOU  728  O   PHE A 147     4585   5197   4703   -535   -413    927       O  
ATOM    729  CB  PHE A 147       1.267 -14.938 -37.698  1.00 36.01           C  
ANISOU  729  CB  PHE A 147     4511   4930   4241   -545   -537    750       C  
ATOM    730  CG  PHE A 147       0.869 -13.647 -37.034  1.00 33.53           C  
ANISOU  730  CG  PHE A 147     4081   4715   3943   -535   -558    818       C  
ATOM    731  CD1 PHE A 147       1.821 -12.686 -36.734  1.00 31.82           C  
ANISOU  731  CD1 PHE A 147     3851   4553   3685   -473   -503    862       C  
ATOM    732  CD2 PHE A 147      -0.455 -13.397 -36.709  1.00 33.44           C  
ANISOU  732  CD2 PHE A 147     3973   4738   3994   -586   -633    834       C  
ATOM    733  CE1 PHE A 147       1.460 -11.501 -36.124  1.00 30.29           C  
ANISOU  733  CE1 PHE A 147     3586   4419   3503   -459   -529    908       C  
ATOM    734  CE2 PHE A 147      -0.821 -12.213 -36.098  1.00 32.20           C  
ANISOU  734  CE2 PHE A 147     3724   4660   3852   -547   -640    881       C  
ATOM    735  CZ  PHE A 147       0.138 -11.264 -35.806  1.00 30.70           C  
ANISOU  735  CZ  PHE A 147     3558   4495   3612   -481   -590    910       C  
ATOM    736  N   LEU A 148      -0.011 -16.797 -35.586  1.00 37.09           N  
ANISOU  736  N   LEU A 148     4523   4955   4615   -672   -533    836       N  
ATOM    737  CA  LEU A 148      -0.877 -17.047 -34.438  1.00 36.65           C  
ANISOU  737  CA  LEU A 148     4352   4923   4650   -744   -529    914       C  
ATOM    738  C   LEU A 148      -0.142 -17.823 -33.352  1.00 36.42           C  
ANISOU  738  C   LEU A 148     4341   4829   4665   -721   -446    986       C  
ATOM    739  O   LEU A 148      -0.271 -17.519 -32.161  1.00 35.38           O  
ANISOU  739  O   LEU A 148     4120   4769   4552   -721   -398   1071       O  
ATOM    740  CB  LEU A 148      -2.127 -17.815 -34.866  1.00 46.32           C  
ANISOU  740  CB  LEU A 148     5561   6098   5939   -882   -625    890       C  
ATOM    741  CG  LEU A 148      -3.099 -18.175 -33.742  1.00 46.54           C  
ANISOU  741  CG  LEU A 148     5451   6165   6067   -981   -608    985       C  
ATOM    742  CD1 LEU A 148      -3.691 -16.916 -33.126  1.00 45.63           C  
ANISOU  742  CD1 LEU A 148     5173   6221   5942   -929   -573   1032       C  
ATOM    743  CD2 LEU A 148      -4.195 -19.096 -34.253  1.00 48.59           C  
ANISOU  743  CD2 LEU A 148     5695   6364   6403  -1146   -717    968       C  
ATOM    744  N   ARG A 149       0.627 -18.824 -33.774  1.00 44.97           N  
ANISOU  744  N   ARG A 149     5550   5776   5759   -689   -431    951       N  
ATOM    745  CA  ARG A 149       1.424 -19.633 -32.858  1.00 45.08           C  
ANISOU  745  CA  ARG A 149     5593   5709   5824   -648   -371   1029       C  
ATOM    746  C   ARG A 149       2.332 -18.745 -32.006  1.00 43.04           C  
ANISOU  746  C   ARG A 149     5264   5566   5523   -551   -309   1099       C  
ATOM    747  O   ARG A 149       2.232 -18.725 -30.769  1.00 42.14           O  
ANISOU  747  O   ARG A 149     5093   5493   5426   -568   -283   1200       O  
ATOM    748  CB  ARG A 149       2.270 -20.632 -33.651  1.00121.87           C  
ANISOU  748  CB  ARG A 149    15472  15267  15566   -583   -360    959       C  
ATOM    749  CG  ARG A 149       2.691 -21.872 -32.879  1.00123.19           C  
ANISOU  749  CG  ARG A 149    15692  15296  15819   -552   -329   1042       C  
ATOM    750  CD  ARG A 149       1.528 -22.838 -32.703  1.00123.99           C  
ANISOU  750  CD  ARG A 149    15825  15279  16006   -710   -386   1085       C  
ATOM    751  NE  ARG A 149       1.934 -24.062 -32.020  1.00126.05           N  
ANISOU  751  NE  ARG A 149    16210  15332  16352   -679   -379   1131       N  
ATOM    752  CZ  ARG A 149       2.462 -25.118 -32.630  1.00127.93           C  
ANISOU  752  CZ  ARG A 149    16608  15352  16647   -729   -431   1056       C  
ATOM    753  NH1 ARG A 149       2.652 -25.103 -33.943  1.00128.93           N  
ANISOU  753  NH1 ARG A 149    16786  15460  16743   -827   -502    929       N  
ATOM    754  NH2 ARG A 149       2.802 -26.190 -31.927  1.00128.85           N  
ANISOU  754  NH2 ARG A 149    16848  15259  16851   -682   -425   1107       N  
ATOM    755  N   ASP A 150       3.206 -18.003 -32.681  1.00 38.65           N  
ANISOU  755  N   ASP A 150     4718   5068   4901   -464   -290   1050       N  
ATOM    756  CA  ASP A 150       4.143 -17.113 -32.001  1.00 36.90           C  
ANISOU  756  CA  ASP A 150     4431   4951   4640   -394   -253   1111       C  
ATOM    757  C   ASP A 150       3.438 -16.078 -31.129  1.00 35.21           C  
ANISOU  757  C   ASP A 150     4134   4850   4397   -443   -268   1154       C  
ATOM    758  O   ASP A 150       3.843 -15.840 -29.991  1.00 34.49           O  
ANISOU  758  O   ASP A 150     4006   4806   4294   -431   -249   1232       O  
ATOM    759  CB  ASP A 150       5.061 -16.420 -33.012  1.00 58.38           C  
ANISOU  759  CB  ASP A 150     7166   7721   7295   -326   -232   1057       C  
ATOM    760  CG  ASP A 150       6.152 -17.337 -33.533  1.00 60.55           C  
ANISOU  760  CG  ASP A 150     7485   7929   7592   -225   -172   1046       C  
ATOM    761  OD1 ASP A 150       5.891 -18.550 -33.687  1.00 62.69           O  
ANISOU  761  OD1 ASP A 150     7827   8066   7926   -210   -166   1032       O  
ATOM    762  OD2 ASP A 150       7.273 -16.845 -33.780  1.00 60.52           O  
ANISOU  762  OD2 ASP A 150     7444   8002   7550   -160   -127   1056       O  
ATOM    763  N   ALA A 151       2.379 -15.477 -31.664  1.00 41.85           N  
ANISOU  763  N   ALA A 151     4949   5733   5219   -488   -306   1100       N  
ATOM    764  CA  ALA A 151       1.627 -14.455 -30.942  1.00 41.31           C  
ANISOU  764  CA  ALA A 151     4804   5765   5127   -503   -309   1122       C  
ATOM    765  C   ALA A 151       1.081 -14.987 -29.622  1.00 41.83           C  
ANISOU  765  C   ALA A 151     4823   5848   5222   -549   -270   1196       C  
ATOM    766  O   ALA A 151       1.249 -14.364 -28.570  1.00 41.66           O  
ANISOU  766  O   ALA A 151     4774   5902   5152   -528   -237   1236       O  
ATOM    767  CB  ALA A 151       0.493 -13.917 -31.811  1.00 22.55           C  
ANISOU  767  CB  ALA A 151     2397   3419   2753   -529   -365   1061       C  
ATOM    768  N   CYS A 152       0.429 -16.144 -29.684  1.00 32.02           N  
ANISOU  768  N   CYS A 152     3586   4530   4049   -622   -274   1215       N  
ATOM    769  CA  CYS A 152      -0.129 -16.767 -28.490  1.00 32.71           C  
ANISOU  769  CA  CYS A 152     3632   4633   4164   -690   -230   1308       C  
ATOM    770  C   CYS A 152       0.959 -17.156 -27.493  1.00 32.11           C  
ANISOU  770  C   CYS A 152     3608   4538   4055   -649   -195   1396       C  
ATOM    771  O   CYS A 152       0.773 -17.029 -26.278  1.00 32.34           O  
ANISOU  771  O   CYS A 152     3607   4646   4033   -666   -149   1470       O  
ATOM    772  CB  CYS A 152      -0.976 -17.985 -28.859  1.00 30.10           C  
ANISOU  772  CB  CYS A 152     3308   4203   3926   -804   -259   1321       C  
ATOM    773  SG  CYS A 152      -2.533 -17.586 -29.689  1.00 31.37           S  
ANISOU  773  SG  CYS A 152     3350   4432   4134   -891   -314   1263       S  
ATOM    774  N   THR A 153       2.092 -17.629 -28.008  1.00 42.92           N  
ANISOU  774  N   THR A 153     5051   5812   5444   -588   -216   1389       N  
ATOM    775  CA  THR A 153       3.223 -17.967 -27.145  1.00 42.66           C  
ANISOU  775  CA  THR A 153     5049   5765   5394   -537   -206   1485       C  
ATOM    776  C   THR A 153       3.711 -16.746 -26.359  1.00 41.68           C  
ANISOU  776  C   THR A 153     4888   5778   5171   -496   -204   1499       C  
ATOM    777  O   THR A 153       3.836 -16.789 -25.125  1.00 41.77           O  
ANISOU  777  O   THR A 153     4904   5841   5126   -507   -196   1589       O  
ATOM    778  CB  THR A 153       4.397 -18.552 -27.952  1.00 86.53           C  
ANISOU  778  CB  THR A 153    10664  11206  11006   -449   -221   1469       C  
ATOM    779  OG1 THR A 153       3.966 -19.734 -28.637  1.00 87.98           O  
ANISOU  779  OG1 THR A 153    10915  11248  11265   -484   -232   1411       O  
ATOM    780  CG2 THR A 153       5.556 -18.901 -27.030  1.00 86.89           C  
ANISOU  780  CG2 THR A 153    10731  11215  11069   -399   -227   1596       C  
ATOM    781  N   TYR A 154       3.984 -15.663 -27.084  1.00 42.78           N  
ANISOU  781  N   TYR A 154     5008   5969   5279   -460   -221   1411       N  
ATOM    782  CA  TYR A 154       4.420 -14.409 -26.472  1.00 42.25           C  
ANISOU  782  CA  TYR A 154     4926   6004   5123   -439   -235   1407       C  
ATOM    783  C   TYR A 154       3.406 -13.902 -25.449  1.00 43.11           C  
ANISOU  783  C   TYR A 154     5024   6194   5164   -475   -203   1415       C  
ATOM    784  O   TYR A 154       3.778 -13.487 -24.347  1.00 43.42           O  
ANISOU  784  O   TYR A 154     5088   6294   5115   -474   -206   1458       O  
ATOM    785  CB  TYR A 154       4.655 -13.335 -27.539  1.00 39.63           C  
ANISOU  785  CB  TYR A 154     4589   5690   4779   -413   -260   1319       C  
ATOM    786  CG  TYR A 154       5.992 -13.424 -28.243  1.00 39.09           C  
ANISOU  786  CG  TYR A 154     4520   5603   4730   -369   -275   1327       C  
ATOM    787  CD1 TYR A 154       7.172 -13.118 -27.575  1.00 38.94           C  
ANISOU  787  CD1 TYR A 154     4479   5633   4684   -354   -303   1392       C  
ATOM    788  CD2 TYR A 154       6.073 -13.791 -29.581  1.00 39.27           C  
ANISOU  788  CD2 TYR A 154     4558   5573   4789   -345   -260   1271       C  
ATOM    789  CE1 TYR A 154       8.396 -13.189 -28.215  1.00 39.09           C  
ANISOU  789  CE1 TYR A 154     4459   5660   4733   -312   -304   1412       C  
ATOM    790  CE2 TYR A 154       7.292 -13.867 -30.229  1.00 39.52           C  
ANISOU  790  CE2 TYR A 154     4575   5610   4829   -293   -244   1279       C  
ATOM    791  CZ  TYR A 154       8.450 -13.564 -29.542  1.00 39.47           C  
ANISOU  791  CZ  TYR A 154     4515   5664   4817   -275   -260   1356       C  
ATOM    792  OH  TYR A 154       9.665 -13.637 -30.184  1.00 40.31           O  
ANISOU  792  OH  TYR A 154     4570   5800   4946   -222   -231   1377       O  
ATOM    793  N   ALA A 155       2.129 -13.938 -25.822  1.00 43.17           N  
ANISOU  793  N   ALA A 155     4989   6208   5205   -506   -171   1372       N  
ATOM    794  CA  ALA A 155       1.055 -13.508 -24.931  1.00 44.83           C  
ANISOU  794  CA  ALA A 155     5162   6510   5361   -522   -111   1375       C  
ATOM    795  C   ALA A 155       1.066 -14.300 -23.629  1.00 45.41           C  
ANISOU  795  C   ALA A 155     5256   6613   5385   -568    -61   1485       C  
ATOM    796  O   ALA A 155       0.966 -13.727 -22.541  1.00 46.60           O  
ANISOU  796  O   ALA A 155     5430   6855   5422   -556    -18   1499       O  
ATOM    797  CB  ALA A 155      -0.294 -13.637 -25.623  1.00 35.51           C  
ANISOU  797  CB  ALA A 155     3894   5342   4257   -552    -91   1334       C  
ATOM    798  N   THR A 156       1.201 -15.617 -23.751  1.00 47.27           N  
ANISOU  798  N   THR A 156     5505   6759   5696   -618    -70   1564       N  
ATOM    799  CA  THR A 156       1.247 -16.497 -22.588  1.00 47.85           C  
ANISOU  799  CA  THR A 156     5613   6838   5728   -670    -35   1696       C  
ATOM    800  C   THR A 156       2.430 -16.174 -21.680  1.00 47.43           C  
ANISOU  800  C   THR A 156     5632   6824   5566   -622    -76   1748       C  
ATOM    801  O   THR A 156       2.265 -16.005 -20.469  1.00 48.45           O  
ANISOU  801  O   THR A 156     5795   7046   5568   -644    -38   1807       O  
ATOM    802  CB  THR A 156       1.321 -17.977 -23.004  1.00 51.92           C  
ANISOU  802  CB  THR A 156     6158   7207   6364   -724    -59   1772       C  
ATOM    803  OG1 THR A 156       0.187 -18.303 -23.816  1.00 52.60           O  
ANISOU  803  OG1 THR A 156     6181   7261   6544   -800    -42   1729       O  
ATOM    804  CG2 THR A 156       1.332 -18.875 -21.776  1.00 52.67           C  
ANISOU  804  CG2 THR A 156     6304   7296   6412   -782    -32   1934       C  
ATOM    805  N   ALA A 157       3.620 -16.083 -22.269  1.00 44.35           N  
ANISOU  805  N   ALA A 157     5259   6376   5217   -561   -155   1728       N  
ATOM    806  CA  ALA A 157       4.828 -15.792 -21.497  1.00 44.12           C  
ANISOU  806  CA  ALA A 157     5269   6388   5105   -527   -222   1787       C  
ATOM    807  C   ALA A 157       4.727 -14.459 -20.755  1.00 44.67           C  
ANISOU  807  C   ALA A 157     5368   6577   5026   -530   -224   1727       C  
ATOM    808  O   ALA A 157       4.962 -14.386 -19.540  1.00 45.37           O  
ANISOU  808  O   ALA A 157     5518   6735   4985   -550   -246   1793       O  
ATOM    809  CB  ALA A 157       6.053 -15.809 -22.404  1.00 23.51           C  
ANISOU  809  CB  ALA A 157     2632   3718   2583   -461   -290   1769       C  
ATOM    810  N   LEU A 158       4.370 -13.410 -21.492  1.00 40.24           N  
ANISOU  810  N   LEU A 158     4783   6031   4476   -509   -208   1599       N  
ATOM    811  CA  LEU A 158       4.227 -12.077 -20.914  1.00 41.31           C  
ANISOU  811  CA  LEU A 158     4968   6241   4484   -498   -214   1520       C  
ATOM    812  C   LEU A 158       3.174 -12.051 -19.807  1.00 43.44           C  
ANISOU  812  C   LEU A 158     5271   6597   4636   -512   -115   1526       C  
ATOM    813  O   LEU A 158       3.353 -11.382 -18.784  1.00 44.76           O  
ANISOU  813  O   LEU A 158     5527   6832   4646   -510   -123   1505       O  
ATOM    814  CB  LEU A 158       3.894 -11.046 -21.996  1.00 23.32           C  
ANISOU  814  CB  LEU A 158     2665   3933   2262   -461   -221   1396       C  
ATOM    815  CG  LEU A 158       4.996 -10.767 -23.021  1.00 22.65           C  
ANISOU  815  CG  LEU A 158     2561   3791   2253   -454   -305   1387       C  
ATOM    816  CD1 LEU A 158       4.558  -9.694 -24.008  1.00 21.39           C  
ANISOU  816  CD1 LEU A 158     2400   3604   2125   -429   -313   1283       C  
ATOM    817  CD2 LEU A 158       6.286 -10.370 -22.327  1.00 23.73           C  
ANISOU  817  CD2 LEU A 158     2738   3959   2320   -479   -397   1435       C  
ATOM    818  N   ASN A 159       2.081 -12.781 -20.013  1.00 30.92           N  
ANISOU  818  N   ASN A 159     3615   5014   3119   -534    -21   1555       N  
ATOM    819  CA  ASN A 159       1.054 -12.904 -18.982  1.00 32.69           C  
ANISOU  819  CA  ASN A 159     3841   5342   3238   -557     99   1587       C  
ATOM    820  C   ASN A 159       1.586 -13.591 -17.728  1.00 34.09           C  
ANISOU  820  C   ASN A 159     4107   5560   3285   -608     92   1720       C  
ATOM    821  O   ASN A 159       1.211 -13.238 -16.607  1.00 35.74           O  
ANISOU  821  O   ASN A 159     4384   5879   3318   -610    164   1723       O  
ATOM    822  CB  ASN A 159      -0.174 -13.649 -19.510  1.00 64.19           C  
ANISOU  822  CB  ASN A 159     7707   9330   7350   -600    189   1615       C  
ATOM    823  CG  ASN A 159      -1.101 -12.754 -20.303  1.00 65.55           C  
ANISOU  823  CG  ASN A 159     7788   9527   7592   -540    222   1489       C  
ATOM    824  OD1 ASN A 159      -1.564 -13.122 -21.381  1.00 64.87           O  
ANISOU  824  OD1 ASN A 159     7611   9382   7652   -562    195   1474       O  
ATOM    825  ND2 ASN A 159      -1.377 -11.570 -19.772  1.00 67.87           N  
ANISOU  825  ND2 ASN A 159     8115   9897   7775   -459    271   1395       N  
ATOM    826  N   VAL A 160       2.461 -14.574 -17.923  1.00 61.51           N  
ANISOU  826  N   VAL A 160     7589   8943   6836   -637      6   1830       N  
ATOM    827  CA  VAL A 160       3.075 -15.278 -16.801  1.00 61.73           C  
ANISOU  827  CA  VAL A 160     7704   8996   6754   -676    -33   1980       C  
ATOM    828  C   VAL A 160       3.982 -14.351 -15.993  1.00 62.16           C  
ANISOU  828  C   VAL A 160     7857   9122   6639   -653   -125   1947       C  
ATOM    829  O   VAL A 160       3.876 -14.279 -14.764  1.00 63.60           O  
ANISOU  829  O   VAL A 160     8138   9400   6625   -684   -106   2004       O  
ATOM    830  CB  VAL A 160       3.868 -16.515 -17.269  1.00 41.65           C  
ANISOU  830  CB  VAL A 160     5147   6319   4359   -681   -119   2102       C  
ATOM    831  CG1 VAL A 160       4.757 -17.037 -16.149  1.00 42.10           C  
ANISOU  831  CG1 VAL A 160     5294   6398   4303   -696   -202   2260       C  
ATOM    832  CG2 VAL A 160       2.917 -17.597 -17.749  1.00 41.76           C  
ANISOU  832  CG2 VAL A 160     5111   6250   4508   -739    -40   2155       C  
ATOM    833  N   VAL A 161       4.867 -13.637 -16.685  1.00 41.37           N  
ANISOU  833  N   VAL A 161     5203   6445   4070   -611   -228   1859       N  
ATOM    834  CA  VAL A 161       5.758 -12.693 -16.012  1.00 41.84           C  
ANISOU  834  CA  VAL A 161     5350   6558   3989   -615   -341   1823       C  
ATOM    835  C   VAL A 161       4.957 -11.620 -15.275  1.00 44.07           C  
ANISOU  835  C   VAL A 161     5735   6927   4082   -610   -265   1702       C  
ATOM    836  O   VAL A 161       5.261 -11.271 -14.126  1.00 45.42           O  
ANISOU  836  O   VAL A 161     6036   7174   4049   -640   -313   1715       O  
ATOM    837  CB  VAL A 161       6.722 -12.014 -17.001  1.00 28.73           C  
ANISOU  837  CB  VAL A 161     3632   4837   2449   -592   -449   1753       C  
ATOM    838  CG1 VAL A 161       7.730 -11.158 -16.252  1.00 29.88           C  
ANISOU  838  CG1 VAL A 161     3864   5033   2454   -629   -584   1724       C  
ATOM    839  CG2 VAL A 161       7.434 -13.056 -17.843  1.00 28.67           C  
ANISOU  839  CG2 VAL A 161     3523   4756   2616   -570   -502   1860       C  
ATOM    840  N   SER A 162       3.924 -11.111 -15.939  1.00 48.49           N  
ANISOU  840  N   SER A 162     6243   7475   4705   -564   -150   1584       N  
ATOM    841  CA  SER A 162       3.064 -10.095 -15.346  1.00 51.20           C  
ANISOU  841  CA  SER A 162     6671   7887   4894   -521    -55   1454       C  
ATOM    842  C   SER A 162       2.370 -10.624 -14.094  1.00 53.09           C  
ANISOU  842  C   SER A 162     6966   8249   4958   -543     76   1526       C  
ATOM    843  O   SER A 162       2.241  -9.910 -13.099  1.00 55.44           O  
ANISOU  843  O   SER A 162     7397   8627   5042   -519    125   1447       O  
ATOM    844  CB  SER A 162       2.029  -9.603 -16.358  1.00 71.79           C  
ANISOU  844  CB  SER A 162     9181  10458   7638   -448     35   1335       C  
ATOM    845  OG  SER A 162       1.265  -8.545 -15.810  1.00 74.83           O  
ANISOU  845  OG  SER A 162     9646  10896   7887   -374    127   1202       O  
ATOM    846  N   LEU A 163       1.926 -11.877 -14.148  1.00 43.51           N  
ANISOU  846  N   LEU A 163     5665   7043   3826   -594    137   1676       N  
ATOM    847  CA  LEU A 163       1.326 -12.525 -12.986  1.00 45.06           C  
ANISOU  847  CA  LEU A 163     5908   7355   3858   -642    261   1787       C  
ATOM    848  C   LEU A 163       2.333 -12.645 -11.849  1.00 45.55           C  
ANISOU  848  C   LEU A 163     6136   7462   3709   -690    148   1879       C  
ATOM    849  O   LEU A 163       1.977 -12.512 -10.677  1.00 47.87           O  
ANISOU  849  O   LEU A 163     6549   7881   3759   -707    234   1897       O  
ATOM    850  CB  LEU A 163       0.775 -13.904 -13.353  1.00 45.70           C  
ANISOU  850  CB  LEU A 163     5865   7400   4097   -710    327   1942       C  
ATOM    851  CG  LEU A 163      -0.666 -13.942 -13.864  1.00 46.72           C  
ANISOU  851  CG  LEU A 163     5842   7574   4334   -703    500   1897       C  
ATOM    852  CD1 LEU A 163      -1.038 -15.351 -14.298  1.00 45.61           C  
ANISOU  852  CD1 LEU A 163     5601   7369   4358   -805    522   2057       C  
ATOM    853  CD2 LEU A 163      -1.617 -13.440 -12.790  1.00 49.59           C  
ANISOU  853  CD2 LEU A 163     6240   8116   4485   -676    687   1860       C  
ATOM    854  N   SER A 164       3.591 -12.899 -12.200  1.00 40.04           N  
ANISOU  854  N   SER A 164     5439   6674   3098   -708    -46   1940       N  
ATOM    855  CA  SER A 164       4.657 -12.978 -11.209  1.00 42.40           C  
ANISOU  855  CA  SER A 164     5874   7017   3218   -753   -197   2033       C  
ATOM    856  C   SER A 164       4.830 -11.640 -10.501  1.00 42.99           C  
ANISOU  856  C   SER A 164     6104   7162   3068   -740   -237   1872       C  
ATOM    857  O   SER A 164       4.890 -11.577  -9.270  1.00 45.81           O  
ANISOU  857  O   SER A 164     6625   7624   3156   -778   -245   1904       O  
ATOM    858  CB  SER A 164       5.971 -13.402 -11.865  1.00 60.08           C  
ANISOU  858  CB  SER A 164     8038   9155   5634   -754   -394   2119       C  
ATOM    859  OG  SER A 164       5.837 -14.658 -12.507  1.00 58.81           O  
ANISOU  859  OG  SER A 164     7765   8903   5675   -750   -359   2248       O  
ATOM    860  N   VAL A 165       4.900 -10.570 -11.288  1.00 43.47           N  
ANISOU  860  N   VAL A 165     6133   7153   3230   -692   -265   1699       N  
ATOM    861  CA  VAL A 165       5.038  -9.226 -10.733  1.00 45.33           C  
ANISOU  861  CA  VAL A 165     6533   7408   3283   -679   -314   1525       C  
ATOM    862  C   VAL A 165       3.851  -8.856  -9.840  1.00 48.28           C  
ANISOU  862  C   VAL A 165     7028   7887   3429   -630   -115   1430       C  
ATOM    863  O   VAL A 165       4.030  -8.388  -8.711  1.00 50.14           O  
ANISOU  863  O   VAL A 165     7467   8196   3388   -652   -148   1379       O  
ATOM    864  CB  VAL A 165       5.189  -8.174 -11.847  1.00 43.21           C  
ANISOU  864  CB  VAL A 165     6205   7021   3189   -634   -359   1370       C  
ATOM    865  CG1 VAL A 165       5.284  -6.779 -11.251  1.00 45.72           C  
ANISOU  865  CG1 VAL A 165     6720   7327   3322   -615   -392   1179       C  
ATOM    866  CG2 VAL A 165       6.411  -8.478 -12.699  1.00 40.52           C  
ANISOU  866  CG2 VAL A 165     5758   6603   3035   -686   -548   1455       C  
ATOM    867  N   GLU A 166       2.642  -9.077 -10.350  1.00 53.79           N  
ANISOU  867  N   GLU A 166     7595   8603   4239   -563     92   1408       N  
ATOM    868  CA  GLU A 166       1.422  -8.757  -9.612  1.00 56.73           C  
ANISOU  868  CA  GLU A 166     8031   9094   4427   -493    318   1320       C  
ATOM    869  C   GLU A 166       1.321  -9.539  -8.307  1.00 57.66           C  
ANISOU  869  C   GLU A 166     8248   9362   4297   -562    399   1466       C  
ATOM    870  O   GLU A 166       0.879  -9.003  -7.290  1.00 60.30           O  
ANISOU  870  O   GLU A 166     8733   9814   4364   -521    531   1381       O  
ATOM    871  CB  GLU A 166       0.182  -9.011 -10.474  1.00121.40           C  
ANISOU  871  CB  GLU A 166    16011  17287  12826   -417    506   1291       C  
ATOM    872  CG  GLU A 166       0.049  -8.078 -11.667  1.00121.83           C  
ANISOU  872  CG  GLU A 166    16021  17226  13042   -313    473   1109       C  
ATOM    873  CD  GLU A 166      -0.196  -6.637 -11.261  1.00124.10           C  
ANISOU  873  CD  GLU A 166    16199  17580  13372   -186    696   1010       C  
ATOM    874  OE1 GLU A 166      -0.737  -6.410 -10.158  1.00125.52           O  
ANISOU  874  OE1 GLU A 166    16342  17915  13436   -181    893   1071       O  
ATOM    875  OE2 GLU A 166       0.152  -5.730 -12.047  1.00124.54           O  
ANISOU  875  OE2 GLU A 166    16198  17541  13581    -90    675    885       O  
ATOM    876  N   LEU A 167       1.729 -10.804  -8.338  1.00 74.31           N  
ANISOU  876  N   LEU A 167    10287  11462   6488   -659    325   1688       N  
ATOM    877  CA  LEU A 167       1.715 -11.634  -7.139  1.00 75.27           C  
ANISOU  877  CA  LEU A 167    10517  11710   6375   -738    374   1862       C  
ATOM    878  C   LEU A 167       2.744 -11.126  -6.132  1.00 76.23           C  
ANISOU  878  C   LEU A 167    10882  11874   6210   -776    198   1836       C  
ATOM    879  O   LEU A 167       2.478 -11.086  -4.926  1.00 78.46           O  
ANISOU  879  O   LEU A 167    11343  12298   6172   -795    289   1845       O  
ATOM    880  CB  LEU A 167       1.985 -13.100  -7.485  1.00 71.03           C  
ANISOU  880  CB  LEU A 167     9859  11111   6016   -825    313   2111       C  
ATOM    881  CG  LEU A 167       1.856 -14.092  -6.326  1.00 72.22           C  
ANISOU  881  CG  LEU A 167    10075  11382   5984   -912    430   2323       C  
ATOM    882  CD1 LEU A 167       0.463 -14.029  -5.719  1.00 74.02           C  
ANISOU  882  CD1 LEU A 167    10211  11731   6183   -895    731   2291       C  
ATOM    883  CD2 LEU A 167       2.179 -15.508  -6.780  1.00 70.38           C  
ANISOU  883  CD2 LEU A 167     9766  11036   5940   -990    314   2567       C  
ATOM    884  N   TYR A 168       3.915 -10.739  -6.633  1.00 69.22           N  
ANISOU  884  N   TYR A 168     9999  10872   5430   -795    -53   1805       N  
ATOM    885  CA  TYR A 168       4.950 -10.157  -5.783  1.00 70.10           C  
ANISOU  885  CA  TYR A 168    10321  11014   5298   -852   -265   1776       C  
ATOM    886  C   TYR A 168       4.426  -8.921  -5.064  1.00 72.97           C  
ANISOU  886  C   TYR A 168    10896  11432   5397   -799   -174   1534       C  
ATOM    887  O   TYR A 168       4.577  -8.789  -3.850  1.00 74.97           O  
ANISOU  887  O   TYR A 168    11380  11794   5310   -841   -200   1525       O  
ATOM    888  CB  TYR A 168       6.195  -9.790  -6.594  1.00 54.18           C  
ANISOU  888  CB  TYR A 168     8224   8871   3490   -884   -531   1772       C  
ATOM    889  CG  TYR A 168       7.252  -9.063  -5.787  1.00 56.46           C  
ANISOU  889  CG  TYR A 168     8708   9186   3559   -962   -776   1723       C  
ATOM    890  CD1 TYR A 168       8.187  -9.766  -5.039  1.00 58.97           C  
ANISOU  890  CD1 TYR A 168     9073   9566   3766  -1051   -980   1921       C  
ATOM    891  CD2 TYR A 168       7.314  -7.673  -5.773  1.00 56.45           C  
ANISOU  891  CD2 TYR A 168     8848   9136   3464   -953   -823   1485       C  
ATOM    892  CE1 TYR A 168       9.153  -9.109  -4.300  1.00 61.44           C  
ANISOU  892  CE1 TYR A 168     9554   9913   3877  -1141  -1230   1883       C  
ATOM    893  CE2 TYR A 168       8.276  -7.007  -5.037  1.00 58.95           C  
ANISOU  893  CE2 TYR A 168     9353   9465   3579  -1051  -1067   1436       C  
ATOM    894  CZ  TYR A 168       9.193  -7.730  -4.303  1.00 61.46           C  
ANISOU  894  CZ  TYR A 168     9700   9867   3786  -1151  -1275   1636       C  
ATOM    895  OH  TYR A 168      10.154  -7.072  -3.569  1.00 64.40           O  
ANISOU  895  OH  TYR A 168    10250  10261   3956  -1266  -1546   1594       O  
ATOM    896  N   LEU A 169       3.813  -8.017  -5.822  1.00 57.43           N  
ANISOU  896  N   LEU A 169     8862   9380   3579   -699    -73   1336       N  
ATOM    897  CA  LEU A 169       3.244  -6.803  -5.246  1.00 59.84           C  
ANISOU  897  CA  LEU A 169     9365   9699   3670   -614     25   1087       C  
ATOM    898  C   LEU A 169       2.094  -7.129  -4.299  1.00 62.45           C  
ANISOU  898  C   LEU A 169     9776  10205   3744   -553    311   1080       C  
ATOM    899  O   LEU A 169       1.809  -6.372  -3.370  1.00 65.16           O  
ANISOU  899  O   LEU A 169    10372  10618   3767   -517    363    930       O  
ATOM    900  CB  LEU A 169       2.770  -5.852  -6.347  1.00 54.59           C  
ANISOU  900  CB  LEU A 169     8590   8894   3256   -501     78    907       C  
ATOM    901  CG  LEU A 169       3.860  -5.167  -7.174  1.00 52.55           C  
ANISOU  901  CG  LEU A 169     8326   8466   3176   -557   -187    853       C  
ATOM    902  CD1 LEU A 169       3.242  -4.293  -8.256  1.00 51.87           C  
ANISOU  902  CD1 LEU A 169     8150   8246   3312   -441   -113    692       C  
ATOM    903  CD2 LEU A 169       4.775  -4.348  -6.277  1.00 55.50           C  
ANISOU  903  CD2 LEU A 169     8981   8821   3285   -641   -394    752       C  
ATOM    904  N   ALA A 170       1.441  -8.262  -4.535  1.00 73.75           N  
ANISOU  904  N   ALA A 170    10997  11711   5311   -549    498   1242       N  
ATOM    905  CA  ALA A 170       0.325  -8.692  -3.702  1.00 76.06           C  
ANISOU  905  CA  ALA A 170    11316  12193   5391   -506    795   1268       C  
ATOM    906  C   ALA A 170       0.796  -9.203  -2.344  1.00 77.23           C  
ANISOU  906  C   ALA A 170    11691  12484   5168   -611    759   1399       C  
ATOM    907  O   ALA A 170       0.126  -8.996  -1.333  1.00 80.15           O  
ANISOU  907  O   ALA A 170    12241  13005   5208   -563    945   1311       O  
ATOM    908  CB  ALA A 170      -0.491  -9.759  -4.416  1.00 68.43           C  
ANISOU  908  CB  ALA A 170    10053  11261   4685   -516    973   1433       C  
ATOM    909  N   ILE A 171       1.947  -9.868  -2.318  1.00 74.27           N  
ANISOU  909  N   ILE A 171    11313  12067   4839   -744    522   1611       N  
ATOM    910  CA  ILE A 171       2.445 -10.456  -1.075  1.00 75.42           C  
ANISOU  910  CA  ILE A 171    11666  12345   4643   -850    459   1775       C  
ATOM    911  C   ILE A 171       3.437  -9.565  -0.323  1.00 76.87           C  
ANISOU  911  C   ILE A 171    12152  12533   4523   -887    226   1644       C  
ATOM    912  O   ILE A 171       3.673  -9.761   0.870  1.00 80.16           O  
ANISOU  912  O   ILE A 171    12821  13100   4536   -913    286   1632       O  
ATOM    913  CB  ILE A 171       3.084 -11.843  -1.309  1.00112.76           C  
ANISOU  913  CB  ILE A 171    16266  17038   9539   -966    321   2096       C  
ATOM    914  CG1 ILE A 171       4.451 -11.704  -1.981  1.00113.69           C  
ANISOU  914  CG1 ILE A 171    16601  17306   9290  -1070    281   2294       C  
ATOM    915  CG2 ILE A 171       2.161 -12.729  -2.132  1.00110.47           C  
ANISOU  915  CG2 ILE A 171    15878  16571   9526   -991      5   2118       C  
ATOM    916  CD1 ILE A 171       5.181 -13.018  -2.146  1.00111.76           C  
ANISOU  916  CD1 ILE A 171    16251  17014   9200  -1166    166   2620       C  
ATOM    917  N   CYS A 172       4.016  -8.589  -1.017  1.00 81.65           N  
ANISOU  917  N   CYS A 172    12735  12977   5311   -900    -39   1547       N  
ATOM    918  CA  CYS A 172       5.001  -7.703  -0.400  1.00 82.70           C  
ANISOU  918  CA  CYS A 172    13131  13095   5197   -968   -305   1433       C  
ATOM    919  C   CYS A 172       4.411  -6.360   0.019  1.00 85.50           C  
ANISOU  919  C   CYS A 172    13728  13444   5315   -878   -195   1110       C  
ATOM    920  O   CYS A 172       4.673  -5.878   1.122  1.00 87.77           O  
ANISOU  920  O   CYS A 172    14325  13810   5212   -922   -270   1020       O  
ATOM    921  CB  CYS A 172       6.201  -7.487  -1.324  1.00 82.39           C  
ANISOU  921  CB  CYS A 172    12957  12895   5451  -1034   -625   1465       C  
ATOM    922  SG  CYS A 172       7.438  -8.797  -1.245  1.00 79.44           S  
ANISOU  922  SG  CYS A 172    12355  12519   5307  -1121   -802   1830       S  
ATOM    923  N   HIS A 173       3.617  -5.756  -0.859  1.00121.54           N  
ANISOU  923  N   HIS A 173    18160  17905  10114   -744    -28    934       N  
ATOM    924  CA  HIS A 173       2.981  -4.480  -0.550  1.00124.17           C  
ANISOU  924  CA  HIS A 173    18703  18189  10287   -621     83    617       C  
ATOM    925  C   HIS A 173       1.472  -4.545  -0.759  1.00125.71           C  
ANISOU  925  C   HIS A 173    18766  18461  10537   -440    476    542       C  
ATOM    926  O   HIS A 173       0.947  -3.885  -1.653  1.00125.18           O  
ANISOU  926  O   HIS A 173    18520  18273  10769   -327    554    439       O  
ATOM    927  CB  HIS A 173       3.566  -3.368  -1.421  1.00 94.22           C  
ANISOU  927  CB  HIS A 173    14896  14165   6737   -622   -137    455       C  
ATOM    928  CG  HIS A 173       5.061  -3.291  -1.384  1.00 92.65           C  
ANISOU  928  CG  HIS A 173    14758  13901   6545   -809   -524    547       C  
ATOM    929  ND1 HIS A 173       5.744  -2.496  -0.490  1.00 93.60           N  
ANISOU  929  ND1 HIS A 173    15187  13961   6416   -893   -750    381       N  
ATOM    930  CD2 HIS A 173       6.003  -3.908  -2.136  1.00 90.36           C  
ANISOU  930  CD2 HIS A 173    14250  13599   6485   -926   -727    788       C  
ATOM    931  CE1 HIS A 173       7.044  -2.627  -0.692  1.00 91.96           C  
ANISOU  931  CE1 HIS A 173    14923  13725   6294  -1065  -1082    529       C  
ATOM    932  NE2 HIS A 173       7.227  -3.478  -1.685  1.00 90.04           N  
ANISOU  932  NE2 HIS A 173    14357  13513   6342  -1074  -1065    777       N  
ATOM    933  N   PRO A 174       0.768  -5.328   0.074  1.00122.46           N  
ANISOU  933  N   PRO A 174    18430  18263   9834   -418    723    610       N  
ATOM    934  CA  PRO A 174      -0.677  -5.507  -0.102  1.00123.76           C  
ANISOU  934  CA  PRO A 174    18415  18558  10048   -274   1114    604       C  
ATOM    935  C   PRO A 174      -1.453  -4.232   0.213  1.00125.13           C  
ANISOU  935  C   PRO A 174    18598  18643  10300    -55   1282    304       C  
ATOM    936  O   PRO A 174      -2.529  -4.016  -0.342  1.00125.61           O  
ANISOU  936  O   PRO A 174    18391  18740  10594     67   1520    312       O  
ATOM    937  CB  PRO A 174      -1.016  -6.598   0.917  1.00117.46           C  
ANISOU  937  CB  PRO A 174    17826  18006   8798   -303   1304    670       C  
ATOM    938  CG  PRO A 174       0.001  -6.431   1.986  1.00116.56           C  
ANISOU  938  CG  PRO A 174    17920  17892   8478   -495    984    811       C  
ATOM    939  CD  PRO A 174       1.263  -6.002   1.288  1.00115.05           C  
ANISOU  939  CD  PRO A 174    17781  17469   8466   -536    632    686       C  
ATOM    940  N   PHE A 175      -0.906  -3.401   1.094  1.00154.14           N  
ANISOU  940  N   PHE A 175    22582  22200  13783     -4   1156     46       N  
ATOM    941  CA  PHE A 175      -1.539  -2.137   1.452  1.00154.75           C  
ANISOU  941  CA  PHE A 175    22691  22154  13951    219   1293   -239       C  
ATOM    942  C   PHE A 175      -1.363  -1.103   0.343  1.00152.64           C  
ANISOU  942  C   PHE A 175    22289  21623  14086    224   1070   -295       C  
ATOM    943  O   PHE A 175      -2.198  -0.215   0.171  1.00153.03           O  
ANISOU  943  O   PHE A 175    22323  21546  14275    412   1167   -494       O  
ATOM    944  CB  PHE A 175      -0.995  -1.610   2.785  1.00210.16           C  
ANISOU  944  CB  PHE A 175    30130  29176  20544    319   1354   -523       C  
ATOM    945  CG  PHE A 175       0.507  -1.570   2.861  1.00213.79           C  
ANISOU  945  CG  PHE A 175    30683  29920  20627    383   1683   -500       C  
ATOM    946  CD1 PHE A 175       1.226  -2.696   3.232  1.00213.12           C  
ANISOU  946  CD1 PHE A 175    30265  30038  20673    433   1990   -310       C  
ATOM    947  CD2 PHE A 175       1.198  -0.405   2.575  1.00217.99           C  
ANISOU  947  CD2 PHE A 175    31634  30521  20670    385   1691   -668       C  
ATOM    948  CE1 PHE A 175       2.606  -2.662   3.305  1.00216.52           C  
ANISOU  948  CE1 PHE A 175    30760  30747  20762    478   2313   -267       C  
ATOM    949  CE2 PHE A 175       2.579  -0.366   2.649  1.00221.45           C  
ANISOU  949  CE2 PHE A 175    32159  31240  20741    445   2018   -639       C  
ATOM    950  CZ  PHE A 175       3.283  -1.496   3.014  1.00220.70           C  
ANISOU  950  CZ  PHE A 175    31709  31356  20790    491   2338   -430       C  
ATOM    951  N   LYS A 176      -0.273  -1.228  -0.408  1.00145.05           N  
ANISOU  951  N   LYS A 176    21218  20585  13310     27    782   -106       N  
ATOM    952  CA  LYS A 176      -0.043  -0.382  -1.572  1.00142.71           C  
ANISOU  952  CA  LYS A 176    20694  20099  13433     22    636    -78       C  
ATOM    953  C   LYS A 176      -0.700  -1.007  -2.798  1.00141.85           C  
ANISOU  953  C   LYS A 176    20218  20088  13591     93    865     76       C  
ATOM    954  O   LYS A 176      -0.882  -0.349  -3.822  1.00140.25           O  
ANISOU  954  O   LYS A 176    19799  19764  13725    146    840     79       O  
ATOM    955  CB  LYS A 176       1.457  -0.204  -1.822  1.00104.78           C  
ATOM    956  CG  LYS A 176       2.209   0.508  -0.708  1.00104.78           C  
ATOM    957  CD  LYS A 176       1.912   2.000  -0.683  1.00104.78           C  
ATOM    958  CE  LYS A 176       2.765   2.710   0.361  1.00104.78           C  
ATOM    959  NZ  LYS A 176       2.584   4.188   0.326  1.00104.78           N  
ATOM    960  N   ALA A 177      -1.052  -2.285  -2.686  1.00139.51           N  
ANISOU  960  N   ALA A 177    19863  20015  13131     79   1080    214       N  
ATOM    961  CA  ALA A 177      -1.671  -3.014  -3.789  1.00139.12           C  
ANISOU  961  CA  ALA A 177    19489  20082  13290    146   1333    338       C  
ATOM    962  C   ALA A 177      -3.187  -2.858  -3.792  1.00141.76           C  
ANISOU  962  C   ALA A 177    19837  20529  13497    369   1663    157       C  
ATOM    963  O   ALA A 177      -3.814  -2.883  -4.849  1.00141.97           O  
ANISOU  963  O   ALA A 177    19579  20655  13710    455   1886    221       O  
ATOM    964  CB  ALA A 177      -1.292  -4.485  -3.738  1.00101.24           C  
ANISOU  964  CB  ALA A 177    14587  15450   8429    -17   1376    623       C  
ATOM    965  N   LYS A 178      -3.775  -2.710  -2.609  1.00177.61           N  
ANISOU  965  N   LYS A 178    24707  25059  17716    464   1694    -69       N  
ATOM    966  CA  LYS A 178      -5.210  -2.470  -2.510  1.00180.01           C  
ANISOU  966  CA  LYS A 178    25048  25416  17931    727   1986   -295       C  
ATOM    967  C   LYS A 178      -5.543  -1.085  -3.052  1.00179.11           C  
ANISOU  967  C   LYS A 178    24862  25057  18133    870   1880   -456       C  
ATOM    968  O   LYS A 178      -6.624  -0.866  -3.596  1.00180.31           O  
ANISOU  968  O   LYS A 178    24880  25227  18404   1101   2102   -574       O  
ATOM    969  CB  LYS A 178      -5.709  -2.652  -1.075  1.00145.80           C  
ATOM    970  CG  LYS A 178      -5.757  -4.109  -0.640  1.00145.80           C  
ATOM    971  CD  LYS A 178      -6.489  -4.285   0.678  1.00145.80           C  
ATOM    972  CE  LYS A 178      -6.607  -5.758   1.039  1.00145.80           C  
ATOM    973  NZ  LYS A 178      -7.365  -5.962   2.303  1.00145.80           N  
ATOM    974  N   THR A 179      -4.607  -0.154  -2.902  1.00201.25           N  
ANISOU  974  N   THR A 179    27754  27639  21070    731   1538   -450       N  
ATOM    975  CA  THR A 179      -4.633   1.069  -3.691  1.00200.08           C  
ANISOU  975  CA  THR A 179    27528  27251  21242    817   1400   -548       C  
ATOM    976  C   THR A 179      -4.214   0.635  -5.088  1.00199.23           C  
ANISOU  976  C   THR A 179    27006  27228  21464    876   1547   -395       C  
ATOM    977  O   THR A 179      -3.055   0.773  -5.477  1.00200.38           O  
ANISOU  977  O   THR A 179    27031  27329  21774   1089   1681   -507       O  
ATOM    978  CB  THR A 179      -3.656   2.124  -3.147  1.00163.15           C  
ANISOU  978  CB  THR A 179    22929  22375  16685    606   1025   -485       C  
ATOM    979  OG1 THR A 179      -2.324   1.596  -3.152  1.00165.19           O  
ANISOU  979  OG1 THR A 179    23573  22542  16649    540    860   -641       O  
ATOM    980  CG2 THR A 179      -4.034   2.520  -1.724  1.00161.03           C  
ANISOU  980  CG2 THR A 179    22535  21886  16763    679    911   -536       C  
ATOM    981  N   LEU A 180      -5.178   0.109  -5.836  1.00170.46           N  
ANISOU  981  N   LEU A 180    23157  23702  17911    687   1512   -138       N  
ATOM    982  CA  LEU A 180      -4.903  -0.749  -6.984  1.00169.97           C  
ANISOU  982  CA  LEU A 180    22716  23755  18110    702   1664     27       C  
ATOM    983  C   LEU A 180      -4.800  -0.038  -8.330  1.00169.47           C  
ANISOU  983  C   LEU A 180    22481  23538  18373    839   1617    -51       C  
ATOM    984  O   LEU A 180      -5.419   1.004  -8.556  1.00171.36           O  
ANISOU  984  O   LEU A 180    22523  23869  18717   1015   1833    -90       O  
ATOM    985  CB  LEU A 180      -5.974  -1.846  -7.058  1.00132.60           C  
ANISOU  985  CB  LEU A 180    17891  19282  13208    813   2019     37       C  
ATOM    986  CG  LEU A 180      -5.884  -2.960  -8.103  1.00132.24           C  
ANISOU  986  CG  LEU A 180    17484  19429  13333    742   2193    268       C  
ATOM    987  CD1 LEU A 180      -4.566  -3.710  -7.994  1.00133.48           C  
ANISOU  987  CD1 LEU A 180    17369  19664  13683    959   2420    196       C  
ATOM    988  CD2 LEU A 180      -7.059  -3.913  -7.954  1.00134.57           C  
ANISOU  988  CD2 LEU A 180    17848  19958  13326    633   2372    401       C  
ATOM    989  N   MET A 181      -3.988  -0.618  -9.209  1.00177.44           N  
ANISOU  989  N   MET A 181    23578  24322  19521    763   1336    -78       N  
ATOM    990  CA  MET A 181      -4.021  -0.306 -10.624  1.00176.10           C  
ANISOU  990  CA  MET A 181    23312  23970  19629    875   1242   -153       C  
ATOM    991  C   MET A 181      -5.415  -0.692 -11.090  1.00176.37           C  
ANISOU  991  C   MET A 181    23017  24123  19874   1014   1441   -101       C  
ATOM    992  O   MET A 181      -5.742  -1.877 -11.138  1.00175.52           O  
ANISOU  992  O   MET A 181    22668  24169  19854    902   1513     86       O  
ATOM    993  CB  MET A 181      -2.989  -1.153 -11.368  1.00140.74           C  
ANISOU  993  CB  MET A 181    18789  19339  15345    691    962    -37       C  
ATOM    994  CG  MET A 181      -1.570  -1.048 -10.829  1.00140.33           C  
ANISOU  994  CG  MET A 181    18990  19204  15126    515    743    -34       C  
ATOM    995  SD  MET A 181      -0.519  -2.410 -11.379  1.00140.19           S  
ANISOU  995  SD  MET A 181    18931  19390  14946    318    766    179       S  
ATOM    996  CE  MET A 181       1.067  -1.902 -10.715  1.00137.03           C  
ANISOU  996  CE  MET A 181    18187  18993  14885    220    719    399       C  
ATOM    997  N   SER A 182      -6.232   0.306 -11.419  1.00130.99           N  
ANISOU  997  N   SER A 182    17257  18292  14221   1250   1508   -257       N  
ATOM    998  CA  SER A 182      -7.648   0.097 -11.738  1.00132.35           C  
ANISOU  998  CA  SER A 182    17115  18608  14564   1419   1719   -227       C  
ATOM    999  C   SER A 182      -7.905  -0.978 -12.795  1.00130.15           C  
ANISOU  999  C   SER A 182    16523  18378  14552   1262   1632    -13       C  
ATOM   1000  O   SER A 182      -7.023  -1.311 -13.589  1.00127.99           O  
ANISOU 1000  O   SER A 182    16286  17952  14392   1110   1392     53       O  
ATOM   1001  CB  SER A 182      -8.299   1.416 -12.169  1.00142.02           C  
ANISOU 1001  CB  SER A 182    18378  19678  15906   1696   1727   -411       C  
ATOM   1002  OG  SER A 182      -7.700   1.927 -13.348  1.00146.38           O  
ANISOU 1002  OG  SER A 182    19226  20187  16207   1869   1843   -629       O  
ATOM   1003  N   ARG A 183      -9.123  -1.516 -12.786  1.00 88.26           N  
ANISOU 1003  N   ARG A 183    10909  13287   9338   1292   1832     93       N  
ATOM   1004  CA  ARG A 183      -9.534  -2.543 -13.740  1.00 86.29           C  
ANISOU 1004  CA  ARG A 183    10374  13092   9320   1121   1756    294       C  
ATOM   1005  C   ARG A 183      -9.350  -2.087 -15.183  1.00 85.74           C  
ANISOU 1005  C   ARG A 183    10250  12826   9500   1146   1527    279       C  
ATOM   1006  O   ARG A 183      -8.963  -2.875 -16.047  1.00 83.66           O  
ANISOU 1006  O   ARG A 183     9891  12515   9381    967   1369    410       O  
ATOM   1007  CB  ARG A 183     -10.994  -2.945 -13.509  1.00117.86           C  
ANISOU 1007  CB  ARG A 183    14036  17344  13402   1170   2003    389       C  
ATOM   1008  CG  ARG A 183     -11.195  -4.045 -12.480  1.00117.96           C  
ANISOU 1008  CG  ARG A 183    14075  17574  13171   1087   2232    462       C  
ATOM   1009  CD  ARG A 183     -12.659  -4.459 -12.411  1.00119.40           C  
ANISOU 1009  CD  ARG A 183    13917  18023  13427   1165   2511    539       C  
ATOM   1010  NE  ARG A 183     -12.846  -5.718 -11.692  1.00119.09           N  
ANISOU 1010  NE  ARG A 183    13779  18168  13304    934   2629    745       N  
ATOM   1011  CZ  ARG A 183     -14.015  -6.339 -11.564  1.00119.80           C  
ANISOU 1011  CZ  ARG A 183    13525  18478  13516    879   2810    895       C  
ATOM   1012  NH1 ARG A 183     -15.108  -5.820 -12.107  1.00120.76           N  
ANISOU 1012  NH1 ARG A 183    13347  18682  13855   1051   2888    859       N  
ATOM   1013  NH2 ARG A 183     -14.091  -7.481 -10.893  1.00119.67           N  
ANISOU 1013  NH2 ARG A 183    13458  18598  13412    646   2901   1092       N  
ATOM   1014  N   SER A 184      -9.632  -0.813 -15.436  1.00128.26           N  
ANISOU 1014  N   SER A 184    15720  18090  14925   1373   1512    118       N  
ATOM   1015  CA  SER A 184      -9.480  -0.242 -16.770  1.00127.79           C  
ANISOU 1015  CA  SER A 184    15661  17827  15067   1405   1288    102       C  
ATOM   1016  C   SER A 184      -8.021  -0.276 -17.216  1.00126.32           C  
ANISOU 1016  C   SER A 184    15719  17453  14826   1212   1050    118       C  
ATOM   1017  O   SER A 184      -7.714  -0.674 -18.341  1.00124.73           O  
ANISOU 1017  O   SER A 184    15439  17174  14780   1087    877    215       O  
ATOM   1018  CB  SER A 184     -10.012   1.192 -16.803  1.00102.60           C  
ANISOU 1018  CB  SER A 184    12557  14519  11906   1698   1322    -73       C  
ATOM   1019  OG  SER A 184      -9.299   2.023 -15.904  1.00103.98           O  
ANISOU 1019  OG  SER A 184    13079  14581  11848   1759   1341   -238       O  
ATOM   1020  N   ARG A 185      -7.125   0.139 -16.325  1.00 97.41           N  
ANISOU 1020  N   ARG A 185    12345  13729  10935   1183   1043     23       N  
ATOM   1021  CA  ARG A 185      -5.696   0.132 -16.617  1.00 95.90           C  
ANISOU 1021  CA  ARG A 185    12362  13386  10690    994    821     46       C  
ATOM   1022  C   ARG A 185      -5.172  -1.292 -16.781  1.00 93.09           C  
ANISOU 1022  C   ARG A 185    11884  13123  10361    759    768    232       C  
ATOM   1023  O   ARG A 185      -4.243  -1.537 -17.552  1.00 91.24           O  
ANISOU 1023  O   ARG A 185    11666  12781  10219    623    581    303       O  
ATOM   1024  CB  ARG A 185      -4.919   0.863 -15.519  1.00126.19           C  
ANISOU 1024  CB  ARG A 185    16523  17160  14264   1000    817    -91       C  
ATOM   1025  CG  ARG A 185      -5.224   2.351 -15.426  1.00127.32           C  
ANISOU 1025  CG  ARG A 185    16912  17046  14415   1072    655   -238       C  
ATOM   1026  CD  ARG A 185      -4.511   2.993 -14.247  1.00126.81           C  
ANISOU 1026  CD  ARG A 185    17166  16897  14118    950    543   -318       C  
ATOM   1027  NE  ARG A 185      -4.857   4.404 -14.101  1.00128.56           N  
ANISOU 1027  NE  ARG A 185    17593  17151  14102   1100    698   -496       N  
ATOM   1028  CZ  ARG A 185      -4.449   5.174 -13.097  1.00128.34           C  
ANISOU 1028  CZ  ARG A 185    17871  17063  13828   1019    618   -599       C  
ATOM   1029  NH1 ARG A 185      -3.677   4.668 -12.145  1.00130.00           N  
ANISOU 1029  NH1 ARG A 185    18280  17308  13805   1173    778   -776       N  
ATOM   1030  NH2 ARG A 185      -4.812   6.449 -13.044  1.00126.38           N  
ANISOU 1030  NH2 ARG A 185    17728  16728  13563    786    379   -526       N  
ATOM   1031  N   THR A 186      -5.775  -2.226 -16.052  1.00 64.20           N  
ANISOU 1031  N   THR A 186     8107   9663   6623    718    940    315       N  
ATOM   1032  CA  THR A 186      -5.408  -3.634 -16.157  1.00 61.37           C  
ANISOU 1032  CA  THR A 186     7646   9378   6295    509    900    495       C  
ATOM   1033  C   THR A 186      -5.798  -4.186 -17.523  1.00 60.08           C  
ANISOU 1033  C   THR A 186     7249   9187   6392    459    822    594       C  
ATOM   1034  O   THR A 186      -5.008  -4.874 -18.169  1.00 57.66           O  
ANISOU 1034  O   THR A 186     6944   8806   6158    311    675    685       O  
ATOM   1035  CB  THR A 186      -6.072  -4.479 -15.053  1.00 54.37           C  
ANISOU 1035  CB  THR A 186     6688   8703   5267    471   1110    578       C  
ATOM   1036  OG1 THR A 186      -5.604  -4.045 -13.769  1.00 55.42           O  
ANISOU 1036  OG1 THR A 186     7074   8863   5120    496   1161    491       O  
ATOM   1037  CG2 THR A 186      -5.739  -5.952 -15.235  1.00 51.32           C  
ANISOU 1037  CG2 THR A 186     6205   8356   4941    260   1054    775       C  
ATOM   1038  N   LYS A 187      -7.017  -3.879 -17.957  1.00 75.24           N  
ANISOU 1038  N   LYS A 187     8971  11171   8445    589    918    571       N  
ATOM   1039  CA  LYS A 187      -7.487  -4.286 -19.277  1.00 74.02           C  
ANISOU 1039  CA  LYS A 187     8605  10994   8526    549    826    650       C  
ATOM   1040  C   LYS A 187      -6.620  -3.664 -20.367  1.00 73.32           C  
ANISOU 1040  C   LYS A 187     8635  10705   8516    539    607    610       C  
ATOM   1041  O   LYS A 187      -6.293  -4.312 -21.366  1.00 70.99           O  
ANISOU 1041  O   LYS A 187     8272  10361   8338    418    483    694       O  
ATOM   1042  CB  LYS A 187      -8.952  -3.889 -19.476  1.00 86.11           C  
ANISOU 1042  CB  LYS A 187     9900  12638  10180    713    951    626       C  
ATOM   1043  CG  LYS A 187      -9.927  -4.612 -18.558  1.00 88.60           C  
ANISOU 1043  CG  LYS A 187    10011  13182  10471    676   1167    716       C  
ATOM   1044  CD  LYS A 187     -11.366  -4.209 -18.847  1.00 91.05           C  
ANISOU 1044  CD  LYS A 187    10041  13621  10932    840   1282    704       C  
ATOM   1045  CE  LYS A 187     -11.580  -2.717 -18.641  1.00 92.93           C  
ANISOU 1045  CE  LYS A 187    10382  13826  11100   1120   1372    531       C  
ATOM   1046  NZ  LYS A 187     -12.990  -2.312 -18.902  1.00 95.82           N  
ANISOU 1046  NZ  LYS A 187    10451  14331  11625   1315   1495    525       N  
ATOM   1047  N   LYS A 188      -6.250  -2.403 -20.163  1.00 56.94           N  
ANISOU 1047  N   LYS A 188     6752   8512   6371    664    566    480       N  
ATOM   1048  CA  LYS A 188      -5.356  -1.703 -21.077  1.00 56.37           C  
ANISOU 1048  CA  LYS A 188     6819   8247   6352    639    367    452       C  
ATOM   1049  C   LYS A 188      -4.006  -2.406 -21.150  1.00 53.46           C  
ANISOU 1049  C   LYS A 188     6548   7835   5929    436    253    530       C  
ATOM   1050  O   LYS A 188      -3.394  -2.484 -22.216  1.00 50.69           O  
ANISOU 1050  O   LYS A 188     6194   7394   5672    355    113    580       O  
ATOM   1051  CB  LYS A 188      -5.164  -0.250 -20.635  1.00 39.97           C  
ANISOU 1051  CB  LYS A 188     4963   6034   4189    785    347    300       C  
ATOM   1052  CG  LYS A 188      -6.348   0.661 -20.926  1.00 41.98           C  
ANISOU 1052  CG  LYS A 188     5137   6268   4546   1021    409    220       C  
ATOM   1053  CD  LYS A 188      -6.105   2.064 -20.390  1.00 44.06           C  
ANISOU 1053  CD  LYS A 188     5666   6354   4720   1165    379     60       C  
ATOM   1054  CE  LYS A 188      -7.202   3.028 -20.822  1.00 45.32           C  
ANISOU 1054  CE  LYS A 188     5754   6456   5012   1423    413    -11       C  
ATOM   1055  NZ  LYS A 188      -8.553   2.577 -20.390  1.00 46.34           N  
ANISOU 1055  NZ  LYS A 188     5642   6801   5165   1577    638    -16       N  
ATOM   1056  N   PHE A 189      -3.547  -2.918 -20.012  1.00 54.82           N  
ANISOU 1056  N   PHE A 189     6803   8082   5945    364    318    547       N  
ATOM   1057  CA  PHE A 189      -2.271  -3.621 -19.955  1.00 51.58           C  
ANISOU 1057  CA  PHE A 189     6468   7644   5485    193    212    632       C  
ATOM   1058  C   PHE A 189      -2.352  -4.979 -20.646  1.00 48.30           C  
ANISOU 1058  C   PHE A 189     5877   7280   5194     82    204    768       C  
ATOM   1059  O   PHE A 189      -1.394  -5.412 -21.287  1.00 44.34           O  
ANISOU 1059  O   PHE A 189     5391   6709   4746    -17     86    828       O  
ATOM   1060  CB  PHE A 189      -1.804  -3.787 -18.508  1.00 81.09           C  
ANISOU 1060  CB  PHE A 189    10349  11451   9011    151    265    623       C  
ATOM   1061  CG  PHE A 189      -0.423  -4.357 -18.381  1.00 77.22           C  
ANISOU 1061  CG  PHE A 189     9933  10932   8475     -5    133    713       C  
ATOM   1062  CD1 PHE A 189       0.672  -3.655 -18.853  1.00 75.82           C  
ANISOU 1062  CD1 PHE A 189     9865  10629   8316    -56    -35    685       C  
ATOM   1063  CD2 PHE A 189      -0.215  -5.589 -17.784  1.00 74.89           C  
ANISOU 1063  CD2 PHE A 189     9590  10737   8129    -99    174    838       C  
ATOM   1064  CE1 PHE A 189       1.947  -4.169 -18.738  1.00 72.24           C  
ANISOU 1064  CE1 PHE A 189     9442  10169   7837   -188   -153    777       C  
ATOM   1065  CE2 PHE A 189       1.060  -6.109 -17.667  1.00 71.63           C  
ANISOU 1065  CE2 PHE A 189     9229  10297   7691   -217     46    928       C  
ATOM   1066  CZ  PHE A 189       2.142  -5.398 -18.145  1.00 70.34           C  
ANISOU 1066  CZ  PHE A 189     9146  10029   7553   -255   -114    896       C  
ATOM   1067  N   ILE A 190      -3.496  -5.644 -20.514  1.00 52.32           N  
ANISOU 1067  N   ILE A 190     6221   7908   5750     98    335    815       N  
ATOM   1068  CA  ILE A 190      -3.734  -6.908 -21.202  1.00 49.57           C  
ANISOU 1068  CA  ILE A 190     5718   7587   5530    -11    323    933       C  
ATOM   1069  C   ILE A 190      -3.699  -6.686 -22.708  1.00 48.18           C  
ANISOU 1069  C   ILE A 190     5483   7315   5510     -7    198    920       C  
ATOM   1070  O   ILE A 190      -3.051  -7.434 -23.449  1.00 44.49           O  
ANISOU 1070  O   ILE A 190     5010   6789   5106   -107    110    981       O  
ATOM   1071  CB  ILE A 190      -5.097  -7.515 -20.819  1.00 67.07           C  
ANISOU 1071  CB  ILE A 190     7750   9949   7782     -6    480    985       C  
ATOM   1072  CG1 ILE A 190      -5.145  -7.825 -19.323  1.00 67.62           C  
ANISOU 1072  CG1 ILE A 190     7887  10133   7672    -23    622   1015       C  
ATOM   1073  CG2 ILE A 190      -5.364  -8.778 -21.623  1.00 64.31           C  
ANISOU 1073  CG2 ILE A 190     7260   9597   7578   -140    439   1097       C  
ATOM   1074  CD1 ILE A 190      -4.140  -8.857 -18.882  1.00 64.47           C  
ANISOU 1074  CD1 ILE A 190     7584   9708   7203   -168    567   1127       C  
ATOM   1075  N   SER A 191      -4.399  -5.645 -23.150  1.00 42.82           N  
ANISOU 1075  N   SER A 191     4770   6617   4882    122    193    839       N  
ATOM   1076  CA  SER A 191      -4.413  -5.269 -24.559  1.00 40.89           C  
ANISOU 1076  CA  SER A 191     4490   6287   4761    137     66    831       C  
ATOM   1077  C   SER A 191      -2.999  -4.968 -25.047  1.00 37.80           C  
ANISOU 1077  C   SER A 191     4261   5769   4332     75    -63    827       C  
ATOM   1078  O   SER A 191      -2.602  -5.392 -26.134  1.00 34.28           O  
ANISOU 1078  O   SER A 191     3795   5274   3955      7   -153    868       O  
ATOM   1079  CB  SER A 191      -5.320  -4.058 -24.777  1.00 53.22           C  
ANISOU 1079  CB  SER A 191     6012   7838   6371    310     75    752       C  
ATOM   1080  OG  SER A 191      -6.636  -4.320 -24.320  1.00 54.99           O  
ANISOU 1080  OG  SER A 191     6043   8205   6645    376    206    765       O  
ATOM   1081  N   ALA A 192      -2.243  -4.243 -24.228  1.00 38.25           N  
ANISOU 1081  N   ALA A 192     4478   5781   4273     92    -68    778       N  
ATOM   1082  CA  ALA A 192      -0.857  -3.916 -24.544  1.00 34.69           C  
ANISOU 1082  CA  ALA A 192     4160   5230   3788     15   -186    787       C  
ATOM   1083  C   ALA A 192      -0.019  -5.180 -24.717  1.00 30.93           C  
ANISOU 1083  C   ALA A 192     3646   4782   3321   -113   -205    883       C  
ATOM   1084  O   ALA A 192       0.809  -5.266 -25.625  1.00 27.70           O  
ANISOU 1084  O   ALA A 192     3255   4316   2953   -172   -289    917       O  
ATOM   1085  CB  ALA A 192      -0.263  -3.024 -23.463  1.00 20.91           C  
ANISOU 1085  CB  ALA A 192     2590   3441   1913     35   -199    717       C  
ATOM   1086  N   ILE A 193      -0.243  -6.156 -23.842  1.00 48.80           N  
ANISOU 1086  N   ILE A 193     5862   7133   5548   -147   -120    931       N  
ATOM   1087  CA  ILE A 193       0.459  -7.433 -23.910  1.00 45.64           C  
ANISOU 1087  CA  ILE A 193     5430   6743   5170   -245   -134   1027       C  
ATOM   1088  C   ILE A 193       0.132  -8.170 -25.206  1.00 43.91           C  
ANISOU 1088  C   ILE A 193     5112   6492   5079   -274   -159   1056       C  
ATOM   1089  O   ILE A 193       1.032  -8.642 -25.903  1.00 41.10           O  
ANISOU 1089  O   ILE A 193     4774   6085   4758   -321   -217   1090       O  
ATOM   1090  CB  ILE A 193       0.115  -8.334 -22.706  1.00 43.27           C  
ANISOU 1090  CB  ILE A 193     5107   6530   4803   -278    -38   1089       C  
ATOM   1091  CG1 ILE A 193       0.752  -7.780 -21.431  1.00 44.39           C  
ANISOU 1091  CG1 ILE A 193     5381   6703   4782   -273    -39   1071       C  
ATOM   1092  CG2 ILE A 193       0.588  -9.760 -22.948  1.00 40.42           C  
ANISOU 1092  CG2 ILE A 193     4704   6150   4504   -363    -54   1195       C  
ATOM   1093  CD1 ILE A 193       0.490  -8.622 -20.202  1.00 45.17           C  
ANISOU 1093  CD1 ILE A 193     5484   6897   4781   -311     53   1146       C  
ATOM   1094  N   TRP A 194      -1.156  -8.258 -25.525  1.00 51.79           N  
ANISOU 1094  N   TRP A 194     6006   7529   6143   -244   -116   1039       N  
ATOM   1095  CA  TRP A 194      -1.597  -8.915 -26.753  1.00 50.35           C  
ANISOU 1095  CA  TRP A 194     5742   7319   6070   -283   -160   1055       C  
ATOM   1096  C   TRP A 194      -0.992  -8.274 -28.000  1.00 48.19           C  
ANISOU 1096  C   TRP A 194     5528   6968   5814   -266   -262   1019       C  
ATOM   1097  O   TRP A 194      -0.469  -8.965 -28.880  1.00 45.94           O  
ANISOU 1097  O   TRP A 194     5255   6639   5562   -319   -307   1038       O  
ATOM   1098  CB  TRP A 194      -3.124  -8.899 -26.852  1.00 57.66           C  
ANISOU 1098  CB  TRP A 194     6524   8316   7067   -258   -118   1047       C  
ATOM   1099  CG  TRP A 194      -3.781 -10.047 -26.148  1.00 58.15           C  
ANISOU 1099  CG  TRP A 194     6493   8443   7157   -341    -35   1119       C  
ATOM   1100  CD1 TRP A 194      -4.477 -10.005 -24.973  1.00 60.74           C  
ANISOU 1100  CD1 TRP A 194     6760   8876   7441   -326     89   1147       C  
ATOM   1101  CD2 TRP A 194      -3.801 -11.414 -26.577  1.00 56.23           C  
ANISOU 1101  CD2 TRP A 194     6222   8155   6987   -459    -66   1179       C  
ATOM   1102  NE1 TRP A 194      -4.930 -11.261 -24.646  1.00 60.14           N  
ANISOU 1102  NE1 TRP A 194     6610   8830   7412   -444    135   1239       N  
ATOM   1103  CE2 TRP A 194      -4.528 -12.143 -25.613  1.00 57.54           C  
ANISOU 1103  CE2 TRP A 194     6307   8394   7162   -527     33   1256       C  
ATOM   1104  CE3 TRP A 194      -3.275 -12.090 -27.682  1.00 53.92           C  
ANISOU 1104  CE3 TRP A 194     5982   7761   6745   -513   -162   1170       C  
ATOM   1105  CZ2 TRP A 194      -4.743 -13.515 -25.724  1.00 56.56           C  
ANISOU 1105  CZ2 TRP A 194     6158   8222   7111   -659     21   1331       C  
ATOM   1106  CZ3 TRP A 194      -3.488 -13.452 -27.788  1.00 53.39           C  
ANISOU 1106  CZ3 TRP A 194     5899   7643   6742   -624   -169   1222       C  
ATOM   1107  CH2 TRP A 194      -4.216 -14.150 -26.814  1.00 54.66           C  
ANISOU 1107  CH2 TRP A 194     5985   7856   6927   -703    -87   1306       C  
ATOM   1108  N   LEU A 195      -1.064  -6.949 -28.064  1.00 41.77           N  
ANISOU 1108  N   LEU A 195     4766   6134   4970   -190   -293    968       N  
ATOM   1109  CA  LEU A 195      -0.545  -6.209 -29.209  1.00 39.81           C  
ANISOU 1109  CA  LEU A 195     4586   5812   4726   -182   -387    953       C  
ATOM   1110  C   LEU A 195       0.968  -6.350 -29.341  1.00 37.08           C  
ANISOU 1110  C   LEU A 195     4325   5428   4335   -249   -414    986       C  
ATOM   1111  O   LEU A 195       1.490  -6.516 -30.446  1.00 35.01           O  
ANISOU 1111  O   LEU A 195     4081   5136   4084   -283   -458   1003       O  
ATOM   1112  CB  LEU A 195      -0.944  -4.738 -29.112  1.00 64.03           C  
ANISOU 1112  CB  LEU A 195     7708   8841   7781    -85   -418    901       C  
ATOM   1113  CG  LEU A 195      -2.451  -4.504 -29.215  1.00 66.87           C  
ANISOU 1113  CG  LEU A 195     7955   9244   8211     10   -404    875       C  
ATOM   1114  CD1 LEU A 195      -2.829  -3.152 -28.644  1.00 69.51           C  
ANISOU 1114  CD1 LEU A 195     8353   9531   8529    141   -402    813       C  
ATOM   1115  CD2 LEU A 195      -2.913  -4.626 -30.659  1.00 65.05           C  
ANISOU 1115  CD2 LEU A 195     7670   9001   8046     -9   -498    901       C  
ATOM   1116  N   ALA A 196       1.666  -6.293 -28.211  1.00 33.01           N  
ANISOU 1116  N   ALA A 196     3853   4927   3761   -268   -387    999       N  
ATOM   1117  CA  ALA A 196       3.110  -6.494 -28.198  1.00 30.87           C  
ANISOU 1117  CA  ALA A 196     3623   4644   3464   -331   -416   1046       C  
ATOM   1118  C   ALA A 196       3.449  -7.895 -28.696  1.00 29.40           C  
ANISOU 1118  C   ALA A 196     3377   4470   3325   -363   -386   1094       C  
ATOM   1119  O   ALA A 196       4.450  -8.100 -29.387  1.00 27.84           O  
ANISOU 1119  O   ALA A 196     3183   4259   3136   -388   -403   1124       O  
ATOM   1120  CB  ALA A 196       3.666  -6.276 -26.800  1.00 16.40           C  
ANISOU 1120  CB  ALA A 196     1841   2834   1555   -349   -416   1055       C  
ATOM   1121  N   SER A 197       2.599  -8.854 -28.343  1.00 47.04           N  
ANISOU 1121  N   SER A 197     5555   6725   5591   -361   -336   1101       N  
ATOM   1122  CA  SER A 197       2.773 -10.236 -28.771  1.00 46.21           C  
ANISOU 1122  CA  SER A 197     5420   6598   5540   -391   -315   1137       C  
ATOM   1123  C   SER A 197       2.614 -10.355 -30.281  1.00 45.50           C  
ANISOU 1123  C   SER A 197     5334   6468   5486   -393   -347   1097       C  
ATOM   1124  O   SER A 197       3.381 -11.059 -30.942  1.00 44.81           O  
ANISOU 1124  O   SER A 197     5267   6344   5413   -400   -342   1105       O  
ATOM   1125  CB  SER A 197       1.764 -11.141 -28.067  1.00 35.79           C  
ANISOU 1125  CB  SER A 197     4050   5299   4250   -415   -263   1163       C  
ATOM   1126  OG  SER A 197       1.822 -10.955 -26.666  1.00 36.51           O  
ANISOU 1126  OG  SER A 197     4156   5442   4276   -412   -226   1199       O  
ATOM   1127  N   ALA A 198       1.614  -9.665 -30.820  1.00 39.54           N  
ANISOU 1127  N   ALA A 198     4564   5722   4736   -376   -382   1054       N  
ATOM   1128  CA  ALA A 198       1.399  -9.646 -32.263  1.00 39.00           C  
ANISOU 1128  CA  ALA A 198     4516   5628   4674   -383   -436   1021       C  
ATOM   1129  C   ALA A 198       2.605  -9.039 -32.977  1.00 37.65           C  
ANISOU 1129  C   ALA A 198     4417   5440   4446   -379   -453   1029       C  
ATOM   1130  O   ALA A 198       3.088  -9.579 -33.978  1.00 37.46           O  
ANISOU 1130  O   ALA A 198     4432   5399   4402   -393   -458   1017       O  
ATOM   1131  CB  ALA A 198       0.132  -8.874 -32.601  1.00 16.27           C  
ANISOU 1131  CB  ALA A 198     1593   2770   1817   -353   -488    994       C  
ATOM   1132  N   LEU A 199       3.086  -7.917 -32.447  1.00 26.51           N  
ANISOU 1132  N   LEU A 199     3031   4038   3004   -368   -460   1050       N  
ATOM   1133  CA  LEU A 199       4.253  -7.239 -33.003  1.00 25.58           C  
ANISOU 1133  CA  LEU A 199     2964   3915   2842   -391   -474   1080       C  
ATOM   1134  C   LEU A 199       5.473  -8.152 -33.009  1.00 25.23           C  
ANISOU 1134  C   LEU A 199     2893   3892   2800   -406   -417   1116       C  
ATOM   1135  O   LEU A 199       6.219  -8.199 -33.987  1.00 25.22           O  
ANISOU 1135  O   LEU A 199     2909   3904   2770   -417   -396   1132       O  
ATOM   1136  CB  LEU A 199       4.566  -5.971 -32.210  1.00 39.74           C  
ANISOU 1136  CB  LEU A 199     4796   5694   4611   -400   -511   1094       C  
ATOM   1137  CG  LEU A 199       3.524  -4.854 -32.251  1.00 40.81           C  
ANISOU 1137  CG  LEU A 199     4977   5783   4744   -357   -569   1057       C  
ATOM   1138  CD1 LEU A 199       3.915  -3.737 -31.297  1.00 41.69           C  
ANISOU 1138  CD1 LEU A 199     5160   5851   4828   -365   -605   1054       C  
ATOM   1139  CD2 LEU A 199       3.351  -4.328 -33.667  1.00 40.47           C  
ANISOU 1139  CD2 LEU A 199     4979   5714   4685   -361   -622   1071       C  
ATOM   1140  N   LEU A 200       5.675  -8.872 -31.911  1.00 29.21           N  
ANISOU 1140  N   LEU A 200     3355   4407   3338   -398   -385   1137       N  
ATOM   1141  CA  LEU A 200       6.793  -9.802 -31.812  1.00 29.38           C  
ANISOU 1141  CA  LEU A 200     3339   4443   3382   -386   -339   1182       C  
ATOM   1142  C   LEU A 200       6.576 -11.032 -32.691  1.00 30.22           C  
ANISOU 1142  C   LEU A 200     3459   4508   3515   -353   -293   1147       C  
ATOM   1143  O   LEU A 200       7.521 -11.759 -32.997  1.00 31.09           O  
ANISOU 1143  O   LEU A 200     3550   4619   3645   -314   -242   1168       O  
ATOM   1144  CB  LEU A 200       7.020 -10.217 -30.357  1.00 24.40           C  
ANISOU 1144  CB  LEU A 200     2674   3827   2768   -385   -340   1231       C  
ATOM   1145  CG  LEU A 200       7.542  -9.119 -29.424  1.00 24.40           C  
ANISOU 1145  CG  LEU A 200     2680   3867   2723   -424   -393   1262       C  
ATOM   1146  CD1 LEU A 200       7.520  -9.583 -27.973  1.00 25.08           C  
ANISOU 1146  CD1 LEU A 200     2762   3973   2793   -425   -401   1299       C  
ATOM   1147  CD2 LEU A 200       8.947  -8.690 -29.829  1.00 24.37           C  
ANISOU 1147  CD2 LEU A 200     2633   3905   2722   -452   -409   1319       C  
ATOM   1148  N   ALA A 201       5.329 -11.254 -33.099  1.00 35.42           N  
ANISOU 1148  N   ALA A 201     4150   5129   4178   -366   -317   1090       N  
ATOM   1149  CA  ALA A 201       4.994 -12.394 -33.948  1.00 36.81           C  
ANISOU 1149  CA  ALA A 201     4370   5245   4371   -357   -298   1039       C  
ATOM   1150  C   ALA A 201       5.035 -12.035 -35.430  1.00 37.39           C  
ANISOU 1150  C   ALA A 201     4509   5327   4370   -357   -309    988       C  
ATOM   1151  O   ALA A 201       4.961 -12.913 -36.291  1.00 39.18           O  
ANISOU 1151  O   ALA A 201     4802   5504   4579   -350   -298    927       O  
ATOM   1152  CB  ALA A 201       3.631 -12.949 -33.579  1.00 58.98           C  
ANISOU 1152  CB  ALA A 201     7168   8013   7229   -398   -334   1016       C  
ATOM   1153  N   ILE A 202       5.148 -10.741 -35.713  1.00 33.06           N  
ANISOU 1153  N   ILE A 202     3962   4831   3768   -372   -335   1015       N  
ATOM   1154  CA  ILE A 202       5.249 -10.235 -37.088  1.00 33.56           C  
ANISOU 1154  CA  ILE A 202     4097   4914   3739   -384   -349    993       C  
ATOM   1155  C   ILE A 202       6.225 -10.960 -38.045  1.00 35.42           C  
ANISOU 1155  C   ILE A 202     4382   5161   3914   -350   -259    968       C  
ATOM   1156  O   ILE A 202       5.842 -11.277 -39.172  1.00 36.92           O  
ANISOU 1156  O   ILE A 202     4666   5339   4023   -356   -272    907       O  
ATOM   1157  CB  ILE A 202       5.510  -8.703 -37.111  1.00 31.67           C  
ANISOU 1157  CB  ILE A 202     3860   4711   3461   -413   -390   1053       C  
ATOM   1158  CG1 ILE A 202       4.270  -7.947 -36.631  1.00 30.99           C  
ANISOU 1158  CG1 ILE A 202     3767   4598   3410   -416   -484   1043       C  
ATOM   1159  CG2 ILE A 202       5.906  -8.233 -38.504  1.00 32.40           C  
ANISOU 1159  CG2 ILE A 202     4032   4834   3444   -433   -383   1064       C  
ATOM   1160  CD1 ILE A 202       4.412  -6.442 -36.696  1.00 30.40           C  
ANISOU 1160  CD1 ILE A 202     3724   4516   3308   -432   -537   1091       C  
ATOM   1161  N   PRO A 203       7.475 -11.229 -37.609  1.00 36.07           N  
ANISOU 1161  N   PRO A 203     4400   5276   4030   -307   -167   1012       N  
ATOM   1162  CA  PRO A 203       8.445 -11.853 -38.523  1.00 38.57           C  
ANISOU 1162  CA  PRO A 203     4747   5618   4292   -246    -55    983       C  
ATOM   1163  C   PRO A 203       7.986 -13.157 -39.182  1.00 41.28           C  
ANISOU 1163  C   PRO A 203     5199   5872   4616   -203    -39    871       C  
ATOM   1164  O   PRO A 203       8.512 -13.513 -40.235  1.00 43.81           O  
ANISOU 1164  O   PRO A 203     5605   6208   4836   -163     34    812       O  
ATOM   1165  CB  PRO A 203       9.645 -12.131 -37.615  1.00 23.26           C  
ANISOU 1165  CB  PRO A 203     2683   3713   2442   -190     16   1054       C  
ATOM   1166  CG  PRO A 203       9.568 -11.082 -36.589  1.00 22.99           C  
ANISOU 1166  CG  PRO A 203     2573   3713   2448   -261    -63   1136       C  
ATOM   1167  CD  PRO A 203       8.104 -10.891 -36.318  1.00 22.38           C  
ANISOU 1167  CD  PRO A 203     2560   3573   2371   -309   -165   1092       C  
ATOM   1168  N   MET A 204       7.030 -13.855 -38.577  1.00 35.57           N  
ANISOU 1168  N   MET A 204     4483   5054   3978   -219   -105    841       N  
ATOM   1169  CA  MET A 204       6.532 -15.105 -39.143  1.00 38.63           C  
ANISOU 1169  CA  MET A 204     4985   5328   4364   -204   -114    737       C  
ATOM   1170  C   MET A 204       5.689 -14.877 -40.396  1.00 39.64           C  
ANISOU 1170  C   MET A 204     5235   5454   4372   -267   -189    655       C  
ATOM   1171  O   MET A 204       5.525 -15.781 -41.214  1.00 43.01           O  
ANISOU 1171  O   MET A 204     5796   5801   4744   -256   -187    549       O  
ATOM   1172  CB  MET A 204       5.742 -15.898 -38.100  1.00 45.68           C  
ANISOU 1172  CB  MET A 204     5847   6126   5383   -241   -175    752       C  
ATOM   1173  CG  MET A 204       6.621 -16.510 -37.031  1.00 45.88           C  
ANISOU 1173  CG  MET A 204     5801   6120   5510   -166   -107    820       C  
ATOM   1174  SD  MET A 204       7.926 -17.522 -37.757  1.00 50.63           S  
ANISOU 1174  SD  MET A 204     6473   6663   6101    -15     23    759       S  
ATOM   1175  CE  MET A 204       9.064 -17.650 -36.381  1.00 49.92           C  
ANISOU 1175  CE  MET A 204     6236   6590   6139     71     66    892       C  
ATOM   1176  N   LEU A 205       5.162 -13.666 -40.544  1.00 40.52           N  
ANISOU 1176  N   LEU A 205     5313   5644   4439   -329   -267    705       N  
ATOM   1177  CA  LEU A 205       4.365 -13.315 -41.715  1.00 41.21           C  
ANISOU 1177  CA  LEU A 205     5505   5747   4405   -385   -360    655       C  
ATOM   1178  C   LEU A 205       5.240 -13.185 -42.956  1.00 43.05           C  
ANISOU 1178  C   LEU A 205     5847   6038   4470   -346   -268    626       C  
ATOM   1179  O   LEU A 205       4.750 -13.243 -44.083  1.00 44.66           O  
ANISOU 1179  O   LEU A 205     6189   6244   4536   -380   -325    560       O  
ATOM   1180  CB  LEU A 205       3.606 -12.008 -41.473  1.00 21.66           C  
ANISOU 1180  CB  LEU A 205     2959   3328   1944   -436   -469    732       C  
ATOM   1181  CG  LEU A 205       2.512 -12.036 -40.404  1.00 21.03           C  
ANISOU 1181  CG  LEU A 205     2773   3216   2001   -472   -557    751       C  
ATOM   1182  CD1 LEU A 205       1.917 -10.652 -40.212  1.00 21.72           C  
ANISOU 1182  CD1 LEU A 205     2797   3357   2099   -481   -642    818       C  
ATOM   1183  CD2 LEU A 205       1.431 -13.038 -40.781  1.00 21.70           C  
ANISOU 1183  CD2 LEU A 205     2908   3238   2101   -533   -650    671       C  
ATOM   1184  N   PHE A 206       6.541 -13.013 -42.740  1.00 33.95           N  
ANISOU 1184  N   PHE A 206     4628   4946   3324   -281   -126    683       N  
ATOM   1185  CA  PHE A 206       7.487 -12.830 -43.834  1.00 35.67           C  
ANISOU 1185  CA  PHE A 206     4915   5250   3386   -243     -3    677       C  
ATOM   1186  C   PHE A 206       8.477 -13.988 -43.933  1.00 39.12           C  
ANISOU 1186  C   PHE A 206     5370   5663   3831   -122    161    606       C  
ATOM   1187  O   PHE A 206       9.124 -14.173 -44.963  1.00 41.60           O  
ANISOU 1187  O   PHE A 206     5774   6033   3997    -68    282    555       O  
ATOM   1188  CB  PHE A 206       8.246 -11.510 -43.665  1.00 44.95           C  
ANISOU 1188  CB  PHE A 206     5985   6540   4554   -277     35    817       C  
ATOM   1189  CG  PHE A 206       7.355 -10.300 -43.602  1.00 42.31           C  
ANISOU 1189  CG  PHE A 206     5662   6208   4203   -372   -118    884       C  
ATOM   1190  CD1 PHE A 206       6.978  -9.642 -44.761  1.00 42.69           C  
ANISOU 1190  CD1 PHE A 206     5834   6300   4085   -422   -165    898       C  
ATOM   1191  CD2 PHE A 206       6.900  -9.817 -42.385  1.00 39.79           C  
ANISOU 1191  CD2 PHE A 206     5241   5848   4029   -398   -212    933       C  
ATOM   1192  CE1 PHE A 206       6.161  -8.530 -44.709  1.00 40.75           C  
ANISOU 1192  CE1 PHE A 206     5602   6041   3839   -486   -316    968       C  
ATOM   1193  CE2 PHE A 206       6.081  -8.704 -42.328  1.00 38.03           C  
ANISOU 1193  CE2 PHE A 206     5032   5615   3802   -454   -344    985       C  
ATOM   1194  CZ  PHE A 206       5.711  -8.060 -43.492  1.00 38.57           C  
ANISOU 1194  CZ  PHE A 206     5215   5712   3726   -493   -401   1007       C  
ATOM   1195  N   THR A 207       8.593 -14.763 -42.857  1.00 41.61           N  
ANISOU 1195  N   THR A 207     5601   5894   4313    -69    169    606       N  
ATOM   1196  CA  THR A 207       9.521 -15.889 -42.815  1.00 45.22           C  
ANISOU 1196  CA  THR A 207     6062   6305   4813     73    312    551       C  
ATOM   1197  C   THR A 207       8.939 -17.114 -43.513  1.00 49.06           C  
ANISOU 1197  C   THR A 207     6750   6637   5251    105    291    386       C  
ATOM   1198  O   THR A 207       9.646 -17.837 -44.215  1.00 52.45           O  
ANISOU 1198  O   THR A 207     7275   7039   5612    229    426    290       O  
ATOM   1199  CB  THR A 207       9.886 -16.267 -41.366  1.00 45.44           C  
ANISOU 1199  CB  THR A 207     5930   6296   5040    119    313    639       C  
ATOM   1200  OG1 THR A 207      10.384 -15.111 -40.680  1.00 41.84           O  
ANISOU 1200  OG1 THR A 207     5311   5965   4622     57    291    780       O  
ATOM   1201  CG2 THR A 207      10.947 -17.361 -41.346  1.00 48.93           C  
ANISOU 1201  CG2 THR A 207     6343   6712   5537    293    467    614       C  
ATOM   1202  N   MET A 208       7.644 -17.338 -43.323  1.00 52.21           N  
ANISOU 1202  N   MET A 208     7214   6937   5686     -8    123    351       N  
ATOM   1203  CA  MET A 208       6.995 -18.533 -43.848  1.00 55.76           C  
ANISOU 1203  CA  MET A 208     7853   7218   6116    -19     63    203       C  
ATOM   1204  C   MET A 208       6.205 -18.245 -45.123  1.00 56.19           C  
ANISOU 1204  C   MET A 208     8080   7295   5976   -111    -31    108       C  
ATOM   1205  O   MET A 208       5.819 -17.104 -45.385  1.00 53.24           O  
ANISOU 1205  O   MET A 208     7654   7039   5536   -201   -116    182       O  
ATOM   1206  CB  MET A 208       6.077 -19.142 -42.787  1.00 29.68           C  
ANISOU 1206  CB  MET A 208     4498   3789   2989   -105    -68    237       C  
ATOM   1207  CG  MET A 208       6.748 -19.352 -41.439  1.00 29.12           C  
ANISOU 1207  CG  MET A 208     4278   3693   3092    -25      2    342       C  
ATOM   1208  SD  MET A 208       8.124 -20.516 -41.510  1.00 34.12           S  
ANISOU 1208  SD  MET A 208     4991   4218   3756    185    173    270       S  
ATOM   1209  CE  MET A 208       7.259 -22.031 -41.916  1.00 36.19           C  
ANISOU 1209  CE  MET A 208     5510   4219   4019    134     76    102       C  
ATOM   1210  N   GLY A 209       5.968 -19.290 -45.912  1.00 45.09           N  
ANISOU 1210  N   GLY A 209     6893   5766   4473    -84    -28    -57       N  
ATOM   1211  CA  GLY A 209       5.198 -19.160 -47.135  1.00 45.44           C  
ANISOU 1211  CA  GLY A 209     7129   5825   4313   -180   -140   -159       C  
ATOM   1212  C   GLY A 209       5.072 -20.467 -47.892  1.00 48.89           C  
ANISOU 1212  C   GLY A 209     7832   6083   4663   -157   -152   -362       C  
ATOM   1213  O   GLY A 209       5.423 -21.531 -47.381  1.00 51.10           O  
ANISOU 1213  O   GLY A 209     8149   6202   5066    -63    -77   -422       O  
ATOM   1214  N   LEU A 210       4.571 -20.388 -49.120  1.00 48.30           N  
ANISOU 1214  N   LEU A 210     7959   6024   4371   -244   -258   -470       N  
ATOM   1215  CA  LEU A 210       4.366 -21.576 -49.939  1.00 51.41           C  
ANISOU 1215  CA  LEU A 210     8649   6240   4646   -242   -293   -686       C  
ATOM   1216  C   LEU A 210       5.497 -21.792 -50.937  1.00 53.54           C  
ANISOU 1216  C   LEU A 210     9101   6556   4686    -66    -66   -812       C  
ATOM   1217  O   LEU A 210       5.955 -20.849 -51.584  1.00 52.42           O  
ANISOU 1217  O   LEU A 210     8936   6620   4363    -41     25   -751       O  
ATOM   1218  CB  LEU A 210       3.036 -21.485 -50.689  1.00 44.59           C  
ANISOU 1218  CB  LEU A 210     7921   5361   3660   -449   -563   -746       C  
ATOM   1219  CG  LEU A 210       1.773 -21.343 -49.839  1.00 42.97           C  
ANISOU 1219  CG  LEU A 210     7538   5115   3676   -630   -791   -639       C  
ATOM   1220  CD1 LEU A 210       0.535 -21.457 -50.711  1.00 43.10           C  
ANISOU 1220  CD1 LEU A 210     7705   5101   3570   -826  -1062   -724       C  
ATOM   1221  CD2 LEU A 210       1.753 -22.384 -48.728  1.00 44.47           C  
ANISOU 1221  CD2 LEU A 210     7672   5107   4120   -612   -760   -640       C  
ATOM   1222  N   GLN A 211       5.941 -23.040 -51.057  1.00 33.44           N  
ANISOU 1222  N   GLN A 211     6740   3816   2148     61     33   -983       N  
ATOM   1223  CA  GLN A 211       6.942 -23.405 -52.056  1.00 37.44           C  
ANISOU 1223  CA  GLN A 211     7451   4352   2424    246    260  -1139       C  
ATOM   1224  C   GLN A 211       6.634 -24.760 -52.679  1.00 41.90           C  
ANISOU 1224  C   GLN A 211     8372   4654   2894    267    207  -1402       C  
ATOM   1225  O   GLN A 211       6.163 -25.670 -52.000  1.00 41.38           O  
ANISOU 1225  O   GLN A 211     8350   4349   3024    198     63  -1442       O  
ATOM   1226  CB  GLN A 211       8.348 -23.420 -51.451  1.00 71.81           C  
ANISOU 1226  CB  GLN A 211    11609   8769   6907    487    545  -1061       C  
ATOM   1227  CG  GLN A 211       8.963 -22.045 -51.258  1.00 69.24           C  
ANISOU 1227  CG  GLN A 211    10990   8726   6595    484    644   -836       C  
ATOM   1228  CD  GLN A 211      10.444 -22.117 -50.943  1.00 70.27           C  
ANISOU 1228  CD  GLN A 211    10967   8958   6776    723    944   -792       C  
ATOM   1229  OE1 GLN A 211      11.139 -21.100 -50.929  1.00 68.97           O  
ANISOU 1229  OE1 GLN A 211    10645   9034   6527    741   1082   -665       O  
ATOM   1230  NE2 GLN A 211      10.937 -23.325 -50.692  1.00 72.62           N  
ANISOU 1230  NE2 GLN A 211    11302   9069   7222    904   1040   -886       N  
ATOM   1231  N   ASN A 212       6.896 -24.886 -53.975  1.00 46.81           N  
ANISOU 1231  N   ASN A 212     9264   5315   3205    355    325  -1582       N  
ATOM   1232  CA  ASN A 212       6.704 -26.154 -54.666  1.00 52.00           C  
ANISOU 1232  CA  ASN A 212    10313   5718   3729    373    270  -1862       C  
ATOM   1233  C   ASN A 212       7.999 -26.958 -54.686  1.00 55.00           C  
ANISOU 1233  C   ASN A 212    10801   6005   4092    692    586  -2008       C  
ATOM   1234  O   ASN A 212       8.847 -26.762 -55.556  1.00 57.40           O  
ANISOU 1234  O   ASN A 212    11125   6505   4179    860    842  -2040       O  
ATOM   1235  CB  ASN A 212       6.202 -25.923 -56.093  1.00 56.59           C  
ANISOU 1235  CB  ASN A 212    11176   6386   3938    226    135  -1991       C  
ATOM   1236  CG  ASN A 212       5.510 -27.143 -56.671  1.00 61.83           C  
ANISOU 1236  CG  ASN A 212    12249   6760   4484    154    -31  -2271       C  
ATOM   1237  OD1 ASN A 212       6.153 -28.144 -56.985  1.00 62.85           O  
ANISOU 1237  OD1 ASN A 212    12474   6823   4582   -108   -351  -2292       O  
ATOM   1238  ND2 ASN A 212       4.193 -27.062 -56.822  1.00 65.72           N  
ANISOU 1238  ND2 ASN A 212    12982   7073   4915    385    179  -2489       N  
ATOM   1239  N   LEU A 213       8.148 -27.861 -53.722  1.00 56.38           N  
ANISOU 1239  N   LEU A 213    11037   5883   4503    781    573  -2085       N  
ATOM   1240  CA  LEU A 213       9.389 -28.612 -53.561  1.00 59.41           C  
ANISOU 1240  CA  LEU A 213    11489   6152   4932   1114    861  -2204       C  
ATOM   1241  C   LEU A 213       9.407 -29.914 -54.358  1.00 65.89           C  
ANISOU 1241  C   LEU A 213    12767   6634   5632   1187    832  -2526       C  
ATOM   1242  O   LEU A 213      10.221 -30.799 -54.095  1.00 68.11           O  
ANISOU 1242  O   LEU A 213    13127   6670   6081   1411    951  -2617       O  
ATOM   1243  CB  LEU A 213       9.657 -28.897 -52.082  1.00 56.88           C  
ANISOU 1243  CB  LEU A 213    10861   5751   5002   1217    902  -2013       C  
ATOM   1244  CG  LEU A 213       9.859 -27.671 -51.189  1.00 50.62           C  
ANISOU 1244  CG  LEU A 213     9625   5240   4368   1138    904  -1700       C  
ATOM   1245  CD1 LEU A 213      10.265 -28.090 -49.786  1.00 48.40           C  
ANISOU 1245  CD1 LEU A 213     9097   4880   4414   1311   1000  -1555       C  
ATOM   1246  CD2 LEU A 213      10.888 -26.727 -51.791  1.00 50.99           C  
ANISOU 1246  CD2 LEU A 213     9544   5642   4189   1203   1107  -1633       C  
ATOM   1247  N   SER A 214       8.511 -30.029 -55.332  1.00 69.95           N  
ANISOU 1247  N   SER A 214    13596   7128   5852   1002    663  -2698       N  
ATOM   1248  CA  SER A 214       8.495 -31.195 -56.205  1.00 76.59           C  
ANISOU 1248  CA  SER A 214    14916   7637   6548   1027    593  -3023       C  
ATOM   1249  C   SER A 214       9.696 -31.170 -57.143  1.00 82.21           C  
ANISOU 1249  C   SER A 214    15844   8292   7102   1408    947  -3249       C  
ATOM   1250  O   SER A 214      10.417 -30.173 -57.208  1.00 86.92           O  
ANISOU 1250  O   SER A 214    16748   8533   7747   1544    960  -3477       O  
ATOM   1251  CB  SER A 214       7.196 -31.253 -57.008  1.00 78.17           C  
ANISOU 1251  CB  SER A 214    15397   7875   6426    743    332  -3152       C  
ATOM   1252  OG  SER A 214       7.029 -30.090 -57.799  1.00 73.06           O  
ANISOU 1252  OG  SER A 214    14468   7427   5865    448     85  -2903       O  
ATOM   1253  N   GLY A 215       9.908 -32.268 -57.861  1.00 80.78           N  
ANISOU 1253  N   GLY A 215    15501   8458   6735   1578   1237  -3181       N  
ATOM   1254  CA  GLY A 215      11.038 -32.391 -58.764  1.00 86.75           C  
ANISOU 1254  CA  GLY A 215    16430   9229   7301   1942   1607  -3385       C  
ATOM   1255  C   GLY A 215      11.070 -31.310 -59.826  1.00 89.85           C  
ANISOU 1255  C   GLY A 215    16957   9941   7240   1908   1732  -3451       C  
ATOM   1256  O   GLY A 215      12.055 -30.585 -59.957  1.00 90.93           O  
ANISOU 1256  O   GLY A 215    16920  10368   7262   2122   2071  -3385       O  
ATOM   1257  N   ASP A 216       9.984 -31.201 -60.584  1.00 92.82           N  
ANISOU 1257  N   ASP A 216    17641  10270   7358   1625   1447  -3571       N  
ATOM   1258  CA  ASP A 216       9.881 -30.189 -61.627  1.00 95.07           C  
ANISOU 1258  CA  ASP A 216    18041  10871   7212   1518   1483  -3578       C  
ATOM   1259  C   ASP A 216       9.525 -28.832 -61.033  1.00 88.35           C  
ANISOU 1259  C   ASP A 216    16808  10291   6468   1247   1293  -3232       C  
ATOM   1260  O   ASP A 216       9.737 -27.794 -61.660  1.00 88.62           O  
ANISOU 1260  O   ASP A 216    16783  10650   6238   1185   1372  -3118       O  
ATOM   1261  CB  ASP A 216       8.830 -30.597 -62.662  1.00151.93           C  
ATOM   1262  CG  ASP A 216       9.130 -31.940 -63.299  1.00151.93           C  
ATOM   1263  OD1 ASP A 216      10.322 -32.302 -63.389  1.00151.93           O  
ATOM   1264  OD2 ASP A 216       8.175 -32.634 -63.710  1.00151.93           O  
ATOM   1265  N   GLY A 217       8.984 -28.845 -59.819  1.00 81.57           N  
ANISOU 1265  N   GLY A 217    15703   9289   5998   1090   1048  -3063       N  
ATOM   1266  CA  GLY A 217       8.549 -27.626 -59.164  1.00 75.31           C  
ANISOU 1266  CA  GLY A 217    14555   8712   5349    850    857  -2750       C  
ATOM   1267  C   GLY A 217       7.205 -27.167 -59.692  1.00 76.08           C  
ANISOU 1267  C   GLY A 217    14829   8785   5295    514    464  -2772       C  
ATOM   1268  O   GLY A 217       6.799 -26.025 -59.476  1.00 72.00           O  
ANISOU 1268  O   GLY A 217    14059   8448   4849    314    285  -2534       O  
ATOM   1269  N   THR A 218       6.511 -28.065 -60.385  1.00 81.79           N  
ANISOU 1269  N   THR A 218    15988   9276   5813    455    320  -3061       N  
ATOM   1270  CA  THR A 218       5.231 -27.741 -61.005  1.00 84.04           C  
ANISOU 1270  CA  THR A 218    16478   9551   5901    138    -60  -3108       C  
ATOM   1271  C   THR A 218       4.117 -28.682 -60.551  1.00 83.25           C  
ANISOU 1271  C   THR A 218    16404   9148   6079    -94   -419  -3139       C  
ATOM   1272  O   THR A 218       2.950 -28.478 -60.882  1.00 82.87           O  
ANISOU 1272  O   THR A 218    16319   9148   6021   -386   -762  -3052       O  
ATOM   1273  CB  THR A 218       5.324 -27.788 -62.542  1.00 92.07           C  
ANISOU 1273  CB  THR A 218    18001  10554   6426    171    -26  -3411       C  
ATOM   1274  OG1 THR A 218       5.734 -29.097 -62.957  1.00 96.64           O  
ANISOU 1274  OG1 THR A 218    18916  10780   7024    317     43  -3718       O  
ATOM   1275  CG2 THR A 218       6.330 -26.766 -63.049  1.00 93.57           C  
ANISOU 1275  CG2 THR A 218    18170  11068   6314    385    347  -3370       C  
ATOM   1276  N   HIS A 219       4.482 -29.710 -59.791  1.00 83.49           N  
ANISOU 1276  N   HIS A 219    16491   8868   6363     35   -341  -3250       N  
ATOM   1277  CA  HIS A 219       3.509 -30.680 -59.299  1.00 84.17           C  
ANISOU 1277  CA  HIS A 219    16667   8628   6688   -188   -661  -3307       C  
ATOM   1278  C   HIS A 219       2.729 -30.104 -58.119  1.00 77.33           C  
ANISOU 1278  C   HIS A 219    15340   7837   6204   -370   -830  -2988       C  
ATOM   1279  O   HIS A 219       3.319 -29.722 -57.108  1.00 72.06           O  
ANISOU 1279  O   HIS A 219    14337   7253   5789   -209   -625  -2794       O  
ATOM   1280  CB  HIS A 219       4.212 -31.979 -58.897  1.00 87.32           C  
ANISOU 1280  CB  HIS A 219    17303   8647   7228     22   -515  -3521       C  
ATOM   1281  CG  HIS A 219       3.290 -33.152 -58.757  1.00 90.32           C  
ANISOU 1281  CG  HIS A 219    17903   8645   7768   -220   -843  -3641       C  
ATOM   1282  ND1 HIS A 219       3.601 -34.403 -59.244  1.00 97.28           N  
ANISOU 1282  ND1 HIS A 219    19261   9156   8544   -148   -853  -3968       N  
ATOM   1283  CD2 HIS A 219       2.071 -33.266 -58.180  1.00 87.79           C  
ANISOU 1283  CD2 HIS A 219    17390   8250   7714   -536  -1165  -3474       C  
ATOM   1284  CE1 HIS A 219       2.611 -35.236 -58.978  1.00 98.89           C  
ANISOU 1284  CE1 HIS A 219    19563   9064   8945   -432  -1185  -3990       C  
ATOM   1285  NE2 HIS A 219       1.669 -34.571 -58.333  1.00 93.23           N  
ANISOU 1285  NE2 HIS A 219    18432   8535   8457   -673  -1372  -3687       N  
ATOM   1286  N   PRO A 220       1.393 -30.038 -58.253  1.00 77.87           N  
ANISOU 1286  N   PRO A 220    15391   7891   6305   -705  -1206  -2934       N  
ATOM   1287  CA  PRO A 220       0.484 -29.489 -57.238  1.00 72.60           C  
ANISOU 1287  CA  PRO A 220    14312   7307   5966   -906  -1397  -2651       C  
ATOM   1288  C   PRO A 220       0.603 -30.183 -55.884  1.00 68.98           C  
ANISOU 1288  C   PRO A 220    13655   6646   5908   -826  -1297  -2549       C  
ATOM   1289  O   PRO A 220       0.262 -29.591 -54.861  1.00 63.29           O  
ANISOU 1289  O   PRO A 220    12537   6073   5437   -845  -1274  -2288       O  
ATOM   1290  CB  PRO A 220      -0.900 -29.755 -57.836  1.00 77.23           C  
ANISOU 1290  CB  PRO A 220    15056   7779   6507  -1256  -1813  -2726       C  
ATOM   1291  CG  PRO A 220      -0.671 -29.787 -59.308  1.00 83.87           C  
ANISOU 1291  CG  PRO A 220    16355   8597   6916  -1257  -1861  -3002       C  
ATOM   1292  CD  PRO A 220       0.673 -30.432 -59.478  1.00 84.46           C  
ANISOU 1292  CD  PRO A 220    16590   8712   6790   -901  -1459  -3131       C  
ATOM   1293  N   GLY A 221       1.074 -31.426 -55.884  1.00 72.75           N  
ANISOU 1293  N   GLY A 221    14428   6778   6434   -736  -1247  -2756       N  
ATOM   1294  CA  GLY A 221       1.252 -32.174 -54.653  1.00 70.43           C  
ANISOU 1294  CA  GLY A 221    14006   6255   6502   -655  -1167  -2669       C  
ATOM   1295  C   GLY A 221       2.507 -31.771 -53.902  1.00 65.33           C  
ANISOU 1295  C   GLY A 221    13071   5774   5976   -345   -828  -2510       C  
ATOM   1296  O   GLY A 221       2.695 -32.147 -52.745  1.00 61.44           O  
ANISOU 1296  O   GLY A 221    12322   5225   5797   -317   -788  -2324       O  
ATOM   1297  N   GLY A 222       3.367 -31.002 -54.562  1.00 65.81           N  
ANISOU 1297  N   GLY A 222    13178   6049   5780   -123   -586  -2577       N  
ATOM   1298  CA  GLY A 222       4.607 -30.550 -53.959  1.00 61.73           C  
ANISOU 1298  CA  GLY A 222    12381   5722   5354    159   -266  -2428       C  
ATOM   1299  C   GLY A 222       4.470 -29.198 -53.285  1.00 55.11           C  
ANISOU 1299  C   GLY A 222    11099   5190   4651     56   -295  -2118       C  
ATOM   1300  O   GLY A 222       5.433 -28.668 -52.733  1.00 51.23           O  
ANISOU 1300  O   GLY A 222    10331   4839   4294    239    -80  -1958       O  
ATOM   1301  N   LEU A 223       3.265 -28.640 -53.336  1.00 96.36           N  
ANISOU 1301  N   LEU A 223    16257  10517   9838   -231   -568  -2037       N  
ATOM   1302  CA  LEU A 223       2.985 -27.348 -52.722  1.00 93.30           C  
ANISOU 1302  CA  LEU A 223    15476  10397   9575   -331   -617  -1760       C  
ATOM   1303  C   LEU A 223       2.970 -27.461 -51.203  1.00 92.43           C  
ANISOU 1303  C   LEU A 223    15083  10204   9831   -329   -607  -1573       C  
ATOM   1304  O   LEU A 223       1.998 -27.937 -50.620  1.00 92.50           O  
ANISOU 1304  O   LEU A 223    15117  10010  10020   -499   -796  -1568       O  
ATOM   1305  CB  LEU A 223       1.641 -26.809 -53.212  1.00 59.21           C  
ANISOU 1305  CB  LEU A 223    11156   6174   5166   -625   -931  -1724       C  
ATOM   1306  CG  LEU A 223       1.198 -25.484 -52.592  1.00 55.81           C  
ANISOU 1306  CG  LEU A 223    10356   6025   4822   -707   -983  -1461       C  
ATOM   1307  CD1 LEU A 223       2.173 -24.379 -52.962  1.00 54.76           C  
ANISOU 1307  CD1 LEU A 223    10141   6147   4516   -524   -746  -1390       C  
ATOM   1308  CD2 LEU A 223      -0.216 -25.130 -53.020  1.00 54.45           C  
ANISOU 1308  CD2 LEU A 223    10184   5924   4578   -976  -1308  -1434       C  
ATOM   1309  N   VAL A 224       4.046 -27.018 -50.563  1.00 41.96           N  
ANISOU 1309  N   VAL A 224     8425   3977   3539   -150   -391  -1412       N  
ATOM   1310  CA  VAL A 224       4.160 -27.135 -49.114  1.00 40.96           C  
ANISOU 1310  CA  VAL A 224     8043   3791   3726   -125   -363  -1232       C  
ATOM   1311  C   VAL A 224       4.356 -25.789 -48.421  1.00 38.01           C  
ANISOU 1311  C   VAL A 224     7309   3707   3425   -127   -308   -992       C  
ATOM   1312  O   VAL A 224       4.863 -24.833 -49.015  1.00 36.76           O  
ANISOU 1312  O   VAL A 224     7095   3779   3090    -71   -213   -963       O  
ATOM   1313  CB  VAL A 224       5.315 -28.076 -48.715  1.00 36.83           C  
ANISOU 1313  CB  VAL A 224     7590   3096   3309    145   -144  -1293       C  
ATOM   1314  CG1 VAL A 224       5.080 -29.474 -49.272  1.00 42.39           C  
ANISOU 1314  CG1 VAL A 224     8662   3450   3994    146   -215  -1524       C  
ATOM   1315  CG2 VAL A 224       6.647 -27.521 -49.197  1.00 37.08           C  
ANISOU 1315  CG2 VAL A 224     7582   3329   3176    395    130  -1318       C  
ATOM   1316  N   CYS A 225       3.938 -25.728 -47.159  1.00 54.07           N  
ANISOU 1316  N   CYS A 225     9117   5716   5709   -199   -371   -820       N  
ATOM   1317  CA  CYS A 225       4.195 -24.576 -46.308  1.00 50.72           C  
ANISOU 1317  CA  CYS A 225     8370   5523   5377   -188   -316   -604       C  
ATOM   1318  C   CYS A 225       5.560 -24.751 -45.661  1.00 51.44           C  
ANISOU 1318  C   CYS A 225     8352   5625   5566     48    -91   -540       C  
ATOM   1319  O   CYS A 225       5.834 -25.776 -45.038  1.00 52.68           O  
ANISOU 1319  O   CYS A 225     8547   5586   5884    125    -61   -544       O  
ATOM   1320  CB  CYS A 225       3.114 -24.447 -45.237  1.00 50.46           C  
ANISOU 1320  CB  CYS A 225     8157   5472   5542   -377   -485   -458       C  
ATOM   1321  SG  CYS A 225       3.312 -23.024 -44.140  1.00 46.02           S  
ANISOU 1321  SG  CYS A 225     7237   5175   5075   -373   -438   -218       S  
ATOM   1322  N   THR A 226       6.415 -23.748 -45.813  1.00 43.16           N  
ANISOU 1322  N   THR A 226     7167   4806   4425    155     56   -470       N  
ATOM   1323  CA  THR A 226       7.814 -23.881 -45.438  1.00 44.08           C  
ANISOU 1323  CA  THR A 226     7171   4966   4611    383    273   -419       C  
ATOM   1324  C   THR A 226       8.439 -22.494 -45.276  1.00 41.45           C  
ANISOU 1324  C   THR A 226     6596   4917   4237    395    360   -262       C  
ATOM   1325  O   THR A 226       7.875 -21.499 -45.745  1.00 39.56           O  
ANISOU 1325  O   THR A 226     6348   4821   3862    266    285   -236       O  
ATOM   1326  CB  THR A 226       8.581 -24.685 -46.520  1.00 35.82           C  
ANISOU 1326  CB  THR A 226     6356   3828   3424    579    439   -616       C  
ATOM   1327  OG1 THR A 226       9.843 -25.128 -46.009  1.00 36.98           O  
ANISOU 1327  OG1 THR A 226     6378   3978   3693    820    637   -565       O  
ATOM   1328  CG2 THR A 226       8.805 -23.835 -47.765  1.00 35.45           C  
ANISOU 1328  CG2 THR A 226     6395   3977   3095    570    512   -688       C  
ATOM   1329  N   PRO A 227       9.587 -22.412 -44.581  1.00 44.70           N  
ANISOU 1329  N   PRO A 227     6808   5400   4775    540    499   -144       N  
ATOM   1330  CA  PRO A 227      10.333 -21.150 -44.584  1.00 42.19           C  
ANISOU 1330  CA  PRO A 227     6283   5341   4406    549    592     -9       C  
ATOM   1331  C   PRO A 227      10.756 -20.760 -45.997  1.00 43.08           C  
ANISOU 1331  C   PRO A 227     6506   5583   4279    609    735   -102       C  
ATOM   1332  O   PRO A 227      11.462 -21.519 -46.662  1.00 45.96           O  
ANISOU 1332  O   PRO A 227     6990   5892   4581    784    894   -229       O  
ATOM   1333  CB  PRO A 227      11.564 -21.476 -43.735  1.00 46.24           C  
ANISOU 1333  CB  PRO A 227     6595   5876   5098    714    713    102       C  
ATOM   1334  CG  PRO A 227      11.090 -22.521 -42.794  1.00 49.30           C  
ANISOU 1334  CG  PRO A 227     7128   6012   5594    844    724     -3       C  
ATOM   1335  CD  PRO A 227      10.115 -23.358 -43.580  1.00 49.65           C  
ANISOU 1335  CD  PRO A 227     7374   5879   5614    669    536    -99       C  
ATOM   1336  N   ILE A 228      10.314 -19.589 -46.446  1.00 61.91           N  
ANISOU 1336  N   ILE A 228     8861   8135   6527    472    683    -36       N  
ATOM   1337  CA  ILE A 228      10.683 -19.075 -47.760  1.00 62.55           C  
ANISOU 1337  CA  ILE A 228     9065   8350   6349    493    800   -101       C  
ATOM   1338  C   ILE A 228      11.904 -18.174 -47.642  1.00 61.27           C  
ANISOU 1338  C   ILE A 228     8689   8418   6172    550    980     47       C  
ATOM   1339  O   ILE A 228      12.112 -17.275 -48.457  1.00 61.35           O  
ANISOU 1339  O   ILE A 228     8756   8583   5970    534   1083     51       O  
ATOM   1340  CB  ILE A 228       9.534 -18.271 -48.389  1.00 34.13           C  
ANISOU 1340  CB  ILE A 228     5595   4785   2586    298    614   -111       C  
ATOM   1341  CG1 ILE A 228       9.054 -17.188 -47.420  1.00 30.52           C  
ANISOU 1341  CG1 ILE A 228     4931   4410   2253    157    474     78       C  
ATOM   1342  CG2 ILE A 228       8.390 -19.195 -48.772  1.00 35.86           C  
ANISOU 1342  CG2 ILE A 228     6038   4798   2788    229    441   -272       C  
ATOM   1343  CD1 ILE A 228       7.999 -16.270 -47.998  1.00 30.10           C  
ANISOU 1343  CD1 ILE A 228     4974   4388   2075    -12    278     90       C  
ATOM   1344  N   VAL A 229      12.712 -18.428 -46.620  1.00 56.86           N  
ANISOU 1344  N   VAL A 229     7886   7886   5834    600   1009    180       N  
ATOM   1345  CA  VAL A 229      13.843 -17.573 -46.291  1.00 55.61           C  
ANISOU 1345  CA  VAL A 229     7492   7942   5696    629   1154    338       C  
ATOM   1346  C   VAL A 229      15.111 -18.415 -46.145  1.00 58.14           C  
ANISOU 1346  C   VAL A 229     7697   8280   6113    863   1367    319       C  
ATOM   1347  O   VAL A 229      15.051 -19.560 -45.693  1.00 60.32           O  
ANISOU 1347  O   VAL A 229     8067   8372   6479    998   1370    204       O  
ATOM   1348  CB  VAL A 229      13.559 -16.788 -44.988  1.00 52.10           C  
ANISOU 1348  CB  VAL A 229     6839   7540   5416    490   1005    520       C  
ATOM   1349  CG1 VAL A 229      14.765 -15.984 -44.562  1.00 51.99           C  
ANISOU 1349  CG1 VAL A 229     6662   7450   5642    588    994    575       C  
ATOM   1350  CG2 VAL A 229      12.357 -15.875 -45.173  1.00 50.28           C  
ANISOU 1350  CG2 VAL A 229     6457   7527   5120    405   1078    676       C  
ATOM   1351  N   ASP A 230      16.251 -17.853 -46.545  1.00 48.74           N  
ANISOU 1351  N   ASP A 230     6300   7308   4912    910   1541    438       N  
ATOM   1352  CA  ASP A 230      17.535 -18.545 -46.438  1.00 51.21           C  
ANISOU 1352  CA  ASP A 230     6457   7678   5323   1149   1757    439       C  
ATOM   1353  C   ASP A 230      17.852 -18.974 -45.004  1.00 50.66           C  
ANISOU 1353  C   ASP A 230     6206   7509   5535   1222   1663    525       C  
ATOM   1354  O   ASP A 230      17.221 -18.516 -44.050  1.00 47.88           O  
ANISOU 1354  O   ASP A 230     5808   7095   5288   1065   1453    615       O  
ATOM   1355  CB  ASP A 230      18.669 -17.680 -47.000  1.00 97.97           C  
ANISOU 1355  CB  ASP A 230    12160  13888  11175   1150   1960    574       C  
ATOM   1356  CG  ASP A 230      18.773 -16.332 -46.312  1.00 94.55           C  
ANISOU 1356  CG  ASP A 230    11521  13583  10821    926   1825    791       C  
ATOM   1357  OD1 ASP A 230      18.082 -15.386 -46.746  1.00 92.77           O  
ANISOU 1357  OD1 ASP A 230    11409  13392  10446    728   1732    822       O  
ATOM   1358  OD2 ASP A 230      19.547 -16.219 -45.339  1.00 93.75           O  
ANISOU 1358  OD2 ASP A 230    11155  13537  10927    949   1801    928       O  
ATOM   1359  N   THR A 231      18.843 -19.851 -44.868  1.00 81.42           N  
ANISOU 1359  N   THR A 231    10004  11390   9542   1473   1822    499       N  
ATOM   1360  CA  THR A 231      19.158 -20.489 -43.591  1.00 81.55           C  
ANISOU 1360  CA  THR A 231     9879  11292   9814   1577   1735    576       C  
ATOM   1361  C   THR A 231      19.547 -19.510 -42.483  1.00 78.49           C  
ANISOU 1361  C   THR A 231     9192  11061   9571   1443   1623    808       C  
ATOM   1362  O   THR A 231      19.031 -19.592 -41.368  1.00 76.88           O  
ANISOU 1362  O   THR A 231     8963  10743   9507   1377   1433    877       O  
ATOM   1363  CB  THR A 231      20.279 -21.535 -43.756  1.00 82.40           C  
ANISOU 1363  CB  THR A 231     9917  11376  10016   1905   1944    518       C  
ATOM   1364  OG1 THR A 231      19.901 -22.488 -44.758  1.00 85.06           O  
ANISOU 1364  OG1 THR A 231    10571  11541  10207   2034   2043    278       O  
ATOM   1365  CG2 THR A 231      20.533 -22.257 -42.443  1.00 82.49           C  
ANISOU 1365  CG2 THR A 231     9815  11239  10288   2018   1826    605       C  
ATOM   1366  N   ALA A 232      20.452 -18.587 -42.794  1.00 70.54           N  
ANISOU 1366  N   ALA A 232     7970  10313   8518   1391   1738    927       N  
ATOM   1367  CA  ALA A 232      20.981 -17.654 -41.800  1.00 68.00           C  
ANISOU 1367  CA  ALA A 232     7366  10144   8325   1252   1631   1142       C  
ATOM   1368  C   ALA A 232      19.901 -16.789 -41.150  1.00 64.12           C  
ANISOU 1368  C   ALA A 232     6973   9577   7813    989   1382   1186       C  
ATOM   1369  O   ALA A 232      19.818 -16.697 -39.922  1.00 62.23           O  
ANISOU 1369  O   ALA A 232     6633   9297   7715    930   1216   1286       O  
ATOM   1370  CB  ALA A 232      22.064 -16.780 -42.421  1.00 61.38           C  
ANISOU 1370  CB  ALA A 232     6307   9590   7424   1209   1804   1257       C  
ATOM   1371  N   THR A 233      19.077 -16.157 -41.978  1.00 52.21           N  
ANISOU 1371  N   THR A 233     5664   8053   6121    844   1359   1112       N  
ATOM   1372  CA  THR A 233      18.025 -15.282 -41.480  1.00 48.58           C  
ANISOU 1372  CA  THR A 233     5299   7526   5635    620   1142   1143       C  
ATOM   1373  C   THR A 233      17.016 -16.069 -40.640  1.00 48.13           C  
ANISOU 1373  C   THR A 233     5384   7245   5660    635    985   1064       C  
ATOM   1374  O   THR A 233      16.572 -15.603 -39.587  1.00 45.10           O  
ANISOU 1374  O   THR A 233     4985   6817   5336    502    811   1129       O  
ATOM   1375  CB  THR A 233      17.306 -14.557 -42.634  1.00 52.60           C  
ANISOU 1375  CB  THR A 233     5993   8062   5930    490   1150   1084       C  
ATOM   1376  OG1 THR A 233      18.273 -13.970 -43.515  1.00 54.88           O  
ANISOU 1376  OG1 THR A 233     6487   8275   6092    618   1264    911       O  
ATOM   1377  CG2 THR A 233      16.383 -13.473 -42.095  1.00 52.96           C  
ANISOU 1377  CG2 THR A 233     5891   8330   5902    399   1260   1216       C  
ATOM   1378  N   LEU A 234      16.667 -17.265 -41.107  1.00 53.82           N  
ANISOU 1378  N   LEU A 234     6249   7821   6377    796   1054    925       N  
ATOM   1379  CA  LEU A 234      15.794 -18.164 -40.355  1.00 54.09           C  
ANISOU 1379  CA  LEU A 234     6414   7634   6502    809    921    863       C  
ATOM   1380  C   LEU A 234      16.381 -18.451 -38.976  1.00 53.09           C  
ANISOU 1380  C   LEU A 234     6102   7501   6569    862    854    999       C  
ATOM   1381  O   LEU A 234      15.673 -18.401 -37.963  1.00 50.94           O  
ANISOU 1381  O   LEU A 234     5854   7140   6362    762    694   1044       O  
ATOM   1382  CB  LEU A 234      15.577 -19.474 -41.115  1.00 30.70           C  
ANISOU 1382  CB  LEU A 234     3658   4504   3504    972   1012    686       C  
ATOM   1383  CG  LEU A 234      14.732 -20.515 -40.379  1.00 31.52           C  
ANISOU 1383  CG  LEU A 234     3909   4356   3713    977    880    629       C  
ATOM   1384  CD1 LEU A 234      13.329 -19.983 -40.130  1.00 29.20           C  
ANISOU 1384  CD1 LEU A 234     3718   4008   3369    749    697    621       C  
ATOM   1385  CD2 LEU A 234      14.686 -21.831 -41.145  1.00 35.88           C  
ANISOU 1385  CD2 LEU A 234     4678   4722   4233   1143    974    448       C  
ATOM   1386  N   LYS A 235      17.680 -18.741 -38.951  1.00 45.95           N  
ANISOU 1386  N   LYS A 235     5006   6705   5748   1023    980   1070       N  
ATOM   1387  CA  LYS A 235      18.406 -18.920 -37.700  1.00 45.04           C  
ANISOU 1387  CA  LYS A 235     4683   6620   5807   1074    906   1223       C  
ATOM   1388  C   LYS A 235      18.222 -17.692 -36.821  1.00 40.95           C  
ANISOU 1388  C   LYS A 235     4061   6211   5287    850    747   1353       C  
ATOM   1389  O   LYS A 235      18.016 -17.809 -35.616  1.00 39.05           O  
ANISOU 1389  O   LYS A 235     3793   5912   5131    804    600   1433       O  
ATOM   1390  CB  LYS A 235      19.899 -19.145 -37.955  1.00 37.37           C  
ANISOU 1390  CB  LYS A 235     3473   5805   4921   1267   1070   1296       C  
ATOM   1391  CG  LYS A 235      20.264 -20.509 -38.512  1.00 41.58           C  
ANISOU 1391  CG  LYS A 235     4089   6209   5501   1547   1225   1179       C  
ATOM   1392  CD  LYS A 235      21.772 -20.629 -38.695  1.00 43.98           C  
ANISOU 1392  CD  LYS A 235     4106   6697   5908   1754   1392   1271       C  
ATOM   1393  CE  LYS A 235      22.178 -22.022 -39.155  1.00 47.80           C  
ANISOU 1393  CE  LYS A 235     4678   7037   6445   2071   1560   1143       C  
ATOM   1394  NZ  LYS A 235      23.657 -22.147 -39.301  1.00 51.29           N  
ANISOU 1394  NZ  LYS A 235     4808   7678   7002   2301   1740   1237       N  
ATOM   1395  N   VAL A 236      18.286 -16.514 -37.433  1.00 47.49           N  
ANISOU 1395  N   VAL A 236     4852   7187   6005    710    778   1372       N  
ATOM   1396  CA  VAL A 236      18.132 -15.268 -36.688  1.00 43.91           C  
ANISOU 1396  CA  VAL A 236     4329   6815   5540    498    630   1478       C  
ATOM   1397  C   VAL A 236      16.755 -15.140 -36.025  1.00 41.27           C  
ANISOU 1397  C   VAL A 236     4176   6331   5175    379    468   1426       C  
ATOM   1398  O   VAL A 236      16.668 -14.968 -34.806  1.00 39.16           O  
ANISOU 1398  O   VAL A 236     3861   6051   4968    310    332   1506       O  
ATOM   1399  CB  VAL A 236      18.418 -14.037 -37.571  1.00 42.86           C  
ANISOU 1399  CB  VAL A 236     4163   6832   5290    366    693   1506       C  
ATOM   1400  CG1 VAL A 236      18.106 -12.755 -36.819  1.00 39.43           C  
ANISOU 1400  CG1 VAL A 236     3733   6414   4834    146    521   1579       C  
ATOM   1401  CG2 VAL A 236      19.865 -14.047 -38.035  1.00 45.31           C  
ANISOU 1401  CG2 VAL A 236     4228   7338   5650    443    844   1606       C  
ATOM   1402  N   VAL A 237      15.684 -15.237 -36.812  1.00 47.22           N  
ANISOU 1402  N   VAL A 237     5133   6981   5828    357    483   1295       N  
ATOM   1403  CA  VAL A 237      14.339 -15.080 -36.250  1.00 44.93           C  
ANISOU 1403  CA  VAL A 237     4985   6572   5515    246    344   1249       C  
ATOM   1404  C   VAL A 237      14.000 -16.181 -35.239  1.00 45.38           C  
ANISOU 1404  C   VAL A 237     5068   6497   5679    306    279   1260       C  
ATOM   1405  O   VAL A 237      13.295 -15.932 -34.255  1.00 43.12           O  
ANISOU 1405  O   VAL A 237     4801   6174   5408    210    161   1297       O  
ATOM   1406  CB  VAL A 237      13.234 -14.954 -37.341  1.00 22.62           C  
ANISOU 1406  CB  VAL A 237     2350   3677   2566    203    356   1117       C  
ATOM   1407  CG1 VAL A 237      13.819 -14.417 -38.640  1.00 23.94           C  
ANISOU 1407  CG1 VAL A 237     2507   3975   2612    127    405   1134       C  
ATOM   1408  CG2 VAL A 237      12.523 -16.277 -37.575  1.00 22.12           C  
ANISOU 1408  CG2 VAL A 237     2406   3499   2497    341    447    998       C  
ATOM   1409  N   ILE A 238      14.523 -17.384 -35.468  1.00 43.00           N  
ANISOU 1409  N   ILE A 238     4773   6119   5447    473    363   1232       N  
ATOM   1410  CA  ILE A 238      14.296 -18.494 -34.547  1.00 43.45           C  
ANISOU 1410  CA  ILE A 238     4869   6029   5612    537    302   1260       C  
ATOM   1411  C   ILE A 238      15.023 -18.247 -33.227  1.00 41.34           C  
ANISOU 1411  C   ILE A 238     4433   5846   5427    528    219   1422       C  
ATOM   1412  O   ILE A 238      14.489 -18.523 -32.149  1.00 39.64           O  
ANISOU 1412  O   ILE A 238     4258   5562   5241    469    113   1477       O  
ATOM   1413  CB  ILE A 238      14.729 -19.850 -35.153  1.00 59.13           C  
ANISOU 1413  CB  ILE A 238     6926   7882   7660    737    409   1185       C  
ATOM   1414  CG1 ILE A 238      13.775 -20.265 -36.276  1.00 61.50           C  
ANISOU 1414  CG1 ILE A 238     7451   8048   7868    712    439   1011       C  
ATOM   1415  CG2 ILE A 238      14.755 -20.936 -34.090  1.00 59.06           C  
ANISOU 1415  CG2 ILE A 238     6926   7729   7785    818    340   1263       C  
ATOM   1416  CD1 ILE A 238      14.065 -21.639 -36.842  1.00 65.37           C  
ANISOU 1416  CD1 ILE A 238     8061   8379   8398    905    542    904       C  
ATOM   1417  N   GLN A 239      16.242 -17.721 -33.320  1.00 46.76           N  
ANISOU 1417  N   GLN A 239     4931   6695   6142    575    265   1505       N  
ATOM   1418  CA  GLN A 239      17.002 -17.339 -32.136  1.00 45.11           C  
ANISOU 1418  CA  GLN A 239     4553   6593   5995    538    160   1661       C  
ATOM   1419  C   GLN A 239      16.241 -16.290 -31.337  1.00 41.84           C  
ANISOU 1419  C   GLN A 239     4188   6211   5498    333     27   1683       C  
ATOM   1420  O   GLN A 239      16.072 -16.420 -30.123  1.00 40.49           O  
ANISOU 1420  O   GLN A 239     4020   6021   5344    290    -89   1760       O  
ATOM   1421  CB  GLN A 239      18.376 -16.790 -32.524  1.00 70.79           C  
ANISOU 1421  CB  GLN A 239     7573  10035   9286    583    227   1745       C  
ATOM   1422  CG  GLN A 239      19.413 -17.846 -32.853  1.00 74.10           C  
ANISOU 1422  CG  GLN A 239     7877  10454   9821    823    347   1766       C  
ATOM   1423  CD  GLN A 239      20.719 -17.241 -33.333  1.00 75.56           C  
ANISOU 1423  CD  GLN A 239     7816  10858  10036    857    450   1840       C  
ATOM   1424  OE1 GLN A 239      21.036 -16.092 -33.022  1.00 73.97           O  
ANISOU 1424  OE1 GLN A 239     7491  10808   9805    685    377   1928       O  
ATOM   1425  NE2 GLN A 239      21.481 -18.011 -34.102  1.00 78.87           N  
ANISOU 1425  NE2 GLN A 239     8165  11290  10511   1076    628   1802       N  
ATOM   1426  N   VAL A 240      15.778 -15.254 -32.033  1.00 31.16           N  
ANISOU 1426  N   VAL A 240     2886   4906   4047    217     48   1615       N  
ATOM   1427  CA  VAL A 240      15.026 -14.174 -31.404  1.00 28.45           C  
ANISOU 1427  CA  VAL A 240     2606   4577   3626     48    -64   1615       C  
ATOM   1428  C   VAL A 240      13.785 -14.695 -30.687  1.00 27.42           C  
ANISOU 1428  C   VAL A 240     2616   4318   3482     26   -122   1573       C  
ATOM   1429  O   VAL A 240      13.507 -14.306 -29.552  1.00 26.51           O  
ANISOU 1429  O   VAL A 240     2513   4217   3340    -54   -220   1621       O  
ATOM   1430  CB  VAL A 240      14.624 -13.100 -32.433  1.00 19.46           C  
ANISOU 1430  CB  VAL A 240     1526   3474   2394    -46    -30   1546       C  
ATOM   1431  CG1 VAL A 240      13.695 -12.072 -31.804  1.00 19.61           C  
ANISOU 1431  CG1 VAL A 240     1637   3467   2346   -182   -139   1525       C  
ATOM   1432  CG2 VAL A 240      15.866 -12.425 -33.000  1.00 20.36           C  
ANISOU 1432  CG2 VAL A 240     1491   3733   2512    -70     20   1619       C  
ATOM   1433  N   ASN A 241      13.049 -15.585 -31.346  1.00 43.33           N  
ANISOU 1433  N   ASN A 241     4740   6214   5510     90    -60   1486       N  
ATOM   1434  CA  ASN A 241      11.864 -16.177 -30.736  1.00 42.63           C  
ANISOU 1434  CA  ASN A 241     4766   6008   5425     53   -106   1461       C  
ATOM   1435  C   ASN A 241      12.201 -17.037 -29.519  1.00 42.86           C  
ANISOU 1435  C   ASN A 241     4768   5997   5521     98   -157   1572       C  
ATOM   1436  O   ASN A 241      11.492 -17.006 -28.514  1.00 41.55           O  
ANISOU 1436  O   ASN A 241     4650   5811   5327     21   -219   1609       O  
ATOM   1437  CB  ASN A 241      11.074 -16.991 -31.762  1.00 47.71           C  
ANISOU 1437  CB  ASN A 241     5534   6522   6074     89    -48   1347       C  
ATOM   1438  CG  ASN A 241       9.809 -17.591 -31.178  1.00 47.21           C  
ANISOU 1438  CG  ASN A 241     5567   6344   6027     22    -98   1335       C  
ATOM   1439  OD1 ASN A 241       9.754 -18.785 -30.875  1.00 48.60           O  
ANISOU 1439  OD1 ASN A 241     5792   6397   6276     75    -97   1364       O  
ATOM   1440  ND2 ASN A 241       8.785 -16.761 -31.011  1.00 44.88           N  
ANISOU 1440  ND2 ASN A 241     5294   6087   5671    -93   -141   1303       N  
ATOM   1441  N   THR A 242      13.288 -17.797 -29.613  1.00 57.24           N  
ANISOU 1441  N   THR A 242     6507   7814   7426    231   -126   1632       N  
ATOM   1442  CA  THR A 242      13.718 -18.661 -28.519  1.00 57.57           C  
ANISOU 1442  CA  THR A 242     6522   7813   7541    295   -188   1757       C  
ATOM   1443  C   THR A 242      14.102 -17.837 -27.294  1.00 55.80           C  
ANISOU 1443  C   THR A 242     6217   7722   7263    202   -301   1869       C  
ATOM   1444  O   THR A 242      13.786 -18.207 -26.163  1.00 55.25           O  
ANISOU 1444  O   THR A 242     6195   7621   7176    168   -378   1953       O  
ATOM   1445  CB  THR A 242      14.907 -19.549 -28.933  1.00 58.77           C  
ANISOU 1445  CB  THR A 242     6580   7942   7809    489   -131   1800       C  
ATOM   1446  OG1 THR A 242      14.564 -20.297 -30.106  1.00 60.99           O  
ANISOU 1446  OG1 THR A 242     6960   8102   8113    580    -16   1668       O  
ATOM   1447  CG2 THR A 242      15.272 -20.510 -27.809  1.00 59.27           C  
ANISOU 1447  CG2 THR A 242     6646   7916   7957    572   -207   1935       C  
ATOM   1448  N   PHE A 243      14.774 -16.713 -27.524  1.00 49.16           N  
ANISOU 1448  N   PHE A 243     5268   7025   6385    148   -316   1871       N  
ATOM   1449  CA  PHE A 243      15.167 -15.831 -26.430  1.00 47.95           C  
ANISOU 1449  CA  PHE A 243     5059   6989   6170     41   -440   1956       C  
ATOM   1450  C   PHE A 243      13.973 -15.103 -25.818  1.00 46.30           C  
ANISOU 1450  C   PHE A 243     4987   6767   5838    -97   -480   1894       C  
ATOM   1451  O   PHE A 243      13.761 -15.150 -24.606  1.00 45.98           O  
ANISOU 1451  O   PHE A 243     4999   6734   5737   -144   -559   1955       O  
ATOM   1452  CB  PHE A 243      16.199 -14.802 -26.902  1.00 45.16           C  
ANISOU 1452  CB  PHE A 243     4555   6780   5826      0   -452   1980       C  
ATOM   1453  CG  PHE A 243      17.593 -15.345 -27.025  1.00 46.90           C  
ANISOU 1453  CG  PHE A 243     4581   7074   6165    124   -445   2090       C  
ATOM   1454  CD1 PHE A 243      18.262 -15.827 -25.913  1.00 47.31           C  
ANISOU 1454  CD1 PHE A 243     4557   7159   6261    162   -564   2229       C  
ATOM   1455  CD2 PHE A 243      18.246 -15.346 -28.246  1.00 48.34           C  
ANISOU 1455  CD2 PHE A 243     4651   7307   6411    207   -318   2061       C  
ATOM   1456  CE1 PHE A 243      19.543 -16.320 -26.023  1.00 49.03           C  
ANISOU 1456  CE1 PHE A 243     4569   7454   6608    295   -566   2341       C  
ATOM   1457  CE2 PHE A 243      19.529 -15.836 -28.360  1.00 50.24           C  
ANISOU 1457  CE2 PHE A 243     4684   7634   6773    342   -293   2164       C  
ATOM   1458  CZ  PHE A 243      20.180 -16.322 -27.246  1.00 50.53           C  
ANISOU 1458  CZ  PHE A 243     4625   7698   6876    392   -423   2306       C  
ATOM   1459  N   MET A 244      13.194 -14.438 -26.664  1.00 42.49           N  
ANISOU 1459  N   MET A 244     4562   6269   5313   -149   -421   1777       N  
ATOM   1460  CA  MET A 244      12.155 -13.525 -26.196  1.00 41.24           C  
ANISOU 1460  CA  MET A 244     4507   6112   5051   -256   -451   1711       C  
ATOM   1461  C   MET A 244      10.862 -14.203 -25.746  1.00 41.09           C  
ANISOU 1461  C   MET A 244     4591   6012   5011   -259   -423   1689       C  
ATOM   1462  O   MET A 244      10.129 -13.657 -24.923  1.00 40.65           O  
ANISOU 1462  O   MET A 244     4597   5982   4866   -326   -453   1680       O  
ATOM   1463  CB  MET A 244      11.854 -12.468 -27.263  1.00 53.29           C  
ANISOU 1463  CB  MET A 244     6054   7643   6551   -297   -410   1611       C  
ATOM   1464  CG  MET A 244      13.050 -11.596 -27.596  1.00 53.29           C  
ANISOU 1464  CG  MET A 244     5967   7732   6546   -347   -448   1645       C  
ATOM   1465  SD  MET A 244      13.724 -10.803 -26.124  1.00 53.17           S  
ANISOU 1465  SD  MET A 244     5941   7793   6466   -452   -596   1719       S  
ATOM   1466  CE  MET A 244      15.472 -10.794 -26.514  1.00 54.39           C  
ANISOU 1466  CE  MET A 244     5901   8041   6721   -399   -631   1862       C  
ATOM   1467  N   SER A 245      10.578 -15.385 -26.282  1.00 54.18           N  
ANISOU 1467  N   SER A 245     6269   7569   6747   -192   -361   1680       N  
ATOM   1468  CA  SER A 245       9.337 -16.072 -25.939  1.00 54.09           C  
ANISOU 1468  CA  SER A 245     6343   7476   6732   -223   -334   1667       C  
ATOM   1469  C   SER A 245       9.552 -17.191 -24.926  1.00 54.82           C  
ANISOU 1469  C   SER A 245     6459   7517   6854   -198   -362   1791       C  
ATOM   1470  O   SER A 245       8.591 -17.726 -24.373  1.00 54.85           O  
ANISOU 1470  O   SER A 245     6528   7471   6841   -252   -345   1815       O  
ATOM   1471  CB  SER A 245       8.653 -16.624 -27.193  1.00 48.85           C  
ANISOU 1471  CB  SER A 245     5722   6712   6127   -204   -271   1569       C  
ATOM   1472  OG  SER A 245       9.422 -17.659 -27.779  1.00 48.99           O  
ANISOU 1472  OG  SER A 245     5804   6650   6161   -257   -257   1572       O  
ATOM   1473  N   PHE A 246      10.810 -17.544 -24.678  1.00 55.34           N  
ANISOU 1473  N   PHE A 246     6461   7599   6966   -119   -407   1884       N  
ATOM   1474  CA  PHE A 246      11.109 -18.663 -23.790  1.00 56.24           C  
ANISOU 1474  CA  PHE A 246     6602   7648   7119    -75   -449   2021       C  
ATOM   1475  C   PHE A 246      12.138 -18.325 -22.712  1.00 56.38           C  
ANISOU 1475  C   PHE A 246     6555   7778   7088    -70   -558   2149       C  
ATOM   1476  O   PHE A 246      11.782 -18.127 -21.553  1.00 56.15           O  
ANISOU 1476  O   PHE A 246     6585   7803   6947   -149   -613   2216       O  
ATOM   1477  CB  PHE A 246      11.558 -19.885 -24.597  1.00 39.22           C  
ANISOU 1477  CB  PHE A 246     4450   5343   5106     56   -407   2025       C  
ATOM   1478  CG  PHE A 246      11.753 -21.122 -23.768  1.00 40.33           C  
ANISOU 1478  CG  PHE A 246     4643   5374   5305    110   -454   2171       C  
ATOM   1479  CD1 PHE A 246      10.666 -21.780 -23.216  1.00 40.33           C  
ANISOU 1479  CD1 PHE A 246     4766   5271   5287     23   -446   2210       C  
ATOM   1480  CD2 PHE A 246      13.021 -21.631 -23.549  1.00 41.55           C  
ANISOU 1480  CD2 PHE A 246     4715   5530   5540    247   -511   2285       C  
ATOM   1481  CE1 PHE A 246      10.843 -22.918 -22.454  1.00 41.50           C  
ANISOU 1481  CE1 PHE A 246     4980   5301   5485     61   -496   2365       C  
ATOM   1482  CE2 PHE A 246      13.204 -22.769 -22.789  1.00 42.70           C  
ANISOU 1482  CE2 PHE A 246     4920   5558   5744    308   -570   2435       C  
ATOM   1483  CZ  PHE A 246      12.114 -23.414 -22.242  1.00 42.66           C  
ANISOU 1483  CZ  PHE A 246     5065   5433   5709    210   -563   2478       C  
ATOM   1484  N   LEU A 247      13.408 -18.261 -23.104  1.00 43.97           N  
ANISOU 1484  N   LEU A 247     4858   6256   5595     21   -589   2185       N  
ATOM   1485  CA  LEU A 247      14.516 -18.083 -22.162  1.00 44.45           C  
ANISOU 1485  CA  LEU A 247     4827   6421   5641     36   -718   2327       C  
ATOM   1486  C   LEU A 247      14.369 -16.873 -21.233  1.00 43.57           C  
ANISOU 1486  C   LEU A 247     4746   6444   5366   -111   -812   2328       C  
ATOM   1487  O   LEU A 247      14.276 -17.028 -20.014  1.00 43.85           O  
ANISOU 1487  O   LEU A 247     4848   6511   5302   -157   -902   2427       O  
ATOM   1488  CB  LEU A 247      15.846 -18.004 -22.917  1.00 41.62           C  
ANISOU 1488  CB  LEU A 247     4285   6124   5404    144   -716   2348       C  
ATOM   1489  CG  LEU A 247      16.220 -19.242 -23.736  1.00 43.34           C  
ANISOU 1489  CG  LEU A 247     4460   6221   5785    337   -650   2384       C  
ATOM   1490  CD1 LEU A 247      17.524 -19.020 -24.488  1.00 44.47           C  
ANISOU 1490  CD1 LEU A 247     4396   6467   6035    447   -619   2398       C  
ATOM   1491  CD2 LEU A 247      16.318 -20.466 -22.842  1.00 44.19           C  
ANISOU 1491  CD2 LEU A 247     4612   6251   5928    405   -745   2548       C  
ATOM   1492  N   PHE A 248      14.350 -15.679 -21.816  1.00 50.83           N  
ANISOU 1492  N   PHE A 248     5636   7430   6244   -183   -793   2216       N  
ATOM   1493  CA  PHE A 248      14.275 -14.429 -21.055  1.00 50.32           C  
ANISOU 1493  CA  PHE A 248     5619   7467   6033   -316   -885   2189       C  
ATOM   1494  C   PHE A 248      13.062 -14.322 -20.103  1.00 50.15           C  
ANISOU 1494  C   PHE A 248     5768   7429   5856   -388   -869   2154       C  
ATOM   1495  O   PHE A 248      13.242 -14.182 -18.883  1.00 50.76           O  
ANISOU 1495  O   PHE A 248     5907   7573   5804   -444   -971   2225       O  
ATOM   1496  CB  PHE A 248      14.364 -13.228 -22.015  1.00 76.42           C  
ANISOU 1496  CB  PHE A 248     8883  10806   9348   -372   -854   2075       C  
ATOM   1497  CG  PHE A 248      14.283 -11.889 -21.340  1.00 76.22           C  
ANISOU 1497  CG  PHE A 248     8927  10849   9187   -507   -955   2031       C  
ATOM   1498  CD1 PHE A 248      15.386 -11.352 -20.699  1.00 76.97           C  
ANISOU 1498  CD1 PHE A 248     8964  11039   9243   -576  -1116   2123       C  
ATOM   1499  CD2 PHE A 248      13.111 -11.153 -21.377  1.00 75.62           C  
ANISOU 1499  CD2 PHE A 248     8975  10731   9027   -561   -898   1895       C  
ATOM   1500  CE1 PHE A 248      15.317 -10.115 -20.089  1.00 77.19           C  
ANISOU 1500  CE1 PHE A 248     9088  11105   9138   -710  -1221   2065       C  
ATOM   1501  CE2 PHE A 248      13.034  -9.917 -20.769  1.00 75.93           C  
ANISOU 1501  CE2 PHE A 248     9106  10802   8943   -668   -988   1839       C  
ATOM   1502  CZ  PHE A 248      14.138  -9.396 -20.124  1.00 76.76           C  
ANISOU 1502  CZ  PHE A 248     9181  10986   8998   -749  -1151   1916       C  
ATOM   1503  N   PRO A 249      11.827 -14.411 -20.642  1.00 51.66           N  
ANISOU 1503  N   PRO A 249     6031   7547   6053   -385   -740   2051       N  
ATOM   1504  CA  PRO A 249      10.680 -14.183 -19.755  1.00 51.84           C  
ANISOU 1504  CA  PRO A 249     6183   7585   5931   -449   -704   2019       C  
ATOM   1505  C   PRO A 249      10.489 -15.290 -18.719  1.00 52.69           C  
ANISOU 1505  C   PRO A 249     6349   7682   5991   -446   -719   2159       C  
ATOM   1506  O   PRO A 249       9.965 -15.018 -17.642  1.00 53.37           O  
ANISOU 1506  O   PRO A 249     6535   7834   5909   -508   -730   2176       O  
ATOM   1507  CB  PRO A 249       9.495 -14.157 -20.723  1.00 29.81           C  
ANISOU 1507  CB  PRO A 249     3405   4723   3199   -438   -572   1902       C  
ATOM   1508  CG  PRO A 249       9.915 -15.025 -21.837  1.00 29.05           C  
ANISOU 1508  CG  PRO A 249     3229   4539   3267   -361   -540   1915       C  
ATOM   1509  CD  PRO A 249      11.391 -14.802 -21.996  1.00 29.75           C  
ANISOU 1509  CD  PRO A 249     3221   4681   3401   -327   -626   1968       C  
ATOM   1510  N   MET A 250      10.905 -16.513 -19.035  1.00 55.41           N  
ANISOU 1510  N   MET A 250     6649   7937   6470   -370   -714   2257       N  
ATOM   1511  CA  MET A 250      10.778 -17.613 -18.082  1.00 56.39           C  
ANISOU 1511  CA  MET A 250     6840   8025   6561   -368   -742   2415       C  
ATOM   1512  C   MET A 250      11.877 -17.587 -17.026  1.00 57.23           C  
ANISOU 1512  C   MET A 250     6941   8223   6581   -370   -902   2553       C  
ATOM   1513  O   MET A 250      11.675 -18.048 -15.903  1.00 58.17           O  
ANISOU 1513  O   MET A 250     7158   8371   6573   -412   -943   2672       O  
ATOM   1514  CB  MET A 250      10.747 -18.968 -18.789  1.00 47.76           C  
ANISOU 1514  CB  MET A 250     5729   6769   5649   -281   -696   2471       C  
ATOM   1515  CG  MET A 250       9.423 -19.280 -19.460  1.00 47.38           C  
ANISOU 1515  CG  MET A 250     5727   6624   5650   -321   -563   2376       C  
ATOM   1516  SD  MET A 250       8.025 -19.161 -18.324  1.00 47.75           S  
ANISOU 1516  SD  MET A 250     5877   6740   5524   -458   -492   2405       S  
ATOM   1517  CE  MET A 250       7.253 -17.643 -18.883  1.00 46.77           C  
ANISOU 1517  CE  MET A 250     5716   6714   5342   -497   -415   2194       C  
ATOM   1518  N   LEU A 251      13.041 -17.056 -17.386  1.00 39.52           N  
ANISOU 1518  N   LEU A 251     4577   6037   4401   -334   -997   2548       N  
ATOM   1519  CA  LEU A 251      14.099 -16.854 -16.407  1.00 42.14           C  
ANISOU 1519  CA  LEU A 251     4881   6478   4651   -357  -1179   2672       C  
ATOM   1520  C   LEU A 251      13.631 -15.794 -15.419  1.00 42.71           C  
ANISOU 1520  C   LEU A 251     5091   6657   4478   -490  -1222   2610       C  
ATOM   1521  O   LEU A 251      13.718 -15.979 -14.197  1.00 45.24           O  
ANISOU 1521  O   LEU A 251     5512   7041   4636   -537  -1319   2720       O  
ATOM   1522  CB  LEU A 251      15.398 -16.421 -17.087  1.00 51.48           C  
ANISOU 1522  CB  LEU A 251     5878   7720   5963   -317  -1260   2668       C  
ATOM   1523  CG  LEU A 251      16.638 -16.342 -16.194  1.00 52.50           C  
ANISOU 1523  CG  LEU A 251     5916   7962   6069   -325  -1471   2825       C  
ATOM   1524  CD1 LEU A 251      16.894 -17.675 -15.508  1.00 53.64           C  
ANISOU 1524  CD1 LEU A 251     6084   8055   6242   -232  -1535   3019       C  
ATOM   1525  CD2 LEU A 251      17.845 -15.920 -17.010  1.00 52.48           C  
ANISOU 1525  CD2 LEU A 251     5683   8020   6239   -276  -1510   2831       C  
ATOM   1526  N   VAL A 252      13.116 -14.692 -15.959  1.00 46.60           N  
ANISOU 1526  N   VAL A 252     5606   7162   4938   -543  -1147   2431       N  
ATOM   1527  CA  VAL A 252      12.546 -13.633 -15.130  1.00 47.21           C  
ANISOU 1527  CA  VAL A 252     5833   7313   4791   -644  -1162   2335       C  
ATOM   1528  C   VAL A 252      11.433 -14.168 -14.229  1.00 48.15           C  
ANISOU 1528  C   VAL A 252     6098   7439   4757   -660  -1066   2371       C  
ATOM   1529  O   VAL A 252      11.406 -13.895 -13.029  1.00 49.42           O  
ANISOU 1529  O   VAL A 252     6391   7688   4699   -724  -1134   2407       O  
ATOM   1530  CB  VAL A 252      12.002 -12.477 -15.991  1.00 34.78           C  
ANISOU 1530  CB  VAL A 252     4265   5712   3238   -666  -1073   2138       C  
ATOM   1531  CG1 VAL A 252      11.243 -11.481 -15.128  1.00 35.10           C  
ANISOU 1531  CG1 VAL A 252     4483   5799   3054   -732  -1052   2023       C  
ATOM   1532  CG2 VAL A 252      13.142 -11.791 -16.729  1.00 34.50           C  
ANISOU 1532  CG2 VAL A 252     4107   5690   3311   -688  -1178   2117       C  
ATOM   1533  N   ALA A 253      10.530 -14.948 -14.813  1.00 51.41           N  
ANISOU 1533  N   ALA A 253     6489   7766   5279   -615   -909   2369       N  
ATOM   1534  CA  ALA A 253       9.390 -15.493 -14.082  1.00 52.35           C  
ANISOU 1534  CA  ALA A 253     6715   7895   5280   -647   -791   2414       C  
ATOM   1535  C   ALA A 253       9.819 -16.458 -12.982  1.00 53.44           C  
ANISOU 1535  C   ALA A 253     6923   8055   5326   -663   -879   2626       C  
ATOM   1536  O   ALA A 253       9.213 -16.499 -11.914  1.00 54.71           O  
ANISOU 1536  O   ALA A 253     7212   8290   5283   -724   -829   2675       O  
ATOM   1537  CB  ALA A 253       8.418 -16.176 -15.039  1.00 44.34           C  
ANISOU 1537  CB  ALA A 253     5641   6775   4434   -617   -634   2377       C  
ATOM   1538  N   SER A 254      10.859 -17.241 -13.252  1.00 54.29           N  
ANISOU 1538  N   SER A 254     6947   8105   5578   -601  -1004   2758       N  
ATOM   1539  CA  SER A 254      11.358 -18.206 -12.279  1.00 55.53           C  
ANISOU 1539  CA  SER A 254     7167   8263   5669   -599  -1108   2982       C  
ATOM   1540  C   SER A 254      12.038 -17.496 -11.112  1.00 56.57           C  
ANISOU 1540  C   SER A 254     7370   8543   5581   -658  -1290   3034       C  
ATOM   1541  O   SER A 254      11.856 -17.875  -9.950  1.00 57.94           O  
ANISOU 1541  O   SER A 254     7671   8772   5573   -702  -1354   3188       O  
ATOM   1542  CB  SER A 254      12.325 -19.191 -12.937  1.00 58.61           C  
ANISOU 1542  CB  SER A 254     7439   8521   6309   -481  -1175   3106       C  
ATOM   1543  OG  SER A 254      13.442 -18.518 -13.490  1.00 57.99           O  
ANISOU 1543  OG  SER A 254     7209   8480   6344   -420  -1287   3061       O  
ATOM   1544  N   ILE A 255      12.825 -16.470 -11.426  1.00 47.23           N  
ANISOU 1544  N   ILE A 255     6125   7424   4398   -676  -1377   2906       N  
ATOM   1545  CA  ILE A 255      13.448 -15.650 -10.391  1.00 49.79           C  
ANISOU 1545  CA  ILE A 255     6531   7882   4505   -760  -1566   2925       C  
ATOM   1546  C   ILE A 255      12.382 -15.002  -9.511  1.00 50.23           C  
ANISOU 1546  C   ILE A 255     6802   8016   4269   -847  -1466   2817       C  
ATOM   1547  O   ILE A 255      12.427 -15.090  -8.275  1.00 53.43           O  
ANISOU 1547  O   ILE A 255     7364   8517   4421   -910  -1553   2909       O  
ATOM   1548  CB  ILE A 255      14.332 -14.551 -11.006  1.00 48.67           C  
ANISOU 1548  CB  ILE A 255     6269   7773   4450   -784  -1684   2812       C  
ATOM   1549  CG1 ILE A 255      15.564 -15.169 -11.669  1.00 49.28           C  
ANISOU 1549  CG1 ILE A 255     6120   7823   4782   -695  -1798   2948       C  
ATOM   1550  CG2 ILE A 255      14.744 -13.547  -9.945  1.00 51.18           C  
ANISOU 1550  CG2 ILE A 255     6721   8214   4512   -909  -1864   2776       C  
ATOM   1551  CD1 ILE A 255      16.448 -14.159 -12.370  1.00 48.37           C  
ANISOU 1551  CD1 ILE A 255     5848   7747   4785   -727  -1882   2858       C  
ATOM   1552  N   LEU A 256      11.416 -14.364 -10.166  1.00 53.71           N  
ANISOU 1552  N   LEU A 256     7248   8419   4741   -840  -1279   2624       N  
ATOM   1553  CA  LEU A 256      10.317 -13.701  -9.476  1.00 54.96           C  
ANISOU 1553  CA  LEU A 256     7582   8647   4654   -885  -1142   2499       C  
ATOM   1554  C   LEU A 256       9.525 -14.671  -8.609  1.00 56.10           C  
ANISOU 1554  C   LEU A 256     7825   8831   4661   -901  -1028   2647       C  
ATOM   1555  O   LEU A 256       9.081 -14.312  -7.525  1.00 58.16           O  
ANISOU 1555  O   LEU A 256     8264   9204   4632   -954   -994   2633       O  
ATOM   1556  CB  LEU A 256       9.388 -13.009 -10.477  1.00 50.23           C  
ANISOU 1556  CB  LEU A 256     6929   7988   4167   -845   -960   2293       C  
ATOM   1557  CG  LEU A 256       9.934 -11.755 -11.165  1.00 49.58           C  
ANISOU 1557  CG  LEU A 256     6802   7871   4164   -850  -1050   2130       C  
ATOM   1558  CD1 LEU A 256       8.929 -11.212 -12.173  1.00 49.26           C  
ANISOU 1558  CD1 LEU A 256     6722   7767   4228   -799   -870   1953       C  
ATOM   1559  CD2 LEU A 256      10.298 -10.692 -10.141  1.00 51.18           C  
ANISOU 1559  CD2 LEU A 256     7179   8153   4114   -931  -1198   2056       C  
ATOM   1560  N   ASN A 257       9.354 -15.900  -9.087  1.00 64.40           N  
ANISOU 1560  N   ASN A 257     8772   9785   5911   -861   -965   2787       N  
ATOM   1561  CA  ASN A 257       8.638 -16.920  -8.324  1.00 65.53           C  
ANISOU 1561  CA  ASN A 257     9004   9945   5951   -898   -867   2960       C  
ATOM   1562  C   ASN A 257       9.436 -17.434  -7.131  1.00 66.92           C  
ANISOU 1562  C   ASN A 257     9298  10186   5943   -937  -1050   3176       C  
ATOM   1563  O   ASN A 257       8.863 -17.797  -6.102  1.00 68.53           O  
ANISOU 1563  O   ASN A 257     9652  10473   5913  -1001   -981   3287       O  
ATOM   1564  CB  ASN A 257       8.213 -18.081  -9.225  1.00 59.52           C  
ANISOU 1564  CB  ASN A 257     8120   9028   5466   -859   -766   3042       C  
ATOM   1565  CG  ASN A 257       6.953 -17.776 -10.012  1.00 59.05           C  
ANISOU 1565  CG  ASN A 257     7996   8948   5494   -863   -544   2881       C  
ATOM   1566  OD1 ASN A 257       5.848 -18.108  -9.584  1.00 60.09           O  
ANISOU 1566  OD1 ASN A 257     8169   9117   5548   -921   -379   2931       O  
ATOM   1567  ND2 ASN A 257       7.112 -17.132 -11.163  1.00 57.65           N  
ANISOU 1567  ND2 ASN A 257     7708   8721   5478   -807   -542   2699       N  
ATOM   1568  N   THR A 258      10.758 -17.471  -7.274  1.00 68.93           N  
ANISOU 1568  N   THR A 258     9477  10416   6298   -899  -1283   3246       N  
ATOM   1569  CA  THR A 258      11.629 -17.818  -6.158  1.00 71.37           C  
ANISOU 1569  CA  THR A 258     9885  10802   6431   -933  -1501   3451       C  
ATOM   1570  C   THR A 258      11.493 -16.762  -5.065  1.00 73.21           C  
ANISOU 1570  C   THR A 258    10321  11206   6290  -1031  -1540   3354       C  
ATOM   1571  O   THR A 258      11.281 -17.083  -3.886  1.00 76.03           O  
ANISOU 1571  O   THR A 258    10863  11660   6366  -1095  -1554   3488       O  
ATOM   1572  CB  THR A 258      13.103 -17.908  -6.596  1.00 60.89           C  
ANISOU 1572  CB  THR A 258     8394   9442   5299   -868  -1750   3525       C  
ATOM   1573  OG1 THR A 258      13.257 -18.956  -7.562  1.00 59.28           O  
ANISOU 1573  OG1 THR A 258     8023   9072   5427   -753  -1700   3602       O  
ATOM   1574  CG2 THR A 258      14.000 -18.190  -5.400  1.00 65.69           C  
ANISOU 1574  CG2 THR A 258     9094  10145   5721   -904  -2005   3744       C  
ATOM   1575  N   VAL A 259      11.604 -15.499  -5.471  1.00 61.48           N  
ANISOU 1575  N   VAL A 259     8818   9748   4793  -1044  -1554   3118       N  
ATOM   1576  CA  VAL A 259      11.433 -14.375  -4.556  1.00 63.25           C  
ANISOU 1576  CA  VAL A 259     9254  10101   4675  -1126  -1586   2974       C  
ATOM   1577  C   VAL A 259      10.051 -14.410  -3.904  1.00 63.98           C  
ANISOU 1577  C   VAL A 259     9515  10266   4529  -1144  -1323   2931       C  
ATOM   1578  O   VAL A 259       9.903 -14.109  -2.720  1.00 67.53           O  
ANISOU 1578  O   VAL A 259    10187  10845   4626  -1209  -1347   2953       O  
ATOM   1579  CB  VAL A 259      11.636 -13.026  -5.280  1.00 59.45           C  
ANISOU 1579  CB  VAL A 259     8731   9589   4269  -1130  -1609   2714       C  
ATOM   1580  CG1 VAL A 259      11.407 -11.864  -4.328  1.00 61.42           C  
ANISOU 1580  CG1 VAL A 259     9237   9938   4162  -1203  -1623   2539       C  
ATOM   1581  CG2 VAL A 259      13.031 -12.954  -5.884  1.00 59.43           C  
ANISOU 1581  CG2 VAL A 259     8553   9550   4477  -1137  -1866   2771       C  
ATOM   1582  N   ILE A 260       9.047 -14.794  -4.687  1.00 61.68           N  
ANISOU 1582  N   ILE A 260     9111   9902   4425  -1089  -1072   2874       N  
ATOM   1583  CA  ILE A 260       7.680 -14.919  -4.196  1.00 62.41           C  
ANISOU 1583  CA  ILE A 260     9297  10071   4345  -1102   -797   2851       C  
ATOM   1584  C   ILE A 260       7.584 -15.992  -3.116  1.00 66.62           C  
ANISOU 1584  C   ILE A 260     9951  10678   4685  -1167   -794   3118       C  
ATOM   1585  O   ILE A 260       6.936 -15.793  -2.090  1.00 69.44           O  
ANISOU 1585  O   ILE A 260    10487  11179   4718  -1214   -662   3117       O  
ATOM   1586  CB  ILE A 260       6.698 -15.235  -5.345  1.00 57.01           C  
ANISOU 1586  CB  ILE A 260     8423   9288   3951  -1045   -570   2784       C  
ATOM   1587  CG1 ILE A 260       6.373 -13.964  -6.130  1.00 53.56           C  
ANISOU 1587  CG1 ILE A 260     7932   8823   3596   -984   -505   2500       C  
ATOM   1588  CG2 ILE A 260       5.412 -15.837  -4.809  1.00 58.71           C  
ANISOU 1588  CG2 ILE A 260     8679   9585   4043  -1081   -309   2864       C  
ATOM   1589  CD1 ILE A 260       5.617 -14.220  -7.416  1.00 50.04           C  
ANISOU 1589  CD1 ILE A 260     7280   8268   3466   -927   -354   2438       C  
ATOM   1590  N   ALA A 261       8.243 -17.124  -3.348  1.00 83.83           N  
ANISOU 1590  N   ALA A 261    12039  12754   7058  -1161   -935   3349       N  
ATOM   1591  CA  ALA A 261       8.261 -18.208  -2.373  1.00 85.35           C  
ANISOU 1591  CA  ALA A 261    12353  12986   7091  -1222   -968   3635       C  
ATOM   1592  C   ALA A 261       8.905 -17.747  -1.069  1.00 87.37           C  
ANISOU 1592  C   ALA A 261    12837  13403   6958  -1287  -1150   3689       C  
ATOM   1593  O   ALA A 261       8.336 -17.921   0.016  1.00 89.51           O  
ANISOU 1593  O   ALA A 261    13302  13807   6901  -1360  -1047   3786       O  
ATOM   1594  CB  ALA A 261       8.997 -19.413  -2.935  1.00 69.82           C  
ANISOU 1594  CB  ALA A 261    10252  10846   5432  -1175  -1118   3856       C  
ATOM   1595  N   ASN A 262      10.089 -17.151  -1.183  1.00 81.26           N  
ANISOU 1595  N   ASN A 262    12038  12627   6209  -1272  -1421   3627       N  
ATOM   1596  CA  ASN A 262      10.806 -16.656  -0.010  1.00 85.16           C  
ANISOU 1596  CA  ASN A 262    12747  13269   6341  -1349  -1645   3668       C  
ATOM   1597  C   ASN A 262      10.010 -15.620   0.786  1.00 86.56           C  
ANISOU 1597  C   ASN A 262    13161  13597   6130  -1402  -1481   3454       C  
ATOM   1598  O   ASN A 262       9.923 -15.698   2.013  1.00 90.72           O  
ANISOU 1598  O   ASN A 262    13931  14270   6268  -1476  -1499   3548       O  
ATOM   1599  CB  ASN A 262      12.168 -16.085  -0.412  1.00 91.54           C  
ANISOU 1599  CB  ASN A 262    13448  14047   7286  -1340  -1962   3619       C  
ATOM   1600  CG  ASN A 262      13.089 -17.135  -1.004  1.00 90.78           C  
ANISOU 1600  CG  ASN A 262    13125  13828   7541  -1264  -2131   3843       C  
ATOM   1601  OD1 ASN A 262      13.018 -18.312  -0.650  1.00 90.02           O  
ANISOU 1601  OD1 ASN A 262    12943  13620   7642  -1205  -1993   3985       O  
ATOM   1602  ND2 ASN A 262      13.961 -16.712  -1.912  1.00 91.25           N  
ANISOU 1602  ND2 ASN A 262    13084  13904   7684  -1265  -2431   3874       N  
ATOM   1603  N   LYS A 263       9.426 -14.660   0.078  1.00101.85           N  
ANISOU 1603  N   LYS A 263    15036  15496   8168  -1353  -1317   3167       N  
ATOM   1604  CA  LYS A 263       8.645 -13.602   0.712  1.00103.86           C  
ANISOU 1604  CA  LYS A 263    15498  15865   8099  -1362  -1137   2928       C  
ATOM   1605  C   LYS A 263       7.344 -14.129   1.312  1.00105.57           C  
ANISOU 1605  C   LYS A 263    15800  16192   8122  -1368   -820   3016       C  
ATOM   1606  O   LYS A 263       6.826 -13.566   2.276  1.00108.05           O  
ANISOU 1606  O   LYS A 263    16351  16660   8043  -1393   -699   2925       O  
ATOM   1607  CB  LYS A 263       8.355 -12.476  -0.281  1.00104.39           C  
ANISOU 1607  CB  LYS A 263    15450  15836   8377  -1284  -1028   2629       C  
ATOM   1608  CG  LYS A 263       9.568 -11.627  -0.622  1.00103.54           C  
ANISOU 1608  CG  LYS A 263    15291  15641   8411  -1305  -1322   2522       C  
ATOM   1609  CD  LYS A 263      10.068 -10.873   0.599  1.00104.77           C  
ANISOU 1609  CD  LYS A 263    15722  15897   8188  -1401  -1549   2453       C  
ATOM   1610  CE  LYS A 263      11.315 -10.065   0.278  1.00104.08           C  
ANISOU 1610  CE  LYS A 263    15563  15726   8257  -1451  -1849   2358       C  
ATOM   1611  NZ  LYS A 263      12.452 -10.940  -0.123  1.00105.31           N  
ANISOU 1611  NZ  LYS A 263    15949  15981   8085  -1580  -2157   2378       N  
ATOM   1612  N   LEU A 264       6.814 -15.201   0.732  1.00 84.56           N  
ANISOU 1612  N   LEU A 264    12945  13451   5732  -1351   -680   3190       N  
ATOM   1613  CA  LEU A 264       5.636 -15.856   1.284  1.00 86.88           C  
ANISOU 1613  CA  LEU A 264    13285  13845   5878  -1389   -396   3326       C  
ATOM   1614  C   LEU A 264       6.013 -16.525   2.595  1.00 92.56           C  
ANISOU 1614  C   LEU A 264    14241  14693   6234  -1488   -507   3576       C  
ATOM   1615  O   LEU A 264       5.261 -16.477   3.568  1.00 96.11           O  
ANISOU 1615  O   LEU A 264    14873  15319   6323  -1533   -304   3588       O  
ATOM   1616  CB  LEU A 264       5.080 -16.896   0.312  1.00111.96           C  
ANISOU 1616  CB  LEU A 264    16215  16880   9445  -1379   -276   3476       C  
ATOM   1617  CG  LEU A 264       3.859 -17.670   0.817  1.00113.59           C  
ANISOU 1617  CG  LEU A 264    16442  17184   9535  -1451     15   3644       C  
ATOM   1618  CD1 LEU A 264       2.629 -16.773   0.866  1.00115.23           C  
ANISOU 1618  CD1 LEU A 264    16677  17558   9549  -1415    334   3416       C  
ATOM   1619  CD2 LEU A 264       3.601 -18.904  -0.033  1.00111.94           C  
ANISOU 1619  CD2 LEU A 264    16009  16801   9723  -1469     76   3801       C  
ATOM   1620  N   THR A 265       7.186 -17.152   2.609  1.00 94.38           N  
ANISOU 1620  N   THR A 265    14464  14843   6555  -1514   -827   3782       N  
ATOM   1621  CA  THR A 265       7.719 -17.759   3.824  1.00 99.11           C  
ANISOU 1621  CA  THR A 265    15293  15556   6811  -1604   -992   4038       C  
ATOM   1622  C   THR A 265       7.886 -16.708   4.923  1.00102.33           C  
ANISOU 1622  C   THR A 265    15988  16154   6740  -1647  -1044   3861       C  
ATOM   1623  O   THR A 265       7.437 -16.899   6.059  1.00107.24           O  
ANISOU 1623  O   THR A 265    16857  16945   6947  -1724   -980   3983       O  
ATOM   1624  CB  THR A 265       9.069 -18.453   3.553  1.00113.04           C  
ANISOU 1624  CB  THR A 265    16975  17198   8778  -1596  -1365   4269       C  
ATOM   1625  OG1 THR A 265       8.862 -19.599   2.717  1.00111.65           O  
ANISOU 1625  OG1 THR A 265    16714  16978   8731  -1552  -1604   4072       O  
ATOM   1626  CG2 THR A 265       9.719 -18.896   4.850  1.00111.25           C  
ANISOU 1626  CG2 THR A 265    16513  16767   8990  -1545  -1306   4447       C  
ATOM   1627  N   VAL A 266       8.522 -15.593   4.569  1.00150.71           N  
ANISOU 1627  N   VAL A 266    22097  22244  12920  -1604  -1162   3573       N  
ATOM   1628  CA  VAL A 266       8.718 -14.483   5.496  1.00152.83           C  
ANISOU 1628  CA  VAL A 266    22654  22653  12760  -1641  -1220   3353       C  
ATOM   1629  C   VAL A 266       7.384 -13.947   6.017  1.00155.18           C  
ANISOU 1629  C   VAL A 266    23113  23096  12753  -1613   -825   3185       C  
ATOM   1630  O   VAL A 266       7.246 -13.648   7.204  1.00158.27           O  
ANISOU 1630  O   VAL A 266    23811  23663  12662  -1668   -799   3166       O  
ATOM   1631  CB  VAL A 266       9.518 -13.335   4.839  1.00124.08           C  
ANISOU 1631  CB  VAL A 266    18946  18904   9294  -1609  -1414   3072       C  
ATOM   1632  CG1 VAL A 266       9.612 -12.137   5.772  1.00126.58           C  
ANISOU 1632  CG1 VAL A 266    19547  19314   9235  -1612  -1335   2751       C  
ATOM   1633  CG2 VAL A 266      10.906 -13.815   4.444  1.00122.84           C  
ANISOU 1633  CG2 VAL A 266    18742  18704   9228  -1675  -1855   3227       C  
ATOM   1634  N   MET A 267       6.402 -13.841   5.126  1.00 95.26           N  
ANISOU 1634  N   MET A 267    15311  15443   5441  -1524   -517   3071       N  
ATOM   1635  CA  MET A 267       5.075 -13.357   5.498  1.00 96.09           C  
ANISOU 1635  CA  MET A 267    15498  15682   5330  -1464   -123   2887       C  
ATOM   1636  C   MET A 267       4.384 -14.297   6.481  1.00100.86           C  
ANISOU 1636  C   MET A 267    16209  16475   5639  -1533    124   3127       C  
ATOM   1637  O   MET A 267       3.781 -13.851   7.457  1.00103.66           O  
ANISOU 1637  O   MET A 267    16714  17006   5666  -1500    420   2997       O  
ATOM   1638  CB  MET A 267       4.200 -13.168   4.257  1.00138.79           C  
ANISOU 1638  CB  MET A 267    20616  20970  11149  -1347    100   2710       C  
ATOM   1639  CG  MET A 267       2.776 -12.743   4.574  1.00138.64           C  
ANISOU 1639  CG  MET A 267    20429  21026  11223  -1335    471   2830       C  
ATOM   1640  SD  MET A 267       1.727 -12.629   3.113  1.00138.65           S  
ANISOU 1640  SD  MET A 267    20221  20995  11465  -1173    787   2510       S  
ATOM   1641  CE  MET A 267       0.159 -12.195   3.861  1.00138.30           C  
ANISOU 1641  CE  MET A 267    19943  21049  11557  -1219   1142   2749       C  
ATOM   1642  N   VAL A 268       4.470 -15.597   6.213  1.00125.13           N  
ANISOU 1642  N   VAL A 268    19213  19509   8823  -1625      3   3481       N  
ATOM   1643  CA  VAL A 268       3.904 -16.605   7.102  1.00127.53           C  
ANISOU 1643  CA  VAL A 268    19631  19972   8855  -1723    195   3763       C  
ATOM   1644  C   VAL A 268       4.568 -16.528   8.473  1.00131.34           C  
ANISOU 1644  C   VAL A 268    20490  20649   8766  -1768    138   3746       C  
ATOM   1645  O   VAL A 268       3.906 -16.650   9.505  1.00134.89           O  
ANISOU 1645  O   VAL A 268    21057  21228   8968  -1777    385   3837       O  
ATOM   1646  CB  VAL A 268       4.056 -18.029   6.518  1.00105.52           C  
ANISOU 1646  CB  VAL A 268    16713  17045   6334  -1806     23   4152       C  
ATOM   1647  CG1 VAL A 268       3.723 -19.085   7.562  1.00109.74           C  
ANISOU 1647  CG1 VAL A 268    17346  17673   6677  -1885    232   4415       C  
ATOM   1648  CG2 VAL A 268       3.173 -18.196   5.289  1.00 99.67           C  
ANISOU 1648  CG2 VAL A 268    15621  16087   6162  -1745     81   4128       C  
ATOM   1649  N   HIS A 269       5.878 -16.302   8.477  1.00225.32           N  
ANISOU 1649  N   HIS A 269    32550  32518  20546  -1754   -180   3575       N  
ATOM   1650  CA  HIS A 269       6.624 -16.185   9.726  1.00229.47           C  
ANISOU 1650  CA  HIS A 269    33406  33160  20623  -1744   -264   3466       C  
ATOM   1651  C   HIS A 269       6.295 -14.897  10.477  1.00232.55           C  
ANISOU 1651  C   HIS A 269    33969  33726  20665  -1671    113   3181       C  
ATOM   1652  O   HIS A 269       6.496 -14.809  11.688  1.00236.69           O  
ANISOU 1652  O   HIS A 269    34676  34406  20852  -1651    319   3223       O  
ATOM   1653  CB  HIS A 269       8.126 -16.271   9.460  1.00258.31           C  
ANISOU 1653  CB  HIS A 269    37149  36722  24276  -1760   -699   3322       C  
ATOM   1654  CG  HIS A 269       8.559 -17.586   8.893  1.00258.60           C  
ANISOU 1654  CG  HIS A 269    37031  36616  24609  -1806  -1080   3594       C  
ATOM   1655  ND1 HIS A 269       7.691 -18.642   8.721  1.00256.21           N  
ANISOU 1655  ND1 HIS A 269    36425  36171  24752  -1807  -1101   3795       N  
ATOM   1656  CD2 HIS A 269       9.767 -18.015   8.457  1.00261.21           C  
ANISOU 1656  CD2 HIS A 269    37458  36927  24865  -1838  -1454   3690       C  
ATOM   1657  CE1 HIS A 269       8.346 -19.667   8.204  1.00257.41           C  
ANISOU 1657  CE1 HIS A 269    36499  36216  25091  -1821  -1456   3999       C  
ATOM   1658  NE2 HIS A 269       9.607 -19.314   8.039  1.00260.43           N  
ANISOU 1658  NE2 HIS A 269    37107  36677  25169  -1843  -1677   3945       N  
ATOM   1659  N   GLN A 270       5.791 -13.902   9.755  1.00118.93           N  
ANISOU 1659  N   GLN A 270    19520  19309   6358  -1618    210   2892       N  
ATOM   1660  CA  GLN A 270       5.426 -12.627  10.361  1.00121.78           C  
ANISOU 1660  CA  GLN A 270    20025  19811   6436  -1510    574   2585       C  
ATOM   1661  C   GLN A 270       4.149 -12.752  11.185  1.00120.74           C  
ANISOU 1661  C   GLN A 270    19687  19805   6383  -1466   1043   2700       C  
ATOM   1662  O   GLN A 270       3.078 -13.039  10.650  1.00120.26           O  
ANISOU 1662  O   GLN A 270    19479  19745   6468  -1321   1345   2464       O  
ATOM   1663  CB  GLN A 270       5.254 -11.553   9.284  1.00 20.00           C  
ATOM   1664  N   PRO A 297      -5.991 -13.602   7.520  1.00194.64           N  
ANISOU 1664  N   PRO A 297    27136  29558  17261   -963   3319   2553       N  
ATOM   1665  CA  PRO A 297      -7.319 -14.141   7.211  1.00193.57           C  
ANISOU 1665  CA  PRO A 297    26958  29471  17119  -1205   3298   2969       C  
ATOM   1666  C   PRO A 297      -7.266 -15.117   6.041  1.00189.99           C  
ANISOU 1666  C   PRO A 297    26104  28874  17210  -1296   3284   3155       C  
ATOM   1667  O   PRO A 297      -6.379 -15.970   5.991  1.00187.30           O  
ANISOU 1667  O   PRO A 297    25748  28337  17078  -1443   2995   3378       O  
ATOM   1668  CB  PRO A 297      -8.116 -12.895   6.816  1.00150.53           C  
ANISOU 1668  CB  PRO A 297    21587  24372  11236  -1227   3725   3061       C  
ATOM   1669  CG  PRO A 297      -7.421 -11.770   7.500  1.00153.33           C  
ANISOU 1669  CG  PRO A 297    21868  24852  11540   -972   4031   2702       C  
ATOM   1670  CD  PRO A 297      -5.968 -12.130   7.480  1.00151.92           C  
ANISOU 1670  CD  PRO A 297    21836  24425  11462   -816   3718   2371       C  
ATOM   1671  N   GLY A 298      -8.206 -14.987   5.111  1.00143.51           N  
ANISOU 1671  N   GLY A 298    19902  23082  11545  -1205   3585   3061       N  
ATOM   1672  CA  GLY A 298      -8.224 -15.822   3.925  1.00140.78           C  
ANISOU 1672  CA  GLY A 298    19179  22597  11716  -1285   3557   3192       C  
ATOM   1673  C   GLY A 298      -7.235 -15.328   2.888  1.00137.20           C  
ANISOU 1673  C   GLY A 298    18679  21822  11630  -1212   3191   3033       C  
ATOM   1674  O   GLY A 298      -6.980 -16.000   1.886  1.00134.53           O  
ANISOU 1674  O   GLY A 298    18191  21280  11645  -1335   2987   3200       O  
ATOM   1675  N   ARG A 299      -6.678 -14.146   3.135  1.00163.59           N  
ANISOU 1675  N   ARG A 299    22165  25115  14875  -1013   3114   2704       N  
ATOM   1676  CA  ARG A 299      -5.705 -13.549   2.229  1.00160.74           C  
ANISOU 1676  CA  ARG A 299    21788  24472  14812   -937   2782   2533       C  
ATOM   1677  C   ARG A 299      -4.452 -14.411   2.138  1.00158.32           C  
ANISOU 1677  C   ARG A 299    21651  23986  14516  -1084   2411   2716       C  
ATOM   1678  O   ARG A 299      -3.874 -14.562   1.066  1.00155.27           O  
ANISOU 1678  O   ARG A 299    21158  23365  14471  -1089   2151   2703       O  
ATOM   1679  CB  ARG A 299      -5.345 -12.128   2.675  1.00200.18           C  
ANISOU 1679  CB  ARG A 299    26964  29452  19642   -720   2769   2163       C  
ATOM   1680  CG  ARG A 299      -4.431 -11.395   1.703  1.00199.33           C  
ANISOU 1680  CG  ARG A 299    27187  29206  19342   -748   2415   2091       C  
ATOM   1681  CD  ARG A 299      -4.339  -9.904   2.005  1.00199.19           C  
ANISOU 1681  CD  ARG A 299    27270  29049  19363   -569   2295   1739       C  
ATOM   1682  NE  ARG A 299      -3.605  -9.622   3.235  1.00199.46           N  
ANISOU 1682  NE  ARG A 299    27663  29030  19091   -607   2026   1657       N  
ATOM   1683  CZ  ARG A 299      -4.144  -9.077   4.321  1.00198.31           C  
ANISOU 1683  CZ  ARG A 299    27605  28676  19067   -571   1730   1480       C  
ATOM   1684  NH1 ARG A 299      -5.428  -8.748   4.334  1.00196.83           N  
ANISOU 1684  NH1 ARG A 299    27188  28313  19286   -487   1676   1370       N  
ATOM   1685  NH2 ARG A 299      -3.397  -8.855   5.394  1.00198.70           N  
ANISOU 1685  NH2 ARG A 299    27971  28699  18827   -633   1480   1425       N  
ATOM   1686  N   VAL A 300      -4.042 -14.981   3.266  1.00110.36           N  
ANISOU 1686  N   VAL A 300    15839  18032   8063  -1193   2388   2889       N  
ATOM   1687  CA  VAL A 300      -2.880 -15.862   3.300  1.00108.47           C  
ANISOU 1687  CA  VAL A 300    15748  17641   7826  -1322   2038   3096       C  
ATOM   1688  C   VAL A 300      -3.152 -17.151   2.526  1.00106.06           C  
ANISOU 1688  C   VAL A 300    15210  17193   7895  -1463   1981   3383       C  
ATOM   1689  O   VAL A 300      -2.286 -17.648   1.803  1.00103.11           O  
ANISOU 1689  O   VAL A 300    14797  16587   7795  -1485   1681   3442       O  
ATOM   1690  CB  VAL A 300      -2.477 -16.204   4.747  1.00102.57           C  
ANISOU 1690  CB  VAL A 300    15326  17074   6571  -1419   2041   3257       C  
ATOM   1691  CG1 VAL A 300      -1.260 -17.117   4.763  1.00102.46           C  
ANISOU 1691  CG1 VAL A 300    15410  16910   6608  -1562   1698   3548       C  
ATOM   1692  CG2 VAL A 300      -2.202 -14.932   5.532  1.00104.38           C  
ANISOU 1692  CG2 VAL A 300    15846  17389   6423  -1296   2001   2961       C  
ATOM   1693  N   GLN A 301      -4.363 -17.682   2.677  1.00129.47           N  
ANISOU 1693  N   GLN A 301    18018  20295  10878  -1556   2276   3555       N  
ATOM   1694  CA  GLN A 301      -4.773 -18.887   1.962  1.00127.70           C  
ANISOU 1694  CA  GLN A 301    17593  19927  11000  -1711   2235   3824       C  
ATOM   1695  C   GLN A 301      -4.746 -18.661   0.453  1.00125.02           C  
ANISOU 1695  C   GLN A 301    16982  19382  11139  -1633   2143   3660       C  
ATOM   1696  O   GLN A 301      -4.109 -19.414  -0.290  1.00122.43           O  
ANISOU 1696  O   GLN A 301    16594  18811  11112  -1690   1906   3769       O  
ATOM   1697  CB  GLN A 301      -6.180 -19.311   2.393  1.00146.34           C  
ANISOU 1697  CB  GLN A 301    19831  22494  13278  -1854   2580   4042       C  
ATOM   1698  CG  GLN A 301      -6.341 -19.569   3.885  1.00149.41           C  
ANISOU 1698  CG  GLN A 301    20476  23056  13235  -1994   2659   4311       C  
ATOM   1699  CD  GLN A 301      -5.985 -20.991   4.286  1.00151.38           C  
ANISOU 1699  CD  GLN A 301    20684  23651  13181  -2003   3093   4312       C  
ATOM   1700  OE1 GLN A 301      -6.186 -21.391   5.433  1.00152.07           O  
ANISOU 1700  OE1 GLN A 301    20471  23830  13478  -1981   3351   4244       O  
ATOM   1701  NE2 GLN A 301      -5.458 -21.763   3.340  1.00152.49           N  
ANISOU 1701  NE2 GLN A 301    21122  23962  12854  -2023   3169   4376       N  
ATOM   1702  N   ALA A 302      -5.439 -17.615   0.011  1.00 98.04           N  
ANISOU 1702  N   ALA A 302    13412  16061   7777  -1488   2332   3397       N  
ATOM   1703  CA  ALA A 302      -5.500 -17.274  -1.407  1.00 95.85           C  
ANISOU 1703  CA  ALA A 302    12887  15612   7919  -1404   2253   3229       C  
ATOM   1704  C   ALA A 302      -4.115 -16.969  -1.968  1.00 93.30           C  
ANISOU 1704  C   ALA A 302    12671  15047   7731  -1331   1898   3111       C  
ATOM   1705  O   ALA A 302      -3.808 -17.315  -3.111  1.00 90.75           O  
ANISOU 1705  O   ALA A 302    12201  14516   7766  -1345   1736   3120       O  
ATOM   1706  CB  ALA A 302      -6.437 -16.095  -1.629  1.00138.19           C  
ANISOU 1706  CB  ALA A 302    18107  21128  13271  -1232   2498   2964       C  
ATOM   1707  N   LEU A 303      -3.282 -16.325  -1.157  1.00107.83           N  
ANISOU 1707  N   LEU A 303    14772  16926   9273  -1261   1782   3002       N  
ATOM   1708  CA  LEU A 303      -1.918 -16.002  -1.559  1.00105.80           C  
ANISOU 1708  CA  LEU A 303    14618  16476   9105  -1206   1449   2902       C  
ATOM   1709  C   LEU A 303      -1.089 -17.263  -1.773  1.00103.90           C  
ANISOU 1709  C   LEU A 303    14405  16071   9003  -1324   1201   3163       C  
ATOM   1710  O   LEU A 303      -0.412 -17.397  -2.790  1.00101.41           O  
ANISOU 1710  O   LEU A 303    13999  15552   8980  -1291    988   3127       O  
ATOM   1711  CB  LEU A 303      -1.246 -15.092  -0.529  1.00 92.44           C  
ANISOU 1711  CB  LEU A 303    13205  14878   7042  -1130   1378   2732       C  
ATOM   1712  CG  LEU A 303      -1.156 -13.606  -0.887  1.00 89.90           C  
ANISOU 1712  CG  LEU A 303    12877  14520   6763   -963   1384   2388       C  
ATOM   1713  CD1 LEU A 303      -2.486 -13.072  -1.398  1.00 90.29           C  
ANISOU 1713  CD1 LEU A 303    12727  14672   6906   -863   1707   2260       C  
ATOM   1714  CD2 LEU A 303      -0.679 -12.798   0.310  1.00 92.17           C  
ANISOU 1714  CD2 LEU A 303    13481  14886   6654   -918   1304   2231       C  
ATOM   1715  N   ARG A 304      -1.145 -18.181  -0.811  1.00 95.48           N  
ANISOU 1715  N   ARG A 304    13468  15089   7722  -1452   1234   3430       N  
ATOM   1716  CA  ARG A 304      -0.427 -19.448  -0.919  1.00 94.05           C  
ANISOU 1716  CA  ARG A 304    13318  14733   7684  -1548   1005   3697       C  
ATOM   1717  C   ARG A 304      -0.890 -20.216  -2.152  1.00 91.99           C  
ANISOU 1717  C   ARG A 304    12815  14286   7852  -1591   1024   3768       C  
ATOM   1718  O   ARG A 304      -0.071 -20.752  -2.913  1.00 89.76           O  
ANISOU 1718  O   ARG A 304    12496  13780   7831  -1577    794   3826       O  
ATOM   1719  CB  ARG A 304      -0.638 -20.296   0.337  1.00109.64           C  
ANISOU 1719  CB  ARG A 304    15485  16828   9347  -1685   1048   3994       C  
ATOM   1720  CG  ARG A 304       0.170 -21.584   0.352  1.00108.54           C  
ANISOU 1720  CG  ARG A 304    15442  16505   9295  -1741    749   4251       C  
ATOM   1721  CD  ARG A 304      -0.203 -22.467   1.533  1.00110.53           C  
ANISOU 1721  CD  ARG A 304    15928  16883   9186  -1864    753   4542       C  
ATOM   1722  NE  ARG A 304      -0.006 -21.796   2.815  1.00112.30           N  
ANISOU 1722  NE  ARG A 304    16329  17387   8954  -1854    917   4427       N  
ATOM   1723  CZ  ARG A 304       1.126 -21.827   3.511  1.00114.19           C  
ANISOU 1723  CZ  ARG A 304    16839  17763   8784  -1916    841   4584       C  
ATOM   1724  NH1 ARG A 304       2.174 -22.496   3.048  1.00115.05           N  
ANISOU 1724  NH1 ARG A 304    17058  17754   8904  -1988    590   4880       N  
ATOM   1725  NH2 ARG A 304       1.211 -21.188   4.670  1.00115.97           N  
ANISOU 1725  NH2 ARG A 304    17238  18241   8586  -1897   1009   4443       N  
ATOM   1726  N   ARG A 305      -2.208 -20.261  -2.343  1.00 88.25           N  
ANISOU 1726  N   ARG A 305    12172  13909   7449  -1638   1297   3753       N  
ATOM   1727  CA  ARG A 305      -2.789 -20.880  -3.528  1.00 86.26           C  
ANISOU 1727  CA  ARG A 305    11690  13494   7591  -1695   1316   3796       C  
ATOM   1728  C   ARG A 305      -2.188 -20.287  -4.797  1.00 81.27           C  
ANISOU 1728  C   ARG A 305    10944  12696   7241  -1557   1155   3552       C  
ATOM   1729  O   ARG A 305      -1.693 -21.018  -5.650  1.00 79.21           O  
ANISOU 1729  O   ARG A 305    10605  12212   7278  -1577   1004   3602       O  
ATOM   1730  CB  ARG A 305      -4.313 -20.723  -3.543  1.00104.17           C  
ANISOU 1730  CB  ARG A 305    13769  15936   9876  -1768   1633   3804       C  
ATOM   1731  CG  ARG A 305      -5.045 -21.644  -2.582  1.00108.56           C  
ANISOU 1731  CG  ARG A 305    14396  16645  10206  -1945   1816   4091       C  
ATOM   1732  CD  ARG A 305      -6.504 -21.815  -2.984  1.00110.46           C  
ANISOU 1732  CD  ARG A 305    14390  17063  10516  -2025   2130   4107       C  
ATOM   1733  NE  ARG A 305      -7.268 -20.577  -2.849  1.00110.63           N  
ANISOU 1733  NE  ARG A 305    14335  17312  10390  -1858   2336   3842       N  
ATOM   1734  CZ  ARG A 305      -8.031 -20.283  -1.802  1.00113.26           C  
ANISOU 1734  CZ  ARG A 305    14482  17888  10665  -1881   2656   3843       C  
ATOM   1735  NH1 ARG A 305      -8.138 -21.140  -0.796  1.00116.01           N  
ANISOU 1735  NH1 ARG A 305    14694  18296  11089  -2095   2805   4109       N  
ATOM   1736  NH2 ARG A 305      -8.691 -19.134  -1.762  1.00113.47           N  
ANISOU 1736  NH2 ARG A 305    14456  18094  10566  -1689   2830   3585       N  
ATOM   1737  N   GLY A 306      -2.217 -18.962  -4.903  1.00 70.12           N  
ANISOU 1737  N   GLY A 306     9539  11385   5718  -1416   1190   3290       N  
ATOM   1738  CA  GLY A 306      -1.656 -18.273  -6.053  1.00 65.44           C  
ANISOU 1738  CA  GLY A 306     8863  10650   5348  -1290   1039   3064       C  
ATOM   1739  C   GLY A 306      -0.189 -18.588  -6.278  1.00 63.94           C  
ANISOU 1739  C   GLY A 306     8772  10280   5241  -1269    742   3118       C  
ATOM   1740  O   GLY A 306       0.255 -18.722  -7.419  1.00 60.80           O  
ANISOU 1740  O   GLY A 306     8264   9703   5133  -1229    615   3062       O  
ATOM   1741  N   VAL A 307       0.559 -18.710  -5.186  1.00 63.19           N  
ANISOU 1741  N   VAL A 307     8882  10246   4883  -1292    633   3228       N  
ATOM   1742  CA  VAL A 307       1.977 -19.045  -5.252  1.00 62.60           C  
ANISOU 1742  CA  VAL A 307     8885  10031   4871  -1268    345   3308       C  
ATOM   1743  C   VAL A 307       2.189 -20.420  -5.872  1.00 62.54           C  
ANISOU 1743  C   VAL A 307     8798   9820   5146  -1319    261   3510       C  
ATOM   1744  O   VAL A 307       2.923 -20.560  -6.855  1.00 59.80           O  
ANISOU 1744  O   VAL A 307     8369   9300   5055  -1248    101   3463       O  
ATOM   1745  CB  VAL A 307       2.631 -19.018  -3.856  1.00 65.23           C  
ANISOU 1745  CB  VAL A 307     9451  10486   4847  -1306    240   3433       C  
ATOM   1746  CG1 VAL A 307       4.030 -19.615  -3.908  1.00 65.39           C  
ANISOU 1746  CG1 VAL A 307     9512  10367   4964  -1284    -66   3565       C  
ATOM   1747  CG2 VAL A 307       2.670 -17.600  -3.315  1.00 65.27           C  
ANISOU 1747  CG2 VAL A 307     9574  10656   4569  -1247    282   3201       C  
ATOM   1748  N   LEU A 308       1.544 -21.432  -5.294  1.00 68.05           N  
ANISOU 1748  N   LEU A 308     9527  10533   5795  -1442    380   3733       N  
ATOM   1749  CA  LEU A 308       1.670 -22.797  -5.802  1.00 68.59           C  
ANISOU 1749  CA  LEU A 308     9558  10381   6121  -1503    302   3934       C  
ATOM   1750  C   LEU A 308       1.216 -22.902  -7.260  1.00 64.95           C  
ANISOU 1750  C   LEU A 308     8902   9765   6011  -1477    338   3789       C  
ATOM   1751  O   LEU A 308       1.894 -23.522  -8.089  1.00 63.41           O  
ANISOU 1751  O   LEU A 308     8678   9349   6066  -1430    184   3813       O  
ATOM   1752  CB  LEU A 308       0.895 -23.782  -4.921  1.00131.07           C  
ANISOU 1752  CB  LEU A 308    17548  18343  13909  -1671    438   4205       C  
ATOM   1753  CG  LEU A 308       1.622 -24.357  -3.700  1.00132.57           C  
ANISOU 1753  CG  LEU A 308    17958  18563  13848  -1719    316   4468       C  
ATOM   1754  CD1 LEU A 308       2.925 -25.030  -4.114  1.00131.39           C  
ANISOU 1754  CD1 LEU A 308    17849  18160  13911  -1648     40   4594       C  
ATOM   1755  CD2 LEU A 308       1.876 -23.294  -2.644  1.00133.84           C  
ANISOU 1755  CD2 LEU A 308    18258  18961  13632  -1667    301   4375       C  
ATOM   1756  N   VAL A 309       0.078 -22.281  -7.565  1.00 78.43           N  
ANISOU 1756  N   VAL A 309    10479  11594   7727  -1497    539   3638       N  
ATOM   1757  CA  VAL A 309      -0.448 -22.245  -8.927  1.00 77.00           C  
ANISOU 1757  CA  VAL A 309    10114  11296   7846  -1479    566   3491       C  
ATOM   1758  C   VAL A 309       0.574 -21.678  -9.895  1.00 74.91           C  
ANISOU 1758  C   VAL A 309     9822  10913   7728  -1329    390   3306       C  
ATOM   1759  O   VAL A 309       0.941 -22.332 -10.864  1.00 73.50           O  
ANISOU 1759  O   VAL A 309     9591  10531   7802  -1310    288   3302       O  
ATOM   1760  CB  VAL A 309      -1.719 -21.381  -9.035  1.00 68.79           C  
ANISOU 1760  CB  VAL A 309     8926  10443   6769  -1487    791   3340       C  
ATOM   1761  CG1 VAL A 309      -2.083 -21.154 -10.498  1.00 67.23           C  
ANISOU 1761  CG1 VAL A 309     8554  10137   6854  -1432    765   3152       C  
ATOM   1762  CG2 VAL A 309      -2.863 -22.032  -8.310  1.00 70.70           C  
ANISOU 1762  CG2 VAL A 309     9124  10789   6950  -1656    988   3529       C  
ATOM   1763  N   LEU A 310       1.032 -20.461  -9.618  1.00 55.85           N  
ANISOU 1763  N   LEU A 310     7452   8624   5144  -1230    358   3153       N  
ATOM   1764  CA  LEU A 310       1.956 -19.768 -10.506  1.00 52.40           C  
ANISOU 1764  CA  LEU A 310     6978   8104   4829  -1107    207   2980       C  
ATOM   1765  C   LEU A 310       3.253 -20.549 -10.693  1.00 52.60           C  
ANISOU 1765  C   LEU A 310     7051   7963   4972  -1069     -1   3104       C  
ATOM   1766  O   LEU A 310       3.794 -20.612 -11.800  1.00 50.08           O  
ANISOU 1766  O   LEU A 310     6649   7504   4877   -997    -88   3022       O  
ATOM   1767  CB  LEU A 310       2.249 -18.366  -9.977  1.00 58.94           C  
ANISOU 1767  CB  LEU A 310     7877   9086   5433  -1037    196   2820       C  
ATOM   1768  CG  LEU A 310       2.980 -17.434 -10.941  1.00 57.40           C  
ANISOU 1768  CG  LEU A 310     7629   8821   5358   -935     65   2632       C  
ATOM   1769  CD1 LEU A 310       2.184 -17.263 -12.225  1.00 56.16           C  
ANISOU 1769  CD1 LEU A 310     7312   8583   5443   -904    140   2498       C  
ATOM   1770  CD2 LEU A 310       3.221 -16.100 -10.273  1.00 58.65           C  
ANISOU 1770  CD2 LEU A 310     7889   9113   5284   -893     53   2482       C  
ATOM   1771  N   ARG A 311       3.742 -21.145  -9.608  1.00 53.12           N  
ANISOU 1771  N   ARG A 311     7249   8053   4880  -1109    -77   3307       N  
ATOM   1772  CA  ARG A 311       4.923 -22.000  -9.676  1.00 53.95           C  
ANISOU 1772  CA  ARG A 311     7392   8007   5101  -1055   -277   3454       C  
ATOM   1773  C   ARG A 311       4.680 -23.140 -10.660  1.00 53.40           C  
ANISOU 1773  C   ARG A 311     7263   7706   5321  -1062   -269   3522       C  
ATOM   1774  O   ARG A 311       5.498 -23.398 -11.554  1.00 51.84           O  
ANISOU 1774  O   ARG A 311     7013   7352   5330   -957   -387   3489       O  
ATOM   1775  CB  ARG A 311       5.261 -22.563  -8.293  1.00 73.79           C  
ANISOU 1775  CB  ARG A 311    10067  10590   7380  -1107   -357   3688       C  
ATOM   1776  CG  ARG A 311       6.539 -23.388  -8.248  1.00 73.71           C  
ANISOU 1776  CG  ARG A 311    10090  10442   7476  -1030   -583   3859       C  
ATOM   1777  CD  ARG A 311       6.742 -24.016  -6.877  1.00 75.68           C  
ANISOU 1777  CD  ARG A 311    10508  10725   7523  -1107   -640   4141       C  
ATOM   1778  NE  ARG A 311       6.686 -23.027  -5.804  1.00 77.04           N  
ANISOU 1778  NE  ARG A 311    10797  11143   7331  -1168   -620   4123       N  
ATOM   1779  CZ  ARG A 311       6.810 -23.315  -4.512  1.00 78.96           C  
ANISOU 1779  CZ  ARG A 311    11211  11473   7318  -1231   -695   4344       C  
ATOM   1780  NH1 ARG A 311       7.001 -24.569  -4.124  1.00 79.70           N  
ANISOU 1780  NH1 ARG A 311    11370  11418   7496  -1242   -798   4618       N  
ATOM   1781  NH2 ARG A 311       6.743 -22.347  -3.608  1.00 80.33           N  
ANISOU 1781  NH2 ARG A 311    11509  11874   7141  -1282   -668   4290       N  
ATOM   1782  N   ALA A 312       3.539 -23.806 -10.498  1.00 53.69           N  
ANISOU 1782  N   ALA A 312     7307   7724   5368  -1190   -123   3610       N  
ATOM   1783  CA  ALA A 312       3.159 -24.914 -11.370  1.00 53.60           C  
ANISOU 1783  CA  ALA A 312     7264   7482   5619  -1233   -115   3667       C  
ATOM   1784  C   ALA A 312       3.045 -24.489 -12.834  1.00 49.51           C  
ANISOU 1784  C   ALA A 312     6612   6882   5318  -1160   -106   3429       C  
ATOM   1785  O   ALA A 312       3.413 -25.241 -13.736  1.00 48.64           O  
ANISOU 1785  O   ALA A 312     6500   6555   5427  -1105   -187   3421       O  
ATOM   1786  CB  ALA A 312       1.856 -25.541 -10.894  1.00 56.39           C  
ANISOU 1786  CB  ALA A 312     7631   7866   5931  -1419     44   3802       C  
ATOM   1787  N   VAL A 313       2.538 -23.281 -13.059  1.00 47.30           N  
ANISOU 1787  N   VAL A 313     6236   6771   4965  -1151     -8   3238       N  
ATOM   1788  CA  VAL A 313       2.365 -22.751 -14.407  1.00 43.66           C  
ANISOU 1788  CA  VAL A 313     5656   6257   4674  -1087     -4   3020       C  
ATOM   1789  C   VAL A 313       3.712 -22.467 -15.063  1.00 41.68           C  
ANISOU 1789  C   VAL A 313     5404   5923   4508   -936   -151   2942       C  
ATOM   1790  O   VAL A 313       3.926 -22.795 -16.233  1.00 39.84           O  
ANISOU 1790  O   VAL A 313     5130   5538   4472   -881   -189   2859       O  
ATOM   1791  CB  VAL A 313       1.512 -21.466 -14.402  1.00 42.02           C  
ANISOU 1791  CB  VAL A 313     5358   6250   4358  -1087    118   2846       C  
ATOM   1792  CG1 VAL A 313       1.434 -20.873 -15.802  1.00 38.45           C  
ANISOU 1792  CG1 VAL A 313     4801   5741   4065  -1010     93   2637       C  
ATOM   1793  CG2 VAL A 313       0.120 -21.759 -13.867  1.00 44.09           C  
ANISOU 1793  CG2 VAL A 313     5570   6609   4573  -1225    288   2915       C  
ATOM   1794  N   VAL A 314       4.618 -21.859 -14.304  1.00 47.42           N  
ANISOU 1794  N   VAL A 314     6177   6761   5079   -876   -234   2970       N  
ATOM   1795  CA  VAL A 314       5.961 -21.580 -14.801  1.00 46.21           C  
ANISOU 1795  CA  VAL A 314     5992   6563   5001   -747   -374   2921       C  
ATOM   1796  C   VAL A 314       6.695 -22.874 -15.144  1.00 47.19           C  
ANISOU 1796  C   VAL A 314     6140   6481   5308   -678   -468   3051       C  
ATOM   1797  O   VAL A 314       7.240 -23.019 -16.244  1.00 45.48           O  
ANISOU 1797  O   VAL A 314     5860   6150   5271   -580   -497   2955       O  
ATOM   1798  CB  VAL A 314       6.793 -20.771 -13.783  1.00 42.31           C  
ANISOU 1798  CB  VAL A 314     5546   6231   4299   -726   -472   2954       C  
ATOM   1799  CG1 VAL A 314       8.233 -20.638 -14.257  1.00 41.74           C  
ANISOU 1799  CG1 VAL A 314     5411   6117   4332   -609   -629   2948       C  
ATOM   1800  CG2 VAL A 314       6.173 -19.402 -13.562  1.00 40.97           C  
ANISOU 1800  CG2 VAL A 314     5370   6231   3965   -761   -389   2784       C  
ATOM   1801  N   ILE A 315       6.697 -23.815 -14.202  1.00 45.46           N  
ANISOU 1801  N   ILE A 315     6025   6208   5037   -721   -508   3269       N  
ATOM   1802  CA  ILE A 315       7.355 -25.101 -14.414  1.00 47.01           C  
ANISOU 1802  CA  ILE A 315     6266   6183   5412   -637   -603   3406       C  
ATOM   1803  C   ILE A 315       6.777 -25.831 -15.626  1.00 45.62           C  
ANISOU 1803  C   ILE A 315     6085   5793   5457   -646   -534   3322       C  
ATOM   1804  O   ILE A 315       7.521 -26.337 -16.469  1.00 44.90           O  
ANISOU 1804  O   ILE A 315     5979   5534   5548   -512   -590   3281       O  
ATOM   1805  CB  ILE A 315       7.258 -26.009 -13.168  1.00 51.32           C  
ANISOU 1805  CB  ILE A 315     6949   6694   5858   -692   -668   3682       C  
ATOM   1806  CG1 ILE A 315       7.982 -25.368 -11.983  1.00 53.15           C  
ANISOU 1806  CG1 ILE A 315     7230   6669   6295   -570   -782   3821       C  
ATOM   1807  CG2 ILE A 315       7.845 -27.383 -13.458  1.00 52.94           C  
ANISOU 1807  CG2 ILE A 315     7228   6918   5968   -882   -532   3764       C  
ATOM   1808  CD1 ILE A 315       7.901 -26.177 -10.705  1.00 52.54           C  
ANISOU 1808  CD1 ILE A 315     7055   6601   6306   -369   -914   3788       C  
ATOM   1809  N   ALA A 316       5.451 -25.868 -15.713  1.00 65.59           N  
ANISOU 1809  N   ALA A 316     8620   8335   7964   -801   -412   3289       N  
ATOM   1810  CA  ALA A 316       4.777 -26.525 -16.829  1.00 65.80           C  
ANISOU 1810  CA  ALA A 316     8647   8171   8182   -846   -365   3203       C  
ATOM   1811  C   ALA A 316       5.126 -25.865 -18.159  1.00 64.60           C  
ANISOU 1811  C   ALA A 316     8400   8013   8131   -735   -364   2965       C  
ATOM   1812  O   ALA A 316       5.327 -26.549 -19.161  1.00 65.13           O  
ANISOU 1812  O   ALA A 316     8498   7878   8370   -675   -387   2896       O  
ATOM   1813  CB  ALA A 316       3.272 -26.530 -16.618  1.00 45.52           C  
ANISOU 1813  CB  ALA A 316     6060   5671   5564  -1049   -243   3218       C  
ATOM   1814  N   PHE A 317       5.197 -24.537 -18.162  1.00 49.82           N  
ANISOU 1814  N   PHE A 317     6430   6356   6141   -708   -336   2840       N  
ATOM   1815  CA  PHE A 317       5.545 -23.796 -19.369  1.00 48.71           C  
ANISOU 1815  CA  PHE A 317     6203   6232   6070   -615   -333   2634       C  
ATOM   1816  C   PHE A 317       6.954 -24.157 -19.817  1.00 48.96           C  
ANISOU 1816  C   PHE A 317     6233   6163   6207   -442   -420   2641       C  
ATOM   1817  O   PHE A 317       7.178 -24.479 -20.986  1.00 49.23           O  
ANISOU 1817  O   PHE A 317     6260   6069   6374   -364   -411   2527       O  
ATOM   1818  CB  PHE A 317       5.434 -22.287 -19.131  1.00 54.60           C  
ANISOU 1818  CB  PHE A 317     6869   7211   6665   -623   -302   2528       C  
ATOM   1819  CG  PHE A 317       5.573 -21.461 -20.382  1.00 53.51           C  
ANISOU 1819  CG  PHE A 317     6651   7093   6588   -561   -289   2330       C  
ATOM   1820  CD1 PHE A 317       6.822 -21.103 -20.862  1.00 53.03           C  
ANISOU 1820  CD1 PHE A 317     6547   7039   6562   -437   -351   2284       C  
ATOM   1821  CD2 PHE A 317       4.452 -21.040 -21.076  1.00 53.19           C  
ANISOU 1821  CD2 PHE A 317     6568   7076   6567   -632   -217   2207       C  
ATOM   1822  CE1 PHE A 317       6.951 -20.341 -22.008  1.00 52.21           C  
ANISOU 1822  CE1 PHE A 317     6380   6959   6497   -394   -332   2122       C  
ATOM   1823  CE2 PHE A 317       4.574 -20.279 -22.224  1.00 52.34           C  
ANISOU 1823  CE2 PHE A 317     6403   6984   6499   -579   -216   2043       C  
ATOM   1824  CZ  PHE A 317       5.825 -19.929 -22.689  1.00 51.81           C  
ANISOU 1824  CZ  PHE A 317     6314   6918   6452   -464   -268   2003       C  
ATOM   1825  N   VAL A 318       7.897 -24.106 -18.881  1.00 46.64           N  
ANISOU 1825  N   VAL A 318     5940   5938   5843   -378   -503   2775       N  
ATOM   1826  CA  VAL A 318       9.288 -24.432 -19.175  1.00 47.20           C  
ANISOU 1826  CA  VAL A 318     5970   5943   6020   -201   -588   2809       C  
ATOM   1827  C   VAL A 318       9.430 -25.850 -19.724  1.00 48.83           C  
ANISOU 1827  C   VAL A 318     6261   5880   6414   -116   -594   2852       C  
ATOM   1828  O   VAL A 318      10.026 -26.054 -20.783  1.00 49.39           O  
ANISOU 1828  O   VAL A 318     6296   5856   6614     20   -577   2741       O  
ATOM   1829  CB  VAL A 318      10.181 -24.278 -17.930  1.00 40.42           C  
ANISOU 1829  CB  VAL A 318     5100   5199   5057   -166   -706   2984       C  
ATOM   1830  CG1 VAL A 318      11.587 -24.779 -18.220  1.00 41.45           C  
ANISOU 1830  CG1 VAL A 318     5157   5263   5332     29   -796   3042       C  
ATOM   1831  CG2 VAL A 318      10.211 -22.827 -17.476  1.00 39.45           C  
ANISOU 1831  CG2 VAL A 318     4918   5322   4749   -241   -716   2914       C  
ATOM   1832  N   VAL A 319       8.869 -26.820 -19.006  1.00 51.82           N  
ANISOU 1832  N   VAL A 319     6764   6127   6797   -199   -611   3011       N  
ATOM   1833  CA  VAL A 319       8.959 -28.223 -19.404  1.00 53.61           C  
ANISOU 1833  CA  VAL A 319     7110   6057   7202   -129   -634   3068       C  
ATOM   1834  C   VAL A 319       8.316 -28.487 -20.765  1.00 52.54           C  
ANISOU 1834  C   VAL A 319     7011   5773   7179   -156   -557   2868       C  
ATOM   1835  O   VAL A 319       8.904 -29.153 -21.618  1.00 53.18           O  
ANISOU 1835  O   VAL A 319     7139   5660   7406     -5   -564   2796       O  
ATOM   1836  CB  VAL A 319       8.320 -29.155 -18.351  1.00 46.55           C  
ANISOU 1836  CB  VAL A 319     6360   5047   6281   -259   -668   3295       C  
ATOM   1837  CG1 VAL A 319       8.258 -30.586 -18.869  1.00 48.59           C  
ANISOU 1837  CG1 VAL A 319     6769   4956   6736   -202   -698   3341       C  
ATOM   1838  CG2 VAL A 319       9.099 -29.093 -17.047  1.00 49.17           C  
ANISOU 1838  CG2 VAL A 319     6684   5508   6489   -218   -767   3506       C  
ATOM   1839  N   CYS A 320       7.113 -27.958 -20.967  1.00 67.09           N  
ANISOU 1839  N   CYS A 320     8832   7713   8948   -338   -486   2776       N  
ATOM   1840  CA  CYS A 320       6.388 -28.184 -22.214  1.00 67.59           C  
ANISOU 1840  CA  CYS A 320     8929   7652   9099   -394   -439   2597       C  
ATOM   1841  C   CYS A 320       7.060 -27.522 -23.414  1.00 67.29           C  
ANISOU 1841  C   CYS A 320     8814   7669   9085   -248   -411   2390       C  
ATOM   1842  O   CYS A 320       7.120 -28.103 -24.497  1.00 68.74           O  
ANISOU 1842  O   CYS A 320     9074   7679   9367   -198   -399   2258       O  
ATOM   1843  CB  CYS A 320       4.941 -27.701 -22.099  1.00 46.98           C  
ANISOU 1843  CB  CYS A 320     6277   5163   6410   -619   -380   2569       C  
ATOM   1844  SG  CYS A 320       3.895 -28.703 -21.020  1.00 48.22           S  
ANISOU 1844  SG  CYS A 320     6536   5209   6575   -838   -381   2790       S  
ATOM   1845  N   TRP A 321       7.567 -26.309 -23.221  1.00 40.57           N  
ANISOU 1845  N   TRP A 321     5293   4522   5598   -191   -402   2363       N  
ATOM   1846  CA  TRP A 321       8.118 -25.542 -24.335  1.00 40.21           C  
ANISOU 1846  CA  TRP A 321     5164   4559   5555    -88   -366   2187       C  
ATOM   1847  C   TRP A 321       9.613 -25.764 -24.575  1.00 41.40           C  
ANISOU 1847  C   TRP A 321     5269   4680   5782    134   -383   2201       C  
ATOM   1848  O   TRP A 321      10.155 -25.305 -25.581  1.00 41.84           O  
ANISOU 1848  O   TRP A 321     5267   4775   5853    230   -334   2063       O  
ATOM   1849  CB  TRP A 321       7.818 -24.049 -24.166  1.00 42.46           C  
ANISOU 1849  CB  TRP A 321     5330   5102   5701   -166   -344   2129       C  
ATOM   1850  CG  TRP A 321       6.386 -23.701 -24.428  1.00 41.69           C  
ANISOU 1850  CG  TRP A 321     5241   5041   5558   -332   -303   2048       C  
ATOM   1851  CD1 TRP A 321       5.401 -23.519 -23.500  1.00 41.05           C  
ANISOU 1851  CD1 TRP A 321     5152   5047   5399   -476   -286   2127       C  
ATOM   1852  CD2 TRP A 321       5.773 -23.499 -25.708  1.00 41.86           C  
ANISOU 1852  CD2 TRP A 321     5268   5029   5609   -364   -273   1878       C  
ATOM   1853  NE1 TRP A 321       4.215 -23.211 -24.122  1.00 40.80           N  
ANISOU 1853  NE1 TRP A 321     5095   5042   5367   -587   -247   2021       N  
ATOM   1854  CE2 TRP A 321       4.417 -23.195 -25.478  1.00 41.18           C  
ANISOU 1854  CE2 TRP A 321     5156   5012   5479   -527   -253   1871       C  
ATOM   1855  CE3 TRP A 321       6.240 -23.546 -27.027  1.00 42.88           C  
ANISOU 1855  CE3 TRP A 321     5421   5086   5785   -268   -259   1736       C  
ATOM   1856  CZ2 TRP A 321       3.523 -22.940 -26.516  1.00 41.28           C  
ANISOU 1856  CZ2 TRP A 321     5155   5022   5508   -598   -246   1735       C  
ATOM   1857  CZ3 TRP A 321       5.350 -23.290 -28.056  1.00 43.02           C  
ANISOU 1857  CZ3 TRP A 321     5455   5097   5793   -348   -249   1596       C  
ATOM   1858  CH2 TRP A 321       4.008 -22.991 -27.794  1.00 42.11           C  
ANISOU 1858  CH2 TRP A 321     5304   5049   5648   -513   -256   1601       C  
ATOM   1859  N   LEU A 322      10.276 -26.467 -23.662  1.00 51.80           N  
ANISOU 1859  N   LEU A 322     6601   5939   7143    217   -449   2378       N  
ATOM   1860  CA  LEU A 322      11.710 -26.723 -23.816  1.00 53.13           C  
ANISOU 1860  CA  LEU A 322     6691   6094   7403    444   -470   2415       C  
ATOM   1861  C   LEU A 322      12.084 -27.561 -25.053  1.00 55.67           C  
ANISOU 1861  C   LEU A 322     7085   6203   7864    613   -406   2288       C  
ATOM   1862  O   LEU A 322      12.923 -27.133 -25.842  1.00 56.37           O  
ANISOU 1862  O   LEU A 322     7067   6377   7975    752   -345   2187       O  
ATOM   1863  CB  LEU A 322      12.327 -27.315 -22.540  1.00 46.90           C  
ANISOU 1863  CB  LEU A 322     5899   5288   6636    505   -578   2650       C  
ATOM   1864  CG  LEU A 322      13.843 -27.533 -22.570  1.00 48.38           C  
ANISOU 1864  CG  LEU A 322     5966   5480   6936    753   -616   2716       C  
ATOM   1865  CD1 LEU A 322      14.567 -26.218 -22.816  1.00 47.13           C  
ANISOU 1865  CD1 LEU A 322     5596   5608   6704    762   -622   2681       C  
ATOM   1866  CD2 LEU A 322      14.327 -28.181 -21.284  1.00 49.30           C  
ANISOU 1866  CD2 LEU A 322     6127   5505   7100    822   -741   2959       C  
ATOM   1867  N   PRO A 323      11.473 -28.750 -25.230  1.00 60.67           N  
ANISOU 1867  N   PRO A 323     7909   6558   8586    597   -414   2290       N  
ATOM   1868  CA  PRO A 323      11.867 -29.549 -26.398  1.00 63.51           C  
ANISOU 1868  CA  PRO A 323     8371   6699   9063    770   -354   2146       C  
ATOM   1869  C   PRO A 323      11.421 -28.914 -27.714  1.00 63.73           C  
ANISOU 1869  C   PRO A 323     8401   6792   9022    720   -263   1909       C  
ATOM   1870  O   PRO A 323      12.042 -29.148 -28.751  1.00 66.00           O  
ANISOU 1870  O   PRO A 323     8710   7014   9353    896   -185   1770       O  
ATOM   1871  CB  PRO A 323      11.125 -30.875 -26.183  1.00 55.83           C  
ANISOU 1871  CB  PRO A 323     7630   5405   8179    695   -406   2201       C  
ATOM   1872  CG  PRO A 323      10.733 -30.881 -24.746  1.00 54.16           C  
ANISOU 1872  CG  PRO A 323     7400   5254   7922    559   -494   2438       C  
ATOM   1873  CD  PRO A 323      10.474 -29.456 -24.412  1.00 51.28           C  
ANISOU 1873  CD  PRO A 323     6859   5228   7395    427   -475   2427       C  
ATOM   1874  N   TYR A 324      10.351 -28.127 -27.662  1.00 46.77           N  
ANISOU 1874  N   TYR A 324     6232   4778   6760    492   -270   1868       N  
ATOM   1875  CA  TYR A 324       9.816 -27.450 -28.840  1.00 46.79           C  
ANISOU 1875  CA  TYR A 324     6235   4858   6684    423   -211   1668       C  
ATOM   1876  C   TYR A 324      10.858 -26.549 -29.493  1.00 46.83           C  
ANISOU 1876  C   TYR A 324     6090   5060   6642    567   -136   1595       C  
ATOM   1877  O   TYR A 324      11.101 -26.638 -30.698  1.00 48.97           O  
ANISOU 1877  O   TYR A 324     6411   5291   6903    658    -60   1434       O  
ATOM   1878  CB  TYR A 324       8.576 -26.636 -28.456  1.00 53.20           C  
ANISOU 1878  CB  TYR A 324     7007   5813   7396    177   -242   1679       C  
ATOM   1879  CG  TYR A 324       8.055 -25.715 -29.540  1.00 52.78           C  
ANISOU 1879  CG  TYR A 324     6926   5878   7253    107   -204   1505       C  
ATOM   1880  CD1 TYR A 324       7.227 -26.191 -30.547  1.00 54.66           C  
ANISOU 1880  CD1 TYR A 324     7301   5967   7500     37   -209   1359       C  
ATOM   1881  CD2 TYR A 324       8.377 -24.364 -29.543  1.00 50.66           C  
ANISOU 1881  CD2 TYR A 324     6504   5859   6885     99   -181   1494       C  
ATOM   1882  CE1 TYR A 324       6.742 -25.350 -31.534  1.00 54.45           C  
ANISOU 1882  CE1 TYR A 324     7254   6055   7381    -28   -194   1216       C  
ATOM   1883  CE2 TYR A 324       7.898 -23.517 -30.523  1.00 50.31           C  
ANISOU 1883  CE2 TYR A 324     6446   5911   6761     38   -158   1356       C  
ATOM   1884  CZ  TYR A 324       7.081 -24.014 -31.516  1.00 52.22           C  
ANISOU 1884  CZ  TYR A 324     6818   6019   7007    -20   -166   1222       C  
ATOM   1885  OH  TYR A 324       6.604 -23.168 -32.492  1.00 52.02           O  
ANISOU 1885  OH  TYR A 324     6783   6095   6890    -79   -161   1100       O  
ATOM   1886  N   HIS A 325      11.475 -25.689 -28.690  1.00 49.95           N  
ANISOU 1886  N   HIS A 325     6309   5670   6998    575   -160   1716       N  
ATOM   1887  CA  HIS A 325      12.488 -24.766 -29.188  1.00 49.81           C  
ANISOU 1887  CA  HIS A 325     6127   5855   6945    676   -102   1680       C  
ATOM   1888  C   HIS A 325      13.757 -25.493 -29.623  1.00 52.59           C  
ANISOU 1888  C   HIS A 325     6438   6137   7408    934    -38   1682       C  
ATOM   1889  O   HIS A 325      14.467 -25.035 -30.519  1.00 53.79           O  
ANISOU 1889  O   HIS A 325     6501   6396   7539   1036     60   1593       O  
ATOM   1890  CB  HIS A 325      12.817 -23.705 -28.136  1.00 68.35           C  
ANISOU 1890  CB  HIS A 325     8312   8430   9226    594   -169   1813       C  
ATOM   1891  CG  HIS A 325      11.708 -22.729 -27.897  1.00 65.79           C  
ANISOU 1891  CG  HIS A 325     8004   8213   8780    382   -197   1777       C  
ATOM   1892  ND1 HIS A 325      11.466 -21.659 -28.732  1.00 65.13           N  
ANISOU 1892  ND1 HIS A 325     7892   8239   8615    317   -151   1650       N  
ATOM   1893  CD2 HIS A 325      10.778 -22.658 -26.916  1.00 63.98           C  
ANISOU 1893  CD2 HIS A 325     7814   7999   8496    235   -259   1855       C  
ATOM   1894  CE1 HIS A 325      10.433 -20.973 -28.276  1.00 62.90           C  
ANISOU 1894  CE1 HIS A 325     7625   8024   8249    154   -190   1647       C  
ATOM   1895  NE2 HIS A 325       9.997 -21.558 -27.176  1.00 62.27           N  
ANISOU 1895  NE2 HIS A 325     7582   7898   8180    103   -244   1765       N  
ATOM   1896  N   VAL A 326      14.037 -26.624 -28.985  1.00 40.26           N  
ANISOU 1896  N   VAL A 326     4937   4397   5964   1045    -88   1793       N  
ATOM   1897  CA  VAL A 326      15.191 -27.439 -29.348  1.00 43.08           C  
ANISOU 1897  CA  VAL A 326     5258   4658   6450   1324    -29   1801       C  
ATOM   1898  C   VAL A 326      15.020 -27.998 -30.758  1.00 46.12           C  
ANISOU 1898  C   VAL A 326     5798   4883   6843   1432     95   1583       C  
ATOM   1899  O   VAL A 326      15.976 -28.067 -31.532  1.00 48.17           O  
ANISOU 1899  O   VAL A 326     5969   5203   7128   1636    215   1510       O  
ATOM   1900  CB  VAL A 326      15.410 -28.593 -28.344  1.00 40.11           C  
ANISOU 1900  CB  VAL A 326     4957   4078   6205   1421   -127   1971       C  
ATOM   1901  CG1 VAL A 326      16.499 -29.539 -28.833  1.00 43.42           C  
ANISOU 1901  CG1 VAL A 326     5371   4347   6777   1742    -56   1952       C  
ATOM   1902  CG2 VAL A 326      15.761 -28.041 -26.972  1.00 41.14           C  
ANISOU 1902  CG2 VAL A 326     4928   4393   6310   1349   -251   2193       C  
ATOM   1903  N   ARG A 327      13.791 -28.377 -31.092  1.00 57.63           N  
ANISOU 1903  N   ARG A 327     7482   6147   8267   1286     67   1479       N  
ATOM   1904  CA  ARG A 327      13.494 -28.945 -32.401  1.00 60.72           C  
ANISOU 1904  CA  ARG A 327     8065   6366   8637   1351    155   1258       C  
ATOM   1905  C   ARG A 327      13.637 -27.916 -33.521  1.00 61.03           C  
ANISOU 1905  C   ARG A 327     8025   6629   8535   1330    262   1111       C  
ATOM   1906  O   ARG A 327      14.172 -28.217 -34.588  1.00 63.99           O  
ANISOU 1906  O   ARG A 327     8454   6968   8889   1503    389    964       O  
ATOM   1907  CB  ARG A 327      12.083 -29.533 -32.421  1.00 51.62           C  
ANISOU 1907  CB  ARG A 327     7153   4984   7475   1143     66   1197       C  
ATOM   1908  CG  ARG A 327      11.721 -30.199 -33.735  1.00 54.91           C  
ANISOU 1908  CG  ARG A 327     7799   5210   7853   1177    123    957       C  
ATOM   1909  CD  ARG A 327      10.275 -30.644 -33.746  1.00 54.85           C  
ANISOU 1909  CD  ARG A 327     7995   5008   7837    923      8    911       C  
ATOM   1910  NE  ARG A 327       9.359 -29.543 -33.464  1.00 51.62           N  
ANISOU 1910  NE  ARG A 327     7461   4821   7332    660    -56    968       N  
ATOM   1911  CZ  ARG A 327       8.956 -28.656 -34.367  1.00 51.24           C  
ANISOU 1911  CZ  ARG A 327     7373   4949   7146    563    -31    844       C  
ATOM   1912  NH1 ARG A 327       9.391 -28.733 -35.617  1.00 53.96           N  
ANISOU 1912  NH1 ARG A 327     7801   5289   7412    688     58    661       N  
ATOM   1913  NH2 ARG A 327       8.117 -27.688 -34.022  1.00 48.17           N  
ANISOU 1913  NH2 ARG A 327     6868   4743   6692    351    -92    908       N  
ATOM   1914  N   ARG A 328      13.149 -26.703 -33.277  1.00 53.54           N  
ANISOU 1914  N   ARG A 328     6960   5903   7481   1123    215   1155       N  
ATOM   1915  CA  ARG A 328      13.206 -25.645 -34.281  1.00 53.66           C  
ANISOU 1915  CA  ARG A 328     6906   6126   7357   1076    296   1047       C  
ATOM   1916  C   ARG A 328      14.638 -25.168 -34.501  1.00 54.42           C  
ANISOU 1916  C   ARG A 328     6792   6416   7468   1260    411   1091       C  
ATOM   1917  O   ARG A 328      15.004 -24.758 -35.602  1.00 56.43           O  
ANISOU 1917  O   ARG A 328     7044   6761   7637   1330    538    973       O  
ATOM   1918  CB  ARG A 328      12.295 -24.479 -33.891  1.00 56.53           C  
ANISOU 1918  CB  ARG A 328     7203   6651   7625    825    206   1095       C  
ATOM   1919  CG  ARG A 328      10.820 -24.839 -33.903  1.00 56.20           C  
ANISOU 1919  CG  ARG A 328     7341   6465   7547    638    124   1014       C  
ATOM   1920  CD  ARG A 328       9.957 -23.735 -33.320  1.00 52.45           C  
ANISOU 1920  CD  ARG A 328     6779   6134   7016    426     36   1095       C  
ATOM   1921  NE  ARG A 328       9.817 -22.589 -34.213  1.00 51.81           N  
ANISOU 1921  NE  ARG A 328     6658   6219   6809    341     54   1010       N  
ATOM   1922  CZ  ARG A 328      10.105 -21.337 -33.872  1.00 49.72           C  
ANISOU 1922  CZ  ARG A 328     6238   6166   6488    328     70   1069       C  
ATOM   1923  NH1 ARG A 328      10.555 -21.065 -32.654  1.00 48.14           N  
ANISOU 1923  NH1 ARG A 328     5897   6053   6340    386     64   1206       N  
ATOM   1924  NH2 ARG A 328       9.943 -20.355 -34.748  1.00 49.27           N  
ANISOU 1924  NH2 ARG A 328     6174   6225   6320    250     77    998       N  
ATOM   1925  N   LEU A 329      15.443 -25.224 -33.445  1.00 54.52           N  
ANISOU 1925  N   LEU A 329     6624   6506   7583   1330    364   1272       N  
ATOM   1926  CA  LEU A 329      16.868 -24.950 -33.565  1.00 55.41           C  
ANISOU 1926  CA  LEU A 329     6506   6798   7748   1513    459   1340       C  
ATOM   1927  C   LEU A 329      17.525 -26.087 -34.338  1.00 59.33           C  
ANISOU 1927  C   LEU A 329     7073   7141   8328   1798    596   1242       C  
ATOM   1928  O   LEU A 329      18.435 -25.867 -35.134  1.00 61.34           O  
ANISOU 1928  O   LEU A 329     7208   7534   8564   1949    754   1190       O  
ATOM   1929  CB  LEU A 329      17.513 -24.805 -32.185  1.00 46.10           C  
ANISOU 1929  CB  LEU A 329     5131   5718   6668   1518    340   1563       C  
ATOM   1930  CG  LEU A 329      17.200 -23.529 -31.399  1.00 42.44           C  
ANISOU 1930  CG  LEU A 329     4568   5444   6113   1272    221   1660       C  
ATOM   1931  CD1 LEU A 329      17.827 -23.580 -30.013  1.00 40.87           C  
ANISOU 1931  CD1 LEU A 329     4224   5309   5996   1287     88   1869       C  
ATOM   1932  CD2 LEU A 329      17.677 -22.300 -32.158  1.00 42.21           C  
ANISOU 1932  CD2 LEU A 329     4395   5654   5990   1204    301   1619       C  
ATOM   1933  N   MET A 330      17.046 -27.303 -34.097  1.00 58.73           N  
ANISOU 1933  N   MET A 330     7199   6771   8343   1871    542   1219       N  
ATOM   1934  CA  MET A 330      17.549 -28.491 -34.777  1.00 62.39           C  
ANISOU 1934  CA  MET A 330     7790   7022   8892   2150    658   1105       C  
ATOM   1935  C   MET A 330      17.208 -28.449 -36.265  1.00 65.01           C  
ANISOU 1935  C   MET A 330     8295   7330   9076   2163    802    857       C  
ATOM   1936  O   MET A 330      17.936 -28.991 -37.097  1.00 67.96           O  
ANISOU 1936  O   MET A 330     8681   7679   9460   2416    973    746       O  
ATOM   1937  CB  MET A 330      16.962 -29.750 -34.130  1.00 76.94           C  
ANISOU 1937  CB  MET A 330     9862   8519  10852   2166    538   1134       C  
ATOM   1938  CG  MET A 330      17.337 -31.059 -34.805  1.00 80.77           C  
ANISOU 1938  CG  MET A 330    10546   8714  11429   2446    637    993       C  
ATOM   1939  SD  MET A 330      16.583 -32.492 -34.009  1.00 81.25           S  
ANISOU 1939  SD  MET A 330    10922   8333  11617   2394    471   1030       S  
ATOM   1940  CE  MET A 330      17.174 -33.819 -35.058  1.00 86.00           C  
ANISOU 1940  CE  MET A 330    11809   8604  12262   2697    618    771       C  
ATOM   1941  N   PHE A 331      16.098 -27.793 -36.589  1.00 65.80           N  
ANISOU 1941  N   PHE A 331     8523   7445   9030   1894    732    776       N  
ATOM   1942  CA  PHE A 331      15.615 -27.712 -37.964  1.00 68.21           C  
ANISOU 1942  CA  PHE A 331     9017   7731   9167   1861    826    551       C  
ATOM   1943  C   PHE A 331      16.568 -26.952 -38.882  1.00 69.56           C  
ANISOU 1943  C   PHE A 331     9027   8172   9231   1974   1016    508       C  
ATOM   1944  O   PHE A 331      16.703 -27.288 -40.058  1.00 72.68           O  
ANISOU 1944  O   PHE A 331     9565   8521   9529   2116   1168    326       O  
ATOM   1945  CB  PHE A 331      14.226 -27.063 -37.999  1.00 52.46           C  
ANISOU 1945  CB  PHE A 331     7129   5750   7053   1541    686    518       C  
ATOM   1946  CG  PHE A 331      13.676 -26.868 -39.387  1.00 54.75           C  
ANISOU 1946  CG  PHE A 331     7606   6045   7153   1479    745    308       C  
ATOM   1947  CD1 PHE A 331      13.018 -27.900 -40.035  1.00 57.36           C  
ANISOU 1947  CD1 PHE A 331     8242   6100   7453   1495    725    122       C  
ATOM   1948  CD2 PHE A 331      13.805 -25.650 -40.037  1.00 54.09           C  
ANISOU 1948  CD2 PHE A 331     7410   6231   6913   1392    806    302       C  
ATOM   1949  CE1 PHE A 331      12.507 -27.725 -41.304  1.00 59.41           C  
ANISOU 1949  CE1 PHE A 331     8688   6370   7516   1428    758    -72       C  
ATOM   1950  CE2 PHE A 331      13.296 -25.469 -41.307  1.00 55.94           C  
ANISOU 1950  CE2 PHE A 331     7827   6476   6953   1333    847    125       C  
ATOM   1951  CZ  PHE A 331      12.646 -26.509 -41.941  1.00 58.71           C  
ANISOU 1951  CZ  PHE A 331     8480   6567   7261   1351    820    -65       C  
ATOM   1952  N   CYS A 332      17.232 -25.934 -38.345  1.00 61.42           N  
ANISOU 1952  N   CYS A 332     7710   7422   8206   1900   1010    675       N  
ATOM   1953  CA  CYS A 332      18.037 -25.044 -39.174  1.00 62.27           C  
ANISOU 1953  CA  CYS A 332     7652   7807   8202   1938   1175    664       C  
ATOM   1954  C   CYS A 332      19.538 -25.096 -38.890  1.00 62.99           C  
ANISOU 1954  C   CYS A 332     7453   8059   8423   2176   1307    785       C  
ATOM   1955  O   CYS A 332      20.336 -24.605 -39.687  1.00 64.59           O  
ANISOU 1955  O   CYS A 332     7532   8463   8549   2268   1495    756       O  
ATOM   1956  CB  CYS A 332      17.532 -23.605 -39.045  1.00 68.79           C  
ANISOU 1956  CB  CYS A 332     8376   8843   8920   1654   1078    751       C  
ATOM   1957  SG  CYS A 332      17.477 -22.980 -37.351  1.00 64.11           S  
ANISOU 1957  SG  CYS A 332     7564   8332   8464   1508    880    993       S  
ATOM   1958  N   TYR A 333      19.924 -25.688 -37.763  1.00 70.91           N  
ANISOU 1958  N   TYR A 333     8337   8985   9620   2273   1208    932       N  
ATOM   1959  CA  TYR A 333      21.336 -25.714 -37.378  1.00 71.33           C  
ANISOU 1959  CA  TYR A 333     8075   9208   9819   2490   1297   1076       C  
ATOM   1960  C   TYR A 333      22.095 -26.956 -37.844  1.00 74.75           C  
ANISOU 1960  C   TYR A 333     8554   9494  10353   2858   1469    978       C  
ATOM   1961  O   TYR A 333      23.326 -26.952 -37.896  1.00 75.97           O  
ANISOU 1961  O   TYR A 333     8444   9833  10589   3074   1624   1042       O  
ATOM   1962  CB  TYR A 333      21.501 -25.519 -35.868  1.00 82.91           C  
ANISOU 1962  CB  TYR A 333     9355  10712  11433   2414   1092   1309       C  
ATOM   1963  CG  TYR A 333      21.697 -24.075 -35.468  1.00 80.06           C  
ANISOU 1963  CG  TYR A 333     8754  10649  11017   2183   1019   1453       C  
ATOM   1964  CD1 TYR A 333      22.962 -23.502 -35.474  1.00 80.53           C  
ANISOU 1964  CD1 TYR A 333     8476  10978  11141   2267   1106   1577       C  
ATOM   1965  CD2 TYR A 333      20.621 -23.282 -35.091  1.00 76.99           C  
ANISOU 1965  CD2 TYR A 333     8471  10264  10515   1880    864   1463       C  
ATOM   1966  CE1 TYR A 333      23.152 -22.184 -35.113  1.00 78.06           C  
ANISOU 1966  CE1 TYR A 333     7963  10912  10782   2035   1023   1706       C  
ATOM   1967  CE2 TYR A 333      20.802 -21.959 -34.727  1.00 74.35           C  
ANISOU 1967  CE2 TYR A 333     7949  10168  10130   1676    793   1580       C  
ATOM   1968  CZ  TYR A 333      22.070 -21.418 -34.741  1.00 74.95           C  
ANISOU 1968  CZ  TYR A 333     7716  10490  10272   1743    865   1700       C  
ATOM   1969  OH  TYR A 333      22.259 -20.105 -34.382  1.00 72.50           O  
ANISOU 1969  OH  TYR A 333     7238  10392   9916   1520    777   1814       O  
ATOM   1970  N   ILE A 334      21.368 -28.015 -38.179  1.00 75.98           N  
ANISOU 1970  N   ILE A 334     9042   9317  10512   2930   1443    822       N  
ATOM   1971  CA  ILE A 334      22.002 -29.221 -38.696  1.00 79.32           C  
ANISOU 1971  CA  ILE A 334     9576   9551  11012   3286   1611    686       C  
ATOM   1972  C   ILE A 334      22.326 -29.059 -40.178  1.00 81.81           C  
ANISOU 1972  C   ILE A 334    10005   9954  11124   3359   1852    462       C  
ATOM   1973  O   ILE A 334      21.447 -28.749 -40.982  1.00 82.29           O  
ANISOU 1973  O   ILE A 334    10358   9908  11001   3181   1823    290       O  
ATOM   1974  CB  ILE A 334      21.123 -30.470 -38.492  1.00 59.60           C  
ANISOU 1974  CB  ILE A 334     7425   6627   8595   3324   1481    599       C  
ATOM   1975  CG1 ILE A 334      20.897 -30.725 -37.001  1.00 57.26           C  
ANISOU 1975  CG1 ILE A 334     7023   6247   8486   3267   1256    841       C  
ATOM   1976  CG2 ILE A 334      21.766 -31.688 -39.141  1.00 63.17           C  
ANISOU 1976  CG2 ILE A 334     8033   6854   9115   3705   1661    429       C  
ATOM   1977  CD1 ILE A 334      20.234 -32.050 -36.705  1.00 58.25           C  
ANISOU 1977  CD1 ILE A 334     7464   5949   8721   3323   1135    798       C  
ATOM   1978  N   SER A 335      23.590 -29.270 -40.531  1.00106.10           N  
ANISOU 1978  N   SER A 335    12844  13242  14228   3617   2089    473       N  
ATOM   1979  CA  SER A 335      24.044 -29.101 -41.908  1.00108.16           C  
ANISOU 1979  CA  SER A 335    13187  13636  14273   3694   2349    281       C  
ATOM   1980  C   SER A 335      23.448 -30.151 -42.842  1.00110.97           C  
ANISOU 1980  C   SER A 335    13939  13665  14559   3914   2457     -3       C  
ATOM   1981  O   SER A 335      22.949 -31.184 -42.395  1.00111.61           O  
ANISOU 1981  O   SER A 335    14193  13413  14801   4052   2352    -35       O  
ATOM   1982  CB  SER A 335      25.573 -29.139 -41.978  1.00130.02           C  
ANISOU 1982  CB  SER A 335    15554  16752  17095   3902   2591    392       C  
ATOM   1983  OG  SER A 335      26.076 -30.368 -41.485  1.00131.75           O  
ANISOU 1983  OG  SER A 335    15853  17127  17079   3958   2859    222       O  
ATOM   1984  N   ASP A 336      23.513 -29.876 -44.141  1.00 98.41           N  
ANISOU 1984  N   ASP A 336    12508  12165  12720   3937   2663   -205       N  
ATOM   1985  CA  ASP A 336      22.922 -30.745 -45.154  1.00100.99           C  
ANISOU 1985  CA  ASP A 336    13264  12192  12915   4095   2755   -510       C  
ATOM   1986  C   ASP A 336      23.579 -32.122 -45.209  1.00103.61           C  
ANISOU 1986  C   ASP A 336    13630  12300  13436   4540   2899   -592       C  
ATOM   1987  O   ASP A 336      22.921 -33.122 -45.497  1.00105.27           O  
ANISOU 1987  O   ASP A 336    14216  12116  13666   4639   2835   -781       O  
ATOM   1988  CB  ASP A 336      22.995 -30.081 -46.532  1.00121.92           C  
ANISOU 1988  CB  ASP A 336    16028  15054  15241   4070   2984   -686       C  
ATOM   1989  CG  ASP A 336      22.269 -28.750 -46.577  1.00118.83           C  
ANISOU 1989  CG  ASP A 336    15502  14959  14689   3689   2889   -551       C  
ATOM   1990  OD1 ASP A 336      22.179 -28.082 -45.525  1.00116.19           O  
ANISOU 1990  OD1 ASP A 336    14915  14724  14509   3491   2697   -311       O  
ATOM   1991  OD2 ASP A 336      21.787 -28.371 -47.666  1.00118.99           O  
ANISOU 1991  OD2 ASP A 336    15685  15107  14420   3593   3003   -685       O  
ATOM   1992  N   GLU A 337      24.878 -32.167 -44.931  1.00120.81           N  
ANISOU 1992  N   GLU A 337    15414  14725  15765   4805   3085   -445       N  
ATOM   1993  CA  GLU A 337      25.629 -33.416 -44.999  1.00123.53           C  
ANISOU 1993  CA  GLU A 337    15736  14899  16299   5276   3253   -509       C  
ATOM   1994  C   GLU A 337      25.355 -34.326 -43.803  1.00123.23           C  
ANISOU 1994  C   GLU A 337    15778  14497  16546   5348   2999   -405       C  
ATOM   1995  O   GLU A 337      25.580 -35.534 -43.870  1.00125.77           O  
ANISOU 1995  O   GLU A 337    16308  14492  16988   5683   3062   -541       O  
ATOM   1996  CB  GLU A 337      27.129 -33.136 -45.115  1.00218.55           C  
ANISOU 1996  CB  GLU A 337    27263  27334  28440   5521   3502   -340       C  
ATOM   1997  CG  GLU A 337      27.527 -32.417 -46.394  1.00216.03           C  
ANISOU 1997  CG  GLU A 337    26496  27314  28272   5282   3322      6       C  
ATOM   1998  CD  GLU A 337      29.024 -32.202 -46.498  1.00216.35           C  
ANISOU 1998  CD  GLU A 337    26024  27775  28402   5477   3564    172       C  
ATOM   1999  OE1 GLU A 337      29.739 -32.513 -45.522  1.00218.70           O  
ANISOU 1999  OE1 GLU A 337    26297  28140  28659   5829   3891     25       O  
ATOM   2000  OE2 GLU A 337      29.486 -31.724 -47.556  1.00214.26           O  
ANISOU 2000  OE2 GLU A 337    25381  27780  28247   5275   3428    447       O  
ATOM   2001  N   GLN A 338      24.867 -33.742 -42.714  1.00122.94           N  
ANISOU 2001  N   GLN A 338    15592  14508  16610   5037   2715   -163       N  
ATOM   2002  CA  GLN A 338      24.587 -34.506 -41.502  1.00122.29           C  
ANISOU 2002  CA  GLN A 338    15574  14114  16777   5064   2464    -25       C  
ATOM   2003  C   GLN A 338      23.185 -35.108 -41.509  1.00122.40           C  
ANISOU 2003  C   GLN A 338    16081  13703  16720   4868   2273   -191       C  
ATOM   2004  O   GLN A 338      22.924 -36.098 -40.824  1.00123.03           O  
ANISOU 2004  O   GLN A 338    16341  13419  16986   4983   2135   -166       O  
ATOM   2005  CB  GLN A 338      24.781 -33.635 -40.258  1.00152.27           C  
ANISOU 2005  CB  GLN A 338    19015  18148  20694   4819   2247    304       C  
ATOM   2006  CG  GLN A 338      26.229 -33.273 -39.975  1.00152.24           C  
ANISOU 2006  CG  GLN A 338    18508  18484  20854   5039   2360    520       C  
ATOM   2007  CD  GLN A 338      26.387 -32.433 -38.723  1.00149.87           C  
ANISOU 2007  CD  GLN A 338    17891  18637  20415   4770   2402    637       C  
ATOM   2008  OE1 GLN A 338      25.970 -31.275 -38.681  1.00148.91           O  
ANISOU 2008  OE1 GLN A 338    17925  18608  20046   4544   2469    495       O  
ATOM   2009  NE2 GLN A 338      26.989 -33.015 -37.692  1.00148.97           N  
ANISOU 2009  NE2 GLN A 338    17340  18801  20463   4783   2345    905       N  
ATOM   2010  N   TRP A 339      22.286 -34.509 -42.284  1.00 88.44           N  
ANISOU 2010  N   TRP A 339    11993   9452  12159   4565   2253   -346       N  
ATOM   2011  CA  TRP A 339      20.908 -34.984 -42.361  1.00 88.43           C  
ANISOU 2011  CA  TRP A 339    12427   9090  12085   4329   2055   -493       C  
ATOM   2012  C   TRP A 339      20.798 -36.358 -43.017  1.00 91.71           C  
ANISOU 2012  C   TRP A 339    13246   9086  12514   4611   2142   -762       C  
ATOM   2013  O   TRP A 339      20.887 -36.485 -44.238  1.00 94.01           O  
ANISOU 2013  O   TRP A 339    13631   9423  12668   4859   2398   -982       O  
ATOM   2014  CB  TRP A 339      20.025 -33.978 -43.104  1.00 78.87           C  
ANISOU 2014  CB  TRP A 339    11327   8053  10588   3965   2017   -598       C  
ATOM   2015  CG  TRP A 339      19.532 -32.855 -42.245  1.00 75.48           C  
ANISOU 2015  CG  TRP A 339    10659   7860  10162   3601   1821   -360       C  
ATOM   2016  CD1 TRP A 339      19.965 -31.561 -42.258  1.00 73.77           C  
ANISOU 2016  CD1 TRP A 339    10114   8056   9861   3480   1884   -223       C  
ATOM   2017  CD2 TRP A 339      18.512 -32.928 -41.243  1.00 73.40           C  
ANISOU 2017  CD2 TRP A 339    10476   7425   9988   3315   1540   -236       C  
ATOM   2018  NE1 TRP A 339      19.276 -30.822 -41.327  1.00 70.81           N  
ANISOU 2018  NE1 TRP A 339     9628   7761   9515   3153   1655    -38       N  
ATOM   2019  CE2 TRP A 339      18.378 -31.638 -40.690  1.00 70.44           C  
ANISOU 2019  CE2 TRP A 339     9818   7377   9569   3052   1453    -42       C  
ATOM   2020  CE3 TRP A 339      17.697 -33.957 -40.761  1.00 73.73           C  
ANISOU 2020  CE3 TRP A 339    10806   7068  10141   3250   1359   -266       C  
ATOM   2021  CZ2 TRP A 339      17.463 -31.349 -39.679  1.00 67.70           C  
ANISOU 2021  CZ2 TRP A 339     9463   6985   9275   2753   1212    109       C  
ATOM   2022  CZ3 TRP A 339      16.791 -33.670 -39.758  1.00 71.03           C  
ANISOU 2022  CZ3 TRP A 339    10437   6698   9855   2932   1120    -95       C  
ATOM   2023  CH2 TRP A 339      16.681 -32.376 -39.227  1.00 68.00           C  
ANISOU 2023  CH2 TRP A 339     9764   6660   9415   2699   1058     84       C  
ATOM   2024  N   THR A 340      20.605 -37.385 -42.195  1.00118.32           N  
ANISOU 2024  N   THR A 340    16868  12044  16044   4567   1930   -743       N  
ATOM   2025  CA  THR A 340      20.386 -38.736 -42.694  1.00121.32           C  
ANISOU 2025  CA  THR A 340    17684  11956  16456   4790   1961   -995       C  
ATOM   2026  C   THR A 340      18.897 -39.059 -42.667  1.00120.76           C  
ANISOU 2026  C   THR A 340    18003  11556  16324   4417   1697  -1083       C  
ATOM   2027  O   THR A 340      18.083 -38.226 -42.268  1.00118.08           O  
ANISOU 2027  O   THR A 340    17567  11385  15914   4019   1521   -953       O  
ATOM   2028  CB  THR A 340      21.144 -39.781 -41.852  1.00109.53           C  
ANISOU 2028  CB  THR A 340    16138  10204  15276   5168   1962   -872       C  
ATOM   2029  OG1 THR A 340      20.638 -39.779 -40.511  1.00107.11           O  
ANISOU 2029  OG1 THR A 340    15716   9823  15158   4948   1688   -574       O  
ATOM   2030  CG2 THR A 340      22.633 -39.470 -41.829  1.00110.34           C  
ANISOU 2030  CG2 THR A 340    15824  10640  15460   5555   2223   -780       C  
ATOM   2031  N   THR A 341      18.543 -40.266 -43.096  1.00 97.85           N  
ANISOU 2031  N   THR A 341    15539   8184  13455   4547   1670  -1305       N  
ATOM   2032  CA  THR A 341      17.158 -40.719 -43.036  1.00 97.60           C  
ANISOU 2032  CA  THR A 341    15884   7803  13397   4193   1408  -1384       C  
ATOM   2033  C   THR A 341      16.741 -40.881 -41.578  1.00 95.44           C  
ANISOU 2033  C   THR A 341    15481   7417  13362   3991   1158  -1063       C  
ATOM   2034  O   THR A 341      15.600 -40.578 -41.199  1.00 93.36           O  
ANISOU 2034  O   THR A 341    15262   7152  13057   3570    942   -978       O  
ATOM   2035  CB  THR A 341      16.969 -42.056 -43.775  1.00 93.29           C  
ANISOU 2035  CB  THR A 341    15852   6737  12857   4398   1428  -1689       C  
ATOM   2036  OG1 THR A 341      17.766 -43.069 -43.148  1.00 98.48           O  
ANISOU 2036  OG1 THR A 341    16511   7107  13802   4770   1459  -1591       O  
ATOM   2037  CG2 THR A 341      17.382 -41.924 -45.235  1.00 96.97           C  
ANISOU 2037  CG2 THR A 341    16471   7317  13058   4622   1696  -2021       C  
ATOM   2038  N   PHE A 342      17.684 -41.353 -40.768  1.00 87.58           N  
ANISOU 2038  N   PHE A 342    14316   6348  12613   4303   1195   -878       N  
ATOM   2039  CA  PHE A 342      17.475 -41.512 -39.335  1.00 85.93           C  
ANISOU 2039  CA  PHE A 342    13986   6039  12625   4166    977   -555       C  
ATOM   2040  C   PHE A 342      17.095 -40.190 -38.685  1.00 78.40           C  
ANISOU 2040  C   PHE A 342    12662   5529  11597   3827    887   -315       C  
ATOM   2041  O   PHE A 342      16.112 -40.117 -37.956  1.00 75.23           O  
ANISOU 2041  O   PHE A 342    12305   5063  11217   3472    674   -169       O  
ATOM   2042  CB  PHE A 342      18.727 -42.076 -38.662  1.00112.77           C  
ANISOU 2042  CB  PHE A 342    17225   9342  16279   4606   1050   -396       C  
ATOM   2043  CG  PHE A 342      18.697 -41.992 -37.160  1.00110.53           C  
ANISOU 2043  CG  PHE A 342    16731   9080  16187   4484    847    -23       C  
ATOM   2044  CD1 PHE A 342      17.942 -42.886 -36.418  1.00110.87           C  
ANISOU 2044  CD1 PHE A 342    17057   8704  16364   4316    621     82       C  
ATOM   2045  CD2 PHE A 342      19.424 -41.020 -36.491  1.00108.14           C  
ANISOU 2045  CD2 PHE A 342    15956   9215  15919   4525    877    229       C  
ATOM   2046  CE1 PHE A 342      17.911 -42.811 -35.039  1.00108.84           C  
ANISOU 2046  CE1 PHE A 342    16623   8480  16253   4200    443    433       C  
ATOM   2047  CE2 PHE A 342      19.397 -40.940 -35.113  1.00106.08           C  
ANISOU 2047  CE2 PHE A 342    15525   8980  15802   4410    684    564       C  
ATOM   2048  CZ  PHE A 342      18.640 -41.837 -34.386  1.00106.44           C  
ANISOU 2048  CZ  PHE A 342    15862   8620  15962   4253    473    668       C  
ATOM   2049  N   LEU A 343      17.877 -39.149 -38.954  1.00104.79           N  
ANISOU 2049  N   LEU A 343    15645   9320  14851   3937   1058   -275       N  
ATOM   2050  CA  LEU A 343      17.614 -37.830 -38.386  1.00101.29           C  
ANISOU 2050  CA  LEU A 343    14859   9299  14327   3642    988    -69       C  
ATOM   2051  C   LEU A 343      16.311 -37.234 -38.909  1.00100.07           C  
ANISOU 2051  C   LEU A 343    14851   9211  13960   3228    890   -185       C  
ATOM   2052  O   LEU A 343      15.710 -36.379 -38.262  1.00 97.11           O  
ANISOU 2052  O   LEU A 343    14300   9046  13553   2921    760    -11       O  
ATOM   2053  CB  LEU A 343      18.781 -36.877 -38.657  1.00 96.39           C  
ANISOU 2053  CB  LEU A 343    13850   9117  13656   3844   1196    -22       C  
ATOM   2054  CG  LEU A 343      20.031 -37.073 -37.798  1.00 96.78           C  
ANISOU 2054  CG  LEU A 343    13613   9223  13934   4190   1249    185       C  
ATOM   2055  CD1 LEU A 343      21.080 -36.025 -38.137  1.00 96.43           C  
ANISOU 2055  CD1 LEU A 343    13169   9638  13830   4336   1453    228       C  
ATOM   2056  CD2 LEU A 343      19.676 -37.019 -36.319  1.00 94.34           C  
ANISOU 2056  CD2 LEU A 343    13178   8888  13778   4016   1007    496       C  
ATOM   2057  N   PHE A 344      15.882 -37.696 -40.079  1.00 88.31           N  
ANISOU 2057  N   PHE A 344    13685   7546  12323   3231    951   -482       N  
ATOM   2058  CA  PHE A 344      14.638 -37.244 -40.690  1.00 87.55           C  
ANISOU 2058  CA  PHE A 344    13750   7492  12026   2858    843   -609       C  
ATOM   2059  C   PHE A 344      13.446 -37.818 -39.926  1.00 86.55           C  
ANISOU 2059  C   PHE A 344    13809   7073  12003   2544    583   -516       C  
ATOM   2060  O   PHE A 344      12.624 -37.075 -39.356  1.00 83.89           O  
ANISOU 2060  O   PHE A 344    13329   6918  11629   2206    444   -371       O  
ATOM   2061  CB  PHE A 344      14.598 -37.695 -42.152  1.00 65.93           C  
ANISOU 2061  CB  PHE A 344    11338   4617   9096   2974    969   -957       C  
ATOM   2062  CG  PHE A 344      13.620 -36.938 -43.006  1.00 62.66           C  
ANISOU 2062  CG  PHE A 344    11029   4349   8430   2641    893  -1093       C  
ATOM   2063  CD1 PHE A 344      13.958 -35.708 -43.544  1.00 59.21           C  
ANISOU 2063  CD1 PHE A 344    10360   4339   7799   2603   1017  -1090       C  
ATOM   2064  CD2 PHE A 344      12.373 -37.469 -43.292  1.00 63.80           C  
ANISOU 2064  CD2 PHE A 344    11508   4198   8535   2366    690  -1219       C  
ATOM   2065  CE1 PHE A 344      13.066 -35.014 -44.339  1.00 57.36           C  
ANISOU 2065  CE1 PHE A 344    10227   4232   7335   2312    934  -1202       C  
ATOM   2066  CE2 PHE A 344      11.477 -36.780 -44.087  1.00 61.41           C  
ANISOU 2066  CE2 PHE A 344    11286   4039   8007   2068    602  -1335       C  
ATOM   2067  CZ  PHE A 344      11.823 -35.550 -44.610  1.00 58.18           C  
ANISOU 2067  CZ  PHE A 344    10648   4054   7404   2052    723  -1325       C  
ATOM   2068  N   ASP A 345      13.367 -39.147 -39.910  1.00 75.92           N  
ANISOU 2068  N   ASP A 345    12781   5272  10796   2663    525   -594       N  
ATOM   2069  CA  ASP A 345      12.303 -39.848 -39.198  1.00 75.40           C  
ANISOU 2069  CA  ASP A 345    12919   4888  10841   2366    286   -504       C  
ATOM   2070  C   ASP A 345      12.270 -39.419 -37.733  1.00 72.38           C  
ANISOU 2070  C   ASP A 345    12237   4666  10601   2236    183   -147       C  
ATOM   2071  O   ASP A 345      11.203 -39.129 -37.177  1.00 70.16           O  
ANISOU 2071  O   ASP A 345    11921   4428  10309   1868     21    -20       O  
ATOM   2072  CB  ASP A 345      12.505 -41.360 -39.299  1.00149.94           C  
ANISOU 2072  CB  ASP A 345    22747  13791  20432   2566    255   -624       C  
ATOM   2073  CG  ASP A 345      12.658 -41.833 -40.732  1.00153.02           C  
ANISOU 2073  CG  ASP A 345    23460  14011  20668   2747    379   -998       C  
ATOM   2074  OD1 ASP A 345      11.963 -41.289 -41.615  1.00152.54           O  
ANISOU 2074  OD1 ASP A 345    23443  14140  20374   2549    385  -1172       O  
ATOM   2075  OD2 ASP A 345      13.473 -42.748 -40.978  1.00155.85           O  
ANISOU 2075  OD2 ASP A 345    24035  14046  21132   3099    470  -1120       O  
ATOM   2076  N   PHE A 346      13.451 -39.368 -37.123  1.00 78.07           N  
ANISOU 2076  N   PHE A 346    12730   5491  11445   2544    281     12       N  
ATOM   2077  CA  PHE A 346      13.594 -38.905 -35.750  1.00 75.38           C  
ANISOU 2077  CA  PHE A 346    12098   5334  11212   2462    194    345       C  
ATOM   2078  C   PHE A 346      13.072 -37.486 -35.595  1.00 70.89           C  
ANISOU 2078  C   PHE A 346    11251   5204  10483   2174    177    424       C  
ATOM   2079  O   PHE A 346      12.416 -37.177 -34.607  1.00 68.31           O  
ANISOU 2079  O   PHE A 346    10816   4959  10181   1919     45    635       O  
ATOM   2080  CB  PHE A 346      15.054 -38.975 -35.293  1.00 82.37           C  
ANISOU 2080  CB  PHE A 346    12753   6313  12230   2858    305    478       C  
ATOM   2081  CG  PHE A 346      15.310 -38.311 -33.968  1.00 79.36           C  
ANISOU 2081  CG  PHE A 346    12036   6213  11905   2772    223    800       C  
ATOM   2082  CD1 PHE A 346      15.061 -38.985 -32.785  1.00 80.25           C  
ANISOU 2082  CD1 PHE A 346    12210   6124  12159   2678     53   1044       C  
ATOM   2083  CD2 PHE A 346      15.809 -37.018 -33.906  1.00 76.28           C  
ANISOU 2083  CD2 PHE A 346    11289   6281  11414   2774    311    862       C  
ATOM   2084  CE1 PHE A 346      15.294 -38.383 -31.565  1.00 78.01           C  
ANISOU 2084  CE1 PHE A 346    11643   6103  11894   2595    -27   1330       C  
ATOM   2085  CE2 PHE A 346      16.043 -36.408 -32.686  1.00 73.89           C  
ANISOU 2085  CE2 PHE A 346    10706   6223  11145   2685    221   1140       C  
ATOM   2086  CZ  PHE A 346      15.786 -37.092 -31.514  1.00 74.73           C  
ANISOU 2086  CZ  PHE A 346    10883   6137  11373   2601     53   1368       C  
ATOM   2087  N   TYR A 347      13.365 -36.628 -36.570  1.00 52.96           N  
ANISOU 2087  N   TYR A 347     8872   3208   8041   2225    318    258       N  
ATOM   2088  CA  TYR A 347      12.894 -35.248 -36.521  1.00 47.11           C  
ANISOU 2088  CA  TYR A 347     7892   2861   7147   1972    305    316       C  
ATOM   2089  C   TYR A 347      11.377 -35.193 -36.487  1.00 45.03           C  
ANISOU 2089  C   TYR A 347     7771   2518   6821   1583    140    298       C  
ATOM   2090  O   TYR A 347      10.797 -34.378 -35.770  1.00 41.31           O  
ANISOU 2090  O   TYR A 347     7108   2267   6322   1348     59    461       O  
ATOM   2091  CB  TYR A 347      13.403 -34.431 -37.712  1.00 51.64           C  
ANISOU 2091  CB  TYR A 347     8381   3700   7540   2081    480    132       C  
ATOM   2092  CG  TYR A 347      12.815 -33.036 -37.770  1.00 47.25           C  
ANISOU 2092  CG  TYR A 347     7614   3511   6830   1819    452    187       C  
ATOM   2093  CD1 TYR A 347      13.347 -32.008 -37.004  1.00 44.65           C  
ANISOU 2093  CD1 TYR A 347     6943   3507   6514   1831    482    384       C  
ATOM   2094  CD2 TYR A 347      11.719 -32.752 -38.578  1.00 46.02           C  
ANISOU 2094  CD2 TYR A 347     7605   3362   6520   1558    380     44       C  
ATOM   2095  CE1 TYR A 347      12.810 -30.735 -37.044  1.00 40.93           C  
ANISOU 2095  CE1 TYR A 347     6306   3337   5911   1603    452    427       C  
ATOM   2096  CE2 TYR A 347      11.174 -31.482 -38.622  1.00 43.28           C  
ANISOU 2096  CE2 TYR A 347     7070   3329   6045   1343    349    100       C  
ATOM   2097  CZ  TYR A 347      11.725 -30.478 -37.854  1.00 40.81           C  
ANISOU 2097  CZ  TYR A 347     6441   3314   5752   1372    391    287       C  
ATOM   2098  OH  TYR A 347      11.188 -29.212 -37.897  1.00 38.44           O  
ANISOU 2098  OH  TYR A 347     5980   3294   5332   1169    357    334       O  
ATOM   2099  N   HIS A 348      10.729 -36.052 -37.265  1.00 53.25           N  
ANISOU 2099  N   HIS A 348     9144   3251   7838   1514     88     95       N  
ATOM   2100  CA  HIS A 348       9.269 -36.009 -37.324  1.00 52.07           C  
ANISOU 2100  CA  HIS A 348     9101   3052   7634   1129    -77     77       C  
ATOM   2101  C   HIS A 348       8.565 -36.662 -36.121  1.00 52.49           C  
ANISOU 2101  C   HIS A 348     9192   2903   7850    924   -237    295       C  
ATOM   2102  O   HIS A 348       7.536 -36.158 -35.647  1.00 50.19           O  
ANISOU 2102  O   HIS A 348     8801   2740   7530    606   -345    402       O  
ATOM   2103  CB  HIS A 348       8.764 -36.553 -38.661  1.00 60.26           C  
ANISOU 2103  CB  HIS A 348    10465   3873   8557   1077   -100   -220       C  
ATOM   2104  CG  HIS A 348       9.212 -35.743 -39.838  1.00 58.87           C  
ANISOU 2104  CG  HIS A 348    10244   3955   8170   1195     43   -412       C  
ATOM   2105  ND1 HIS A 348      10.456 -35.891 -40.413  1.00 61.07           N  
ANISOU 2105  ND1 HIS A 348    10545   4245   8414   1556    242   -534       N  
ATOM   2106  CD2 HIS A 348       8.591 -34.761 -40.533  1.00 56.26           C  
ANISOU 2106  CD2 HIS A 348     9836   3891   7649   1001     22   -485       C  
ATOM   2107  CE1 HIS A 348      10.578 -35.041 -41.418  1.00 59.89           C  
ANISOU 2107  CE1 HIS A 348    10345   4360   8049   1563    344   -672       C  
ATOM   2108  NE2 HIS A 348       9.460 -34.345 -41.512  1.00 57.57           N  
ANISOU 2108  NE2 HIS A 348    10001   4216   7658   1230    203   -643       N  
ATOM   2109  N   TYR A 349       9.114 -37.766 -35.619  1.00 63.30           N  
ANISOU 2109  N   TYR A 349    10685   3976   9390   1115   -244    380       N  
ATOM   2110  CA  TYR A 349       8.590 -38.350 -34.384  1.00 62.03           C  
ANISOU 2110  CA  TYR A 349    10542   3651   9374    935   -382    630       C  
ATOM   2111  C   TYR A 349       8.770 -37.359 -33.233  1.00 58.56           C  
ANISOU 2111  C   TYR A 349     9748   3584   8917    884   -368    890       C  
ATOM   2112  O   TYR A 349       7.884 -37.188 -32.385  1.00 56.09           O  
ANISOU 2112  O   TYR A 349     9359   3343   8610    601   -465   1068       O  
ATOM   2113  CB  TYR A 349       9.279 -39.677 -34.059  1.00 59.70           C  
ANISOU 2113  CB  TYR A 349    10472   2943   9268   1174   -401    679       C  
ATOM   2114  CG  TYR A 349       8.837 -40.839 -34.925  1.00 64.87           C  
ANISOU 2114  CG  TYR A 349    11541   3140   9968   1138   -470    461       C  
ATOM   2115  CD1 TYR A 349       7.540 -41.331 -34.851  1.00 66.65           C  
ANISOU 2115  CD1 TYR A 349    11945   3158  10221    759   -640    486       C  
ATOM   2116  CD2 TYR A 349       9.720 -41.457 -35.802  1.00 68.61           C  
ANISOU 2116  CD2 TYR A 349    12225   3386  10455   1482   -365    229       C  
ATOM   2117  CE1 TYR A 349       7.132 -42.396 -35.635  1.00 71.89           C  
ANISOU 2117  CE1 TYR A 349    13002   3385  10926    699   -728    283       C  
ATOM   2118  CE2 TYR A 349       9.319 -42.523 -36.590  1.00 73.91           C  
ANISOU 2118  CE2 TYR A 349    13311   3616  11156   1449   -437      9       C  
ATOM   2119  CZ  TYR A 349       8.025 -42.986 -36.502  1.00 75.49           C  
ANISOU 2119  CZ  TYR A 349    13698   3601  11384   1047   -630     37       C  
ATOM   2120  OH  TYR A 349       7.625 -44.044 -37.284  1.00 81.24           O  
ANISOU 2120  OH  TYR A 349    14853   3874  12141    989   -724   -186       O  
ATOM   2121  N   PHE A 350       9.922 -36.698 -33.226  1.00 55.62           N  
ANISOU 2121  N   PHE A 350     9162   3455   8515   1156   -243    905       N  
ATOM   2122  CA  PHE A 350      10.223 -35.668 -32.242  1.00 52.34           C  
ANISOU 2122  CA  PHE A 350     8419   3405   8060   1125   -230   1116       C  
ATOM   2123  C   PHE A 350       9.263 -34.497 -32.400  1.00 49.65           C  
ANISOU 2123  C   PHE A 350     7947   3350   7566    825   -253   1087       C  
ATOM   2124  O   PHE A 350       8.908 -33.843 -31.422  1.00 46.51           O  
ANISOU 2124  O   PHE A 350     7381   3145   7145    654   -304   1274       O  
ATOM   2125  CB  PHE A 350      11.669 -35.195 -32.397  1.00 74.95           C  
ANISOU 2125  CB  PHE A 350    11080   6486  10912   1446    -93   1095       C  
ATOM   2126  CG  PHE A 350      12.142 -34.301 -31.289  1.00 71.74           C  
ANISOU 2126  CG  PHE A 350    10372   6382  10504   1453   -109   1333       C  
ATOM   2127  CD1 PHE A 350      12.013 -34.690 -29.968  1.00 69.71           C  
ANISOU 2127  CD1 PHE A 350    10097   6092  10297   1297   -233   1573       C  
ATOM   2128  CD2 PHE A 350      12.739 -33.083 -31.569  1.00 70.88           C  
ANISOU 2128  CD2 PHE A 350    10007   6592  10330   1601     -5   1320       C  
ATOM   2129  CE1 PHE A 350      12.453 -33.874 -28.944  1.00 66.96           C  
ANISOU 2129  CE1 PHE A 350     9499   6020   9921   1298   -260   1778       C  
ATOM   2130  CE2 PHE A 350      13.184 -32.262 -30.548  1.00 68.05           C  
ANISOU 2130  CE2 PHE A 350     9389   6500   9965   1587    -43   1529       C  
ATOM   2131  CZ  PHE A 350      13.040 -32.659 -29.235  1.00 66.12           C  
ANISOU 2131  CZ  PHE A 350     9148   6216   9757   1440   -175   1750       C  
ATOM   2132  N   TYR A 351       8.845 -34.239 -33.637  1.00 47.64           N  
ANISOU 2132  N   TYR A 351     7780   3119   7201    773   -217    851       N  
ATOM   2133  CA  TYR A 351       7.844 -33.213 -33.906  1.00 45.45           C  
ANISOU 2133  CA  TYR A 351     7402   3078   6790    503   -255    808       C  
ATOM   2134  C   TYR A 351       6.554 -33.581 -33.192  1.00 43.90           C  
ANISOU 2134  C   TYR A 351     7257   2775   6649    193   -390    933       C  
ATOM   2135  O   TYR A 351       5.964 -32.755 -32.476  1.00 40.88           O  
ANISOU 2135  O   TYR A 351     6678   2636   6219     13   -415   1065       O  
ATOM   2136  CB  TYR A 351       7.600 -33.073 -35.412  1.00 49.95           C  
ANISOU 2136  CB  TYR A 351     8118   3623   7236    499   -224    536       C  
ATOM   2137  CG  TYR A 351       6.548 -32.050 -35.783  1.00 47.93           C  
ANISOU 2137  CG  TYR A 351     7753   3614   6844    249   -273    493       C  
ATOM   2138  CD1 TYR A 351       6.890 -30.722 -35.996  1.00 46.63           C  
ANISOU 2138  CD1 TYR A 351     7374   3788   6557    301   -191    490       C  
ATOM   2139  CD2 TYR A 351       5.214 -32.414 -35.928  1.00 47.42           C  
ANISOU 2139  CD2 TYR A 351     7795   3438   6785    -39   -411    465       C  
ATOM   2140  CE1 TYR A 351       5.936 -29.784 -36.335  1.00 44.83           C  
ANISOU 2140  CE1 TYR A 351     7054   3765   6215     97   -244    458       C  
ATOM   2141  CE2 TYR A 351       4.252 -31.483 -36.268  1.00 45.62           C  
ANISOU 2141  CE2 TYR A 351     7446   3440   6448   -243   -464    436       C  
ATOM   2142  CZ  TYR A 351       4.618 -30.169 -36.470  1.00 44.30           C  
ANISOU 2142  CZ  TYR A 351     7080   3593   6160   -162   -380    431       C  
ATOM   2143  OH  TYR A 351       3.666 -29.235 -36.809  1.00 42.53           O  
ANISOU 2143  OH  TYR A 351     6744   3579   5836   -344   -440    409       O  
ATOM   2144  N   MET A 352       6.129 -34.828 -33.389  1.00 66.57           N  
ANISOU 2144  N   MET A 352    10394   5277   9623    134   -470    891       N  
ATOM   2145  CA  MET A 352       4.958 -35.355 -32.692  1.00 65.45           C  
ANISOU 2145  CA  MET A 352    10306   5009   9552   -176   -596   1028       C  
ATOM   2146  C   MET A 352       5.066 -35.123 -31.186  1.00 62.82           C  
ANISOU 2146  C   MET A 352     9787   4818   9262   -216   -595   1319       C  
ATOM   2147  O   MET A 352       4.139 -34.600 -30.559  1.00 60.39           O  
ANISOU 2147  O   MET A 352     9332   4698   8914   -462   -627   1439       O  
ATOM   2148  CB  MET A 352       4.787 -36.849 -32.973  1.00 68.34           C  
ANISOU 2148  CB  MET A 352    11006   4912  10047   -204   -684    970       C  
ATOM   2149  CG  MET A 352       4.471 -37.189 -34.417  1.00 70.89           C  
ANISOU 2149  CG  MET A 352    11564   5062  10310   -231   -718    675       C  
ATOM   2150  SD  MET A 352       4.262 -38.963 -34.664  1.00 74.37           S  
ANISOU 2150  SD  MET A 352    12438   4910  10908   -233   -826    594       S  
ATOM   2151  CE  MET A 352       3.817 -39.017 -36.398  1.00 76.63           C  
ANISOU 2151  CE  MET A 352    12958   5099  11057   -349   -890    240       C  
ATOM   2152  N   LEU A 353       6.210 -35.499 -30.619  1.00 47.85           N  
ANISOU 2152  N   LEU A 353     7892   2846   7440     37   -556   1430       N  
ATOM   2153  CA  LEU A 353       6.435 -35.368 -29.179  1.00 48.30           C  
ANISOU 2153  CA  LEU A 353     7808   3020   7523     16   -572   1711       C  
ATOM   2154  C   LEU A 353       6.326 -33.916 -28.700  1.00 44.44           C  
ANISOU 2154  C   LEU A 353     7027   2965   6892    -52   -520   1770       C  
ATOM   2155  O   LEU A 353       5.478 -33.588 -27.860  1.00 44.47           O  
ANISOU 2155  O   LEU A 353     6937   3107   6853   -275   -548   1921       O  
ATOM   2156  CB  LEU A 353       7.801 -35.955 -28.803  1.00 57.86           C  
ANISOU 2156  CB  LEU A 353     9057   4091   8836    334   -554   1806       C  
ATOM   2157  CG  LEU A 353       8.042 -36.439 -27.368  1.00 56.42           C  
ANISOU 2157  CG  LEU A 353     8797   3946   8693    340   -606   2111       C  
ATOM   2158  CD1 LEU A 353       9.220 -37.402 -27.335  1.00 59.14           C  
ANISOU 2158  CD1 LEU A 353     9318   3950   9202    590   -646   2193       C  
ATOM   2159  CD2 LEU A 353       8.286 -35.283 -26.411  1.00 53.71           C  
ANISOU 2159  CD2 LEU A 353     8166   4004   8238    428   -555   2194       C  
ATOM   2160  N   THR A 354       7.188 -33.056 -29.237  1.00 47.38           N  
ANISOU 2160  N   THR A 354     7266   3545   7189    140   -437   1649       N  
ATOM   2161  CA  THR A 354       7.257 -31.655 -28.825  1.00 44.29           C  
ANISOU 2161  CA  THR A 354     6622   3535   6671    104   -394   1692       C  
ATOM   2162  C   THR A 354       5.923 -30.933 -28.970  1.00 42.44           C  
ANISOU 2162  C   THR A 354     6322   3455   6346   -171   -412   1648       C  
ATOM   2163  O   THR A 354       5.512 -30.188 -28.078  1.00 40.06           O  
ANISOU 2163  O   THR A 354     5873   3369   5979   -293   -412   1778       O  
ATOM   2164  CB  THR A 354       8.321 -30.877 -29.625  1.00 51.50           C  
ANISOU 2164  CB  THR A 354     7423   4618   7525    325   -303   1551       C  
ATOM   2165  OG1 THR A 354       7.977 -30.881 -31.016  1.00 53.56           O  
ANISOU 2165  OG1 THR A 354     7799   4804   7746    313   -273   1316       O  
ATOM   2166  CG2 THR A 354       9.692 -31.504 -29.445  1.00 53.28           C  
ANISOU 2166  CG2 THR A 354     7652   4741   7851    616   -274   1611       C  
ATOM   2167  N   ASN A 355       5.247 -31.151 -30.093  1.00 40.12           N  
ANISOU 2167  N   ASN A 355     6141   3056   6047   -259   -431   1462       N  
ATOM   2168  CA  ASN A 355       3.965 -30.494 -30.315  1.00 38.55           C  
ANISOU 2168  CA  ASN A 355     5858   3011   5778   -505   -462   1422       C  
ATOM   2169  C   ASN A 355       2.862 -31.038 -29.405  1.00 39.13           C  
ANISOU 2169  C   ASN A 355     5941   3012   5912   -753   -523   1590       C  
ATOM   2170  O   ASN A 355       1.990 -30.286 -28.948  1.00 38.28           O  
ANISOU 2170  O   ASN A 355     5673   3122   5747   -924   -517   1653       O  
ATOM   2171  CB  ASN A 355       3.570 -30.569 -31.786  1.00 58.68           C  
ANISOU 2171  CB  ASN A 355     8523   5478   8293   -542   -490   1189       C  
ATOM   2172  CG  ASN A 355       4.382 -29.625 -32.655  1.00 58.68           C  
ANISOU 2172  CG  ASN A 355     8451   5665   8181   -361   -412   1044       C  
ATOM   2173  OD1 ASN A 355       3.908 -28.559 -33.040  1.00 57.33           O  
ANISOU 2173  OD1 ASN A 355     8179   5694   7911   -448   -417    970       O  
ATOM   2174  ND2 ASN A 355       5.616 -30.009 -32.954  1.00 60.34           N  
ANISOU 2174  ND2 ASN A 355     8704   5812   8411   -106   -337   1016       N  
ATOM   2175  N   ALA A 356       2.910 -32.342 -29.136  1.00 38.97           N  
ANISOU 2175  N   ALA A 356     6108   2688   6012   -766   -573   1671       N  
ATOM   2176  CA  ALA A 356       2.020 -32.936 -28.144  1.00 42.25           C  
ANISOU 2176  CA  ALA A 356     6538   3030   6487  -1001   -620   1873       C  
ATOM   2177  C   ALA A 356       2.211 -32.231 -26.805  1.00 41.75           C  
ANISOU 2177  C   ALA A 356     6289   3230   6344   -991   -560   2076       C  
ATOM   2178  O   ALA A 356       1.240 -31.907 -26.115  1.00 42.50           O  
ANISOU 2178  O   ALA A 356     6265   3485   6397  -1200   -544   2189       O  
ATOM   2179  CB  ALA A 356       2.284 -34.425 -28.005  1.00 45.31           C  
ANISOU 2179  CB  ALA A 356     7177   3023   7015   -983   -686   1945       C  
ATOM   2180  N   LEU A 357       3.469 -31.979 -26.454  1.00 54.93           N  
ANISOU 2180  N   LEU A 357     7928   4957   7986   -746   -525   2116       N  
ATOM   2181  CA  LEU A 357       3.783 -31.230 -25.240  1.00 52.70           C  
ANISOU 2181  CA  LEU A 357     7489   4931   7604   -725   -487   2286       C  
ATOM   2182  C   LEU A 357       3.236 -29.806 -25.293  1.00 50.30           C  
ANISOU 2182  C   LEU A 357     6983   4961   7168   -798   -429   2206       C  
ATOM   2183  O   LEU A 357       2.773 -29.273 -24.282  1.00 48.75           O  
ANISOU 2183  O   LEU A 357     6679   4965   6881   -896   -395   2334       O  
ATOM   2184  CB  LEU A 357       5.292 -31.206 -24.988  1.00 39.26           C  
ANISOU 2184  CB  LEU A 357     5776   3232   5907   -450   -486   2330       C  
ATOM   2185  CG  LEU A 357       5.903 -32.474 -24.390  1.00 43.01           C  
ANISOU 2185  CG  LEU A 357     6416   3422   6503   -351   -548   2488       C  
ATOM   2186  CD1 LEU A 357       7.388 -32.285 -24.133  1.00 42.93           C  
ANISOU 2186  CD1 LEU A 357     6337   3473   6502    -69   -552   2534       C  
ATOM   2187  CD2 LEU A 357       5.178 -32.858 -23.111  1.00 46.19           C  
ANISOU 2187  CD2 LEU A 357     6858   3809   6884   -555   -581   2735       C  
ATOM   2188  N   VAL A 358       3.295 -29.194 -26.474  1.00 53.34           N  
ANISOU 2188  N   VAL A 358     7335   5398   7534   -741   -415   1996       N  
ATOM   2189  CA  VAL A 358       2.747 -27.855 -26.672  1.00 51.29           C  
ANISOU 2189  CA  VAL A 358     6904   5420   7165   -799   -374   1913       C  
ATOM   2190  C   VAL A 358       1.260 -27.825 -26.338  1.00 51.01           C  
ANISOU 2190  C   VAL A 358     6804   5450   7127  -1048   -375   1968       C  
ATOM   2191  O   VAL A 358       0.792 -26.935 -25.623  1.00 49.42           O  
ANISOU 2191  O   VAL A 358     6457   5485   6836  -1106   -323   2031       O  
ATOM   2192  CB  VAL A 358       2.962 -27.357 -28.118  1.00 38.17           C  
ANISOU 2192  CB  VAL A 358     5245   3775   5484   -710   -372   1691       C  
ATOM   2193  CG1 VAL A 358       2.127 -26.115 -28.391  1.00 36.35           C  
ANISOU 2193  CG1 VAL A 358     4860   3789   5161   -800   -354   1620       C  
ATOM   2194  CG2 VAL A 358       4.438 -27.084 -28.377  1.00 38.37           C  
ANISOU 2194  CG2 VAL A 358     5269   3819   5492   -466   -338   1651       C  
ATOM   2195  N   TYR A 359       0.517 -28.804 -26.844  1.00 53.43           N  
ANISOU 2195  N   TYR A 359     7217   5549   7535  -1196   -434   1943       N  
ATOM   2196  CA  TYR A 359      -0.913 -28.863 -26.554  1.00 53.54           C  
ANISOU 2196  CA  TYR A 359     7140   5634   7569  -1450   -439   2011       C  
ATOM   2197  C   TYR A 359      -1.199 -29.251 -25.102  1.00 53.43           C  
ANISOU 2197  C   TYR A 359     7098   5658   7544  -1558   -392   2252       C  
ATOM   2198  O   TYR A 359      -2.229 -28.864 -24.539  1.00 53.09           O  
ANISOU 2198  O   TYR A 359     6905   5804   7464  -1717   -337   2335       O  
ATOM   2199  CB  TYR A 359      -1.634 -29.784 -27.538  1.00 79.44           C  
ANISOU 2199  CB  TYR A 359    10538   8684  10962  -1610   -537   1921       C  
ATOM   2200  CG  TYR A 359      -1.659 -29.224 -28.941  1.00 79.69           C  
ANISOU 2200  CG  TYR A 359    10575   8742  10962  -1544   -582   1687       C  
ATOM   2201  CD1 TYR A 359      -2.376 -28.068 -29.234  1.00 78.24           C  
ANISOU 2201  CD1 TYR A 359    10200   8825  10705  -1575   -564   1621       C  
ATOM   2202  CD2 TYR A 359      -0.962 -29.842 -29.970  1.00 81.65           C  
ANISOU 2202  CD2 TYR A 359    11032   8748  11243  -1440   -638   1536       C  
ATOM   2203  CE1 TYR A 359      -2.401 -27.548 -30.513  1.00 78.58           C  
ANISOU 2203  CE1 TYR A 359    10259   8894  10703  -1520   -616   1429       C  
ATOM   2204  CE2 TYR A 359      -0.979 -29.329 -31.251  1.00 82.19           C  
ANISOU 2204  CE2 TYR A 359    11123   8856  11252  -1386   -672   1329       C  
ATOM   2205  CZ  TYR A 359      -1.700 -28.183 -31.517  1.00 80.56           C  
ANISOU 2205  CZ  TYR A 359    10725   8918  10967  -1434   -668   1285       C  
ATOM   2206  OH  TYR A 359      -1.720 -27.671 -32.792  1.00 81.20           O  
ANISOU 2206  OH  TYR A 359    10840   9039  10974  -1386   -713   1099       O  
ATOM   2207  N   VAL A 360      -0.283 -30.008 -24.499  1.00 52.72           N  
ANISOU 2207  N   VAL A 360     7150   5403   7480  -1461   -407   2372       N  
ATOM   2208  CA  VAL A 360      -0.354 -30.283 -23.067  1.00 52.62           C  
ANISOU 2208  CA  VAL A 360     7131   5445   7419  -1534   -365   2614       C  
ATOM   2209  C   VAL A 360      -0.298 -28.962 -22.306  1.00 50.60           C  
ANISOU 2209  C   VAL A 360     6703   5530   6994  -1467   -275   2634       C  
ATOM   2210  O   VAL A 360      -1.068 -28.734 -21.370  1.00 50.53           O  
ANISOU 2210  O   VAL A 360     6607   5690   6904  -1603   -201   2768       O  
ATOM   2211  CB  VAL A 360       0.789 -31.210 -22.596  1.00 51.38           C  
ANISOU 2211  CB  VAL A 360     7155   5055   7312  -1397   -420   2738       C  
ATOM   2212  CG1 VAL A 360       0.917 -31.178 -21.080  1.00 52.14           C  
ANISOU 2212  CG1 VAL A 360     7232   5278   7301  -1428   -381   2983       C  
ATOM   2213  CG2 VAL A 360       0.563 -32.632 -23.086  1.00 53.80           C  
ANISOU 2213  CG2 VAL A 360     7663   4992   7786  -1496   -504   2758       C  
ATOM   2214  N   SER A 361       0.609 -28.086 -22.732  1.00 43.84           N  
ANISOU 2214  N   SER A 361     5806   4770   6080  -1263   -277   2496       N  
ATOM   2215  CA  SER A 361       0.700 -26.741 -22.174  1.00 42.05           C  
ANISOU 2215  CA  SER A 361     5440   4839   5699  -1199   -210   2476       C  
ATOM   2216  C   SER A 361      -0.585 -25.967 -22.432  1.00 41.68           C  
ANISOU 2216  C   SER A 361     5240   4976   5620  -1326   -147   2398       C  
ATOM   2217  O   SER A 361      -1.015 -25.162 -21.604  1.00 41.17           O  
ANISOU 2217  O   SER A 361     5072   5140   5432  -1345    -65   2440       O  
ATOM   2218  CB  SER A 361       1.883 -25.986 -22.779  1.00 48.40           C  
ANISOU 2218  CB  SER A 361     6228   5686   6475   -984   -237   2337       C  
ATOM   2219  OG  SER A 361       1.852 -24.613 -22.423  1.00 46.88           O  
ANISOU 2219  OG  SER A 361     5915   5752   6145   -947   -188   2290       O  
ATOM   2220  N   ALA A 362      -1.192 -26.212 -23.589  1.00 60.48           N  
ANISOU 2220  N   ALA A 362     7612   7257   8110  -1406   -189   2283       N  
ATOM   2221  CA  ALA A 362      -2.436 -25.539 -23.946  1.00 60.51           C  
ANISOU 2221  CA  ALA A 362     7452   7428   8110  -1520   -153   2215       C  
ATOM   2222  C   ALA A 362      -3.616 -26.018 -23.101  1.00 61.85           C  
ANISOU 2222  C   ALA A 362     7544   7653   8303  -1739    -93   2381       C  
ATOM   2223  O   ALA A 362      -4.640 -25.340 -23.014  1.00 62.16           O  
ANISOU 2223  O   ALA A 362     7406   7883   8330  -1824    -34   2365       O  
ATOM   2224  CB  ALA A 362      -2.735 -25.721 -25.425  1.00103.34           C  
ANISOU 2224  CB  ALA A 362    12895  12740  13630  -1541   -243   2044       C  
ATOM   2225  N   ALA A 363      -3.471 -27.182 -22.474  1.00 49.72           N  
ANISOU 2225  N   ALA A 363     6134   5952   6805  -1828   -105   2552       N  
ATOM   2226  CA  ALA A 363      -4.570 -27.757 -21.698  1.00 51.22           C  
ANISOU 2226  CA  ALA A 363     6261   6181   7021  -2064    -44   2737       C  
ATOM   2227  C   ALA A 363      -4.307 -27.867 -20.191  1.00 51.41           C  
ANISOU 2227  C   ALA A 363     6314   6312   6908  -2072     54   2947       C  
ATOM   2228  O   ALA A 363      -5.179 -28.303 -19.440  1.00 53.79           O  
ANISOU 2228  O   ALA A 363     6541   6703   7193  -2262    142   3113       O  
ATOM   2229  CB  ALA A 363      -4.955 -29.117 -22.265  1.00 61.07           C  
ANISOU 2229  CB  ALA A 363     7637   7127   8440  -2242   -151   2785       C  
ATOM   2230  N   ILE A 364      -3.119 -27.464 -19.749  1.00 64.51           N  
ANISOU 2230  N   ILE A 364     8074   7976   8462  -1876     39   2947       N  
ATOM   2231  CA  ILE A 364      -2.716 -27.681 -18.357  1.00 64.93           C  
ANISOU 2231  CA  ILE A 364     8200   8095   8374  -1881     93   3154       C  
ATOM   2232  C   ILE A 364      -3.346 -26.723 -17.333  1.00 64.98           C  
ANISOU 2232  C   ILE A 364     8073   8432   8185  -1901    248   3192       C  
ATOM   2233  O   ILE A 364      -3.721 -27.145 -16.238  1.00 66.19           O  
ANISOU 2233  O   ILE A 364     8252   8664   8233  -2018    332   3393       O  
ATOM   2234  CB  ILE A 364      -1.171 -27.700 -18.201  1.00 47.54           C  
ANISOU 2234  CB  ILE A 364     6145   5788   6131  -1670     -2   3157       C  
ATOM   2235  CG1 ILE A 364      -0.778 -28.074 -16.770  1.00 50.72           C  
ANISOU 2235  CG1 ILE A 364     6647   6232   6391  -1692     16   3397       C  
ATOM   2236  CG2 ILE A 364      -0.559 -26.366 -18.601  1.00 43.67           C  
ANISOU 2236  CG2 ILE A 364     5573   5458   5560  -1475     -5   2958       C  
ATOM   2237  CD1 ILE A 364      -1.236 -29.458 -16.349  1.00 55.03           C  
ANISOU 2237  CD1 ILE A 364     7298   6597   7015  -1892     11   3626       C  
ATOM   2238  N   ASN A 365      -3.476 -25.449 -17.695  1.00 52.44           N  
ANISOU 2238  N   ASN A 365     6356   7028   6541  -1787    290   3001       N  
ATOM   2239  CA  ASN A 365      -3.921 -24.418 -16.750  1.00 52.79           C  
ANISOU 2239  CA  ASN A 365     6303   7367   6390  -1754    435   2998       C  
ATOM   2240  C   ASN A 365      -5.281 -24.624 -16.056  1.00 54.78           C  
ANISOU 2240  C   ASN A 365     6424   7791   6599  -1936    601   3132       C  
ATOM   2241  O   ASN A 365      -5.363 -24.501 -14.832  1.00 56.80           O  
ANISOU 2241  O   ASN A 365     6715   8207   6662  -1955    717   3257       O  
ATOM   2242  CB  ASN A 365      -3.833 -23.018 -17.376  1.00 66.04           C  
ANISOU 2242  CB  ASN A 365     7882   9167   8042  -1591    436   2762       C  
ATOM   2243  CG  ASN A 365      -2.405 -22.585 -17.636  1.00 64.32           C  
ANISOU 2243  CG  ASN A 365     7781   8857   7799  -1412    312   2663       C  
ATOM   2244  OD1 ASN A 365      -2.066 -22.154 -18.737  1.00 63.07           O  
ANISOU 2244  OD1 ASN A 365     7609   8596   7758  -1337    224   2517       O  
ATOM   2245  ND2 ASN A 365      -1.559 -22.695 -16.620  1.00 64.45           N  
ANISOU 2245  ND2 ASN A 365     7908   8924   7656  -1350    303   2750       N  
ATOM   2246  N   PRO A 366      -6.349 -24.927 -16.821  1.00 73.78           N  
ANISOU 2246  N   PRO A 366     8677  10181   9176  -2077    615   3111       N  
ATOM   2247  CA  PRO A 366      -7.648 -25.110 -16.159  1.00 75.81           C  
ANISOU 2247  CA  PRO A 366     8769  10628   9407  -2258    784   3253       C  
ATOM   2248  C   PRO A 366      -7.661 -26.300 -15.204  1.00 77.02           C  
ANISOU 2248  C   PRO A 366     9044  10706   9513  -2441    821   3527       C  
ATOM   2249  O   PRO A 366      -8.431 -26.304 -14.244  1.00 78.65           O  
ANISOU 2249  O   PRO A 366     9163  11123   9598  -2549   1001   3675       O  
ATOM   2250  CB  PRO A 366      -8.603 -25.370 -17.329  1.00 55.21           C  
ANISOU 2250  CB  PRO A 366     5989   7959   7029  -2390    725   3187       C  
ATOM   2251  CG  PRO A 366      -7.932 -24.759 -18.511  1.00 50.64           C  
ANISOU 2251  CG  PRO A 366     5451   7266   6524  -2213    577   2953       C  
ATOM   2252  CD  PRO A 366      -6.475 -25.006 -18.288  1.00 48.88           C  
ANISOU 2252  CD  PRO A 366     5475   6871   6226  -2079    484   2955       C  
ATOM   2253  N   ILE A 367      -6.823 -27.296 -15.474  1.00 95.10           N  
ANISOU 2253  N   ILE A 367    11537  12698  11897  -2466    660   3598       N  
ATOM   2254  CA  ILE A 367      -6.721 -28.468 -14.612  1.00 96.36           C  
ANISOU 2254  CA  ILE A 367    11850  12740  12023  -2625    664   3871       C  
ATOM   2255  C   ILE A 367      -6.128 -28.092 -13.257  1.00 96.49           C  
ANISOU 2255  C   ILE A 367    11975  12923  11762  -2522    746   3977       C  
ATOM   2256  O   ILE A 367      -6.590 -28.556 -12.214  1.00 98.11           O  
ANISOU 2256  O   ILE A 367    12203  13238  11836  -2669    868   4202       O  
ATOM   2257  CB  ILE A 367      -5.864 -29.571 -15.265  1.00 63.40           C  
ANISOU 2257  CB  ILE A 367     7888   8178   8021  -2624    458   3900       C  
ATOM   2258  CG1 ILE A 367      -6.477 -30.001 -16.599  1.00 62.66           C  
ANISOU 2258  CG1 ILE A 367     7723   7907   8177  -2732    362   3774       C  
ATOM   2259  CG2 ILE A 367      -5.722 -30.765 -14.332  1.00 68.12           C  
ANISOU 2259  CG2 ILE A 367     8660   8629   8592  -2783    449   4201       C  
ATOM   2260  CD1 ILE A 367      -5.692 -31.079 -17.314  1.00 62.42           C  
ANISOU 2260  CD1 ILE A 367     7919   7484   8314  -2707    171   3760       C  
ATOM   2261  N   LEU A 368      -5.109 -27.239 -13.282  1.00 77.01           N  
ANISOU 2261  N   LEU A 368     9579  10484   9199  -2282    676   3817       N  
ATOM   2262  CA  LEU A 368      -4.447 -26.794 -12.061  1.00 77.15           C  
ANISOU 2262  CA  LEU A 368     9715  10655   8946  -2179    714   3887       C  
ATOM   2263  C   LEU A 368      -5.386 -25.972 -11.185  1.00 78.56           C  
ANISOU 2263  C   LEU A 368     9773  11173   8903  -2210    943   3890       C  
ATOM   2264  O   LEU A 368      -5.377 -26.102  -9.962  1.00 79.79           O  
ANISOU 2264  O   LEU A 368    10033  11464   8822  -2250   1030   4053       O  
ATOM   2265  CB  LEU A 368      -3.197 -25.976 -12.396  1.00 57.64           C  
ANISOU 2265  CB  LEU A 368     7309   8148   6442  -1935    579   3695       C  
ATOM   2266  CG  LEU A 368      -2.071 -26.705 -13.132  1.00 56.30           C  
ANISOU 2266  CG  LEU A 368     7267   7674   6449  -1854    372   3700       C  
ATOM   2267  CD1 LEU A 368      -0.927 -25.750 -13.441  1.00 52.67           C  
ANISOU 2267  CD1 LEU A 368     6827   7240   5946  -1628    268   3520       C  
ATOM   2268  CD2 LEU A 368      -1.579 -27.892 -12.324  1.00 60.19           C  
ANISOU 2268  CD2 LEU A 368     7943   8022   6904  -1930    306   3977       C  
ATOM   2269  N   TYR A 369      -6.195 -25.129 -11.822  1.00 87.48           N  
ANISOU 2269  N   TYR A 369    10691  12444  10105  -2181   1041   3708       N  
ATOM   2270  CA  TYR A 369      -7.128 -24.258 -11.111  1.00 89.14           C  
ANISOU 2270  CA  TYR A 369    10763  12976  10130  -2170   1274   3677       C  
ATOM   2271  C   TYR A 369      -8.132 -25.061 -10.288  1.00 91.48           C  
ANISOU 2271  C   TYR A 369    11008  13399  10354  -2397   1456   3937       C  
ATOM   2272  O   TYR A 369      -8.458 -24.696  -9.158  1.00 93.08           O  
ANISOU 2272  O   TYR A 369    11228  13848  10293  -2388   1642   4004       O  
ATOM   2273  CB  TYR A 369      -7.877 -23.357 -12.095  1.00 64.61           C  
ANISOU 2273  CB  TYR A 369     7417   9961   7170  -2094   1322   3455       C  
ATOM   2274  CG  TYR A 369      -6.992 -22.466 -12.938  1.00 59.55           C  
ANISOU 2274  CG  TYR A 369     6820   9225   6579  -1879   1169   3205       C  
ATOM   2275  CD1 TYR A 369      -5.737 -22.070 -12.492  1.00 57.78           C  
ANISOU 2275  CD1 TYR A 369     6799   8954   6200  -1736   1067   3157       C  
ATOM   2276  CD2 TYR A 369      -7.418 -22.015 -14.183  1.00 56.88           C  
ANISOU 2276  CD2 TYR A 369     6317   8853   6441  -1832   1118   3030       C  
ATOM   2277  CE1 TYR A 369      -4.930 -21.254 -13.264  1.00 53.60           C  
ANISOU 2277  CE1 TYR A 369     6296   8346   5722  -1563    934   2948       C  
ATOM   2278  CE2 TYR A 369      -6.621 -21.198 -14.962  1.00 52.64           C  
ANISOU 2278  CE2 TYR A 369     5827   8232   5939  -1650    986   2822       C  
ATOM   2279  CZ  TYR A 369      -5.378 -20.822 -14.498  1.00 51.05           C  
ANISOU 2279  CZ  TYR A 369     5819   7986   5590  -1522    902   2784       C  
ATOM   2280  OH  TYR A 369      -4.578 -20.012 -15.269  1.00 47.26           O  
ANISOU 2280  OH  TYR A 369     5373   7432   5151  -1364    778   2594       O  
ATOM   2281  N   ASN A 370      -8.616 -26.157 -10.866  1.00 80.29           N  
ANISOU 2281  N   ASN A 370     9535  11811   9161  -2609   1403   4083       N  
ATOM   2282  CA  ASN A 370      -9.599 -27.010 -10.208  1.00 85.69           C  
ANISOU 2282  CA  ASN A 370    10162  12588   9809  -2867   1561   4358       C  
ATOM   2283  C   ASN A 370      -9.034 -27.777  -9.018  1.00 88.84           C  
ANISOU 2283  C   ASN A 370    10818  12943   9995  -2936   1556   4613       C  
ATOM   2284  O   ASN A 370      -9.737 -28.020  -8.037  1.00 92.92           O  
ANISOU 2284  O   ASN A 370    11323  13696  10287  -3033   1765   4782       O  
ATOM   2285  CB  ASN A 370     -10.209 -27.991 -11.210  1.00104.36           C  
ANISOU 2285  CB  ASN A 370    12422  14742  12487  -3100   1468   4444       C  
ATOM   2286  CG  ASN A 370     -11.282 -27.355 -12.070  1.00104.72           C  
ANISOU 2286  CG  ASN A 370    12153  14926  12707  -3115   1531   4281       C  
ATOM   2287  OD1 ASN A 370     -10.989 -26.665 -13.046  1.00103.90           O  
ANISOU 2287  OD1 ASN A 370    11951  14962  12564  -2895   1559   4043       O  
ATOM   2288  ND2 ASN A 370     -12.537 -27.594 -11.714  1.00106.18           N  
ANISOU 2288  ND2 ASN A 370    12180  15070  13091  -3386   1544   4421       N  
ATOM   2289  N   LEU A 371      -7.765 -28.156  -9.111  1.00 82.92           N  
ANISOU 2289  N   LEU A 371    10297  11896   9313  -2878   1321   4645       N  
ATOM   2290  CA  LEU A 371      -7.121 -28.940  -8.064  1.00 86.25           C  
ANISOU 2290  CA  LEU A 371    10971  12222   9578  -2944   1264   4911       C  
ATOM   2291  C   LEU A 371      -6.891 -28.134  -6.790  1.00 87.77           C  
ANISOU 2291  C   LEU A 371    11266  12698   9386  -2849   1391   4952       C  
ATOM   2292  O   LEU A 371      -7.261 -28.563  -5.698  1.00 92.61           O  
ANISOU 2292  O   LEU A 371    11979  13407   9801  -2997   1498   5217       O  
ATOM   2293  CB  LEU A 371      -5.792 -29.507  -8.568  1.00 79.24           C  
ANISOU 2293  CB  LEU A 371    10285  10984   8839  -2823    981   4890       C  
ATOM   2294  CG  LEU A 371      -5.878 -30.593  -9.641  1.00 80.40           C  
ANISOU 2294  CG  LEU A 371    10494  10762   9293  -2969    829   4998       C  
ATOM   2295  CD1 LEU A 371      -4.500 -30.902 -10.197  1.00 80.17           C  
ANISOU 2295  CD1 LEU A 371    10239  10727   9496  -3129    894   4902       C  
ATOM   2296  CD2 LEU A 371      -6.522 -31.850  -9.074  1.00 76.80           C  
ANISOU 2296  CD2 LEU A 371    10183  10017   8980  -2757    585   4870       C  
ATOM   2297  N   VAL A 372      -6.283 -26.963  -6.940  1.00 93.89           N  
ANISOU 2297  N   VAL A 372    12028  13601  10044  -2613   1376   4693       N  
ATOM   2298  CA  VAL A 372      -5.872 -26.150  -5.800  1.00 94.86           C  
ANISOU 2298  CA  VAL A 372    12288  13962   9794  -2509   1457   4692       C  
ATOM   2299  C   VAL A 372      -7.037 -25.426  -5.119  1.00 96.98           C  
ANISOU 2299  C   VAL A 372    12415  14587   9845  -2549   1774   4667       C  
ATOM   2300  O   VAL A 372      -7.090 -25.338  -3.891  1.00 99.08           O  
ANISOU 2300  O   VAL A 372    12800  15041   9804  -2621   1915   4842       O  
ATOM   2301  CB  VAL A 372      -4.789 -25.130  -6.218  1.00 75.84           C  
ANISOU 2301  CB  VAL A 372     9951  11523   7342  -2254   1290   4431       C  
ATOM   2302  CG1 VAL A 372      -5.296 -24.258  -7.352  1.00 71.27           C  
ANISOU 2302  CG1 VAL A 372     9158  10939   6982  -2143   1304   4139       C  
ATOM   2303  CG2 VAL A 372      -4.350 -24.283  -5.032  1.00 77.33           C  
ANISOU 2303  CG2 VAL A 372    10278  11967   7136  -2162   1374   4393       C  
ATOM   2304  N   SER A 373      -7.973 -24.919  -5.915  1.00 91.42           N  
ANISOU 2304  N   SER A 373    11459  13981   9294  -2492   1888   4455       N  
ATOM   2305  CA  SER A 373      -9.065 -24.112  -5.386  1.00 93.55           C  
ANISOU 2305  CA  SER A 373    11565  14593   9387  -2473   2195   4391       C  
ATOM   2306  C   SER A 373     -10.386 -24.871  -5.400  1.00 95.17           C  
ANISOU 2306  C   SER A 373    11524  14892   9746  -2706   2387   4572       C  
ATOM   2307  O   SER A 373     -10.833 -25.339  -6.447  1.00 94.24           O  
ANISOU 2307  O   SER A 373    11225  14621   9962  -2789   2299   4544       O  
ATOM   2308  CB  SER A 373      -9.199 -22.809  -6.178  1.00 81.05           C  
ANISOU 2308  CB  SER A 373     9854  13084   7856  -2233   2206   4044       C  
ATOM   2309  OG  SER A 373     -10.235 -21.998  -5.654  1.00 83.54           O  
ANISOU 2309  OG  SER A 373     9980  13711   8052  -2192   2509   3975       O  
ATOM   2310  N   ALA A 374     -11.005 -24.987  -4.230  1.00128.89           N  
ANISOU 2310  N   ALA A 374    15787  19424  13761  -2822   2649   4761       N  
ATOM   2311  CA  ALA A 374     -12.292 -25.657  -4.107  1.00130.83           C  
ANISOU 2311  CA  ALA A 374    15779  19806  14122  -3066   2863   4964       C  
ATOM   2312  C   ALA A 374     -13.398 -24.817  -4.736  1.00131.45           C  
ANISOU 2312  C   ALA A 374    15494  20075  14376  -2979   3024   4758       C  
ATOM   2313  O   ALA A 374     -14.336 -25.352  -5.326  1.00132.28           O  
ANISOU 2313  O   ALA A 374    15330  20198  14732  -3173   3085   4868       O  
ATOM   2314  CB  ALA A 374     -12.605 -25.943  -2.648  1.00160.02           C  
ANISOU 2314  CB  ALA A 374    19564  23770  17464  -3194   3128   5216       C  
ATOM   2315  N   ASN A 375     -13.276 -23.499  -4.607  1.00151.21           N  
ANISOU 2315  N   ASN A 375    17992  22710  16753  -2690   3079   4467       N  
ATOM   2316  CA  ASN A 375     -14.262 -22.572  -5.152  1.00152.17           C  
ANISOU 2316  CA  ASN A 375    17783  23015  17019  -2560   3232   4265       C  
ATOM   2317  C   ASN A 375     -14.368 -22.678  -6.668  1.00150.13           C  
ANISOU 2317  C   ASN A 375    17352  22522  17169  -2572   2993   4146       C  
ATOM   2318  O   ASN A 375     -15.429 -23.009  -7.207  1.00151.13           O  
ANISOU 2318  O   ASN A 375    17153  22740  17530  -2681   3075   4183       O  
ATOM   2319  CB  ASN A 375     -13.915 -21.135  -4.758  1.00149.57           C  
ANISOU 2319  CB  ASN A 375    17546  22841  16443  -2237   3328   3979       C  
ATOM   2320  CG  ASN A 375     -13.650 -20.986  -3.274  1.00151.60           C  
ANISOU 2320  CG  ASN A 375    18053  23293  16253  -2209   3513   4060       C  
ATOM   2321  OD1 ASN A 375     -14.574 -20.808  -2.481  1.00154.43           O  
ANISOU 2321  OD1 ASN A 375    18290  23971  16416  -2185   3845   4090       O  
ATOM   2322  ND2 ASN A 375     -12.380 -21.056  -2.890  1.00150.33           N  
ANISOU 2322  ND2 ASN A 375    18241  22953  15923  -2205   3298   4095       N  
ATOM   2323  N   PHE A 376     -13.255 -22.405  -7.346  1.00163.36           N  
ANISOU 2323  N   PHE A 376    19242  23908  18921  -2465   2699   4008       N  
ATOM   2324  CA  PHE A 376     -13.197 -22.457  -8.803  1.00161.46           C  
ANISOU 2324  CA  PHE A 376    18888  23432  19027  -2468   2463   3886       C  
ATOM   2325  C   PHE A 376     -13.604 -23.829  -9.323  1.00161.63           C  
ANISOU 2325  C   PHE A 376    18822  23303  19288  -2782   2387   4124       C  
ATOM   2326  O   PHE A 376     -14.136 -23.947 -10.422  1.00161.81           O  
ANISOU 2326  O   PHE A 376    18610  23279  19591  -2871   2321   4086       O  
ATOM   2327  CB  PHE A 376     -11.793 -22.104  -9.303  1.00132.97           C  
ANISOU 2327  CB  PHE A 376    15546  19552  15423  -2307   2185   3727       C  
ATOM   2328  CG  PHE A 376     -11.689 -22.006 -10.801  1.00132.24           C  
ANISOU 2328  CG  PHE A 376    15523  19561  15160  -2018   2210   3465       C  
ATOM   2329  CD1 PHE A 376     -11.931 -20.804 -11.446  1.00131.71           C  
ANISOU 2329  CD1 PHE A 376    15311  19471  15263  -1854   2143   3224       C  
ATOM   2330  CD2 PHE A 376     -11.348 -23.112 -11.564  1.00132.27           C  
ANISOU 2330  CD2 PHE A 376    15755  19672  14828  -1920   2285   3463       C  
ATOM   2331  CE1 PHE A 376     -11.837 -20.708 -12.821  1.00131.32           C  
ANISOU 2331  CE1 PHE A 376    15345  19484  15067  -1600   2155   2992       C  
ATOM   2332  CE2 PHE A 376     -11.255 -23.022 -12.940  1.00131.85           C  
ANISOU 2332  CE2 PHE A 376    15789  19686  14621  -1673   2291   3216       C  
ATOM   2333  CZ  PHE A 376     -11.498 -21.818 -13.569  1.00131.40           C  
ANISOU 2333  CZ  PHE A 376    15588  19587  14752  -1514   2228   2981       C  
ATOM   2334  N   ARG A 377     -13.344 -24.862  -8.530  1.00104.94           N  
ANISOU 2334  N   ARG A 377    11844  16045  11984  -2956   2387   4377       N  
ATOM   2335  CA  ARG A 377     -13.752 -26.214  -8.880  1.00105.48           C  
ANISOU 2335  CA  ARG A 377    11887  15942  12249  -3274   2316   4633       C  
ATOM   2336  C   ARG A 377     -15.270 -26.340  -8.812  1.00108.31           C  
ANISOU 2336  C   ARG A 377    11903  16573  12679  -3480   2564   4781       C  
ATOM   2337  O   ARG A 377     -15.895 -26.928  -9.696  1.00109.23           O  
ANISOU 2337  O   ARG A 377    11893  16570  13041  -3754   2496   4936       O  
ATOM   2338  CB  ARG A 377     -13.088 -27.223  -7.944  1.00117.83           C  
ANISOU 2338  CB  ARG A 377    13773  17364  13632  -3380   2263   4878       C  
ATOM   2339  CG  ARG A 377     -13.491 -28.666  -8.178  1.00119.60           C  
ANISOU 2339  CG  ARG A 377    14031  17381  14029  -3715   2194   5175       C  
ATOM   2340  CD  ARG A 377     -12.537 -29.603  -7.459  1.00119.19           C  
ANISOU 2340  CD  ARG A 377    14344  17119  13824  -3742   2068   5372       C  
ATOM   2341  NE  ARG A 377     -12.313 -29.189  -6.077  1.00120.33           N  
ANISOU 2341  NE  ARG A 377    14592  17544  13584  -3701   2279   5499       N  
ATOM   2342  CZ  ARG A 377     -11.218 -29.473  -5.381  1.00120.29           C  
ANISOU 2342  CZ  ARG A 377    14889  17477  13340  -3565   2181   5533       C  
ATOM   2343  NH1 ARG A 377     -10.239 -30.170  -5.940  1.00119.22           N  
ANISOU 2343  NH1 ARG A 377    14952  17017  13329  -3444   1888   5455       N  
ATOM   2344  NH2 ARG A 377     -11.097 -29.054  -4.129  1.00121.57           N  
ANISOU 2344  NH2 ARG A 377    15148  17914  13131  -3545   2376   5642       N  
ATOM   2345  N   GLN A 378     -15.856 -25.772  -7.762  1.00177.15           N  
ANISOU 2345  N   GLN A 378    20465  25656  21187  -3346   2851   4726       N  
ATOM   2346  CA  GLN A 378     -17.304 -25.792  -7.583  1.00179.82           C  
ANISOU 2346  CA  GLN A 378    20427  26305  21593  -3497   3119   4847       C  
ATOM   2347  C   GLN A 378     -18.025 -25.034  -8.693  1.00179.59           C  
ANISOU 2347  C   GLN A 378    20058  26330  21847  -3402   3068   4637       C  
ATOM   2348  O   GLN A 378     -19.099 -25.443  -9.133  1.00180.76           O  
ANISOU 2348  O   GLN A 378    19897  26553  22231  -3628   3102   4761       O  
ATOM   2349  CB  GLN A 378     -17.693 -25.220  -6.217  1.00204.89           C  
ANISOU 2349  CB  GLN A 378    23582  29862  24407  -3389   3480   4894       C  
ATOM   2350  CG  GLN A 378     -17.399 -26.144  -5.047  1.00206.44           C  
ANISOU 2350  CG  GLN A 378    23493  30374  24573  -3124   3703   4661       C  
ATOM   2351  CD  GLN A 378     -17.688 -25.497  -3.707  1.00208.73           C  
ANISOU 2351  CD  GLN A 378    23339  30904  25067  -3274   3903   4763       C  
ATOM   2352  OE1 GLN A 378     -18.013 -24.312  -3.632  1.00209.95           O  
ANISOU 2352  OE1 GLN A 378    23474  31056  25242  -3508   3985   4954       O  
ATOM   2353  NE2 GLN A 378     -17.571 -26.276  -2.638  1.00209.55           N  
ANISOU 2353  NE2 GLN A 378    23118  31154  25348  -3103   3938   4581       N  
ATOM   2354  N   VAL A 379     -17.433 -23.931  -9.145  1.00210.18           N  
ANISOU 2354  N   VAL A 379    23993  30162  25705  -3085   2969   4332       N  
ATOM   2355  CA  VAL A 379     -18.039 -23.134 -10.210  1.00210.22           C  
ANISOU 2355  CA  VAL A 379    23690  30230  25953  -2968   2920   4136       C  
ATOM   2356  C   VAL A 379     -17.837 -23.795 -11.583  1.00208.37           C  
ANISOU 2356  C   VAL A 379    23451  29679  26042  -3117   2589   4107       C  
ATOM   2357  O   VAL A 379     -18.736 -23.791 -12.441  1.00208.98           O  
ANISOU 2357  O   VAL A 379    23219  29820  26364  -3168   2541   4061       O  
ATOM   2358  CB  VAL A 379     -17.497 -21.690 -10.211  1.00 94.34           C  
ANISOU 2358  CB  VAL A 379     9069  15629  11147  -2577   2945   3828       C  
ATOM   2359  CG1 VAL A 379     -18.417 -20.785 -10.997  1.00 98.06           C  
ANISOU 2359  CG1 VAL A 379     9403  16476  11376  -2422   3311   3819       C  
ATOM   2360  CG2 VAL A 379     -17.373 -21.173  -8.788  1.00 89.64           C  
ANISOU 2360  CG2 VAL A 379     8889  14777  10391  -2439   2751   3713       C  
ATOM   2361  N   PHE A 380     -16.652 -24.371 -11.772  1.00143.93           N  
ANISOU 2361  N   PHE A 380    15630  21182  17877  -3177   2359   4131       N  
ATOM   2362  CA  PHE A 380     -16.329 -25.135 -12.972  1.00142.33           C  
ANISOU 2362  CA  PHE A 380    15467  20660  17953  -3319   2057   4099       C  
ATOM   2363  C   PHE A 380     -17.335 -26.267 -13.130  1.00144.18           C  
ANISOU 2363  C   PHE A 380    15473  20929  18379  -3688   2093   4345       C  
ATOM   2364  O   PHE A 380     -17.810 -26.541 -14.232  1.00144.46           O  
ANISOU 2364  O   PHE A 380    15265  20959  18666  -3797   1983   4299       O  
ATOM   2365  CB  PHE A 380     -14.911 -25.706 -12.864  1.00156.53           C  
ANISOU 2365  CB  PHE A 380    17673  22105  19695  -3301   1845   4103       C  
ATOM   2366  CG  PHE A 380     -14.370 -26.260 -14.155  1.00154.99           C  
ANISOU 2366  CG  PHE A 380    17570  21557  19761  -3409   1544   4040       C  
ATOM   2367  CD1 PHE A 380     -14.763 -27.508 -14.611  1.00153.14           C  
ANISOU 2367  CD1 PHE A 380    17674  21005  19505  -3331   1348   3996       C  
ATOM   2368  CD2 PHE A 380     -13.455 -25.537 -14.905  1.00155.62           C  
ANISOU 2368  CD2 PHE A 380    17404  21627  20097  -3580   1454   4021       C  
ATOM   2369  CE1 PHE A 380     -14.267 -28.019 -15.795  1.00152.05           C  
ANISOU 2369  CE1 PHE A 380    17643  20544  19582  -3406   1096   3921       C  
ATOM   2370  CE2 PHE A 380     -12.955 -26.044 -16.091  1.00154.45           C  
ANISOU 2370  CE2 PHE A 380    17379  21152  20153  -3677   1179   3946       C  
ATOM   2371  CZ  PHE A 380     -13.361 -27.287 -16.535  1.00152.71           C  
ANISOU 2371  CZ  PHE A 380    17513  20613  19895  -3582   1012   3889       C  
ATOM   2372  N   LEU A 381     -17.652 -26.922 -12.018  1.00106.29           N  
ANISOU 2372  N   LEU A 381    10755  16176  13455  -3892   2240   4616       N  
ATOM   2373  CA  LEU A 381     -18.640 -27.992 -12.018  1.00108.31           C  
ANISOU 2373  CA  LEU A 381    10810  16465  13878  -4277   2287   4887       C  
ATOM   2374  C   LEU A 381     -20.058 -27.429 -12.056  1.00110.52           C  
ANISOU 2374  C   LEU A 381    10606  17128  14259  -4310   2492   4893       C  
ATOM   2375  O   LEU A 381     -21.005 -28.142 -12.381  1.00112.35           O  
ANISOU 2375  O   LEU A 381    10605  17339  14746  -4564   2409   4974       O  
ATOM   2376  CB  LEU A 381     -18.457 -28.902 -10.800  1.00108.26           C  
ANISOU 2376  CB  LEU A 381    10987  16472  13673  -4465   2442   5191       C  
ATOM   2377  CG  LEU A 381     -17.155 -29.704 -10.751  1.00106.58           C  
ANISOU 2377  CG  LEU A 381    11219  15847  13429  -4509   2211   5260       C  
ATOM   2378  CD1 LEU A 381     -17.126 -30.610  -9.531  1.00109.61           C  
ANISOU 2378  CD1 LEU A 381    11803  16241  13601  -4628   2352   5511       C  
ATOM   2379  CD2 LEU A 381     -16.972 -30.510 -12.030  1.00106.23           C  
ANISOU 2379  CD2 LEU A 381    11227  15428  13708  -4731   1911   5263       C  
ATOM   2380  N   SER A 382     -20.201 -26.151 -11.719  1.00345.43           N  
ANISOU 2380  N   SER A 382    40233  47201  43815  -4020   2738   4771       N  
ATOM   2381  CA  SER A 382     -21.499 -25.492 -11.796  1.00347.73           C  
ANISOU 2381  CA  SER A 382    40054  47874  44195  -3982   2954   4760       C  
ATOM   2382  C   SER A 382     -21.907 -25.331 -13.252  1.00346.98           C  
ANISOU 2382  C   SER A 382    39726  47712  44401  -3935   2722   4574       C  
ATOM   2383  O   SER A 382     -23.059 -25.580 -13.611  1.00348.79           O  
ANISOU 2383  O   SER A 382    39576  48108  44843  -4082   2750   4640       O  
ATOM   2384  CB  SER A 382     -21.463 -24.125 -11.108  1.00204.30           C  
ANISOU 2384  CB  SER A 382    21866  30017  25743  -3627   3251   4624       C  
ATOM   2385  OG  SER A 382     -20.953 -24.222  -9.788  1.00204.17           O  
ANISOU 2385  OG  SER A 382    22161  30014  25402  -3626   3404   4743       O  
ATOM   2386  N   THR A 383     -20.960 -24.914 -14.089  1.00170.59           N  
ANISOU 2386  N   THR A 383    17636  25112  22069  -3712   2475   4321       N  
ATOM   2387  CA  THR A 383     -21.223 -24.796 -15.524  1.00169.79           C  
ANISOU 2387  CA  THR A 383    17373  24927  22213  -3647   2234   4134       C  
ATOM   2388  C   THR A 383     -21.487 -26.149 -16.158  1.00169.51           C  
ANISOU 2388  C   THR A 383    17294  24660  22453  -4008   1965   4241       C  
ATOM   2389  O   THR A 383     -22.547 -26.384 -16.742  1.00169.94           O  
ANISOU 2389  O   THR A 383    17052  24783  22734  -4075   1840   4193       O  
ATOM   2390  CB  THR A 383     -20.021 -24.169 -16.267  1.00130.13           C  
ANISOU 2390  CB  THR A 383    12660  19683  17100  -3328   2053   3852       C  
ATOM   2391  OG1 THR A 383     -18.857 -24.259 -15.436  1.00128.61           O  
ANISOU 2391  OG1 THR A 383    12863  19328  16674  -3278   2079   3882       O  
ATOM   2392  CG2 THR A 383     -20.285 -22.704 -16.580  1.00130.86           C  
ANISOU 2392  CG2 THR A 383    12585  20025  17112  -2966   2199   3654       C  
ATOM   2393  N   LEU A 384     -20.489 -27.022 -16.055  1.00137.75           N  
ANISOU 2393  N   LEU A 384    13578  20351  18409  -4237   1862   4383       N  
ATOM   2394  CA  LEU A 384     -20.538 -28.352 -16.654  1.00137.73           C  
ANISOU 2394  CA  LEU A 384    13593  20083  18652  -4594   1604   4481       C  
ATOM   2395  C   LEU A 384     -21.769 -29.128 -16.191  1.00140.48           C  
ANISOU 2395  C   LEU A 384    13527  20667  19180  -4918   1703   4701       C  
ATOM   2396  O   LEU A 384     -21.709 -29.882 -15.225  1.00141.76           O  
ANISOU 2396  O   LEU A 384    13502  21128  19229  -4856   1996   4783       O  
ATOM   2397  CB  LEU A 384     -19.263 -29.123 -16.309  1.00132.83           C  
ANISOU 2397  CB  LEU A 384    13404  19100  17965  -4746   1499   4602       C  
ATOM   2398  CG  LEU A 384     -18.661 -30.013 -17.391  1.00126.19           C  
ANISOU 2398  CG  LEU A 384    12982  17970  16994  -4460   1347   4392       C  
ATOM   2399  CD1 LEU A 384     -17.242 -30.424 -17.018  1.00127.12           C  
ANISOU 2399  CD1 LEU A 384    13472  17805  17023  -4585   1311   4565       C  
ATOM   2400  CD2 LEU A 384     -19.526 -31.242 -17.629  1.00122.41           C  
ANISOU 2400  CD2 LEU A 384    12568  17248  16693  -4409   1040   4156       C  
TER    2401      LEU A 384                                                      
ATOM   2402  N   SER B  49      -0.214  36.891 -38.393  1.00125.03           N  
ATOM   2403  CA  SER B  49       0.588  37.153 -39.582  1.00125.03           C  
ATOM   2404  C   SER B  49       0.158  36.273 -40.750  1.00125.03           C  
ATOM   2405  O   SER B  49      -1.007  35.889 -40.855  1.00125.03           O  
ATOM   2406  CB  SER B  49       2.075  36.939 -39.286  1.00118.93           C  
ATOM   2407  OG  SER B  49       2.544  37.868 -38.325  1.00118.93           O  
ATOM   2408  N   GLY B  50       1.107  35.958 -41.625  1.00162.91           N  
ATOM   2409  CA  GLY B  50       0.834  35.129 -42.785  1.00162.91           C  
ATOM   2410  C   GLY B  50       1.936  34.119 -43.045  1.00162.91           C  
ATOM   2411  O   GLY B  50       3.043  34.262 -42.526  1.00162.91           O  
ATOM   2412  N   PRO B  51       1.641  33.087 -43.852  1.00213.07           N  
ATOM   2413  CA  PRO B  51       0.335  32.848 -44.478  1.00213.07           C  
ATOM   2414  C   PRO B  51      -0.663  32.238 -43.497  1.00213.07           C  
ATOM   2415  O   PRO B  51      -0.330  32.047 -42.327  1.00213.07           O  
ATOM   2416  CB  PRO B  51       0.665  31.844 -45.582  1.00 88.90           C  
ATOM   2417  CG  PRO B  51       1.825  31.086 -45.044  1.00 88.90           C  
ATOM   2418  CD  PRO B  51       2.638  32.080 -44.261  1.00 88.90           C  
ATOM   2419  N   ASN B  52      -1.867  31.932 -43.972  1.00124.48           N  
ANISOU 2419  N   ASN B  52    22537   7964  16799    473  -4782   3327       N  
ATOM   2420  CA  ASN B  52      -2.923  31.409 -43.107  1.00120.73           C  
ANISOU 2420  CA  ASN B  52    21756   7959  16158    303  -4701   3514       C  
ATOM   2421  C   ASN B  52      -2.747  29.943 -42.720  1.00116.14           C  
ANISOU 2421  C   ASN B  52    20972   7642  15515    263  -4560   3329       C  
ATOM   2422  O   ASN B  52      -3.697  29.161 -42.754  1.00114.60           O  
ANISOU 2422  O   ASN B  52    20822   7448  15276    -48  -4486   3222       O  
ATOM   2423  CB  ASN B  52      -4.300  31.627 -43.740  1.00155.37           C  
ANISOU 2423  CB  ASN B  52    26186  12447  20400   -194  -4711   3811       C  
ATOM   2424  CG  ASN B  52      -4.742  33.076 -43.690  1.00156.11           C  
ANISOU 2424  CG  ASN B  52    26461  12364  20489   -600  -4699   3755       C  
ATOM   2425  OD1 ASN B  52      -3.923  33.984 -43.542  1.00153.04           O  
ANISOU 2425  OD1 ASN B  52    25929  12215  20004   -887  -4588   3725       O  
ATOM   2426  ND2 ASN B  52      -6.045  33.301 -43.808  1.00160.44           N  
ANISOU 2426  ND2 ASN B  52    27317  12497  21146   -629  -4821   3745       N  
ATOM   2427  N   SER B  53      -1.523  29.580 -42.355  1.00279.01           N  
ANISOU 2427  N   SER B  53    41241  28647  36123    565  -4441   3222       N  
ATOM   2428  CA  SER B  53      -1.238  28.261 -41.811  1.00275.07           C  
ANISOU 2428  CA  SER B  53    40367  28611  35534    533  -4197   2989       C  
ATOM   2429  C   SER B  53      -0.774  28.429 -40.372  1.00276.82           C  
ANISOU 2429  C   SER B  53    40683  28684  35811    543  -4110   2668       C  
ATOM   2430  O   SER B  53       0.389  28.184 -40.050  1.00275.46           O  
ANISOU 2430  O   SER B  53    40484  28631  35546    188  -4025   2623       O  
ATOM   2431  CB  SER B  53      -0.163  27.557 -42.638  1.00 99.33           C  
ANISOU 2431  CB  SER B  53    17920   6739  13081     95  -4094   3167       C  
ATOM   2432  OG  SER B  53       1.027  28.324 -42.686  1.00101.65           O  
ANISOU 2432  OG  SER B  53    18209   7122  13291     38  -4191   3481       O  
ATOM   2433  N   ASP B  54      -1.693  28.857 -39.512  1.00124.27           N  
ANISOU 2433  N   ASP B  54    21469   9113  16635    956  -4130   2444       N  
ATOM   2434  CA  ASP B  54      -1.364  29.172 -38.124  1.00125.14           C  
ANISOU 2434  CA  ASP B  54    21736   9033  16779    987  -4063   2130       C  
ATOM   2435  C   ASP B  54      -1.025  27.939 -37.285  1.00121.53           C  
ANISOU 2435  C   ASP B  54    20926   9019  16230   1021  -3818   1873       C  
ATOM   2436  O   ASP B  54      -1.727  27.611 -36.329  1.00122.78           O  
ANISOU 2436  O   ASP B  54    21048   9159  16442   1357  -3717   1596       O  
ATOM   2437  CB  ASP B  54      -2.497  29.970 -37.470  1.00162.71           C  
ANISOU 2437  CB  ASP B  54    26783  13326  21712   1424  -4164   1973       C  
ATOM   2438  CG  ASP B  54      -3.845  29.295 -37.614  1.00168.23           C  
ANISOU 2438  CG  ASP B  54    27910  13498  22510   1354  -4425   2206       C  
ATOM   2439  OD1 ASP B  54      -3.945  28.330 -38.401  1.00171.09           O  
ANISOU 2439  OD1 ASP B  54    28632  13495  22879   1090  -4525   2174       O  
ATOM   2440  OD2 ASP B  54      -4.804  29.735 -36.947  1.00169.93           O  
ANISOU 2440  OD2 ASP B  54    28110  13659  22795   1551  -4544   2431       O  
ATOM   2441  N   LEU B  55       0.059  27.262 -37.649  1.00 92.11           N  
ANISOU 2441  N   LEU B  55    16948   5690  12362    674  -3717   1978       N  
ATOM   2442  CA  LEU B  55       0.557  26.136 -36.870  1.00 85.95           C  
ANISOU 2442  CA  LEU B  55    15870   5306  11482    616  -3504   1773       C  
ATOM   2443  C   LEU B  55       1.728  26.601 -36.013  1.00 86.37           C  
ANISOU 2443  C   LEU B  55    16132   5200  11486    303  -3519   1653       C  
ATOM   2444  O   LEU B  55       2.516  25.792 -35.524  1.00 82.58           O  
ANISOU 2444  O   LEU B  55    15467   5016  10894     -7  -3425   1667       O  
ATOM   2445  CB  LEU B  55       0.991  24.984 -37.781  1.00 92.93           C  
ANISOU 2445  CB  LEU B  55    16395   6671  12244    407  -3399   1946       C  
ATOM   2446  CG  LEU B  55      -0.077  24.259 -38.609  1.00 90.40           C  
ANISOU 2446  CG  LEU B  55    15743   6675  11930    696  -3315   1961       C  
ATOM   2447  CD1 LEU B  55      -1.367  24.104 -37.813  1.00 95.11           C  
ANISOU 2447  CD1 LEU B  55    16466   7044  12627    936  -3489   2137       C  
ATOM   2448  CD2 LEU B  55      -0.343  24.975 -39.924  1.00 85.99           C  
ANISOU 2448  CD2 LEU B  55    14883   6563  11229    439  -3205   2092       C  
ATOM   2449  N   ASP B  56       1.826  27.914 -35.833  1.00 89.94           N  
ANISOU 2449  N   ASP B  56    16971   5179  12024    395  -3646   1528       N  
ATOM   2450  CA  ASP B  56       2.915  28.519 -35.076  1.00 92.14           C  
ANISOU 2450  CA  ASP B  56    17525   5216  12265     57  -3731   1452       C  
ATOM   2451  C   ASP B  56       2.816  28.201 -33.588  1.00 91.83           C  
ANISOU 2451  C   ASP B  56    17607   5080  12205    239  -3657   1080       C  
ATOM   2452  O   ASP B  56       1.761  28.369 -32.977  1.00 91.59           O  
ANISOU 2452  O   ASP B  56    17533   5047  12218    676  -3559    881       O  
ATOM   2453  CB  ASP B  56       2.921  30.036 -35.276  1.00110.10           C  
ANISOU 2453  CB  ASP B  56    20225   6969  14639    -80  -3976   1633       C  
ATOM   2454  CG  ASP B  56       2.988  30.433 -36.737  1.00110.79           C  
ANISOU 2454  CG  ASP B  56    20497   6728  14870    374  -4064   1627       C  
ATOM   2455  OD1 ASP B  56       1.918  30.575 -37.364  1.00109.17           O  
ANISOU 2455  OD1 ASP B  56    20188   6590  14703    804  -3945   1386       O  
ATOM   2456  OD2 ASP B  56       4.111  30.607 -37.257  1.00114.50           O  
ANISOU 2456  OD2 ASP B  56    21205   6882  15418    303  -4249   1876       O  
ATOM   2457  N   VAL B  57       3.921  27.742 -33.010  1.00 92.19           N  
ANISOU 2457  N   VAL B  57    17791   5065  12171   -109  -3704    995       N  
ATOM   2458  CA  VAL B  57       3.985  27.485 -31.578  1.00 92.00           C  
ANISOU 2458  CA  VAL B  57    17894   4983  12077    -12  -3644    651       C  
ATOM   2459  C   VAL B  57       4.541  28.702 -30.848  1.00 98.49           C  
ANISOU 2459  C   VAL B  57    19202   5304  12915   -237  -3856    559       C  
ATOM   2460  O   VAL B  57       5.685  29.101 -31.066  1.00101.65           O  
ANISOU 2460  O   VAL B  57    19750   5520  13353   -620  -4031    788       O  
ATOM   2461  CB  VAL B  57       4.855  26.258 -31.259  1.00 85.66           C  
ANISOU 2461  CB  VAL B  57    16751   4670  11127   -228  -3490    593       C  
ATOM   2462  CG1 VAL B  57       5.064  26.135 -29.760  1.00 86.10           C  
ANISOU 2462  CG1 VAL B  57    16798   4774  11142   -770  -3608    803       C  
ATOM   2463  CG2 VAL B  57       4.217  24.997 -31.822  1.00 79.52           C  
ANISOU 2463  CG2 VAL B  57    15511   4372  10331    -32  -3287    673       C  
ATOM   2464  N   ASN B  58       3.723  29.289 -29.980  1.00157.26           N  
ANISOU 2464  N   ASN B  58    26902  12523  20325      1  -3838    224       N  
ATOM   2465  CA  ASN B  58       4.096  30.514 -29.283  1.00159.50           C  
ANISOU 2465  CA  ASN B  58    27696  12291  20617   -169  -4047     84       C  
ATOM   2466  C   ASN B  58       4.946  30.277 -28.037  1.00158.55           C  
ANISOU 2466  C   ASN B  58    27612  12294  20337   -524  -4075    -72       C  
ATOM   2467  O   ASN B  58       4.446  30.327 -26.914  1.00160.14           O  
ANISOU 2467  O   ASN B  58    28113  12274  20457   -415  -4097   -387       O  
ATOM   2468  CB  ASN B  58       2.850  31.326 -28.923  1.00182.83           C  
ANISOU 2468  CB  ASN B  58    30992  14842  23632    329  -4037   -200       C  
ATOM   2469  CG  ASN B  58       2.084  31.790 -30.148  1.00187.90           C  
ANISOU 2469  CG  ASN B  58    31660  15275  24459    666  -4072    -28       C  
ATOM   2470  OD1 ASN B  58       2.664  32.001 -31.213  1.00191.81           O  
ANISOU 2470  OD1 ASN B  58    32266  15558  25055    438  -4251    268       O  
ATOM   2471  ND2 ASN B  58       0.774  31.951 -30.002  1.00187.91           N  
ANISOU 2471  ND2 ASN B  58    31543  15351  24502   1207  -3900   -196       N  
ATOM   2472  N   THR B  59       6.233  30.021 -28.247  1.00103.02           N  
ANISOU 2472  N   THR B  59    20277   5613  13254   -944  -4079    151       N  
ATOM   2473  CA  THR B  59       7.184  29.899 -27.149  1.00102.85           C  
ANISOU 2473  CA  THR B  59    20271   5704  13104  -1335  -4151     63       C  
ATOM   2474  C   THR B  59       8.290  30.937 -27.312  1.00109.83           C  
ANISOU 2474  C   THR B  59    21521   6156  14052  -1774  -4443    181       C  
ATOM   2475  O   THR B  59       8.882  31.060 -28.385  1.00111.00           O  
ANISOU 2475  O   THR B  59    21603   6270  14304  -2036  -4531    506       O  
ATOM   2476  CB  THR B  59       7.797  28.489 -27.078  1.00 95.90           C  
ANISOU 2476  CB  THR B  59    18872   5413  12153  -1566  -4016    248       C  
ATOM   2477  OG1 THR B  59       8.343  28.138 -28.355  1.00 95.52           O  
ANISOU 2477  OG1 THR B  59    18645   5438  12210  -1762  -4045    610       O  
ATOM   2478  CG2 THR B  59       6.740  27.468 -26.687  1.00 89.32           C  
ANISOU 2478  CG2 THR B  59    17697   4991  11248  -1167  -3741    117       C  
ATOM   2479  N   ASP B  60       8.559  31.682 -26.244  1.00119.55           N  
ANISOU 2479  N   ASP B  60    23154   7054  15216  -1857  -4592    -85       N  
ATOM   2480  CA  ASP B  60       9.500  32.799 -26.293  1.00126.50           C  
ANISOU 2480  CA  ASP B  60    24442   7464  16160  -2277  -4896    -16       C  
ATOM   2481  C   ASP B  60      10.922  32.383 -26.665  1.00125.63           C  
ANISOU 2481  C   ASP B  60    24070   7608  16056  -2870  -5002    290       C  
ATOM   2482  O   ASP B  60      11.307  31.224 -26.508  1.00119.89           O  
ANISOU 2482  O   ASP B  60    22900   7412  15242  -2973  -4859    354       O  
ATOM   2483  CB  ASP B  60       9.501  33.559 -24.964  1.00126.90           C  
ANISOU 2483  CB  ASP B  60    24888   7244  16085  -2240  -4997   -394       C  
ATOM   2484  CG  ASP B  60       9.801  32.662 -23.779  1.00124.11           C  
ANISOU 2484  CG  ASP B  60    24378   7238  15540  -2400  -4957   -569       C  
ATOM   2485  OD1 ASP B  60       8.848  32.098 -23.203  1.00119.51           O  
ANISOU 2485  OD1 ASP B  60    23624   6945  14839  -2011  -4721   -777       O  
ATOM   2486  OD2 ASP B  60      10.989  32.523 -23.422  1.00125.55           O  
ANISOU 2486  OD2 ASP B  60    24523   7503  15678  -2892  -5129   -475       O  
ATOM   2487  N   ILE B  61      11.694  33.348 -27.155  1.00125.67           N  
ANISOU 2487  N   ILE B  61    24196   7415  16138  -3186  -5170    483       N  
ATOM   2488  CA  ILE B  61      13.057  33.103 -27.614  1.00125.39           C  
ANISOU 2488  CA  ILE B  61    23881   7641  16119  -3730  -5250    795       C  
ATOM   2489  C   ILE B  61      13.983  32.728 -26.458  1.00125.15           C  
ANISOU 2489  C   ILE B  61    23757   7831  15964  -4043  -5329    661       C  
ATOM   2490  O   ILE B  61      14.920  31.952 -26.633  1.00122.71           O  
ANISOU 2490  O   ILE B  61    23071   7909  15645  -4364  -5302    864       O  
ATOM   2491  CB  ILE B  61      13.625  34.335 -28.350  1.00130.03           C  
ANISOU 2491  CB  ILE B  61    24644   7960  16801  -3986  -5414    995       C  
ATOM   2492  CG1 ILE B  61      12.598  34.881 -29.345  1.00131.11           C  
ANISOU 2492  CG1 ILE B  61    24936   7828  17051  -3643  -5367   1093       C  
ATOM   2493  CG2 ILE B  61      14.930  33.991 -29.056  1.00129.56           C  
ANISOU 2493  CG2 ILE B  61    24234   8223  16769  -4501  -5447   1355       C  
ATOM   2494  CD1 ILE B  61      13.073  36.096 -30.111  1.00135.25           C  
ANISOU 2494  CD1 ILE B  61    25923   7872  17596  -3303  -5445    805       C  
ATOM   2495  N   TYR B  62      13.712  33.286 -25.282  1.00127.92           N  
ANISOU 2495  N   TYR B  62    24444   7947  16211  -3934  -5422    321       N  
ATOM   2496  CA  TYR B  62      14.500  33.006 -24.084  1.00128.40           C  
ANISOU 2496  CA  TYR B  62    24466   8192  16130  -4211  -5525    173       C  
ATOM   2497  C   TYR B  62      14.521  31.512 -23.769  1.00123.42           C  
ANISOU 2497  C   TYR B  62    23508   7979  15407  -4154  -5379    123       C  
ATOM   2498  O   TYR B  62      15.588  30.909 -23.607  1.00122.26           O  
ANISOU 2498  O   TYR B  62    23066   8172  15214  -4510  -5433    237       O  
ATOM   2499  CB  TYR B  62      13.938  33.795 -22.897  1.00148.58           C  
ANISOU 2499  CB  TYR B  62    27482  10405  18564  -4031  -5625   -208       C  
ATOM   2500  CG  TYR B  62      14.580  33.479 -21.563  1.00149.74           C  
ANISOU 2500  CG  TYR B  62    27622  10747  18525  -4246  -5722   -400       C  
ATOM   2501  CD1 TYR B  62      15.809  34.023 -21.215  1.00151.44           C  
ANISOU 2501  CD1 TYR B  62    27755  11049  18734  -4743  -5930   -252       C  
ATOM   2502  CD2 TYR B  62      13.946  32.650 -20.645  1.00149.35           C  
ANISOU 2502  CD2 TYR B  62    27643  10806  18298  -3944  -5605   -722       C  
ATOM   2503  CE1 TYR B  62      16.395  33.741 -19.995  1.00152.63           C  
ANISOU 2503  CE1 TYR B  62    27890  11388  18713  -4931  -6035   -410       C  
ATOM   2504  CE2 TYR B  62      14.525  32.363 -19.423  1.00150.53           C  
ANISOU 2504  CE2 TYR B  62    27790  11149  18255  -4135  -5700   -886       C  
ATOM   2505  CZ  TYR B  62      15.749  32.911 -19.103  1.00152.14           C  
ANISOU 2505  CZ  TYR B  62    27909  11433  18463  -4627  -5923   -725       C  
ATOM   2506  OH  TYR B  62      16.328  32.629 -17.887  1.00153.43           O  
ANISOU 2506  OH  TYR B  62    28060  11799  18435  -4811  -6032   -871       O  
ATOM   2507  N   SER B  63      13.332  30.923 -23.694  1.00137.36           N  
ANISOU 2507  N   SER B  63    25251   9797  17142  -3663  -5160    -33       N  
ATOM   2508  CA  SER B  63      13.191  29.499 -23.419  1.00130.39           C  
ANISOU 2508  CA  SER B  63    23900   9496  16144  -3470  -4907    -61       C  
ATOM   2509  C   SER B  63      13.816  28.657 -24.526  1.00126.20           C  
ANISOU 2509  C   SER B  63    22842   9403  15704  -3674  -4795    314       C  
ATOM   2510  O   SER B  63      14.389  27.603 -24.260  1.00122.90           O  
ANISOU 2510  O   SER B  63    22042   9442  15210  -3801  -4714    372       O  
ATOM   2511  CB  SER B  63      11.716  29.131 -23.247  1.00110.12           C  
ANISOU 2511  CB  SER B  63    21345   6963  13532  -2860  -4652   -277       C  
ATOM   2512  OG  SER B  63      10.969  29.464 -24.405  1.00109.37           O  
ANISOU 2512  OG  SER B  63    21205   6752  13598  -2641  -4565    -95       O  
ATOM   2513  N   LYS B  64      13.706  29.126 -25.765  1.00107.93           N  
ANISOU 2513  N   LYS B  64    20525   6939  13545  -3697  -4793    569       N  
ATOM   2514  CA  LYS B  64      14.284  28.419 -26.902  1.00104.48           C  
ANISOU 2514  CA  LYS B  64    19636   6881  13181  -3895  -4685    929       C  
ATOM   2515  C   LYS B  64      15.807  28.365 -26.816  1.00107.12           C  
ANISOU 2515  C   LYS B  64    19799   7376  13524  -4453  -4842   1112       C  
ATOM   2516  O   LYS B  64      16.414  27.325 -27.067  1.00102.83           O  
ANISOU 2516  O   LYS B  64    18799   7319  12954  -4563  -4713   1256       O  
ATOM   2517  CB  LYS B  64      13.853  29.066 -28.221  1.00106.82           C  
ANISOU 2517  CB  LYS B  64    20046   6922  13618  -3860  -4697   1170       C  
ATOM   2518  CG  LYS B  64      12.394  28.840 -28.582  1.00103.23           C  
ANISOU 2518  CG  LYS B  64    19589   6453  13179  -3317  -4507   1091       C  
ATOM   2519  CD  LYS B  64      12.091  29.363 -29.979  1.00107.04           C  
ANISOU 2519  CD  LYS B  64    20250   6625  13796  -3322  -4580   1339       C  
ATOM   2520  CE  LYS B  64      10.662  29.053 -30.393  1.00101.96           C  
ANISOU 2520  CE  LYS B  64    19333   6242  13167  -2952  -4360   1448       C  
ATOM   2521  NZ  LYS B  64      10.371  29.529 -31.771  1.00 99.54           N  
ANISOU 2521  NZ  LYS B  64    19108   5877  12836  -2409  -4243   1153       N  
ATOM   2522  N   VAL B  65      16.416  29.491 -26.457  1.00114.64           N  
ANISOU 2522  N   VAL B  65    21120   7912  14524  -4802  -5127   1109       N  
ATOM   2523  CA  VAL B  65      17.866  29.577 -26.322  1.00117.56           C  
ANISOU 2523  CA  VAL B  65    21310   8446  14910  -5328  -5288   1286       C  
ATOM   2524  C   VAL B  65      18.351  28.754 -25.133  1.00116.12           C  
ANISOU 2524  C   VAL B  65    20971   8550  14601  -5421  -5327   1107       C  
ATOM   2525  O   VAL B  65      19.364  28.057 -25.221  1.00115.10           O  
ANISOU 2525  O   VAL B  65    20435   8814  14483  -5720  -5324   1301       O  
ATOM   2526  CB  VAL B  65      18.339  31.041 -26.179  1.00123.06           C  
ANISOU 2526  CB  VAL B  65    22327   8796  15636  -5529  -5503   1282       C  
ATOM   2527  CG1 VAL B  65      19.829  31.099 -25.874  1.00125.21           C  
ANISOU 2527  CG1 VAL B  65    22354   9315  15906  -6013  -5647   1444       C  
ATOM   2528  CG2 VAL B  65      18.024  31.825 -27.443  1.00124.58           C  
ANISOU 2528  CG2 VAL B  65    22627   8756  15951  -5476  -5470   1502       C  
ATOM   2529  N   LEU B  66      17.620  28.833 -24.024  1.00117.26           N  
ANISOU 2529  N   LEU B  66    21401   8546  14606  -5118  -5334    741       N  
ATOM   2530  CA  LEU B  66      17.956  28.051 -22.837  1.00115.47           C  
ANISOU 2530  CA  LEU B  66    21042   8617  14215  -5136  -5350    553       C  
ATOM   2531  C   LEU B  66      17.922  26.554 -23.143  1.00107.78           C  
ANISOU 2531  C   LEU B  66    19504   8241  13206  -4948  -5069    668       C  
ATOM   2532  O   LEU B  66      18.879  25.825 -22.860  1.00106.98           O  
ANISOU 2532  O   LEU B  66    19065   8504  13080  -5204  -5107    782       O  
ATOM   2533  CB  LEU B  66      16.995  28.378 -21.691  1.00115.03           C  
ANISOU 2533  CB  LEU B  66    21424   8286  13995  -4792  -5365    136       C  
ATOM   2534  CG  LEU B  66      17.265  27.686 -20.354  1.00113.69           C  
ANISOU 2534  CG  LEU B  66    21188   8397  13613  -4774  -5379    -86       C  
ATOM   2535  CD1 LEU B  66      18.644  28.051 -19.830  1.00119.23           C  
ANISOU 2535  CD1 LEU B  66    21890   9115  14297  -5325  -5693     -7       C  
ATOM   2536  CD2 LEU B  66      16.189  28.044 -19.340  1.00115.17           C  
ANISOU 2536  CD2 LEU B  66    21826   8308  13626  -4391  -5344   -495       C  
ATOM   2537  N   VAL B  67      16.816  26.109 -23.731  1.00100.19           N  
ANISOU 2537  N   VAL B  67    18446   7370  12253  -4501  -4800    641       N  
ATOM   2538  CA  VAL B  67      16.640  24.708 -24.099  1.00 92.68           C  
ANISOU 2538  CA  VAL B  67    17000   6941  11275  -4296  -4528    737       C  
ATOM   2539  C   VAL B  67      17.695  24.256 -25.106  1.00 92.03           C  
ANISOU 2539  C   VAL B  67    16496   7158  11313  -4609  -4493   1104       C  
ATOM   2540  O   VAL B  67      18.225  23.153 -25.002  1.00 88.26           O  
ANISOU 2540  O   VAL B  67    15603   7124  10806  -4639  -4377   1196       O  
ATOM   2541  CB  VAL B  67      15.219  24.446 -24.649  1.00 94.26           C  
ANISOU 2541  CB  VAL B  67    17200   7138  11476  -3781  -4272    647       C  
ATOM   2542  CG1 VAL B  67      15.142  23.097 -25.346  1.00 88.93           C  
ANISOU 2542  CG1 VAL B  67    16022   6975  10792  -3615  -4009    776       C  
ATOM   2543  CG2 VAL B  67      14.201  24.524 -23.523  1.00 94.98           C  
ANISOU 2543  CG2 VAL B  67    17631   7025  11434  -3441  -4255    280       C  
ATOM   2544  N   THR B  68      18.006  25.118 -26.069  1.00 96.20           N  
ANISOU 2544  N   THR B  68    17140   7438  11973  -4838  -4589   1316       N  
ATOM   2545  CA  THR B  68      19.048  24.826 -27.048  1.00 96.80           C  
ANISOU 2545  CA  THR B  68    16847   7779  12156  -5164  -4553   1673       C  
ATOM   2546  C   THR B  68      20.394  24.618 -26.359  1.00100.00           C  
ANISOU 2546  C   THR B  68    17052   8385  12561  -5593  -4726   1753       C  
ATOM   2547  O   THR B  68      21.125  23.679 -26.677  1.00 97.66           O  
ANISOU 2547  O   THR B  68    16292   8527  12290  -5699  -4607   1943       O  
ATOM   2548  CB  THR B  68      19.180  25.954 -28.091  1.00101.75           C  
ANISOU 2548  CB  THR B  68    17691   8061  12908  -5361  -4645   1892       C  
ATOM   2549  OG1 THR B  68      17.933  26.123 -28.777  1.00 98.89           O  
ANISOU 2549  OG1 THR B  68    17468   7553  12552  -4952  -4489   1850       O  
ATOM   2550  CG2 THR B  68      20.269  25.628 -29.102  1.00102.97           C  
ANISOU 2550  CG2 THR B  68    17454   8518  13152  -5716  -4589   2267       C  
ATOM   2551  N   ALA B  69      20.708  25.493 -25.408  1.00121.43           N  
ANISOU 2551  N   ALA B  69    20119  10772  15247  -5829  -5013   1603       N  
ATOM   2552  CA  ALA B  69      21.958  25.409 -24.659  1.00124.26           C  
ANISOU 2552  CA  ALA B  69    20325  11287  15602  -6256  -5231   1662       C  
ATOM   2553  C   ALA B  69      22.045  24.111 -23.858  1.00120.37           C  
ANISOU 2553  C   ALA B  69    19510  11235  14988  -6081  -5124   1550       C  
ATOM   2554  O   ALA B  69      23.068  23.419 -23.890  1.00120.17           O  
ANISOU 2554  O   ALA B  69    19066  11587  15005  -6318  -5137   1740       O  
ATOM   2555  CB  ALA B  69      22.108  26.612 -23.741  1.00115.61           C  
ANISOU 2555  CB  ALA B  69    19693   9779  14454  -6426  -5523   1472       C  
ATOM   2556  N   ILE B  70      20.970  23.789 -23.143  1.00100.90           N  
ANISOU 2556  N   ILE B  70    17237   8723  12377  -5660  -5017   1253       N  
ATOM   2557  CA  ILE B  70      20.899  22.541 -22.387  1.00 96.16           C  
ANISOU 2557  CA  ILE B  70    16369   8517  11648  -5455  -4896   1145       C  
ATOM   2558  C   ILE B  70      21.103  21.344 -23.313  1.00 90.62           C  
ANISOU 2558  C   ILE B  70    15128   8274  11027  -5346  -4627   1387       C  
ATOM   2559  O   ILE B  70      21.856  20.419 -22.999  1.00 89.55           O  
ANISOU 2559  O   ILE B  70    14626   8519  10882  -5443  -4616   1482       O  
ATOM   2560  CB  ILE B  70      19.547  22.400 -21.657  1.00 92.67           C  
ANISOU 2560  CB  ILE B  70    16218   7949  11045  -4990  -4770    809       C  
ATOM   2561  CG1 ILE B  70      19.364  23.536 -20.647  1.00 98.65           C  
ANISOU 2561  CG1 ILE B  70    17513   8283  11684  -5079  -5028    531       C  
ATOM   2562  CG2 ILE B  70      19.449  21.053 -20.960  1.00 87.34           C  
ANISOU 2562  CG2 ILE B  70    15231   7705  10248  -4764  -4603    747       C  
ATOM   2563  CD1 ILE B  70      18.045  23.490 -19.907  1.00 96.18           C  
ANISOU 2563  CD1 ILE B  70    17493   7851  11199  -4623  -4891    192       C  
ATOM   2564  N   TYR B  71      20.435  21.385 -24.462  1.00 87.91           N  
ANISOU 2564  N   TYR B  71    14754   7885  10763  -5142  -4422   1486       N  
ATOM   2565  CA  TYR B  71      20.546  20.346 -25.479  1.00 83.26           C  
ANISOU 2565  CA  TYR B  71    13708   7687  10240  -5032  -4161   1703       C  
ATOM   2566  C   TYR B  71      21.980  20.181 -25.974  1.00 86.58           C  
ANISOU 2566  C   TYR B  71    13763   8360  10774  -5437  -4222   2005       C  
ATOM   2567  O   TYR B  71      22.429  19.065 -26.222  1.00 83.72           O  
ANISOU 2567  O   TYR B  71    12975   8409  10425  -5393  -4073   2122       O  
ATOM   2568  CB  TYR B  71      19.629  20.662 -26.664  1.00 80.71           C  
ANISOU 2568  CB  TYR B  71    13475   7219   9971  -4801  -3984   1768       C  
ATOM   2569  CG  TYR B  71      18.216  20.141 -26.523  1.00 75.12           C  
ANISOU 2569  CG  TYR B  71    12872   6496   9177  -4312  -3798   1543       C  
ATOM   2570  CD1 TYR B  71      17.553  20.185 -25.303  1.00 73.75           C  
ANISOU 2570  CD1 TYR B  71    12863   6284   8874  -4119  -3830   1261       C  
ATOM   2571  CD2 TYR B  71      17.541  19.616 -27.617  1.00 71.66           C  
ANISOU 2571  CD2 TYR B  71    12357   6096   8777  -4054  -3591   1622       C  
ATOM   2572  CE1 TYR B  71      16.262  19.713 -25.176  1.00 69.01           C  
ANISOU 2572  CE1 TYR B  71    12328   5691   8202  -3684  -3646   1072       C  
ATOM   2573  CE2 TYR B  71      16.249  19.144 -27.500  1.00 66.97           C  
ANISOU 2573  CE2 TYR B  71    11825   5502   8119  -3626  -3432   1432       C  
ATOM   2574  CZ  TYR B  71      15.615  19.194 -26.278  1.00 65.59           C  
ANISOU 2574  CZ  TYR B  71    11792   5298   7833  -3444  -3452   1162       C  
ATOM   2575  OH  TYR B  71      14.328  18.725 -26.157  1.00 61.26           O  
ANISOU 2575  OH  TYR B  71    11279   4769   7228  -3030  -3280    988       O  
ATOM   2576  N   LEU B  72      22.691  21.295 -26.120  1.00 92.78           N  
ANISOU 2576  N   LEU B  72    14711   8894  11648  -5826  -4434   2137       N  
ATOM   2577  CA  LEU B  72      24.073  21.258 -26.588  1.00 96.90           C  
ANISOU 2577  CA  LEU B  72    14880   9648  12291  -6246  -4499   2441       C  
ATOM   2578  C   LEU B  72      25.013  20.691 -25.527  1.00 98.72           C  
ANISOU 2578  C   LEU B  72    14876  10136  12498  -6442  -4660   2422       C  
ATOM   2579  O   LEU B  72      25.904  19.897 -25.838  1.00 98.94           O  
ANISOU 2579  O   LEU B  72    14433  10557  12602  -6576  -4584   2640       O  
ATOM   2580  CB  LEU B  72      24.537  22.649 -27.027  1.00103.90           C  
ANISOU 2580  CB  LEU B  72    16025  10173  13280  -6641  -4704   2592       C  
ATOM   2581  CG  LEU B  72      23.858  23.225 -28.273  1.00103.32           C  
ANISOU 2581  CG  LEU B  72    16132   9876  13249  -6514  -4560   2699       C  
ATOM   2582  CD1 LEU B  72      24.458  24.573 -28.651  1.00109.99           C  
ANISOU 2582  CD1 LEU B  72    17205  10403  14183  -6887  -4757   2860       C  
ATOM   2583  CD2 LEU B  72      23.944  22.249 -29.438  1.00 99.20           C  
ANISOU 2583  CD2 LEU B  72    15175   9764  12751  -6366  -4240   2917       C  
ATOM   2584  N   ALA B  73      24.813  21.100 -24.276  1.00100.42           N  
ANISOU 2584  N   ALA B  73    15421  10133  12600  -6448  -4884   2162       N  
ATOM   2585  CA  ALA B  73      25.612  20.580 -23.170  1.00102.50           C  
ANISOU 2585  CA  ALA B  73    15510  10625  12812  -6620  -5070   2126       C  
ATOM   2586  C   ALA B  73      25.424  19.071 -23.032  1.00 96.26           C  
ANISOU 2586  C   ALA B  73    14341  10270  11964  -6285  -4834   2114       C  
ATOM   2587  O   ALA B  73      26.396  18.313 -22.945  1.00 97.26           O  
ANISOU 2587  O   ALA B  73    14043  10761  12149  -6429  -4855   2283       O  
ATOM   2588  CB  ALA B  73      25.247  21.284 -21.873  1.00105.66           C  
ANISOU 2588  CB  ALA B  73    16402  10684  13061  -6655  -5340   1821       C  
ATOM   2589  N   LEU B  74      24.165  18.642 -23.023  1.00 98.39           N  
ANISOU 2589  N   LEU B  74    14760  10494  12132  -5838  -4613   1922       N  
ATOM   2590  CA  LEU B  74      23.838  17.223 -22.964  1.00 96.09           C  
ANISOU 2590  CA  LEU B  74    14153  10570  11788  -5505  -4376   1904       C  
ATOM   2591  C   LEU B  74      24.374  16.493 -24.193  1.00 94.93           C  
ANISOU 2591  C   LEU B  74    13541  10745  11785  -5501  -4146   2184       C  
ATOM   2592  O   LEU B  74      24.712  15.310 -24.125  1.00 93.43           O  
ANISOU 2592  O   LEU B  74    12989  10911  11599  -5355  -4006   2249       O  
ATOM   2593  CB  LEU B  74      22.325  17.024 -22.845  1.00 78.97           C  
ANISOU 2593  CB  LEU B  74    12250   8259   9496  -5055  -4188   1655       C  
ATOM   2594  CG  LEU B  74      21.675  17.517 -21.550  1.00 80.37           C  
ANISOU 2594  CG  LEU B  74    12868   8173   9497  -4970  -4348   1346       C  
ATOM   2595  CD1 LEU B  74      20.161  17.432 -21.646  1.00 75.44           C  
ANISOU 2595  CD1 LEU B  74    12461   7417   8786  -4524  -4125   1137       C  
ATOM   2596  CD2 LEU B  74      22.186  16.723 -20.357  1.00 81.36           C  
ANISOU 2596  CD2 LEU B  74    12865   8543   9503  -5029  -4474   1289       C  
ATOM   2597  N   PHE B  75      24.456  17.209 -25.310  1.00 84.36           N  
ANISOU 2597  N   PHE B  75    12229   9269  10553  -5657  -4105   2350       N  
ATOM   2598  CA  PHE B  75      24.987  16.645 -26.545  1.00 83.50           C  
ANISOU 2598  CA  PHE B  75    11716   9451  10560  -5678  -3880   2617       C  
ATOM   2599  C   PHE B  75      26.467  16.326 -26.411  1.00 88.00           C  
ANISOU 2599  C   PHE B  75    11873  10324  11236  -6013  -3983   2845       C  
ATOM   2600  O   PHE B  75      26.880  15.193 -26.639  1.00 85.95           O  
ANISOU 2600  O   PHE B  75    11198  10442  11018  -5892  -3806   2958       O  
ATOM   2601  CB  PHE B  75      24.770  17.596 -27.724  1.00 85.18           C  
ANISOU 2601  CB  PHE B  75    12102   9429  10835  -5774  -3820   2745       C  
ATOM   2602  CG  PHE B  75      25.322  17.085 -29.025  1.00 84.82           C  
ANISOU 2602  CG  PHE B  75    11673   9681  10871  -5795  -3573   3015       C  
ATOM   2603  CD1 PHE B  75      24.595  16.196 -29.801  1.00 79.19           C  
ANISOU 2603  CD1 PHE B  75    10850   9130  10111  -5421  -3279   2987       C  
ATOM   2604  CD2 PHE B  75      26.568  17.493 -29.474  1.00 90.52           C  
ANISOU 2604  CD2 PHE B  75    12150  10530  11713  -6194  -3631   3294       C  
ATOM   2605  CE1 PHE B  75      25.101  15.724 -30.998  1.00 79.32           C  
ANISOU 2605  CE1 PHE B  75    10545   9417  10176  -5432  -3045   3215       C  
ATOM   2606  CE2 PHE B  75      27.079  17.024 -30.668  1.00 90.59           C  
ANISOU 2606  CE2 PHE B  75    11813  10831  11778  -6200  -3377   3536       C  
ATOM   2607  CZ  PHE B  75      26.344  16.138 -31.431  1.00 84.99           C  
ANISOU 2607  CZ  PHE B  75    11024  10269  10998  -5811  -3082   3486       C  
ATOM   2608  N   VAL B  76      27.266  17.326 -26.051  1.00 94.52           N  
ANISOU 2608  N   VAL B  76    12810  10983  12118  -6434  -4275   2915       N  
ATOM   2609  CA  VAL B  76      28.704  17.114 -25.925  1.00 99.57           C  
ANISOU 2609  CA  VAL B  76    13034  11920  12879  -6783  -4399   3147       C  
ATOM   2610  C   VAL B  76      29.042  16.120 -24.810  1.00 98.28           C  
ANISOU 2610  C   VAL B  76    12652  12029  12660  -6662  -4475   3058       C  
ATOM   2611  O   VAL B  76      29.834  15.198 -25.019  1.00 98.17           O  
ANISOU 2611  O   VAL B  76    12157  12410  12733  -6634  -4357   3233       O  
ATOM   2612  CB  VAL B  76      29.489  18.440 -25.754  1.00106.37           C  
ANISOU 2612  CB  VAL B  76    14068  12547  13799  -7227  -4690   3233       C  
ATOM   2613  CG1 VAL B  76      29.534  19.202 -27.071  1.00107.69           C  
ANISOU 2613  CG1 VAL B  76    14273  12596  14047  -7337  -4550   3427       C  
ATOM   2614  CG2 VAL B  76      28.881  19.298 -24.657  1.00107.63           C  
ANISOU 2614  CG2 VAL B  76    14776  12290  13830  -7249  -4965   2943       C  
ATOM   2615  N   VAL B  77      28.422  16.291 -23.644  1.00101.55           N  
ANISOU 2615  N   VAL B  77    13428  12234  12923  -6568  -4658   2788       N  
ATOM   2616  CA  VAL B  77      28.672  15.396 -22.516  1.00100.93           C  
ANISOU 2616  CA  VAL B  77    13197  12389  12762  -6467  -4757   2704       C  
ATOM   2617  C   VAL B  77      28.281  13.956 -22.847  1.00 96.04           C  
ANISOU 2617  C   VAL B  77    12294  12072  12126  -6036  -4434   2705       C  
ATOM   2618  O   VAL B  77      29.054  13.021 -22.616  1.00 96.06           O  
ANISOU 2618  O   VAL B  77    11903  12418  12178  -6008  -4424   2824       O  
ATOM   2619  CB  VAL B  77      27.928  15.855 -21.244  1.00 97.25           C  
ANISOU 2619  CB  VAL B  77    13229  11628  12095  -6419  -4981   2393       C  
ATOM   2620  CG1 VAL B  77      28.047  14.806 -20.148  1.00 96.23           C  
ANISOU 2620  CG1 VAL B  77    12956  11756  11850  -6275  -5051   2315       C  
ATOM   2621  CG2 VAL B  77      28.471  17.193 -20.767  1.00104.61           C  
ANISOU 2621  CG2 VAL B  77    14446  12262  13041  -6871  -5341   2381       C  
ATOM   2622  N   GLY B  78      27.087  13.788 -23.406  1.00 87.64           N  
ANISOU 2622  N   GLY B  78    11428  10870  11001  -5704  -4180   2581       N  
ATOM   2623  CA  GLY B  78      26.587  12.473 -23.761  1.00 81.60           C  
ANISOU 2623  CA  GLY B  78    10450  10341  10214  -5302  -3881   2560       C  
ATOM   2624  C   GLY B  78      27.401  11.787 -24.842  1.00 81.63           C  
ANISOU 2624  C   GLY B  78     9969  10675  10372  -5303  -3667   2821       C  
ATOM   2625  O   GLY B  78      27.779  10.623 -24.699  1.00 80.13           O  
ANISOU 2625  O   GLY B  78     9452  10787  10209  -5136  -3565   2878       O  
ATOM   2626  N   THR B  79      27.668  12.507 -25.927  1.00 91.50           N  
ANISOU 2626  N   THR B  79    11185  11863  11718  -5483  -3593   2980       N  
ATOM   2627  CA  THR B  79      28.421  11.951 -27.047  1.00 91.43           C  
ANISOU 2627  CA  THR B  79    10740  12163  11836  -5488  -3360   3225       C  
ATOM   2628  C   THR B  79      29.850  11.596 -26.653  1.00 92.91           C  
ANISOU 2628  C   THR B  79    10487  12665  12148  -5723  -3484   3425       C  
ATOM   2629  O   THR B  79      30.312  10.488 -26.924  1.00 92.39           O  
ANISOU 2629  O   THR B  79    10027  12928  12146  -5547  -3300   3529       O  
ATOM   2630  CB  THR B  79      28.444  12.900 -28.261  1.00 83.61           C  
ANISOU 2630  CB  THR B  79     9832  11037  10900  -5671  -3269   3372       C  
ATOM   2631  OG1 THR B  79      28.806  14.219 -27.833  1.00 89.07           O  
ANISOU 2631  OG1 THR B  79    10752  11468  11621  -6069  -3565   3404       O  
ATOM   2632  CG2 THR B  79      27.078  12.942 -28.930  1.00 78.39           C  
ANISOU 2632  CG2 THR B  79     9490  10160  10135  -5365  -3080   3221       C  
ATOM   2633  N   VAL B  80      30.545  12.533 -26.013  1.00 94.76           N  
ANISOU 2633  N   VAL B  80    10788  12794  12425  -6119  -3802   3480       N  
ATOM   2634  CA  VAL B  80      31.910  12.277 -25.562  1.00100.05           C  
ANISOU 2634  CA  VAL B  80    11030  13764  13222  -6370  -3965   3677       C  
ATOM   2635  C   VAL B  80      31.950  11.108 -24.581  1.00 97.79           C  
ANISOU 2635  C   VAL B  80    10595  13680  12882  -6113  -4007   3582       C  
ATOM   2636  O   VAL B  80      32.742  10.178 -24.745  1.00 98.74           O  
ANISOU 2636  O   VAL B  80    10250  14153  13112  -6029  -3904   3745       O  
ATOM   2637  CB  VAL B  80      32.550  13.525 -24.917  1.00103.40           C  
ANISOU 2637  CB  VAL B  80    11628  13997  13662  -6791  -4315   3705       C  
ATOM   2638  CG1 VAL B  80      33.827  13.154 -24.177  1.00106.36           C  
ANISOU 2638  CG1 VAL B  80    11645  14664  14104  -6869  -4458   3826       C  
ATOM   2639  CG2 VAL B  80      32.829  14.585 -25.973  1.00105.59           C  
ANISOU 2639  CG2 VAL B  80    11974  14137  14007  -7003  -4231   3853       C  
ATOM   2640  N   GLY B  81      31.079  11.152 -23.576  1.00 99.94           N  
ANISOU 2640  N   GLY B  81    11266  13725  12980  -5976  -4145   3323       N  
ATOM   2641  CA  GLY B  81      31.012  10.102 -22.575  1.00 98.31           C  
ANISOU 2641  CA  GLY B  81    10982  13679  12693  -5749  -4203   3231       C  
ATOM   2642  C   GLY B  81      30.773   8.721 -23.160  1.00 93.97           C  
ANISOU 2642  C   GLY B  81    10157  13372  12176  -5341  -3871   3263       C  
ATOM   2643  O   GLY B  81      31.528   7.785 -22.890  1.00 94.97           O  
ANISOU 2643  O   GLY B  81     9932  13784  12367  -5252  -3885   3370       O  
ATOM   2644  N   ASN B  82      29.727   8.597 -23.970  1.00 91.61           N  
ANISOU 2644  N   ASN B  82    10017  12953  11837  -5095  -3583   3176       N  
ATOM   2645  CA  ASN B  82      29.372   7.314 -24.569  1.00 89.98           C  
ANISOU 2645  CA  ASN B  82     9611  12932  11645  -4708  -3270   3176       C  
ATOM   2646  C   ASN B  82      30.397   6.808 -25.584  1.00 90.78           C  
ANISOU 2646  C   ASN B  82     9228  13342  11924  -4718  -3072   3422       C  
ATOM   2647  O   ASN B  82      30.626   5.603 -25.692  1.00 90.37           O  
ANISOU 2647  O   ASN B  82     8885  13528  11924  -4470  -2926   3474       O  
ATOM   2648  CB  ASN B  82      27.978   7.376 -25.201  1.00 73.48           C  
ANISOU 2648  CB  ASN B  82     7858  10615   9445  -4449  -3052   2994       C  
ATOM   2649  CG  ASN B  82      26.879   7.556 -24.171  1.00 70.64           C  
ANISOU 2649  CG  ASN B  82     7908  10021   8910  -4319  -3171   2739       C  
ATOM   2650  OD1 ASN B  82      26.475   6.602 -23.505  1.00 67.96           O  
ANISOU 2650  OD1 ASN B  82     7553   9768   8501  -4072  -3124   2652       O  
ATOM   2651  ND2 ASN B  82      26.386   8.782 -24.039  1.00 71.61           N  
ANISOU 2651  ND2 ASN B  82     8407   9841   8959  -4481  -3316   2623       N  
ATOM   2652  N   SER B  83      31.011   7.726 -26.325  1.00 81.75           N  
ANISOU 2652  N   SER B  83     8005  12190  10868  -4996  -3055   3576       N  
ATOM   2653  CA  SER B  83      32.033   7.350 -27.298  1.00 84.74           C  
ANISOU 2653  CA  SER B  83     7914  12879  11404  -5032  -2854   3821       C  
ATOM   2654  C   SER B  83      33.293   6.839 -26.607  1.00 89.66           C  
ANISOU 2654  C   SER B  83     8104  13800  12164  -5150  -3021   3988       C  
ATOM   2655  O   SER B  83      33.835   5.794 -26.978  1.00 89.99           O  
ANISOU 2655  O   SER B  83     7751  14136  12306  -4942  -2833   4100       O  
ATOM   2656  CB  SER B  83      32.375   8.525 -28.216  1.00 88.29           C  
ANISOU 2656  CB  SER B  83     8390  13251  11905  -5350  -2821   3969       C  
ATOM   2657  OG  SER B  83      31.247   8.924 -28.974  1.00 92.21           O  
ANISOU 2657  OG  SER B  83     9108  13530  12397  -5732  -3161   3965       O  
ATOM   2658  N   VAL B  84      33.756   7.580 -25.604  1.00111.25           N  
ANISOU 2658  N   VAL B  84    10922  16447  14899  -5477  -3384   4000       N  
ATOM   2659  CA  VAL B  84      34.922   7.168 -24.828  1.00113.07           C  
ANISOU 2659  CA  VAL B  84    10765  16945  15249  -5620  -3609   4157       C  
ATOM   2660  C   VAL B  84      34.634   5.855 -24.101  1.00112.06           C  
ANISOU 2660  C   VAL B  84    10574  16932  15070  -5255  -3598   4062       C  
ATOM   2661  O   VAL B  84      35.520   5.014 -23.944  1.00113.25           O  
ANISOU 2661  O   VAL B  84    10279  17391  15357  -5169  -3589   4225       O  
ATOM   2662  CB  VAL B  84      35.361   8.264 -23.829  1.00119.19           C  
ANISOU 2662  CB  VAL B  84    11789  17527  15969  -5961  -3978   4120       C  
ATOM   2663  CG1 VAL B  84      36.484   7.763 -22.934  1.00120.27           C  
ANISOU 2663  CG1 VAL B  84    11683  17867  16147  -5952  -4184   4192       C  
ATOM   2664  CG2 VAL B  84      35.805   9.512 -24.576  1.00120.35           C  
ANISOU 2664  CG2 VAL B  84    11940  17598  16187  -6255  -3947   4252       C  
ATOM   2665  N   THR B  85      33.386   5.677 -23.677  1.00 93.81           N  
ANISOU 2665  N   THR B  85     8702  14374  12569  -5035  -3592   3809       N  
ATOM   2666  CA  THR B  85      32.960   4.426 -23.056  1.00 90.71           C  
ANISOU 2666  CA  THR B  85     8296  14060  12110  -4683  -3553   3719       C  
ATOM   2667  C   THR B  85      33.066   3.263 -24.040  1.00 89.12           C  
ANISOU 2667  C   THR B  85     7761  14079  12023  -4345  -3198   3808       C  
ATOM   2668  O   THR B  85      33.622   2.210 -23.717  1.00 90.08           O  
ANISOU 2668  O   THR B  85     7580  14420  12226  -4164  -3199   3900       O  
ATOM   2669  CB  THR B  85      31.513   4.517 -22.534  1.00 81.57           C  
ANISOU 2669  CB  THR B  85     7665  12601  10728  -4502  -3546   3437       C  
ATOM   2670  OG1 THR B  85      31.430   5.526 -21.520  1.00 84.04           O  
ANISOU 2670  OG1 THR B  85     8314  12698  10920  -4792  -3866   3330       O  
ATOM   2671  CG2 THR B  85      31.070   3.183 -21.954  1.00 78.82           C  
ANISOU 2671  CG2 THR B  85     7296  12341  10312  -4169  -3509   3370       C  
ATOM   2672  N   LEU B  86      32.534   3.463 -25.243  1.00 84.49           N  
ANISOU 2672  N   LEU B  86     7245  13421  11436  -4257  -2903   3780       N  
ATOM   2673  CA  LEU B  86      32.575   2.441 -26.285  1.00 84.18           C  
ANISOU 2673  CA  LEU B  86     6936  13568  11481  -3948  -2551   3842       C  
ATOM   2674  C   LEU B  86      34.004   2.085 -26.681  1.00 88.05           C  
ANISOU 2674  C   LEU B  86     6868  14406  12181  -4025  -2512   4104       C  
ATOM   2675  O   LEU B  86      34.306   0.925 -26.960  1.00 87.95           O  
ANISOU 2675  O   LEU B  86     6565  14595  12258  -3730  -2331   4162       O  
ATOM   2676  CB  LEU B  86      31.785   2.891 -27.517  1.00 76.87           C  
ANISOU 2676  CB  LEU B  86     6216  12502  10491  -3898  -2279   3773       C  
ATOM   2677  CG  LEU B  86      30.267   2.727 -27.446  1.00 70.28           C  
ANISOU 2677  CG  LEU B  86     5817  11400   9483  -3651  -2182   3524       C  
ATOM   2678  CD1 LEU B  86      29.611   3.267 -28.703  1.00 68.10           C  
ANISOU 2678  CD1 LEU B  86     5698  11020   9159  -3626  -1940   3494       C  
ATOM   2679  CD2 LEU B  86      29.901   1.269 -27.238  1.00 67.10           C  
ANISOU 2679  CD2 LEU B  86     5338  11083   9074  -3273  -2054   3451       C  
ATOM   2680  N   PHE B  87      34.880   3.085 -26.708  1.00111.77           N  
ANISOU 2680  N   PHE B  87     9720  17476  15272  -4419  -2680   4265       N  
ATOM   2681  CA  PHE B  87      36.283   2.846 -27.025  1.00114.15           C  
ANISOU 2681  CA  PHE B  87     9456  18128  15786  -4534  -2664   4534       C  
ATOM   2682  C   PHE B  87      36.976   2.132 -25.869  1.00115.32           C  
ANISOU 2682  C   PHE B  87     9389  18425  16000  -4433  -2889   4583       C  
ATOM   2683  O   PHE B  87      37.922   1.371 -26.072  1.00117.05           O  
ANISOU 2683  O   PHE B  87     9209  18900  16364  -4252  -2763   4721       O  
ATOM   2684  CB  PHE B  87      36.999   4.159 -27.345  1.00197.89           C  
ATOM   2685  CG  PHE B  87      38.415   3.979 -27.814  1.00197.89           C  
ATOM   2686  CD1 PHE B  87      38.689   3.730 -29.148  1.00197.89           C  
ATOM   2687  CD2 PHE B  87      39.471   4.059 -26.921  1.00197.89           C  
ATOM   2688  CE1 PHE B  87      39.991   3.563 -29.583  1.00197.89           C  
ATOM   2689  CE2 PHE B  87      40.773   3.893 -27.349  1.00197.89           C  
ATOM   2690  CZ  PHE B  87      41.034   3.645 -28.682  1.00197.89           C  
ATOM   2691  N   THR B  88      36.494   2.384 -24.656  1.00109.13           N  
ANISOU 2691  N   THR B  88     8909  17463  15092  -4526  -3212   4457       N  
ATOM   2692  CA  THR B  88      37.037   1.755 -23.458  1.00110.51           C  
ANISOU 2692  CA  THR B  88     8976  17734  15280  -4437  -3450   4486       C  
ATOM   2693  C   THR B  88      36.703   0.268 -23.430  1.00108.72           C  
ANISOU 2693  C   THR B  88     8620  17616  15075  -4018  -3307   4463       C  
ATOM   2694  O   THR B  88      37.553  -0.566 -23.113  1.00110.47           O  
ANISOU 2694  O   THR B  88     8549  18023  15402  -3833  -3333   4573       O  
ATOM   2695  CB  THR B  88      36.491   2.421 -22.178  1.00125.64           C  
ANISOU 2695  CB  THR B  88    11312  19413  17012  -4669  -3830   4341       C  
ATOM   2696  OG1 THR B  88      36.952   3.776 -22.108  1.00126.68           O  
ANISOU 2696  OG1 THR B  88    11601  19405  17128  -5050  -3964   4351       O  
ATOM   2697  CG2 THR B  88      36.950   1.669 -20.938  1.00127.10           C  
ANISOU 2697  CG2 THR B  88    11390  19710  17195  -4601  -4080   4391       C  
ATOM   2698  N   LEU B  89      35.461  -0.058 -23.775  1.00132.15           N  
ANISOU 2698  N   LEU B  89    11961  20357  17892  -3770  -3076   4250       N  
ATOM   2699  CA  LEU B  89      34.996  -1.441 -23.752  1.00131.13           C  
ANISOU 2699  CA  LEU B  89    11853  20229  17741  -3336  -2890   4171       C  
ATOM   2700  C   LEU B  89      35.674  -2.304 -24.815  1.00132.12           C  
ANISOU 2700  C   LEU B  89    11552  20592  18055  -3076  -2571   4305       C  
ATOM   2701  O   LEU B  89      35.681  -3.531 -24.717  1.00132.26           O  
ANISOU 2701  O   LEU B  89    11431  20689  18132  -2744  -2486   4321       O  
ATOM   2702  CB  LEU B  89      33.476  -1.494 -23.917  1.00115.89           C  
ANISOU 2702  CB  LEU B  89    10429  17997  15610  -3179  -2737   3913       C  
ATOM   2703  CG  LEU B  89      32.682  -0.786 -22.817  1.00114.82           C  
ANISOU 2703  CG  LEU B  89    10741  17620  15268  -3342  -3008   3747       C  
ATOM   2704  CD1 LEU B  89      31.196  -0.809 -23.124  1.00112.45           C  
ANISOU 2704  CD1 LEU B  89    10866  17065  14798  -3128  -2820   3511       C  
ATOM   2705  CD2 LEU B  89      32.964  -1.418 -21.463  1.00115.56           C  
ANISOU 2705  CD2 LEU B  89    10772  17801  15334  -3335  -3304   3803       C  
ATOM   2706  N   ALA B  90      36.242  -1.658 -25.828  1.00119.96           N  
ANISOU 2706  N   ALA B  90     9819  19159  16602  -3224  -2390   4402       N  
ATOM   2707  CA  ALA B  90      36.928  -2.370 -26.901  1.00121.18           C  
ANISOU 2707  CA  ALA B  90     9556  19565  16922  -2999  -2068   4532       C  
ATOM   2708  C   ALA B  90      38.431  -2.438 -26.648  1.00123.92           C  
ANISOU 2708  C   ALA B  90     9371  20226  17487  -3026  -2196   4773       C  
ATOM   2709  O   ALA B  90      39.226  -2.490 -27.587  1.00125.68           O  
ANISOU 2709  O   ALA B  90     9309  20623  17822  -3059  -2012   4894       O  
ATOM   2710  CB  ALA B  90      36.642  -1.712 -28.242  1.00 93.45           C  
ANISOU 2710  CB  ALA B  90     6045  16065  13396  -3155  -1816   4557       C  
ATOM   2711  N   ARG B  91      38.813  -2.438 -25.375  1.00149.57           N  
ANISOU 2711  N   ARG B  91    12629  23463  20738  -2949  -2470   4779       N  
ATOM   2712  CA  ARG B  91      40.219  -2.498 -24.994  1.00152.25           C  
ANISOU 2712  CA  ARG B  91    12631  23991  21227  -2901  -2583   4935       C  
ATOM   2713  C   ARG B  91      40.392  -3.136 -23.620  1.00152.26           C  
ANISOU 2713  C   ARG B  91    12669  23966  21218  -2667  -2786   4924       C  
ATOM   2714  O   ARG B  91      40.182  -4.337 -23.452  1.00153.58           O  
ANISOU 2714  O   ARG B  91    12532  24288  21536  -2395  -2724   5028       O  
ATOM   2715  CB  ARG B  91      40.837  -1.098 -25.005  1.00 20.00           C  
ATOM   2716  N   LEU B  98      33.953 -12.643 -16.559  1.00159.28           N  
ANISOU 2716  N   LEU B  98    15241  23916  21363   -868  -3642   4700       N  
ATOM   2717  CA  LEU B  98      32.704 -12.475 -15.825  1.00156.57           C  
ANISOU 2717  CA  LEU B  98    15375  23306  20807   -843  -3449   4464       C  
ATOM   2718  C   LEU B  98      32.146 -11.069 -16.017  1.00154.72           C  
ANISOU 2718  C   LEU B  98    15381  23010  20395  -1180  -3463   4285       C  
ATOM   2719  O   LEU B  98      30.931 -10.869 -16.031  1.00152.72           O  
ANISOU 2719  O   LEU B  98    15419  22574  20035  -1167  -3229   4081       O  
ATOM   2720  CB  LEU B  98      32.902 -12.766 -14.333  1.00161.59           C  
ANISOU 2720  CB  LEU B  98    16315  23821  21259   -764  -3613   4484       C  
ATOM   2721  CG  LEU B  98      33.035 -14.229 -13.894  1.00158.89           C  
ANISOU 2721  CG  LEU B  98    16275  23238  20856   -524  -3338   4348       C  
ATOM   2722  CD1 LEU B  98      34.391 -14.820 -14.261  1.00159.63           C  
ANISOU 2722  CD1 LEU B  98    16112  23322  21219   -191  -3067   4392       C  
ATOM   2723  CD2 LEU B  98      32.779 -14.363 -12.400  1.00158.23           C  
ANISOU 2723  CD2 LEU B  98    16445  23072  20604   -468  -3522   4422       C  
ATOM   2724  N   GLN B  99      33.042 -10.100 -16.167  1.00197.74           N  
ANISOU 2724  N   GLN B  99    20708  28605  25817  -1483  -3755   4368       N  
ATOM   2725  CA  GLN B  99      32.650  -8.714 -16.388  1.00196.55           C  
ANISOU 2725  CA  GLN B  99    20744  28399  25537  -1821  -3801   4224       C  
ATOM   2726  C   GLN B  99      32.544  -8.429 -17.884  1.00196.04           C  
ANISOU 2726  C   GLN B  99    20558  28320  25609  -1809  -3480   4149       C  
ATOM   2727  O   GLN B  99      31.861  -7.493 -18.302  1.00194.73           O  
ANISOU 2727  O   GLN B  99    20644  28020  25322  -1993  -3406   3983       O  
ATOM   2728  CB  GLN B  99      33.665  -7.768 -15.739  1.00170.67           C  
ANISOU 2728  CB  GLN B  99    17280  25302  22264  -2144  -4185   4364       C  
ATOM   2729  CG  GLN B  99      33.294  -6.294 -15.810  1.00169.79           C  
ANISOU 2729  CG  GLN B  99    17447  25088  21979  -2516  -4308   4210       C  
ATOM   2730  CD  GLN B  99      34.379  -5.393 -15.253  1.00171.74           C  
ANISOU 2730  CD  GLN B  99    17379  25514  22362  -2827  -4525   4349       C  
ATOM   2731  OE1 GLN B  99      35.365  -5.865 -14.689  1.00173.79           O  
ANISOU 2731  OE1 GLN B  99    17246  25943  22845  -2727  -4489   4518       O  
ATOM   2732  NE2 GLN B  99      34.202  -4.086 -15.413  1.00171.32           N  
ANISOU 2732  NE2 GLN B  99    17577  25351  22167  -3169  -4670   4225       N  
ATOM   2733  N   SER B 100      33.214  -9.256 -18.682  1.00384.55           N  
ANISOU 2733  N   SER B 100    44055  52331  49728  -1576  -3287   4273       N  
ATOM   2734  CA  SER B 100      33.280  -9.068 -20.130  1.00384.40           C  
ANISOU 2734  CA  SER B 100    43889  52334  49833  -1536  -2965   4225       C  
ATOM   2735  C   SER B 100      31.907  -9.071 -20.799  1.00381.41           C  
ANISOU 2735  C   SER B 100    43879  51712  49329  -1392  -2664   3995       C  
ATOM   2736  O   SER B 100      31.692  -8.377 -21.792  1.00380.51           O  
ANISOU 2736  O   SER B 100    43803  51561  49215  -1475  -2464   3904       O  
ATOM   2737  CB  SER B 100      34.170 -10.141 -20.763  1.00125.03           C  
ANISOU 2737  CB  SER B 100    10558  19691  17255  -1272  -2815   4404       C  
ATOM   2738  OG  SER B 100      35.477 -10.108 -20.217  1.00129.36           O  
ANISOU 2738  OG  SER B 100    10719  20487  17942  -1395  -3099   4635       O  
ATOM   2739  N   THR B 101      30.983  -9.853 -20.251  1.00102.86           N  
ANISOU 2739  N   THR B 101     8863  16274  13946  -1188  -2642   3916       N  
ATOM   2740  CA  THR B 101      29.636  -9.945 -20.801  1.00100.98           C  
ANISOU 2740  CA  THR B 101     8961  15811  13597  -1055  -2382   3709       C  
ATOM   2741  C   THR B 101      28.818  -8.707 -20.454  1.00 98.97           C  
ANISOU 2741  C   THR B 101     9075  15402  13127  -1306  -2431   3531       C  
ATOM   2742  O   THR B 101      27.962  -8.280 -21.228  1.00 97.77           O  
ANISOU 2742  O   THR B 101     9082  15133  12934  -1298  -2213   3385       O  
ATOM   2743  CB  THR B 101      28.898 -11.173 -20.260  1.00 99.81           C  
ANISOU 2743  CB  THR B 101     8984  15536  13406   -791  -2357   3694       C  
ATOM   2744  OG1 THR B 101      28.663 -10.999 -18.859  1.00 98.73           O  
ANISOU 2744  OG1 THR B 101     9109  15335  13069   -934  -2610   3678       O  
ATOM   2745  CG2 THR B 101      29.722 -12.433 -20.490  1.00102.21           C  
ANISOU 2745  CG2 THR B 101     8943  15971  13924   -537  -2366   3886       C  
ATOM   2746  N   VAL B 102      29.081  -8.143 -19.279  1.00102.20           N  
ANISOU 2746  N   VAL B 102     9629  15810  13393  -1516  -2724   3541       N  
ATOM   2747  CA  VAL B 102      28.407  -6.928 -18.837  1.00100.59           C  
ANISOU 2747  CA  VAL B 102     9779  15458  12984  -1750  -2800   3371       C  
ATOM   2748  C   VAL B 102      28.811  -5.761 -19.736  1.00100.70           C  
ANISOU 2748  C   VAL B 102     9724  15484  13054  -1972  -2752   3344       C  
ATOM   2749  O   VAL B 102      28.011  -4.861 -20.013  1.00 99.12           O  
ANISOU 2749  O   VAL B 102     9813  15116  12731  -2074  -2685   3178       O  
ATOM   2750  CB  VAL B 102      28.752  -6.605 -17.369  1.00100.55           C  
ANISOU 2750  CB  VAL B 102     9933  15467  12806  -1931  -3141   3393       C  
ATOM   2751  CG1 VAL B 102      27.966  -5.397 -16.885  1.00 99.50           C  
ANISOU 2751  CG1 VAL B 102     9918  15306  12583  -2276  -3330   3329       C  
ATOM   2752  CG2 VAL B 102      28.473  -7.811 -16.485  1.00 99.72           C  
ANISOU 2752  CG2 VAL B 102    10190  15209  12492  -1803  -3109   3269       C  
ATOM   2753  N   ASP B 103      30.057  -5.798 -20.200  1.00 96.94           N  
ANISOU 2753  N   ASP B 103     8853  15209  12774  -2032  -2771   3519       N  
ATOM   2754  CA  ASP B 103      30.582  -4.790 -21.114  1.00 97.39           C  
ANISOU 2754  CA  ASP B 103     8793  15305  12906  -2246  -2707   3538       C  
ATOM   2755  C   ASP B 103      29.778  -4.740 -22.411  1.00 96.21           C  
ANISOU 2755  C   ASP B 103     8770  15037  12751  -2112  -2370   3411       C  
ATOM   2756  O   ASP B 103      29.686  -3.694 -23.053  1.00 95.99           O  
ANISOU 2756  O   ASP B 103     8822  14950  12702  -2302  -2321   3368       O  
ATOM   2757  CB  ASP B 103      32.057  -5.062 -21.420  1.00128.43           C  
ANISOU 2757  CB  ASP B 103    12223  19511  17063  -2299  -2753   3774       C  
ATOM   2758  CG  ASP B 103      32.958  -4.814 -20.224  1.00129.84           C  
ANISOU 2758  CG  ASP B 103    12266  19818  17248  -2510  -3136   3912       C  
ATOM   2759  OD1 ASP B 103      32.454  -4.830 -19.082  1.00129.13           O  
ANISOU 2759  OD1 ASP B 103    12506  19591  16965  -2685  -3368   3808       O  
ATOM   2760  OD2 ASP B 103      34.173  -4.604 -20.427  1.00131.81           O  
ANISOU 2760  OD2 ASP B 103    12078  20312  17691  -2498  -3205   4122       O  
ATOM   2761  N   TYR B 104      29.201  -5.875 -22.792  1.00 79.74           N  
ANISOU 2761  N   TYR B 104     6706  12910  10684  -1795  -2152   3359       N  
ATOM   2762  CA  TYR B 104      28.353  -5.943 -23.977  1.00 78.67           C  
ANISOU 2762  CA  TYR B 104     6730  12647  10514  -1662  -1858   3221       C  
ATOM   2763  C   TYR B 104      27.062  -5.155 -23.770  1.00 76.79           C  
ANISOU 2763  C   TYR B 104     6920  12176  10081  -1757  -1889   3027       C  
ATOM   2764  O   TYR B 104      26.654  -4.376 -24.634  1.00 76.11           O  
ANISOU 2764  O   TYR B 104     6964  11998   9956  -1830  -1765   2944       O  
ATOM   2765  CB  TYR B 104      28.040  -7.399 -24.334  1.00109.96           C  
ANISOU 2765  CB  TYR B 104    10635  16604  14541  -1312  -1649   3204       C  
ATOM   2766  CG  TYR B 104      29.208  -8.149 -24.938  1.00111.88           C  
ANISOU 2766  CG  TYR B 104    10461  17062  14987  -1168  -1538   3367       C  
ATOM   2767  CD1 TYR B 104      30.153  -7.492 -25.714  1.00112.34           C  
ANISOU 2767  CD1 TYR B 104    10392  17179  15115  -1072  -1256   3356       C  
ATOM   2768  CD2 TYR B 104      29.365  -9.514 -24.732  1.00113.33           C  
ANISOU 2768  CD2 TYR B 104    10374  17399  15286  -1121  -1715   3536       C  
ATOM   2769  CE1 TYR B 104      31.222  -8.172 -26.269  1.00114.24           C  
ANISOU 2769  CE1 TYR B 104    10244  17627  15535   -919  -1127   3497       C  
ATOM   2770  CE2 TYR B 104      30.431 -10.203 -25.282  1.00115.25           C  
ANISOU 2770  CE2 TYR B 104    10212  17848  15732   -963  -1605   3688       C  
ATOM   2771  CZ  TYR B 104      31.356  -9.527 -26.050  1.00115.73           C  
ANISOU 2771  CZ  TYR B 104    10149  17965  15859   -856  -1298   3662       C  
ATOM   2772  OH  TYR B 104      32.418 -10.207 -26.601  1.00117.80           O  
ANISOU 2772  OH  TYR B 104    10000  18442  16316   -677  -1161   3805       O  
ATOM   2773  N   TYR B 105      26.425  -5.362 -22.620  1.00 76.04           N  
ANISOU 2773  N   TYR B 105     7040  11991   9860  -1745  -2051   2963       N  
ATOM   2774  CA  TYR B 105      25.215  -4.625 -22.270  1.00 74.14           C  
ANISOU 2774  CA  TYR B 105     7190  11547   9433  -1819  -2084   2780       C  
ATOM   2775  C   TYR B 105      25.502  -3.130 -22.185  1.00 74.10           C  
ANISOU 2775  C   TYR B 105     7285  11492   9377  -2123  -2247   2757       C  
ATOM   2776  O   TYR B 105      24.739  -2.309 -22.702  1.00 72.98           O  
ANISOU 2776  O   TYR B 105     7363  11197   9170  -2179  -2165   2635       O  
ATOM   2777  CB  TYR B 105      24.641  -5.125 -20.943  1.00 66.44           C  
ANISOU 2777  CB  TYR B 105     6400  10523   8322  -1754  -2221   2737       C  
ATOM   2778  CG  TYR B 105      24.182  -6.566 -20.967  1.00 66.23           C  
ANISOU 2778  CG  TYR B 105     6359  10484   8323  -1471  -2064   2740       C  
ATOM   2779  CD1 TYR B 105      22.945  -6.912 -21.497  1.00 64.69           C  
ANISOU 2779  CD1 TYR B 105     6377  10139   8064  -1331  -1866   2593       C  
ATOM   2780  CD2 TYR B 105      24.980  -7.579 -20.448  1.00 67.69           C  
ANISOU 2780  CD2 TYR B 105     6317  10796   8606  -1349  -2131   2897       C  
ATOM   2781  CE1 TYR B 105      22.521  -8.228 -21.518  1.00 64.74           C  
ANISOU 2781  CE1 TYR B 105     6383  10114   8101  -1101  -1738   2599       C  
ATOM   2782  CE2 TYR B 105      24.564  -8.898 -20.464  1.00 67.74           C  
ANISOU 2782  CE2 TYR B 105     6336  10757   8646  -1097  -1999   2904       C  
ATOM   2783  CZ  TYR B 105      23.333  -9.216 -21.001  1.00 66.34           C  
ANISOU 2783  CZ  TYR B 105     6385  10420   8400   -986  -1803   2752       C  
ATOM   2784  OH  TYR B 105      22.909 -10.524 -21.022  1.00 66.60           O  
ANISOU 2784  OH  TYR B 105     6444  10391   8472   -762  -1686   2762       O  
ATOM   2785  N   LEU B 106      26.611  -2.789 -21.535  1.00 76.47           N  
ANISOU 2785  N   LEU B 106     7426  11914   9713  -2320  -2491   2883       N  
ATOM   2786  CA  LEU B 106      27.036  -1.397 -21.415  1.00 77.00           C  
ANISOU 2786  CA  LEU B 106     7579  11930   9748  -2642  -2683   2879       C  
ATOM   2787  C   LEU B 106      27.258  -0.762 -22.785  1.00 77.30           C  
ANISOU 2787  C   LEU B 106     7506  11967   9896  -2736  -2522   2922       C  
ATOM   2788  O   LEU B 106      26.876   0.387 -23.019  1.00 76.92           O  
ANISOU 2788  O   LEU B 106     7680  11760   9786  -2919  -2567   2842       O  
ATOM   2789  CB  LEU B 106      28.310  -1.294 -20.573  1.00 64.06           C  
ANISOU 2789  CB  LEU B 106     5722  10459   8159  -2844  -2980   3037       C  
ATOM   2790  CG  LEU B 106      28.141  -1.038 -19.073  1.00 65.87           C  
ANISOU 2790  CG  LEU B 106     6184  10638   8205  -2933  -3263   2973       C  
ATOM   2791  CD1 LEU B 106      27.270  -2.101 -18.419  1.00 62.44           C  
ANISOU 2791  CD1 LEU B 106     5962  10129   7634  -2658  -3155   2861       C  
ATOM   2792  CD2 LEU B 106      29.496  -0.958 -18.388  1.00 71.64           C  
ANISOU 2792  CD2 LEU B 106     6610  11588   9021  -3076  -3537   3172       C  
ATOM   2793  N   GLY B 107      27.876  -1.521 -23.685  1.00 66.87           N  
ANISOU 2793  N   GLY B 107     5855  10821   8732  -2599  -2329   3050       N  
ATOM   2794  CA  GLY B 107      28.125  -1.058 -25.037  1.00 67.25           C  
ANISOU 2794  CA  GLY B 107     5779  10905   8868  -2661  -2138   3108       C  
ATOM   2795  C   GLY B 107      26.833  -0.847 -25.799  1.00 65.63           C  
ANISOU 2795  C   GLY B 107     5873  10502   8562  -2538  -1934   2942       C  
ATOM   2796  O   GLY B 107      26.707   0.099 -26.578  1.00 65.48           O  
ANISOU 2796  O   GLY B 107     5938  10406   8534  -2683  -1878   2941       O  
ATOM   2797  N   SER B 108      25.871  -1.735 -25.572  1.00 56.98           N  
ANISOU 2797  N   SER B 108     4931   9324   7393  -2278  -1833   2815       N  
ATOM   2798  CA  SER B 108      24.556  -1.612 -26.187  1.00 53.80           C  
ANISOU 2798  CA  SER B 108     4806   8739   6894  -2155  -1667   2654       C  
ATOM   2799  C   SER B 108      23.869  -0.334 -25.718  1.00 52.95           C  
ANISOU 2799  C   SER B 108     5029   8422   6665  -2333  -1820   2535       C  
ATOM   2800  O   SER B 108      23.290   0.402 -26.521  1.00 52.21           O  
ANISOU 2800  O   SER B 108     5102   8197   6536  -2365  -1734   2473       O  
ATOM   2801  CB  SER B 108      23.692  -2.828 -25.855  1.00 47.85           C  
ANISOU 2801  CB  SER B 108     4138   7946   6096  -1873  -1562   2555       C  
ATOM   2802  OG  SER B 108      22.431  -2.744 -26.496  1.00 46.01           O  
ANISOU 2802  OG  SER B 108     4171   7540   5770  -1777  -1438   2399       O  
ATOM   2803  N   LEU B 109      23.942  -0.079 -24.415  1.00 47.58           N  
ANISOU 2803  N   LEU B 109     4454   7710   5917  -2441  -2052   2506       N  
ATOM   2804  CA  LEU B 109      23.384   1.140 -23.836  1.00 47.52           C  
ANISOU 2804  CA  LEU B 109     4775   7494   5786  -2601  -2210   2378       C  
ATOM   2805  C   LEU B 109      24.025   2.384 -24.446  1.00 50.24           C  
ANISOU 2805  C   LEU B 109     5105   7792   6191  -2883  -2299   2459       C  
ATOM   2806  O   LEU B 109      23.328   3.316 -24.860  1.00 49.03           O  
ANISOU 2806  O   LEU B 109     5209   7436   5984  -2946  -2294   2365       O  
ATOM   2807  CB  LEU B 109      23.577   1.147 -22.317  1.00 50.16           C  
ANISOU 2807  CB  LEU B 109     5216   7827   6014  -2670  -2447   2337       C  
ATOM   2808  CG  LEU B 109      22.803   0.100 -21.513  1.00 47.94           C  
ANISOU 2808  CG  LEU B 109     5038   7547   5629  -2428  -2384   2244       C  
ATOM   2809  CD1 LEU B 109      23.225   0.127 -20.053  1.00 51.13           C  
ANISOU 2809  CD1 LEU B 109     5508   7997   5921  -2525  -2633   2248       C  
ATOM   2810  CD2 LEU B 109      21.306   0.329 -21.645  1.00 44.23           C  
ANISOU 2810  CD2 LEU B 109     4876   6880   5047  -2291  -2249   2052       C  
ATOM   2811  N   ALA B 110      25.354   2.386 -24.504  1.00 53.53           N  
ANISOU 2811  N   ALA B 110     5209   8399   6731  -3049  -2379   2646       N  
ATOM   2812  CA  ALA B 110      26.101   3.508 -25.062  1.00 57.17           C  
ANISOU 2812  CA  ALA B 110     5608   8846   7266  -3353  -2468   2761       C  
ATOM   2813  C   ALA B 110      25.739   3.755 -26.524  1.00 55.39           C  
ANISOU 2813  C   ALA B 110     5388   8581   7079  -3307  -2227   2789       C  
ATOM   2814  O   ALA B 110      25.625   4.903 -26.958  1.00 56.68           O  
ANISOU 2814  O   ALA B 110     5712   8590   7234  -3508  -2280   2800       O  
ATOM   2815  CB  ALA B 110      27.596   3.275 -24.915  1.00 61.99           C  
ANISOU 2815  CB  ALA B 110     5818   9716   8019  -3517  -2575   2977       C  
ATOM   2816  N   LEU B 111      25.559   2.674 -27.277  1.00 53.72           N  
ANISOU 2816  N   LEU B 111     5015   8497   6900  -3044  -1973   2803       N  
ATOM   2817  CA  LEU B 111      25.159   2.777 -28.676  1.00 52.31           C  
ANISOU 2817  CA  LEU B 111     4858   8293   6722  -2970  -1737   2816       C  
ATOM   2818  C   LEU B 111      23.765   3.386 -28.790  1.00 49.16           C  
ANISOU 2818  C   LEU B 111     4856   7620   6202  -2902  -1734   2637       C  
ATOM   2819  O   LEU B 111      23.525   4.271 -29.618  1.00 49.47           O  
ANISOU 2819  O   LEU B 111     5031   7541   6226  -3010  -1700   2660       O  
ATOM   2820  CB  LEU B 111      25.190   1.403 -29.348  1.00 75.07           C  
ANISOU 2820  CB  LEU B 111     7523  11353   9644  -2683  -1484   2834       C  
ATOM   2821  CG  LEU B 111      24.853   1.373 -30.840  1.00 73.89           C  
ANISOU 2821  CG  LEU B 111     7405  11202   9468  -2579  -1229   2833       C  
ATOM   2822  CD1 LEU B 111      25.829   2.231 -31.626  1.00 75.06           C  
ANISOU 2822  CD1 LEU B 111     7402  11444   9671  -2824  -1191   3013       C  
ATOM   2823  CD2 LEU B 111      24.847  -0.056 -31.362  1.00 73.20           C  
ANISOU 2823  CD2 LEU B 111     7145  11260   9405  -2283  -1004   2813       C  
ATOM   2824  N   SER B 112      22.852   2.910 -27.947  1.00 56.58           N  
ANISOU 2824  N   SER B 112     5974   8466   7059  -2721  -1769   2473       N  
ATOM   2825  CA  SER B 112      21.483   3.414 -27.936  1.00 55.05           C  
ANISOU 2825  CA  SER B 112     6126   8033   6760  -2623  -1761   2298       C  
ATOM   2826  C   SER B 112      21.446   4.900 -27.591  1.00 55.64           C  
ANISOU 2826  C   SER B 112     6450   7892   6799  -2857  -1959   2265       C  
ATOM   2827  O   SER B 112      20.583   5.635 -28.072  1.00 54.96           O  
ANISOU 2827  O   SER B 112     6613   7604   6666  -2823  -1936   2180       O  
ATOM   2828  CB  SER B 112      20.617   2.621 -26.955  1.00 49.64           C  
ANISOU 2828  CB  SER B 112     5550   7319   5993  -2412  -1766   2148       C  
ATOM   2829  OG  SER B 112      21.054   2.804 -25.620  1.00 50.02           O  
ANISOU 2829  OG  SER B 112     5635   7371   6002  -2531  -1978   2132       O  
ATOM   2830  N   ASP B 113      22.387   5.336 -26.758  1.00 60.85           N  
ANISOU 2830  N   ASP B 113     7049   8586   7486  -3094  -2168   2334       N  
ATOM   2831  CA  ASP B 113      22.508   6.751 -26.423  1.00 61.90           C  
ANISOU 2831  CA  ASP B 113     7430   8496   7591  -3347  -2381   2303       C  
ATOM   2832  C   ASP B 113      23.045   7.552 -27.608  1.00 63.54           C  
ANISOU 2832  C   ASP B 113     7571   8682   7889  -3566  -2355   2469       C  
ATOM   2833  O   ASP B 113      22.494   8.597 -27.968  1.00 64.01           O  
ANISOU 2833  O   ASP B 113     7905   8493   7922  -3653  -2409   2426       O  
ATOM   2834  CB  ASP B 113      23.419   6.941 -25.208  1.00124.13           C  
ANISOU 2834  CB  ASP B 113    15286  16420  15460  -3548  -2641   2314       C  
ATOM   2835  CG  ASP B 113      22.862   6.295 -23.954  1.00122.94           C  
ANISOU 2835  CG  ASP B 113    15280  16253  15179  -3362  -2690   2143       C  
ATOM   2836  OD1 ASP B 113      21.626   6.146 -23.857  1.00121.09           O  
ANISOU 2836  OD1 ASP B 113    15084  16028  14898  -3074  -2500   2049       O  
ATOM   2837  OD2 ASP B 113      23.662   5.940 -23.062  1.00123.90           O  
ANISOU 2837  OD2 ASP B 113    15482  16358  15238  -3516  -2923   2109       O  
ATOM   2838  N   LEU B 114      24.121   7.052 -28.210  1.00 68.44           N  
ANISOU 2838  N   LEU B 114     7827   9562   8615  -3646  -2265   2666       N  
ATOM   2839  CA  LEU B 114      24.765   7.736 -29.327  1.00 69.47           C  
ANISOU 2839  CA  LEU B 114     7848   9724   8823  -3864  -2210   2854       C  
ATOM   2840  C   LEU B 114      23.840   7.906 -30.528  1.00 68.48           C  
ANISOU 2840  C   LEU B 114     7888   9485   8648  -3718  -2013   2827       C  
ATOM   2841  O   LEU B 114      23.882   8.934 -31.203  1.00 69.26           O  
ANISOU 2841  O   LEU B 114     8109   9450   8756  -3908  -2040   2918       O  
ATOM   2842  CB  LEU B 114      26.047   7.012 -29.749  1.00 70.04           C  
ANISOU 2842  CB  LEU B 114     7462  10139   9012  -3920  -2101   3061       C  
ATOM   2843  CG  LEU B 114      27.286   7.266 -28.891  1.00 71.82           C  
ANISOU 2843  CG  LEU B 114     7468  10490   9331  -4201  -2331   3187       C  
ATOM   2844  CD1 LEU B 114      28.515   6.633 -29.521  1.00 73.86           C  
ANISOU 2844  CD1 LEU B 114     7241  11104   9721  -4213  -2181   3402       C  
ATOM   2845  CD2 LEU B 114      27.498   8.758 -28.685  1.00 74.76           C  
ANISOU 2845  CD2 LEU B 114     8034  10653   9719  -4578  -2554   3245       C  
ATOM   2846  N   LEU B 115      23.010   6.901 -30.795  1.00 66.99           N  
ANISOU 2846  N   LEU B 115     7706   9346   8402  -3392  -1832   2711       N  
ATOM   2847  CA  LEU B 115      22.057   6.984 -31.899  1.00 65.80           C  
ANISOU 2847  CA  LEU B 115     7711   9100   8192  -3238  -1666   2675       C  
ATOM   2848  C   LEU B 115      21.089   8.150 -31.708  1.00 66.22           C  
ANISOU 2848  C   LEU B 115     8154   8820   8188  -3274  -1806   2564       C  
ATOM   2849  O   LEU B 115      20.873   8.950 -32.624  1.00 66.49           O  
ANISOU 2849  O   LEU B 115     8321   8730   8214  -3363  -1786   2642       O  
ATOM   2850  CB  LEU B 115      21.284   5.672 -32.054  1.00 65.88           C  
ANISOU 2850  CB  LEU B 115     7666   9210   8156  -2899  -1482   2556       C  
ATOM   2851  CG  LEU B 115      22.082   4.482 -32.589  1.00 65.24           C  
ANISOU 2851  CG  LEU B 115     7241   9424   8123  -2803  -1285   2659       C  
ATOM   2852  CD1 LEU B 115      21.206   3.240 -32.687  1.00 62.90           C  
ANISOU 2852  CD1 LEU B 115     6956   9165   7779  -2482  -1134   2521       C  
ATOM   2853  CD2 LEU B 115      22.700   4.817 -33.938  1.00 65.60           C  
ANISOU 2853  CD2 LEU B 115     7175   9571   8177  -2923  -1140   2831       C  
ATOM   2854  N   ILE B 116      20.518   8.241 -30.510  1.00 63.16           N  
ANISOU 2854  N   ILE B 116     7953   8287   7757  -3196  -1944   2386       N  
ATOM   2855  CA  ILE B 116      19.608   9.325 -30.159  1.00 63.49           C  
ANISOU 2855  CA  ILE B 116     8367   8006   7748  -3189  -2071   2253       C  
ATOM   2856  C   ILE B 116      20.297  10.683 -30.248  1.00 65.36           C  
ANISOU 2856  C   ILE B 116     8739   8062   8030  -3522  -2263   2357       C  
ATOM   2857  O   ILE B 116      19.773  11.617 -30.859  1.00 66.09           O  
ANISOU 2857  O   ILE B 116     9078   7914   8117  -3558  -2300   2362       O  
ATOM   2858  CB  ILE B 116      19.047   9.146 -28.733  1.00 54.32           C  
ANISOU 2858  CB  ILE B 116     7367   6757   6515  -3040  -2162   2037       C  
ATOM   2859  CG1 ILE B 116      18.183   7.886 -28.655  1.00 51.69           C  
ANISOU 2859  CG1 ILE B 116     6940   6562   6141  -2719  -1974   1939       C  
ATOM   2860  CG2 ILE B 116      18.244  10.369 -28.319  1.00 55.17           C  
ANISOU 2860  CG2 ILE B 116     7861   6526   6577  -3036  -2296   1895       C  
ATOM   2861  CD1 ILE B 116      16.961   7.929 -29.545  1.00 50.69           C  
ANISOU 2861  CD1 ILE B 116     6979   6356   5927  -2557  -2026   1737       C  
ATOM   2862  N   LEU B 117      21.478  10.782 -29.646  1.00 80.73           N  
ANISOU 2862  N   LEU B 117    10521  10122  10031  -3774  -2395   2452       N  
ATOM   2863  CA  LEU B 117      22.207  12.047 -29.594  1.00 82.66           C  
ANISOU 2863  CA  LEU B 117    10882  10196  10328  -4133  -2604   2556       C  
ATOM   2864  C   LEU B 117      22.644  12.551 -30.969  1.00 83.37           C  
ANISOU 2864  C   LEU B 117    10897  10300  10478  -4304  -2510   2780       C  
ATOM   2865  O   LEU B 117      22.612  13.753 -31.234  1.00 84.64           O  
ANISOU 2865  O   LEU B 117    11319  10187  10651  -4479  -2629   2820       O  
ATOM   2866  CB  LEU B 117      23.421  11.923 -28.672  1.00 66.43           C  
ANISOU 2866  CB  LEU B 117     8619   8301   8323  -4377  -2776   2625       C  
ATOM   2867  CG  LEU B 117      23.097  11.709 -27.193  1.00 65.47           C  
ANISOU 2867  CG  LEU B 117     8663   8099   8114  -4303  -2947   2413       C  
ATOM   2868  CD1 LEU B 117      24.349  11.349 -26.414  1.00 68.56           C  
ANISOU 2868  CD1 LEU B 117     8769   8730   8553  -4498  -3089   2512       C  
ATOM   2869  CD2 LEU B 117      22.440  12.950 -26.612  1.00 67.38           C  
ANISOU 2869  CD2 LEU B 117     9354   7951   8297  -4411  -3157   2262       C  
ATOM   2870  N   LEU B 118      23.047  11.634 -31.841  1.00 87.95           N  
ANISOU 2870  N   LEU B 118    11137  11193  11089  -4248  -2293   2928       N  
ATOM   2871  CA  LEU B 118      23.565  12.012 -33.152  1.00 88.52           C  
ANISOU 2871  CA  LEU B 118    11109  11333  11193  -4412  -2172   3156       C  
ATOM   2872  C   LEU B 118      22.472  12.191 -34.204  1.00 87.56           C  
ANISOU 2872  C   LEU B 118    11218  11062  10991  -4218  -2041   3124       C  
ATOM   2873  O   LEU B 118      22.596  13.032 -35.095  1.00 88.52           O  
ANISOU 2873  O   LEU B 118    11464  11057  11114  -4396  -2053   3274       O  
ATOM   2874  CB  LEU B 118      24.603  10.995 -33.638  1.00 66.24           C  
ANISOU 2874  CB  LEU B 118     7835   8914   8421  -4414  -1971   3319       C  
ATOM   2875  CG  LEU B 118      25.933  10.943 -32.882  1.00 70.15           C  
ANISOU 2875  CG  LEU B 118     8029   9600   9026  -4666  -2098   3438       C  
ATOM   2876  CD1 LEU B 118      26.843   9.876 -33.470  1.00 71.13           C  
ANISOU 2876  CD1 LEU B 118     7698  10123   9205  -4602  -1861   3594       C  
ATOM   2877  CD2 LEU B 118      26.616  12.300 -32.895  1.00 76.01           C  
ANISOU 2877  CD2 LEU B 118     8865  10179   9835  -5092  -2306   3594       C  
ATOM   2878  N   LEU B 119      21.402  11.408 -34.102  1.00 77.92           N  
ANISOU 2878  N   LEU B 119    10050   9857   9700  -3866  -1929   2943       N  
ATOM   2879  CA  LEU B 119      20.350  11.443 -35.117  1.00 76.80           C  
ANISOU 2879  CA  LEU B 119    10077   9623   9482  -3667  -1805   2920       C  
ATOM   2880  C   LEU B 119      19.102  12.217 -34.689  1.00 77.20           C  
ANISOU 2880  C   LEU B 119    10506   9326   9500  -3528  -1944   2744       C  
ATOM   2881  O   LEU B 119      18.610  13.069 -35.431  1.00 77.73           O  
ANISOU 2881  O   LEU B 119    10799   9186   9550  -3556  -1980   2805       O  
ATOM   2882  CB  LEU B 119      19.969  10.023 -35.547  1.00 62.57           C  
ANISOU 2882  CB  LEU B 119     8071   8076   7627  -3376  -1572   2858       C  
ATOM   2883  CG  LEU B 119      21.110   9.183 -36.126  1.00 62.31           C  
ANISOU 2883  CG  LEU B 119     7669   8389   7619  -3443  -1390   3016       C  
ATOM   2884  CD1 LEU B 119      20.600   7.839 -36.619  1.00 60.04           C  
ANISOU 2884  CD1 LEU B 119     7250   8292   7273  -3133  -1176   2922       C  
ATOM   2885  CD2 LEU B 119      21.819   9.939 -37.239  1.00 64.11           C  
ANISOU 2885  CD2 LEU B 119     7865   8659   7837  -3683  -1325   3255       C  
ATOM   2886  N   ALA B 120      18.595  11.923 -33.496  1.00 66.99           N  
ANISOU 2886  N   ALA B 120     9281   7975   8198  -3370  -2017   2533       N  
ATOM   2887  CA  ALA B 120      17.331  12.501 -33.044  1.00 67.40           C  
ANISOU 2887  CA  ALA B 120     9653   7742   8215  -3173  -2102   2343       C  
ATOM   2888  C   ALA B 120      17.449  13.964 -32.618  1.00 69.46           C  
ANISOU 2888  C   ALA B 120    10228   7657   8508  -3369  -2329   2331       C  
ATOM   2889  O   ALA B 120      16.529  14.753 -32.833  1.00 70.28           O  
ANISOU 2889  O   ALA B 120    10614   7488   8602  -3247  -2384   2262       O  
ATOM   2890  CB  ALA B 120      16.736  11.667 -31.918  1.00 45.16           C  
ANISOU 2890  CB  ALA B 120     6801   4998   5360  -2936  -2075   2128       C  
ATOM   2891  N   MET B 121      18.580  14.321 -32.017  1.00 76.94           N  
ANISOU 2891  N   MET B 121    11128   8606   9499  -3668  -2474   2398       N  
ATOM   2892  CA  MET B 121      18.768  15.671 -31.481  1.00 78.99           C  
ANISOU 2892  CA  MET B 121    11707   8519   9789  -3881  -2715   2368       C  
ATOM   2893  C   MET B 121      18.712  16.820 -32.501  1.00 80.41           C  
ANISOU 2893  C   MET B 121    12085   8458  10011  -4045  -2770   2540       C  
ATOM   2894  O   MET B 121      17.952  17.767 -32.305  1.00 81.68           O  
ANISOU 2894  O   MET B 121    12599   8266  10171  -3964  -2884   2440       O  
ATOM   2895  CB  MET B 121      20.036  15.759 -30.621  1.00 78.67           C  
ANISOU 2895  CB  MET B 121    11568   8542   9783  -4189  -2886   2397       C  
ATOM   2896  CG  MET B 121      20.465  17.183 -30.310  1.00 80.99           C  
ANISOU 2896  CG  MET B 121    12208   8460  10105  -4451  -3154   2369       C  
ATOM   2897  SD  MET B 121      21.400  17.323 -28.777  1.00 82.13           S  
ANISOU 2897  SD  MET B 121    12256   8672  10277  -4827  -3399   2385       S  
ATOM   2898  CE  MET B 121      20.111  17.032 -27.570  1.00 80.87           C  
ANISOU 2898  CE  MET B 121    12164   8574   9991  -4518  -3404   2074       C  
ATOM   2899  N   PRO B 122      19.510  16.751 -33.586  1.00 77.93           N  
ANISOU 2899  N   PRO B 122    11550   8328   9730  -4267  -2684   2804       N  
ATOM   2900  CA  PRO B 122      19.471  17.890 -34.512  1.00 80.33           C  
ANISOU 2900  CA  PRO B 122    12063   8395  10062  -4449  -2746   2989       C  
ATOM   2901  C   PRO B 122      18.126  18.028 -35.222  1.00 78.87           C  
ANISOU 2901  C   PRO B 122    12089   8052   9826  -4143  -2671   2939       C  
ATOM   2902  O   PRO B 122      17.708  19.145 -35.526  1.00 81.48           O  
ANISOU 2902  O   PRO B 122    12727   8050  10179  -4207  -2795   3001       O  
ATOM   2903  CB  PRO B 122      20.574  17.557 -35.522  1.00 74.05           C  
ANISOU 2903  CB  PRO B 122    10931   7922   9284  -4690  -2602   3273       C  
ATOM   2904  CG  PRO B 122      20.693  16.075 -35.477  1.00 69.64           C  
ANISOU 2904  CG  PRO B 122    10015   7756   8689  -4481  -2400   3204       C  
ATOM   2905  CD  PRO B 122      20.441  15.704 -34.047  1.00 66.77           C  
ANISOU 2905  CD  PRO B 122     9707   7335   8328  -4348  -2516   2951       C  
ATOM   2906  N   VAL B 123      17.462  16.904 -35.477  1.00 64.43           N  
ANISOU 2906  N   VAL B 123    10095   6450   7933  -3820  -2484   2836       N  
ATOM   2907  CA  VAL B 123      16.152  16.914 -36.119  1.00 62.39           C  
ANISOU 2907  CA  VAL B 123    10001   6075   7629  -3514  -2426   2775       C  
ATOM   2908  C   VAL B 123      15.103  17.561 -35.217  1.00 61.53           C  
ANISOU 2908  C   VAL B 123    10208   5626   7544  -3311  -2573   2542       C  
ATOM   2909  O   VAL B 123      14.335  18.419 -35.656  1.00 63.44           O  
ANISOU 2909  O   VAL B 123    10726   5577   7804  -3221  -2658   2556       O  
ATOM   2910  CB  VAL B 123      15.700  15.488 -36.498  1.00 57.65           C  
ANISOU 2910  CB  VAL B 123     9135   5810   6960  -3242  -2202   2712       C  
ATOM   2911  CG1 VAL B 123      14.249  15.489 -36.954  1.00 55.44           C  
ANISOU 2911  CG1 VAL B 123     9019   5400   6645  -2910  -2182   2601       C  
ATOM   2912  CG2 VAL B 123      16.607  14.915 -37.576  1.00 59.09           C  
ANISOU 2912  CG2 VAL B 123     9065   6289   7098  -3390  -2035   2940       C  
ATOM   2913  N   GLU B 124      15.080  17.148 -33.954  1.00 62.34           N  
ANISOU 2913  N   GLU B 124    10273   5771   7642  -3233  -2599   2333       N  
ATOM   2914  CA  GLU B 124      14.138  17.698 -32.986  1.00 61.59           C  
ANISOU 2914  CA  GLU B 124    10462   5391   7547  -3022  -2706   2088       C  
ATOM   2915  C   GLU B 124      14.429  19.164 -32.685  1.00 66.83           C  
ANISOU 2915  C   GLU B 124    11478   5649   8265  -3233  -2938   2094       C  
ATOM   2916  O   GLU B 124      13.516  19.987 -32.632  1.00 68.13           O  
ANISOU 2916  O   GLU B 124    11951   5485   8451  -3055  -3020   1992       O  
ATOM   2917  CB  GLU B 124      14.163  16.889 -31.686  1.00 62.45           C  
ANISOU 2917  CB  GLU B 124    10448   5669   7609  -2918  -2671   1880       C  
ATOM   2918  CG  GLU B 124      13.358  17.514 -30.557  1.00 63.79           C  
ANISOU 2918  CG  GLU B 124    10911   5571   7754  -2706  -2757   1617       C  
ATOM   2919  CD  GLU B 124      13.501  16.765 -29.248  1.00 62.78           C  
ANISOU 2919  CD  GLU B 124    10705   5593   7556  -2685  -2756   1439       C  
ATOM   2920  OE1 GLU B 124      13.939  15.597 -29.269  1.00 60.58           O  
ANISOU 2920  OE1 GLU B 124    10107   5655   7253  -2716  -2644   1499       O  
ATOM   2921  OE2 GLU B 124      13.176  17.349 -28.195  1.00 64.26           O  
ANISOU 2921  OE2 GLU B 124    11164   5548   7703  -2630  -2868   1240       O  
ATOM   2922  N   LEU B 125      15.705  19.484 -32.488  1.00 67.07           N  
ANISOU 2922  N   LEU B 125    11460   5698   8326  -3613  -3048   2217       N  
ATOM   2923  CA  LEU B 125      16.111  20.846 -32.151  1.00 72.85           C  
ANISOU 2923  CA  LEU B 125    12525   6039   9113  -3873  -3290   2232       C  
ATOM   2924  C   LEU B 125      15.725  21.833 -33.250  1.00 76.42           C  
ANISOU 2924  C   LEU B 125    13213   6204   9616  -3896  -3342   2400       C  
ATOM   2925  O   LEU B 125      15.502  23.014 -32.987  1.00 80.39           O  
ANISOU 2925  O   LEU B 125    14097   6280  10165  -3924  -3525   2338       O  
ATOM   2926  CB  LEU B 125      17.618  20.907 -31.881  1.00 76.34           C  
ANISOU 2926  CB  LEU B 125    12802   6612   9591  -4315  -3393   2382       C  
ATOM   2927  CG  LEU B 125      18.159  22.168 -31.204  1.00 82.69           C  
ANISOU 2927  CG  LEU B 125    13937   7032  10449  -4638  -3676   2372       C  
ATOM   2928  CD1 LEU B 125      17.418  22.436 -29.906  1.00 82.28           C  
ANISOU 2928  CD1 LEU B 125    14220   6697  10345  -4426  -3798   2038       C  
ATOM   2929  CD2 LEU B 125      19.655  22.047 -30.953  1.00 85.87           C  
ANISOU 2929  CD2 LEU B 125    14091   7644  10890  -5066  -3769   2524       C  
ATOM   2930  N   TYR B 126      15.633  21.336 -34.479  1.00 76.19           N  
ANISOU 2930  N   TYR B 126    12972   6403   9571  -3875  -3182   2610       N  
ATOM   2931  CA  TYR B 126      15.256  22.169 -35.614  1.00 79.49           C  
ANISOU 2931  CA  TYR B 126    13591   6598  10014  -3890  -3218   2802       C  
ATOM   2932  C   TYR B 126      13.745  22.238 -35.818  1.00 77.23           C  
ANISOU 2932  C   TYR B 126    13484   6143   9716  -3455  -3191   2657       C  
ATOM   2933  O   TYR B 126      13.182  23.323 -35.967  1.00 80.58           O  
ANISOU 2933  O   TYR B 126    14265   6154  10196  -3382  -3346   2622       O  
ATOM   2934  CB  TYR B 126      15.930  21.668 -36.894  1.00 78.97           C  
ANISOU 2934  CB  TYR B 126    13236   6864   9905  -4054  -3054   3091       C  
ATOM   2935  CG  TYR B 126      15.433  22.348 -38.152  1.00 82.23           C  
ANISOU 2935  CG  TYR B 126    13837   7099  10306  -4058  -3073   3310       C  
ATOM   2936  CD1 TYR B 126      15.842  23.633 -38.479  1.00 88.62           C  
ANISOU 2936  CD1 TYR B 126    14882   7614  11173  -4391  -3237   3524       C  
ATOM   2937  CD2 TYR B 126      14.553  21.703 -39.012  1.00 79.32           C  
ANISOU 2937  CD2 TYR B 126    13416   6856   9865  -3743  -2942   3315       C  
ATOM   2938  CE1 TYR B 126      15.388  24.257 -39.626  1.00 91.92           C  
ANISOU 2938  CE1 TYR B 126    15487   7866  11570  -4399  -3262   3746       C  
ATOM   2939  CE2 TYR B 126      14.095  22.319 -40.161  1.00 82.59           C  
ANISOU 2939  CE2 TYR B 126    14011   7118  10253  -3747  -2978   3526       C  
ATOM   2940  CZ  TYR B 126      14.516  23.596 -40.463  1.00 88.84           C  
ANISOU 2940  CZ  TYR B 126    15042   7616  11095  -4069  -3134   3746       C  
ATOM   2941  OH  TYR B 126      14.063  24.214 -41.606  1.00 92.39           O  
ANISOU 2941  OH  TYR B 126    15686   7910  11508  -4075  -3177   3977       O  
ATOM   2942  N   ASN B 127      13.093  21.080 -35.824  1.00 71.01           N  
ANISOU 2942  N   ASN B 127    12443   5672   8866  -3166  -3000   2575       N  
ATOM   2943  CA  ASN B 127      11.683  21.004 -36.197  1.00 69.13           C  
ANISOU 2943  CA  ASN B 127    12299   5346   8622  -2775  -2960   2488       C  
ATOM   2944  C   ASN B 127      10.691  20.893 -35.039  1.00 66.42           C  
ANISOU 2944  C   ASN B 127    12060   4881   8295  -2439  -2970   2175       C  
ATOM   2945  O   ASN B 127       9.481  20.899 -35.257  1.00 65.53           O  
ANISOU 2945  O   ASN B 127    12027   4672   8200  -2108  -2953   2098       O  
ATOM   2946  CB  ASN B 127      11.453  19.863 -37.193  1.00 65.74           C  
ANISOU 2946  CB  ASN B 127    11565   5300   8114  -2649  -2761   2587       C  
ATOM   2947  CG  ASN B 127      11.200  20.364 -38.602  1.00 68.74           C  
ANISOU 2947  CG  ASN B 127    12058   5588   8472  -2643  -2788   2816       C  
ATOM   2948  OD1 ASN B 127      10.591  21.415 -38.799  1.00 71.79           O  
ANISOU 2948  OD1 ASN B 127    12741   5619   8915  -2537  -2935   2829       O  
ATOM   2949  ND2 ASN B 127      11.668  19.613 -39.591  1.00 68.20           N  
ANISOU 2949  ND2 ASN B 127    11765   5836   8313  -2747  -2645   2997       N  
ATOM   2950  N   PHE B 128      11.195  20.794 -33.814  1.00 65.41           N  
ANISOU 2950  N   PHE B 128    11925   4772   8155  -2523  -2999   2001       N  
ATOM   2951  CA  PHE B 128      10.317  20.644 -32.658  1.00 63.02           C  
ANISOU 2951  CA  PHE B 128    11720   4385   7839  -2218  -2984   1702       C  
ATOM   2952  C   PHE B 128      10.558  21.708 -31.588  1.00 67.00           C  
ANISOU 2952  C   PHE B 128    12577   4515   8367  -2320  -3173   1548       C  
ATOM   2953  O   PHE B 128       9.748  21.872 -30.675  1.00 66.68           O  
ANISOU 2953  O   PHE B 128    12719   4300   8315  -2045  -3180   1302       O  
ATOM   2954  CB  PHE B 128      10.452  19.241 -32.059  1.00 57.50           C  
ANISOU 2954  CB  PHE B 128    10694   4088   7065  -2139  -2817   1586       C  
ATOM   2955  CG  PHE B 128       9.905  18.153 -32.937  1.00 53.64           C  
ANISOU 2955  CG  PHE B 128     9912   3917   6553  -1949  -2631   1660       C  
ATOM   2956  CD1 PHE B 128       8.701  18.319 -33.601  1.00 53.66           C  
ANISOU 2956  CD1 PHE B 128     9979   3826   6586  -1671  -2607   1668       C  
ATOM   2957  CD2 PHE B 128      10.597  16.966 -33.104  1.00 50.55           C  
ANISOU 2957  CD2 PHE B 128     9187   3910   6112  -2047  -2494   1723       C  
ATOM   2958  CE1 PHE B 128       8.196  17.320 -34.410  1.00 50.71           C  
ANISOU 2958  CE1 PHE B 128     9348   3737   6181  -1519  -2461   1730       C  
ATOM   2959  CE2 PHE B 128      10.097  15.963 -33.912  1.00 47.66           C  
ANISOU 2959  CE2 PHE B 128     8582   3808   5716  -1881  -2334   1775       C  
ATOM   2960  CZ  PHE B 128       8.894  16.140 -34.566  1.00 47.76           C  
ANISOU 2960  CZ  PHE B 128     8670   3726   5748  -1629  -2323   1776       C  
ATOM   2961  N   ILE B 129      11.669  22.428 -31.704  1.00 71.23           N  
ANISOU 2961  N   ILE B 129    13207   4928   8929  -2720  -3322   1689       N  
ATOM   2962  CA  ILE B 129      11.992  23.493 -30.758  1.00 75.98           C  
ANISOU 2962  CA  ILE B 129    14171   5148   9549  -2870  -3533   1552       C  
ATOM   2963  C   ILE B 129      11.947  24.866 -31.429  1.00 82.23           C  
ANISOU 2963  C   ILE B 129    15317   5490  10438  -2990  -3713   1693       C  
ATOM   2964  O   ILE B 129      11.327  25.797 -30.914  1.00 85.44           O  
ANISOU 2964  O   ILE B 129    16096   5489  10878  -2818  -3830   1521       O  
ATOM   2965  CB  ILE B 129      13.369  23.270 -30.077  1.00 77.06           C  
ANISOU 2965  CB  ILE B 129    14190   5440   9650  -3263  -3619   1574       C  
ATOM   2966  CG1 ILE B 129      13.224  22.389 -28.833  1.00 72.85           C  
ANISOU 2966  CG1 ILE B 129    13525   5142   9010  -3098  -3533   1323       C  
ATOM   2967  CG2 ILE B 129      13.992  24.593 -29.664  1.00 84.04           C  
ANISOU 2967  CG2 ILE B 129    15454   5896  10581  -3570  -3888   1563       C  
ATOM   2968  CD1 ILE B 129      12.901  20.942 -29.118  1.00 66.31           C  
ANISOU 2968  CD1 ILE B 129    12284   4773   8138  -2891  -3287   1354       C  
ATOM   2969  N   TRP B 130      12.595  24.984 -32.585  1.00101.59           N  
ANISOU 2969  N   TRP B 130    17659   8012  12929  -3273  -3727   2008       N  
ATOM   2970  CA  TRP B 130      12.658  26.259 -33.295  1.00103.62           C  
ANISOU 2970  CA  TRP B 130    18248   7850  13274  -3443  -3906   2188       C  
ATOM   2971  C   TRP B 130      11.596  26.379 -34.385  1.00103.89           C  
ANISOU 2971  C   TRP B 130    18356   7778  13339  -3128  -3852   2287       C  
ATOM   2972  O   TRP B 130      10.550  26.992 -34.176  1.00105.47           O  
ANISOU 2972  O   TRP B 130    18864   7617  13592  -2838  -3935   2140       O  
ATOM   2973  CB  TRP B 130      14.055  26.483 -33.881  1.00 94.17           C  
ANISOU 2973  CB  TRP B 130    16922   6759  12099  -3953  -3963   2499       C  
ATOM   2974  CG  TRP B 130      15.098  26.776 -32.843  1.00 96.92           C  
ANISOU 2974  CG  TRP B 130    17305   7063  12456  -4315  -4113   2431       C  
ATOM   2975  CD1 TRP B 130      15.964  25.888 -32.276  1.00 94.68           C  
ANISOU 2975  CD1 TRP B 130    16663   7182  12130  -4535  -4044   2460       C  
ATOM   2976  CD2 TRP B 130      15.381  28.048 -32.245  1.00102.95           C  
ANISOU 2976  CD2 TRP B 130    18495   7346  13275  -4499  -4375   2319       C  
ATOM   2977  NE1 TRP B 130      16.769  26.526 -31.364  1.00 98.94           N  
ANISOU 2977  NE1 TRP B 130    17360   7540  12693  -4856  -4258   2385       N  
ATOM   2978  CE2 TRP B 130      16.431  27.854 -31.326  1.00104.10           C  
ANISOU 2978  CE2 TRP B 130    18506   7646  13399  -4850  -4466   2290       C  
ATOM   2979  CE3 TRP B 130      14.848  29.332 -32.399  1.00107.94           C  
ANISOU 2979  CE3 TRP B 130    19618   7420  13974  -4396  -4552   2240       C  
ATOM   2980  CZ2 TRP B 130      16.959  28.894 -30.564  1.00110.08           C  
ANISOU 2980  CZ2 TRP B 130    19613   8026  14189  -5123  -4736   2177       C  
ATOM   2981  CZ3 TRP B 130      15.373  30.363 -31.642  1.00113.86           C  
ANISOU 2981  CZ3 TRP B 130    20730   7774  14759  -4652  -4806   2118       C  
ATOM   2982  CH2 TRP B 130      16.418  30.138 -30.736  1.00114.62           C  
ANISOU 2982  CH2 TRP B 130    20677   8057  14816  -5011  -4892   2081       C  
ATOM   2983  N   VAL B 131      11.872  25.799 -35.549  1.00 88.59           N  
ANISOU 2983  N   VAL B 131    16139   6158  11364  -3177  -3717   2532       N  
ATOM   2984  CA  VAL B 131      10.938  25.858 -36.669  1.00 88.69           C  
ANISOU 2984  CA  VAL B 131    16201   6112  11387  -2903  -3681   2649       C  
ATOM   2985  C   VAL B 131       9.903  24.741 -36.569  1.00 82.25           C  
ANISOU 2985  C   VAL B 131    15085   5656  10508  -2519  -3478   2507       C  
ATOM   2986  O   VAL B 131      10.139  23.621 -37.016  1.00 78.59           O  
ANISOU 2986  O   VAL B 131    14277   5619   9966  -2581  -3311   2598       O  
ATOM   2987  CB  VAL B 131      11.672  25.760 -38.019  1.00 91.97           C  
ANISOU 2987  CB  VAL B 131    16575   6589  11780  -3199  -3687   3028       C  
ATOM   2988  CG1 VAL B 131      10.700  25.984 -39.168  1.00 99.43           C  
ANISOU 2988  CG1 VAL B 131    17918   7044  12814  -3472  -3922   3182       C  
ATOM   2989  CG2 VAL B 131      12.807  26.767 -38.075  1.00 89.75           C  
ANISOU 2989  CG2 VAL B 131    15914   6767  11421  -3511  -3535   3161       C  
ATOM   2990  N   HIS B 132       8.753  25.055 -35.982  1.00 81.34           N  
ANISOU 2990  N   HIS B 132    15109   5361  10436  -2118  -3491   2284       N  
ATOM   2991  CA  HIS B 132       7.716  24.056 -35.740  1.00 75.62           C  
ANISOU 2991  CA  HIS B 132    14111   4952   9668  -1760  -3312   2119       C  
ATOM   2992  C   HIS B 132       6.998  23.631 -37.020  1.00 74.79           C  
ANISOU 2992  C   HIS B 132    13864   5006   9546  -1582  -3249   2295       C  
ATOM   2993  O   HIS B 132       6.371  22.573 -37.069  1.00 70.15           O  
ANISOU 2993  O   HIS B 132    12986   4762   8908  -1388  -3093   2228       O  
ATOM   2994  CB  HIS B 132       6.708  24.578 -34.714  1.00 94.80           C  
ANISOU 2994  CB  HIS B 132    16712   7163  12146  -1406  -3329   1807       C  
ATOM   2995  CG  HIS B 132       7.339  25.065 -33.447  1.00 95.37           C  
ANISOU 2995  CG  HIS B 132    16926   7113  12195  -1564  -3384   1604       C  
ATOM   2996  ND1 HIS B 132       7.577  24.242 -32.368  1.00 96.02           N  
ANISOU 2996  ND1 HIS B 132    17103   7115  12265  -1285  -3344   1294       N  
ATOM   2997  CD2 HIS B 132       7.786  26.293 -33.090  1.00 96.22           C  
ANISOU 2997  CD2 HIS B 132    17096   7180  12282  -1980  -3481   1672       C  
ATOM   2998  CE1 HIS B 132       8.142  24.941 -31.399  1.00 96.27           C  
ANISOU 2998  CE1 HIS B 132    17272   7054  12251  -1523  -3424   1171       C  
ATOM   2999  NE2 HIS B 132       8.280  26.188 -31.812  1.00 96.53           N  
ANISOU 2999  NE2 HIS B 132    17280   7107  12289  -1950  -3519   1398       N  
ATOM   3000  N   HIS B 133       7.093  24.462 -38.053  1.00 80.55           N  
ANISOU 3000  N   HIS B 133    14814   5480  10313  -1662  -3386   2524       N  
ATOM   3001  CA  HIS B 133       6.461  24.173 -39.337  1.00 80.67           C  
ANISOU 3001  CA  HIS B 133    14732   5630  10288  -1533  -3361   2722       C  
ATOM   3002  C   HIS B 133       7.125  24.968 -40.458  1.00 86.00           C  
ANISOU 3002  C   HIS B 133    15599   6131  10945  -1839  -3483   3052       C  
ATOM   3003  O   HIS B 133       7.525  26.113 -40.253  1.00 90.83           O  
ANISOU 3003  O   HIS B 133    16525   6351  11636  -2007  -3645   3103       O  
ATOM   3004  CB  HIS B 133       4.959  24.478 -39.284  1.00106.73           C  
ANISOU 3004  CB  HIS B 133    18135   8742  13677  -1079  -3422   2604       C  
ATOM   3005  CG  HIS B 133       4.639  25.926 -39.082  1.00109.88           C  
ANISOU 3005  CG  HIS B 133    18947   8603  14200  -1001  -3625   2597       C  
ATOM   3006  ND1 HIS B 133       3.632  26.567 -39.771  1.00112.27           N  
ANISOU 3006  ND1 HIS B 133    19436   8649  14572   -792  -3764   2743       N  
ATOM   3007  CD2 HIS B 133       5.185  26.857 -38.264  1.00111.00           C  
ANISOU 3007  CD2 HIS B 133    19368   8398  14410  -1100  -3724   2457       C  
ATOM   3008  CE1 HIS B 133       3.576  27.831 -39.391  1.00114.76           C  
ANISOU 3008  CE1 HIS B 133    20131   8469  15003   -754  -3932   2696       C  
ATOM   3009  NE2 HIS B 133       4.507  28.032 -38.476  1.00114.08           N  
ANISOU 3009  NE2 HIS B 133    20117   8315  14914   -943  -3910   2514       N  
ATOM   3010  N   PRO B 134       7.249  24.361 -41.650  1.00 84.63           N  
ANISOU 3010  N   PRO B 134    15254   6244  10658  -1924  -3403   3278       N  
ATOM   3011  CA  PRO B 134       6.809  22.999 -41.969  1.00 79.55           C  
ANISOU 3011  CA  PRO B 134    14264   6047   9912  -1756  -3223   3223       C  
ATOM   3012  C   PRO B 134       7.872  21.951 -41.654  1.00 75.69           C  
ANISOU 3012  C   PRO B 134    13476   5943   9341  -1986  -3035   3174       C  
ATOM   3013  O   PRO B 134       9.008  22.299 -41.334  1.00 77.56           O  
ANISOU 3013  O   PRO B 134    13749   6139   9583  -2321  -3047   3255       O  
ATOM   3014  CB  PRO B 134       6.587  23.067 -43.478  1.00 82.39           C  
ANISOU 3014  CB  PRO B 134    14663   6473  10170  -1805  -3258   3516       C  
ATOM   3015  CG  PRO B 134       7.619  24.035 -43.943  1.00 87.72           C  
ANISOU 3015  CG  PRO B 134    15569   6919  10842  -2179  -3356   3766       C  
ATOM   3016  CD  PRO B 134       7.757  25.062 -42.843  1.00 89.93           C  
ANISOU 3016  CD  PRO B 134    16106   6781  11284  -2193  -3500   3619       C  
ATOM   3017  N   TRP B 135       7.498  20.679 -41.746  1.00 70.81           N  
ANISOU 3017  N   TRP B 135    12562   5683   8659  -1808  -2874   3048       N  
ATOM   3018  CA  TRP B 135       8.440  19.584 -41.552  1.00 67.41           C  
ANISOU 3018  CA  TRP B 135    11838   5627   8150  -1987  -2690   3016       C  
ATOM   3019  C   TRP B 135       9.393  19.505 -42.740  1.00 69.82           C  
ANISOU 3019  C   TRP B 135    12078   6118   8333  -2281  -2620   3295       C  
ATOM   3020  O   TRP B 135       8.960  19.462 -43.893  1.00 71.22           O  
ANISOU 3020  O   TRP B 135    12285   6362   8416  -2221  -2619   3448       O  
ATOM   3021  CB  TRP B 135       7.689  18.263 -41.374  1.00 62.25           C  
ANISOU 3021  CB  TRP B 135    10916   5277   7459  -1715  -2547   2830       C  
ATOM   3022  CG  TRP B 135       8.585  17.075 -41.199  1.00 59.07           C  
ANISOU 3022  CG  TRP B 135    10219   5244   6981  -1860  -2360   2801       C  
ATOM   3023  CD1 TRP B 135       8.913  16.151 -42.147  1.00 58.17           C  
ANISOU 3023  CD1 TRP B 135     9912   5448   6742  -1912  -2219   2905       C  
ATOM   3024  CD2 TRP B 135       9.271  16.681 -40.002  1.00 56.74           C  
ANISOU 3024  CD2 TRP B 135     9800   5032   6728  -1958  -2300   2657       C  
ATOM   3025  NE1 TRP B 135       9.760  15.207 -41.617  1.00 55.52           N  
ANISOU 3025  NE1 TRP B 135     9333   5376   6385  -2019  -2067   2835       N  
ATOM   3026  CE2 TRP B 135       9.995  15.510 -40.302  1.00 54.58           C  
ANISOU 3026  CE2 TRP B 135     9244   5126   6369  -2053  -2122   2693       C  
ATOM   3027  CE3 TRP B 135       9.341  17.206 -38.708  1.00 56.57           C  
ANISOU 3027  CE3 TRP B 135     9892   4807   6796  -1968  -2386   2499       C  
ATOM   3028  CZ2 TRP B 135      10.777  14.853 -39.355  1.00 52.32           C  
ANISOU 3028  CZ2 TRP B 135     8769   5008   6103  -2152  -2038   2595       C  
ATOM   3029  CZ3 TRP B 135      10.120  16.554 -37.771  1.00 54.23           C  
ANISOU 3029  CZ3 TRP B 135     9417   4690   6496  -2085  -2309   2400       C  
ATOM   3030  CH2 TRP B 135      10.826  15.389 -38.098  1.00 52.15           C  
ANISOU 3030  CH2 TRP B 135     8857   4793   6165  -2173  -2142   2457       C  
ATOM   3031  N   ALA B 136      10.691  19.487 -42.456  1.00 70.57           N  
ANISOU 3031  N   ALA B 136    12078   6311   8422  -2597  -2560   3364       N  
ATOM   3032  CA  ALA B 136      11.699  19.587 -43.506  1.00 73.88           C  
ANISOU 3032  CA  ALA B 136    12453   6878   8741  -2910  -2489   3647       C  
ATOM   3033  C   ALA B 136      12.566  18.338 -43.654  1.00 71.05           C  
ANISOU 3033  C   ALA B 136    11751   6981   8264  -2958  -2249   3656       C  
ATOM   3034  O   ALA B 136      13.684  18.415 -44.163  1.00 73.31           O  
ANISOU 3034  O   ALA B 136    11985   7450   8420  -3110  -2147   3870       O  
ATOM   3035  CB  ALA B 136      12.577  20.813 -43.274  1.00 78.04           C  
ANISOU 3035  CB  ALA B 136    13105   7195   9351  -3268  -2593   3771       C  
ATOM   3036  N   PHE B 137      12.055  17.191 -43.219  1.00 80.16           N  
ANISOU 3036  N   PHE B 137    12685   8317   9455  -2822  -2154   3426       N  
ATOM   3037  CA  PHE B 137      12.822  15.951 -43.307  1.00 77.97           C  
ANISOU 3037  CA  PHE B 137    12088   8445   9094  -2869  -1933   3422       C  
ATOM   3038  C   PHE B 137      12.077  14.831 -44.029  1.00 75.71           C  
ANISOU 3038  C   PHE B 137    11690   8389   8689  -2616  -1808   3352       C  
ATOM   3039  O   PHE B 137      12.594  13.723 -44.164  1.00 73.86           O  
ANISOU 3039  O   PHE B 137    11206   8460   8396  -2589  -1629   3292       O  
ATOM   3040  CB  PHE B 137      13.272  15.489 -41.920  1.00 61.21           C  
ANISOU 3040  CB  PHE B 137     9781   6408   7068  -2887  -1901   3241       C  
ATOM   3041  CG  PHE B 137      14.174  16.463 -41.222  1.00 64.07           C  
ANISOU 3041  CG  PHE B 137    10261   6542   7541  -3143  -2051   3283       C  
ATOM   3042  CD1 PHE B 137      15.479  16.646 -41.650  1.00 67.60           C  
ANISOU 3042  CD1 PHE B 137    10602   7092   7989  -3490  -2015   3490       C  
ATOM   3043  CD2 PHE B 137      13.721  17.195 -40.138  1.00 63.63           C  
ANISOU 3043  CD2 PHE B 137    10420   6171   7584  -3041  -2226   3112       C  
ATOM   3044  CE1 PHE B 137      16.313  17.544 -41.012  1.00 70.73           C  
ANISOU 3044  CE1 PHE B 137    11108   7273   8493  -3756  -2177   3531       C  
ATOM   3045  CE2 PHE B 137      14.551  18.094 -39.494  1.00 66.66           C  
ANISOU 3045  CE2 PHE B 137    10944   6328   8059  -3288  -2381   3134       C  
ATOM   3046  CZ  PHE B 137      15.849  18.268 -39.932  1.00 70.27           C  
ANISOU 3046  CZ  PHE B 137    11296   6880   8523  -3658  -2369   3346       C  
ATOM   3047  N   GLY B 138      10.867  15.123 -44.491  1.00 61.96           N  
ANISOU 3047  N   GLY B 138    10134   6492   6915  -2432  -1916   3362       N  
ATOM   3048  CA  GLY B 138      10.100  14.168 -45.269  1.00 60.01           C  
ANISOU 3048  CA  GLY B 138     9808   6445   6551  -2218  -1837   3310       C  
ATOM   3049  C   GLY B 138       9.376  13.118 -44.450  1.00 55.20           C  
ANISOU 3049  C   GLY B 138     9036   5935   6003  -1956  -1792   3044       C  
ATOM   3050  O   GLY B 138       9.587  12.990 -43.240  1.00 52.99           O  
ANISOU 3050  O   GLY B 138     8687   5603   5842  -1932  -1797   2891       O  
ATOM   3051  N   ASP B 139       8.519  12.360 -45.127  1.00 55.17           N  
ANISOU 3051  N   ASP B 139     8979   6079   5905  -1776  -1754   2997       N  
ATOM   3052  CA  ASP B 139       7.720  11.319 -44.493  1.00 51.11           C  
ANISOU 3052  CA  ASP B 139     8308   5671   5441  -1541  -1711   2769       C  
ATOM   3053  C   ASP B 139       8.609  10.247 -43.865  1.00 48.30           C  
ANISOU 3053  C   ASP B 139     7714   5551   5085  -1600  -1528   2665       C  
ATOM   3054  O   ASP B 139       8.385   9.824 -42.725  1.00 45.30           O  
ANISOU 3054  O   ASP B 139     7228   5178   4807  -1485  -1511   2487       O  
ATOM   3055  CB  ASP B 139       6.779  10.689 -45.522  1.00 71.72           C  
ANISOU 3055  CB  ASP B 139    10922   8392   7938  -1386  -1730   2773       C  
ATOM   3056  CG  ASP B 139       5.607   9.975 -44.882  1.00 70.63           C  
ANISOU 3056  CG  ASP B 139    10656   8301   7881  -1141  -1739   2561       C  
ATOM   3057  OD1 ASP B 139       4.565  10.626 -44.652  1.00 71.44           O  
ANISOU 3057  OD1 ASP B 139    10832   8293   8020   -968  -1879   2549       O  
ATOM   3058  OD2 ASP B 139       5.724   8.762 -44.615  1.00 69.16           O  
ANISOU 3058  OD2 ASP B 139    10287   8266   7725  -1123  -1609   2420       O  
ATOM   3059  N   ALA B 140       9.621   9.819 -44.615  1.00 69.19           N  
ANISOU 3059  N   ALA B 140    10277   8396   7617  -1769  -1388   2785       N  
ATOM   3060  CA  ALA B 140      10.565   8.814 -44.141  1.00 67.93           C  
ANISOU 3060  CA  ALA B 140     9884   8459   7466  -1820  -1213   2713       C  
ATOM   3061  C   ALA B 140      11.398   9.347 -42.980  1.00 68.48           C  
ANISOU 3061  C   ALA B 140     9907   8434   7679  -1936  -1253   2686       C  
ATOM   3062  O   ALA B 140      11.834   8.586 -42.116  1.00 67.31           O  
ANISOU 3062  O   ALA B 140     9588   8392   7595  -1890  -1182   2558       O  
ATOM   3063  CB  ALA B 140      11.464   8.354 -45.277  1.00 48.42           C  
ANISOU 3063  CB  ALA B 140     7341   6213   4845  -1968  -1046   2863       C  
ATOM   3064  N   GLY B 141      11.616  10.658 -42.970  1.00 69.54           N  
ANISOU 3064  N   GLY B 141    10210   8355   7859  -2095  -1381   2810       N  
ATOM   3065  CA  GLY B 141      12.311  11.305 -41.874  1.00 70.74           C  
ANISOU 3065  CA  GLY B 141    10368   8372   8138  -2221  -1464   2778       C  
ATOM   3066  C   GLY B 141      11.471  11.273 -40.613  1.00 70.54           C  
ANISOU 3066  C   GLY B 141    10400   8194   8208  -2010  -1559   2559       C  
ATOM   3067  O   GLY B 141      11.980  11.012 -39.524  1.00 70.56           O  
ANISOU 3067  O   GLY B 141    10308   8224   8279  -2020  -1554   2442       O  
ATOM   3068  N   CYS B 142      10.177  11.536 -40.767  1.00 46.45           N  
ANISOU 3068  N   CYS B 142     7497   4999   5154  -1812  -1644   2510       N  
ATOM   3069  CA  CYS B 142       9.242  11.485 -39.646  1.00 44.09           C  
ANISOU 3069  CA  CYS B 142     7245   4568   4940  -1582  -1713   2310       C  
ATOM   3070  C   CYS B 142       9.159  10.078 -39.053  1.00 40.25           C  
ANISOU 3070  C   CYS B 142     6532   4305   4455  -1453  -1584   2145       C  
ATOM   3071  O   CYS B 142       9.492   9.851 -37.872  1.00 38.45           O  
ANISOU 3071  O   CYS B 142     6276   4043   4289  -1414  -1593   2008       O  
ATOM   3072  CB  CYS B 142       7.853  11.933 -40.107  1.00 78.52           C  
ANISOU 3072  CB  CYS B 142    11746   8791   9299  -1379  -1808   2315       C  
ATOM   3073  SG  CYS B 142       6.545  11.739 -38.878  1.00 79.24           S  
ANISOU 3073  SG  CYS B 142    11861   8750   9499  -1066  -1865   2081       S  
ATOM   3074  N   ARG B 143       8.707   9.142 -39.888  1.00 44.83           N  
ANISOU 3074  N   ARG B 143     6971   5104   4956  -1393  -1469   2161       N  
ATOM   3075  CA  ARG B 143       8.552   7.746 -39.494  1.00 41.83           C  
ANISOU 3075  CA  ARG B 143     6393   4920   4581  -1276  -1351   2020       C  
ATOM   3076  C   ARG B 143       9.844   7.185 -38.911  1.00 41.11           C  
ANISOU 3076  C   ARG B 143     6147   4966   4505  -1419  -1260   2023       C  
ATOM   3077  O   ARG B 143       9.832   6.525 -37.871  1.00 39.14           O  
ANISOU 3077  O   ARG B 143     5803   4763   4305  -1351  -1232   1897       O  
ATOM   3078  CB  ARG B 143       8.116   6.900 -40.692  1.00 62.12           C  
ANISOU 3078  CB  ARG B 143     8884   7661   7057  -1193  -1268   2036       C  
ATOM   3079  CG  ARG B 143       6.751   7.258 -41.254  1.00 63.00           C  
ANISOU 3079  CG  ARG B 143     9107   7673   7158  -1036  -1375   2028       C  
ATOM   3080  CD  ARG B 143       6.458   6.451 -42.511  1.00 62.22           C  
ANISOU 3080  CD  ARG B 143     8956   7745   6939  -1000  -1316   2056       C  
ATOM   3081  NE  ARG B 143       5.147   5.809 -42.463  1.00 62.31           N  
ANISOU 3081  NE  ARG B 143     8933   7759   6982   -807  -1375   1950       N  
ATOM   3082  CZ  ARG B 143       4.032   6.341 -42.952  1.00 63.80           C  
ANISOU 3082  CZ  ARG B 143     9228   7843   7169   -710  -1516   1996       C  
ATOM   3083  NH1 ARG B 143       4.060   7.533 -43.533  1.00 65.18           N  
ANISOU 3083  NH1 ARG B 143     9578   7881   7305   -785  -1614   2149       N  
ATOM   3084  NH2 ARG B 143       2.886   5.680 -42.860  1.00 64.18           N  
ANISOU 3084  NH2 ARG B 143     9199   7923   7262   -544  -1566   1904       N  
ATOM   3085  N   GLY B 144      10.956   7.462 -39.585  1.00 58.07           N  
ANISOU 3085  N   GLY B 144     8265   7190   6611  -1619  -1216   2181       N  
ATOM   3086  CA  GLY B 144      12.258   7.000 -39.140  1.00 57.93           C  
ANISOU 3086  CA  GLY B 144     8065   7330   6616  -1758  -1130   2215       C  
ATOM   3087  C   GLY B 144      12.649   7.584 -37.797  1.00 59.21           C  
ANISOU 3087  C   GLY B 144     8256   7374   6869  -1849  -1240   2165       C  
ATOM   3088  O   GLY B 144      13.226   6.891 -36.958  1.00 58.74           O  
ANISOU 3088  O   GLY B 144     8034   7441   6844  -1871  -1196   2119       O  
ATOM   3089  N   TYR B 145      12.335   8.861 -37.599  1.00 50.44           N  
ANISOU 3089  N   TYR B 145     7366   6010   5790  -1900  -1394   2174       N  
ATOM   3090  CA  TYR B 145      12.586   9.540 -36.330  1.00 52.35           C  
ANISOU 3090  CA  TYR B 145     7693   6100   6098  -1991  -1521   2107       C  
ATOM   3091  C   TYR B 145      11.877   8.825 -35.183  1.00 51.02           C  
ANISOU 3091  C   TYR B 145     7478   5964   5945  -1801  -1505   1905       C  
ATOM   3092  O   TYR B 145      12.521   8.345 -34.235  1.00 50.93           O  
ANISOU 3092  O   TYR B 145     7349   6054   5948  -1867  -1500   1867       O  
ATOM   3093  CB  TYR B 145      12.124  11.000 -36.418  1.00 52.83           C  
ANISOU 3093  CB  TYR B 145     8043   5844   6186  -2031  -1685   2128       C  
ATOM   3094  CG  TYR B 145      12.170  11.775 -35.119  1.00 55.35           C  
ANISOU 3094  CG  TYR B 145     8520   5955   6556  -2079  -1829   2011       C  
ATOM   3095  CD1 TYR B 145      13.362  12.315 -34.651  1.00 57.88           C  
ANISOU 3095  CD1 TYR B 145     8855   6230   6907  -2361  -1925   2092       C  
ATOM   3096  CD2 TYR B 145      11.015  11.988 -34.375  1.00 55.47           C  
ANISOU 3096  CD2 TYR B 145     8674   5820   6582  -1848  -1871   1818       C  
ATOM   3097  CE1 TYR B 145      13.405  13.031 -33.468  1.00 59.90           C  
ANISOU 3097  CE1 TYR B 145     9286   6284   7189  -2418  -2075   1970       C  
ATOM   3098  CE2 TYR B 145      11.048  12.702 -33.192  1.00 57.68           C  
ANISOU 3098  CE2 TYR B 145     9128   5907   6880  -1882  -1993   1691       C  
ATOM   3099  CZ  TYR B 145      12.245  13.221 -32.743  1.00 59.58           C  
ANISOU 3099  CZ  TYR B 145     9410   6091   7138  -2170  -2104   1762       C  
ATOM   3100  OH  TYR B 145      12.283  13.934 -31.565  1.00 61.27           O  
ANISOU 3100  OH  TYR B 145     9826   6102   7350  -2216  -2242   1622       O  
ATOM   3101  N   TYR B 146      10.553   8.739 -35.277  1.00 57.51           N  
ANISOU 3101  N   TYR B 146     8380   6712   6760  -1568  -1497   1793       N  
ATOM   3102  CA  TYR B 146       9.777   8.127 -34.196  1.00 56.59           C  
ANISOU 3102  CA  TYR B 146     8230   6623   6651  -1383  -1467   1613       C  
ATOM   3103  C   TYR B 146      10.117   6.646 -33.974  1.00 54.00           C  
ANISOU 3103  C   TYR B 146     7657   6556   6304  -1343  -1329   1597       C  
ATOM   3104  O   TYR B 146      10.250   6.192 -32.826  1.00 53.61           O  
ANISOU 3104  O   TYR B 146     7548   6567   6256  -1305  -1314   1503       O  
ATOM   3105  CB  TYR B 146       8.277   8.342 -34.412  1.00 44.04           C  
ANISOU 3105  CB  TYR B 146     6742   4919   5073  -1147  -1479   1522       C  
ATOM   3106  CG  TYR B 146       7.853   9.775 -34.175  1.00 47.34           C  
ANISOU 3106  CG  TYR B 146     7417   5046   5525  -1126  -1618   1495       C  
ATOM   3107  CD1 TYR B 146       7.870  10.706 -35.205  1.00 48.69           C  
ANISOU 3107  CD1 TYR B 146     7722   5072   5706  -1171  -1697   1623       C  
ATOM   3108  CD2 TYR B 146       7.455  10.200 -32.914  1.00 49.42           C  
ANISOU 3108  CD2 TYR B 146     7808   5169   5800  -1054  -1671   1340       C  
ATOM   3109  CE1 TYR B 146       7.493  12.018 -34.988  1.00 52.04           C  
ANISOU 3109  CE1 TYR B 146     8400   5199   6175  -1139  -1833   1603       C  
ATOM   3110  CE2 TYR B 146       7.075  11.508 -32.686  1.00 52.86           C  
ANISOU 3110  CE2 TYR B 146     8502   5314   6270  -1014  -1795   1298       C  
ATOM   3111  CZ  TYR B 146       7.096  12.415 -33.726  1.00 54.17           C  
ANISOU 3111  CZ  TYR B 146     8796   5318   6468  -1053  -1880   1431       C  
ATOM   3112  OH  TYR B 146       6.717  13.722 -33.505  1.00 57.81           O  
ANISOU 3112  OH  TYR B 146     9531   5458   6975  -1001  -2012   1394       O  
ATOM   3113  N   PHE B 147      10.276   5.909 -35.072  1.00 47.88           N  
ANISOU 3113  N   PHE B 147     6763   5927   5502  -1349  -1232   1691       N  
ATOM   3114  CA  PHE B 147      10.674   4.504 -35.012  1.00 46.06           C  
ANISOU 3114  CA  PHE B 147     6321   5919   5260  -1308  -1100   1681       C  
ATOM   3115  C   PHE B 147      12.000   4.336 -34.280  1.00 46.78           C  
ANISOU 3115  C   PHE B 147     6289   6107   5378  -1456  -1101   1729       C  
ATOM   3116  O   PHE B 147      12.135   3.463 -33.420  1.00 46.09           O  
ANISOU 3116  O   PHE B 147     6092   6116   5304  -1396  -1064   1663       O  
ATOM   3117  CB  PHE B 147      10.771   3.907 -36.420  1.00 43.63           C  
ANISOU 3117  CB  PHE B 147     5943   5733   4902  -1302   -997   1768       C  
ATOM   3118  CG  PHE B 147      11.335   2.514 -36.453  1.00 42.64           C  
ANISOU 3118  CG  PHE B 147     5620   5814   4770  -1266   -858   1762       C  
ATOM   3119  CD1 PHE B 147      10.525   1.420 -36.204  1.00 41.44           C  
ANISOU 3119  CD1 PHE B 147     5410   5714   4624  -1103   -802   1648       C  
ATOM   3120  CD2 PHE B 147      12.672   2.299 -36.746  1.00 43.46           C  
ANISOU 3120  CD2 PHE B 147     5590   6055   4870  -1394   -782   1876       C  
ATOM   3121  CE1 PHE B 147      11.038   0.140 -36.235  1.00 41.16           C  
ANISOU 3121  CE1 PHE B 147     5218   5832   4590  -1061   -683   1641       C  
ATOM   3122  CE2 PHE B 147      13.192   1.021 -36.775  1.00 43.21           C  
ANISOU 3122  CE2 PHE B 147     5380   6196   4842  -1329   -651   1864       C  
ATOM   3123  CZ  PHE B 147      12.373  -0.060 -36.521  1.00 42.10           C  
ANISOU 3123  CZ  PHE B 147     5216   6075   4708  -1160   -607   1743       C  
ATOM   3124  N   LEU B 148      12.975   5.171 -34.627  1.00 41.53           N  
ANISOU 3124  N   LEU B 148     5638   5418   4723  -1659  -1153   1859       N  
ATOM   3125  CA  LEU B 148      14.285   5.124 -33.987  1.00 42.96           C  
ANISOU 3125  CA  LEU B 148     5681   5699   4942  -1828  -1179   1929       C  
ATOM   3126  C   LEU B 148      14.180   5.402 -32.493  1.00 43.96           C  
ANISOU 3126  C   LEU B 148     5887   5731   5083  -1836  -1305   1818       C  
ATOM   3127  O   LEU B 148      14.775   4.685 -31.677  1.00 44.12           O  
ANISOU 3127  O   LEU B 148     5762   5881   5118  -1852  -1302   1810       O  
ATOM   3128  CB  LEU B 148      15.244   6.123 -34.636  1.00 48.63           C  
ANISOU 3128  CB  LEU B 148     6412   6390   5675  -2072  -1228   2099       C  
ATOM   3129  CG  LEU B 148      16.627   6.223 -33.990  1.00 50.66           C  
ANISOU 3129  CG  LEU B 148     6504   6758   5989  -2282  -1279   2196       C  
ATOM   3130  CD1 LEU B 148      17.331   4.873 -34.007  1.00 49.76           C  
ANISOU 3130  CD1 LEU B 148     6099   6914   5893  -2210  -1124   2237       C  
ATOM   3131  CD2 LEU B 148      17.468   7.279 -34.689  1.00 53.04           C  
ANISOU 3131  CD2 LEU B 148     6837   7005   6311  -2547  -1338   2373       C  
ATOM   3132  N   ARG B 149      13.424   6.440 -32.137  1.00 45.97           N  
ANISOU 3132  N   ARG B 149     6383   5760   5325  -1813  -1416   1731       N  
ATOM   3133  CA  ARG B 149      13.219   6.767 -30.727  1.00 47.19           C  
ANISOU 3133  CA  ARG B 149     6657   5812   5462  -1807  -1527   1602       C  
ATOM   3134  C   ARG B 149      12.661   5.576 -29.948  1.00 44.78           C  
ANISOU 3134  C   ARG B 149     6257   5633   5126  -1618  -1439   1488       C  
ATOM   3135  O   ARG B 149      13.263   5.130 -28.959  1.00 44.88           O  
ANISOU 3135  O   ARG B 149     6200   5733   5121  -1667  -1477   1469       O  
ATOM   3136  CB  ARG B 149      12.302   7.982 -30.570  1.00112.74           C  
ANISOU 3136  CB  ARG B 149    15246  13838  13753  -1756  -1630   1507       C  
ATOM   3137  CG  ARG B 149      12.901   9.277 -31.082  1.00114.23           C  
ANISOU 3137  CG  ARG B 149    15591  13843  13970  -1992  -1781   1596       C  
ATOM   3138  CD  ARG B 149      12.034  10.471 -30.715  1.00116.70           C  
ANISOU 3138  CD  ARG B 149    16216  13852  14273  -1922  -1900   1465       C  
ATOM   3139  NE  ARG B 149      12.050  10.752 -29.282  1.00119.19           N  
ANISOU 3139  NE  ARG B 149    16705  13974  14609  -2178  -2080   1513       N  
ATOM   3140  CZ  ARG B 149      12.852  11.641 -28.703  1.00121.11           C  
ANISOU 3140  CZ  ARG B 149    17123  14079  14816  -2240  -2213   1383       C  
ATOM   3141  NH1 ARG B 149      13.708  12.341 -29.434  1.00120.79           N  
ANISOU 3141  NH1 ARG B 149    17103  14089  14704  -2055  -2169   1204       N  
ATOM   3142  NH2 ARG B 149      12.799  11.831 -27.392  1.00123.33           N  
ANISOU 3142  NH2 ARG B 149    17569  14170  15122  -2500  -2393   1433       N  
ATOM   3143  N   ASP B 150      11.522   5.057 -30.406  1.00 46.43           N  
ANISOU 3143  N   ASP B 150     6460   5855   5328  -1416  -1332   1428       N  
ATOM   3144  CA  ASP B 150      10.896   3.906 -29.757  1.00 44.73           C  
ANISOU 3144  CA  ASP B 150     6159   5749   5090  -1249  -1242   1334       C  
ATOM   3145  C   ASP B 150      11.851   2.720 -29.634  1.00 43.74           C  
ANISOU 3145  C   ASP B 150     5811   5828   4980  -1293  -1177   1412       C  
ATOM   3146  O   ASP B 150      11.998   2.144 -28.551  1.00 43.55           O  
ANISOU 3146  O   ASP B 150     5744   5873   4931  -1269  -1185   1371       O  
ATOM   3147  CB  ASP B 150       9.621   3.490 -30.495  1.00 30.71           C  
ANISOU 3147  CB  ASP B 150     4379   3966   3322  -1062  -1147   1286       C  
ATOM   3148  CG  ASP B 150       8.386   4.206 -29.975  1.00 31.73           C  
ANISOU 3148  CG  ASP B 150     4686   3930   3439   -933  -1190   1166       C  
ATOM   3149  OD1 ASP B 150       8.530   5.310 -29.404  1.00 33.86           O  
ANISOU 3149  OD1 ASP B 150     5131   4036   3699  -1000  -1299   1136       O  
ATOM   3150  OD2 ASP B 150       7.272   3.658 -30.138  1.00 31.51           O  
ANISOU 3150  OD2 ASP B 150     4620   3934   3419   -763  -1114   1100       O  
ATOM   3151  N   ALA B 151      12.507   2.377 -30.740  1.00 38.13           N  
ANISOU 3151  N   ALA B 151     4968   5214   4305  -1348  -1110   1529       N  
ATOM   3152  CA  ALA B 151      13.449   1.262 -30.766  1.00 38.10           C  
ANISOU 3152  CA  ALA B 151     4747   5400   4332  -1358  -1032   1605       C  
ATOM   3153  C   ALA B 151      14.538   1.419 -29.709  1.00 39.68           C  
ANISOU 3153  C   ALA B 151     4880   5652   4546  -1498  -1139   1654       C  
ATOM   3154  O   ALA B 151      14.834   0.478 -28.967  1.00 39.49           O  
ANISOU 3154  O   ALA B 151     4736   5740   4531  -1448  -1123   1657       O  
ATOM   3155  CB  ALA B 151      14.066   1.123 -32.148  1.00 25.59           C  
ANISOU 3155  CB  ALA B 151     3053   3904   2768  -1402   -936   1717       C  
ATOM   3156  N   CYS B 152      15.123   2.611 -29.637  1.00 38.65           N  
ANISOU 3156  N   CYS B 152     4836   5430   4418  -1681  -1266   1698       N  
ATOM   3157  CA  CYS B 152      16.166   2.881 -28.653  1.00 40.32           C  
ANISOU 3157  CA  CYS B 152     4992   5685   4640  -1849  -1404   1749       C  
ATOM   3158  C   CYS B 152      15.645   2.762 -27.220  1.00 39.72           C  
ANISOU 3158  C   CYS B 152     5038   5561   4491  -1789  -1490   1623       C  
ATOM   3159  O   CYS B 152      16.329   2.214 -26.349  1.00 40.24           O  
ANISOU 3159  O   CYS B 152     4992   5744   4552  -1830  -1551   1659       O  
ATOM   3160  CB  CYS B 152      16.794   4.257 -28.887  1.00 59.37           C  
ANISOU 3160  CB  CYS B 152     7502   7983   7074  -2084  -1537   1820       C  
ATOM   3161  SG  CYS B 152      17.876   4.335 -30.333  1.00 60.72           S  
ANISOU 3161  SG  CYS B 152     7466   8284   7322  -2230  -1445   2026       S  
ATOM   3162  N   THR B 153      14.436   3.267 -26.982  1.00 48.66           N  
ANISOU 3162  N   THR B 153     6393   6533   5562  -1682  -1491   1481       N  
ATOM   3163  CA  THR B 153      13.817   3.147 -25.661  1.00 48.48           C  
ANISOU 3163  CA  THR B 153     6501   6476   5445  -1608  -1540   1352       C  
ATOM   3164  C   THR B 153      13.670   1.683 -25.244  1.00 47.07           C  
ANISOU 3164  C   THR B 153     6172   6460   5255  -1464  -1430   1357       C  
ATOM   3165  O   THR B 153      14.100   1.286 -24.152  1.00 47.52           O  
ANISOU 3165  O   THR B 153     6218   6589   5251  -1486  -1496   1351       O  
ATOM   3166  CB  THR B 153      12.429   3.816 -25.611  1.00105.44           C  
ANISOU 3166  CB  THR B 153    13955  13503  12604  -1481  -1524   1198       C  
ATOM   3167  OG1 THR B 153      11.564   3.209 -26.579  1.00103.98           O  
ANISOU 3167  OG1 THR B 153    13706  13344  12459  -1301  -1369   1184       O  
ATOM   3168  CG2 THR B 153      12.540   5.303 -25.895  1.00107.44           C  
ANISOU 3168  CG2 THR B 153    14393  13554  12874  -1612  -1645   1192       C  
ATOM   3169  N   TYR B 154      13.064   0.888 -26.124  1.00 37.59           N  
ANISOU 3169  N   TYR B 154     4870   5306   4105  -1325  -1277   1372       N  
ATOM   3170  CA  TYR B 154      12.864  -0.537 -25.866  1.00 36.78           C  
ANISOU 3170  CA  TYR B 154     4636   5329   4009  -1196  -1171   1384       C  
ATOM   3171  C   TYR B 154      14.183  -1.255 -25.606  1.00 37.72           C  
ANISOU 3171  C   TYR B 154     4565   5595   4172  -1269  -1210   1509       C  
ATOM   3172  O   TYR B 154      14.301  -2.033 -24.654  1.00 38.10           O  
ANISOU 3172  O   TYR B 154     4578   5714   4182  -1229  -1230   1518       O  
ATOM   3173  CB  TYR B 154      12.131  -1.205 -27.032  1.00 41.00           C  
ANISOU 3173  CB  TYR B 154     5104   5873   4599  -1069  -1023   1381       C  
ATOM   3174  CG  TYR B 154      10.654  -0.895 -27.095  1.00 40.47           C  
ANISOU 3174  CG  TYR B 154     5169   5710   4497   -944   -972   1263       C  
ATOM   3175  CD1 TYR B 154       9.796  -1.312 -26.084  1.00 40.76           C  
ANISOU 3175  CD1 TYR B 154     5239   5766   4481   -846   -931   1191       C  
ATOM   3176  CD2 TYR B 154      10.113  -0.201 -28.172  1.00 40.22           C  
ANISOU 3176  CD2 TYR B 154     5213   5579   4487   -922   -964   1238       C  
ATOM   3177  CE1 TYR B 154       8.445  -1.040 -26.136  1.00 41.11           C  
ANISOU 3177  CE1 TYR B 154     5365   5747   4508   -728   -872   1093       C  
ATOM   3178  CE2 TYR B 154       8.761   0.080 -28.233  1.00 40.51           C  
ANISOU 3178  CE2 TYR B 154     5338   5542   4510   -794   -926   1142       C  
ATOM   3179  CZ  TYR B 154       7.931  -0.344 -27.212  1.00 41.12           C  
ANISOU 3179  CZ  TYR B 154     5422   5654   4548   -695   -874   1067       C  
ATOM   3180  OH  TYR B 154       6.583  -0.072 -27.264  1.00 42.20           O  
ANISOU 3180  OH  TYR B 154     5609   5740   4684   -564   -825    980       O  
ATOM   3181  N   ALA B 155      15.170  -0.987 -26.457  1.00 47.45           N  
ANISOU 3181  N   ALA B 155     5669   6879   5482  -1373  -1219   1617       N  
ATOM   3182  CA  ALA B 155      16.492  -1.587 -26.312  1.00 49.10           C  
ANISOU 3182  CA  ALA B 155     5657   7242   5756  -1432  -1250   1749       C  
ATOM   3183  C   ALA B 155      17.086  -1.268 -24.945  1.00 50.32           C  
ANISOU 3183  C   ALA B 155     5844   7418   5856  -1552  -1436   1765       C  
ATOM   3184  O   ALA B 155      17.605  -2.154 -24.259  1.00 51.13           O  
ANISOU 3184  O   ALA B 155     5820   7636   5971  -1519  -1470   1832       O  
ATOM   3185  CB  ALA B 155      17.416  -1.111 -27.421  1.00 35.77           C  
ANISOU 3185  CB  ALA B 155     3827   5612   4150  -1543  -1222   1863       C  
ATOM   3186  N   THR B 156      16.992  -0.001 -24.551  1.00 48.43           N  
ANISOU 3186  N   THR B 156     5792   7056   5551  -1689  -1566   1700       N  
ATOM   3187  CA  THR B 156      17.510   0.442 -23.261  1.00 49.69           C  
ANISOU 3187  CA  THR B 156     6031   7216   5631  -1825  -1765   1691       C  
ATOM   3188  C   THR B 156      16.840  -0.289 -22.101  1.00 48.90           C  
ANISOU 3188  C   THR B 156     6029   7137   5414  -1696  -1758   1612       C  
ATOM   3189  O   THR B 156      17.519  -0.836 -21.225  1.00 49.86           O  
ANISOU 3189  O   THR B 156     6071   7370   5504  -1732  -1861   1682       O  
ATOM   3190  CB  THR B 156      17.322   1.957 -23.072  1.00 72.71           C  
ANISOU 3190  CB  THR B 156     9190   9951   8487  -1980  -1899   1603       C  
ATOM   3191  OG1 THR B 156      17.933   2.654 -24.165  1.00 74.05           O  
ANISOU 3191  OG1 THR B 156     9270  10104   8764  -2133  -1917   1706       O  
ATOM   3192  CG2 THR B 156      17.957   2.415 -21.767  1.00 74.01           C  
ANISOU 3192  CG2 THR B 156     9465  10110   8546  -2131  -2119   1575       C  
ATOM   3193  N   ALA B 157      15.509  -0.299 -22.104  1.00 48.42           N  
ANISOU 3193  N   ALA B 157     6129   6978   5289  -1547  -1637   1481       N  
ATOM   3194  CA  ALA B 157      14.749  -0.948 -21.037  1.00 48.09           C  
ANISOU 3194  CA  ALA B 157     6185   6960   5125  -1430  -1600   1410       C  
ATOM   3195  C   ALA B 157      15.082  -2.435 -20.919  1.00 48.03           C  
ANISOU 3195  C   ALA B 157     5980   7099   5168  -1339  -1538   1527       C  
ATOM   3196  O   ALA B 157      15.363  -2.939 -19.824  1.00 48.75           O  
ANISOU 3196  O   ALA B 157     6089   7263   5168  -1344  -1613   1560       O  
ATOM   3197  CB  ALA B 157      13.257  -0.753 -21.255  1.00 29.43           C  
ANISOU 3197  CB  ALA B 157     3970   4490   2721  -1280  -1456   1271       C  
ATOM   3198  N   LEU B 158      15.057  -3.131 -22.052  1.00 50.20           N  
ANISOU 3198  N   LEU B 158     6086   7408   5581  -1255  -1406   1590       N  
ATOM   3199  CA  LEU B 158      15.361  -4.559 -22.076  1.00 50.74           C  
ANISOU 3199  CA  LEU B 158     5986   7578   5715  -1147  -1336   1690       C  
ATOM   3200  C   LEU B 158      16.785  -4.840 -21.599  1.00 52.57           C  
ANISOU 3200  C   LEU B 158     6051   7932   5991  -1232  -1477   1835       C  
ATOM   3201  O   LEU B 158      17.029  -5.827 -20.902  1.00 53.44           O  
ANISOU 3201  O   LEU B 158     6097   8115   6094  -1166  -1502   1913       O  
ATOM   3202  CB  LEU B 158      15.139  -5.138 -23.475  1.00 39.74           C  
ANISOU 3202  CB  LEU B 158     4476   6176   4447  -1041  -1169   1704       C  
ATOM   3203  CG  LEU B 158      13.693  -5.161 -23.976  1.00 38.20           C  
ANISOU 3203  CG  LEU B 158     4405   5884   4225   -940  -1037   1584       C  
ATOM   3204  CD1 LEU B 158      13.614  -5.794 -25.355  1.00 38.11           C  
ANISOU 3204  CD1 LEU B 158     4286   5873   4320   -853   -901   1601       C  
ATOM   3205  CD2 LEU B 158      12.791  -5.892 -22.991  1.00 38.27           C  
ANISOU 3205  CD2 LEU B 158     4499   5889   4151   -859  -1003   1547       C  
ATOM   3206  N   ASN B 159      17.719  -3.970 -21.972  1.00 46.30           N  
ANISOU 3206  N   ASN B 159     5181   7162   5249  -1383  -1577   1883       N  
ATOM   3207  CA  ASN B 159      19.094  -4.093 -21.495  1.00 48.36           C  
ANISOU 3207  CA  ASN B 159     5262   7555   5560  -1488  -1737   2027       C  
ATOM   3208  C   ASN B 159      19.204  -3.902 -19.984  1.00 48.76           C  
ANISOU 3208  C   ASN B 159     5449   7620   5457  -1572  -1931   2014       C  
ATOM   3209  O   ASN B 159      19.999  -4.573 -19.322  1.00 50.08           O  
ANISOU 3209  O   ASN B 159     5484   7906   5637  -1572  -2042   2138       O  
ATOM   3210  CB  ASN B 159      20.021  -3.118 -22.224  1.00 55.98           C  
ANISOU 3210  CB  ASN B 159     6113   8544   6611  -1666  -1805   2087       C  
ATOM   3211  CG  ASN B 159      20.432  -3.619 -23.592  1.00 56.78           C  
ANISOU 3211  CG  ASN B 159     5987   8717   6868  -1586  -1632   2169       C  
ATOM   3212  OD1 ASN B 159      20.288  -2.917 -24.590  1.00 56.57           O  
ANISOU 3212  OD1 ASN B 159     5975   8643   6875  -1654  -1563   2152       O  
ATOM   3213  ND2 ASN B 159      20.951  -4.839 -23.645  1.00 58.00           N  
ANISOU 3213  ND2 ASN B 159     5945   8982   7110  -1434  -1558   2261       N  
ATOM   3214  N   VAL B 160      18.401  -2.986 -19.446  1.00 61.42           N  
ANISOU 3214  N   VAL B 160     7325   9103   6909  -1631  -1971   1865       N  
ATOM   3215  CA  VAL B 160      18.373  -2.747 -18.005  1.00 62.05           C  
ANISOU 3215  CA  VAL B 160     7587   9188   6799  -1703  -2137   1822       C  
ATOM   3216  C   VAL B 160      17.842  -3.968 -17.258  1.00 61.81           C  
ANISOU 3216  C   VAL B 160     7577   9217   6689  -1546  -2063   1851       C  
ATOM   3217  O   VAL B 160      18.433  -4.408 -16.267  1.00 63.00           O  
ANISOU 3217  O   VAL B 160     7710   9466   6761  -1585  -2212   1942       O  
ATOM   3218  CB  VAL B 160      17.528  -1.505 -17.647  1.00 41.78           C  
ANISOU 3218  CB  VAL B 160     5331   6462   4081  -1765  -2161   1629       C  
ATOM   3219  CG1 VAL B 160      17.307  -1.422 -16.144  1.00 43.70           C  
ANISOU 3219  CG1 VAL B 160     5796   6717   4090  -1790  -2276   1558       C  
ATOM   3220  CG2 VAL B 160      18.203  -0.242 -18.157  1.00 42.97           C  
ANISOU 3220  CG2 VAL B 160     5497   6538   4292  -1967  -2298   1621       C  
ATOM   3221  N   VAL B 161      16.730  -4.518 -17.741  1.00 48.54           N  
ANISOU 3221  N   VAL B 161     5934   7478   5031  -1382  -1846   1787       N  
ATOM   3222  CA  VAL B 161      16.162  -5.720 -17.134  1.00 48.54           C  
ANISOU 3222  CA  VAL B 161     5953   7517   4970  -1248  -1759   1826       C  
ATOM   3223  C   VAL B 161      17.149  -6.885 -17.208  1.00 49.71           C  
ANISOU 3223  C   VAL B 161     5870   7771   5246  -1194  -1801   2016       C  
ATOM   3224  O   VAL B 161      17.333  -7.627 -16.235  1.00 50.63           O  
ANISOU 3224  O   VAL B 161     6007   7951   5276  -1172  -1879   2107       O  
ATOM   3225  CB  VAL B 161      14.834  -6.124 -17.803  1.00 36.88           C  
ANISOU 3225  CB  VAL B 161     4522   5960   3531  -1103  -1525   1736       C  
ATOM   3226  CG1 VAL B 161      14.290  -7.398 -17.175  1.00 37.03           C  
ANISOU 3226  CG1 VAL B 161     4554   6015   3501   -995  -1442   1799       C  
ATOM   3227  CG2 VAL B 161      13.821  -4.998 -17.684  1.00 35.79           C  
ANISOU 3227  CG2 VAL B 161     4598   5723   3279  -1121  -1480   1556       C  
ATOM   3228  N   SER B 162      17.790  -7.029 -18.364  1.00 37.72           N  
ANISOU 3228  N   SER B 162     4136   6271   3926  -1164  -1747   2079       N  
ATOM   3229  CA  SER B 162      18.792  -8.070 -18.564  1.00 39.04           C  
ANISOU 3229  CA  SER B 162     4066   6529   4237  -1079  -1767   2249       C  
ATOM   3230  C   SER B 162      19.954  -7.929 -17.584  1.00 42.85           C  
ANISOU 3230  C   SER B 162     4452   7135   4693  -1195  -2014   2380       C  
ATOM   3231  O   SER B 162      20.427  -8.920 -17.026  1.00 44.84           O  
ANISOU 3231  O   SER B 162     4588   7463   4987  -1116  -2083   2527       O  
ATOM   3232  CB  SER B 162      19.312  -8.046 -20.002  1.00 40.35           C  
ANISOU 3232  CB  SER B 162     4030   6699   4600  -1017  -1634   2270       C  
ATOM   3233  OG  SER B 162      18.284  -8.373 -20.921  1.00 40.81           O  
ANISOU 3233  OG  SER B 162     4033   6783   4687  -1174  -1705   2255       O  
ATOM   3234  N   LEU B 163      20.411  -6.697 -17.378  1.00 54.47           N  
ANISOU 3234  N   LEU B 163     5979   8618   6099  -1387  -2163   2332       N  
ATOM   3235  CA  LEU B 163      21.479  -6.434 -16.416  1.00 56.14           C  
ANISOU 3235  CA  LEU B 163     6121   8945   6264  -1537  -2433   2443       C  
ATOM   3236  C   LEU B 163      21.029  -6.736 -14.989  1.00 57.47           C  
ANISOU 3236  C   LEU B 163     6502   9125   6208  -1542  -2552   2440       C  
ATOM   3237  O   LEU B 163      21.825  -7.178 -14.156  1.00 60.63           O  
ANISOU 3237  O   LEU B 163     6809   9640   6586  -1568  -2742   2590       O  
ATOM   3238  CB  LEU B 163      21.975  -4.990 -16.528  1.00 49.45           C  
ANISOU 3238  CB  LEU B 163     5319   8076   5394  -1768  -2571   2378       C  
ATOM   3239  CG  LEU B 163      23.041  -4.725 -17.593  1.00 50.31           C  
ANISOU 3239  CG  LEU B 163     5126   8266   5722  -1842  -2575   2488       C  
ATOM   3240  CD1 LEU B 163      23.398  -3.248 -17.639  1.00 51.67           C  
ANISOU 3240  CD1 LEU B 163     5388   8383   5859  -2099  -2716   2424       C  
ATOM   3241  CD2 LEU B 163      24.277  -5.571 -17.328  1.00 53.89           C  
ANISOU 3241  CD2 LEU B 163     5272   8905   6298  -1822  -2714   2703       C  
ATOM   3242  N   SER B 164      19.749  -6.497 -14.713  1.00 64.48           N  
ANISOU 3242  N   SER B 164     7668   9906   6924  -1511  -2436   2279       N  
ATOM   3243  CA  SER B 164      19.180  -6.825 -13.411  1.00 64.81           C  
ANISOU 3243  CA  SER B 164     7931   9967   6728  -1502  -2496   2268       C  
ATOM   3244  C   SER B 164      19.232  -8.331 -13.177  1.00 65.32           C  
ANISOU 3244  C   SER B 164     7884  10084   6849  -1343  -2441   2432       C  
ATOM   3245  O   SER B 164      19.634  -8.791 -12.105  1.00 66.55           O  
ANISOU 3245  O   SER B 164     8073  10327   6887  -1365  -2605   2555       O  
ATOM   3246  CB  SER B 164      17.740  -6.319 -13.306  1.00 57.24           C  
ANISOU 3246  CB  SER B 164     7251   8895   5604  -1469  -2328   2063       C  
ATOM   3247  OG  SER B 164      17.677  -4.915 -13.485  1.00 57.07           O  
ANISOU 3247  OG  SER B 164     7358   8793   5535  -1598  -2386   1908       O  
ATOM   3248  N   VAL B 165      18.832  -9.091 -14.193  1.00 52.46           N  
ANISOU 3248  N   VAL B 165     6143   8393   5399  -1187  -2220   2436       N  
ATOM   3249  CA  VAL B 165      18.870 -10.548 -14.121  1.00 52.93           C  
ANISOU 3249  CA  VAL B 165     6112   8458   5543  -1028  -2153   2582       C  
ATOM   3250  C   VAL B 165      20.299 -11.059 -13.937  1.00 55.55           C  
ANISOU 3250  C   VAL B 165     6205   8898   6003  -1008  -2339   2788       C  
ATOM   3251  O   VAL B 165      20.561 -11.905 -13.078  1.00 57.80           O  
ANISOU 3251  O   VAL B 165     6506   9228   6228   -962  -2447   2937       O  
ATOM   3252  CB  VAL B 165      18.260 -11.190 -15.383  1.00 52.93           C  
ANISOU 3252  CB  VAL B 165     6032   8354   5726   -881  -1900   2530       C  
ATOM   3253  CG1 VAL B 165      18.423 -12.702 -15.344  1.00 53.74           C  
ANISOU 3253  CG1 VAL B 165     6037   8435   5947   -720  -1856   2685       C  
ATOM   3254  CG2 VAL B 165      16.794 -10.811 -15.514  1.00 50.47           C  
ANISOU 3254  CG2 VAL B 165     5931   7949   5297   -881  -1726   2355       C  
ATOM   3255  N   GLU B 166      21.217 -10.535 -14.745  1.00 55.19           N  
ANISOU 3255  N   GLU B 166     5931   8903   6136  -1043  -2376   2810       N  
ATOM   3256  CA  GLU B 166      22.620 -10.933 -14.683  1.00 58.22           C  
ANISOU 3256  CA  GLU B 166     6034   9410   6678  -1008  -2534   3009       C  
ATOM   3257  C   GLU B 166      23.220 -10.665 -13.307  1.00 62.00           C  
ANISOU 3257  C   GLU B 166     6543  10011   7004  -1161  -2845   3112       C  
ATOM   3258  O   GLU B 166      23.907 -11.518 -12.742  1.00 65.02           O  
ANISOU 3258  O   GLU B 166     6765  10487   7452  -1095  -2999   3308       O  
ATOM   3259  CB  GLU B 166      23.437 -10.206 -15.755  1.00 74.40           C  
ANISOU 3259  CB  GLU B 166     7816  11509   8943  -1026  -2479   3010       C  
ATOM   3260  CG  GLU B 166      23.127 -10.621 -17.187  1.00 74.31           C  
ANISOU 3260  CG  GLU B 166     7705  11415   9113   -828  -2205   2973       C  
ATOM   3261  CD  GLU B 166      23.857 -11.881 -17.613  1.00 76.04           C  
ANISOU 3261  CD  GLU B 166     7574  11745   9572   -752  -2184   3090       C  
ATOM   3262  OE1 GLU B 166      24.226 -12.693 -16.738  1.00 77.32           O  
ANISOU 3262  OE1 GLU B 166     7539  12057   9780   -845  -2392   3227       O  
ATOM   3263  OE2 GLU B 166      24.068 -12.055 -18.832  1.00 76.28           O  
ANISOU 3263  OE2 GLU B 166     7522  11720   9738   -599  -1959   3046       O  
ATOM   3264  N   LEU B 167      22.956  -9.477 -12.771  1.00 58.74           N  
ANISOU 3264  N   LEU B 167     6346   9589   6385  -1360  -2947   2978       N  
ATOM   3265  CA  LEU B 167      23.473  -9.103 -11.461  1.00 63.14           C  
ANISOU 3265  CA  LEU B 167     6987  10251   6755  -1527  -3255   3047       C  
ATOM   3266  C   LEU B 167      22.865  -9.973 -10.364  1.00 64.44           C  
ANISOU 3266  C   LEU B 167     7353  10416   6717  -1445  -3284   3116       C  
ATOM   3267  O   LEU B 167      23.551 -10.361  -9.416  1.00 68.62           O  
ANISOU 3267  O   LEU B 167     7839  11057   7177  -1476  -3527   3286       O  
ATOM   3268  CB  LEU B 167      23.202  -7.624 -11.176  1.00 63.27           C  
ANISOU 3268  CB  LEU B 167     7227  10224   6589  -1754  -3347   2858       C  
ATOM   3269  CG  LEU B 167      23.833  -7.069  -9.897  1.00 68.31           C  
ANISOU 3269  CG  LEU B 167     7886  10973   7096  -1986  -3706   2915       C  
ATOM   3270  CD1 LEU B 167      25.344  -7.244  -9.924  1.00 71.26           C  
ANISOU 3270  CD1 LEU B 167     8513  11394   7169  -2008  -3865   2948       C  
ATOM   3271  CD2 LEU B 167      23.464  -5.610  -9.705  1.00 68.13           C  
ANISOU 3271  CD2 LEU B 167     8011  10869   7005  -2204  -3766   2729       C  
ATOM   3272  N   TYR B 168      21.577 -10.278 -10.501  1.00 61.16           N  
ANISOU 3272  N   TYR B 168     7149   9882   6205  -1349  -3042   2997       N  
ATOM   3273  CA  TYR B 168      20.898 -11.149  -9.548  1.00 62.26           C  
ANISOU 3273  CA  TYR B 168     7479  10019   6159  -1276  -3023   3073       C  
ATOM   3274  C   TYR B 168      21.536 -12.534  -9.521  1.00 64.07           C  
ANISOU 3274  C   TYR B 168     7500  10278   6567  -1115  -3072   3319       C  
ATOM   3275  O   TYR B 168      21.841 -13.065  -8.454  1.00 67.75           O  
ANISOU 3275  O   TYR B 168     8026  10816   6900  -1119  -3254   3486       O  
ATOM   3276  CB  TYR B 168      19.409 -11.267  -9.884  1.00 69.37           C  
ANISOU 3276  CB  TYR B 168     8574  10794   6989  -1197  -2723   2917       C  
ATOM   3277  CG  TYR B 168      18.674 -12.282  -9.036  1.00 70.02           C  
ANISOU 3277  CG  TYR B 168     8824  10869   6912  -1123  -2658   3015       C  
ATOM   3278  CD1 TYR B 168      18.142 -11.930  -7.803  1.00 70.55           C  
ANISOU 3278  CD1 TYR B 168     9176  10989   6640  -1221  -2708   2967       C  
ATOM   3279  CD2 TYR B 168      18.514 -13.595  -9.468  1.00 70.37           C  
ANISOU 3279  CD2 TYR B 168     8756  10846   7135   -961  -2539   3156       C  
ATOM   3280  CE1 TYR B 168      17.471 -12.853  -7.025  1.00 71.54           C  
ANISOU 3280  CE1 TYR B 168     9453  11121   6608  -1170  -2635   3076       C  
ATOM   3281  CE2 TYR B 168      17.850 -14.525  -8.695  1.00 71.14           C  
ANISOU 3281  CE2 TYR B 168     9013  10925   7093   -917  -2484   3266       C  
ATOM   3282  CZ  TYR B 168      17.328 -14.148  -7.476  1.00 71.59           C  
ANISOU 3282  CZ  TYR B 168     9336  11056   6811  -1027  -2527   3234       C  
ATOM   3283  OH  TYR B 168      16.662 -15.072  -6.703  1.00 72.56           O  
ANISOU 3283  OH  TYR B 168     9614  11173   6782   -998  -2459   3362       O  
ATOM   3284  N   LEU B 169      21.728 -13.115 -10.700  1.00 73.53           N  
ANISOU 3284  N   LEU B 169     8466  11413   8057   -966  -2910   3340       N  
ATOM   3285  CA  LEU B 169      22.314 -14.447 -10.808  1.00 75.18           C  
ANISOU 3285  CA  LEU B 169     8474  11620   8471   -778  -2932   3552       C  
ATOM   3286  C   LEU B 169      23.774 -14.455 -10.370  1.00 79.72           C  
ANISOU 3286  C   LEU B 169     8823  12355   9110   -816  -3236   3744       C  
ATOM   3287  O   LEU B 169      24.286 -15.475  -9.906  1.00 82.87           O  
ANISOU 3287  O   LEU B 169     9150  12783   9553   -702  -3365   3957       O  
ATOM   3288  CB  LEU B 169      22.189 -14.974 -12.238  1.00 60.05           C  
ANISOU 3288  CB  LEU B 169     6371   9605   6839   -614  -2689   3497       C  
ATOM   3289  CG  LEU B 169      20.755 -15.175 -12.726  1.00 56.05           C  
ANISOU 3289  CG  LEU B 169     6046   8931   6318   -535  -2409   3363       C  
ATOM   3290  CD1 LEU B 169      20.734 -15.652 -14.168  1.00 53.38           C  
ANISOU 3290  CD1 LEU B 169     5528   8507   6247   -381  -2205   3310       C  
ATOM   3291  CD2 LEU B 169      20.018 -16.150 -11.821  1.00 57.48           C  
ANISOU 3291  CD2 LEU B 169     6398   9044   6400   -462  -2408   3491       C  
ATOM   3292  N   ALA B 170      24.439 -13.315 -10.518  1.00 68.99           N  
ANISOU 3292  N   ALA B 170     7350  11097   7766   -982  -3359   3679       N  
ATOM   3293  CA  ALA B 170      25.835 -13.195 -10.121  1.00 73.83           C  
ANISOU 3293  CA  ALA B 170     7716  11883   8453  -1057  -3663   3855       C  
ATOM   3294  C   ALA B 170      25.971 -13.071  -8.607  1.00 78.15           C  
ANISOU 3294  C   ALA B 170     8454  12518   8720  -1183  -3961   3958       C  
ATOM   3295  O   ALA B 170      26.955 -13.527  -8.027  1.00 82.70           O  
ANISOU 3295  O   ALA B 170     8854  13212   9354  -1145  -4205   4185       O  
ATOM   3296  CB  ALA B 170      26.486 -12.007 -10.812  1.00 73.70           C  
ANISOU 3296  CB  ALA B 170     7549  11939   8516  -1242  -3713   3755       C  
ATOM   3297  N   ILE B 171      24.979 -12.456  -7.969  1.00 79.88           N  
ANISOU 3297  N   ILE B 171     9034  12687   8630  -1325  -3939   3792       N  
ATOM   3298  CA  ILE B 171      25.035 -12.228  -6.527  1.00 84.07           C  
ANISOU 3298  CA  ILE B 171     9799  13306   8839  -1465  -4207   3855       C  
ATOM   3299  C   ILE B 171      24.443 -13.387  -5.717  1.00 85.28           C  
ANISOU 3299  C   ILE B 171    10101  13429   8874  -1317  -4178   4014       C  
ATOM   3300  O   ILE B 171      24.852 -13.632  -4.581  1.00 90.10           O  
ANISOU 3300  O   ILE B 171    10743  14146   9344  -1353  -4452   4204       O  
ATOM   3301  CB  ILE B 171      24.366 -10.884  -6.133  1.00 82.96           C  
ANISOU 3301  CB  ILE B 171    10000  13132   8388  -1677  -4206   3602       C  
ATOM   3302  CG1 ILE B 171      24.752 -10.480  -4.709  1.00 88.07           C  
ANISOU 3302  CG1 ILE B 171    10886  13890   8685  -1835  -4514   3663       C  
ATOM   3303  CG2 ILE B 171      22.854 -10.955  -6.283  1.00 78.26           C  
ANISOU 3303  CG2 ILE B 171     9648  12386   7700  -1584  -3854   3414       C  
ATOM   3304  CD1 ILE B 171      24.199  -9.138  -4.291  1.00 88.01           C  
ANISOU 3304  CD1 ILE B 171    11225  13848   8367  -2034  -4534   3404       C  
ATOM   3305  N   CYS B 172      23.492 -14.107  -6.306  1.00 84.62           N  
ANISOU 3305  N   CYS B 172    10108  13197   8849  -1164  -3860   3950       N  
ATOM   3306  CA  CYS B 172      22.886 -15.254  -5.636  1.00 85.76           C  
ANISOU 3306  CA  CYS B 172    10408  13290   8889  -1045  -3811   4104       C  
ATOM   3307  C   CYS B 172      23.756 -16.498  -5.763  1.00 88.61           C  
ANISOU 3307  C   CYS B 172    10510  13657   9501   -859  -3936   4383       C  
ATOM   3308  O   CYS B 172      23.680 -17.408  -4.937  1.00 92.53           O  
ANISOU 3308  O   CYS B 172    11098  14190   9868   -831  -4109   4596       O  
ATOM   3309  CB  CYS B 172      21.484 -15.528  -6.182  1.00 80.56           C  
ANISOU 3309  CB  CYS B 172     9905  12468   8236   -959  -3448   3962       C  
ATOM   3310  SG  CYS B 172      20.219 -14.399  -5.565  1.00 78.69           S  
ANISOU 3310  SG  CYS B 172    10000  12223   7675  -1131  -3289   3664       S  
ATOM   3311  N   HIS B 173      24.583 -16.531  -6.802  1.00 97.39           N  
ANISOU 3311  N   HIS B 173    11305  14733  10965   -722  -3844   4386       N  
ATOM   3312  CA  HIS B 173      25.524 -17.626  -6.997  1.00 99.87           C  
ANISOU 3312  CA  HIS B 173    11359  15042  11544   -506  -3937   4633       C  
ATOM   3313  C   HIS B 173      26.929 -17.066  -7.200  1.00101.65           C  
ANISOU 3313  C   HIS B 173    11197  15416  12009   -503  -4100   4693       C  
ATOM   3314  O   HIS B 173      27.485 -17.163  -8.290  1.00100.80           O  
ANISOU 3314  O   HIS B 173    10829  15263  12208   -332  -3938   4684       O  
ATOM   3315  CB  HIS B 173      25.112 -18.469  -8.204  1.00121.11           C  
ANISOU 3315  CB  HIS B 173    14024  17529  14465   -280  -3624   4598       C  
ATOM   3316  CG  HIS B 173      23.662 -18.842  -8.211  1.00120.01           C  
ANISOU 3316  CG  HIS B 173    14224  17243  14131   -310  -3417   4508       C  
ATOM   3317  ND1 HIS B 173      23.181 -19.979  -7.597  1.00117.07           N  
ANISOU 3317  ND1 HIS B 173    13908  16721  13854   -261  -3102   4316       N  
ATOM   3318  CD2 HIS B 173      22.586 -18.227  -8.758  1.00121.63           C  
ANISOU 3318  CD2 HIS B 173    14719  17447  14050   -392  -3479   4593       C  
ATOM   3319  CE1 HIS B 173      21.873 -20.049  -7.766  1.00116.95           C  
ANISOU 3319  CE1 HIS B 173    14178  16620  13638   -314  -2981   4290       C  
ATOM   3320  NE2 HIS B 173      21.486 -18.998  -8.466  1.00119.71           N  
ANISOU 3320  NE2 HIS B 173    14675  17059  13750   -393  -3192   4457       N  
ATOM   3321  N   PRO B 174      27.512 -16.488  -6.137  1.00150.30           N  
ANISOU 3321  N   PRO B 174    17316  21764  18029   -694  -4426   4765       N  
ATOM   3322  CA  PRO B 174      28.763 -15.725  -6.224  1.00152.53           C  
ANISOU 3322  CA  PRO B 174    17227  22213  18514   -761  -4596   4812       C  
ATOM   3323  C   PRO B 174      29.962 -16.558  -6.670  1.00154.94           C  
ANISOU 3323  C   PRO B 174    17129  22556  19186   -494  -4610   5026       C  
ATOM   3324  O   PRO B 174      30.954 -15.998  -7.138  1.00155.09           O  
ANISOU 3324  O   PRO B 174    16808  22661  19458   -470  -4558   5011       O  
ATOM   3325  CB  PRO B 174      28.978 -15.238  -4.784  1.00101.59           C  
ANISOU 3325  CB  PRO B 174    10878  15903  11817   -991  -4947   4861       C  
ATOM   3326  CG  PRO B 174      27.650 -15.382  -4.113  1.00100.89           C  
ANISOU 3326  CG  PRO B 174    11248  15743  11342  -1091  -4934   4782       C  
ATOM   3327  CD  PRO B 174      27.025 -16.575  -4.751  1.00 98.16           C  
ANISOU 3327  CD  PRO B 174    11016  15229  11051   -865  -4664   4822       C  
ATOM   3328  N   PHE B 175      29.874 -17.875  -6.525  1.00133.98           N  
ANISOU 3328  N   PHE B 175    14528  19819  16557   -291  -4647   5204       N  
ATOM   3329  CA  PHE B 175      30.985 -18.753  -6.877  1.00136.16           C  
ANISOU 3329  CA  PHE B 175    14478  20082  17173     -1  -4630   5371       C  
ATOM   3330  C   PHE B 175      30.845 -19.317  -8.287  1.00135.48           C  
ANISOU 3330  C   PHE B 175    14328  19826  17322    266  -4314   5341       C  
ATOM   3331  O   PHE B 175      31.692 -19.077  -9.148  1.00136.85           O  
ANISOU 3331  O   PHE B 175    14159  20023  17813    480  -4223   5395       O  
ATOM   3332  CB  PHE B 175      31.102 -19.898  -5.868  1.00149.50           C  
ANISOU 3332  CB  PHE B 175    16278  21735  18790     91  -4821   5549       C  
ATOM   3333  CG  PHE B 175      31.298 -19.440  -4.454  1.00150.28           C  
ANISOU 3333  CG  PHE B 175    16432  21994  18672   -154  -5122   5560       C  
ATOM   3334  CD1 PHE B 175      32.567 -19.183  -3.965  1.00150.81           C  
ANISOU 3334  CD1 PHE B 175    16785  22032  18484   -194  -5290   5653       C  
ATOM   3335  CD2 PHE B 175      30.212 -19.265  -3.612  1.00150.51           C  
ANISOU 3335  CD2 PHE B 175    16247  22198  18740   -358  -5234   5475       C  
ATOM   3336  CE1 PHE B 175      32.751 -18.760  -2.662  1.00151.67           C  
ANISOU 3336  CE1 PHE B 175    16962  22285  18379   -416  -5569   5654       C  
ATOM   3337  CE2 PHE B 175      30.389 -18.843  -2.309  1.00151.41           C  
ANISOU 3337  CE2 PHE B 175    16432  22441  18656   -593  -5520   5478       C  
ATOM   3338  CZ  PHE B 175      31.660 -18.590  -1.833  1.00151.97           C  
ANISOU 3338  CZ  PHE B 175    16789  22484  18468   -616  -5690   5562       C  
ATOM   3339  N   LYS B 176      29.773 -20.067  -8.516  1.00169.46           N  
ANISOU 3339  N   LYS B 176    18996  23931  21461    244  -4092   5190       N  
ATOM   3340  CA  LYS B 176      29.574 -20.734  -9.797  1.00168.77           C  
ANISOU 3340  CA  LYS B 176    18950  23625  21553    451  -3744   5069       C  
ATOM   3341  C   LYS B 176      28.483 -20.094 -10.645  1.00167.03           C  
ANISOU 3341  C   LYS B 176    18635  23424  21406    368  -3502   4811       C  
ATOM   3342  O   LYS B 176      27.614 -20.785 -11.178  1.00166.91           O  
ANISOU 3342  O   LYS B 176    18521  23295  21602    554  -3244   4721       O  
ATOM   3343  CB  LYS B 176      29.273 -22.218  -9.591  1.00177.24           C  
ATOM   3344  CG  LYS B 176      30.457 -23.018  -9.082  1.00177.24           C  
ATOM   3345  CD  LYS B 176      30.126 -24.495  -8.996  1.00177.24           C  
ATOM   3346  CE  LYS B 176      31.333 -25.301  -8.552  1.00177.24           C  
ATOM   3347  NZ  LYS B 176      31.020 -26.751  -8.451  1.00177.24           N  
ATOM   3348  N   ALA B 177      28.527 -18.774 -10.766  1.00182.54           N  
ANISOU 3348  N   ALA B 177    20647  25526  23184     87  -3597   4697       N  
ATOM   3349  CA  ALA B 177      27.668 -18.088 -11.714  1.00180.88           C  
ANISOU 3349  CA  ALA B 177    20382  25331  23013    -25  -3397   4467       C  
ATOM   3350  C   ALA B 177      28.309 -18.190 -13.085  1.00182.05           C  
ANISOU 3350  C   ALA B 177    20105  25624  23442     49  -3384   4517       C  
ATOM   3351  O   ALA B 177      27.613 -18.185 -14.102  1.00180.57           O  
ANISOU 3351  O   ALA B 177    19854  25461  23294    -48  -3225   4354       O  
ATOM   3352  CB  ALA B 177      27.494 -16.630 -11.327  1.00155.89           C  
ANISOU 3352  CB  ALA B 177    17432  22235  19563   -343  -3507   4327       C  
ATOM   3353  N   LYS B 178      29.637 -18.316 -13.090  1.00183.11           N  
ANISOU 3353  N   LYS B 178    19941  25861  23771    224  -3542   4749       N  
ATOM   3354  CA  LYS B 178      30.442 -18.123 -14.290  1.00184.56           C  
ANISOU 3354  CA  LYS B 178    19689  26202  24235    315  -3491   4802       C  
ATOM   3355  C   LYS B 178      29.951 -16.833 -14.911  1.00184.46           C  
ANISOU 3355  C   LYS B 178    19631  26053  24405    540  -3112   4659       C  
ATOM   3356  O   LYS B 178      30.223 -15.736 -14.420  1.00184.77           O  
ANISOU 3356  O   LYS B 178    19398  26207  24601    547  -2975   4612       O  
ATOM   3357  CB  LYS B 178      30.251 -19.273 -15.284  1.00122.23           C  
ATOM   3358  CG  LYS B 178      30.437 -20.667 -14.711  1.00122.23           C  
ATOM   3359  CD  LYS B 178      30.103 -21.718 -15.763  1.00122.23           C  
ATOM   3360  CE  LYS B 178      30.268 -23.131 -15.228  1.00122.23           C  
ATOM   3361  NZ  LYS B 178      29.904 -24.146 -16.255  1.00122.23           N  
ATOM   3362  N   THR B 179      29.210 -16.990 -15.999  1.00210.20           N  
ANISOU 3362  N   THR B 179    23158  29070  27638    714  -2947   4598       N  
ATOM   3363  CA  THR B 179      28.302 -15.965 -16.480  1.00209.35           C  
ANISOU 3363  CA  THR B 179    23077  28808  27658    897  -2601   4431       C  
ATOM   3364  C   THR B 179      27.204 -16.702 -17.234  1.00207.11           C  
ANISOU 3364  C   THR B 179    22900  28540  27253    669  -2433   4197       C  
ATOM   3365  O   THR B 179      27.427 -17.805 -17.738  1.00207.26           O  
ANISOU 3365  O   THR B 179    22706  28642  27403    701  -2263   4126       O  
ATOM   3366  CB  THR B 179      28.991 -14.919 -17.373  1.00108.92           C  
ANISOU 3366  CB  THR B 179    10685  15807  14894   1051  -2489   4395       C  
ATOM   3367  OG1 THR B 179      30.269 -14.578 -16.821  1.00111.34           O  
ANISOU 3367  OG1 THR B 179    10892  16065  15349   1301  -2622   4618       O  
ATOM   3368  CG2 THR B 179      28.138 -13.666 -17.447  1.00108.07           C  
ANISOU 3368  CG2 THR B 179    10656  15532  14876   1186  -2150   4188       C  
ATOM   3369  N   LEU B 180      26.023 -16.099 -17.288  1.00108.64           N  
ANISOU 3369  N   LEU B 180    10759  15992  14526    447  -2483   4089       N  
ATOM   3370  CA  LEU B 180      24.821 -16.758 -17.786  1.00105.47           C  
ANISOU 3370  CA  LEU B 180    10502  15595  13977    209  -2384   3883       C  
ATOM   3371  C   LEU B 180      24.996 -17.419 -19.148  1.00103.18           C  
ANISOU 3371  C   LEU B 180    10157  15243  13801    297  -2078   3718       C  
ATOM   3372  O   LEU B 180      24.416 -18.470 -19.418  1.00102.10           O  
ANISOU 3372  O   LEU B 180     9966  15192  13636    128  -2027   3620       O  
ATOM   3373  CB  LEU B 180      23.671 -15.754 -17.840  1.00 74.23           C  
ANISOU 3373  CB  LEU B 180     6390  11850   9961    -47  -2609   3934       C  
ATOM   3374  CG  LEU B 180      22.275 -16.324 -18.082  1.00 71.37           C  
ANISOU 3374  CG  LEU B 180     6265  11472   9379   -337  -2624   3755       C  
ATOM   3375  CD1 LEU B 180      21.999 -17.461 -17.112  1.00 72.79           C  
ANISOU 3375  CD1 LEU B 180     6208  11817   9632   -523  -2685   3757       C  
ATOM   3376  CD2 LEU B 180      21.254 -15.220 -17.920  1.00 72.68           C  
ANISOU 3376  CD2 LEU B 180     6693  11630   9291   -493  -2857   3780       C  
ATOM   3377  N   MET B 181      25.808 -16.807 -20.001  1.00 95.54           N  
ANISOU 3377  N   MET B 181     9243  14114  12945    546  -1884   3684       N  
ATOM   3378  CA  MET B 181      25.986 -17.308 -21.354  1.00 95.66           C  
ANISOU 3378  CA  MET B 181     9232  14060  13054    656  -1594   3527       C  
ATOM   3379  C   MET B 181      27.439 -17.272 -21.789  1.00 96.58           C  
ANISOU 3379  C   MET B 181     9006  14372  13320    679  -1508   3549       C  
ATOM   3380  O   MET B 181      28.300 -16.694 -21.122  1.00 95.90           O  
ANISOU 3380  O   MET B 181     8764  14470  13205    472  -1642   3604       O  
ATOM   3381  CB  MET B 181      25.192 -16.459 -22.343  1.00 88.23           C  
ANISOU 3381  CB  MET B 181     8590  13003  11930    482  -1477   3316       C  
ATOM   3382  CG  MET B 181      23.700 -16.418 -22.124  1.00 87.38           C  
ANISOU 3382  CG  MET B 181     8804  12714  11683    464  -1508   3284       C  
ATOM   3383  SD  MET B 181      22.996 -14.940 -22.877  1.00 86.55           S  
ANISOU 3383  SD  MET B 181     8832  12691  11365    243  -1795   3387       S  
ATOM   3384  CE  MET B 181      21.344 -15.511 -23.252  1.00 84.99           C  
ANISOU 3384  CE  MET B 181     8690  12588  11015    -37  -1798   3225       C  
ATOM   3385  N   SER B 182      27.696 -17.896 -22.932  1.00116.55           N  
ANISOU 3385  N   SER B 182    11425  16855  16003    927  -1279   3506       N  
ATOM   3386  CA  SER B 182      28.965 -17.741 -23.613  1.00117.82           C  
ANISOU 3386  CA  SER B 182    11235  17212  16317    999  -1156   3546       C  
ATOM   3387  C   SER B 182      28.942 -16.377 -24.284  1.00116.26           C  
ANISOU 3387  C   SER B 182    11015  17139  16017    724  -1107   3459       C  
ATOM   3388  O   SER B 182      27.886 -15.751 -24.392  1.00114.23           O  
ANISOU 3388  O   SER B 182    11048  16760  15592    564  -1062   3301       O  
ATOM   3389  CB  SER B 182      29.149 -18.845 -24.654  1.00135.08           C  
ANISOU 3389  CB  SER B 182    13403  19291  18631   1313   -873   3457       C  
ATOM   3390  OG  SER B 182      29.072 -20.129 -24.057  1.00138.05           O  
ANISOU 3390  OG  SER B 182    13751  19558  19146   1594   -922   3563       O  
ATOM   3391  N   ARG B 183      30.103 -15.913 -24.730  1.00138.04           N  
ANISOU 3391  N   ARG B 183    13419  20140  18888    667  -1123   3575       N  
ATOM   3392  CA  ARG B 183      30.199 -14.602 -25.360  1.00136.88           C  
ANISOU 3392  CA  ARG B 183    13226  20117  18666    389  -1095   3530       C  
ATOM   3393  C   ARG B 183      29.363 -14.532 -26.637  1.00136.09           C  
ANISOU 3393  C   ARG B 183    13303  19912  18493    425   -802   3337       C  
ATOM   3394  O   ARG B 183      28.685 -13.533 -26.895  1.00134.49           O  
ANISOU 3394  O   ARG B 183    13264  19683  18152    190   -793   3240       O  
ATOM   3395  CB  ARG B 183      31.661 -14.251 -25.643  1.00146.25           C  
ANISOU 3395  CB  ARG B 183    13955  21590  20021    353  -1126   3711       C  
ATOM   3396  CG  ARG B 183      32.513 -14.155 -24.386  1.00147.05           C  
ANISOU 3396  CG  ARG B 183    13858  21832  20180    242  -1462   3913       C  
ATOM   3397  CD  ARG B 183      33.948 -13.770 -24.705  1.00149.20           C  
ANISOU 3397  CD  ARG B 183    13619  22400  20668    268  -1464   4109       C  
ATOM   3398  NE  ARG B 183      34.755 -13.666 -23.492  1.00149.59           N  
ANISOU 3398  NE  ARG B 183    13503  22623  20711    -50  -1782   4257       N  
ATOM   3399  CZ  ARG B 183      36.045 -13.344 -23.472  1.00151.04           C  
ANISOU 3399  CZ  ARG B 183    13266  23077  21043   -174  -1816   4417       C  
ATOM   3400  NH1 ARG B 183      36.687 -13.090 -24.605  1.00152.15           N  
ANISOU 3400  NH1 ARG B 183    13101  23363  21345     10  -1525   4452       N  
ATOM   3401  NH2 ARG B 183      36.694 -13.275 -22.317  1.00151.52           N  
ANISOU 3401  NH2 ARG B 183    13214  23268  21086   -491  -2139   4541       N  
ATOM   3402  N   SER B 184      29.402 -15.606 -27.420  1.00138.57           N  
ANISOU 3402  N   SER B 184    13600  20156  18896    727   -576   3281       N  
ATOM   3403  CA  SER B 184      28.614 -15.698 -28.644  1.00138.02           C  
ANISOU 3403  CA  SER B 184    13723  19976  18743    789   -309   3091       C  
ATOM   3404  C   SER B 184      27.119 -15.650 -28.340  1.00136.14           C  
ANISOU 3404  C   SER B 184    13900  19498  18330    683   -359   2933       C  
ATOM   3405  O   SER B 184      26.363 -14.949 -29.014  1.00134.71           O  
ANISOU 3405  O   SER B 184    13896  19269  18019    542   -268   2803       O  
ATOM   3406  CB  SER B 184      28.955 -16.981 -29.405  1.00114.16           C  
ANISOU 3406  CB  SER B 184    10622  16907  15847   1151    -80   3054       C  
ATOM   3407  OG  SER B 184      28.629 -18.130 -28.642  1.00114.18           O  
ANISOU 3407  OG  SER B 184    10768  16716  15901   1339   -173   3063       O  
ATOM   3408  N   ARG B 185      26.699 -16.393 -27.321  1.00 82.18           N  
ANISOU 3408  N   ARG B 185     7207  12521  11495    754   -503   2960       N  
ATOM   3409  CA  ARG B 185      25.299 -16.409 -26.911  1.00 80.62           C  
ANISOU 3409  CA  ARG B 185     7369  12119  11142    653   -558   2837       C  
ATOM   3410  C   ARG B 185      24.857 -15.051 -26.381  1.00 78.74           C  
ANISOU 3410  C   ARG B 185     7221  11939  10759    343   -701   2818       C  
ATOM   3411  O   ARG B 185      23.727 -14.624 -26.616  1.00 77.31           O  
ANISOU 3411  O   ARG B 185     7292  11639  10442    233   -661   2677       O  
ATOM   3412  CB  ARG B 185      25.057 -17.472 -25.840  1.00145.50           C  
ANISOU 3412  CB  ARG B 185    15688  20208  19388    764   -698   2914       C  
ATOM   3413  CG  ARG B 185      25.147 -18.902 -26.334  1.00146.25           C  
ANISOU 3413  CG  ARG B 185    15986  20070  19513    974   -558   2814       C  
ATOM   3414  CD  ARG B 185      24.802 -19.872 -25.219  1.00148.89           C  
ANISOU 3414  CD  ARG B 185    16136  20408  20028   1274   -404   2841       C  
ATOM   3415  NE  ARG B 185      24.896 -21.264 -25.649  1.00149.00           N  
ANISOU 3415  NE  ARG B 185    16117  20466  20029   1316   -165   2702       N  
ATOM   3416  CZ  ARG B 185      24.702 -22.305 -24.846  1.00151.05           C  
ANISOU 3416  CZ  ARG B 185    16237  20743  20410   1575     24   2681       C  
ATOM   3417  NH1 ARG B 185      24.404 -22.112 -23.569  1.00152.54           N  
ANISOU 3417  NH1 ARG B 185    16296  20895  20767   1830     -4   2791       N  
ATOM   3418  NH2 ARG B 185      24.807 -23.540 -25.318  1.00151.67           N  
ANISOU 3418  NH2 ARG B 185    16316  20876  20436   1590    244   2552       N  
ATOM   3419  N   THR B 186      25.748 -14.383 -25.656  1.00 75.91           N  
ANISOU 3419  N   THR B 186     6653  11755  10434    207   -876   2961       N  
ATOM   3420  CA  THR B 186      25.445 -13.074 -25.091  1.00 74.44           C  
ANISOU 3420  CA  THR B 186     6554  11611  10117    -89  -1031   2945       C  
ATOM   3421  C   THR B 186      25.268 -12.043 -26.201  1.00 73.66           C  
ANISOU 3421  C   THR B 186     6478  11537   9974   -215   -884   2848       C  
ATOM   3422  O   THR B 186      24.340 -11.233 -26.165  1.00 72.15           O  
ANISOU 3422  O   THR B 186     6526  11246   9643   -372   -908   2733       O  
ATOM   3423  CB  THR B 186      26.544 -12.608 -24.117  1.00 93.77           C  
ANISOU 3423  CB  THR B 186     8761  14246  12622   -222  -1269   3124       C  
ATOM   3424  OG1 THR B 186      26.765 -13.619 -23.125  1.00 94.30           O  
ANISOU 3424  OG1 THR B 186     8845  14286  12699   -123  -1436   3223       O  
ATOM   3425  CG2 THR B 186      26.136 -11.313 -23.432  1.00 92.40           C  
ANISOU 3425  CG2 THR B 186     8710  14087  12309   -537  -1431   3086       C  
ATOM   3426  N   LYS B 187      26.157 -12.084 -27.190  1.00 63.08           N  
ANISOU 3426  N   LYS B 187     4887  10331   8748   -134   -726   2901       N  
ATOM   3427  CA  LYS B 187      26.043 -11.202 -28.347  1.00 62.23           C  
ANISOU 3427  CA  LYS B 187     4797  10256   8589   -243   -568   2832       C  
ATOM   3428  C   LYS B 187      24.759 -11.491 -29.121  1.00 60.91           C  
ANISOU 3428  C   LYS B 187     4936   9898   8308   -166   -412   2643       C  
ATOM   3429  O   LYS B 187      24.070 -10.569 -29.570  1.00 59.17           O  
ANISOU 3429  O   LYS B 187     4888   9619   7973   -326   -398   2557       O  
ATOM   3430  CB  LYS B 187      27.264 -11.344 -29.257  1.00 91.71           C  
ANISOU 3430  CB  LYS B 187     8200  14187  12457   -136   -389   2929       C  
ATOM   3431  CG  LYS B 187      28.553 -10.818 -28.643  1.00 92.79           C  
ANISOU 3431  CG  LYS B 187     7994  14551  12710   -279   -537   3128       C  
ATOM   3432  CD  LYS B 187      29.742 -11.012 -29.571  1.00 94.47           C  
ANISOU 3432  CD  LYS B 187     7859  14982  13054   -173   -322   3225       C  
ATOM   3433  CE  LYS B 187      30.012 -12.485 -29.828  1.00 96.19           C  
ANISOU 3433  CE  LYS B 187     7965  15193  13389    201   -157   3217       C  
ATOM   3434  NZ  LYS B 187      31.204 -12.690 -30.698  1.00 98.09           N  
ANISOU 3434  NZ  LYS B 187     7852  15664  13754    333     77   3306       N  
ATOM   3435  N   LYS B 188      24.445 -12.777 -29.269  1.00 73.18           N  
ANISOU 3435  N   LYS B 188     6558  11345   9901     76   -313   2585       N  
ATOM   3436  CA  LYS B 188      23.195 -13.206 -29.888  1.00 72.24           C  
ANISOU 3436  CA  LYS B 188     6723  11040   9686    146   -193   2412       C  
ATOM   3437  C   LYS B 188      21.995 -12.626 -29.149  1.00 70.45           C  
ANISOU 3437  C   LYS B 188     6754  10683   9332    -18   -340   2338       C  
ATOM   3438  O   LYS B 188      20.993 -12.253 -29.763  1.00 68.70           O  
ANISOU 3438  O   LYS B 188     6732  10362   9008    -74   -276   2212       O  
ATOM   3439  CB  LYS B 188      23.094 -14.734 -29.896  1.00 60.20           C  
ANISOU 3439  CB  LYS B 188     5233   9400   8240    414   -102   2377       C  
ATOM   3440  CG  LYS B 188      23.891 -15.425 -30.991  1.00 61.98           C  
ANISOU 3440  CG  LYS B 188     5284   9704   8559    626    113   2377       C  
ATOM   3441  CD  LYS B 188      23.715 -16.936 -30.914  1.00 63.83           C  
ANISOU 3441  CD  LYS B 188     5605   9775   8871    895    186   2324       C  
ATOM   3442  CE  LYS B 188      24.392 -17.642 -32.079  1.00 65.78           C  
ANISOU 3442  CE  LYS B 188     5735  10074   9182   1127    431   2277       C  
ATOM   3443  NZ  LYS B 188      25.854 -17.359 -32.133  1.00 66.92           N  
ANISOU 3443  NZ  LYS B 188     5505  10469   9452   1180    467   2437       N  
ATOM   3444  N   PHE B 189      22.104 -12.556 -27.826  1.00 49.18           N  
ANISOU 3444  N   PHE B 189     4052   7998   6638    -85   -534   2420       N  
ATOM   3445  CA  PHE B 189      21.018 -12.056 -26.993  1.00 47.92           C  
ANISOU 3445  CA  PHE B 189     4128   7734   6348   -224   -661   2353       C  
ATOM   3446  C   PHE B 189      20.883 -10.541 -27.096  1.00 46.02           C  
ANISOU 3446  C   PHE B 189     3943   7526   6018   -449   -723   2318       C  
ATOM   3447  O   PHE B 189      19.774 -10.011 -27.047  1.00 43.51           O  
ANISOU 3447  O   PHE B 189     3844   7098   5592   -520   -725   2203       O  
ATOM   3448  CB  PHE B 189      21.209 -12.480 -25.536  1.00 44.26           C  
ANISOU 3448  CB  PHE B 189     3657   7279   5879   -230   -846   2452       C  
ATOM   3449  CG  PHE B 189      20.101 -12.032 -24.627  1.00 42.01           C  
ANISOU 3449  CG  PHE B 189     3621   6897   5443   -344   -943   2377       C  
ATOM   3450  CD1 PHE B 189      18.808 -12.490 -24.817  1.00 41.12           C  
ANISOU 3450  CD1 PHE B 189     3709   6639   5276   -277   -845   2266       C  
ATOM   3451  CD2 PHE B 189      20.354 -11.165 -23.577  1.00 40.68           C  
ANISOU 3451  CD2 PHE B 189     3486   6787   5183   -520  -1130   2413       C  
ATOM   3452  CE1 PHE B 189      17.788 -12.086 -23.985  1.00 38.82           C  
ANISOU 3452  CE1 PHE B 189     3620   6281   4849   -369   -908   2202       C  
ATOM   3453  CE2 PHE B 189      19.337 -10.758 -22.739  1.00 39.38           C  
ANISOU 3453  CE2 PHE B 189     3557   6541   4865   -603  -1194   2330       C  
ATOM   3454  CZ  PHE B 189      18.052 -11.218 -22.944  1.00 37.51           C  
ANISOU 3454  CZ  PHE B 189     3492   6177   4582   -520  -1071   2229       C  
ATOM   3455  N   ILE B 190      22.011  -9.850 -27.230  1.00 55.59           N  
ANISOU 3455  N   ILE B 190     4952   8886   7286   -559   -779   2424       N  
ATOM   3456  CA  ILE B 190      21.996  -8.409 -27.458  1.00 54.11           C  
ANISOU 3456  CA  ILE B 190     4817   8711   7032   -783   -839   2406       C  
ATOM   3457  C   ILE B 190      21.301  -8.116 -28.783  1.00 52.07           C  
ANISOU 3457  C   ILE B 190     4671   8386   6728   -764   -660   2303       C  
ATOM   3458  O   ILE B 190      20.410  -7.259 -28.864  1.00 49.80           O  
ANISOU 3458  O   ILE B 190     4588   7993   6342   -874   -694   2214       O  
ATOM   3459  CB  ILE B 190      23.423  -7.828 -27.488  1.00 57.73           C  
ANISOU 3459  CB  ILE B 190     5001   9351   7582   -917   -915   2562       C  
ATOM   3460  CG1 ILE B 190      24.119  -8.054 -26.144  1.00 59.02           C  
ANISOU 3460  CG1 ILE B 190     5050   9591   7781   -955  -1131   2674       C  
ATOM   3461  CG2 ILE B 190      23.393  -6.347 -27.826  1.00 56.72           C  
ANISOU 3461  CG2 ILE B 190     4953   9205   7392  -1163   -974   2549       C  
ATOM   3462  CD1 ILE B 190      23.430  -7.379 -24.978  1.00 57.82           C  
ANISOU 3462  CD1 ILE B 190     5141   9338   7488  -1114  -1335   2609       C  
ATOM   3463  N   SER B 191      21.711  -8.847 -29.816  1.00 48.53           N  
ANISOU 3463  N   SER B 191     4097   7996   6345   -610   -473   2314       N  
ATOM   3464  CA  SER B 191      21.102  -8.727 -31.133  1.00 47.13           C  
ANISOU 3464  CA  SER B 191     4031   7770   6106   -578   -301   2220       C  
ATOM   3465  C   SER B 191      19.601  -8.995 -31.063  1.00 45.33           C  
ANISOU 3465  C   SER B 191     4075   7360   5788   -523   -299   2070       C  
ATOM   3466  O   SER B 191      18.805  -8.281 -31.674  1.00 43.35           O  
ANISOU 3466  O   SER B 191     3981   7038   5449   -594   -274   1993       O  
ATOM   3467  CB  SER B 191      21.766  -9.692 -32.116  1.00 54.78           C  
ANISOU 3467  CB  SER B 191     4839   8829   7143   -390    -95   2239       C  
ATOM   3468  OG  SER B 191      23.155  -9.431 -32.229  1.00 56.34           O  
ANISOU 3468  OG  SER B 191     4747   9223   7435   -436    -75   2388       O  
ATOM   3469  N   ALA B 192      19.223 -10.020 -30.306  1.00 32.79           N  
ANISOU 3469  N   ALA B 192     2531   5702   4227   -401   -331   2045       N  
ATOM   3470  CA  ALA B 192      17.819 -10.373 -30.131  1.00 31.55           C  
ANISOU 3470  CA  ALA B 192     2598   5389   4001   -361   -332   1923       C  
ATOM   3471  C   ALA B 192      17.045  -9.244 -29.454  1.00 29.00           C  
ANISOU 3471  C   ALA B 192     2425   5010   3586   -517   -460   1881       C  
ATOM   3472  O   ALA B 192      15.899  -8.963 -29.810  1.00 27.42           O  
ANISOU 3472  O   ALA B 192     2389   4713   3318   -526   -435   1778       O  
ATOM   3473  CB  ALA B 192      17.692 -11.662 -29.334  1.00 39.00           C  
ANISOU 3473  CB  ALA B 192     3545   6276   4997   -227   -350   1939       C  
ATOM   3474  N   ILE B 193      17.681  -8.600 -28.479  1.00 42.84           N  
ANISOU 3474  N   ILE B 193     4120   6822   5336   -633   -604   1958       N  
ATOM   3475  CA  ILE B 193      17.085  -7.463 -27.788  1.00 40.75           C  
ANISOU 3475  CA  ILE B 193     4010   6494   4977   -775   -728   1909       C  
ATOM   3476  C   ILE B 193      16.836  -6.314 -28.760  1.00 39.31           C  
ANISOU 3476  C   ILE B 193     3898   6277   4759   -874   -700   1869       C  
ATOM   3477  O   ILE B 193      15.749  -5.731 -28.781  1.00 37.46           O  
ANISOU 3477  O   ILE B 193     3843   5935   4455   -891   -711   1771       O  
ATOM   3478  CB  ILE B 193      17.977  -6.977 -26.623  1.00 57.58           C  
ANISOU 3478  CB  ILE B 193     6076   8698   7104   -897   -905   1997       C  
ATOM   3479  CG1 ILE B 193      17.911  -7.963 -25.453  1.00 58.54           C  
ANISOU 3479  CG1 ILE B 193     6194   8830   7218   -811   -964   2032       C  
ATOM   3480  CG2 ILE B 193      17.559  -5.591 -26.161  1.00 55.81           C  
ANISOU 3480  CG2 ILE B 193     6028   8397   6780  -1055  -1025   1931       C  
ATOM   3481  CD1 ILE B 193      18.734  -7.550 -24.251  1.00 59.41           C  
ANISOU 3481  CD1 ILE B 193     6259   9016   7297   -932  -1162   2118       C  
ATOM   3482  N   TRP B 194      17.842  -6.001 -29.574  1.00 49.92           N  
ANISOU 3482  N   TRP B 194     5093   7719   6156   -936   -660   1958       N  
ATOM   3483  CA  TRP B 194      17.710  -4.933 -30.565  1.00 48.91           C  
ANISOU 3483  CA  TRP B 194     5029   7563   5991  -1042   -631   1951       C  
ATOM   3484  C   TRP B 194      16.614  -5.213 -31.594  1.00 47.58           C  
ANISOU 3484  C   TRP B 194     4992   7315   5772   -936   -506   1851       C  
ATOM   3485  O   TRP B 194      15.802  -4.335 -31.911  1.00 46.01           O  
ANISOU 3485  O   TRP B 194     4953   7017   5510   -993   -539   1797       O  
ATOM   3486  CB  TRP B 194      19.043  -4.678 -31.272  1.00 60.04           C  
ANISOU 3486  CB  TRP B 194     6228   9121   7465  -1126   -580   2086       C  
ATOM   3487  CG  TRP B 194      19.936  -3.720 -30.542  1.00 61.18           C  
ANISOU 3487  CG  TRP B 194     6305   9306   7635  -1335   -747   2182       C  
ATOM   3488  CD1 TRP B 194      21.027  -4.027 -29.781  1.00 63.40           C  
ANISOU 3488  CD1 TRP B 194     6382   9714   7995  -1382   -837   2291       C  
ATOM   3489  CD2 TRP B 194      19.809  -2.294 -30.502  1.00 60.68           C  
ANISOU 3489  CD2 TRP B 194     6389   9144   7522  -1533   -865   2179       C  
ATOM   3490  NE1 TRP B 194      21.589  -2.880 -29.272  1.00 64.41           N  
ANISOU 3490  NE1 TRP B 194     6519   9834   8119  -1617  -1011   2351       N  
ATOM   3491  CE2 TRP B 194      20.860  -1.802 -29.700  1.00 62.86           C  
ANISOU 3491  CE2 TRP B 194     6550   9488   7846  -1713  -1027   2280       C  
ATOM   3492  CE3 TRP B 194      18.910  -1.385 -31.069  1.00 59.01           C  
ANISOU 3492  CE3 TRP B 194     6401   8783   7238  -1573   -861   2105       C  
ATOM   3493  CZ2 TRP B 194      21.036  -0.442 -29.452  1.00 63.61           C  
ANISOU 3493  CZ2 TRP B 194     6766   9488   7914  -1942  -1182   2297       C  
ATOM   3494  CZ3 TRP B 194      19.085  -0.037 -30.821  1.00 59.67           C  
ANISOU 3494  CZ3 TRP B 194     6603   8768   7302  -1777  -1007   2129       C  
ATOM   3495  CH2 TRP B 194      20.140   0.422 -30.018  1.00 62.03           C  
ANISOU 3495  CH2 TRP B 194     6803   9119   7645  -1965  -1164   2219       C  
ATOM   3496  N   LEU B 195      16.596  -6.437 -32.112  1.00 40.91           N  
ANISOU 3496  N   LEU B 195     4086   6502   4954   -778   -376   1828       N  
ATOM   3497  CA  LEU B 195      15.603  -6.834 -33.104  1.00 39.94           C  
ANISOU 3497  CA  LEU B 195     4086   6310   4778   -686   -274   1730       C  
ATOM   3498  C   LEU B 195      14.191  -6.792 -32.531  1.00 38.51           C  
ANISOU 3498  C   LEU B 195     4075   5999   4556   -661   -344   1625       C  
ATOM   3499  O   LEU B 195      13.256  -6.319 -33.186  1.00 37.00           O  
ANISOU 3499  O   LEU B 195     4011   5739   4309   -667   -338   1561       O  
ATOM   3500  CB  LEU B 195      15.920  -8.225 -33.653  1.00 35.65           C  
ANISOU 3500  CB  LEU B 195     3460   5812   4275   -525   -133   1714       C  
ATOM   3501  CG  LEU B 195      17.230  -8.312 -34.439  1.00 37.31           C  
ANISOU 3501  CG  LEU B 195     3498   6166   4513   -511    -10   1800       C  
ATOM   3502  CD1 LEU B 195      17.582  -9.755 -34.763  1.00 39.74           C  
ANISOU 3502  CD1 LEU B 195     3716   6501   4883   -318    114   1780       C  
ATOM   3503  CD2 LEU B 195      17.143  -7.481 -35.710  1.00 36.49           C  
ANISOU 3503  CD2 LEU B 195     3473   6082   4309   -573     72   1789       C  
ATOM   3504  N   ALA B 196      14.047  -7.281 -31.304  1.00 37.25           N  
ANISOU 3504  N   ALA B 196     3911   5820   4424   -632   -408   1619       N  
ATOM   3505  CA  ALA B 196      12.763  -7.237 -30.618  1.00 35.79           C  
ANISOU 3505  CA  ALA B 196     3862   5538   4199   -612   -456   1533       C  
ATOM   3506  C   ALA B 196      12.333  -5.790 -30.418  1.00 33.83           C  
ANISOU 3506  C   ALA B 196     3724   5234   3895   -713   -548   1505       C  
ATOM   3507  O   ALA B 196      11.149  -5.466 -30.511  1.00 32.54           O  
ANISOU 3507  O   ALA B 196     3675   4993   3697   -685   -556   1425       O  
ATOM   3508  CB  ALA B 196      12.843  -7.960 -29.284  1.00 21.30           C  
ANISOU 3508  CB  ALA B 196     2001   3712   2383   -576   -499   1555       C  
ATOM   3509  N   SER B 197      13.307  -4.925 -30.148  1.00 42.68           N  
ANISOU 3509  N   SER B 197     4807   6392   5018   -829   -623   1575       N  
ATOM   3510  CA  SER B 197      13.047  -3.500 -29.971  1.00 41.61           C  
ANISOU 3510  CA  SER B 197     4796   6175   4837   -935   -722   1552       C  
ATOM   3511  C   SER B 197      12.516  -2.877 -31.256  1.00 40.73           C  
ANISOU 3511  C   SER B 197     4758   6009   4708   -942   -681   1539       C  
ATOM   3512  O   SER B 197      11.588  -2.066 -31.227  1.00 39.79           O  
ANISOU 3512  O   SER B 197     4782   5780   4555   -943   -733   1478       O  
ATOM   3513  CB  SER B 197      14.320  -2.779 -29.529  1.00 35.68           C  
ANISOU 3513  CB  SER B 197     3982   5471   4102  -1088   -825   1643       C  
ATOM   3514  OG  SER B 197      14.882  -3.411 -28.394  1.00 36.57           O  
ANISOU 3514  OG  SER B 197     4018   5651   4225  -1082   -881   1672       O  
ATOM   3515  N   ALA B 198      13.114  -3.258 -32.382  1.00 43.72           N  
ANISOU 3515  N   ALA B 198     5040   6468   5102   -934   -584   1598       N  
ATOM   3516  CA  ALA B 198      12.645  -2.794 -33.684  1.00 42.91           C  
ANISOU 3516  CA  ALA B 198     5012   6335   4956   -939   -538   1598       C  
ATOM   3517  C   ALA B 198      11.216  -3.271 -33.939  1.00 41.87           C  
ANISOU 3517  C   ALA B 198     4977   6134   4798   -818   -517   1493       C  
ATOM   3518  O   ALA B 198      10.355  -2.496 -34.371  1.00 41.18           O  
ANISOU 3518  O   ALA B 198     5005   5969   4673   -822   -557   1470       O  
ATOM   3519  CB  ALA B 198      13.573  -3.276 -34.785  1.00 51.67           C  
ANISOU 3519  CB  ALA B 198     5999   7568   6065   -943   -415   1675       C  
ATOM   3520  N   LEU B 199      10.975  -4.550 -33.661  1.00 30.06           N  
ANISOU 3520  N   LEU B 199     3427   4665   3330   -717   -465   1442       N  
ATOM   3521  CA  LEU B 199       9.651  -5.143 -33.828  1.00 29.80           C  
ANISOU 3521  CA  LEU B 199     3458   4577   3287   -625   -452   1351       C  
ATOM   3522  C   LEU B 199       8.600  -4.414 -32.995  1.00 29.05           C  
ANISOU 3522  C   LEU B 199     3449   4400   3190   -616   -536   1296       C  
ATOM   3523  O   LEU B 199       7.468  -4.223 -33.436  1.00 28.99           O  
ANISOU 3523  O   LEU B 199     3503   4342   3171   -570   -555   1245       O  
ATOM   3524  CB  LEU B 199       9.677  -6.627 -33.456  1.00 49.44           C  
ANISOU 3524  CB  LEU B 199     5875   7093   5816   -543   -385   1324       C  
ATOM   3525  CG  LEU B 199      10.462  -7.551 -34.388  1.00 51.02           C  
ANISOU 3525  CG  LEU B 199     6012   7352   6021   -500   -282   1344       C  
ATOM   3526  CD1 LEU B 199      10.490  -8.969 -33.838  1.00 52.95           C  
ANISOU 3526  CD1 LEU B 199     6213   7582   6322   -414   -238   1319       C  
ATOM   3527  CD2 LEU B 199       9.873  -7.523 -35.790  1.00 50.95           C  
ANISOU 3527  CD2 LEU B 199     6085   7330   5942   -490   -248   1302       C  
ATOM   3528  N   LEU B 200       8.982  -4.008 -31.788  1.00 46.01           N  
ANISOU 3528  N   LEU B 200     5597   6540   5344   -652   -586   1304       N  
ATOM   3529  CA  LEU B 200       8.083  -3.264 -30.911  1.00 46.02           C  
ANISOU 3529  CA  LEU B 200     5690   6468   5328   -626   -645   1237       C  
ATOM   3530  C   LEU B 200       7.941  -1.814 -31.365  1.00 45.84           C  
ANISOU 3530  C   LEU B 200     5784   6347   5286   -664   -722   1232       C  
ATOM   3531  O   LEU B 200       6.960  -1.144 -31.037  1.00 46.58           O  
ANISOU 3531  O   LEU B 200     5964   6361   5371   -604   -758   1164       O  
ATOM   3532  CB  LEU B 200       8.581  -3.314 -29.465  1.00 33.11           C  
ANISOU 3532  CB  LEU B 200     4050   4857   3675   -654   -677   1237       C  
ATOM   3533  CG  LEU B 200       8.574  -4.686 -28.787  1.00 33.88           C  
ANISOU 3533  CG  LEU B 200     4064   5023   3786   -601   -616   1244       C  
ATOM   3534  CD1 LEU B 200       9.229  -4.610 -27.421  1.00 34.34           C  
ANISOU 3534  CD1 LEU B 200     4120   5120   3807   -651   -672   1276       C  
ATOM   3535  CD2 LEU B 200       7.154  -5.225 -28.678  1.00 34.73           C  
ANISOU 3535  CD2 LEU B 200     4192   5110   3893   -513   -566   1173       C  
ATOM   3536  N   ALA B 201       8.925  -1.334 -32.120  1.00 44.12           N  
ANISOU 3536  N   ALA B 201     5567   6133   5063   -758   -740   1312       N  
ATOM   3537  CA  ALA B 201       8.922   0.047 -32.595  1.00 44.44           C  
ANISOU 3537  CA  ALA B 201     5734   6062   5089   -818   -823   1335       C  
ATOM   3538  C   ALA B 201       8.191   0.184 -33.926  1.00 44.33           C  
ANISOU 3538  C   ALA B 201     5762   6021   5059   -768   -811   1348       C  
ATOM   3539  O   ALA B 201       7.938   1.297 -34.390  1.00 44.95           O  
ANISOU 3539  O   ALA B 201     5957   5994   5126   -800   -885   1380       O  
ATOM   3540  CB  ALA B 201      10.344   0.574 -32.711  1.00 22.76           C  
ANISOU 3540  CB  ALA B 201     2970   3335   2344   -981   -861   1438       C  
ATOM   3541  N   ILE B 202       7.863  -0.954 -34.533  1.00 44.31           N  
ANISOU 3541  N   ILE B 202     5681   6103   5052   -697   -733   1327       N  
ATOM   3542  CA  ILE B 202       7.115  -0.996 -35.797  1.00 44.52           C  
ANISOU 3542  CA  ILE B 202     5747   6123   5044   -655   -736   1332       C  
ATOM   3543  C   ILE B 202       5.869  -0.085 -35.911  1.00 45.35           C  
ANISOU 3543  C   ILE B 202     5952   6117   5163   -581   -831   1301       C  
ATOM   3544  O   ILE B 202       5.724   0.611 -36.916  1.00 45.74           O  
ANISOU 3544  O   ILE B 202     6083   6121   5173   -599   -885   1358       O  
ATOM   3545  CB  ILE B 202       6.757  -2.456 -36.201  1.00 31.75           C  
ANISOU 3545  CB  ILE B 202     4046   4596   3421   -593   -654   1287       C  
ATOM   3546  CG1 ILE B 202       8.022  -3.229 -36.578  1.00 31.74           C  
ANISOU 3546  CG1 ILE B 202     3973   4692   3394   -644   -556   1336       C  
ATOM   3547  CG2 ILE B 202       5.766  -2.476 -37.352  1.00 32.45           C  
ANISOU 3547  CG2 ILE B 202     4189   4671   3471   -547   -694   1270       C  
ATOM   3548  CD1 ILE B 202       7.755  -4.627 -37.088  1.00 32.62           C  
ANISOU 3548  CD1 ILE B 202     4036   4859   3499   -578   -477   1281       C  
ATOM   3549  N   PRO B 203       4.975  -0.078 -34.895  1.00 41.94           N  
ANISOU 3549  N   PRO B 203     5509   5645   4781   -489   -848   1218       N  
ATOM   3550  CA  PRO B 203       3.758   0.744 -34.997  1.00 43.62           C  
ANISOU 3550  CA  PRO B 203     5790   5759   5022   -387   -928   1187       C  
ATOM   3551  C   PRO B 203       3.983   2.216 -35.344  1.00 44.28           C  
ANISOU 3551  C   PRO B 203     6027   5700   5095   -425  -1026   1246       C  
ATOM   3552  O   PRO B 203       3.095   2.837 -35.927  1.00 45.65           O  
ANISOU 3552  O   PRO B 203     6263   5799   5282   -350  -1103   1265       O  
ATOM   3553  CB  PRO B 203       3.154   0.638 -33.596  1.00 26.15           C  
ANISOU 3553  CB  PRO B 203     3544   3539   2853   -297   -897   1093       C  
ATOM   3554  CG  PRO B 203       3.572  -0.686 -33.128  1.00 25.18           C  
ANISOU 3554  CG  PRO B 203     3306   3538   2724   -333   -803   1079       C  
ATOM   3555  CD  PRO B 203       4.958  -0.896 -33.667  1.00 23.71           C  
ANISOU 3555  CD  PRO B 203     3118   3392   2500   -458   -786   1155       C  
ATOM   3556  N   MET B 204       5.145   2.761 -35.000  1.00 45.65           N  
ANISOU 3556  N   MET B 204     6260   5832   5252   -547  -1035   1285       N  
ATOM   3557  CA  MET B 204       5.439   4.162 -35.289  1.00 46.80           C  
ANISOU 3557  CA  MET B 204     6568   5819   5395   -615  -1137   1350       C  
ATOM   3558  C   MET B 204       5.600   4.426 -36.785  1.00 46.58           C  
ANISOU 3558  C   MET B 204     6585   5796   5319   -681  -1165   1474       C  
ATOM   3559  O   MET B 204       5.505   5.567 -37.236  1.00 48.07           O  
ANISOU 3559  O   MET B 204     6920   5835   5508   -701  -1264   1541       O  
ATOM   3560  CB  MET B 204       6.682   4.622 -34.525  1.00 38.89           C  
ANISOU 3560  CB  MET B 204     5602   4786   4388   -769  -1153   1373       C  
ATOM   3561  CG  MET B 204       6.436   4.822 -33.047  1.00 40.04           C  
ANISOU 3561  CG  MET B 204     5790   4871   4553   -711  -1169   1252       C  
ATOM   3562  SD  MET B 204       5.049   5.936 -32.757  1.00 43.28           S  
ANISOU 3562  SD  MET B 204     6371   5070   5001   -530  -1248   1156       S  
ATOM   3563  CE  MET B 204       4.902   5.841 -30.975  1.00 44.64           C  
ANISOU 3563  CE  MET B 204     6547   5261   5153   -448  -1199    997       C  
ATOM   3564  N   LEU B 205       5.843   3.366 -37.549  1.00 36.85           N  
ANISOU 3564  N   LEU B 205     5242   4725   4034   -710  -1078   1505       N  
ATOM   3565  CA  LEU B 205       5.976   3.475 -38.997  1.00 36.96           C  
ANISOU 3565  CA  LEU B 205     5304   4773   3965   -764  -1085   1611       C  
ATOM   3566  C   LEU B 205       4.616   3.659 -39.662  1.00 37.97           C  
ANISOU 3566  C   LEU B 205     5485   4851   4089   -634  -1175   1596       C  
ATOM   3567  O   LEU B 205       4.524   4.163 -40.781  1.00 38.65           O  
ANISOU 3567  O   LEU B 205     5668   4913   4102   -666  -1235   1695       O  
ATOM   3568  CB  LEU B 205       6.667   2.233 -39.564  1.00 32.82           C  
ANISOU 3568  CB  LEU B 205     4661   4435   3374   -811   -953   1619       C  
ATOM   3569  CG  LEU B 205       8.116   2.006 -39.132  1.00 32.72           C  
ANISOU 3569  CG  LEU B 205     4566   4502   3363   -939   -863   1671       C  
ATOM   3570  CD1 LEU B 205       8.639   0.686 -39.670  1.00 32.27           C  
ANISOU 3570  CD1 LEU B 205     4391   4618   3252   -930   -722   1660       C  
ATOM   3571  CD2 LEU B 205       8.990   3.162 -39.597  1.00 34.70           C  
ANISOU 3571  CD2 LEU B 205     4910   4694   3582  -1097   -905   1814       C  
ATOM   3572  N   PHE B 206       3.562   3.243 -38.966  1.00 37.27           N  
ANISOU 3572  N   PHE B 206     5326   4759   4077   -491  -1186   1484       N  
ATOM   3573  CA  PHE B 206       2.206   3.340 -39.494  1.00 38.69           C  
ANISOU 3573  CA  PHE B 206     5506   4915   4278   -358  -1277   1470       C  
ATOM   3574  C   PHE B 206       1.362   4.347 -38.714  1.00 40.85           C  
ANISOU 3574  C   PHE B 206     5835   5033   4652   -223  -1361   1430       C  
ATOM   3575  O   PHE B 206       0.249   4.679 -39.120  1.00 42.55           O  
ANISOU 3575  O   PHE B 206     6071   5194   4901   -106  -1464   1452       O  
ATOM   3576  CB  PHE B 206       1.521   1.970 -39.476  1.00 50.89           C  
ANISOU 3576  CB  PHE B 206     6896   6603   5837   -299  -1219   1384       C  
ATOM   3577  CG  PHE B 206       2.200   0.937 -40.331  1.00 49.66           C  
ANISOU 3577  CG  PHE B 206     6712   6576   5580   -398  -1144   1402       C  
ATOM   3578  CD1 PHE B 206       1.850   0.784 -41.663  1.00 50.24           C  
ANISOU 3578  CD1 PHE B 206     6840   6693   5558   -414  -1205   1450       C  
ATOM   3579  CD2 PHE B 206       3.178   0.112 -39.801  1.00 48.36           C  
ANISOU 3579  CD2 PHE B 206     6477   6487   5410   -463  -1015   1369       C  
ATOM   3580  CE1 PHE B 206       2.468  -0.165 -42.450  1.00 49.79           C  
ANISOU 3580  CE1 PHE B 206     6782   6748   5390   -490  -1122   1446       C  
ATOM   3581  CE2 PHE B 206       3.799  -0.841 -40.584  1.00 47.94           C  
ANISOU 3581  CE2 PHE B 206     6405   6541   5271   -524   -932   1374       C  
ATOM   3582  CZ  PHE B 206       3.443  -0.979 -41.911  1.00 48.78           C  
ANISOU 3582  CZ  PHE B 206     6580   6683   5270   -535   -977   1403       C  
ATOM   3583  N   THR B 207       1.893   4.828 -37.594  1.00 50.57           N  
ANISOU 3583  N   THR B 207     7093   6194   5927   -231  -1321   1368       N  
ATOM   3584  CA  THR B 207       1.168   5.771 -36.748  1.00 53.31           C  
ANISOU 3584  CA  THR B 207     7514   6385   6356    -88  -1376   1302       C  
ATOM   3585  C   THR B 207       1.479   7.215 -37.130  1.00 54.80           C  
ANISOU 3585  C   THR B 207     7915   6359   6548   -122  -1497   1387       C  
ATOM   3586  O   THR B 207       0.587   8.061 -37.182  1.00 57.54           O  
ANISOU 3586  O   THR B 207     8345   6557   6960     33  -1587   1376       O  
ATOM   3587  CB  THR B 207       1.510   5.572 -35.258  1.00 36.03           C  
ANISOU 3587  CB  THR B 207     5299   4204   4186    -83  -1289   1185       C  
ATOM   3588  OG1 THR B 207       1.345   4.194 -34.904  1.00 34.78           O  
ANISOU 3588  OG1 THR B 207     4958   4237   4018    -85  -1177   1135       O  
ATOM   3589  CG2 THR B 207       0.611   6.434 -34.382  1.00 39.62           C  
ANISOU 3589  CG2 THR B 207     5818   4526   4710    105  -1314   1084       C  
ATOM   3590  N   MET B 208       2.751   7.491 -37.398  1.00 37.64           N  
ANISOU 3590  N   MET B 208     5824   4168   4311   -324  -1499   1482       N  
ATOM   3591  CA  MET B 208       3.192   8.847 -37.704  1.00 39.29           C  
ANISOU 3591  CA  MET B 208     6244   4162   4522   -405  -1612   1581       C  
ATOM   3592  C   MET B 208       3.286   9.087 -39.207  1.00 40.36           C  
ANISOU 3592  C   MET B 208     6442   4304   4589   -476  -1677   1750       C  
ATOM   3593  O   MET B 208       3.598   8.175 -39.973  1.00 39.66           O  
ANISOU 3593  O   MET B 208     6245   4409   4416   -543  -1606   1797       O  
ATOM   3594  CB  MET B 208       4.544   9.125 -37.043  1.00 40.10           C  
ANISOU 3594  CB  MET B 208     6400   4231   4605   -612  -1588   1597       C  
ATOM   3595  CG  MET B 208       4.558   8.878 -35.541  1.00 40.21           C  
ANISOU 3595  CG  MET B 208     6389   4232   4656   -561  -1544   1438       C  
ATOM   3596  SD  MET B 208       3.379   9.916 -34.656  1.00 44.40           S  
ANISOU 3596  SD  MET B 208     7094   4508   5268   -331  -1631   1310       S  
ATOM   3597  CE  MET B 208       4.007  11.544 -35.055  1.00 44.56           C  
ANISOU 3597  CE  MET B 208     6957   4686   5286   -199  -1496   1121       C  
ATOM   3598  N   GLY B 209       3.016  10.320 -39.624  1.00 61.91           N  
ANISOU 3598  N   GLY B 209     9365   6811   7345   -456  -1813   1840       N  
ATOM   3599  CA  GLY B 209       3.105  10.678 -41.028  1.00 62.01           C  
ANISOU 3599  CA  GLY B 209     9473   6811   7277   -530  -1891   2022       C  
ATOM   3600  C   GLY B 209       2.993  12.172 -41.261  1.00 64.92           C  
ANISOU 3600  C   GLY B 209    10087   6883   7694   -519  -2052   2128       C  
ATOM   3601  O   GLY B 209       3.012  12.962 -40.319  1.00 67.08           O  
ANISOU 3601  O   GLY B 209    10472   6946   8066   -463  -2100   2046       O  
ATOM   3602  N   LEU B 210       2.876  12.560 -42.525  1.00 47.01           N  
ANISOU 3602  N   LEU B 210     7924   4589   5346   -572  -2140   2311       N  
ATOM   3603  CA  LEU B 210       2.763  13.968 -42.884  1.00 50.93           C  
ANISOU 3603  CA  LEU B 210     8675   4792   5885   -568  -2309   2446       C  
ATOM   3604  C   LEU B 210       1.312  14.374 -43.106  1.00 52.37           C  
ANISOU 3604  C   LEU B 210     8888   4859   6151   -280  -2449   2431       C  
ATOM   3605  O   LEU B 210       0.520  13.605 -43.653  1.00 51.65           O  
ANISOU 3605  O   LEU B 210     8650   4954   6020   -164  -2452   2421       O  
ATOM   3606  CB  LEU B 210       3.577  14.265 -44.144  1.00 54.02           C  
ANISOU 3606  CB  LEU B 210     9185   5206   6134   -805  -2333   2688       C  
ATOM   3607  CG  LEU B 210       5.090  14.062 -44.057  1.00 53.71           C  
ANISOU 3607  CG  LEU B 210     9113   5268   6026  -1102  -2203   2747       C  
ATOM   3608  CD1 LEU B 210       5.765  14.532 -45.334  1.00 57.71           C  
ANISOU 3608  CD1 LEU B 210     9768   5756   6403  -1323  -2236   3010       C  
ATOM   3609  CD2 LEU B 210       5.659  14.786 -42.846  1.00 53.31           C  
ANISOU 3609  CD2 LEU B 210     9131   5020   6104  -1167  -2222   2653       C  
ATOM   3610  N   GLN B 211       0.967  15.582 -42.672  1.00 66.04           N  
ANISOU 3610  N   GLN B 211    10811   6276   8006   -163  -2571   2424       N  
ATOM   3611  CA  GLN B 211      -0.360  16.136 -42.926  1.00 68.46           C  
ANISOU 3611  CA  GLN B 211    11167   6430   8414    125  -2721   2438       C  
ATOM   3612  C   GLN B 211      -0.289  17.627 -43.227  1.00 71.08           C  
ANISOU 3612  C   GLN B 211    11818   6396   8793     95  -2891   2593       C  
ATOM   3613  O   GLN B 211       0.482  18.357 -42.607  1.00 71.69           O  
ANISOU 3613  O   GLN B 211    12062   6305   8873   -104  -2880   2609       O  
ATOM   3614  CB  GLN B 211      -1.299  15.890 -41.742  1.00 79.67           C  
ANISOU 3614  CB  GLN B 211    12455   7838   9978    402  -2663   2203       C  
ATOM   3615  CG  GLN B 211      -1.865  14.483 -41.669  1.00 77.53           C  
ANISOU 3615  CG  GLN B 211    11869   7910   9681    467  -2530   2081       C  
ATOM   3616  CD  GLN B 211      -2.973  14.355 -40.641  1.00 79.62           C  
ANISOU 3616  CD  GLN B 211    11990   8174  10090    775  -2497   1904       C  
ATOM   3617  OE1 GLN B 211      -3.442  13.253 -40.351  1.00 79.01           O  
ANISOU 3617  OE1 GLN B 211    11665   8328  10027    884  -2455   1855       O  
ATOM   3618  NE2 GLN B 211      -3.400  15.485 -40.085  1.00 82.32           N  
ANISOU 3618  NE2 GLN B 211    12488   8254  10537    912  -2513   1805       N  
ATOM   3619  N   ASN B 212      -1.097  18.074 -44.183  1.00 65.54           N  
ANISOU 3619  N   ASN B 212    11204   5564   8136    283  -3063   2715       N  
ATOM   3620  CA  ASN B 212      -1.162  19.490 -44.517  1.00 70.68           C  
ANISOU 3620  CA  ASN B 212    12177   5861   8818    240  -3242   2906       C  
ATOM   3621  C   ASN B 212      -2.268  20.182 -43.727  1.00 73.25           C  
ANISOU 3621  C   ASN B 212    12652   5833   9345    543  -3353   2802       C  
ATOM   3622  O   ASN B 212      -3.426  20.203 -44.146  1.00 76.41           O  
ANISOU 3622  O   ASN B 212    13342   5886   9806    469  -3439   2848       O  
ATOM   3623  CB  ASN B 212      -1.378  19.682 -46.019  1.00 73.84           C  
ANISOU 3623  CB  ASN B 212    12627   6330   9100    208  -3381   3165       C  
ATOM   3624  CG  ASN B 212      -0.839  21.007 -46.517  1.00 79.23           C  
ANISOU 3624  CG  ASN B 212    13652   6691   9762     60  -3543   3417       C  
ATOM   3625  OD1 ASN B 212      -1.483  22.045 -46.375  1.00 80.51           O  
ANISOU 3625  OD1 ASN B 212    13893   6944   9752   -236  -3523   3615       O  
ATOM   3626  ND2 ASN B 212       0.353  20.979 -47.103  1.00 82.85           N  
ANISOU 3626  ND2 ASN B 212    14317   6768  10392    271  -3700   3419       N  
ATOM   3627  N   LEU B 213      -1.903  20.750 -42.582  1.00 72.51           N  
ANISOU 3627  N   LEU B 213    12363   5828   9360    879  -3345   2662       N  
ATOM   3628  CA  LEU B 213      -2.875  21.366 -41.685  1.00 75.31           C  
ANISOU 3628  CA  LEU B 213    12827   5879   9910   1222  -3425   2551       C  
ATOM   3629  C   LEU B 213      -3.166  22.822 -42.037  1.00 81.56           C  
ANISOU 3629  C   LEU B 213    13941   6286  10762   1278  -3660   2768       C  
ATOM   3630  O   LEU B 213      -3.399  23.648 -41.156  1.00 84.43           O  
ANISOU 3630  O   LEU B 213    14274   6671  11135   1419  -3813   2942       O  
ATOM   3631  CB  LEU B 213      -2.401  21.264 -40.234  1.00 73.05           C  
ANISOU 3631  CB  LEU B 213    12627   5450   9679   1210  -3295   2307       C  
ATOM   3632  CG  LEU B 213      -2.186  19.848 -39.699  1.00 67.10           C  
ANISOU 3632  CG  LEU B 213    11604   5032   8859   1126  -3065   2100       C  
ATOM   3633  CD1 LEU B 213      -1.787  19.881 -38.233  1.00 66.38           C  
ANISOU 3633  CD1 LEU B 213    11628   4760   8835   1210  -2976   1853       C  
ATOM   3634  CD2 LEU B 213      -3.435  19.003 -39.900  1.00 64.71           C  
ANISOU 3634  CD2 LEU B 213    10948   5062   8577   1340  -2994   2042       C  
ATOM   3635  N   SER B 214      -3.151  23.132 -43.329  1.00 87.70           N  
ANISOU 3635  N   SER B 214    15037   6704  11582   1160  -3703   2760       N  
ATOM   3636  CA  SER B 214      -3.502  24.467 -43.791  1.00 94.06           C  
ANISOU 3636  CA  SER B 214    16204   7080  12452   1173  -3927   2966       C  
ATOM   3637  C   SER B 214      -5.017  24.604 -43.874  1.00 98.57           C  
ANISOU 3637  C   SER B 214    16829   7416  13207   1623  -4089   2979       C  
ATOM   3638  O   SER B 214      -5.746  23.632 -43.676  1.00103.60           O  
ANISOU 3638  O   SER B 214    17790   7604  13970   1741  -4228   3006       O  
ATOM   3639  CB  SER B 214      -2.873  24.742 -45.157  1.00 92.16           C  
ANISOU 3639  CB  SER B 214    16047   6928  12042    850  -4018   3290       C  
ATOM   3640  OG  SER B 214      -1.463  24.620 -45.105  1.00 87.55           O  
ANISOU 3640  OG  SER B 214    15289   6693  11284    509  -3837   3275       O  
ATOM   3641  N   GLY B 215      -5.486  25.814 -44.162  1.00 93.25           N  
ANISOU 3641  N   GLY B 215    15837   7035  12557   1872  -4079   2963       N  
ATOM   3642  CA  GLY B 215      -6.910  26.067 -44.289  1.00 97.82           C  
ANISOU 3642  CA  GLY B 215    16404   7449  13315   2302  -4239   3006       C  
ATOM   3643  C   GLY B 215      -7.520  25.287 -45.437  1.00 98.86           C  
ANISOU 3643  C   GLY B 215    16354   7840  13369   2318  -4380   3244       C  
ATOM   3644  O   GLY B 215      -8.578  24.675 -45.293  1.00 98.84           O  
ANISOU 3644  O   GLY B 215    16060   8036  13459   2615  -4401   3197       O  
ATOM   3645  N   ASP B 216      -6.843  25.308 -46.581  1.00101.84           N  
ANISOU 3645  N   ASP B 216    16904   8224  13566   1984  -4478   3504       N  
ATOM   3646  CA  ASP B 216      -7.294  24.573 -47.755  1.00102.77           C  
ANISOU 3646  CA  ASP B 216    16889   8613  13546   1932  -4606   3731       C  
ATOM   3647  C   ASP B 216      -6.570  23.235 -47.862  1.00 97.03           C  
ANISOU 3647  C   ASP B 216    15934   8336  12598   1615  -4417   3676       C  
ATOM   3648  O   ASP B 216      -7.046  22.309 -48.518  1.00 96.36           O  
ANISOU 3648  O   ASP B 216    15647   8567  12401   1605  -4465   3756       O  
ATOM   3649  CB  ASP B 216      -7.071  25.401 -49.023  1.00115.02           C  
ANISOU 3649  CB  ASP B 216    18795   9893  15014   1789  -4839   4073       C  
ATOM   3650  CG  ASP B 216      -5.630  25.847 -49.182  1.00115.24           C  
ANISOU 3650  CG  ASP B 216    19133   9704  14948   1411  -4769   4138       C  
ATOM   3651  OD1 ASP B 216      -4.910  25.917 -48.165  1.00110.51           O  
ANISOU 3651  OD1 ASP B 216    18422   9322  14244   1144  -4545   3992       O  
ATOM   3652  OD2 ASP B 216      -5.217  26.134 -50.325  1.00119.12           O  
ANISOU 3652  OD2 ASP B 216    19908   9876  15475   1358  -4876   4289       O  
ATOM   3653  N   GLY B 217      -5.416  23.143 -47.209  1.00 91.54           N  
ANISOU 3653  N   GLY B 217    15280   7657  11843   1359  -4213   3537       N  
ATOM   3654  CA  GLY B 217      -4.637  21.918 -47.197  1.00 86.29           C  
ANISOU 3654  CA  GLY B 217    14408   7386  10991   1076  -4015   3468       C  
ATOM   3655  C   GLY B 217      -3.756  21.763 -48.421  1.00 87.67           C  
ANISOU 3655  C   GLY B 217    14749   7629  10930    704  -4036   3715       C  
ATOM   3656  O   GLY B 217      -3.462  20.644 -48.844  1.00 84.17           O  
ANISOU 3656  O   GLY B 217    14153   7515  10311    475  -3881   3689       O  
ATOM   3657  N   THR B 218      -3.331  22.888 -48.991  1.00 93.16           N  
ANISOU 3657  N   THR B 218    15763   8011  11621    651  -4220   3961       N  
ATOM   3658  CA  THR B 218      -2.505  22.869 -50.195  1.00 95.53           C  
ANISOU 3658  CA  THR B 218    16235   8373  11687    314  -4253   4238       C  
ATOM   3659  C   THR B 218      -1.177  23.595 -49.999  1.00 96.53           C  
ANISOU 3659  C   THR B 218    16598   8288  11789    -14  -4176   4310       C  
ATOM   3660  O   THR B 218      -0.223  23.367 -50.743  1.00 96.64           O  
ANISOU 3660  O   THR B 218    16650   8470  11597   -350  -4086   4465       O  
ATOM   3661  CB  THR B 218      -3.238  23.494 -51.396  1.00101.73           C  
ANISOU 3661  CB  THR B 218    17221   8993  12440    429  -4531   4532       C  
ATOM   3662  OG1 THR B 218      -3.451  24.889 -51.151  1.00105.81           O  
ANISOU 3662  OG1 THR B 218    17995   9046  13162    577  -4670   4575       O  
ATOM   3663  CG2 THR B 218      -4.577  22.811 -51.622  1.00101.37           C  
ANISOU 3663  CG2 THR B 218    16925   9166  12425    738  -4639   4481       C  
ATOM   3664  N   HIS B 219      -1.118  24.463 -48.994  1.00 97.61           N  
ANISOU 3664  N   HIS B 219    16890   8062  12134     83  -4210   4195       N  
ATOM   3665  CA  HIS B 219       0.087  25.243 -48.728  1.00 99.89           C  
ANISOU 3665  CA  HIS B 219    17447   8080  12428   -228  -4200   4289       C  
ATOM   3666  C   HIS B 219       1.199  24.366 -48.161  1.00 94.98           C  
ANISOU 3666  C   HIS B 219    16648   7716  11723   -522  -3952   4141       C  
ATOM   3667  O   HIS B 219       0.987  23.640 -47.190  1.00 90.32           O  
ANISOU 3667  O   HIS B 219    15852   7250  11217   -393  -3818   3853       O  
ATOM   3668  CB  HIS B 219      -0.219  26.394 -47.769  1.00103.14           C  
ANISOU 3668  CB  HIS B 219    18110   7994  13083    -23  -4335   4192       C  
ATOM   3669  CG  HIS B 219       0.789  27.500 -47.812  1.00107.13           C  
ANISOU 3669  CG  HIS B 219    18947   8152  13606   -334  -4398   4339       C  
ATOM   3670  ND1 HIS B 219       0.550  28.701 -48.445  1.00111.30           N  
ANISOU 3670  ND1 HIS B 219    19727   8287  14272   -220  -4539   4380       N  
ATOM   3671  CD2 HIS B 219       2.041  27.586 -47.304  1.00106.45           C  
ANISOU 3671  CD2 HIS B 219    18895   8128  13423   -760  -4284   4399       C  
ATOM   3672  CE1 HIS B 219       1.610  29.480 -48.322  1.00113.04           C  
ANISOU 3672  CE1 HIS B 219    20138   8335  14477   -574  -4522   4460       C  
ATOM   3673  NE2 HIS B 219       2.529  28.827 -47.636  1.00110.17           N  
ANISOU 3673  NE2 HIS B 219    19633   8251  13975   -908  -4368   4474       N  
ATOM   3674  N   PRO B 220       2.393  24.434 -48.773  1.00 96.35           N  
ANISOU 3674  N   PRO B 220    16895   7984  11731   -915  -3889   4353       N  
ATOM   3675  CA  PRO B 220       3.565  23.635 -48.391  1.00 92.69           C  
ANISOU 3675  CA  PRO B 220    16257   7784  11178  -1225  -3663   4274       C  
ATOM   3676  C   PRO B 220       4.038  23.914 -46.967  1.00 90.56           C  
ANISOU 3676  C   PRO B 220    15987   7343  11076  -1242  -3610   4029       C  
ATOM   3677  O   PRO B 220       4.719  23.078 -46.372  1.00 85.82           O  
ANISOU 3677  O   PRO B 220    15142   7020  10446  -1324  -3422   3850       O  
ATOM   3678  CB  PRO B 220       4.637  24.087 -49.390  1.00 97.31           C  
ANISOU 3678  CB  PRO B 220    17036   8312  11626  -1616  -3682   4603       C  
ATOM   3679  CG  PRO B 220       3.871  24.609 -50.562  1.00102.08           C  
ANISOU 3679  CG  PRO B 220    17845   8771  12169  -1508  -3873   4850       C  
ATOM   3680  CD  PRO B 220       2.662  25.264 -49.961  1.00101.66           C  
ANISOU 3680  CD  PRO B 220    17776   8595  12257  -1059  -4023   4708       C  
ATOM   3681  N   GLY B 221       3.685  25.079 -46.434  1.00 94.35           N  
ANISOU 3681  N   GLY B 221    16759   7365  11723  -1165  -3780   4021       N  
ATOM   3682  CA  GLY B 221       4.069  25.448 -45.085  1.00 93.24           C  
ANISOU 3682  CA  GLY B 221    16682   7021  11723  -1192  -3759   3790       C  
ATOM   3683  C   GLY B 221       3.269  24.709 -44.029  1.00 87.97           C  
ANISOU 3683  C   GLY B 221    15784   6510  11131   -875  -3647   3446       C  
ATOM   3684  O   GLY B 221       3.696  24.598 -42.880  1.00 85.19           O  
ANISOU 3684  O   GLY B 221    15366   6189  10814   -956  -3550   3239       O  
ATOM   3685  N   GLY B 222       2.104  24.199 -44.421  1.00 86.92           N  
ANISOU 3685  N   GLY B 222    15524   6484  11020   -523  -3667   3397       N  
ATOM   3686  CA  GLY B 222       1.237  23.483 -43.504  1.00 82.36           C  
ANISOU 3686  CA  GLY B 222    14706   6076  10513   -218  -3554   3099       C  
ATOM   3687  C   GLY B 222       1.582  22.011 -43.400  1.00 76.51           C  
ANISOU 3687  C   GLY B 222    13616   5806   9649   -338  -3336   2996       C  
ATOM   3688  O   GLY B 222       0.943  21.265 -42.658  1.00 72.50           O  
ANISOU 3688  O   GLY B 222    12911   5447   9187   -158  -3218   2748       O  
ATOM   3689  N   LEU B 223       2.598  21.593 -44.148  1.00 90.26           N  
ANISOU 3689  N   LEU B 223    15287   7779  11229   -634  -3275   3189       N  
ATOM   3690  CA  LEU B 223       3.045  20.206 -44.130  1.00 85.71           C  
ANISOU 3690  CA  LEU B 223    14398   7634  10533   -746  -3070   3106       C  
ATOM   3691  C   LEU B 223       3.811  19.910 -42.846  1.00 83.60           C  
ANISOU 3691  C   LEU B 223    14056   7399  10310   -875  -2947   2912       C  
ATOM   3692  O   LEU B 223       4.948  20.348 -42.679  1.00 84.85           O  
ANISOU 3692  O   LEU B 223    14343   7434  10463  -1161  -2963   2993       O  
ATOM   3693  CB  LEU B 223       3.930  19.913 -45.342  1.00 72.85           C  
ANISOU 3693  CB  LEU B 223    12748   6216   8718  -1036  -3020   3355       C  
ATOM   3694  CG  LEU B 223       4.364  18.457 -45.507  1.00 68.59           C  
ANISOU 3694  CG  LEU B 223    11901   6119   8041  -1112  -2813   3287       C  
ATOM   3695  CD1 LEU B 223       3.149  17.568 -45.715  1.00 65.92           C  
ANISOU 3695  CD1 LEU B 223    11376   5961   7709   -807  -2805   3147       C  
ATOM   3696  CD2 LEU B 223       5.347  18.310 -46.658  1.00 70.81           C  
ANISOU 3696  CD2 LEU B 223    12199   6579   8125  -1385  -2755   3535       C  
ATOM   3697  N   VAL B 224       3.184  19.165 -41.941  1.00 67.81           N  
ANISOU 3697  N   VAL B 224    11843   5571   8350   -674  -2836   2668       N  
ATOM   3698  CA  VAL B 224       3.795  18.870 -40.649  1.00 65.14           C  
ANISOU 3698  CA  VAL B 224    11440   5266   8045   -757  -2735   2471       C  
ATOM   3699  C   VAL B 224       3.842  17.374 -40.350  1.00 60.33           C  
ANISOU 3699  C   VAL B 224    10501   5052   7371   -729  -2545   2339       C  
ATOM   3700  O   VAL B 224       3.081  16.588 -40.921  1.00 58.79           O  
ANISOU 3700  O   VAL B 224    10134   5062   7140   -567  -2499   2334       O  
ATOM   3701  CB  VAL B 224       3.053  19.583 -39.499  1.00 63.64           C  
ANISOU 3701  CB  VAL B 224    11406   4783   7991   -512  -2804   2261       C  
ATOM   3702  CG1 VAL B 224       3.072  21.094 -39.702  1.00 69.13           C  
ANISOU 3702  CG1 VAL B 224    12467   5036   8763   -568  -2995   2368       C  
ATOM   3703  CG2 VAL B 224       1.625  19.071 -39.387  1.00 62.29           C  
ANISOU 3703  CG2 VAL B 224    11100   4688   7881   -125  -2784   2145       C  
ATOM   3704  N   CYS B 225       4.744  16.994 -39.449  1.00 75.38           N  
ANISOU 3704  N   CYS B 225    12327   7050   9263   -895  -2451   2238       N  
ATOM   3705  CA  CYS B 225       4.852  15.617 -38.983  1.00 72.57           C  
ANISOU 3705  CA  CYS B 225    11684   7029   8862   -865  -2279   2106       C  
ATOM   3706  C   CYS B 225       3.957  15.418 -37.764  1.00 73.71           C  
ANISOU 3706  C   CYS B 225    11788   7136   9082   -596  -2248   1863       C  
ATOM   3707  O   CYS B 225       4.159  16.043 -36.723  1.00 76.16           O  
ANISOU 3707  O   CYS B 225    12257   7237   9445   -585  -2296   1743       O  
ATOM   3708  CB  CYS B 225       6.304  15.284 -38.638  1.00 68.90           C  
ANISOU 3708  CB  CYS B 225    11139   6690   8349  -1163  -2204   2133       C  
ATOM   3709  SG  CYS B 225       6.569  13.595 -38.052  1.00 65.08           S  
ANISOU 3709  SG  CYS B 225    10318   6597   7813  -1139  -2003   2001       S  
ATOM   3710  N   THR B 226       2.970  14.539 -37.902  1.00 46.57           N  
ANISOU 3710  N   THR B 226     8144   3909   5640   -390  -2163   1789       N  
ATOM   3711  CA  THR B 226       1.936  14.368 -36.889  1.00 44.85           C  
ANISOU 3711  CA  THR B 226     7867   3677   5495   -114  -2120   1584       C  
ATOM   3712  C   THR B 226       1.396  12.937 -36.933  1.00 41.69           C  
ANISOU 3712  C   THR B 226     7173   3602   5068    -15  -1988   1526       C  
ATOM   3713  O   THR B 226       1.586  12.231 -37.929  1.00 41.43           O  
ANISOU 3713  O   THR B 226     7023   3749   4969   -102  -1969   1643       O  
ATOM   3714  CB  THR B 226       0.781  15.372 -37.133  1.00 55.83           C  
ANISOU 3714  CB  THR B 226     9419   4807   6987    143  -2248   1587       C  
ATOM   3715  OG1 THR B 226      -0.103  15.401 -36.005  1.00 58.16           O  
ANISOU 3715  OG1 THR B 226     9684   5060   7354    408  -2189   1377       O  
ATOM   3716  CG2 THR B 226      -0.004  14.999 -38.384  1.00 56.04           C  
ANISOU 3716  CG2 THR B 226     9335   4949   7010    246  -2299   1726       C  
ATOM   3717  N   PRO B 227       0.750  12.485 -35.842  1.00 59.25           N  
ANISOU 3717  N   PRO B 227     9287   5899   7329    153  -1893   1342       N  
ATOM   3718  CA  PRO B 227       0.031  11.210 -35.919  1.00 57.65           C  
ANISOU 3718  CA  PRO B 227     8814   5968   7122    262  -1785   1294       C  
ATOM   3719  C   PRO B 227      -1.066  11.275 -36.978  1.00 58.54           C  
ANISOU 3719  C   PRO B 227     8864   6093   7287    435  -1868   1373       C  
ATOM   3720  O   PRO B 227      -1.914  12.168 -36.935  1.00 61.65           O  
ANISOU 3720  O   PRO B 227     9351   6303   7772    642  -1953   1354       O  
ATOM   3721  CB  PRO B 227      -0.590  11.078 -34.528  1.00 51.45           C  
ANISOU 3721  CB  PRO B 227     7976   5196   6374    426  -1684   1098       C  
ATOM   3722  CG  PRO B 227       0.334  11.827 -33.639  1.00 54.62           C  
ANISOU 3722  CG  PRO B 227     8647   5300   6804    466  -1760   1030       C  
ATOM   3723  CD  PRO B 227       0.827  12.989 -34.458  1.00 53.33           C  
ANISOU 3723  CD  PRO B 227     8654   5009   6598    203  -1866   1175       C  
ATOM   3724  N   ILE B 228      -1.040  10.339 -37.921  1.00 61.66           N  
ANISOU 3724  N   ILE B 228     9108   6699   7623    355  -1853   1459       N  
ATOM   3725  CA  ILE B 228      -2.001  10.326 -39.018  1.00 62.24           C  
ANISOU 3725  CA  ILE B 228     9123   6807   7719    475  -1960   1553       C  
ATOM   3726  C   ILE B 228      -3.103   9.297 -38.798  1.00 62.48           C  
ANISOU 3726  C   ILE B 228     8893   7040   7808    632  -1900   1462       C  
ATOM   3727  O   ILE B 228      -3.772   8.879 -39.743  1.00 62.57           O  
ANISOU 3727  O   ILE B 228     8807   7139   7829    698  -1989   1534       O  
ATOM   3728  CB  ILE B 228      -1.313  10.035 -40.362  1.00 44.43           C  
ANISOU 3728  CB  ILE B 228     6902   4646   5334    275  -2006   1714       C  
ATOM   3729  CG1 ILE B 228      -0.475   8.758 -40.259  1.00 41.57           C  
ANISOU 3729  CG1 ILE B 228     6394   4519   4881    107  -1854   1667       C  
ATOM   3730  CG2 ILE B 228      -0.451  11.214 -40.783  1.00 46.77           C  
ANISOU 3730  CG2 ILE B 228     7450   4736   5586    127  -2088   1848       C  
ATOM   3731  CD1 ILE B 228       0.226   8.374 -41.545  1.00 42.45           C  
ANISOU 3731  CD1 ILE B 228     6540   4741   4848    -76  -1861   1801       C  
ATOM   3732  N   VAL B 229      -3.287   8.888 -37.549  1.00 54.34           N  
ANISOU 3732  N   VAL B 229     7751   6086   6809    676  -1757   1314       N  
ATOM   3733  CA  VAL B 229      -4.307   7.904 -37.217  1.00 54.87           C  
ANISOU 3733  CA  VAL B 229     7564   6349   6937    799  -1681   1236       C  
ATOM   3734  C   VAL B 229      -5.298   8.492 -36.211  1.00 58.78           C  
ANISOU 3734  C   VAL B 229     8018   6763   7554   1063  -1650   1132       C  
ATOM   3735  O   VAL B 229      -5.008   9.498 -35.559  1.00 60.86           O  
ANISOU 3735  O   VAL B 229     8474   6812   7838   1141  -1665   1084       O  
ATOM   3736  CB  VAL B 229      -3.675   6.609 -36.660  1.00 51.16           C  
ANISOU 3736  CB  VAL B 229     6971   6063   6404    655  -1521   1161       C  
ATOM   3737  CG1 VAL B 229      -3.405   6.740 -35.164  1.00 47.59           C  
ANISOU 3737  CG1 VAL B 229     6541   5702   5839    428  -1530   1250       C  
ATOM   3738  CG2 VAL B 229      -4.554   5.406 -36.969  1.00 51.95           C  
ANISOU 3738  CG2 VAL B 229     7178   6076   6487    637  -1423   1056       C  
ATOM   3739  N   ASP B 230      -6.468   7.869 -36.096  1.00 51.79           N  
ANISOU 3739  N   ASP B 230     6883   6048   6748   1200  -1604   1095       N  
ATOM   3740  CA  ASP B 230      -7.516   8.356 -35.202  1.00 55.47           C  
ANISOU 3740  CA  ASP B 230     7261   6481   7333   1473  -1545   1000       C  
ATOM   3741  C   ASP B 230      -7.088   8.351 -33.733  1.00 56.82           C  
ANISOU 3741  C   ASP B 230     7497   6633   7461   1485  -1369    846       C  
ATOM   3742  O   ASP B 230      -6.127   7.677 -33.356  1.00 54.80           O  
ANISOU 3742  O   ASP B 230     7286   6437   7097   1276  -1294    823       O  
ATOM   3743  CB  ASP B 230      -8.807   7.552 -35.388  1.00 85.27           C  
ANISOU 3743  CB  ASP B 230    10711  10481  11204   1581  -1530   1016       C  
ATOM   3744  CG  ASP B 230      -8.580   6.055 -35.312  1.00 83.12           C  
ANISOU 3744  CG  ASP B 230    10266  10443  10871   1385  -1420    999       C  
ATOM   3745  OD1 ASP B 230      -8.316   5.442 -36.368  1.00 80.29           O  
ANISOU 3745  OD1 ASP B 230     9895  10160  10452   1203  -1506   1085       O  
ATOM   3746  OD2 ASP B 230      -8.670   5.493 -34.199  1.00 84.39           O  
ANISOU 3746  OD2 ASP B 230    10321  10706  11037   1415  -1246    899       O  
ATOM   3747  N   THR B 231      -7.818   9.103 -32.915  1.00 75.32           N  
ANISOU 3747  N   THR B 231     9844   8894   9880   1740  -1305    741       N  
ATOM   3748  CA  THR B 231      -7.470   9.306 -31.510  1.00 77.23           C  
ANISOU 3748  CA  THR B 231    10199   9089  10057   1778  -1150    582       C  
ATOM   3749  C   THR B 231      -7.409   8.004 -30.713  1.00 76.30           C  
ANISOU 3749  C   THR B 231     9898   9228   9867   1656   -976    534       C  
ATOM   3750  O   THR B 231      -6.517   7.818 -29.886  1.00 76.12           O  
ANISOU 3750  O   THR B 231    10004   9193   9726   1520   -902    465       O  
ATOM   3751  CB  THR B 231      -8.457  10.273 -30.825  1.00 85.18           C  
ANISOU 3751  CB  THR B 231    11222   9986  11156   2117  -1089    466       C  
ATOM   3752  OG1 THR B 231      -8.556  11.480 -31.591  1.00 86.24           O  
ANISOU 3752  OG1 THR B 231    11547   9851  11370   2242  -1265    521       O  
ATOM   3753  CG2 THR B 231      -7.992  10.611 -29.417  1.00 86.79           C  
ANISOU 3753  CG2 THR B 231    11600  10123  11254   2146   -939    287       C  
ATOM   3754  N   ALA B 232      -8.358   7.108 -30.964  1.00 76.77           N  
ANISOU 3754  N   ALA B 232     9657   9512   9997   1694   -928    581       N  
ATOM   3755  CA  ALA B 232      -8.407   5.831 -30.259  1.00 75.87           C  
ANISOU 3755  CA  ALA B 232     9361   9633   9832   1580   -769    555       C  
ATOM   3756  C   ALA B 232      -7.157   4.993 -30.521  1.00 72.95           C  
ANISOU 3756  C   ALA B 232     9074   9294   9348   1286   -793    606       C  
ATOM   3757  O   ALA B 232      -6.526   4.493 -29.587  1.00 72.76           O  
ANISOU 3757  O   ALA B 232     9095   9323   9226   1187   -679    548       O  
ATOM   3758  CB  ALA B 232      -9.659   5.057 -30.647  1.00 29.79           C  
ANISOU 3758  CB  ALA B 232     3193   4012   4114   1641   -751    621       C  
ATOM   3759  N   THR B 233      -6.807   4.851 -31.796  1.00 43.76           N  
ANISOU 3759  N   THR B 233     5400   5569   5659   1158   -941    717       N  
ATOM   3760  CA  THR B 233      -5.633   4.086 -32.199  1.00 40.11           C  
ANISOU 3760  CA  THR B 233     4998   5144   5100    904   -957    770       C  
ATOM   3761  C   THR B 233      -4.361   4.687 -31.607  1.00 39.37           C  
ANISOU 3761  C   THR B 233     5150   4898   4910    809   -962    734       C  
ATOM   3762  O   THR B 233      -3.470   3.961 -31.158  1.00 36.90           O  
ANISOU 3762  O   THR B 233     4858   4646   4516    639   -909    737       O  
ATOM   3763  CB  THR B 233      -5.502   4.020 -33.735  1.00 36.77           C  
ANISOU 3763  CB  THR B 233     4564   4723   4684    807  -1105    889       C  
ATOM   3764  OG1 THR B 233      -6.765   3.665 -34.314  1.00 38.21           O  
ANISOU 3764  OG1 THR B 233     4882   4732   4904    915  -1242    934       O  
ATOM   3765  CG2 THR B 233      -4.449   2.997 -34.140  1.00 34.96           C  
ANISOU 3765  CG2 THR B 233     4085   4672   4525    824  -1113    924       C  
ATOM   3766  N   LEU B 234      -4.288   6.015 -31.604  1.00 48.44           N  
ANISOU 3766  N   LEU B 234     6483   5842   6078    917  -1036    707       N  
ATOM   3767  CA  LEU B 234      -3.147   6.720 -31.030  1.00 47.79           C  
ANISOU 3767  CA  LEU B 234     6645   5595   5916    818  -1062    668       C  
ATOM   3768  C   LEU B 234      -3.026   6.429 -29.539  1.00 49.23           C  
ANISOU 3768  C   LEU B 234     6842   5835   6026    834   -925    540       C  
ATOM   3769  O   LEU B 234      -1.935   6.132 -29.042  1.00 46.82           O  
ANISOU 3769  O   LEU B 234     6622   5539   5629    659   -915    533       O  
ATOM   3770  CB  LEU B 234      -3.265   8.227 -31.265  1.00 41.98           C  
ANISOU 3770  CB  LEU B 234     6122   4600   5230    942  -1179    658       C  
ATOM   3771  CG  LEU B 234      -2.100   9.061 -30.724  1.00 41.80           C  
ANISOU 3771  CG  LEU B 234     6374   4372   5137    828  -1232    612       C  
ATOM   3772  CD1 LEU B 234      -0.791   8.626 -31.367  1.00 37.60           C  
ANISOU 3772  CD1 LEU B 234     5876   3872   4539    540  -1291    731       C  
ATOM   3773  CD2 LEU B 234      -2.339  10.548 -30.938  1.00 44.91           C  
ANISOU 3773  CD2 LEU B 234     6991   4477   5595    973  -1350    596       C  
ATOM   3774  N   LYS B 235      -4.154   6.517 -28.835  1.00 52.83           N  
ANISOU 3774  N   LYS B 235     7206   6346   6520   1047   -818    447       N  
ATOM   3775  CA  LYS B 235      -4.214   6.155 -27.424  1.00 53.89           C  
ANISOU 3775  CA  LYS B 235     7340   6572   6564   1078   -664    331       C  
ATOM   3776  C   LYS B 235      -3.677   4.745 -27.237  1.00 50.80           C  
ANISOU 3776  C   LYS B 235     6806   6385   6113    884   -596    392       C  
ATOM   3777  O   LYS B 235      -2.898   4.483 -26.324  1.00 49.63           O  
ANISOU 3777  O   LYS B 235     6744   6263   5850    779   -549    350       O  
ATOM   3778  CB  LYS B 235      -5.652   6.216 -26.900  1.00 51.72           C  
ANISOU 3778  CB  LYS B 235     6924   6379   6348   1340   -530    249       C  
ATOM   3779  CG  LYS B 235      -6.215   7.610 -26.693  1.00 54.61           C  
ANISOU 3779  CG  LYS B 235     7456   6531   6760   1583   -561    149       C  
ATOM   3780  CD  LYS B 235      -7.582   7.533 -26.024  1.00 56.81           C  
ANISOU 3780  CD  LYS B 235     7555   6933   7098   1857   -393     68       C  
ATOM   3781  CE  LYS B 235      -8.219   8.906 -25.862  1.00 59.47           C  
ANISOU 3781  CE  LYS B 235     8062   7043   7489   2139   -412    -44       C  
ATOM   3782  NZ  LYS B 235      -9.557   8.819 -25.208  1.00 61.33           N  
ANISOU 3782  NZ  LYS B 235     8091   7421   7790   2432   -225   -122       N  
ATOM   3783  N   VAL B 236      -4.092   3.842 -28.120  1.00 52.01           N  
ANISOU 3783  N   VAL B 236     6751   6669   6341    838   -606    493       N  
ATOM   3784  CA  VAL B 236      -3.672   2.448 -28.043  1.00 49.11           C  
ANISOU 3784  CA  VAL B 236     6255   6469   5936    668   -549    554       C  
ATOM   3785  C   VAL B 236      -2.157   2.278 -28.182  1.00 45.10           C  
ANISOU 3785  C   VAL B 236     5877   5909   5349    464   -617    600       C  
ATOM   3786  O   VAL B 236      -1.517   1.693 -27.310  1.00 43.43           O  
ANISOU 3786  O   VAL B 236     5678   5766   5055    370   -555    588       O  
ATOM   3787  CB  VAL B 236      -4.404   1.580 -29.087  1.00 33.42           C  
ANISOU 3787  CB  VAL B 236     4055   4597   4045    649   -575    642       C  
ATOM   3788  CG1 VAL B 236      -3.751   0.217 -29.198  1.00 30.01           C  
ANISOU 3788  CG1 VAL B 236     3551   4275   3576    461   -546    704       C  
ATOM   3789  CG2 VAL B 236      -5.874   1.442 -28.720  1.00 36.08           C  
ANISOU 3789  CG2 VAL B 236     4195   5048   4466    816   -484    614       C  
ATOM   3790  N   VAL B 237      -1.582   2.799 -29.263  1.00 55.12           N  
ANISOU 3790  N   VAL B 237     7236   7067   6643    397   -743    664       N  
ATOM   3791  CA  VAL B 237      -0.148   2.639 -29.500  1.00 51.04           C  
ANISOU 3791  CA  VAL B 237     6805   6524   6066    203   -798    725       C  
ATOM   3792  C   VAL B 237       0.700   3.332 -28.427  1.00 51.19           C  
ANISOU 3792  C   VAL B 237     6998   6449   6003    152   -813    661       C  
ATOM   3793  O   VAL B 237       1.741   2.808 -28.009  1.00 48.40           O  
ANISOU 3793  O   VAL B 237     6649   6153   5591      6   -810    690       O  
ATOM   3794  CB  VAL B 237       0.267   3.089 -30.930  1.00 37.13           C  
ANISOU 3794  CB  VAL B 237     5098   4678   4333    133   -914    822       C  
ATOM   3795  CG1 VAL B 237      -0.646   2.449 -31.970  1.00 36.81           C  
ANISOU 3795  CG1 VAL B 237     4903   4741   4343    160   -915    878       C  
ATOM   3796  CG2 VAL B 237       0.238   4.601 -31.069  1.00 39.52           C  
ANISOU 3796  CG2 VAL B 237     5575   4778   4662    218  -1012    803       C  
ATOM   3797  N   ILE B 238       0.240   4.494 -27.966  1.00 53.94           N  
ANISOU 3797  N   ILE B 238     7491   6654   6351    279   -837    569       N  
ATOM   3798  CA  ILE B 238       0.953   5.243 -26.937  1.00 54.74           C  
ANISOU 3798  CA  ILE B 238     7794   6643   6363    232   -870    485       C  
ATOM   3799  C   ILE B 238       0.920   4.497 -25.607  1.00 54.75           C  
ANISOU 3799  C   ILE B 238     7749   6789   6264    236   -754    416       C  
ATOM   3800  O   ILE B 238       1.932   4.409 -24.909  1.00 52.87           O  
ANISOU 3800  O   ILE B 238     7596   6558   5934     96   -791    412       O  
ATOM   3801  CB  ILE B 238       0.374   6.665 -26.757  1.00 60.03           C  
ANISOU 3801  CB  ILE B 238     8661   7094   7052    390   -920    383       C  
ATOM   3802  CG1 ILE B 238       0.713   7.537 -27.967  1.00 59.56           C  
ANISOU 3802  CG1 ILE B 238     8710   6855   7067    329  -1069    475       C  
ATOM   3803  CG2 ILE B 238       0.915   7.314 -25.493  1.00 61.22           C  
ANISOU 3803  CG2 ILE B 238     9030   7145   7087    364   -933    255       C  
ATOM   3804  CD1 ILE B 238       0.290   8.980 -27.815  1.00 61.07           C  
ANISOU 3804  CD1 ILE B 238     9114   6792   7297    491  -1138    390       C  
ATOM   3805  N   GLN B 239      -0.247   3.958 -25.265  1.00 54.33           N  
ANISOU 3805  N   GLN B 239     7555   6860   6229    387   -621    378       N  
ATOM   3806  CA  GLN B 239      -0.392   3.152 -24.059  1.00 54.52           C  
ANISOU 3806  CA  GLN B 239     7517   7044   6155    384   -494    342       C  
ATOM   3807  C   GLN B 239       0.503   1.923 -24.124  1.00 50.52           C  
ANISOU 3807  C   GLN B 239     6906   6661   5626    196   -506    455       C  
ATOM   3808  O   GLN B 239       1.154   1.573 -23.142  1.00 49.37           O  
ANISOU 3808  O   GLN B 239     6823   6565   5368    108   -500    446       O  
ATOM   3809  CB  GLN B 239      -1.846   2.721 -23.863  1.00 36.97           C  
ANISOU 3809  CB  GLN B 239     5117   4951   3980    556   -343    317       C  
ATOM   3810  CG  GLN B 239      -2.758   3.806 -23.319  1.00 41.66           C  
ANISOU 3810  CG  GLN B 239     5803   5463   4562    781   -279    180       C  
ATOM   3811  CD  GLN B 239      -4.222   3.425 -23.415  1.00 44.36           C  
ANISOU 3811  CD  GLN B 239     5914   5948   4994    953   -140    184       C  
ATOM   3812  OE1 GLN B 239      -4.569   2.244 -23.429  1.00 43.23           O  
ANISOU 3812  OE1 GLN B 239     5565   5986   4874    882    -62    267       O  
ATOM   3813  NE2 GLN B 239      -5.089   4.426 -23.494  1.00 47.16           N  
ANISOU 3813  NE2 GLN B 239     6292   6215   5411   1179   -115     99       N  
ATOM   3814  N   VAL B 240       0.531   1.273 -25.284  1.00 35.36           N  
ANISOU 3814  N   VAL B 240     4838   4788   3809    144   -528    559       N  
ATOM   3815  CA  VAL B 240       1.377   0.100 -25.478  1.00 31.70           C  
ANISOU 3815  CA  VAL B 240     4279   4422   3343     -6   -534    660       C  
ATOM   3816  C   VAL B 240       2.849   0.443 -25.258  1.00 29.33           C  
ANISOU 3816  C   VAL B 240     4096   4065   2984   -152   -637    690       C  
ATOM   3817  O   VAL B 240       3.573  -0.293 -24.581  1.00 27.87           O  
ANISOU 3817  O   VAL B 240     3884   3963   2742   -242   -629    731       O  
ATOM   3818  CB  VAL B 240       1.175  -0.529 -26.874  1.00 37.98           C  
ANISOU 3818  CB  VAL B 240     4940   5246   4245    -29   -552    744       C  
ATOM   3819  CG1 VAL B 240       2.252  -1.568 -27.156  1.00 34.88           C  
ANISOU 3819  CG1 VAL B 240     4482   4922   3849   -165   -559    833       C  
ATOM   3820  CG2 VAL B 240      -0.208  -1.155 -26.972  1.00 40.36           C  
ANISOU 3820  CG2 VAL B 240     5092   5635   4610     76   -466    732       C  
ATOM   3821  N   ASN B 241       3.282   1.571 -25.812  1.00 41.36           N  
ANISOU 3821  N   ASN B 241     5744   5444   4527   -182   -742    681       N  
ATOM   3822  CA  ASN B 241       4.655   2.021 -25.609  1.00 39.84           C  
ANISOU 3822  CA  ASN B 241     5650   5197   4292   -344   -851    717       C  
ATOM   3823  C   ASN B 241       4.959   2.352 -24.147  1.00 41.29           C  
ANISOU 3823  C   ASN B 241     5973   5365   4352   -367   -875    631       C  
ATOM   3824  O   ASN B 241       6.034   2.034 -23.641  1.00 39.97           O  
ANISOU 3824  O   ASN B 241     5808   5249   4132   -506   -938    679       O  
ATOM   3825  CB  ASN B 241       4.968   3.228 -26.495  1.00 50.43           C  
ANISOU 3825  CB  ASN B 241     7107   6373   5683   -389   -960    738       C  
ATOM   3826  CG  ASN B 241       6.392   3.725 -26.320  1.00 49.51           C  
ANISOU 3826  CG  ASN B 241     7071   6205   5536   -586  -1079    791       C  
ATOM   3827  OD1 ASN B 241       6.652   4.645 -25.543  1.00 51.43           O  
ANISOU 3827  OD1 ASN B 241     7501   6315   5727   -627  -1169    719       O  
ATOM   3828  ND2 ASN B 241       7.325   3.110 -27.040  1.00 47.11           N  
ANISOU 3828  ND2 ASN B 241     6625   6008   5268   -710  -1082    915       N  
ATOM   3829  N   THR B 242       4.005   2.989 -23.476  1.00 69.51           N  
ANISOU 3829  N   THR B 242     9661   8877   7874   -221   -824    502       N  
ATOM   3830  CA  THR B 242       4.172   3.380 -22.080  1.00 71.27           C  
ANISOU 3830  CA  THR B 242    10057   9076   7948   -223   -837    393       C  
ATOM   3831  C   THR B 242       4.279   2.158 -21.173  1.00 70.33           C  
ANISOU 3831  C   THR B 242     9843   9147   7733   -255   -758    429       C  
ATOM   3832  O   THR B 242       5.084   2.132 -20.242  1.00 70.07           O  
ANISOU 3832  O   THR B 242     9910   9137   7578   -362   -832    419       O  
ATOM   3833  CB  THR B 242       3.005   4.268 -21.608  1.00 74.22           C  
ANISOU 3833  CB  THR B 242    10565   9352   8285    -19   -762    235       C  
ATOM   3834  OG1 THR B 242       2.883   5.401 -22.478  1.00 75.43           O  
ANISOU 3834  OG1 THR B 242    10793   9317   8549     35   -837    223       O  
ATOM   3835  CG2 THR B 242       3.237   4.750 -20.185  1.00 75.93           C  
ANISOU 3835  CG2 THR B 242    11020   9508   8323    -29   -793     99       C  
ATOM   3836  N   PHE B 243       3.467   1.144 -21.454  1.00 56.91           N  
ANISOU 3836  N   PHE B 243     7955   7578   6089   -174   -625    481       N  
ATOM   3837  CA  PHE B 243       3.484  -0.087 -20.673  1.00 56.22           C  
ANISOU 3837  CA  PHE B 243     7777   7656   5927   -206   -547    539       C  
ATOM   3838  C   PHE B 243       4.733  -0.922 -20.946  1.00 53.10           C  
ANISOU 3838  C   PHE B 243     7289   7317   5569   -362   -637    677       C  
ATOM   3839  O   PHE B 243       5.377  -1.408 -20.017  1.00 52.76           O  
ANISOU 3839  O   PHE B 243     7289   7335   5420   -448   -688    710       O  
ATOM   3840  CB  PHE B 243       2.235  -0.930 -20.952  1.00 65.63           C  
ANISOU 3840  CB  PHE B 243     8796   8954   7184    -94   -387    563       C  
ATOM   3841  CG  PHE B 243       0.994  -0.434 -20.261  1.00 69.32           C  
ANISOU 3841  CG  PHE B 243     9315   9438   7586     70   -258    443       C  
ATOM   3842  CD1 PHE B 243       0.956  -0.312 -18.883  1.00 70.80           C  
ANISOU 3842  CD1 PHE B 243     9634   9681   7586     90   -197    371       C  
ATOM   3843  CD2 PHE B 243      -0.144  -0.120 -20.987  1.00 71.42           C  
ANISOU 3843  CD2 PHE B 243     9489   9677   7971    211   -194    407       C  
ATOM   3844  CE1 PHE B 243      -0.183   0.132 -18.244  1.00 73.94           C  
ANISOU 3844  CE1 PHE B 243    10071  10108   7912    259    -48    254       C  
ATOM   3845  CE2 PHE B 243      -1.287   0.325 -20.352  1.00 74.90           C  
ANISOU 3845  CE2 PHE B 243     9944  10147   8365    384    -60    301       C  
ATOM   3846  CZ  PHE B 243      -1.306   0.451 -18.979  1.00 75.95           C  
ANISOU 3846  CZ  PHE B 243    10210  10339   8309    413     27    220       C  
ATOM   3847  N   MET B 244       5.075  -1.083 -22.221  1.00 41.63           N  
ANISOU 3847  N   MET B 244     5709   5848   4262   -389   -655    756       N  
ATOM   3848  CA  MET B 244       6.150  -1.995 -22.610  1.00 39.41           C  
ANISOU 3848  CA  MET B 244     5308   5632   4034   -497   -702    884       C  
ATOM   3849  C   MET B 244       7.558  -1.420 -22.455  1.00 38.67           C  
ANISOU 3849  C   MET B 244     5276   5503   3913   -638   -851    922       C  
ATOM   3850  O   MET B 244       8.508  -2.161 -22.202  1.00 37.98           O  
ANISOU 3850  O   MET B 244     5105   5498   3826   -718   -897   1019       O  
ATOM   3851  CB  MET B 244       5.942  -2.500 -24.042  1.00 67.75           C  
ANISOU 3851  CB  MET B 244     8761   9218   7763   -475   -662    942       C  
ATOM   3852  CG  MET B 244       4.767  -3.452 -24.197  1.00 68.54           C  
ANISOU 3852  CG  MET B 244     8758   9377   7906   -381   -541    939       C  
ATOM   3853  SD  MET B 244       4.850  -4.855 -23.066  1.00 69.07           S  
ANISOU 3853  SD  MET B 244     8770   9561   7912   -397   -472   1003       S  
ATOM   3854  CE  MET B 244       3.521  -4.455 -21.932  1.00 71.58           C  
ANISOU 3854  CE  MET B 244     9152   9912   8132   -296   -365    904       C  
ATOM   3855  N   SER B 245       7.696  -0.108 -22.607  1.00 67.15           N  
ANISOU 3855  N   SER B 245     9021   8982   7508   -671   -935    854       N  
ATOM   3856  CA  SER B 245       9.015   0.514 -22.558  1.00 66.86           C  
ANISOU 3856  CA  SER B 245     9032   8905   7464   -837  -1089    901       C  
ATOM   3857  C   SER B 245       9.327   1.160 -21.211  1.00 68.49           C  
ANISOU 3857  C   SER B 245     9426   9074   7522   -902  -1194    819       C  
ATOM   3858  O   SER B 245      10.476   1.507 -20.937  1.00 68.66           O  
ANISOU 3858  O   SER B 245     9476   9085   7526  -1065  -1344    866       O  
ATOM   3859  CB  SER B 245       9.165   1.549 -23.676  1.00 64.00           C  
ANISOU 3859  CB  SER B 245     8712   8414   7192   -883  -1142    911       C  
ATOM   3860  OG  SER B 245       8.250   2.619 -23.507  1.00 64.32           O  
ANISOU 3860  OG  SER B 245     8796   8412   7230  -1069  -1293    964       O  
ATOM   3861  N   PHE B 246       8.310   1.321 -20.370  1.00 55.90           N  
ANISOU 3861  N   PHE B 246     7958   7466   5813   -781  -1116    696       N  
ATOM   3862  CA  PHE B 246       8.498   2.014 -19.098  1.00 57.77           C  
ANISOU 3862  CA  PHE B 246     8417   7657   5876   -828  -1207    589       C  
ATOM   3863  C   PHE B 246       7.998   1.222 -17.889  1.00 58.63           C  
ANISOU 3863  C   PHE B 246     8550   7900   5825   -755  -1113    559       C  
ATOM   3864  O   PHE B 246       8.797   0.654 -17.148  1.00 58.27           O  
ANISOU 3864  O   PHE B 246     8490   7958   5692   -858  -1197    632       O  
ATOM   3865  CB  PHE B 246       7.843   3.399 -19.140  1.00 51.59           C  
ANISOU 3865  CB  PHE B 246     7858   6675   5069   -757  -1223    429       C  
ATOM   3866  CG  PHE B 246       8.146   4.251 -17.939  1.00 53.67           C  
ANISOU 3866  CG  PHE B 246     8392   6853   5148   -819  -1335    296       C  
ATOM   3867  CD1 PHE B 246       9.385   4.856 -17.796  1.00 53.63           C  
ANISOU 3867  CD1 PHE B 246     8472   6785   5120  -1039  -1550    331       C  
ATOM   3868  CD2 PHE B 246       7.189   4.455 -16.960  1.00 55.96           C  
ANISOU 3868  CD2 PHE B 246     8852   7132   5280   -661  -1226    134       C  
ATOM   3869  CE1 PHE B 246       9.665   5.643 -16.693  1.00 55.68           C  
ANISOU 3869  CE1 PHE B 246     9004   6954   5197  -1114  -1678    197       C  
ATOM   3870  CE2 PHE B 246       7.461   5.241 -15.856  1.00 57.91           C  
ANISOU 3870  CE2 PHE B 246     9380   7293   5329   -713  -1328     -9       C  
ATOM   3871  CZ  PHE B 246       8.701   5.836 -15.722  1.00 57.70           C  
ANISOU 3871  CZ  PHE B 246     9460   7187   5276   -946  -1566     18       C  
ATOM   3872  N   LEU B 247       6.682   1.190 -17.699  1.00 51.50           N  
ANISOU 3872  N   LEU B 247     7675   7006   4886   -579   -942    465       N  
ATOM   3873  CA  LEU B 247       6.071   0.608 -16.501  1.00 52.87           C  
ANISOU 3873  CA  LEU B 247     7897   7306   4884   -510   -829    430       C  
ATOM   3874  C   LEU B 247       6.514  -0.824 -16.185  1.00 51.36           C  
ANISOU 3874  C   LEU B 247     7541   7284   4690   -576   -815    597       C  
ATOM   3875  O   LEU B 247       7.132  -1.075 -15.149  1.00 51.76           O  
ANISOU 3875  O   LEU B 247     7676   7411   4582   -659   -893    628       O  
ATOM   3876  CB  LEU B 247       4.543   0.676 -16.597  1.00 50.87           C  
ANISOU 3876  CB  LEU B 247     7624   7065   4638   -307   -619    336       C  
ATOM   3877  CG  LEU B 247       3.944   2.084 -16.635  1.00 53.71           C  
ANISOU 3877  CG  LEU B 247     8197   7285   4924   -178   -587    138       C  
ATOM   3878  CD1 LEU B 247       2.429   2.028 -16.713  1.00 54.76           C  
ANISOU 3878  CD1 LEU B 247     8605   7386   4813   -243   -679     24       C  
ATOM   3879  CD2 LEU B 247       4.387   2.883 -15.419  1.00 53.73           C  
ANISOU 3879  CD2 LEU B 247     8223   7095   5096   -170   -684    111       C  
ATOM   3880  N   PHE B 248       6.194  -1.751 -17.081  1.00 65.09           N  
ANISOU 3880  N   PHE B 248     9062   9068   6601   -538   -729    703       N  
ATOM   3881  CA  PHE B 248       6.498  -3.171 -16.888  1.00 64.05           C  
ANISOU 3881  CA  PHE B 248     8781   9064   6493   -574   -700    858       C  
ATOM   3882  C   PHE B 248       7.996  -3.488 -16.676  1.00 63.05           C  
ANISOU 3882  C   PHE B 248     8628   8971   6358   -715   -879    975       C  
ATOM   3883  O   PHE B 248       8.367  -4.061 -15.638  1.00 63.74           O  
ANISOU 3883  O   PHE B 248     8757   9152   6310   -757   -918   1041       O  
ATOM   3884  CB  PHE B 248       5.887  -3.999 -18.033  1.00 95.69           C  
ANISOU 3884  CB  PHE B 248    12587  13073  10697   -512   -594    924       C  
ATOM   3885  CG  PHE B 248       6.129  -5.478 -17.924  1.00 95.07           C  
ANISOU 3885  CG  PHE B 248    12374  13083  10663   -536   -558   1073       C  
ATOM   3886  CD1 PHE B 248       5.390  -6.252 -17.045  1.00 96.20           C  
ANISOU 3886  CD1 PHE B 248    12534  13319  10697   -511   -455   1110       C  
ATOM   3887  CD2 PHE B 248       7.074  -6.098 -18.725  1.00 93.72           C  
ANISOU 3887  CD2 PHE B 248    12067  12897  10644   -577   -617   1177       C  
ATOM   3888  CE1 PHE B 248       5.602  -7.612 -16.953  1.00 95.93           C  
ANISOU 3888  CE1 PHE B 248    12397  13337  10715   -538   -433   1257       C  
ATOM   3889  CE2 PHE B 248       7.291  -7.459 -18.638  1.00 93.78           C  
ANISOU 3889  CE2 PHE B 248    11971  12955  10704   -580   -587   1304       C  
ATOM   3890  CZ  PHE B 248       6.553  -8.216 -17.750  1.00 94.83           C  
ANISOU 3890  CZ  PHE B 248    12136  13155  10738   -565   -504   1348       C  
ATOM   3891  N   PRO B 249       8.864  -3.101 -17.635  1.00 56.21           N  
ANISOU 3891  N   PRO B 249     7688   8041   5629   -789   -991   1013       N  
ATOM   3892  CA  PRO B 249      10.272  -3.482 -17.474  1.00 55.82           C  
ANISOU 3892  CA  PRO B 249     7558   8052   5598   -910  -1146   1144       C  
ATOM   3893  C   PRO B 249      10.950  -2.806 -16.282  1.00 57.09           C  
ANISOU 3893  C   PRO B 249     7890   8225   5574  -1023  -1316   1107       C  
ATOM   3894  O   PRO B 249      11.798  -3.429 -15.642  1.00 57.48           O  
ANISOU 3894  O   PRO B 249     7893   8372   5575  -1095  -1428   1222       O  
ATOM   3895  CB  PRO B 249      10.910  -3.014 -18.786  1.00 32.57           C  
ANISOU 3895  CB  PRO B 249     4498   5044   2831   -963  -1197   1177       C  
ATOM   3896  CG  PRO B 249      10.062  -1.892 -19.231  1.00 31.32           C  
ANISOU 3896  CG  PRO B 249     4468   4758   2675   -920  -1152   1036       C  
ATOM   3897  CD  PRO B 249       8.664  -2.272 -18.839  1.00 30.26           C  
ANISOU 3897  CD  PRO B 249     4386   4638   2474   -774   -987    954       C  
ATOM   3898  N   MET B 250      10.586  -1.561 -15.987  1.00 46.55           N  
ANISOU 3898  N   MET B 250     6763   6787   4138  -1036  -1346    947       N  
ATOM   3899  CA  MET B 250      11.163  -0.865 -14.840  1.00 48.06           C  
ANISOU 3899  CA  MET B 250     7161   6968   4131  -1151  -1517    882       C  
ATOM   3900  C   MET B 250      10.613  -1.397 -13.521  1.00 49.36           C  
ANISOU 3900  C   MET B 250     7457   7236   4062  -1097  -1456    854       C  
ATOM   3901  O   MET B 250      11.269  -1.300 -12.486  1.00 50.39           O  
ANISOU 3901  O   MET B 250     7703   7423   4019  -1205  -1614    872       O  
ATOM   3902  CB  MET B 250      10.952   0.647 -14.932  1.00 56.74           C  
ANISOU 3902  CB  MET B 250     8476   7891   5194  -1178  -1573    707       C  
ATOM   3903  CG  MET B 250      11.833   1.337 -15.955  1.00 56.03           C  
ANISOU 3903  CG  MET B 250     8305   7705   5281  -1312  -1709    761       C  
ATOM   3904  SD  MET B 250      13.589   1.015 -15.702  1.00 56.05           S  
ANISOU 3904  SD  MET B 250     8165   7826   5308  -1539  -1955    940       S  
ATOM   3905  CE  MET B 250      13.925  -0.138 -17.033  1.00 53.99           C  
ANISOU 3905  CE  MET B 250     7540   7665   5309  -1483  -1840   1133       C  
ATOM   3906  N   LEU B 251       9.407  -1.955 -13.561  1.00 53.01           N  
ANISOU 3906  N   LEU B 251     7902   7730   4512   -940  -1231    817       N  
ATOM   3907  CA  LEU B 251       8.838  -2.599 -12.385  1.00 54.36           C  
ANISOU 3907  CA  LEU B 251     8166   8022   4469   -891  -1136    824       C  
ATOM   3908  C   LEU B 251       9.650  -3.855 -12.088  1.00 53.66           C  
ANISOU 3908  C   LEU B 251     7932   8058   4400   -959  -1215   1038       C  
ATOM   3909  O   LEU B 251      10.094  -4.078 -10.950  1.00 54.89           O  
ANISOU 3909  O   LEU B 251     8204   8303   4348  -1027  -1314   1085       O  
ATOM   3910  CB  LEU B 251       7.371  -2.953 -12.628  1.00 68.58           C  
ANISOU 3910  CB  LEU B 251     9918   9841   6296   -724   -871    769       C  
ATOM   3911  CG  LEU B 251       6.439  -2.950 -11.416  1.00 70.58           C  
ANISOU 3911  CG  LEU B 251    10289  10218   6308   -661   -720    744       C  
ATOM   3912  CD1 LEU B 251       6.560  -1.641 -10.658  1.00 72.59           C  
ANISOU 3912  CD1 LEU B 251    10843  10459   6279   -697   -809    593       C  
ATOM   3913  CD2 LEU B 251       5.003  -3.178 -11.860  1.00 71.50           C  
ANISOU 3913  CD2 LEU B 251    10330  10345   6492   -500   -464    672       C  
ATOM   3914  N   VAL B 252       9.851  -4.662 -13.130  1.00 44.80           N  
ANISOU 3914  N   VAL B 252     6568   6932   3520   -935  -1179   1165       N  
ATOM   3915  CA  VAL B 252      10.679  -5.861 -13.025  1.00 44.48           C  
ANISOU 3915  CA  VAL B 252     6378   6980   3540   -972  -1254   1370       C  
ATOM   3916  C   VAL B 252      12.078  -5.530 -12.505  1.00 45.34           C  
ANISOU 3916  C   VAL B 252     6510   7128   3590  -1111  -1515   1439       C  
ATOM   3917  O   VAL B 252      12.563  -6.145 -11.550  1.00 47.77           O  
ANISOU 3917  O   VAL B 252     6847   7535   3769  -1153  -1616   1557       O  
ATOM   3918  CB  VAL B 252      10.803  -6.580 -14.386  1.00 34.57           C  
ANISOU 3918  CB  VAL B 252     4881   5688   2567   -916  -1183   1462       C  
ATOM   3919  CG1 VAL B 252      11.793  -7.733 -14.294  1.00 36.05           C  
ANISOU 3919  CG1 VAL B 252     4921   5942   2836   -939  -1285   1662       C  
ATOM   3920  CG2 VAL B 252       9.442  -7.072 -14.852  1.00 32.43           C  
ANISOU 3920  CG2 VAL B 252     4572   5398   2354   -801   -955   1426       C  
ATOM   3921  N   ALA B 253      12.712  -4.545 -13.133  1.00 52.45           N  
ANISOU 3921  N   ALA B 253     7395   7952   4579  -1194  -1633   1376       N  
ATOM   3922  CA  ALA B 253      14.057  -4.123 -12.756  1.00 53.22           C  
ANISOU 3922  CA  ALA B 253     7479   8087   4653  -1353  -1895   1445       C  
ATOM   3923  C   ALA B 253      14.108  -3.597 -11.324  1.00 54.96           C  
ANISOU 3923  C   ALA B 253     7965   8342   4575  -1445  -2038   1368       C  
ATOM   3924  O   ALA B 253      15.106  -3.776 -10.628  1.00 56.82           O  
ANISOU 3924  O   ALA B 253     8187   8665   4734  -1561  -2257   1477       O  
ATOM   3925  CB  ALA B 253      14.576  -3.072 -13.727  1.00 42.58           C  
ANISOU 3925  CB  ALA B 253     6069   6644   3468  -1440  -1970   1395       C  
ATOM   3926  N   SER B 254      13.032  -2.949 -10.890  1.00 70.61           N  
ANISOU 3926  N   SER B 254    10185  10259   6383  -1384  -1915   1179       N  
ATOM   3927  CA  SER B 254      12.955  -2.423  -9.530  1.00 72.60           C  
ANISOU 3927  CA  SER B 254    10733  10530   6319  -1455  -2024   1066       C  
ATOM   3928  C   SER B 254      12.919  -3.558  -8.514  1.00 73.62           C  
ANISOU 3928  C   SER B 254    10913  10813   6246  -1413  -1975   1172       C  
ATOM   3929  O   SER B 254      13.680  -3.559  -7.540  1.00 75.67           O  
ANISOU 3929  O   SER B 254    11371  11141   6239  -1505  -2130   1160       O  
ATOM   3930  CB  SER B 254      11.722  -1.534  -9.365  1.00 54.65           C  
ANISOU 3930  CB  SER B 254     8704   8127   3933  -1377  -1889    813       C  
ATOM   3931  OG  SER B 254      11.740  -0.464 -10.293  1.00 52.86           O  
ANISOU 3931  OG  SER B 254     8426   7919   3737  -1189  -1596    782       O  
ATOM   3932  N   ILE B 255      12.028  -4.520  -8.746  1.00 57.02           N  
ANISOU 3932  N   ILE B 255     8645   8759   4261  -1285  -1769   1280       N  
ATOM   3933  CA  ILE B 255      11.936  -5.693  -7.880  1.00 57.92           C  
ANISOU 3933  CA  ILE B 255     8782   9007   4217  -1259  -1727   1427       C  
ATOM   3934  C   ILE B 255      13.278  -6.417  -7.807  1.00 58.49           C  
ANISOU 3934  C   ILE B 255     8701   9154   4368  -1348  -1965   1653       C  
ATOM   3935  O   ILE B 255      13.804  -6.687  -6.715  1.00 61.30           O  
ANISOU 3935  O   ILE B 255     9177   9615   4501  -1422  -2122   1745       O  
ATOM   3936  CB  ILE B 255      10.867  -6.681  -8.383  1.00 47.45           C  
ANISOU 3936  CB  ILE B 255     7319   7689   3022  -1118  -1449   1487       C  
ATOM   3937  CG1 ILE B 255       9.490  -6.016  -8.406  1.00 46.12           C  
ANISOU 3937  CG1 ILE B 255     7290   7491   2742  -1018  -1209   1287       C  
ATOM   3938  CG2 ILE B 255      10.839  -7.927  -7.513  1.00 49.60           C  
ANISOU 3938  CG2 ILE B 255     7572   8076   3197  -1117  -1442   1697       C  
ATOM   3939  CD1 ILE B 255       8.412  -6.882  -9.019  1.00 43.49           C  
ANISOU 3939  CD1 ILE B 255     6794   7165   2567   -900   -950   1338       C  
ATOM   3940  N   LEU B 256      13.832  -6.711  -8.980  1.00 66.61           N  
ANISOU 3940  N   LEU B 256     9464  10135   5709  -1333  -1992   1744       N  
ATOM   3941  CA  LEU B 256      15.112  -7.404  -9.078  1.00 66.85           C  
ANISOU 3941  CA  LEU B 256     9296  10234   5868  -1381  -2194   1959       C  
ATOM   3942  C   LEU B 256      16.223  -6.670  -8.330  1.00 68.10           C  
ANISOU 3942  C   LEU B 256     9534  10450   5891  -1553  -2504   1967       C  
ATOM   3943  O   LEU B 256      16.978  -7.285  -7.582  1.00 69.23           O  
ANISOU 3943  O   LEU B 256     9627  10700   5978  -1601  -2698   2145       O  
ATOM   3944  CB  LEU B 256      15.500  -7.622 -10.543  1.00 49.20           C  
ANISOU 3944  CB  LEU B 256     6773   7939   3982  -1323  -2137   2016       C  
ATOM   3945  CG  LEU B 256      14.636  -8.624 -11.313  1.00 46.15           C  
ANISOU 3945  CG  LEU B 256     6275   7502   3758  -1167  -1883   2053       C  
ATOM   3946  CD1 LEU B 256      15.164  -8.831 -12.726  1.00 43.91           C  
ANISOU 3946  CD1 LEU B 256     5737   7165   3782  -1117  -1846   2092       C  
ATOM   3947  CD2 LEU B 256      14.556  -9.944 -10.570  1.00 47.97           C  
ANISOU 3947  CD2 LEU B 256     6506   7796   3924  -1111  -1877   2236       C  
ATOM   3948  N   ASN B 257      16.308  -5.357  -8.520  1.00 55.92           N  
ANISOU 3948  N   ASN B 257     8121   8828   4298  -1651  -2567   1780       N  
ATOM   3949  CA  ASN B 257      17.315  -4.551  -7.832  1.00 59.90           C  
ANISOU 3949  CA  ASN B 257     8725   9366   4670  -1846  -2878   1767       C  
ATOM   3950  C   ASN B 257      17.127  -4.510  -6.317  1.00 63.84           C  
ANISOU 3950  C   ASN B 257     9525   9944   4786  -1903  -2985   1730       C  
ATOM   3951  O   ASN B 257      18.103  -4.443  -5.566  1.00 68.06           O  
ANISOU 3951  O   ASN B 257    10097  10567   5199  -2052  -3279   1816       O  
ATOM   3952  CB  ASN B 257      17.365  -3.132  -8.404  1.00 59.06           C  
ANISOU 3952  CB  ASN B 257     8702   9118   4620  -1948  -2919   1575       C  
ATOM   3953  CG  ASN B 257      18.120  -3.062  -9.717  1.00 57.30           C  
ANISOU 3953  CG  ASN B 257     8166   8867   4737  -1985  -2950   1672       C  
ATOM   3954  OD1 ASN B 257      19.287  -2.670  -9.754  1.00 60.01           O  
ANISOU 3954  OD1 ASN B 257     8395   9255   5151  -2155  -3200   1758       O  
ATOM   3955  ND2 ASN B 257      17.459  -3.451 -10.802  1.00 53.09           N  
ANISOU 3955  ND2 ASN B 257     7488   8272   4410  -1833  -2696   1665       N  
ATOM   3956  N   THR B 258      15.875  -4.547  -5.870  1.00 62.75           N  
ANISOU 3956  N   THR B 258     9599   9789   4454  -1788  -2746   1607       N  
ATOM   3957  CA  THR B 258      15.589  -4.620  -4.440  1.00 66.53           C  
ANISOU 3957  CA  THR B 258    10370  10363   4544  -1818  -2789   1579       C  
ATOM   3958  C   THR B 258      16.120  -5.932  -3.863  1.00 68.79           C  
ANISOU 3958  C   THR B 258    10540  10799   4797  -1811  -2890   1857       C  
ATOM   3959  O   THR B 258      16.837  -5.943  -2.849  1.00 73.42           O  
ANISOU 3959  O   THR B 258    11255  11490   5152  -1932  -3148   1937       O  
ATOM   3960  CB  THR B 258      14.079  -4.512  -4.156  1.00 64.80           C  
ANISOU 3960  CB  THR B 258    10346  10117   4156  -1671  -2458   1412       C  
ATOM   3961  OG1 THR B 258      13.594  -3.239  -4.603  1.00 63.12           O  
ANISOU 3961  OG1 THR B 258    10261   9754   3969  -1655  -2378   1153       O  
ATOM   3962  CG2 THR B 258      13.804  -4.658  -2.665  1.00 69.13           C  
ANISOU 3962  CG2 THR B 258    11198  10790   4278  -1698  -2475   1396       C  
ATOM   3963  N   VAL B 259      15.772  -7.035  -4.522  1.00 66.22           N  
ANISOU 3963  N   VAL B 259     9983  10472   4706  -1672  -2700   2006       N  
ATOM   3964  CA  VAL B 259      16.246  -8.350  -4.096  1.00 68.20           C  
ANISOU 3964  CA  VAL B 259    10115  10825   4972  -1641  -2781   2284       C  
ATOM   3965  C   VAL B 259      17.775  -8.406  -4.090  1.00 71.11           C  
ANISOU 3965  C   VAL B 259    10308  11255   5453  -1748  -3130   2448       C  
ATOM   3966  O   VAL B 259      18.383  -8.955  -3.168  1.00 75.30           O  
ANISOU 3966  O   VAL B 259    10888  11901   5819  -1803  -3345   2623       O  
ATOM   3967  CB  VAL B 259      15.687  -9.474  -4.989  1.00 64.01           C  
ANISOU 3967  CB  VAL B 259     9354  10236   4729  -1479  -2536   2397       C  
ATOM   3968  CG1 VAL B 259      16.146 -10.830  -4.482  1.00 66.35           C  
ANISOU 3968  CG1 VAL B 259     9534  10601   5073  -1440  -2644   2689       C  
ATOM   3969  CG2 VAL B 259      14.170  -9.411  -5.030  1.00 61.75           C  
ANISOU 3969  CG2 VAL B 259     9211   9916   4335  -1389  -2207   2266       C  
ATOM   3970  N   ILE B 260      18.387  -7.823  -5.117  1.00 86.80           N  
ANISOU 3970  N   ILE B 260    12085  13176   7719  -1783  -3187   2399       N  
ATOM   3971  CA  ILE B 260      19.841  -7.739  -5.211  1.00 87.68           C  
ANISOU 3971  CA  ILE B 260    11983  13357   7973  -1895  -3500   2543       C  
ATOM   3972  C   ILE B 260      20.423  -6.958  -4.035  1.00 89.51           C  
ANISOU 3972  C   ILE B 260    12444  13670   7896  -2097  -3816   2501       C  
ATOM   3973  O   ILE B 260      21.464  -7.326  -3.490  1.00 90.95           O  
ANISOU 3973  O   ILE B 260    12523  13973   8059  -2176  -4106   2695       O  
ATOM   3974  CB  ILE B 260      20.282  -7.089  -6.542  1.00 68.63           C  
ANISOU 3974  CB  ILE B 260     9335  10861   5881  -1920  -3467   2471       C  
ATOM   3975  CG1 ILE B 260      19.978  -8.023  -7.713  1.00 64.99           C  
ANISOU 3975  CG1 ILE B 260     8581  10362   5749  -1732  -3249   2585       C  
ATOM   3976  CG2 ILE B 260      21.765  -6.765  -6.524  1.00 72.36           C  
ANISOU 3976  CG2 ILE B 260     9648  11417   6430  -2102  -3809   2565       C  
ATOM   3977  CD1 ILE B 260      20.196  -7.390  -9.068  1.00 61.72           C  
ANISOU 3977  CD1 ILE B 260     7984   9862   5606  -1734  -3142   2491       C  
ATOM   3978  N   ALA B 261      19.738  -5.888  -3.641  1.00 76.71           N  
ANISOU 3978  N   ALA B 261    11140  11977   6032  -2174  -3765   2245       N  
ATOM   3979  CA  ALA B 261      20.159  -5.096  -2.490  1.00 81.85           C  
ANISOU 3979  CA  ALA B 261    12073  12678   6349  -2369  -4053   2159       C  
ATOM   3980  C   ALA B 261      20.148  -5.937  -1.216  1.00 85.97           C  
ANISOU 3980  C   ALA B 261    12764  13349   6553  -2366  -4160   2307       C  
ATOM   3981  O   ALA B 261      21.122  -5.941  -0.453  1.00 90.99           O  
ANISOU 3981  O   ALA B 261    13416  14098   7059  -2515  -4510   2430       O  
ATOM   3982  CB  ALA B 261      19.270  -3.873  -2.331  1.00 81.03           C  
ANISOU 3982  CB  ALA B 261    12307  12439   6043  -2402  -3924   1834       C  
ATOM   3983  N   ASN B 262      19.047  -6.652  -0.993  1.00 84.20           N  
ANISOU 3983  N   ASN B 262    12661  13131   6203  -2206  -3866   2307       N  
ATOM   3984  CA  ASN B 262      18.952  -7.546   0.161  1.00 88.13           C  
ANISOU 3984  CA  ASN B 262    13335  13766   6383  -2199  -3930   2465       C  
ATOM   3985  C   ASN B 262      20.070  -8.590   0.176  1.00 90.38           C  
ANISOU 3985  C   ASN B 262    13345  14154   6842  -2190  -4165   2805       C  
ATOM   3986  O   ASN B 262      20.748  -8.783   1.194  1.00 95.75           O  
ANISOU 3986  O   ASN B 262    14133  14964   7286  -2297  -4466   2948       O  
ATOM   3987  CB  ASN B 262      17.585  -8.232   0.203  1.00 96.57           C  
ANISOU 3987  CB  ASN B 262    14524  14820   7347  -2034  -3538   2432       C  
ATOM   3988  CG  ASN B 262      16.450  -7.255   0.442  1.00100.65           C  
ANISOU 3988  CG  ASN B 262    15288  15481   7473  -2050  -3573   2570       C  
ATOM   3989  OD1 ASN B 262      16.626  -6.232   1.105  1.00105.75           O  
ANISOU 3989  OD1 ASN B 262    16095  16232   7850  -2190  -3887   2630       O  
ATOM   3990  ND2 ASN B 262      15.276  -7.568  -0.096  1.00 99.19           N  
ANISOU 3990  ND2 ASN B 262    15133  15305   7247  -1920  -3256   2631       N  
ATOM   3991  N   LYS B 263      20.262  -9.249  -0.964  1.00 87.10           N  
ANISOU 3991  N   LYS B 263    12579  13675   6838  -2055  -4037   2929       N  
ATOM   3992  CA  LYS B 263      21.317 -10.246  -1.116  1.00 88.97           C  
ANISOU 3992  CA  LYS B 263    12529  13984   7292  -1997  -4221   3242       C  
ATOM   3993  C   LYS B 263      22.697  -9.644  -0.872  1.00 93.02           C  
ANISOU 3993  C   LYS B 263    12894  14590   7859  -2162  -4628   3318       C  
ATOM   3994  O   LYS B 263      23.611 -10.335  -0.427  1.00 97.15           O  
ANISOU 3994  O   LYS B 263    13302  15229   8384  -2171  -4896   3569       O  
ATOM   3995  CB  LYS B 263      21.265 -10.875  -2.511  1.00 87.04           C  
ANISOU 3995  CB  LYS B 263    11960  13633   7478  -1812  -3979   3307       C  
ATOM   3996  CG  LYS B 263      20.022 -11.706  -2.781  1.00 88.64           C  
ANISOU 3996  CG  LYS B 263    11931  13871   7878  -1678  -4066   3622       C  
ATOM   3997  CD  LYS B 263      19.955 -12.918  -1.868  1.00 85.91           C  
ANISOU 3997  CD  LYS B 263    11629  13428   7584  -1507  -3751   3683       C  
ATOM   3998  CE  LYS B 263      18.767 -13.804  -2.213  1.00 87.54           C  
ANISOU 3998  CE  LYS B 263    12207  13676   7378  -1560  -3650   3641       C  
ATOM   3999  NZ  LYS B 263      17.472 -13.078  -2.086  1.00 86.73           N  
ANISOU 3999  NZ  LYS B 263    12129  13511   7313  -1428  -3432   3801       N  
ATOM   4000  N   LEU B 264      22.841  -8.355  -1.168  1.00 91.45           N  
ANISOU 4000  N   LEU B 264    12695  14336   7715  -2295  -4675   3106       N  
ATOM   4001  CA  LEU B 264      24.102  -7.654  -0.957  1.00 95.55           C  
ANISOU 4001  CA  LEU B 264    13089  14936   8277  -2499  -5060   3151       C  
ATOM   4002  C   LEU B 264      24.340  -7.405   0.526  1.00100.09           C  
ANISOU 4002  C   LEU B 264    13956  15579   8494  -2630  -5289   3113       C  
ATOM   4003  O   LEU B 264      25.459  -7.562   1.016  1.00102.96           O  
ANISOU 4003  O   LEU B 264    14157  16018   8946  -2690  -5545   3245       O  
ATOM   4004  CB  LEU B 264      24.120  -6.330  -1.724  1.00 93.18           C  
ANISOU 4004  CB  LEU B 264    12773  14520   8111  -2621  -5016   2910       C  
ATOM   4005  CG  LEU B 264      25.402  -5.503  -1.596  1.00 97.05           C  
ANISOU 4005  CG  LEU B 264    13114  15066   8695  -2869  -5383   2932       C  
ATOM   4006  CD1 LEU B 264      26.598  -6.276  -2.132  1.00100.47           C  
ANISOU 4006  CD1 LEU B 264    13919  15467   8788  -3069  -5576   2732       C  
ATOM   4007  CD2 LEU B 264      25.259  -4.168  -2.308  1.00 98.76           C  
ANISOU 4007  CD2 LEU B 264    12915  15406   9203  -2815  -5547   3215       C  
ATOM   4008  N   THR B 265      23.285  -7.010   1.236  1.00100.50           N  
ANISOU 4008  N   THR B 265    14432  15597   8158  -2658  -5167   2911       N  
ATOM   4009  CA  THR B 265      23.370  -6.829   2.683  1.00104.47           C  
ANISOU 4009  CA  THR B 265    15243  16153   8298  -2751  -5324   2844       C  
ATOM   4010  C   THR B 265      23.752  -8.146   3.356  1.00106.41           C  
ANISOU 4010  C   THR B 265    15400  16507   8523  -2641  -5392   3120       C  
ATOM   4011  O   THR B 265      24.663  -8.196   4.195  1.00110.09           O  
ANISOU 4011  O   THR B 265    15875  17048   8908  -2727  -5662   3193       O  
ATOM   4012  CB  THR B 265      22.038  -6.328   3.270  1.00114.32           C  
ANISOU 4012  CB  THR B 265    16956  17356   9126  -2750  -5111   2583       C  
ATOM   4013  OG1 THR B 265      21.687  -5.075   2.670  1.00112.83           O  
ANISOU 4013  OG1 THR B 265    16869  17040   8961  -2839  -5057   2320       O  
ATOM   4014  CG2 THR B 265      22.152  -6.150   4.777  1.00118.59           C  
ANISOU 4014  CG2 THR B 265    17821  17959   9280  -2843  -5273   2502       C  
ATOM   4015  N   VAL B 266      23.056  -9.213   2.975  1.00104.11           N  
ANISOU 4015  N   VAL B 266    15022  16214   8322  -2454  -5157   3281       N  
ATOM   4016  CA  VAL B 266      23.373 -10.544   3.480  1.00105.87           C  
ANISOU 4016  CA  VAL B 266    15162  16504   8560  -2335  -5208   3557       C  
ATOM   4017  C   VAL B 266      24.821 -10.908   3.157  1.00107.31           C  
ANISOU 4017  C   VAL B 266    14952  16729   9091  -2328  -5481   3763       C  
ATOM   4018  O   VAL B 266      25.534 -11.457   3.997  1.00110.84           O  
ANISOU 4018  O   VAL B 266    15398  17255   9463  -2343  -5704   3905       O  
ATOM   4019  CB  VAL B 266      22.426 -11.610   2.894  1.00103.09           C  
ANISOU 4019  CB  VAL B 266    14768  16106   8294  -2143  -4901   3698       C  
ATOM   4020  CG1 VAL B 266      22.848 -13.003   3.332  1.00104.33           C  
ANISOU 4020  CG1 VAL B 266    14696  16280   8662  -2001  -4991   4016       C  
ATOM   4021  CG2 VAL B 266      20.990 -11.329   3.308  1.00103.40           C  
ANISOU 4021  CG2 VAL B 266    15207  16158   7920  -2141  -4660   3581       C  
ATOM   4022  N   MET B 267      25.256 -10.573   1.946  1.00104.84           N  
ANISOU 4022  N   MET B 267    14306  16375   9153  -2305  -5461   3776       N  
ATOM   4023  CA  MET B 267      26.605 -10.902   1.494  1.00106.05           C  
ANISOU 4023  CA  MET B 267    14043  16580   9674  -2266  -5662   3977       C  
ATOM   4024  C   MET B 267      27.701 -10.181   2.271  1.00109.59           C  
ANISOU 4024  C   MET B 267    14447  17103  10091  -2476  -5991   3925       C  
ATOM   4025  O   MET B 267      28.741 -10.769   2.559  1.00112.21           O  
ANISOU 4025  O   MET B 267    14515  17516  10604  -2451  -6205   4119       O  
ATOM   4026  CB  MET B 267      26.763 -10.629  -0.002  1.00102.55           C  
ANISOU 4026  CB  MET B 267    13251  16083   9629  -2161  -5502   4011       C  
ATOM   4027  CG  MET B 267      26.886 -11.885  -0.844  1.00102.91           C  
ANISOU 4027  CG  MET B 267    13007  16162   9933  -2297  -5658   3962       C  
ATOM   4028  SD  MET B 267      27.491 -11.527  -2.501  1.00100.45           S  
ANISOU 4028  SD  MET B 267    12177  15846  10143  -2092  -5518   4139       S  
ATOM   4029  CE  MET B 267      28.992 -10.630  -2.114  1.00101.25           C  
ANISOU 4029  CE  MET B 267    12024  15999  10450  -2321  -5679   4039       C  
ATOM   4030  N   VAL B 268      27.484  -8.911   2.601  1.00110.06           N  
ANISOU 4030  N   VAL B 268    14765  17127   9925  -2679  -6036   3664       N  
ATOM   4031  CA  VAL B 268      28.479  -8.176   3.377  1.00113.90           C  
ANISOU 4031  CA  VAL B 268    15274  17667  10336  -2900  -6356   3606       C  
ATOM   4032  C   VAL B 268      28.458  -8.627   4.836  1.00117.75           C  
ANISOU 4032  C   VAL B 268    16041  18230  10470  -2917  -6509   3654       C  
ATOM   4033  O   VAL B 268      29.497  -8.644   5.504  1.00121.65           O  
ANISOU 4033  O   VAL B 268    16470  18806  10947  -3038  -6811   3724       O  
ATOM   4034  CB  VAL B 268      28.323  -6.636   3.261  1.00113.46           C  
ANISOU 4034  CB  VAL B 268    15425  17517  10168  -3119  -6375   3306       C  
ATOM   4035  CG1 VAL B 268      28.452  -6.197   1.809  1.00109.89           C  
ANISOU 4035  CG1 VAL B 268    14690  16996  10067  -3109  -6232   3278       C  
ATOM   4036  CG2 VAL B 268      27.004  -6.166   3.850  1.00113.02           C  
ANISOU 4036  CG2 VAL B 268    15872  17390   9681  -3125  -6205   3064       C  
ATOM   4037  N   HIS B 269      27.280  -9.013   5.321  1.00149.39           N  
ANISOU 4037  N   HIS B 269    20355  22217  14188  -2801  -6297   3626       N  
ATOM   4038  CA  HIS B 269      27.179  -9.577   6.664  1.00153.25           C  
ANISOU 4038  CA  HIS B 269    21080  22790  14357  -2782  -6408   3722       C  
ATOM   4039  C   HIS B 269      27.896 -10.923   6.749  1.00154.56           C  
ANISOU 4039  C   HIS B 269    20945  23018  14763  -2613  -6493   4059       C  
ATOM   4040  O   HIS B 269      28.408 -11.297   7.804  1.00157.95           O  
ANISOU 4040  O   HIS B 269    21497  23525  14993  -2594  -6640   4195       O  
ATOM   4041  CB  HIS B 269      25.719  -9.708   7.098  1.00122.04           C  
ANISOU 4041  CB  HIS B 269    17550  18811  10011  -2721  -6134   3591       C  
ATOM   4042  CG  HIS B 269      25.135  -8.436   7.630  1.00122.71           C  
ANISOU 4042  CG  HIS B 269    18002  18851   9772  -2879  -6101   3254       C  
ATOM   4043  ND1 HIS B 269      25.907  -7.341   7.946  1.00120.62           N  
ANISOU 4043  ND1 HIS B 269    17696  18485   9651  -2977  -6064   3041       N  
ATOM   4044  CD2 HIS B 269      23.855  -8.087   7.901  1.00125.53           C  
ANISOU 4044  CD2 HIS B 269    18785  19243   9669  -2945  -6099   3091       C  
ATOM   4045  CE1 HIS B 269      25.129  -6.369   8.390  1.00122.11           C  
ANISOU 4045  CE1 HIS B 269    18278  18629   9492  -3091  -6044   2754       C  
ATOM   4046  NE2 HIS B 269      23.880  -6.796   8.372  1.00125.12           N  
ANISOU 4046  NE2 HIS B 269    18944  19098   9498  -3068  -6058   2772       N  
ATOM   4047  N   GLN B 270      27.932 -11.646   5.634  1.00118.64           N  
ANISOU 4047  N   GLN B 270    16013  18429  10637  -2479  -6396   4190       N  
ATOM   4048  CA  GLN B 270      28.695 -12.886   5.550  1.00119.86           C  
ANISOU 4048  CA  GLN B 270    15836  18625  11083  -2306  -6494   4493       C  
ATOM   4049  C   GLN B 270      30.180 -12.575   5.402  1.00122.30           C  
ANISOU 4049  C   GLN B 270    15782  19017  11670  -2397  -6786   4570       C  
ATOM   4050  O   GLN B 270      31.035 -13.337   5.851  1.00124.89           O  
ANISOU 4050  O   GLN B 270    15869  19412  12172  -2292  -6955   4808       O  
ATOM   4051  CB  GLN B 270      28.229 -13.730   4.362  1.00115.91           C  
ANISOU 4051  CB  GLN B 270    15120  18029  10890  -2080  -6212   4598       C  
ATOM   4052  CG  GLN B 270      26.823 -14.288   4.493  1.00113.71           C  
ANISOU 4052  CG  GLN B 270    15150  17670  10385  -1982  -5916   4568       C  
ATOM   4053  CD  GLN B 270      26.349 -14.964   3.220  1.00109.84           C  
ANISOU 4053  CD  GLN B 270    14449  17073  10212  -1786  -5649   4650       C  
ATOM   4054  OE1 GLN B 270      25.192 -15.372   3.113  1.00107.76           O  
ANISOU 4054  OE1 GLN B 270    14384  16734   9824  -1712  -5388   4633       O  
ATOM   4055  NE2 GLN B 270      27.243 -15.083   2.245  1.00109.12           N  
ANISOU 4055  NE2 GLN B 270    13948  16980  10532  -1702  -5705   4741       N  
ATOM   4056  N   ALA B 271      30.474 -11.446   4.767  1.00121.94           N  
ANISOU 4056  N   ALA B 271    15696  18963  11673  -2594  -6838   4374       N  
ATOM   4057  CA  ALA B 271      31.848 -11.045   4.493  1.00124.31           C  
ANISOU 4057  CA  ALA B 271    15650  19345  12238  -2719  -7094   4436       C  
ATOM   4058  C   ALA B 271      32.534 -10.527   5.748  1.00129.64           C  
ANISOU 4058  C   ALA B 271    16413  20132  12714  -2837  -7438   4520       C  
ATOM   4059  O   ALA B 271      33.762 -10.513   5.832  1.00132.43           O  
ANISOU 4059  O   ALA B 271    16433  20584  13301  -2789  -7641   4735       O  
ATOM   4060  CB  ALA B 271      31.882  -9.991   3.393  1.00122.61           C  
ANISOU 4060  CB  ALA B 271    15452  19075  12060  -2938  -7077   4197       C  
ATOM   4061  N   ALA B 272      31.737 -10.097   6.720  1.00131.96           N  
ANISOU 4061  N   ALA B 272    17157  20413  12568  -2981  -7498   4347       N  
ATOM   4062  CA  ALA B 272      32.276  -9.617   7.988  1.00137.07           C  
ANISOU 4062  CA  ALA B 272    17960  21164  12956  -3070  -7799   4427       C  
ATOM   4063  C   ALA B 272      32.951 -10.738   8.781  1.00137.89           C  
ANISOU 4063  C   ALA B 272    18029  21306  13055  -2824  -7763   4690       C  
ATOM   4064  O   ALA B 272      33.753 -10.477   9.677  1.00134.44           O  
ANISOU 4064  O   ALA B 272    17614  20788  12677  -2627  -7472   4734       O  
ATOM   4065  CB  ALA B 272      31.181  -8.963   8.817  1.00137.47           C  
ANISOU 4065  CB  ALA B 272    18532  21184  12516  -3244  -7815   4166       C  
ATOM   4066  N   PHE B 291      32.625 -11.983   8.444  1.00141.66           N  
ANISOU 4066  N   PHE B 291    18454  21899  13472  -2842  -8066   4871       N  
ATOM   4067  CA  PHE B 291      33.174 -13.137   9.149  1.00143.25           C  
ANISOU 4067  CA  PHE B 291    18582  22134  13714  -2612  -8091   5156       C  
ATOM   4068  C   PHE B 291      33.933 -14.075   8.213  1.00141.39           C  
ANISOU 4068  C   PHE B 291    17863  21874  13987  -2380  -8003   5365       C  
ATOM   4069  O   PHE B 291      34.227 -15.215   8.575  1.00142.56           O  
ANISOU 4069  O   PHE B 291    17914  22018  14234  -2160  -8010   5606       O  
ATOM   4070  CB  PHE B 291      32.061 -13.903   9.868  1.00141.89           C  
ANISOU 4070  CB  PHE B 291    18821  21895  13198  -2504  -7847   5134       C  
ATOM   4071  CG  PHE B 291      31.360 -13.102  10.929  1.00143.52           C  
ANISOU 4071  CG  PHE B 291    19512  22126  12895  -2701  -7870   4901       C  
ATOM   4072  CD1 PHE B 291      30.313 -12.257  10.600  1.00140.10           C  
ANISOU 4072  CD1 PHE B 291    19335  21605  12293  -2768  -7601   4624       C  
ATOM   4073  CD2 PHE B 291      31.748 -13.194  12.256  1.00148.75           C  
ANISOU 4073  CD2 PHE B 291    20379  22900  13239  -2804  -8157   4957       C  
ATOM   4074  CE1 PHE B 291      29.666 -11.520  11.573  1.00141.89           C  
ANISOU 4074  CE1 PHE B 291    20013  21851  12050  -2922  -7603   4396       C  
ATOM   4075  CE2 PHE B 291      31.105 -12.459  13.234  1.00150.53           C  
ANISOU 4075  CE2 PHE B 291    21062  23150  12985  -2970  -8164   4731       C  
ATOM   4076  CZ  PHE B 291      30.062 -11.620  12.891  1.00147.13           C  
ANISOU 4076  CZ  PHE B 291    20883  22626  12395  -3021  -7879   4445       C  
ATOM   4077  N   ASN B 292      34.244 -13.585   7.015  1.00138.75           N  
ANISOU 4077  N   ASN B 292    17239  21515  13965  -2427  -7916   5268       N  
ATOM   4078  CA  ASN B 292      34.979 -14.354   6.012  1.00137.34           C  
ANISOU 4078  CA  ASN B 292    16574  21332  14276  -2224  -7831   5436       C  
ATOM   4079  C   ASN B 292      34.291 -15.674   5.662  1.00134.46           C  
ANISOU 4079  C   ASN B 292    16201  20852  14037  -1920  -7552   5563       C  
ATOM   4080  O   ASN B 292      34.922 -16.731   5.655  1.00135.87           O  
ANISOU 4080  O   ASN B 292    16101  21039  14487  -1694  -7591   5796       O  
ATOM   4081  CB  ASN B 292      36.426 -14.596   6.466  1.00134.40           C  
ATOM   4082  CG  ASN B 292      37.348 -14.977   5.319  1.00134.40           C  
ATOM   4083  OD1 ASN B 292      38.204 -14.191   4.911  1.00134.40           O  
ATOM   4084  ND2 ASN B 292      37.187 -16.191   4.802  1.00134.40           N  
ATOM   4085  N   MET B 293      32.995 -15.606   5.376  1.00130.65           N  
ANISOU 4085  N   MET B 293    16024  20253  13364  -1915  -7270   5408       N  
ATOM   4086  CA  MET B 293      32.232 -16.794   5.011  1.00127.93           C  
ANISOU 4086  CA  MET B 293    15708  19781  13117  -1659  -6996   5515       C  
ATOM   4087  C   MET B 293      31.650 -16.675   3.607  1.00122.84           C  
ANISOU 4087  C   MET B 293    14954  19036  12682  -1609  -6687   5374       C  
ATOM   4088  O   MET B 293      30.545 -17.149   3.340  1.00119.81           O  
ANISOU 4088  O   MET B 293    14825  18548  12151  -1566  -6429   5291       O  
ATOM   4089  CB  MET B 293      31.117 -17.056   6.026  1.00128.32           C  
ANISOU 4089  CB  MET B 293    16229  19785  12741  -1673  -6912   5500       C  
ATOM   4090  CG  MET B 293      31.615 -17.462   7.405  1.00133.40           C  
ANISOU 4090  CG  MET B 293    17069  20541  13078  -1773  -7212   5588       C  
ATOM   4091  SD  MET B 293      30.273 -17.848   8.545  1.00133.94           S  
ANISOU 4091  SD  MET B 293    17679  20567  12645  -1773  -7060   5584       S  
ATOM   4092  CE  MET B 293      29.387 -16.292   8.561  1.00132.37           C  
ANISOU 4092  CE  MET B 293    17349  20217  12729  -1457  -6849   5850       C  
ATOM   4093  N   THR B 294      32.401 -16.038   2.714  1.00122.20           N  
ANISOU 4093  N   THR B 294    14489  18997  12942  -1618  -6710   5357       N  
ATOM   4094  CA  THR B 294      31.978 -15.880   1.327  1.00117.70           C  
ANISOU 4094  CA  THR B 294    13790  18348  12581  -1577  -6435   5231       C  
ATOM   4095  C   THR B 294      33.163 -15.591   0.407  1.00117.95           C  
ANISOU 4095  C   THR B 294    13316  18441  13056  -1493  -6458   5315       C  
ATOM   4096  O   THR B 294      34.302 -15.936   0.720  1.00121.38           O  
ANISOU 4096  O   THR B 294    13483  18961  13676  -1399  -6644   5503       O  
ATOM   4097  CB  THR B 294      30.917 -14.768   1.178  1.00 90.45           C  
ATOM   4098  OG1 THR B 294      30.594 -14.593  -0.207  1.00 90.45           O  
ATOM   4099  CG2 THR B 294      31.430 -13.453   1.748  1.00 90.45           C  
ATOM   4100  N   ILE B 295      32.881 -14.957  -0.726  1.00115.05           N  
ANISOU 4100  N   ILE B 295    12819  18039  12855  -1522  -6259   5179       N  
ATOM   4101  CA  ILE B 295      33.901 -14.652  -1.725  1.00115.21           C  
ANISOU 4101  CA  ILE B 295    12368  18132  13274  -1464  -6240   5237       C  
ATOM   4102  C   ILE B 295      34.922 -13.622  -1.245  1.00118.59           C  
ANISOU 4102  C   ILE B 295    12648  18707  13704  -1720  -6521   5217       C  
ATOM   4103  O   ILE B 295      34.775 -13.033  -0.174  1.00120.22           O  
ANISOU 4103  O   ILE B 295    13154  18934  13592  -1954  -6710   5117       O  
ATOM   4104  CB  ILE B 295      33.261 -14.158  -3.035  1.00 94.73           C  
ATOM   4105  CG1 ILE B 295      32.228 -13.070  -2.739  1.00 94.73           C  
ATOM   4106  CG2 ILE B 295      32.610 -15.314  -3.777  1.00 94.73           C  
ATOM   4107  CD1 ILE B 295      31.402 -12.663  -3.938  1.00 94.73           C  
ATOM   4108  N   GLU B 296      35.958 -13.416  -2.054  1.00220.61           N  
ANISOU 4108  N   GLU B 296    25114  31730  26980  -1676  -6540   5312       N  
ATOM   4109  CA  GLU B 296      37.035 -12.486  -1.730  1.00224.07           C  
ANISOU 4109  CA  GLU B 296    25363  32311  27464  -1927  -6796   5317       C  
ATOM   4110  C   GLU B 296      36.536 -11.043  -1.677  1.00222.54           C  
ANISOU 4110  C   GLU B 296    25415  32076  27064  -2259  -6813   5075       C  
ATOM   4111  O   GLU B 296      35.608 -10.682  -2.400  1.00218.50           O  
ANISOU 4111  O   GLU B 296    25015  31463  26543  -2262  -6571   4926       O  
ATOM   4112  CB  GLU B 296      38.175 -12.617  -2.746  1.00175.01           C  
ATOM   4113  CG  GLU B 296      38.988 -13.900  -2.622  1.00175.01           C  
ATOM   4114  CD  GLU B 296      38.257 -15.119  -3.155  1.00175.01           C  
ATOM   4115  OE1 GLU B 296      37.241 -14.946  -3.860  1.00175.01           O  
ATOM   4116  OE2 GLU B 296      38.701 -16.251  -2.868  1.00175.01           O  
ATOM   4117  N   PRO B 297      37.153 -10.217  -0.813  1.00148.20           N  
ANISOU 4117  N   PRO B 297    16092  22730  17487  -2534  -7107   5038       N  
ATOM   4118  CA  PRO B 297      36.778  -8.810  -0.622  1.00147.03           C  
ANISOU 4118  CA  PRO B 297    16267  22513  17085  -2855  -7172   4797       C  
ATOM   4119  C   PRO B 297      36.703  -8.011  -1.922  1.00143.55           C  
ANISOU 4119  C   PRO B 297    15682  22028  16833  -2972  -6993   4675       C  
ATOM   4120  O   PRO B 297      35.781  -7.213  -2.087  1.00140.18           O  
ANISOU 4120  O   PRO B 297    15572  21468  16220  -3070  -6863   4462       O  
ATOM   4121  CB  PRO B 297      37.907  -8.272   0.259  1.00100.74           C  
ATOM   4122  CG  PRO B 297      38.351  -9.450   1.042  1.00100.74           C  
ATOM   4123  CD  PRO B 297      38.233 -10.622   0.106  1.00100.74           C  
ATOM   4124  N   GLY B 298      37.657  -8.221  -2.825  1.00147.48           N  
ANISOU 4124  N   GLY B 298    15705  22639  17691  -2960  -6984   4811       N  
ATOM   4125  CA  GLY B 298      37.685  -7.503  -4.088  1.00144.68           C  
ANISOU 4125  CA  GLY B 298    15184  22262  17527  -3081  -6818   4724       C  
ATOM   4126  C   GLY B 298      36.460  -7.774  -4.940  1.00138.71           C  
ANISOU 4126  C   GLY B 298    14571  21375  16758  -2923  -6487   4603       C  
ATOM   4127  O   GLY B 298      35.864  -6.854  -5.508  1.00136.27           O  
ANISOU 4127  O   GLY B 298    14420  20967  16387  -3094  -6393   4426       O  
ATOM   4128  N   ARG B 299      36.085  -9.047  -5.023  1.00113.73           N  
ANISOU 4128  N   ARG B 299    11361  18199  13653  -2596  -6322   4702       N  
ATOM   4129  CA  ARG B 299      34.899  -9.460  -5.761  1.00109.07           C  
ANISOU 4129  CA  ARG B 299    10915  17486  13041  -2424  -6019   4607       C  
ATOM   4130  C   ARG B 299      33.645  -8.840  -5.151  1.00107.15           C  
ANISOU 4130  C   ARG B 299    11208  17101  12402  -2549  -6023   4395       C  
ATOM   4131  O   ARG B 299      32.713  -8.471  -5.866  1.00103.55           O  
ANISOU 4131  O   ARG B 299    10912  16540  11891  -2541  -5815   4248       O  
ATOM   4132  CB  ARG B 299      34.786 -10.986  -5.763  1.00156.61           C  
ANISOU 4132  CB  ARG B 299    16782  23508  19216  -2050  -5862   4773       C  
ATOM   4133  CG  ARG B 299      33.571 -11.529  -6.494  1.00155.37           C  
ANISOU 4133  CG  ARG B 299    16744  23225  19064  -1873  -5551   4688       C  
ATOM   4134  CD  ARG B 299      33.707 -11.410  -8.001  1.00155.39           C  
ANISOU 4134  CD  ARG B 299    16448  23234  19359  -1516  -5359   4854       C  
ATOM   4135  NE  ARG B 299      32.514 -11.906  -8.681  1.00153.17           N  
ANISOU 4135  NE  ARG B 299    16386  22807  19004  -1338  -5116   4793       N  
ATOM   4136  CZ  ARG B 299      32.294 -13.185  -8.967  1.00152.11           C  
ANISOU 4136  CZ  ARG B 299    16051  22632  19112  -1093  -4858   4830       C  
ATOM   4137  NH1 ARG B 299      33.188 -14.106  -8.635  1.00150.23           N  
ANISOU 4137  NH1 ARG B 299    16076  22222  18785   -957  -4618   4733       N  
ATOM   4138  NH2 ARG B 299      31.177 -13.545  -9.585  1.00153.09           N  
ANISOU 4138  NH2 ARG B 299    15746  22860  19564   -981  -4783   4920       N  
ATOM   4139  N   VAL B 300      33.634  -8.728  -3.826  1.00128.03           N  
ANISOU 4139  N   VAL B 300    14130  19751  14765  -2651  -6251   4378       N  
ATOM   4140  CA  VAL B 300      32.521  -8.110  -3.114  1.00126.77           C  
ANISOU 4140  CA  VAL B 300    14480  19474  14213  -2776  -6250   4163       C  
ATOM   4141  C   VAL B 300      32.431  -6.624  -3.449  1.00125.91           C  
ANISOU 4141  C   VAL B 300    14476  19298  14069  -3058  -6281   3956       C  
ATOM   4142  O   VAL B 300      31.341  -6.088  -3.649  1.00123.47           O  
ANISOU 4142  O   VAL B 300    14428  18865  13623  -3084  -6112   3767       O  
ATOM   4143  CB  VAL B 300      32.657  -8.287  -1.587  1.00112.09           C  
ANISOU 4143  CB  VAL B 300    12891  17651  12049  -2850  -6499   4180       C  
ATOM   4144  CG1 VAL B 300      31.500  -7.615  -0.863  1.00112.04           C  
ANISOU 4144  CG1 VAL B 300    13398  17538  11633  -3062  -6543   3911       C  
ATOM   4145  CG2 VAL B 300      32.725  -9.761  -1.227  1.00112.00           C  
ANISOU 4145  CG2 VAL B 300    12896  17655  12005  -2570  -6425   4354       C  
ATOM   4146  N   GLN B 301      33.585  -5.965  -3.514  1.00111.12           N  
ANISOU 4146  N   GLN B 301    12369  17500  12350  -3260  -6483   4008       N  
ATOM   4147  CA  GLN B 301      33.640  -4.548  -3.856  1.00111.30           C  
ANISOU 4147  CA  GLN B 301    12501  17439  12350  -3555  -6543   3830       C  
ATOM   4148  C   GLN B 301      33.147  -4.303  -5.278  1.00107.50           C  
ANISOU 4148  C   GLN B 301    11875  16892  12076  -3513  -6273   3773       C  
ATOM   4149  O   GLN B 301      32.353  -3.393  -5.520  1.00105.80           O  
ANISOU 4149  O   GLN B 301    11945  16528  11725  -3659  -6214   3559       O  
ATOM   4150  CB  GLN B 301      35.062  -4.006  -3.691  1.00142.10           C  
ANISOU 4150  CB  GLN B 301    16155  21446  16390  -3782  -6822   3935       C  
ATOM   4151  CG  GLN B 301      35.578  -4.025  -2.260  1.00146.12           C  
ANISOU 4151  CG  GLN B 301    16942  21974  16601  -3898  -7113   3910       C  
ATOM   4152  CD  GLN B 301      34.810  -3.089  -1.346  1.00149.92           C  
ANISOU 4152  CD  GLN B 301    17075  22643  17242  -3838  -7317   4166       C  
ATOM   4153  OE1 GLN B 301      34.218  -2.108  -1.795  1.00151.33           O  
ANISOU 4153  OE1 GLN B 301    16801  22938  17757  -3842  -7327   4332       O  
ATOM   4154  NE2 GLN B 301      34.817  -3.390  -0.052  1.00151.74           N  
ANISOU 4154  NE2 GLN B 301    17516  22909  17227  -3766  -7466   4206       N  
ATOM   4155  N   ALA B 302      33.623  -5.119  -6.215  1.00106.33           N  
ANISOU 4155  N   ALA B 302    11298  16849  12252  -3306  -6110   3958       N  
ATOM   4156  CA  ALA B 302      33.208  -5.010  -7.610  1.00102.84           C  
ANISOU 4156  CA  ALA B 302    10704  16367  12006  -3232  -5839   3924       C  
ATOM   4157  C   ALA B 302      31.709  -5.255  -7.756  1.00 98.95           C  
ANISOU 4157  C   ALA B 302    10566  15735  11294  -3097  -5644   3767       C  
ATOM   4158  O   ALA B 302      31.010  -4.526  -8.468  1.00 96.44           O  
ANISOU 4158  O   ALA B 302    10372  15312  10959  -3172  -5509   3617       O  
ATOM   4159  CB  ALA B 302      33.990  -5.988  -8.473  1.00102.80           C  
ANISOU 4159  CB  ALA B 302    10193  16507  12362  -2988  -5686   4148       C  
ATOM   4160  N   LEU B 303      31.225  -6.286  -7.070  1.00 98.69           N  
ANISOU 4160  N   LEU B 303    10704  15703  11092  -2905  -5631   3810       N  
ATOM   4161  CA  LEU B 303      29.811  -6.634  -7.096  1.00 95.38           C  
ANISOU 4161  CA  LEU B 303    10613  15170  10456  -2767  -5436   3688       C  
ATOM   4162  C   LEU B 303      28.974  -5.482  -6.551  1.00 94.55           C  
ANISOU 4162  C   LEU B 303    10995  14913  10015  -2957  -5456   3409       C  
ATOM   4163  O   LEU B 303      27.919  -5.155  -7.096  1.00 89.54           O  
ANISOU 4163  O   LEU B 303    10557  14108   9357  -2880  -5154   3205       O  
ATOM   4164  CB  LEU B 303      29.566  -7.904  -6.279  1.00 95.76           C  
ANISOU 4164  CB  LEU B 303    10727  15250  10409  -2531  -5408   3823       C  
ATOM   4165  CG  LEU B 303      28.336  -8.736  -6.642  1.00 92.46           C  
ANISOU 4165  CG  LEU B 303    10070  14807  10253  -2206  -5114   3939       C  
ATOM   4166  CD1 LEU B 303      28.409  -9.187  -8.092  1.00 93.94           C  
ANISOU 4166  CD1 LEU B 303     9749  15119  10824  -2156  -5132   4110       C  
ATOM   4167  CD2 LEU B 303      28.218  -9.931  -5.715  1.00 93.99           C  
ANISOU 4167  CD2 LEU B 303    10353  15023  10334  -2015  -5155   4103       C  
ATOM   4168  N   ARG B 304      29.460  -4.864  -5.478  1.00104.27           N  
ANISOU 4168  N   ARG B 304    12441  16159  11018  -3154  -5726   3356       N  
ATOM   4169  CA  ARG B 304      28.786  -3.719  -4.876  1.00104.31           C  
ANISOU 4169  CA  ARG B 304    12915  16023  10694  -3338  -5779   3086       C  
ATOM   4170  C   ARG B 304      28.753  -2.540  -5.844  1.00103.59           C  
ANISOU 4170  C   ARG B 304    12803  15824  10734  -3531  -5766   2948       C  
ATOM   4171  O   ARG B 304      27.752  -1.820  -5.929  1.00101.71           O  
ANISOU 4171  O   ARG B 304    12907  15404  10334  -3555  -5622   2701       O  
ATOM   4172  CB  ARG B 304      29.475  -3.315  -3.570  1.00127.14           C  
ANISOU 4172  CB  ARG B 304    16030  18938  13340  -3499  -6056   3046       C  
ATOM   4173  CG  ARG B 304      28.807  -2.156  -2.849  1.00129.50           C  
ANISOU 4173  CG  ARG B 304    16001  19337  13866  -3666  -6307   3193       C  
ATOM   4174  CD  ARG B 304      29.386  -1.963  -1.457  1.00133.14           C  
ANISOU 4174  CD  ARG B 304    16718  19800  14069  -3869  -6601   3121       C  
ATOM   4175  NE  ARG B 304      30.800  -1.599  -1.491  1.00133.14           N  
ANISOU 4175  NE  ARG B 304    17245  19635  13707  -3981  -6594   2826       N  
ATOM   4176  CZ  ARG B 304      31.251  -0.349  -1.444  1.00135.89           C  
ANISOU 4176  CZ  ARG B 304    17862  19918  13850  -4215  -6829   2681       C  
ATOM   4177  NH1 ARG B 304      30.397   0.662  -1.361  1.00139.37           N  
ANISOU 4177  NH1 ARG B 304    18089  20455  14411  -4383  -7106   2817       N  
ATOM   4178  NH2 ARG B 304      32.555  -0.110  -1.479  1.00135.97           N  
ANISOU 4178  NH2 ARG B 304    18362  19766  13535  -4274  -6784   2397       N  
ATOM   4179  N   ARG B 305      29.852  -2.346  -6.569  1.00 99.03           N  
ANISOU 4179  N   ARG B 305    11831  15322  10474  -3639  -5853   3088       N  
ATOM   4180  CA  ARG B 305      29.912  -1.320  -7.603  1.00 98.29           C  
ANISOU 4180  CA  ARG B 305    11683  15128  10534  -3824  -5820   2995       C  
ATOM   4181  C   ARG B 305      28.833  -1.567  -8.648  1.00 91.91           C  
ANISOU 4181  C   ARG B 305    10869  14200   9854  -3593  -5407   2904       C  
ATOM   4182  O   ARG B 305      28.132  -0.642  -9.061  1.00 89.26           O  
ANISOU 4182  O   ARG B 305    10776  13666   9475  -3656  -5270   2693       O  
ATOM   4183  CB  ARG B 305      31.292  -1.285  -8.268  1.00127.31           C  
ANISOU 4183  CB  ARG B 305    14904  18926  14541  -3958  -5929   3188       C  
ATOM   4184  CG  ARG B 305      32.408  -0.774  -7.371  1.00129.98           C  
ANISOU 4184  CG  ARG B 305    15298  19292  14797  -4193  -6243   3203       C  
ATOM   4185  CD  ARG B 305      33.637  -0.390  -8.181  1.00131.80           C  
ANISOU 4185  CD  ARG B 305    15069  19651  15358  -4336  -6333   3400       C  
ATOM   4186  NE  ARG B 305      34.247  -1.535  -8.852  1.00131.99           N  
ANISOU 4186  NE  ARG B 305    14627  19882  15639  -4090  -6227   3650       N  
ATOM   4187  CZ  ARG B 305      35.292  -2.207  -8.380  1.00134.01           C  
ANISOU 4187  CZ  ARG B 305    14456  20304  16156  -4143  -6316   3856       C  
ATOM   4188  NH1 ARG B 305      35.848  -1.850  -7.231  1.00136.31           N  
ANISOU 4188  NH1 ARG B 305    14720  20586  16484  -4455  -6522   3855       N  
ATOM   4189  NH2 ARG B 305      35.783  -3.235  -9.059  1.00134.29           N  
ANISOU 4189  NH2 ARG B 305    14097  20508  16416  -3878  -6197   4062       N  
ATOM   4190  N   GLY B 306      28.698  -2.824  -9.063  1.00 89.14           N  
ANISOU 4190  N   GLY B 306    10265  13938   9667  -3303  -5185   3048       N  
ATOM   4191  CA  GLY B 306      27.661  -3.205 -10.005  1.00 82.79           C  
ANISOU 4191  CA  GLY B 306     9470  13007   8977  -3057  -4770   2953       C  
ATOM   4192  C   GLY B 306      26.272  -2.899  -9.477  1.00 79.42           C  
ANISOU 4192  C   GLY B 306     9504  12394   8276  -2969  -4593   2705       C  
ATOM   4193  O   GLY B 306      25.423  -2.373 -10.203  1.00 75.29           O  
ANISOU 4193  O   GLY B 306     9104  11710   7793  -2917  -4350   2539       O  
ATOM   4194  N   VAL B 307      26.047  -3.223  -8.206  1.00 81.58           N  
ANISOU 4194  N   VAL B 307    10023  12704   8268  -2948  -4716   2691       N  
ATOM   4195  CA  VAL B 307      24.764  -2.969  -7.556  1.00 79.35           C  
ANISOU 4195  CA  VAL B 307    10171  12284   7695  -2865  -4554   2469       C  
ATOM   4196  C   VAL B 307      24.408  -1.486  -7.563  1.00 79.63           C  
ANISOU 4196  C   VAL B 307    10512  12145   7596  -3053  -4603   2218       C  
ATOM   4197  O   VAL B 307      23.326  -1.100  -8.013  1.00 75.70           O  
ANISOU 4197  O   VAL B 307    10215  11483   7062  -2945  -4343   2024       O  
ATOM   4198  CB  VAL B 307      24.752  -3.482  -6.100  1.00 82.89           C  
ANISOU 4198  CB  VAL B 307    10830  12835   7832  -2856  -4723   2522       C  
ATOM   4199  CG1 VAL B 307      23.467  -3.068  -5.401  1.00 81.44           C  
ANISOU 4199  CG1 VAL B 307    11099  12527   7319  -2800  -4559   2278       C  
ATOM   4200  CG2 VAL B 307      24.920  -4.992  -6.065  1.00 82.42           C  
ANISOU 4200  CG2 VAL B 307    10518  12901   7896  -2639  -4648   2764       C  
ATOM   4201  N   LEU B 308      25.324  -0.660  -7.065  1.00 84.64           N  
ANISOU 4201  N   LEU B 308    11182  12811   8168  -3336  -4952   2229       N  
ATOM   4202  CA  LEU B 308      25.096   0.780  -6.997  1.00 85.96           C  
ANISOU 4202  CA  LEU B 308    11664  12789   8208  -3544  -5052   1997       C  
ATOM   4203  C   LEU B 308      24.900   1.405  -8.377  1.00 82.01           C  
ANISOU 4203  C   LEU B 308    11047  12139   7975  -3532  -4840   1936       C  
ATOM   4204  O   LEU B 308      23.987   2.213  -8.575  1.00 79.70           O  
ANISOU 4204  O   LEU B 308    11055  11635   7594  -3497  -4687   1706       O  
ATOM   4205  CB  LEU B 308      26.239   1.474  -6.253  1.00 92.72           C  
ANISOU 4205  CB  LEU B 308    12520  13716   8995  -3881  -5498   2058       C  
ATOM   4206  CG  LEU B 308      26.326   1.190  -4.752  1.00 97.65           C  
ANISOU 4206  CG  LEU B 308    13474  14398   9229  -3975  -5763   1997       C  
ATOM   4207  CD1 LEU B 308      27.535   1.878  -4.139  1.00102.73           C  
ANISOU 4207  CD1 LEU B 308    14022  15092   9919  -4260  -6121   2075       C  
ATOM   4208  CD2 LEU B 308      25.047   1.622  -4.052  1.00 96.88           C  
ANISOU 4208  CD2 LEU B 308    13912  14087   8811  -3941  -5641   1670       C  
ATOM   4209  N   VAL B 309      25.752   1.025  -9.326  1.00 81.49           N  
ANISOU 4209  N   VAL B 309    10544  12188   8230  -3547  -4824   2147       N  
ATOM   4210  CA  VAL B 309      25.648   1.532 -10.692  1.00 78.01           C  
ANISOU 4210  CA  VAL B 309     9962  11638   8041  -3535  -4616   2127       C  
ATOM   4211  C   VAL B 309      24.297   1.188 -11.310  1.00 71.98           C  
ANISOU 4211  C   VAL B 309     9337  10748   7264  -3244  -4234   1988       C  
ATOM   4212  O   VAL B 309      23.602   2.066 -11.821  1.00 69.73           O  
ANISOU 4212  O   VAL B 309     9260  10263   6972  -3250  -4110   1814       O  
ATOM   4213  CB  VAL B 309      26.779   0.994 -11.597  1.00 78.46           C  
ANISOU 4213  CB  VAL B 309     9503  11883   8427  -3541  -4604   2391       C  
ATOM   4214  CG1 VAL B 309      26.442   1.214 -13.064  1.00 74.08           C  
ANISOU 4214  CG1 VAL B 309     8823  11232   8093  -3453  -4310   2370       C  
ATOM   4215  CG2 VAL B 309      28.100   1.659 -11.247  1.00 84.61           C  
ANISOU 4215  CG2 VAL B 309    10105  12770   9272  -3873  -4972   2526       C  
ATOM   4216  N   LEU B 310      23.925  -0.088 -11.246  1.00 69.75           N  
ANISOU 4216  N   LEU B 310     8943  10577   6983  -2996  -4065   2072       N  
ATOM   4217  CA  LEU B 310      22.664  -0.541 -11.825  1.00 64.45           C  
ANISOU 4217  CA  LEU B 310     8357   9811   6320  -2732  -3714   1967       C  
ATOM   4218  C   LEU B 310      21.465   0.136 -11.167  1.00 63.55           C  
ANISOU 4218  C   LEU B 310     8677   9525   5943  -2698  -3641   1710       C  
ATOM   4219  O   LEU B 310      20.511   0.522 -11.846  1.00 59.92           O  
ANISOU 4219  O   LEU B 310     8320   8917   5530  -2590  -3417   1573       O  
ATOM   4220  CB  LEU B 310      22.538  -2.060 -11.722  1.00 63.23           C  
ANISOU 4220  CB  LEU B 310     8034   9795   6195  -2505  -3587   2112       C  
ATOM   4221  CG  LEU B 310      21.317  -2.660 -12.418  1.00 58.11           C  
ANISOU 4221  CG  LEU B 310     7409   9065   5605  -2251  -3235   2038       C  
ATOM   4222  CD1 LEU B 310      21.287  -2.259 -13.885  1.00 55.07           C  
ANISOU 4222  CD1 LEU B 310     6843   8610   5471  -2229  -3071   2033       C  
ATOM   4223  CD2 LEU B 310      21.316  -4.169 -12.273  1.00 57.64           C  
ANISOU 4223  CD2 LEU B 310     7201   9120   5579  -2059  -3143   2192       C  
ATOM   4224  N   ARG B 311      21.523   0.278  -9.846  1.00 70.62           N  
ANISOU 4224  N   ARG B 311     9826  10448   6557  -2783  -3830   1646       N  
ATOM   4225  CA  ARG B 311      20.471   0.958  -9.098  1.00 70.54           C  
ANISOU 4225  CA  ARG B 311    10240  10288   6272  -2744  -3759   1389       C  
ATOM   4226  C   ARG B 311      20.308   2.389  -9.599  1.00 70.71           C  
ANISOU 4226  C   ARG B 311    10444  10089   6332  -2880  -3807   1214       C  
ATOM   4227  O   ARG B 311      19.195   2.829  -9.914  1.00 68.08           O  
ANISOU 4227  O   ARG B 311    10326   9591   5951  -2746  -3602   1022       O  
ATOM   4228  CB  ARG B 311      20.798   0.958  -7.602  1.00 72.75           C  
ANISOU 4228  CB  ARG B 311    10772  10651   6217  -2836  -3979   1356       C  
ATOM   4229  CG  ARG B 311      19.717   1.559  -6.718  1.00 72.28           C  
ANISOU 4229  CG  ARG B 311    10660  10760   6045  -2657  -3868   1480       C  
ATOM   4230  CD  ARG B 311      20.160   1.605  -5.265  1.00 76.41           C  
ANISOU 4230  CD  ARG B 311    11537  11330   6163  -2709  -4001   1384       C  
ATOM   4231  NE  ARG B 311      20.620   0.301  -4.794  1.00 82.06           N  
ANISOU 4231  NE  ARG B 311    12318  12093   6765  -2981  -4402   1419       N  
ATOM   4232  CZ  ARG B 311      21.155   0.084  -3.597  1.00 86.31           C  
ANISOU 4232  CZ  ARG B 311    12865  12808   7121  -3056  -4636   1565       C  
ATOM   4233  NH1 ARG B 311      21.301   1.085  -2.739  1.00 85.45           N  
ANISOU 4233  NH1 ARG B 311    12707  12829   6928  -2877  -4498   1698       N  
ATOM   4234  NH2 ARG B 311      21.547  -1.136  -3.255  1.00 91.73           N  
ANISOU 4234  NH2 ARG B 311    13603  13535   7713  -3322  -5023   1591       N  
ATOM   4235  N   ALA B 312      21.429   3.103  -9.680  1.00 70.63           N  
ANISOU 4235  N   ALA B 312    10337  10076   6423  -3147  -4082   1291       N  
ATOM   4236  CA  ALA B 312      21.439   4.477 -10.172  1.00 71.41           C  
ANISOU 4236  CA  ALA B 312    10605   9948   6579  -3313  -4158   1156       C  
ATOM   4237  C   ALA B 312      20.867   4.570 -11.584  1.00 66.32           C  
ANISOU 4237  C   ALA B 312     9824   9198   6176  -3164  -3875   1155       C  
ATOM   4238  O   ALA B 312      20.138   5.510 -11.903  1.00 65.06           O  
ANISOU 4238  O   ALA B 312     9918   8811   5992  -3130  -3786    971       O  
ATOM   4239  CB  ALA B 312      22.849   5.044 -10.131  1.00 76.61           C  
ANISOU 4239  CB  ALA B 312    11116  10653   7340  -3648  -4501   1290       C  
ATOM   4240  N   VAL B 313      21.198   3.591 -12.421  1.00 68.97           N  
ANISOU 4240  N   VAL B 313     9771   9695   6737  -3062  -3736   1358       N  
ATOM   4241  CA  VAL B 313      20.692   3.547 -13.790  1.00 64.49           C  
ANISOU 4241  CA  VAL B 313     9061   9058   6384  -2920  -3472   1374       C  
ATOM   4242  C   VAL B 313      19.174   3.393 -13.817  1.00 61.50           C  
ANISOU 4242  C   VAL B 313     8892   8574   5901  -2650  -3200   1199       C  
ATOM   4243  O   VAL B 313      18.483   4.115 -14.539  1.00 59.99           O  
ANISOU 4243  O   VAL B 313     8815   8205   5772  -2590  -3070   1089       O  
ATOM   4244  CB  VAL B 313      21.342   2.405 -14.601  1.00 57.51           C  
ANISOU 4244  CB  VAL B 313     7740   8380   5730  -2841  -3369   1610       C  
ATOM   4245  CG1 VAL B 313      20.616   2.205 -15.922  1.00 52.85           C  
ANISOU 4245  CG1 VAL B 313     7045   7722   5311  -2671  -3082   1604       C  
ATOM   4246  CG2 VAL B 313      22.816   2.694 -14.838  1.00 61.39           C  
ANISOU 4246  CG2 VAL B 313     7971   8988   6367  -3098  -3606   1795       C  
ATOM   4247  N   VAL B 314      18.665   2.453 -13.025  1.00 59.55           N  
ANISOU 4247  N   VAL B 314     8688   8439   5497  -2495  -3122   1187       N  
ATOM   4248  CA  VAL B 314      17.225   2.222 -12.930  1.00 57.36           C  
ANISOU 4248  CA  VAL B 314     8575   8100   5119  -2249  -2860   1042       C  
ATOM   4249  C   VAL B 314      16.490   3.481 -12.477  1.00 58.69           C  
ANISOU 4249  C   VAL B 314     9127   8056   5115  -2255  -2872    791       C  
ATOM   4250  O   VAL B 314      15.536   3.927 -13.129  1.00 58.18           O  
ANISOU 4250  O   VAL B 314     9142   7850   5114  -2112  -2686    676       O  
ATOM   4251  CB  VAL B 314      16.898   1.065 -11.962  1.00 52.15           C  
ANISOU 4251  CB  VAL B 314     7911   7607   4295  -2124  -2796   1092       C  
ATOM   4252  CG1 VAL B 314      15.396   0.970 -11.733  1.00 49.68           C  
ANISOU 4252  CG1 VAL B 314     7783   7236   3856  -1903  -2536    933       C  
ATOM   4253  CG2 VAL B 314      17.444  -0.250 -12.498  1.00 50.91           C  
ANISOU 4253  CG2 VAL B 314     7391   7619   4332  -2062  -2744   1326       C  
ATOM   4254  N   ILE B 315      16.947   4.054 -11.365  1.00 57.05           N  
ANISOU 4254  N   ILE B 315     9164   7823   4690  -2415  -3102    704       N  
ATOM   4255  CA  ILE B 315      16.337   5.265 -10.820  1.00 58.84           C  
ANISOU 4255  CA  ILE B 315     9795   7832   4729  -2418  -3132    445       C  
ATOM   4256  C   ILE B 315      16.343   6.402 -11.837  1.00 58.09           C  
ANISOU 4256  C   ILE B 315     9754   7499   4819  -2494  -3160    385       C  
ATOM   4257  O   ILE B 315      15.311   7.034 -12.083  1.00 56.62           O  
ANISOU 4257  O   ILE B 315     9780   7123   4610  -2341  -3013    205       O  
ATOM   4258  CB  ILE B 315      17.055   5.736  -9.540  1.00 64.51           C  
ANISOU 4258  CB  ILE B 315    10779   8557   5175  -2616  -3418    365       C  
ATOM   4259  CG1 ILE B 315      16.986   4.657  -8.459  1.00 65.53           C  
ANISOU 4259  CG1 ILE B 315    10903   8914   5081  -2528  -3382    422       C  
ATOM   4260  CG2 ILE B 315      16.445   7.033  -9.028  1.00 66.86           C  
ANISOU 4260  CG2 ILE B 315    11522   8597   5283  -2612  -3446     74       C  
ATOM   4261  CD1 ILE B 315      17.725   5.021  -7.189  1.00 63.05           C  
ANISOU 4261  CD1 ILE B 315    10732   8606   4617  -2244  -3065    286       C  
ATOM   4262  N   ALA B 316      17.509   6.652 -12.427  1.00 61.15           N  
ANISOU 4262  N   ALA B 316     9934   7903   5396  -2724  -3341    551       N  
ATOM   4263  CA  ALA B 316      17.657   7.721 -13.408  1.00 60.91           C  
ANISOU 4263  CA  ALA B 316     9938   7658   5546  -2835  -3382    537       C  
ATOM   4264  C   ALA B 316      16.729   7.515 -14.600  1.00 55.75           C  
ANISOU 4264  C   ALA B 316     9163   6955   5062  -2597  -3090    547       C  
ATOM   4265  O   ALA B 316      16.143   8.472 -15.109  1.00 55.04           O  
ANISOU 4265  O   ALA B 316     9263   6629   5018  -2553  -3044    430       O  
ATOM   4266  CB  ALA B 316      19.102   7.828 -13.870  1.00 61.38           C  
ANISOU 4266  CB  ALA B 316     9733   7802   5785  -3126  -3597    754       C  
ATOM   4267  N   PHE B 317      16.595   6.266 -15.037  1.00 51.52           N  
ANISOU 4267  N   PHE B 317     8325   6633   4616  -2443  -2907    686       N  
ATOM   4268  CA  PHE B 317      15.709   5.942 -16.150  1.00 46.94           C  
ANISOU 4268  CA  PHE B 317     7618   6031   4184  -2226  -2645    702       C  
ATOM   4269  C   PHE B 317      14.263   6.270 -15.798  1.00 45.43           C  
ANISOU 4269  C   PHE B 317     7689   5708   3863  -1993  -2479    485       C  
ATOM   4270  O   PHE B 317      13.577   6.967 -16.552  1.00 43.58           O  
ANISOU 4270  O   PHE B 317     7537   5301   3719  -1895  -2385    413       O  
ATOM   4271  CB  PHE B 317      15.830   4.466 -16.539  1.00 64.92           C  
ANISOU 4271  CB  PHE B 317     9557   8552   6557  -2112  -2498    873       C  
ATOM   4272  CG  PHE B 317      15.085   4.105 -17.799  1.00 63.12           C  
ANISOU 4272  CG  PHE B 317     9174   8313   6496  -1938  -2267    911       C  
ATOM   4273  CD1 PHE B 317      13.749   3.738 -17.754  1.00 62.43           C  
ANISOU 4273  CD1 PHE B 317     9162   8202   6358  -1698  -2059    800       C  
ATOM   4274  CD2 PHE B 317      15.723   4.134 -19.027  1.00 62.39           C  
ANISOU 4274  CD2 PHE B 317     8858   8247   6603  -2021  -2260   1061       C  
ATOM   4275  CE1 PHE B 317      13.066   3.405 -18.908  1.00 60.90           C  
ANISOU 4275  CE1 PHE B 317     8829   8001   6311  -1554  -1876    836       C  
ATOM   4276  CE2 PHE B 317      15.045   3.802 -20.185  1.00 60.82           C  
ANISOU 4276  CE2 PHE B 317     8541   8039   6528  -1868  -2062   1089       C  
ATOM   4277  CZ  PHE B 317      13.715   3.437 -20.125  1.00 59.98           C  
ANISOU 4277  CZ  PHE B 317     8518   7900   6371  -1640  -1884    975       C  
ATOM   4278  N   VAL B 318      13.809   5.765 -14.653  1.00 61.38           N  
ANISOU 4278  N   VAL B 318     9833   7819   5669  -1900  -2442    393       N  
ATOM   4279  CA  VAL B 318      12.441   6.006 -14.201  1.00 62.38           C  
ANISOU 4279  CA  VAL B 318    10186   7859   5658  -1667  -2261    191       C  
ATOM   4280  C   VAL B 318      12.133   7.498 -14.108  1.00 64.70           C  
ANISOU 4280  C   VAL B 318    10817   7865   5904  -1685  -2345    -10       C  
ATOM   4281  O   VAL B 318      11.141   7.976 -14.669  1.00 65.24           O  
ANISOU 4281  O   VAL B 318    10949   7789   6050  -1501  -2196   -103       O  
ATOM   4282  CB  VAL B 318      12.170   5.350 -12.834  1.00 46.44           C  
ANISOU 4282  CB  VAL B 318     8279   5993   3374  -1606  -2227    129       C  
ATOM   4283  CG1 VAL B 318      10.798   5.754 -12.316  1.00 46.08           C  
ANISOU 4283  CG1 VAL B 318     8469   5865   3175  -1369  -2026    -90       C  
ATOM   4284  CG2 VAL B 318      12.283   3.837 -12.940  1.00 44.60           C  
ANISOU 4284  CG2 VAL B 318     7737   6012   3197  -1559  -2126    327       C  
ATOM   4285  N   VAL B 319      13.000   8.229 -13.412  1.00 57.95           N  
ANISOU 4285  N   VAL B 319    10176   6915   4927  -1908  -2600    -70       N  
ATOM   4286  CA  VAL B 319      12.813   9.662 -13.204  1.00 60.67           C  
ANISOU 4286  CA  VAL B 319    10889   6953   5208  -1946  -2710   -274       C  
ATOM   4287  C   VAL B 319      12.818  10.453 -14.511  1.00 60.39           C  
ANISOU 4287  C   VAL B 319    10808   6710   5425  -1983  -2725   -215       C  
ATOM   4288  O   VAL B 319      11.931  11.273 -14.752  1.00 61.91           O  
ANISOU 4288  O   VAL B 319    11220   6668   5636  -1826  -2650   -369       O  
ATOM   4289  CB  VAL B 319      13.891  10.241 -12.263  1.00 59.51           C  
ANISOU 4289  CB  VAL B 319    10975   6745   4892  -2230  -3022   -332       C  
ATOM   4290  CG1 VAL B 319      13.777  11.756 -12.186  1.00 63.07           C  
ANISOU 4290  CG1 VAL B 319    11831   6836   5298  -2283  -3151   -546       C  
ATOM   4291  CG2 VAL B 319      13.774   9.621 -10.880  1.00 61.65           C  
ANISOU 4291  CG2 VAL B 319    11353   7203   4868  -2183  -3015   -407       C  
ATOM   4292  N   CYS B 320      13.816  10.203 -15.353  1.00 71.49           N  
ANISOU 4292  N   CYS B 320    11929   8209   7023  -2179  -2815     15       N  
ATOM   4293  CA  CYS B 320      13.954  10.945 -16.602  1.00 71.60           C  
ANISOU 4293  CA  CYS B 320    11895   8050   7258  -2249  -2837    102       C  
ATOM   4294  C   CYS B 320      12.840  10.641 -17.599  1.00 70.56           C  
ANISOU 4294  C   CYS B 320    11643   7916   7252  -1967  -2576    113       C  
ATOM   4295  O   CYS B 320      12.423  11.519 -18.357  1.00 71.71           O  
ANISOU 4295  O   CYS B 320    11913   7832   7503  -1920  -2568     80       O  
ATOM   4296  CB  CYS B 320      15.315  10.677 -17.246  1.00 66.54           C  
ANISOU 4296  CB  CYS B 320    10954   7551   6776  -2525  -2969    355       C  
ATOM   4297  SG  CYS B 320      16.719  11.387 -16.361  1.00 68.60           S  
ANISOU 4297  SG  CYS B 320    11355   7745   6964  -2928  -3340    371       S  
ATOM   4298  N   TRP B 321      12.355   9.403 -17.596  1.00 45.20           N  
ANISOU 4298  N   TRP B 321     8195   4950   4031  -1788  -2380    168       N  
ATOM   4299  CA  TRP B 321      11.353   8.992 -18.576  1.00 44.10           C  
ANISOU 4299  CA  TRP B 321     7899   4840   4019  -1553  -2154    202       C  
ATOM   4300  C   TRP B 321       9.907   9.156 -18.109  1.00 45.54           C  
ANISOU 4300  C   TRP B 321     8247   4950   4106  -1258  -1981      6       C  
ATOM   4301  O   TRP B 321       8.987   9.106 -18.924  1.00 45.46           O  
ANISOU 4301  O   TRP B 321     8144   4921   4209  -1065  -1826     16       O  
ATOM   4302  CB  TRP B 321      11.604   7.555 -19.043  1.00 54.92           C  
ANISOU 4302  CB  TRP B 321     8902   6493   5470  -1532  -2036    385       C  
ATOM   4303  CG  TRP B 321      12.764   7.436 -19.977  1.00 53.77           C  
ANISOU 4303  CG  TRP B 321     8541   6408   5480  -1743  -2131    589       C  
ATOM   4304  CD1 TRP B 321      14.031   7.039 -19.666  1.00 53.37           C  
ANISOU 4304  CD1 TRP B 321     8342   6503   5430  -1954  -2267    718       C  
ATOM   4305  CD2 TRP B 321      12.766   7.726 -21.379  1.00 53.31           C  
ANISOU 4305  CD2 TRP B 321     8384   6279   5592  -1762  -2092    695       C  
ATOM   4306  NE1 TRP B 321      14.822   7.059 -20.789  1.00 52.82           N  
ANISOU 4306  NE1 TRP B 321     8072   6468   5529  -2094  -2293    894       N  
ATOM   4307  CE2 TRP B 321      14.069   7.478 -21.854  1.00 52.68           C  
ANISOU 4307  CE2 TRP B 321     8093   6318   5603  -1986  -2185    883       C  
ATOM   4308  CE3 TRP B 321      11.792   8.170 -22.280  1.00 53.69           C  
ANISOU 4308  CE3 TRP B 321     8496   6184   5717  -1607  -1991    659       C  
ATOM   4309  CZ2 TRP B 321      14.424   7.659 -23.188  1.00 52.39           C  
ANISOU 4309  CZ2 TRP B 321     7923   6268   5714  -2065  -2157   1029       C  
ATOM   4310  CZ3 TRP B 321      12.145   8.349 -23.604  1.00 53.18           C  
ANISOU 4310  CZ3 TRP B 321     8314   6097   5794  -1691  -1989    809       C  
ATOM   4311  CH2 TRP B 321      13.450   8.094 -24.045  1.00 52.53           C  
ANISOU 4311  CH2 TRP B 321     8036   6140   5782  -1921  -2061    989       C  
ATOM   4312  N   LEU B 322       9.706   9.357 -16.810  1.00 57.29           N  
ANISOU 4312  N   LEU B 322     9975   6409   5383  -1222  -2006   -168       N  
ATOM   4313  CA  LEU B 322       8.350   9.508 -16.276  1.00 59.15           C  
ANISOU 4313  CA  LEU B 322    10357   6601   5516   -930  -1816   -359       C  
ATOM   4314  C   LEU B 322       7.546  10.686 -16.861  1.00 61.48           C  
ANISOU 4314  C   LEU B 322    10837   6611   5911   -769  -1791   -477       C  
ATOM   4315  O   LEU B 322       6.439  10.476 -17.359  1.00 62.05           O  
ANISOU 4315  O   LEU B 322    10794   6713   6070   -522  -1601   -489       O  
ATOM   4316  CB  LEU B 322       8.349   9.550 -14.743  1.00 60.28           C  
ANISOU 4316  CB  LEU B 322    10743   6782   5377   -922  -1834   -530       C  
ATOM   4317  CG  LEU B 322       6.972   9.696 -14.092  1.00 62.49           C  
ANISOU 4317  CG  LEU B 322    11164   7048   5531   -610  -1606   -730       C  
ATOM   4318  CD1 LEU B 322       6.098   8.490 -14.400  1.00 60.90           C  
ANISOU 4318  CD1 LEU B 322    10649   7121   5370   -444  -1359   -624       C  
ATOM   4319  CD2 LEU B 322       7.105   9.900 -12.590  1.00 64.73           C  
ANISOU 4319  CD2 LEU B 322    11784   7301   5511   -624  -1656   -933       C  
ATOM   4320  N   PRO B 323       8.089  11.921 -16.810  1.00 76.67           N  
ANISOU 4320  N   PRO B 323    13046   8252   7834   -910  -1993   -555       N  
ATOM   4321  CA  PRO B 323       7.287  13.040 -17.325  1.00 79.06           C  
ANISOU 4321  CA  PRO B 323    13542   8260   8240   -736  -1975   -660       C  
ATOM   4322  C   PRO B 323       7.092  12.964 -18.837  1.00 78.12           C  
ANISOU 4322  C   PRO B 323    13180   8140   8363   -704  -1930   -470       C  
ATOM   4323  O   PRO B 323       6.113  13.498 -19.361  1.00 79.94           O  
ANISOU 4323  O   PRO B 323    13460   8228   8688   -469  -1841   -525       O  
ATOM   4324  CB  PRO B 323       8.135  14.271 -16.978  1.00 48.23           C  
ANISOU 4324  CB  PRO B 323     9980   4052   4293   -967  -2239   -741       C  
ATOM   4325  CG  PRO B 323       9.092  13.811 -15.934  1.00 50.79           C  
ANISOU 4325  CG  PRO B 323    10350   4526   4421  -1185  -2360   -764       C  
ATOM   4326  CD  PRO B 323       9.381  12.392 -16.281  1.00 46.67           C  
ANISOU 4326  CD  PRO B 323     9418   4370   3945  -1225  -2255   -556       C  
ATOM   4327  N   TYR B 324       8.024  12.309 -19.521  1.00 42.22           N  
ANISOU 4327  N   TYR B 324     8378   3757   3908   -930  -1994   -250       N  
ATOM   4328  CA  TYR B 324       7.950  12.132 -20.968  1.00 40.81           C  
ANISOU 4328  CA  TYR B 324     7970   3612   3926   -925  -1950    -62       C  
ATOM   4329  C   TYR B 324       6.693  11.367 -21.370  1.00 40.56           C  
ANISOU 4329  C   TYR B 324     7736   3733   3942   -633  -1722    -66       C  
ATOM   4330  O   TYR B 324       5.959  11.789 -22.266  1.00 41.94           O  
ANISOU 4330  O   TYR B 324     7902   3796   4240   -483  -1681    -43       O  
ATOM   4331  CB  TYR B 324       9.200  11.409 -21.475  1.00 64.44           C  
ANISOU 4331  CB  TYR B 324    10706   6803   6974  -1195  -2021    155       C  
ATOM   4332  CG  TYR B 324       9.118  10.947 -22.912  1.00 62.88           C  
ANISOU 4332  CG  TYR B 324    10257   6695   6940  -1185  -1944    345       C  
ATOM   4333  CD1 TYR B 324       9.347  11.829 -23.959  1.00 63.96           C  
ANISOU 4333  CD1 TYR B 324    10470   6640   7192  -1288  -2041    443       C  
ATOM   4334  CD2 TYR B 324       8.828   9.624 -23.220  1.00 60.19           C  
ANISOU 4334  CD2 TYR B 324     9622   6623   6624  -1085  -1781    428       C  
ATOM   4335  CE1 TYR B 324       9.280  11.409 -25.273  1.00 62.50           C  
ANISOU 4335  CE1 TYR B 324    10076   6548   7122  -1283  -1970    614       C  
ATOM   4336  CE2 TYR B 324       8.758   9.193 -24.529  1.00 58.46           C  
ANISOU 4336  CE2 TYR B 324     9201   6481   6528  -1078  -1717    582       C  
ATOM   4337  CZ  TYR B 324       8.985  10.090 -25.554  1.00 59.63           C  
ANISOU 4337  CZ  TYR B 324     9432   6456   6769  -1174  -1808    673       C  
ATOM   4338  OH  TYR B 324       8.917   9.664 -26.862  1.00 57.88           O  
ANISOU 4338  OH  TYR B 324     9030   6322   6638  -1169  -1742    824       O  
ATOM   4339  N   HIS B 325       6.444  10.250 -20.693  1.00 55.72           N  
ANISOU 4339  N   HIS B 325     9497   5910   5767   -564  -1588    -84       N  
ATOM   4340  CA  HIS B 325       5.276   9.423 -20.983  1.00 55.63           C  
ANISOU 4340  CA  HIS B 325     9276   6064   5797   -322  -1377    -79       C  
ATOM   4341  C   HIS B 325       3.972  10.113 -20.594  1.00 59.34           C  
ANISOU 4341  C   HIS B 325     9908   6401   6239    -34  -1271   -266       C  
ATOM   4342  O   HIS B 325       2.940   9.911 -21.234  1.00 60.57           O  
ANISOU 4342  O   HIS B 325     9915   6600   6500    171  -1145   -247       O  
ATOM   4343  CB  HIS B 325       5.385   8.066 -20.283  1.00 49.42           C  
ANISOU 4343  CB  HIS B 325     8300   5565   4912   -346  -1270    -39       C  
ATOM   4344  CG  HIS B 325       6.419   7.161 -20.876  1.00 45.85           C  
ANISOU 4344  CG  HIS B 325     7623   5272   4528   -554  -1329    157       C  
ATOM   4345  ND1 HIS B 325       6.188   6.410 -22.009  1.00 43.87           N  
ANISOU 4345  ND1 HIS B 325     7132   5115   4424   -533  -1262    299       N  
ATOM   4346  CD2 HIS B 325       7.687   6.884 -20.494  1.00 44.18           C  
ANISOU 4346  CD2 HIS B 325     7387   5143   4256   -774  -1447    232       C  
ATOM   4347  CE1 HIS B 325       7.270   5.709 -22.298  1.00 41.08           C  
ANISOU 4347  CE1 HIS B 325     6624   4890   4097   -716  -1317    442       C  
ATOM   4348  NE2 HIS B 325       8.195   5.979 -21.394  1.00 41.39           N  
ANISOU 4348  NE2 HIS B 325     6773   4931   4023   -861  -1431    414       N  
ATOM   4349  N   VAL B 326       4.025  10.925 -19.542  1.00 45.31           N  
ANISOU 4349  N   VAL B 326     8433   4466   4320    -15  -1324   -449       N  
ATOM   4350  CA  VAL B 326       2.854  11.671 -19.087  1.00 48.78           C  
ANISOU 4350  CA  VAL B 326     9056   4759   4722    278  -1216   -649       C  
ATOM   4351  C   VAL B 326       2.393  12.655 -20.155  1.00 50.74           C  
ANISOU 4351  C   VAL B 326     9375   4749   5156    395  -1281   -629       C  
ATOM   4352  O   VAL B 326       1.195  12.803 -20.407  1.00 52.86           O  
ANISOU 4352  O   VAL B 326     9575   5005   5504    680  -1147   -679       O  
ATOM   4353  CB  VAL B 326       3.145  12.442 -17.783  1.00 36.88           C  
ANISOU 4353  CB  VAL B 326     7911   3101   3001    258  -1281   -866       C  
ATOM   4354  CG1 VAL B 326       1.955  13.309 -17.394  1.00 40.12           C  
ANISOU 4354  CG1 VAL B 326     8543   3308   3393    581  -1176  -1085       C  
ATOM   4355  CG2 VAL B 326       3.489  11.478 -16.663  1.00 37.24           C  
ANISOU 4355  CG2 VAL B 326     7896   3418   2836    192  -1196   -891       C  
ATOM   4356  N   ARG B 327       3.355  13.321 -20.784  1.00 53.02           N  
ANISOU 4356  N   ARG B 327     9785   4841   5516    166  -1491   -537       N  
ATOM   4357  CA  ARG B 327       3.058  14.306 -21.815  1.00 54.61           C  
ANISOU 4357  CA  ARG B 327    10085   4779   5885    233  -1583   -485       C  
ATOM   4358  C   ARG B 327       2.412  13.667 -23.042  1.00 54.08           C  
ANISOU 4358  C   ARG B 327     9703   4868   5977    342  -1492   -314       C  
ATOM   4359  O   ARG B 327       1.482  14.226 -23.626  1.00 56.05           O  
ANISOU 4359  O   ARG B 327     9974   4982   6340    570  -1470   -326       O  
ATOM   4360  CB  ARG B 327       4.329  15.046 -22.226  1.00 64.42           C  
ANISOU 4360  CB  ARG B 327    11497   5817   7162    -90  -1821   -385       C  
ATOM   4361  CG  ARG B 327       4.102  16.085 -23.305  1.00 65.89           C  
ANISOU 4361  CG  ARG B 327    11807   5716   7511    -56  -1932   -301       C  
ATOM   4362  CD  ARG B 327       5.411  16.649 -23.810  1.00 65.02           C  
ANISOU 4362  CD  ARG B 327    11821   5446   7436   -418  -2151   -164       C  
ATOM   4363  NE  ARG B 327       6.320  15.601 -24.263  1.00 61.95           N  
ANISOU 4363  NE  ARG B 327    11131   5354   7050   -672  -2145     33       N  
ATOM   4364  CZ  ARG B 327       6.261  15.025 -25.460  1.00 60.38           C  
ANISOU 4364  CZ  ARG B 327    10673   5312   6954   -691  -2088    233       C  
ATOM   4365  NH1 ARG B 327       5.331  15.393 -26.332  1.00 61.50           N  
ANISOU 4365  NH1 ARG B 327    10814   5352   7201   -487  -2054    275       N  
ATOM   4366  NH2 ARG B 327       7.131  14.080 -25.787  1.00 57.63           N  
ANISOU 4366  NH2 ARG B 327    10072   5224   6598   -904  -2071    387       N  
ATOM   4367  N   ARG B 328       2.908  12.496 -23.429  1.00 50.18           N  
ANISOU 4367  N   ARG B 328     8925   4652   5489    181  -1451   -157       N  
ATOM   4368  CA  ARG B 328       2.381  11.791 -24.592  1.00 49.42           C  
ANISOU 4368  CA  ARG B 328     8542   4715   5518    253  -1377     -3       C  
ATOM   4369  C   ARG B 328       0.961  11.292 -24.342  1.00 51.18           C  
ANISOU 4369  C   ARG B 328     8609   5077   5758    556  -1190    -87       C  
ATOM   4370  O   ARG B 328       0.127  11.289 -25.248  1.00 51.65           O  
ANISOU 4370  O   ARG B 328     8543   5137   5943    712  -1165    -23       O  
ATOM   4371  CB  ARG B 328       3.300  10.633 -24.982  1.00 77.58           C  
ANISOU 4371  CB  ARG B 328    11870   8532   9075     20  -1370    161       C  
ATOM   4372  CG  ARG B 328       4.655  11.084 -25.493  1.00 75.71           C  
ANISOU 4372  CG  ARG B 328    11695   8197   8873   -262  -1534    304       C  
ATOM   4373  CD  ARG B 328       5.562   9.910 -25.831  1.00 71.56           C  
ANISOU 4373  CD  ARG B 328    10949   7923   8316   -472  -1513    428       C  
ATOM   4374  NE  ARG B 328       5.075   9.131 -26.966  1.00 68.57           N  
ANISOU 4374  NE  ARG B 328    10326   7708   8021   -454  -1439    573       N  
ATOM   4375  CZ  ARG B 328       4.606   7.891 -26.875  1.00 66.42           C  
ANISOU 4375  CZ  ARG B 328     9833   7661   7744   -355  -1300    579       C  
ATOM   4376  NH1 ARG B 328       4.564   7.280 -25.698  1.00 66.88           N  
ANISOU 4376  NH1 ARG B 328     9869   7822   7722   -266  -1209    468       N  
ATOM   4377  NH2 ARG B 328       4.184   7.259 -27.964  1.00 64.07           N  
ANISOU 4377  NH2 ARG B 328     9350   7482   7513   -354  -1254    698       N  
ATOM   4378  N   LEU B 329       0.692  10.872 -23.110  1.00 59.23           N  
ANISOU 4378  N   LEU B 329     9631   6224   6647    628  -1063   -220       N  
ATOM   4379  CA  LEU B 329      -0.657  10.487 -22.713  1.00 61.28           C  
ANISOU 4379  CA  LEU B 329     9754   6618   6912    911   -868   -310       C  
ATOM   4380  C   LEU B 329      -1.550  11.720 -22.683  1.00 64.18           C  
ANISOU 4380  C   LEU B 329    10307   6736   7340   1185   -869   -443       C  
ATOM   4381  O   LEU B 329      -2.732  11.657 -23.018  1.00 65.75           O  
ANISOU 4381  O   LEU B 329    10343   6990   7649   1431   -770   -440       O  
ATOM   4382  CB  LEU B 329      -0.645   9.817 -21.338  1.00 57.51           C  
ANISOU 4382  CB  LEU B 329     9277   6323   6250    909   -729   -417       C  
ATOM   4383  CG  LEU B 329       0.039   8.453 -21.238  1.00 54.08           C  
ANISOU 4383  CG  LEU B 329     8624   6158   5767    701   -695   -283       C  
ATOM   4384  CD1 LEU B 329       0.047   7.962 -19.800  1.00 53.61           C  
ANISOU 4384  CD1 LEU B 329     8624   6243   5502    696   -583   -385       C  
ATOM   4385  CD2 LEU B 329      -0.644   7.446 -22.147  1.00 53.88           C  
ANISOU 4385  CD2 LEU B 329     8268   6325   5878    767   -596   -151       C  
ATOM   4386  N   MET B 330      -0.966  12.844 -22.280  1.00 73.76           N  
ANISOU 4386  N   MET B 330    11865   7670   8490   1139   -993   -558       N  
ATOM   4387  CA  MET B 330      -1.677  14.115 -22.225  1.00 76.50           C  
ANISOU 4387  CA  MET B 330    12451   7719   8897   1393  -1020   -695       C  
ATOM   4388  C   MET B 330      -2.067  14.588 -23.621  1.00 77.06           C  
ANISOU 4388  C   MET B 330    12450   7654   9176   1465  -1126   -543       C  
ATOM   4389  O   MET B 330      -3.116  15.206 -23.810  1.00 79.41           O  
ANISOU 4389  O   MET B 330    12767   7827   9579   1769  -1086   -603       O  
ATOM   4390  CB  MET B 330      -0.807  15.170 -21.537  1.00 84.46           C  
ANISOU 4390  CB  MET B 330    13871   8426   9794   1261  -1173   -830       C  
ATOM   4391  CG  MET B 330      -1.343  16.588 -21.621  1.00 87.48           C  
ANISOU 4391  CG  MET B 330    14559   8435  10245   1502  -1233   -973       C  
ATOM   4392  SD  MET B 330      -0.195  17.812 -20.961  1.00 87.76           S  
ANISOU 4392  SD  MET B 330    15097   8079  10167   1273  -1464  -1108       S  
ATOM   4393  CE  MET B 330      -1.076  19.329 -21.323  1.00 90.98           C  
ANISOU 4393  CE  MET B 330    15795   8032  10741   1576  -1548  -1194       C  
ATOM   4394  N   PHE B 331      -1.218  14.282 -24.596  1.00 93.21           N  
ANISOU 4394  N   PHE B 331    14409   9734  11274   1193  -1258   -342       N  
ATOM   4395  CA  PHE B 331      -1.416  14.731 -25.970  1.00 93.32           C  
ANISOU 4395  CA  PHE B 331    14376   9633  11450   1209  -1377   -173       C  
ATOM   4396  C   PHE B 331      -2.678  14.159 -26.614  1.00 94.29           C  
ANISOU 4396  C   PHE B 331    14203   9935  11689   1462  -1268   -116       C  
ATOM   4397  O   PHE B 331      -3.275  14.790 -27.485  1.00 96.10           O  
ANISOU 4397  O   PHE B 331    14464  10001  12049   1648  -1340    -70       O  
ATOM   4398  CB  PHE B 331      -0.188  14.385 -26.822  1.00 47.87           C  
ANISOU 4398  CB  PHE B 331     8550   3948   5690    857  -1494     30       C  
ATOM   4399  CG  PHE B 331      -0.353  14.692 -28.286  1.00 47.61           C  
ANISOU 4399  CG  PHE B 331     8469   3835   5785    846  -1606    220       C  
ATOM   4400  CD1 PHE B 331      -0.236  15.992 -28.751  1.00 49.15           C  
ANISOU 4400  CD1 PHE B 331     8941   3693   6040    811  -1778    267       C  
ATOM   4401  CD2 PHE B 331      -0.617  13.682 -29.199  1.00 45.79           C  
ANISOU 4401  CD2 PHE B 331     7937   3858   5602    855  -1549    358       C  
ATOM   4402  CE1 PHE B 331      -0.383  16.280 -30.093  1.00 49.11           C  
ANISOU 4402  CE1 PHE B 331     8908   3621   6132    793  -1884    460       C  
ATOM   4403  CE2 PHE B 331      -0.767  13.965 -30.544  1.00 45.37           C  
ANISOU 4403  CE2 PHE B 331     7862   3743   5636    839  -1660    532       C  
ATOM   4404  CZ  PHE B 331      -0.649  15.266 -30.991  1.00 47.11           C  
ANISOU 4404  CZ  PHE B 331     8354   3641   5905    809  -1824    590       C  
ATOM   4405  N   CYS B 332      -3.088  12.972 -26.182  1.00 68.38           N  
ANISOU 4405  N   CYS B 332    10634   6983   8364   1461  -1109   -109       N  
ATOM   4406  CA  CYS B 332      -4.203  12.288 -26.828  1.00 68.90           C  
ANISOU 4406  CA  CYS B 332    10384   7251   8543   1635  -1026    -29       C  
ATOM   4407  C   CYS B 332      -5.388  12.009 -25.905  1.00 71.06           C  
ANISOU 4407  C   CYS B 332    10528   7649   8822   1935   -827   -175       C  
ATOM   4408  O   CYS B 332      -6.380  11.421 -26.331  1.00 72.03           O  
ANISOU 4408  O   CYS B 332    10411   7886   9069   2132   -777   -125       O  
ATOM   4409  CB  CYS B 332      -3.722  10.984 -27.467  1.00 79.58           C  
ANISOU 4409  CB  CYS B 332    11475   8884   9875   1405  -1003    119       C  
ATOM   4410  SG  CYS B 332      -2.957   9.823 -26.316  1.00 77.36           S  
ANISOU 4410  SG  CYS B 332    11134   8832   9425   1224   -862     52       S  
ATOM   4411  N   TYR B 333      -5.289  12.423 -24.646  1.00 75.36           N  
ANISOU 4411  N   TYR B 333    11226   8184   9225   1966   -714   -350       N  
ATOM   4412  CA  TYR B 333      -6.376  12.186 -23.696  1.00 77.04           C  
ANISOU 4412  CA  TYR B 333    11315   8550   9409   2235   -489   -489       C  
ATOM   4413  C   TYR B 333      -7.192  13.437 -23.380  1.00 79.80           C  
ANISOU 4413  C   TYR B 333    11835   8665   9822   2587   -459   -643       C  
ATOM   4414  O   TYR B 333      -8.311  13.344 -22.874  1.00 81.33           O  
ANISOU 4414  O   TYR B 333    11849   8995  10059   2871   -274   -717       O  
ATOM   4415  CB  TYR B 333      -5.854  11.545 -22.407  1.00 77.77           C  
ANISOU 4415  CB  TYR B 333    11466   8797   9288   2111   -352   -595       C  
ATOM   4416  CG  TYR B 333      -5.981  10.040 -22.390  1.00 76.19           C  
ANISOU 4416  CG  TYR B 333    10940   8945   9065   1971   -237   -476       C  
ATOM   4417  CD1 TYR B 333      -7.197   9.434 -22.104  1.00 77.10           C  
ANISOU 4417  CD1 TYR B 333    10785   9302   9209   2158    -25   -492       C  
ATOM   4418  CD2 TYR B 333      -4.890   9.225 -22.662  1.00 73.71           C  
ANISOU 4418  CD2 TYR B 333    10585   8712   8712   1653   -338   -341       C  
ATOM   4419  CE1 TYR B 333      -7.324   8.061 -22.087  1.00 75.63           C  
ANISOU 4419  CE1 TYR B 333    10321   9407   9010   2012     68   -375       C  
ATOM   4420  CE2 TYR B 333      -5.008   7.847 -22.648  1.00 72.39           C  
ANISOU 4420  CE2 TYR B 333    10147   8827   8532   1535   -240   -237       C  
ATOM   4421  CZ  TYR B 333      -6.228   7.271 -22.359  1.00 73.38           C  
ANISOU 4421  CZ  TYR B 333    10031   9167   8685   1705    -45   -253       C  
ATOM   4422  OH  TYR B 333      -6.356   5.901 -22.341  1.00 71.97           O  
ANISOU 4422  OH  TYR B 333     9602   9244   8501   1570     41   -141       O  
ATOM   4423  N   ILE B 334      -6.632  14.604 -23.677  1.00 66.69           N  
ANISOU 4423  N   ILE B 334    10516   6649   8174   2572   -635   -688       N  
ATOM   4424  CA  ILE B 334      -7.355  15.855 -23.484  1.00 69.38           C  
ANISOU 4424  CA  ILE B 334    11053   6714   8595   2917   -631   -829       C  
ATOM   4425  C   ILE B 334      -8.269  16.124 -24.675  1.00 70.34           C  
ANISOU 4425  C   ILE B 334    10972   6804   8951   3117   -711   -680       C  
ATOM   4426  O   ILE B 334      -7.821  16.129 -25.822  1.00 69.36           O  
ANISOU 4426  O   ILE B 334    10857   6587   8912   2940   -913   -496       O  
ATOM   4427  CB  ILE B 334      -6.396  17.045 -23.290  1.00 67.43           C  
ANISOU 4427  CB  ILE B 334    11275   6056   8288   2818   -813   -927       C  
ATOM   4428  CG1 ILE B 334      -5.540  16.846 -22.038  1.00 66.80           C  
ANISOU 4428  CG1 ILE B 334    11411   6004   7966   2632   -756  -1090       C  
ATOM   4429  CG2 ILE B 334      -7.172  18.348 -23.193  1.00 70.36           C  
ANISOU 4429  CG2 ILE B 334    11864   6106   8765   3199   -821  -1069       C  
ATOM   4430  CD1 ILE B 334      -4.671  18.037 -21.699  1.00 67.57           C  
ANISOU 4430  CD1 ILE B 334    11985   5694   7995   2542   -933  -1220       C  
ATOM   4431  N   SER B 335      -9.551  16.342 -24.396  1.00165.17           N  
ANISOU 4431  N   SER B 335    22792  18908  21058   3487   -551   -753       N  
ATOM   4432  CA  SER B 335     -10.535  16.595 -25.444  1.00166.11           C  
ANISOU 4432  CA  SER B 335    22683  19026  21406   3711   -628   -612       C  
ATOM   4433  C   SER B 335     -10.247  17.901 -26.178  1.00167.42           C  
ANISOU 4433  C   SER B 335    23170  18760  21682   3820   -853   -592       C  
ATOM   4434  O   SER B 335      -9.555  18.776 -25.657  1.00168.45           O  
ANISOU 4434  O   SER B 335    23696  18577  21732   3837   -891   -749       O  
ATOM   4435  CB  SER B 335     -11.949  16.621 -24.860  1.00182.69           C  
ATOM   4436  OG  SER B 335     -12.916  16.831 -25.874  1.00182.69           O  
ATOM   4437  N   ASP B 336     -10.788  18.024 -27.386  1.00132.43           N  
ANISOU 4437  N   ASP B 336    18582  14308  17428   3883  -1013   -393       N  
ATOM   4438  CA  ASP B 336     -10.547  19.189 -28.234  1.00133.61           C  
ANISOU 4438  CA  ASP B 336    19018  14054  17693   3975  -1246   -324       C  
ATOM   4439  C   ASP B 336     -10.991  20.495 -27.580  1.00136.74           C  
ANISOU 4439  C   ASP B 336    19624  14162  18169   4406  -1181   -523       C  
ATOM   4440  O   ASP B 336     -10.264  21.488 -27.606  1.00137.91           O  
ANISOU 4440  O   ASP B 336    20175  13889  18335   4436  -1333   -570       O  
ATOM   4441  CB  ASP B 336     -11.245  19.019 -29.585  1.00100.64           C  
ANISOU 4441  CB  ASP B 336    14596   9963  13681   3994  -1417    -65       C  
ATOM   4442  CG  ASP B 336     -10.719  17.831 -30.368  1.00 97.65           C  
ANISOU 4442  CG  ASP B 336    13928   9944  13230   3653  -1419     97       C  
ATOM   4443  OD1 ASP B 336     -10.271  16.851 -29.734  1.00 96.54           O  
ANISOU 4443  OD1 ASP B 336    13701  10033  12949   3470  -1254      9       O  
ATOM   4444  OD2 ASP B 336     -10.752  17.877 -31.616  1.00 96.40           O  
ANISOU 4444  OD2 ASP B 336    13646   9832  13150   3575  -1592    311       O  
ATOM   4445  N   GLU B 337     -12.184  20.488 -26.995  1.00127.21           N  
ANISOU 4445  N   GLU B 337    18142  13178  17011   4738   -948   -639       N  
ATOM   4446  CA  GLU B 337     -12.725  21.682 -26.356  1.00130.32           C  
ANISOU 4446  CA  GLU B 337    18697  13341  17477   5195   -837   -849       C  
ATOM   4447  C   GLU B 337     -11.998  22.013 -25.057  1.00130.94           C  
ANISOU 4447  C   GLU B 337    19182  13225  17342   5145   -727  -1124       C  
ATOM   4448  O   GLU B 337     -12.004  23.160 -24.608  1.00133.48           O  
ANISOU 4448  O   GLU B 337    19822  13206  17688   5443   -711  -1315       O  
ATOM   4449  CB  GLU B 337     -14.226  21.527 -26.100  1.00237.82           C  
ATOM   4450  CG  GLU B 337     -15.065  21.448 -27.364  1.00237.82           C  
ATOM   4451  CD  GLU B 337     -16.553  21.421 -27.076  1.00237.82           C  
ATOM   4452  OE1 GLU B 337     -16.929  21.338 -25.888  1.00237.82           O  
ATOM   4453  OE2 GLU B 337     -17.346  21.486 -28.039  1.00237.82           O  
ATOM   4454  N   GLN B 338     -11.371  21.007 -24.456  1.00135.08           N  
ANISOU 4454  N   GLN B 338    19708  13961  17657   4770   -664  -1144       N  
ATOM   4455  CA  GLN B 338     -10.618  21.209 -23.225  1.00135.34           C  
ANISOU 4455  CA  GLN B 338    20109  13856  17458   4672   -580  -1389       C  
ATOM   4456  C   GLN B 338      -9.281  21.891 -23.499  1.00134.78           C  
ANISOU 4456  C   GLN B 338    20495  13380  17337   4375   -855  -1371       C  
ATOM   4457  O   GLN B 338      -8.722  22.552 -22.625  1.00135.80           O  
ANISOU 4457  O   GLN B 338    21033  13234  17330   4376   -860  -1592       O  
ATOM   4458  CB  GLN B 338     -10.394  19.881 -22.499  1.00128.25           C  
ATOM   4459  CG  GLN B 338     -11.661  19.243 -21.958  1.00128.25           C  
ATOM   4460  CD  GLN B 338     -11.379  18.000 -21.135  1.00128.25           C  
ATOM   4461  OE1 GLN B 338     -11.171  16.915 -21.679  1.00128.25           O  
ATOM   4462  NE2 GLN B 338     -11.368  18.154 -19.815  1.00128.25           N  
ATOM   4463  N   TRP B 339      -8.775  21.727 -24.717  1.00131.87           N  
ANISOU 4463  N   TRP B 339    20056  12980  17067   4109  -1081  -1108       N  
ATOM   4464  CA  TRP B 339      -7.511  22.344 -25.108  1.00131.25           C  
ANISOU 4464  CA  TRP B 339    20363  12546  16960   3797  -1343  -1044       C  
ATOM   4465  C   TRP B 339      -7.623  23.862 -25.206  1.00133.93           C  
ANISOU 4465  C   TRP B 339    21107  12368  17414   4056  -1480  -1141       C  
ATOM   4466  O   TRP B 339      -8.178  24.393 -26.168  1.00135.75           O  
ANISOU 4466  O   TRP B 339    21245  12492  17841   4396  -1509  -1073       O  
ATOM   4467  CB  TRP B 339      -7.014  21.774 -26.439  1.00 73.52           C  
ANISOU 4467  CB  TRP B 339    12862   5349   9725   3482  -1525   -727       C  
ATOM   4468  CG  TRP B 339      -6.264  20.487 -26.304  1.00 70.73           C  
ANISOU 4468  CG  TRP B 339    12303   5351   9221   3090  -1471   -645       C  
ATOM   4469  CD1 TRP B 339      -6.724  19.235 -26.589  1.00 69.21           C  
ANISOU 4469  CD1 TRP B 339    11681   5586   9031   3043  -1350   -530       C  
ATOM   4470  CD2 TRP B 339      -4.916  20.325 -25.849  1.00 69.15           C  
ANISOU 4470  CD2 TRP B 339    12319   5098   8859   2695  -1550   -666       C  
ATOM   4471  NE1 TRP B 339      -5.747  18.303 -26.341  1.00 66.86           N  
ANISOU 4471  NE1 TRP B 339    11331   5490   8583   2665  -1340   -483       N  
ATOM   4472  CE2 TRP B 339      -4.627  18.947 -25.884  1.00 66.72           C  
ANISOU 4472  CE2 TRP B 339    11688   5197   8465   2451  -1461   -560       C  
ATOM   4473  CE3 TRP B 339      -3.926  21.212 -25.415  1.00 69.54           C  
ANISOU 4473  CE3 TRP B 339    12799   4789   8834   2520  -1699   -760       C  
ATOM   4474  CZ2 TRP B 339      -3.389  18.434 -25.503  1.00 64.58           C  
ANISOU 4474  CZ2 TRP B 339    11493   4999   8045   2065  -1509   -539       C  
ATOM   4475  CZ3 TRP B 339      -2.698  20.700 -25.035  1.00 67.39           C  
ANISOU 4475  CZ3 TRP B 339    12590   4605   8412   2111  -1756   -736       C  
ATOM   4476  CH2 TRP B 339      -2.440  19.324 -25.082  1.00 64.88           C  
ANISOU 4476  CH2 TRP B 339    11926   4709   8019   1900  -1658   -624       C  
ATOM   4477  N   THR B 340      -7.092  24.555 -24.204  1.00123.65           N  
ANISOU 4477  N   THR B 340    20257  10734  15988   3890  -1577  -1297       N  
ATOM   4478  CA  THR B 340      -7.047  26.011 -24.221  1.00126.13           C  
ANISOU 4478  CA  THR B 340    21026  10499  16396   4077  -1734  -1398       C  
ATOM   4479  C   THR B 340      -5.691  26.478 -24.738  1.00124.98           C  
ANISOU 4479  C   THR B 340    21215  10052  16218   3619  -2017  -1271       C  
ATOM   4480  O   THR B 340      -4.802  25.663 -24.986  1.00122.26           O  
ANISOU 4480  O   THR B 340    20710   9953  15788   3198  -2070  -1105       O  
ATOM   4481  CB  THR B 340      -7.281  26.600 -22.818  1.00115.62           C  
ANISOU 4481  CB  THR B 340    20001   8987  14940   4362  -1573  -1771       C  
ATOM   4482  OG1 THR B 340      -6.244  26.160 -21.932  1.00113.38           O  
ANISOU 4482  OG1 THR B 340    19869   8809  14399   4013  -1544  -1905       O  
ATOM   4483  CG2 THR B 340      -8.631  26.158 -22.272  1.00116.87           C  
ANISOU 4483  CG2 THR B 340    19814   9458  15132   4828  -1265  -1891       C  
ATOM   4484  N   THR B 341      -5.537  27.788 -24.902  1.00123.32           N  
ANISOU 4484  N   THR B 341    21464   9306  16085   3704  -2196  -1344       N  
ATOM   4485  CA  THR B 341      -4.261  28.359 -25.324  1.00122.52           C  
ANISOU 4485  CA  THR B 341    21708   8881  15962   3262  -2469  -1228       C  
ATOM   4486  C   THR B 341      -3.203  28.109 -24.254  1.00121.33           C  
ANISOU 4486  C   THR B 341    21721   8806  15573   2911  -2452  -1401       C  
ATOM   4487  O   THR B 341      -2.038  27.820 -24.558  1.00119.21           O  
ANISOU 4487  O   THR B 341    21446   8607  15240   2432  -2593  -1236       O  
ATOM   4488  CB  THR B 341      -4.376  29.874 -25.573  1.00108.05           C  
ANISOU 4488  CB  THR B 341    20372   6417  14266   3449  -2663  -1293       C  
ATOM   4489  OG1 THR B 341      -4.677  30.541 -24.341  1.00113.18           O  
ANISOU 4489  OG1 THR B 341    21342   6839  14824   3736  -2550  -1669       O  
ATOM   4490  CG2 THR B 341      -5.473  30.168 -26.588  1.00110.60           C  
ANISOU 4490  CG2 THR B 341    20538   6656  14830   3827  -2697  -1115       C  
ATOM   4491  N   PHE B 342      -3.627  28.219 -22.997  1.00106.06           N  
ANISOU 4491  N   PHE B 342    19921   6875  13502   3162  -2274  -1729       N  
ATOM   4492  CA  PHE B 342      -2.758  27.960 -21.858  1.00105.17           C  
ANISOU 4492  CA  PHE B 342    19988   6835  13140   2878  -2256  -1923       C  
ATOM   4493  C   PHE B 342      -2.222  26.537 -21.889  1.00 98.52           C  
ANISOU 4493  C   PHE B 342    18717   6534  12180   2552  -2168  -1763       C  
ATOM   4494  O   PHE B 342      -1.033  26.315 -21.691  1.00 96.65           O  
ANISOU 4494  O   PHE B 342    18561   6327  11834   2106  -2309  -1700       O  
ATOM   4495  CB  PHE B 342      -3.497  28.208 -20.540  1.00114.92           C  
ANISOU 4495  CB  PHE B 342    21409   8025  14227   3264  -2040  -2301       C  
ATOM   4496  CG  PHE B 342      -2.781  27.667 -19.333  1.00113.35           C  
ANISOU 4496  CG  PHE B 342    21306   8024  13735   3010  -1977  -2488       C  
ATOM   4497  CD1 PHE B 342      -1.690  28.335 -18.801  1.00116.96           C  
ANISOU 4497  CD1 PHE B 342    22224   8150  14064   2682  -2203  -2609       C  
ATOM   4498  CD2 PHE B 342      -3.202  26.493 -18.728  1.00108.71           C  
ANISOU 4498  CD2 PHE B 342    20352   7950  13001   3085  -1709  -2530       C  
ATOM   4499  CE1 PHE B 342      -1.031  27.840 -17.691  1.00115.99           C  
ANISOU 4499  CE1 PHE B 342    22189   8218  13664   2444  -2171  -2771       C  
ATOM   4500  CE2 PHE B 342      -2.547  25.994 -17.619  1.00107.66           C  
ANISOU 4500  CE2 PHE B 342    20316   7999  12588   2853  -1665  -2683       C  
ATOM   4501  CZ  PHE B 342      -1.460  26.668 -17.100  1.00111.33           C  
ANISOU 4501  CZ  PHE B 342    21236   8142  12919   2537  -1902  -2805       C  
ATOM   4502  N   LEU B 343      -3.106  25.576 -22.137  1.00107.16           N  
ANISOU 4502  N   LEU B 343    19355   8052  13310   2776  -1941  -1695       N  
ATOM   4503  CA  LEU B 343      -2.709  24.174 -22.194  1.00104.21           C  
ANISOU 4503  CA  LEU B 343    18571   8182  12843   2508  -1844  -1544       C  
ATOM   4504  C   LEU B 343      -1.817  23.892 -23.399  1.00102.00           C  
ANISOU 4504  C   LEU B 343    18155   7945  12657   2112  -2042  -1221       C  
ATOM   4505  O   LEU B 343      -1.027  22.954 -23.387  1.00 99.43           O  
ANISOU 4505  O   LEU B 343    17637   7910  12231   1772  -2043  -1113       O  
ATOM   4506  CB  LEU B 343      -3.938  23.261 -22.215  1.00 98.09           C  
ANISOU 4506  CB  LEU B 343    17347   7808  12113   2836  -1577  -1526       C  
ATOM   4507  CG  LEU B 343      -4.731  23.168 -20.910  1.00 99.54           C  
ANISOU 4507  CG  LEU B 343    17555   8112  12154   3168  -1312  -1819       C  
ATOM   4508  CD1 LEU B 343      -5.876  22.179 -21.049  1.00 99.43           C  
ANISOU 4508  CD1 LEU B 343    17050   8510  12218   3444  -1064  -1748       C  
ATOM   4509  CD2 LEU B 343      -3.819  22.779 -19.757  1.00 98.07           C  
ANISOU 4509  CD2 LEU B 343    17506   8063  11692   2887  -1278  -1962       C  
ATOM   4510  N   PHE B 344      -1.952  24.717 -24.432  1.00 80.96           N  
ANISOU 4510  N   PHE B 344    15597   4985  10180   2169  -2204  -1066       N  
ATOM   4511  CA  PHE B 344      -1.141  24.609 -25.638  1.00 78.80           C  
ANISOU 4511  CA  PHE B 344    15231   4719   9990   1818  -2385   -753       C  
ATOM   4512  C   PHE B 344       0.298  25.017 -25.327  1.00 80.27           C  
ANISOU 4512  C   PHE B 344    15715   4699  10083   1368  -2582   -742       C  
ATOM   4513  O   PHE B 344       1.245  24.221 -25.473  1.00 75.99           O  
ANISOU 4513  O   PHE B 344    14982   4420   9471    993  -2609   -591       O  
ATOM   4514  CB  PHE B 344      -1.726  25.526 -26.716  1.00 86.12           C  
ANISOU 4514  CB  PHE B 344    16250   5347  11125   2029  -2512   -604       C  
ATOM   4515  CG  PHE B 344      -1.283  25.199 -28.115  1.00 83.88           C  
ANISOU 4515  CG  PHE B 344    15796   5154  10919   1749  -2645   -261       C  
ATOM   4516  CD1 PHE B 344      -1.955  24.246 -28.863  1.00 79.48           C  
ANISOU 4516  CD1 PHE B 344    14806   4991  10401   1815  -2539    -91       C  
ATOM   4517  CD2 PHE B 344      -0.215  25.865 -28.692  1.00 86.90           C  
ANISOU 4517  CD2 PHE B 344    16465   5220  11332   1421  -2877   -107       C  
ATOM   4518  CE1 PHE B 344      -1.558  23.951 -30.152  1.00 78.05           C  
ANISOU 4518  CE1 PHE B 344    14496   4895  10264   1570  -2654    209       C  
ATOM   4519  CE2 PHE B 344       0.186  25.574 -29.982  1.00 85.43           C  
ANISOU 4519  CE2 PHE B 344    16130   5132  11198   1171  -2977    212       C  
ATOM   4520  CZ  PHE B 344      -0.486  24.614 -30.712  1.00 80.99           C  
ANISOU 4520  CZ  PHE B 344    15151   4971  10652   1254  -2861    362       C  
ATOM   4521  N   ASP B 345       0.448  26.266 -24.891  1.00 87.81           N  
ANISOU 4521  N   ASP B 345    17136   5181  11045   1411  -2721   -907       N  
ATOM   4522  CA  ASP B 345       1.755  26.804 -24.530  1.00 90.54           C  
ANISOU 4522  CA  ASP B 345    17802   5278  11320    980  -2939   -906       C  
ATOM   4523  C   ASP B 345       2.427  25.936 -23.467  1.00 87.17           C  
ANISOU 4523  C   ASP B 345    17280   5159  10679    747  -2866  -1035       C  
ATOM   4524  O   ASP B 345       3.601  25.571 -23.595  1.00 85.42           O  
ANISOU 4524  O   ASP B 345    16997   5049  10407    307  -2988   -889       O  
ATOM   4525  CB  ASP B 345       1.616  28.244 -24.031  1.00133.31           C  
ANISOU 4525  CB  ASP B 345    23765  10116  16771   1120  -3086  -1114       C  
ATOM   4526  CG  ASP B 345       0.838  29.122 -24.994  1.00135.11           C  
ANISOU 4526  CG  ASP B 345    24107  10014  17217   1408  -3159   -997       C  
ATOM   4527  OD1 ASP B 345       0.860  28.835 -26.210  1.00133.73           O  
ANISOU 4527  OD1 ASP B 345    23696   9957  17161   1295  -3212   -685       O  
ATOM   4528  OD2 ASP B 345       0.206  30.099 -24.538  1.00137.94           O  
ANISOU 4528  OD2 ASP B 345    24798   9993  17620   1758  -3164  -1218       O  
ATOM   4529  N   PHE B 346       1.666  25.599 -22.428  1.00 83.47           N  
ANISOU 4529  N   PHE B 346    16786   4844  10085   1053  -2662  -1295       N  
ATOM   4530  CA  PHE B 346       2.147  24.723 -21.366  1.00 80.52           C  
ANISOU 4530  CA  PHE B 346    16318   4785   9492    888  -2572  -1420       C  
ATOM   4531  C   PHE B 346       2.580  23.376 -21.925  1.00 73.12           C  
ANISOU 4531  C   PHE B 346    14901   4326   8555    652  -2503  -1166       C  
ATOM   4532  O   PHE B 346       3.571  22.811 -21.473  1.00 71.25           O  
ANISOU 4532  O   PHE B 346    14609   4265   8197    310  -2568  -1130       O  
ATOM   4533  CB  PHE B 346       1.072  24.520 -20.293  1.00 84.85           C  
ANISOU 4533  CB  PHE B 346    16874   5455   9910   1302  -2320  -1708       C  
ATOM   4534  CG  PHE B 346       1.427  23.481 -19.263  1.00 81.17           C  
ANISOU 4534  CG  PHE B 346    16236   5390   9216   1170  -2191  -1788       C  
ATOM   4535  CD1 PHE B 346       2.263  23.795 -18.203  1.00 84.25           C  
ANISOU 4535  CD1 PHE B 346    16938   5678   9398    932  -2310  -1963       C  
ATOM   4536  CD2 PHE B 346       0.919  22.193 -19.350  1.00 75.11           C  
ANISOU 4536  CD2 PHE B 346    15007   5092   8442   1274  -1967  -1682       C  
ATOM   4537  CE1 PHE B 346       2.589  22.845 -17.255  1.00 81.41           C  
ANISOU 4537  CE1 PHE B 346    16428   5686   8820    813  -2208  -2019       C  
ATOM   4538  CE2 PHE B 346       1.243  21.240 -18.405  1.00 72.16           C  
ANISOU 4538  CE2 PHE B 346    14490   5067   7862   1152  -1856  -1737       C  
ATOM   4539  CZ  PHE B 346       2.078  21.566 -17.356  1.00 75.34           C  
ANISOU 4539  CZ  PHE B 346    15202   5373   8051    929  -1977  -1900       C  
ATOM   4540  N   TYR B 347       1.836  22.867 -22.904  1.00 72.85           N  
ANISOU 4540  N   TYR B 347    14525   4495   8657    841  -2381   -995       N  
ATOM   4541  CA  TYR B 347       2.184  21.596 -23.533  1.00 68.26           C  
ANISOU 4541  CA  TYR B 347    13510   4339   8086    642  -2313   -760       C  
ATOM   4542  C   TYR B 347       3.542  21.676 -24.213  1.00 67.22           C  
ANISOU 4542  C   TYR B 347    13404   4144   7991    191  -2523   -536       C  
ATOM   4543  O   TYR B 347       4.332  20.734 -24.146  1.00 64.20           O  
ANISOU 4543  O   TYR B 347    12806   4053   7534    -90  -2516   -435       O  
ATOM   4544  CB  TYR B 347       1.128  21.161 -24.551  1.00 69.85           C  
ANISOU 4544  CB  TYR B 347    13393   4713   8435    908  -2187   -616       C  
ATOM   4545  CG  TYR B 347       1.483  19.882 -25.276  1.00 65.16           C  
ANISOU 4545  CG  TYR B 347    12387   4522   7850    707  -2127   -385       C  
ATOM   4546  CD1 TYR B 347       1.282  18.647 -24.674  1.00 62.92           C  
ANISOU 4546  CD1 TYR B 347    11807   4632   7470    755  -1935   -430       C  
ATOM   4547  CD2 TYR B 347       2.031  19.910 -26.554  1.00 64.41           C  
ANISOU 4547  CD2 TYR B 347    12217   4407   7851    470  -2256   -123       C  
ATOM   4548  CE1 TYR B 347       1.608  17.475 -25.325  1.00 60.22           C  
ANISOU 4548  CE1 TYR B 347    11116   4625   7139    584  -1884   -234       C  
ATOM   4549  CE2 TYR B 347       2.362  18.741 -27.213  1.00 60.53           C  
ANISOU 4549  CE2 TYR B 347    11372   4272   7354    305  -2189     65       C  
ATOM   4550  CZ  TYR B 347       2.148  17.526 -26.593  1.00 58.82           C  
ANISOU 4550  CZ  TYR B 347    10878   4418   7054    369  -2008      2       C  
ATOM   4551  OH  TYR B 347       2.476  16.357 -27.242  1.00 55.91           O  
ANISOU 4551  OH  TYR B 347    10184   4375   6686    217  -1945    176       O  
ATOM   4552  N   HIS B 348       3.815  22.797 -24.873  1.00 85.73           N  
ANISOU 4552  N   HIS B 348    16014   6105  10456    122  -2707   -451       N  
ATOM   4553  CA  HIS B 348       5.090  22.924 -25.580  1.00 84.43           C  
ANISOU 4553  CA  HIS B 348    15851   5890  10339   -310  -2891   -206       C  
ATOM   4554  C   HIS B 348       6.296  23.208 -24.669  1.00 84.13           C  
ANISOU 4554  C   HIS B 348    16030   5741  10194   -682  -3056   -279       C  
ATOM   4555  O   HIS B 348       7.390  22.666 -24.886  1.00 82.26           O  
ANISOU 4555  O   HIS B 348    15644   5651   9960  -1062  -3144    -80       O  
ATOM   4556  CB  HIS B 348       4.978  23.930 -26.726  1.00 72.24           C  
ANISOU 4556  CB  HIS B 348    14481   4006   8961   -287  -3029    -36       C  
ATOM   4557  CG  HIS B 348       4.023  23.504 -27.797  1.00 69.41           C  
ANISOU 4557  CG  HIS B 348    13841   3831   8703    -27  -2907    116       C  
ATOM   4558  ND1 HIS B 348       2.661  23.685 -27.693  1.00 69.86           N  
ANISOU 4558  ND1 HIS B 348    13885   3844   8813    429  -2791    -20       N  
ATOM   4559  CD2 HIS B 348       4.230  22.879 -28.981  1.00 66.55           C  
ANISOU 4559  CD2 HIS B 348    13188   3710   8386   -163  -2886    387       C  
ATOM   4560  CE1 HIS B 348       2.071  23.203 -28.773  1.00 67.40           C  
ANISOU 4560  CE1 HIS B 348    13289   3736   8585    546  -2728    169       C  
ATOM   4561  NE2 HIS B 348       3.001  22.709 -29.570  1.00 65.38           N  
ANISOU 4561  NE2 HIS B 348    12878   3650   8315    194  -2783    410       N  
ATOM   4562  N   TYR B 349       6.102  24.038 -23.648  1.00 76.81           N  
ANISOU 4562  N   TYR B 349    15450   4568   9169   -575  -3100   -562       N  
ATOM   4563  CA  TYR B 349       7.159  24.247 -22.659  1.00 79.44           C  
ANISOU 4563  CA  TYR B 349    15971   4846   9367   -920  -3259   -658       C  
ATOM   4564  C   TYR B 349       7.455  22.933 -21.932  1.00 74.21           C  
ANISOU 4564  C   TYR B 349    14979   4665   8553   -993  -3123   -678       C  
ATOM   4565  O   TYR B 349       8.614  22.591 -21.664  1.00 73.88           O  
ANISOU 4565  O   TYR B 349    14834   4780   8457  -1369  -3239   -573       O  
ATOM   4566  CB  TYR B 349       6.774  25.340 -21.656  1.00 83.53           C  
ANISOU 4566  CB  TYR B 349    16988   4953   9796   -771  -3345   -979       C  
ATOM   4567  CG  TYR B 349       6.757  26.741 -22.232  1.00 90.10           C  
ANISOU 4567  CG  TYR B 349    18220   5243  10771   -812  -3552   -955       C  
ATOM   4568  CD1 TYR B 349       7.914  27.319 -22.737  1.00 93.61           C  
ANISOU 4568  CD1 TYR B 349    18805   5485  11278  -1278  -3812   -780       C  
ATOM   4569  CD2 TYR B 349       5.589  27.493 -22.251  1.00 93.28           C  
ANISOU 4569  CD2 TYR B 349    18854   5333  11255   -385  -3490  -1098       C  
ATOM   4570  CE1 TYR B 349       7.905  28.600 -23.260  1.00 99.99           C  
ANISOU 4570  CE1 TYR B 349    19996   5777  12220  -1335  -4010   -742       C  
ATOM   4571  CE2 TYR B 349       5.570  28.775 -22.771  1.00 99.70           C  
ANISOU 4571  CE2 TYR B 349    20051   5622  12206   -410  -3690  -1067       C  
ATOM   4572  CZ  TYR B 349       6.731  29.324 -23.274  1.00102.98           C  
ANISOU 4572  CZ  TYR B 349    20625   5828  12675   -895  -3952   -887       C  
ATOM   4573  OH  TYR B 349       6.717  30.600 -23.793  1.00109.72           O  
ANISOU 4573  OH  TYR B 349    21879   6140  13670   -938  -4158   -841       O  
ATOM   4574  N   PHE B 350       6.393  22.192 -21.631  1.00 68.18           N  
ANISOU 4574  N   PHE B 350    14038   4135   7730   -627  -2879   -797       N  
ATOM   4575  CA  PHE B 350       6.522  20.891 -20.989  1.00 63.23           C  
ANISOU 4575  CA  PHE B 350    13102   3954   6968   -640  -2726   -808       C  
ATOM   4576  C   PHE B 350       7.194  19.906 -21.933  1.00 58.56           C  
ANISOU 4576  C   PHE B 350    12111   3680   6461   -900  -2725   -508       C  
ATOM   4577  O   PHE B 350       7.858  18.970 -21.492  1.00 56.44           O  
ANISOU 4577  O   PHE B 350    11655   3693   6095  -1101  -2724   -461       O  
ATOM   4578  CB  PHE B 350       5.151  20.366 -20.559  1.00 74.11           C  
ANISOU 4578  CB  PHE B 350    14329   5517   8313   -201  -2453   -938       C  
ATOM   4579  CG  PHE B 350       5.211  19.174 -19.650  1.00 72.52           C  
ANISOU 4579  CG  PHE B 350    13922   5698   7933   -188  -2300  -1009       C  
ATOM   4580  CD1 PHE B 350       5.846  19.256 -18.422  1.00 71.70           C  
ANISOU 4580  CD1 PHE B 350    13935   5650   7657   -464  -2422  -1072       C  
ATOM   4581  CD2 PHE B 350       4.616  17.978 -20.014  1.00 71.98           C  
ANISOU 4581  CD2 PHE B 350    13545   5931   7871     89  -2048   -998       C  
ATOM   4582  CE1 PHE B 350       5.899  18.164 -17.582  1.00 70.26           C  
ANISOU 4582  CE1 PHE B 350    13578   5812   7303   -450  -2293  -1118       C  
ATOM   4583  CE2 PHE B 350       4.663  16.884 -19.177  1.00 70.56           C  
ANISOU 4583  CE2 PHE B 350    13191   6088   7528     89  -1909  -1044       C  
ATOM   4584  CZ  PHE B 350       5.306  16.976 -17.960  1.00 69.63           C  
ANISOU 4584  CZ  PHE B 350    13206   6018   7231   -173  -2030  -1101       C  
ATOM   4585  N   TYR B 351       7.014  20.117 -23.234  1.00 70.07           N  
ANISOU 4585  N   TYR B 351    13447   5087   8090   -881  -2725   -305       N  
ATOM   4586  CA  TYR B 351       7.705  19.314 -24.233  1.00 67.54           C  
ANISOU 4586  CA  TYR B 351    12783   5034   7846  -1120  -2719    -23       C  
ATOM   4587  C   TYR B 351       9.200  19.555 -24.102  1.00 66.80           C  
ANISOU 4587  C   TYR B 351    12733   4924   7726  -1562  -2915     79       C  
ATOM   4588  O   TYR B 351       9.993  18.604 -24.042  1.00 64.51           O  
ANISOU 4588  O   TYR B 351    12152   4960   7400  -1749  -2883    195       O  
ATOM   4589  CB  TYR B 351       7.227  19.667 -25.642  1.00 63.66           C  
ANISOU 4589  CB  TYR B 351    12257   4415   7517  -1053  -2727    165       C  
ATOM   4590  CG  TYR B 351       7.957  18.933 -26.744  1.00 61.22           C  
ANISOU 4590  CG  TYR B 351    11610   4386   7267  -1261  -2692    444       C  
ATOM   4591  CD1 TYR B 351       7.533  17.680 -27.167  1.00 59.40           C  
ANISOU 4591  CD1 TYR B 351    11038   4492   7042  -1088  -2500    508       C  
ATOM   4592  CD2 TYR B 351       9.065  19.496 -27.367  1.00 60.87           C  
ANISOU 4592  CD2 TYR B 351    11591   4266   7270  -1633  -2844    642       C  
ATOM   4593  CE1 TYR B 351       8.194  17.005 -28.176  1.00 57.11           C  
ANISOU 4593  CE1 TYR B 351    10466   4445   6789  -1260  -2457    740       C  
ATOM   4594  CE2 TYR B 351       9.734  18.830 -28.376  1.00 58.82           C  
ANISOU 4594  CE2 TYR B 351    11024   4274   7050  -1803  -2784    888       C  
ATOM   4595  CZ  TYR B 351       9.294  17.585 -28.777  1.00 56.87           C  
ANISOU 4595  CZ  TYR B 351    10465   4348   6794  -1605  -2589    926       C  
ATOM   4596  OH  TYR B 351       9.955  16.916 -29.780  1.00 54.79           O  
ANISOU 4596  OH  TYR B 351     9923   4340   6555  -1758  -2521   1149       O  
ATOM   4597  N   MET B 352       9.570  20.834 -24.053  1.00 86.12           N  
ANISOU 4597  N   MET B 352    15542   6980  10201  -1724  -3125     36       N  
ATOM   4598  CA  MET B 352      10.958  21.225 -23.818  1.00 86.04           C  
ANISOU 4598  CA  MET B 352    15606   6908  10177  -2165  -3344    124       C  
ATOM   4599  C   MET B 352      11.521  20.508 -22.595  1.00 84.97           C  
ANISOU 4599  C   MET B 352    15400   7010   9876  -2258  -3354     -6       C  
ATOM   4600  O   MET B 352      12.567  19.857 -22.673  1.00 83.11           O  
ANISOU 4600  O   MET B 352    14911   7030   9637  -2548  -3409    154       O  
ATOM   4601  CB  MET B 352      11.070  22.739 -23.624  1.00 73.61           C  
ANISOU 4601  CB  MET B 352    14504   4826   8638  -2283  -3573     33       C  
ATOM   4602  CG  MET B 352      10.710  23.568 -24.846  1.00 75.70           C  
ANISOU 4602  CG  MET B 352    14873   4816   9071  -2252  -3613    202       C  
ATOM   4603  SD  MET B 352      10.812  25.339 -24.512  1.00 84.43           S  
ANISOU 4603  SD  MET B 352    16586   5272  10221  -2344  -3881     67       S  
ATOM   4604  CE  MET B 352      10.474  26.017 -26.135  1.00 86.13           C  
ANISOU 4604  CE  MET B 352    16808   5280  10638  -2374  -3918    374       C  
ATOM   4605  N   LEU B 353      10.807  20.613 -21.476  1.00 68.62           N  
ANISOU 4605  N   LEU B 353    13542   4868   7662  -1998  -3291   -287       N  
ATOM   4606  CA  LEU B 353      11.246  19.997 -20.222  1.00 68.62           C  
ANISOU 4606  CA  LEU B 353    13521   5081   7471  -2075  -3308   -419       C  
ATOM   4607  C   LEU B 353      11.438  18.482 -20.324  1.00 62.91           C  
ANISOU 4607  C   LEU B 353    12331   4839   6733  -2068  -3144   -266       C  
ATOM   4608  O   LEU B 353      12.526  17.964 -20.049  1.00 63.34           O  
ANISOU 4608  O   LEU B 353    12215   5100   6751  -2353  -3249   -155       O  
ATOM   4609  CB  LEU B 353      10.262  20.321 -19.094  1.00 69.16           C  
ANISOU 4609  CB  LEU B 353    13891   5018   7369  -1753  -3219   -746       C  
ATOM   4610  CG  LEU B 353      10.571  19.700 -17.730  1.00 70.66           C  
ANISOU 4610  CG  LEU B 353    14155   5372   7318  -1847  -3268   -904       C  
ATOM   4611  CD1 LEU B 353      11.932  20.159 -17.227  1.00 76.39           C  
ANISOU 4611  CD1 LEU B 353    15098   5924   8001  -2279  -3592   -894       C  
ATOM   4612  CD2 LEU B 353       9.480  20.043 -16.728  1.00 72.40           C  
ANISOU 4612  CD2 LEU B 353    14663   5490   7355  -1492  -3128  -1223       C  
ATOM   4613  N   THR B 354      10.377  17.782 -20.718  1.00 65.06           N  
ANISOU 4613  N   THR B 354    12397   5279   7042  -1742  -2898   -257       N  
ATOM   4614  CA  THR B 354      10.390  16.324 -20.800  1.00 62.31           C  
ANISOU 4614  CA  THR B 354    11642   5351   6682  -1691  -2727   -137       C  
ATOM   4615  C   THR B 354      11.478  15.799 -21.726  1.00 60.31           C  
ANISOU 4615  C   THR B 354    11084   5283   6549  -1982  -2788    144       C  
ATOM   4616  O   THR B 354      12.229  14.896 -21.356  1.00 58.46           O  
ANISOU 4616  O   THR B 354    10619   5329   6265  -2120  -2791    226       O  
ATOM   4617  CB  THR B 354       9.034  15.766 -21.272  1.00 57.22           C  
ANISOU 4617  CB  THR B 354    10833   4814   6092  -1322  -2476   -152       C  
ATOM   4618  OG1 THR B 354       8.692  16.341 -22.540  1.00 57.82           O  
ANISOU 4618  OG1 THR B 354    10886   4739   6341  -1296  -2485    -13       O  
ATOM   4619  CG2 THR B 354       7.947  16.079 -20.260  1.00 59.36           C  
ANISOU 4619  CG2 THR B 354    11351   4955   6248  -1008  -2376   -421       C  
ATOM   4620  N   ASN B 355      11.562  16.360 -22.929  1.00 62.58           N  
ANISOU 4620  N   ASN B 355    11371   5418   6988  -2066  -2832    297       N  
ATOM   4621  CA  ASN B 355      12.581  15.920 -23.877  1.00 60.98           C  
ANISOU 4621  CA  ASN B 355    10873   5403   6891  -2324  -2855    566       C  
ATOM   4622  C   ASN B 355      13.998  16.247 -23.399  1.00 61.46           C  
ANISOU 4622  C   ASN B 355    10959   5455   6936  -2716  -3079    638       C  
ATOM   4623  O   ASN B 355      14.939  15.475 -23.630  1.00 60.26           O  
ANISOU 4623  O   ASN B 355    10493   5579   6824  -2905  -3076    819       O  
ATOM   4624  CB  ASN B 355      12.310  16.492 -25.269  1.00 60.70           C  
ANISOU 4624  CB  ASN B 355    10843   5222   6998  -2314  -2834    722       C  
ATOM   4625  CG  ASN B 355      11.176  15.776 -25.982  1.00 59.58           C  
ANISOU 4625  CG  ASN B 355    10529   5220   6888  -1986  -2613    732       C  
ATOM   4626  OD1 ASN B 355      11.404  15.007 -26.914  1.00 57.71           O  
ANISOU 4626  OD1 ASN B 355    10015   5200   6712  -2015  -2511    914       O  
ATOM   4627  ND2 ASN B 355       9.947  16.016 -25.538  1.00 60.89           N  
ANISOU 4627  ND2 ASN B 355    10856   5269   7011  -1673  -2537    532       N  
ATOM   4628  N   ALA B 356      14.143  17.383 -22.719  1.00 58.53           N  
ANISOU 4628  N   ALA B 356    10960   4768   6511  -2832  -3277    491       N  
ATOM   4629  CA  ALA B 356      15.413  17.721 -22.085  1.00 63.31           C  
ANISOU 4629  CA  ALA B 356    11614   5358   7083  -3210  -3520    527       C  
ATOM   4630  C   ALA B 356      15.805  16.628 -21.095  1.00 61.70           C  
ANISOU 4630  C   ALA B 356    11205   5488   6751  -3204  -3494    486       C  
ATOM   4631  O   ALA B 356      16.958  16.194 -21.058  1.00 63.04           O  
ANISOU 4631  O   ALA B 356    11127   5873   6952  -3472  -3593    652       O  
ATOM   4632  CB  ALA B 356      15.327  19.069 -21.387  1.00 72.16           C  
ANISOU 4632  CB  ALA B 356    13218   6061   8137  -3297  -3735    326       C  
ATOM   4633  N   LEU B 357      14.835  16.181 -20.302  1.00 61.62           N  
ANISOU 4633  N   LEU B 357    11286   5528   6601  -2891  -3353    281       N  
ATOM   4634  CA  LEU B 357      15.062  15.086 -19.362  1.00 60.19           C  
ANISOU 4634  CA  LEU B 357    10923   5662   6286  -2852  -3308    253       C  
ATOM   4635  C   LEU B 357      15.412  13.788 -20.087  1.00 56.05           C  
ANISOU 4635  C   LEU B 357     9930   5497   5869  -2838  -3155    486       C  
ATOM   4636  O   LEU B 357      16.189  12.974 -19.583  1.00 56.51           O  
ANISOU 4636  O   LEU B 357     9774   5813   5887  -2957  -3205    572       O  
ATOM   4637  CB  LEU B 357      13.839  14.874 -18.468  1.00 72.81           C  
ANISOU 4637  CB  LEU B 357    12703   7249   7713  -2509  -3150      6       C  
ATOM   4638  CG  LEU B 357      13.613  15.905 -17.362  1.00 77.30           C  
ANISOU 4638  CG  LEU B 357    13734   7535   8104  -2513  -3295   -263       C  
ATOM   4639  CD1 LEU B 357      12.389  15.543 -16.539  1.00 75.97           C  
ANISOU 4639  CD1 LEU B 357    13688   7416   7764  -2150  -3086   -485       C  
ATOM   4640  CD2 LEU B 357      14.845  16.017 -16.478  1.00 81.27           C  
ANISOU 4640  CD2 LEU B 357    14302   8086   8492  -2855  -3565   -254       C  
ATOM   4641  N   VAL B 358      14.829  13.597 -21.267  1.00 66.25           N  
ANISOU 4641  N   VAL B 358    11080   6799   7294  -2684  -2978    584       N  
ATOM   4642  CA  VAL B 358      15.141  12.435 -22.092  1.00 63.84           C  
ANISOU 4642  CA  VAL B 358    10367   6801   7090  -2661  -2826    789       C  
ATOM   4643  C   VAL B 358      16.617  12.438 -22.477  1.00 63.98           C  
ANISOU 4643  C   VAL B 358    10170   6937   7204  -3004  -2968   1008       C  
ATOM   4644  O   VAL B 358      17.303  11.417 -22.367  1.00 62.59           O  
ANISOU 4644  O   VAL B 358     9690   7052   7042  -3050  -2935   1126       O  
ATOM   4645  CB  VAL B 358      14.276  12.395 -23.368  1.00 55.65           C  
ANISOU 4645  CB  VAL B 358     9261   5721   6162  -2464  -2643    849       C  
ATOM   4646  CG1 VAL B 358      14.792  11.340 -24.334  1.00 53.50           C  
ANISOU 4646  CG1 VAL B 358     8604   5732   5990  -2499  -2516   1067       C  
ATOM   4647  CG2 VAL B 358      12.819  12.141 -23.016  1.00 55.41           C  
ANISOU 4647  CG2 VAL B 358     9332   5661   6058  -2108  -2475    666       C  
ATOM   4648  N   TYR B 359      17.111  13.591 -22.917  1.00 54.51           N  
ANISOU 4648  N   TYR B 359     9122   5510   6078  -3245  -3126   1070       N  
ATOM   4649  CA  TYR B 359      18.527  13.701 -23.263  1.00 58.04           C  
ANISOU 4649  CA  TYR B 359     9351   6074   6626  -3596  -3260   1292       C  
ATOM   4650  C   TYR B 359      19.431  13.603 -22.032  1.00 61.77           C  
ANISOU 4650  C   TYR B 359     9818   6636   7017  -3811  -3478   1260       C  
ATOM   4651  O   TYR B 359      20.571  13.134 -22.123  1.00 63.66           O  
ANISOU 4651  O   TYR B 359     9746   7110   7329  -4023  -3545   1448       O  
ATOM   4652  CB  TYR B 359      18.801  14.974 -24.064  1.00 80.87           C  
ANISOU 4652  CB  TYR B 359    12408   8695   9621  -3823  -3372   1391       C  
ATOM   4653  CG  TYR B 359      18.200  14.933 -25.450  1.00 80.12           C  
ANISOU 4653  CG  TYR B 359    12248   8579   9612  -3660  -3171   1493       C  
ATOM   4654  CD1 TYR B 359      18.667  14.032 -26.401  1.00 78.48           C  
ANISOU 4654  CD1 TYR B 359    11665   8676   9478  -3635  -2990   1687       C  
ATOM   4655  CD2 TYR B 359      17.152  15.774 -25.803  1.00 81.25           C  
ANISOU 4655  CD2 TYR B 359    12716   8399   9757  -3516  -3167   1390       C  
ATOM   4656  CE1 TYR B 359      18.117  13.982 -27.668  1.00 77.93           C  
ANISOU 4656  CE1 TYR B 359    11557   8594   9459  -3495  -2820   1774       C  
ATOM   4657  CE2 TYR B 359      16.596  15.730 -27.068  1.00 80.74           C  
ANISOU 4657  CE2 TYR B 359    12595   8323   9759  -3371  -3008   1494       C  
ATOM   4658  CZ  TYR B 359      17.083  14.833 -27.995  1.00 79.03           C  
ANISOU 4658  CZ  TYR B 359    12015   8418   9592  -3371  -2839   1684       C  
ATOM   4659  OH  TYR B 359      16.534  14.786 -29.255  1.00 78.62           O  
ANISOU 4659  OH  TYR B 359    11929   8361   9579  -3236  -2694   1782       O  
ATOM   4660  N   VAL B 360      18.915  14.037 -20.883  1.00 69.86           N  
ANISOU 4660  N   VAL B 360    11179   7483   7882  -3744  -3587   1022       N  
ATOM   4661  CA  VAL B 360      19.609  13.836 -19.614  1.00 70.99           C  
ANISOU 4661  CA  VAL B 360    11346   7728   7900  -3905  -3789    966       C  
ATOM   4662  C   VAL B 360      19.792  12.341 -19.368  1.00 68.52           C  
ANISOU 4662  C   VAL B 360    10678   7794   7563  -3758  -3655   1053       C  
ATOM   4663  O   VAL B 360      20.860  11.895 -18.945  1.00 70.27           O  
ANISOU 4663  O   VAL B 360    10673   8226   7798  -3955  -3797   1183       O  
ATOM   4664  CB  VAL B 360      18.845  14.471 -18.430  1.00 67.09           C  
ANISOU 4664  CB  VAL B 360    11310   6986   7198  -3803  -3884    667       C  
ATOM   4665  CG1 VAL B 360      19.422  14.003 -17.102  1.00 69.70           C  
ANISOU 4665  CG1 VAL B 360    11640   7491   7352  -3895  -4042    606       C  
ATOM   4666  CG2 VAL B 360      18.883  15.988 -18.523  1.00 71.88           C  
ANISOU 4666  CG2 VAL B 360    12290   7194   7827  -4010  -4088    582       C  
ATOM   4667  N   SER B 361      18.745  11.571 -19.651  1.00 64.36           N  
ANISOU 4667  N   SER B 361    10098   7345   7012  -3413  -3390    991       N  
ATOM   4668  CA  SER B 361      18.822  10.117 -19.557  1.00 62.12           C  
ANISOU 4668  CA  SER B 361     9490   7386   6727  -3254  -3240   1082       C  
ATOM   4669  C   SER B 361      19.822   9.574 -20.569  1.00 61.43           C  
ANISOU 4669  C   SER B 361     8994   7517   6829  -3380  -3195   1346       C  
ATOM   4670  O   SER B 361      20.506   8.584 -20.313  1.00 60.66           O  
ANISOU 4670  O   SER B 361     8610   7686   6754  -3382  -3190   1465       O  
ATOM   4671  CB  SER B 361      17.451   9.485 -19.799  1.00 92.65           C  
ANISOU 4671  CB  SER B 361    13386  11262  10554  -2888  -2966    973       C  
ATOM   4672  OG  SER B 361      17.532   8.070 -19.803  1.00 90.52           O  
ANISOU 4672  OG  SER B 361    12801  11279  10316  -2750  -2816   1083       O  
ATOM   4673  N   ALA B 362      19.900  10.227 -21.722  1.00 61.53           N  
ANISOU 4673  N   ALA B 362     8990   7415   6975  -3475  -3158   1441       N  
ATOM   4674  CA  ALA B 362      20.823   9.806 -22.769  1.00 61.62           C  
ANISOU 4674  CA  ALA B 362     8630   7632   7154  -3592  -3086   1687       C  
ATOM   4675  C   ALA B 362      22.272  10.162 -22.441  1.00 65.55           C  
ANISOU 4675  C   ALA B 362     8969   8222   7717  -3952  -3325   1842       C  
ATOM   4676  O   ALA B 362      23.198   9.676 -23.091  1.00 66.18           O  
ANISOU 4676  O   ALA B 362     8684   8534   7929  -4048  -3271   2055       O  
ATOM   4677  CB  ALA B 362      20.418  10.412 -24.107  1.00 77.31           C  
ANISOU 4677  CB  ALA B 362    10663   9478   9234  -3575  -2957   1749       C  
ATOM   4678  N   ALA B 363      22.467  11.007 -21.432  1.00 78.03           N  
ANISOU 4678  N   ALA B 363    10818   9625   9204  -4151  -3588   1732       N  
ATOM   4679  CA  ALA B 363      23.810  11.469 -21.087  1.00 81.31           C  
ANISOU 4679  CA  ALA B 363    11104  10107   9683  -4532  -3856   1874       C  
ATOM   4680  C   ALA B 363      24.254  11.110 -19.665  1.00 83.06           C  
ANISOU 4680  C   ALA B 363    11325  10455   9780  -4598  -4070   1816       C  
ATOM   4681  O   ALA B 363      25.378  11.418 -19.269  1.00 86.58           O  
ANISOU 4681  O   ALA B 363    11598  11016  10283  -4901  -4303   1953       O  
ATOM   4682  CB  ALA B 363      23.918  12.971 -21.308  1.00 73.67           C  
ANISOU 4682  CB  ALA B 363    10442   8811   8739  -4815  -4044   1843       C  
ATOM   4683  N   ILE B 364      23.380  10.457 -18.905  1.00 70.19           N  
ANISOU 4683  N   ILE B 364     9878   8816   7975  -4324  -3994   1627       N  
ATOM   4684  CA  ILE B 364      23.653  10.189 -17.492  1.00 73.02           C  
ANISOU 4684  CA  ILE B 364    10326   9256   8162  -4378  -4204   1545       C  
ATOM   4685  C   ILE B 364      24.571   8.983 -17.246  1.00 73.68           C  
ANISOU 4685  C   ILE B 364     9986   9703   8308  -4375  -4229   1744       C  
ATOM   4686  O   ILE B 364      25.416   9.015 -16.350  1.00 78.24           O  
ANISOU 4686  O   ILE B 364    10528  10377   8820  -4580  -4502   1786       O  
ATOM   4687  CB  ILE B 364      22.340  10.044 -16.674  1.00 69.35           C  
ANISOU 4687  CB  ILE B 364    10222   8662   7467  -4090  -4102   1279       C  
ATOM   4688  CG1 ILE B 364      22.642   9.828 -15.189  1.00 73.17           C  
ANISOU 4688  CG1 ILE B 364    10861   9209   7731  -4178  -4338   1186       C  
ATOM   4689  CG2 ILE B 364      21.477   8.916 -17.218  1.00 63.40           C  
ANISOU 4689  CG2 ILE B 364     9287   8059   6741  -3725  -3770   1295       C  
ATOM   4690  CD1 ILE B 364      23.385  10.980 -14.541  1.00 79.64           C  
ANISOU 4690  CD1 ILE B 364    11900   9861   8498  -4554  -4696   1142       C  
ATOM   4691  N   ASN B 365      24.415   7.937 -18.052  1.00 70.30           N  
ANISOU 4691  N   ASN B 365     9244   9463   8003  -4143  -3959   1866       N  
ATOM   4692  CA  ASN B 365      25.117   6.669 -17.826  1.00 70.54           C  
ANISOU 4692  CA  ASN B 365     8896   9814   8094  -4062  -3944   2035       C  
ATOM   4693  C   ASN B 365      26.654   6.704 -17.729  1.00 75.92           C  
ANISOU 4693  C   ASN B 365     9242  10696   8909  -4361  -4185   2260       C  
ATOM   4694  O   ASN B 365      27.216   6.116 -16.804  1.00 78.57           O  
ANISOU 4694  O   ASN B 365     9473  11199   9182  -4393  -4367   2315       O  
ATOM   4695  CB  ASN B 365      24.658   5.603 -18.831  1.00 92.35           C  
ANISOU 4695  CB  ASN B 365    11411  12703  10973  -3758  -3603   2109       C  
ATOM   4696  CG  ASN B 365      23.198   5.241 -18.666  1.00 90.29           C  
ANISOU 4696  CG  ASN B 365    11413  12319  10573  -3448  -3395   1912       C  
ATOM   4697  OD1 ASN B 365      22.424   5.279 -19.622  1.00 89.09           O  
ANISOU 4697  OD1 ASN B 365    11339  12046  10464  -3313  -3186   1851       O  
ATOM   4698  ND2 ASN B 365      22.813   4.887 -17.445  1.00 89.97           N  
ANISOU 4698  ND2 ASN B 365    11503  12322  10361  -3341  -3457   1823       N  
ATOM   4699  N   PRO B 366      27.339   7.378 -18.675  1.00 76.40           N  
ANISOU 4699  N   PRO B 366     9120  10755   9153  -4582  -4190   2405       N  
ATOM   4700  CA  PRO B 366      28.805   7.407 -18.578  1.00 82.17           C  
ANISOU 4700  CA  PRO B 366     9493  11703  10025  -4875  -4416   2633       C  
ATOM   4701  C   PRO B 366      29.296   8.098 -17.309  1.00 87.73           C  
ANISOU 4701  C   PRO B 366    10417  12321  10597  -5181  -4818   2566       C  
ATOM   4702  O   PRO B 366      30.335   7.723 -16.768  1.00 92.35           O  
ANISOU 4702  O   PRO B 366    10725  13128  11237  -5351  -5048   2724       O  
ATOM   4703  CB  PRO B 366      29.221   8.221 -19.808  1.00 95.79           C  
ANISOU 4703  CB  PRO B 366    11072  13389  11937  -5073  -4327   2771       C  
ATOM   4704  CG  PRO B 366      28.093   8.065 -20.764  1.00 89.74           C  
ANISOU 4704  CG  PRO B 366    10442  12497  11158  -4780  -3983   2672       C  
ATOM   4705  CD  PRO B 366      26.866   8.032 -19.909  1.00 86.47           C  
ANISOU 4705  CD  PRO B 366    10461  11870  10523  -4575  -3988   2403       C  
ATOM   4706  N   ILE B 367      28.548   9.094 -16.845  1.00 87.97           N  
ANISOU 4706  N   ILE B 367    10942  12031  10454  -5242  -4907   2331       N  
ATOM   4707  CA  ILE B 367      28.902   9.825 -15.635  1.00 93.34           C  
ANISOU 4707  CA  ILE B 367    11914  12585  10966  -5517  -5282   2218       C  
ATOM   4708  C   ILE B 367      28.794   8.928 -14.405  1.00 93.50           C  
ANISOU 4708  C   ILE B 367    11977  12760  10788  -5358  -5381   2154       C  
ATOM   4709  O   ILE B 367      29.634   8.987 -13.506  1.00 98.93           O  
ANISOU 4709  O   ILE B 367    12614  13561  11415  -5592  -5711   2215       O  
ATOM   4710  CB  ILE B 367      28.000  11.062 -15.447  1.00 92.79           C  
ANISOU 4710  CB  ILE B 367    12401  12107  10746  -5560  -5314   1951       C  
ATOM   4711  CG1 ILE B 367      28.016  11.930 -16.708  1.00 92.92           C  
ANISOU 4711  CG1 ILE B 367    12400  11950  10957  -5718  -5226   2034       C  
ATOM   4712  CG2 ILE B 367      28.435  11.871 -14.235  1.00 98.92           C  
ANISOU 4712  CG2 ILE B 367    13515  12741  11331  -5846  -5709   1812       C  
ATOM   4713  CD1 ILE B 367      27.132  13.154 -16.620  1.00 92.83           C  
ANISOU 4713  CD1 ILE B 367    12926  11515  10830  -5729  -5247   1789       C  
ATOM   4714  N   LEU B 368      27.759   8.094 -14.376  1.00 87.55           N  
ANISOU 4714  N   LEU B 368    11316  12016   9933  -4972  -5102   2043       N  
ATOM   4715  CA  LEU B 368      27.523   7.194 -13.251  1.00 87.38           C  
ANISOU 4715  CA  LEU B 368    11350  12137   9715  -4794  -5150   1996       C  
ATOM   4716  C   LEU B 368      28.624   6.146 -13.124  1.00 89.64           C  
ANISOU 4716  C   LEU B 368    11150  12768  10141  -4811  -5246   2267       C  
ATOM   4717  O   LEU B 368      28.926   5.681 -12.025  1.00 93.11           O  
ANISOU 4717  O   LEU B 368    11604  13337  10437  -4866  -5486   2295       O  
ATOM   4718  CB  LEU B 368      26.165   6.504 -13.394  1.00 80.99           C  
ANISOU 4718  CB  LEU B 368    10692  11272   8808  -4390  -4800   1854       C  
ATOM   4719  CG  LEU B 368      24.931   7.406 -13.369  1.00 78.86           C  
ANISOU 4719  CG  LEU B 368    10906  10684   8373  -4304  -4694   1570       C  
ATOM   4720  CD1 LEU B 368      23.667   6.583 -13.553  1.00 72.95           C  
ANISOU 4720  CD1 LEU B 368    10219   9940   7560  -3911  -4349   1473       C  
ATOM   4721  CD2 LEU B 368      24.876   8.201 -12.075  1.00 83.61           C  
ANISOU 4721  CD2 LEU B 368    11922  11146   8699  -4478  -4984   1380       C  
ATOM   4722  N   TYR B 369      29.219   5.780 -14.254  1.00100.30           N  
ANISOU 4722  N   TYR B 369    12078  14269  11764  -4749  -5054   2467       N  
ATOM   4723  CA  TYR B 369      30.278   4.778 -14.276  1.00101.03           C  
ANISOU 4723  CA  TYR B 369    11671  14688  12029  -4724  -5105   2732       C  
ATOM   4724  C   TYR B 369      31.554   5.321 -13.638  1.00103.80           C  
ANISOU 4724  C   TYR B 369    11865  15158  12417  -5108  -5519   2871       C  
ATOM   4725  O   TYR B 369      32.254   4.607 -12.921  1.00105.60           O  
ANISOU 4725  O   TYR B 369    11877  15598  12649  -5075  -5667   3006       O  
ATOM   4726  CB  TYR B 369      30.567   4.335 -15.711  1.00 87.46           C  
ANISOU 4726  CB  TYR B 369     9559  13086  10588  -4600  -4803   2895       C  
ATOM   4727  CG  TYR B 369      29.378   3.754 -16.445  1.00 80.52           C  
ANISOU 4727  CG  TYR B 369     8793  12112   9690  -4235  -4412   2778       C  
ATOM   4728  CD1 TYR B 369      28.324   3.167 -15.758  1.00 77.23           C  
ANISOU 4728  CD1 TYR B 369     8648  11624   9073  -3979  -4328   2620       C  
ATOM   4729  CD2 TYR B 369      29.313   3.792 -17.831  1.00 77.67           C  
ANISOU 4729  CD2 TYR B 369     8267  11742   9504  -4160  -4132   2834       C  
ATOM   4730  CE1 TYR B 369      27.238   2.636 -16.434  1.00 71.36           C  
ANISOU 4730  CE1 TYR B 369     7991  10800   8325  -3670  -3989   2523       C  
ATOM   4731  CE2 TYR B 369      28.233   3.264 -18.515  1.00 71.74           C  
ANISOU 4731  CE2 TYR B 369     7621  10906   8731  -3845  -3803   2727       C  
ATOM   4732  CZ  TYR B 369      27.199   2.688 -17.812  1.00 68.65           C  
ANISOU 4732  CZ  TYR B 369     7481  10441   8159  -3607  -3740   2573       C  
ATOM   4733  OH  TYR B 369      26.122   2.163 -18.487  1.00 63.21           O  
ANISOU 4733  OH  TYR B 369     6881   9676   7461  -3317  -3430   2476       O  
ATOM   4734  N   ASN B 370      31.846   6.591 -13.902  1.00116.06           N  
ANISOU 4734  N   ASN B 370    13550  16539  14006  -5434  -5658   2833       N  
ATOM   4735  CA  ASN B 370      33.050   7.234 -13.384  1.00118.75           C  
ANISOU 4735  CA  ASN B 370    13830  16895  14394  -5709  -5902   2920       C  
ATOM   4736  C   ASN B 370      32.995   7.496 -11.881  1.00120.34           C  
ANISOU 4736  C   ASN B 370    14404  17002  14317  -5763  -6165   2758       C  
ATOM   4737  O   ASN B 370      34.012   7.414 -11.193  1.00122.81           O  
ANISOU 4737  O   ASN B 370    14545  17476  14641  -5826  -6346   2878       O  
ATOM   4738  CB  ASN B 370      33.319   8.544 -14.130  1.00108.42           C  
ANISOU 4738  CB  ASN B 370    12632  15375  13189  -6006  -5929   2908       C  
ATOM   4739  CG  ASN B 370      33.855   8.319 -15.531  1.00107.85           C  
ANISOU 4739  CG  ASN B 370    12108  15459  13410  -6018  -5704   3136       C  
ATOM   4740  OD1 ASN B 370      33.101   8.029 -16.459  1.00104.98           O  
ANISOU 4740  OD1 ASN B 370    11458  15281  13148  -5766  -5464   3227       O  
ATOM   4741  ND2 ASN B 370      35.166   8.457 -15.690  1.00110.78           N  
ANISOU 4741  ND2 ASN B 370    12426  15756  13909  -6308  -5770   3232       N  
ATOM   4742  N   LEU B 371      31.806   7.810 -11.379  1.00199.60           N  
ANISOU 4742  N   LEU B 371    24957  26781  24101  -5733  -6178   2482       N  
ATOM   4743  CA  LEU B 371      31.626   8.117  -9.964  1.00200.61           C  
ANISOU 4743  CA  LEU B 371    25513  26786  23926  -5782  -6396   2286       C  
ATOM   4744  C   LEU B 371      31.867   6.903  -9.072  1.00200.59           C  
ANISOU 4744  C   LEU B 371    25384  27028  23805  -5591  -6448   2365       C  
ATOM   4745  O   LEU B 371      32.455   7.019  -7.996  1.00202.56           O  
ANISOU 4745  O   LEU B 371    25722  27311  23931  -5709  -6684   2363       O  
ATOM   4746  CB  LEU B 371      30.225   8.678  -9.708  1.00106.39           C  
ANISOU 4746  CB  LEU B 371    14128  14554  11739  -5700  -6324   1971       C  
ATOM   4747  CG  LEU B 371      29.904  10.033 -10.339  1.00108.14           C  
ANISOU 4747  CG  LEU B 371    14685  14435  11971  -5940  -6400   1815       C  
ATOM   4748  CD1 LEU B 371      28.478  10.451 -10.013  1.00106.37           C  
ANISOU 4748  CD1 LEU B 371    14997  13926  11495  -5794  -6306   1495       C  
ATOM   4749  CD2 LEU B 371      30.896  11.087  -9.874  1.00113.20           C  
ANISOU 4749  CD2 LEU B 371    15443  15004  12565  -6228  -6697   1813       C  
ATOM   4750  N   VAL B 372      31.409   5.740  -9.522  1.00150.88           N  
ANISOU 4750  N   VAL B 372    18889  20893  17546  -5298  -6231   2442       N  
ATOM   4751  CA  VAL B 372      31.507   4.523  -8.724  1.00150.69           C  
ANISOU 4751  CA  VAL B 372    18782  21071  17403  -5083  -6253   2519       C  
ATOM   4752  C   VAL B 372      32.825   3.787  -8.947  1.00152.20           C  
ANISOU 4752  C   VAL B 372    18457  21534  17839  -5091  -6333   2813       C  
ATOM   4753  O   VAL B 372      33.601   3.589  -8.012  1.00153.87           O  
ANISOU 4753  O   VAL B 372    18671  21846  17947  -5112  -6530   2868       O  
ATOM   4754  CB  VAL B 372      30.338   3.564  -9.015  1.00106.10           C  
ANISOU 4754  CB  VAL B 372    13147  15472  11692  -4756  -5991   2492       C  
ATOM   4755  CG1 VAL B 372      30.463   2.309  -8.168  1.00106.25           C  
ANISOU 4755  CG1 VAL B 372    13089  15684  11597  -4541  -6012   2598       C  
ATOM   4756  CG2 VAL B 372      29.008   4.257  -8.758  1.00103.48           C  
ANISOU 4756  CG2 VAL B 372    13333  14861  11122  -4682  -5842   2185       C  
ATOM   4757  N   SER B 373      33.069   3.381 -10.189  1.00106.12           N  
ANISOU 4757  N   SER B 373    12183  15816  12320  -5066  -6176   3000       N  
ATOM   4758  CA  SER B 373      34.273   2.628 -10.524  1.00108.12           C  
ANISOU 4758  CA  SER B 373    11919  16337  12824  -5023  -6203   3277       C  
ATOM   4759  C   SER B 373      35.491   3.534 -10.648  1.00112.02           C  
ANISOU 4759  C   SER B 373    12217  16850  13496  -5339  -6362   3387       C  
ATOM   4760  O   SER B 373      35.464   4.531 -11.369  1.00111.66           O  
ANISOU 4760  O   SER B 373    12140  16705  13580  -5496  -6270   3378       O  
ATOM   4761  CB  SER B 373      34.074   1.841 -11.821  1.00131.40           C  
ANISOU 4761  CB  SER B 373    14477  19441  16009  -4751  -5902   3426       C  
ATOM   4762  OG  SER B 373      35.278   1.214 -12.224  1.00133.41           O  
ANISOU 4762  OG  SER B 373    14224  19939  16527  -4702  -5902   3683       O  
ATOM   4763  N   ALA B 374      36.558   3.179  -9.941  1.00124.63           N  
ANISOU 4763  N   ALA B 374    13683  18575  15093  -5436  -6605   3500       N  
ATOM   4764  CA  ALA B 374      37.800   3.938  -9.995  1.00128.96           C  
ANISOU 4764  CA  ALA B 374    14022  19170  15806  -5740  -6782   3627       C  
ATOM   4765  C   ALA B 374      38.625   3.543 -11.216  1.00129.11           C  
ANISOU 4765  C   ALA B 374    13475  19403  16178  -5683  -6585   3875       C  
ATOM   4766  O   ALA B 374      39.221   4.394 -11.874  1.00131.48           O  
ANISOU 4766  O   ALA B 374    13621  19698  16636  -5931  -6613   3959       O  
ATOM   4767  CB  ALA B 374      38.602   3.733  -8.721  1.00124.75           C  
ANISOU 4767  CB  ALA B 374    13489  18737  15173  -5840  -7101   3687       C  
ATOM   4768  N   ASN B 375      38.649   2.246 -11.512  1.00195.38           N  
ANISOU 4768  N   ASN B 375    21569  27980  24687  -5347  -6378   3992       N  
ATOM   4769  CA  ASN B 375      39.396   1.725 -12.652  1.00196.21           C  
ANISOU 4769  CA  ASN B 375    21137  28302  25112  -5231  -6154   4213       C  
ATOM   4770  C   ASN B 375      38.855   2.254 -13.975  1.00193.45           C  
ANISOU 4770  C   ASN B 375    20792  27854  24856  -5261  -5880   4165       C  
ATOM   4771  O   ASN B 375      39.606   2.778 -14.805  1.00195.06           O  
ANISOU 4771  O   ASN B 375    20718  28134  25261  -5412  -5795   4294       O  
ATOM   4772  CB  ASN B 375      39.363   0.195 -12.652  1.00160.56           C  
ANISOU 4772  CB  ASN B 375    16350  23975  20679  -4835  -6008   4328       C  
ATOM   4773  CG  ASN B 375      39.736  -0.396 -11.306  1.00163.18           C  
ANISOU 4773  CG  ASN B 375    16762  24367  20871  -4773  -6271   4355       C  
ATOM   4774  OD1 ASN B 375      40.910  -0.628 -11.020  1.00167.68           O  
ANISOU 4774  OD1 ASN B 375    16997  25126  21585  -4777  -6403   4541       O  
ATOM   4775  ND2 ASN B 375      38.733  -0.647 -10.471  1.00160.54           N  
ANISOU 4775  ND2 ASN B 375    16873  23878  20247  -4711  -6344   4174       N  
ATOM   4776  N   PHE B 376      37.545   2.118 -14.161  1.00169.96           N  
ANISOU 4776  N   PHE B 376    18138  24715  21725  -5118  -5743   3982       N  
ATOM   4777  CA  PHE B 376      36.883   2.598 -15.368  1.00168.06           C  
ANISOU 4777  CA  PHE B 376    17941  24368  21549  -5121  -5487   3921       C  
ATOM   4778  C   PHE B 376      37.056   4.103 -15.519  1.00169.14           C  
ANISOU 4778  C   PHE B 376    18278  24315  21674  -5493  -5596   3862       C  
ATOM   4779  O   PHE B 376      37.087   4.617 -16.632  1.00168.95           O  
ANISOU 4779  O   PHE B 376    18103  24288  21803  -5570  -5408   3931       O  
ATOM   4780  CB  PHE B 376      35.394   2.239 -15.355  1.00139.52           C  
ANISOU 4780  CB  PHE B 376    14677  20597  17738  -4919  -5373   3720       C  
ATOM   4781  CG  PHE B 376      34.663   2.640 -16.608  1.00137.96           C  
ANISOU 4781  CG  PHE B 376    14449  20339  17632  -4852  -5083   3688       C  
ATOM   4782  CD1 PHE B 376      34.639   1.801 -17.709  1.00136.84           C  
ANISOU 4782  CD1 PHE B 376    13973  20373  17647  -4554  -4801   3798       C  
ATOM   4783  CD2 PHE B 376      34.001   3.855 -16.684  1.00137.79           C  
ANISOU 4783  CD2 PHE B 376    14742  20072  17540  -5082  -5093   3546       C  
ATOM   4784  CE1 PHE B 376      33.970   2.165 -18.863  1.00135.53           C  
ANISOU 4784  CE1 PHE B 376    13865  20094  17536  -4421  -4441   3725       C  
ATOM   4785  CE2 PHE B 376      33.331   4.226 -17.836  1.00136.47           C  
ANISOU 4785  CE2 PHE B 376    14598  19810  17444  -4969  -4769   3503       C  
ATOM   4786  CZ  PHE B 376      33.315   3.379 -18.926  1.00135.33           C  
ANISOU 4786  CZ  PHE B 376    14169  19818  17430  -4630  -4429   3585       C  
ATOM   4787  N   ARG B 377      37.162   4.803 -14.394  1.00140.14           N  
ANISOU 4787  N   ARG B 377    14961  20473  17812  -5719  -5894   3735       N  
ATOM   4788  CA  ARG B 377      37.397   6.241 -14.411  1.00141.62           C  
ANISOU 4788  CA  ARG B 377    15378  20448  17985  -6075  -6029   3674       C  
ATOM   4789  C   ARG B 377      38.824   6.542 -14.855  1.00145.15           C  
ANISOU 4789  C   ARG B 377    15387  21083  18679  -6270  -6059   3925       C  
ATOM   4790  O   ARG B 377      39.067   7.495 -15.598  1.00146.40           O  
ANISOU 4790  O   ARG B 377    15551  21141  18932  -6501  -6020   3965       O  
ATOM   4791  CB  ARG B 377      37.127   6.846 -13.032  1.00116.58           C  
ANISOU 4791  CB  ARG B 377    12694  17057  14543  -6246  -6343   3470       C  
ATOM   4792  CG  ARG B 377      37.423   8.333 -12.931  1.00121.71           C  
ANISOU 4792  CG  ARG B 377    13213  17816  15214  -6462  -6641   3585       C  
ATOM   4793  CD  ARG B 377      36.826   8.922 -11.664  1.00124.03           C  
ANISOU 4793  CD  ARG B 377    14035  17856  15235  -6667  -6937   3363       C  
ATOM   4794  NE  ARG B 377      37.202   8.159 -10.478  1.00121.88           N  
ANISOU 4794  NE  ARG B 377    14082  17538  14692  -6440  -6959   3177       N  
ATOM   4795  CZ  ARG B 377      36.698   8.367  -9.266  1.00121.63           C  
ANISOU 4795  CZ  ARG B 377    14608  17231  14377  -6486  -7055   2898       C  
ATOM   4796  NH1 ARG B 377      35.792   9.316  -9.078  1.00123.36           N  
ANISOU 4796  NH1 ARG B 377    15141  17171  14559  -6744  -7149   2767       N  
ATOM   4797  NH2 ARG B 377      37.098   7.625  -8.243  1.00119.90           N  
ANISOU 4797  NH2 ARG B 377    14640  17010  13905  -6264  -7047   2752       N  
ATOM   4798  N   GLN B 378      39.764   5.720 -14.396  1.00172.75           N  
ANISOU 4798  N   GLN B 378    18501  24855  22282  -6163  -6120   4101       N  
ATOM   4799  CA  GLN B 378      41.159   5.846 -14.802  1.00177.55           C  
ANISOU 4799  CA  GLN B 378    18656  25679  23125  -6318  -6152   4346       C  
ATOM   4800  C   GLN B 378      41.299   5.660 -16.307  1.00176.31           C  
ANISOU 4800  C   GLN B 378    18126  25670  23195  -6199  -5795   4493       C  
ATOM   4801  O   GLN B 378      41.960   6.452 -16.978  1.00178.80           O  
ANISOU 4801  O   GLN B 378    18316  25986  23635  -6434  -5753   4597       O  
ATOM   4802  CB  GLN B 378      42.034   4.831 -14.063  1.00198.57           C  
ATOM   4803  CG  GLN B 378      42.249   5.143 -12.592  1.00198.57           C  
ATOM   4804  CD  GLN B 378      43.068   4.080 -11.885  1.00198.57           C  
ATOM   4805  OE1 GLN B 378      43.370   3.031 -12.454  1.00198.57           O  
ATOM   4806  NE2 GLN B 378      43.431   4.347 -10.636  1.00198.57           N  
ATOM   4807  N   VAL B 379      40.667   4.614 -16.833  1.00145.05           N  
ANISOU 4807  N   VAL B 379    14001  21832  19279  -5835  -5533   4502       N  
ATOM   4808  CA  VAL B 379      40.718   4.344 -18.266  1.00143.78           C  
ANISOU 4808  CA  VAL B 379    13504  21813  19310  -5694  -5171   4623       C  
ATOM   4809  C   VAL B 379      39.977   5.423 -19.057  1.00141.35           C  
ANISOU 4809  C   VAL B 379    13488  21272  18945  -5846  -5032   4512       C  
ATOM   4810  O   VAL B 379      40.402   5.812 -20.146  1.00141.86           O  
ANISOU 4810  O   VAL B 379    13329  21416  19154  -5902  -4809   4632       O  
ATOM   4811  CB  VAL B 379      40.130   2.959 -18.604  1.00154.90           C  
ANISOU 4811  CB  VAL B 379    14693  23386  20777  -5255  -4919   4646       C  
ATOM   4812  CG1 VAL B 379      40.355   2.631 -20.071  1.00158.17           C  
ANISOU 4812  CG1 VAL B 379    14670  24082  21348  -5092  -4967   4834       C  
ATOM   4813  CG2 VAL B 379      40.754   1.891 -17.722  1.00151.70           C  
ANISOU 4813  CG2 VAL B 379    14695  22798  20148  -5096  -4984   4436       C  
ATOM   4814  N   PHE B 380      38.873   5.906 -18.495  1.00156.43           N  
ANISOU 4814  N   PHE B 380    15906  22893  20638  -5909  -5162   4283       N  
ATOM   4815  CA  PHE B 380      38.058   6.937 -19.132  1.00154.79           C  
ANISOU 4815  CA  PHE B 380    16026  22422  20365  -6052  -5067   4161       C  
ATOM   4816  C   PHE B 380      38.847   8.230 -19.294  1.00157.58           C  
ANISOU 4816  C   PHE B 380    16418  22676  20779  -6434  -5200   4242       C  
ATOM   4817  O   PHE B 380      38.828   8.849 -20.357  1.00157.71           O  
ANISOU 4817  O   PHE B 380    16344  22681  20900  -6524  -5004   4329       O  
ATOM   4818  CB  PHE B 380      36.791   7.198 -18.312  1.00110.73           C  
ANISOU 4818  CB  PHE B 380    10993  16547  14532  -6030  -5206   3886       C  
ATOM   4819  CG  PHE B 380      35.796   8.098 -18.992  1.00108.98           C  
ANISOU 4819  CG  PHE B 380    11135  16027  14246  -6154  -5124   3747       C  
ATOM   4820  CD1 PHE B 380      34.821   7.569 -19.822  1.00105.32           C  
ANISOU 4820  CD1 PHE B 380    10696  15535  13785  -5941  -4850   3690       C  
ATOM   4821  CD2 PHE B 380      35.827   9.468 -18.792  1.00111.54           C  
ANISOU 4821  CD2 PHE B 380    11786  16086  14508  -6479  -5329   3676       C  
ATOM   4822  CE1 PHE B 380      33.902   8.391 -20.446  1.00104.33           C  
ANISOU 4822  CE1 PHE B 380    10908  15125  13606  -6051  -4784   3571       C  
ATOM   4823  CE2 PHE B 380      34.911  10.295 -19.413  1.00110.18           C  
ANISOU 4823  CE2 PHE B 380    11963  15614  14285  -6574  -5259   3554       C  
ATOM   4824  CZ  PHE B 380      33.947   9.756 -20.241  1.00106.45           C  
ANISOU 4824  CZ  PHE B 380    11507  15119  13820  -6359  -4987   3505       C  
ATOM   4825  N   LEU B 381      39.538   8.634 -18.233  1.00119.47           N  
ANISOU 4825  N   LEU B 381    11741  17773  15876  -6662  -5536   4213       N  
ATOM   4826  CA  LEU B 381      40.340   9.852 -18.267  1.00123.71           C  
ANISOU 4826  CA  LEU B 381    12331  18205  16468  -7043  -5702   4289       C  
ATOM   4827  C   LEU B 381      41.610   9.656 -19.089  1.00126.65           C  
ANISOU 4827  C   LEU B 381    12152  18881  17088  -7098  -5551   4575       C  
ATOM   4828  O   LEU B 381      42.117  10.600 -19.695  1.00128.79           O  
ANISOU 4828  O   LEU B 381    12402  19089  17441  -7342  -5509   4670       O  
ATOM   4829  CB  LEU B 381      40.687  10.321 -16.851  1.00155.15           C  
ANISOU 4829  CB  LEU B 381    16551  22078  20320  -7255  -6097   4207       C  
ATOM   4830  CG  LEU B 381      39.712  11.296 -16.183  1.00153.55           C  
ANISOU 4830  CG  LEU B 381    16970  21524  19850  -7275  -6265   3905       C  
ATOM   4831  CD1 LEU B 381      38.321  10.695 -16.046  1.00152.90           C  
ANISOU 4831  CD1 LEU B 381    17253  21109  19732  -7432  -6197   3792       C  
ATOM   4832  CD2 LEU B 381      40.243  11.734 -14.826  1.00157.31           C  
ANISOU 4832  CD2 LEU B 381    17653  21928  20190  -7476  -6642   3834       C  
ATOM   4833  N   SER B 382      42.120   8.428 -19.107  1.00160.39           N  
ANISOU 4833  N   SER B 382    15987  23479  21476  -6859  -5463   4710       N  
ATOM   4834  CA  SER B 382      43.303   8.108 -19.897  1.00163.86           C  
ANISOU 4834  CA  SER B 382    15876  24234  22150  -6853  -5288   4970       C  
ATOM   4835  C   SER B 382      42.983   8.159 -21.387  1.00161.39           C  
ANISOU 4835  C   SER B 382    15453  23953  21917  -6752  -4902   5021       C  
ATOM   4836  O   SER B 382      43.846   8.468 -22.208  1.00164.56           O  
ANISOU 4836  O   SER B 382    15613  24462  22450  -6920  -4789   5191       O  
ATOM   4837  CB  SER B 382      43.845   6.728 -19.523  1.00130.37           C  
ANISOU 4837  CB  SER B 382    11222  20304  18009  -6558  -5258   5078       C  
ATOM   4838  OG  SER B 382      44.192   6.670 -18.151  1.00131.55           O  
ANISOU 4838  OG  SER B 382    11550  20397  18036  -6593  -5596   4995       O  
ATOM   4839  N   THR B 383      41.735   7.853 -21.728  1.00139.88           N  
ANISOU 4839  N   THR B 383    12907  21138  19102  -6483  -4702   4877       N  
ATOM   4840  CA  THR B 383      41.289   7.875 -23.116  1.00137.29           C  
ANISOU 4840  CA  THR B 383    12523  20821  18818  -6377  -4340   4905       C  
ATOM   4841  C   THR B 383      40.869   9.283 -23.531  1.00137.41           C  
ANISOU 4841  C   THR B 383    12899  20545  18765  -6695  -4388   4857       C  
ATOM   4842  O   THR B 383      41.116   9.710 -24.660  1.00137.86           O  
ANISOU 4842  O   THR B 383    12836  20648  18894  -6752  -4150   4969       O  
ATOM   4843  CB  THR B 383      40.113   6.903 -23.341  1.00135.78           C  
ANISOU 4843  CB  THR B 383    12448  20598  18546  -6019  -4136   4758       C  
ATOM   4844  OG1 THR B 383      40.498   5.583 -22.939  1.00134.31           O  
ANISOU 4844  OG1 THR B 383    12573  20256  18204  -5966  -4395   4579       O  
ATOM   4845  CG2 THR B 383      39.705   6.882 -24.806  1.00136.03           C  
ANISOU 4845  CG2 THR B 383    12001  20965  18722  -5668  -3854   4886       C  
ATOM   4846  N   LEU B 384      40.242  10.001 -22.605  1.00325.55           N  
ANISOU 4846  N   LEU B 384    37186  44066  42444  -6887  -4694   4685       N  
ATOM   4847  CA  LEU B 384      39.762  11.355 -22.863  1.00326.13           C  
ANISOU 4847  CA  LEU B 384    37655  43812  42448  -7185  -4788   4621       C  
ATOM   4848  C   LEU B 384      40.924  12.301 -23.154  1.00331.73           C  
ANISOU 4848  C   LEU B 384    38141  44611  43291  -7504  -4853   4834       C  
ATOM   4849  O   LEU B 384      40.789  13.245 -23.932  1.00332.38           O  
ANISOU 4849  O   LEU B 384    38286  44597  43408  -7658  -4723   4909       O  
ATOM   4850  CB  LEU B 384      38.941  11.861 -21.670  1.00125.67           C  
ANISOU 4850  CB  LEU B 384    12798  18082  16866  -7293  -5113   4375       C  
ATOM   4851  CG  LEU B 384      38.010  13.063 -21.858  1.00127.01           C  
ANISOU 4851  CG  LEU B 384    13473  17845  16938  -7589  -5299   4253       C  
ATOM   4852  CD1 LEU B 384      36.854  12.983 -20.875  1.00125.03           C  
ANISOU 4852  CD1 LEU B 384    13725  17306  16473  -7527  -5511   3962       C  
ATOM   4853  CD2 LEU B 384      38.750  14.382 -21.685  1.00132.72           C  
ANISOU 4853  CD2 LEU B 384    14130  18559  17736  -7958  -5537   4391       C  
ATOM   4854  N   ALA B 385      42.068  12.035 -22.531  1.00195.61           N  
ANISOU 4854  N   ALA B 385    20642  27557  26124  -7607  -5062   4939       N  
ATOM   4855  CA  ALA B 385      43.254  12.864 -22.718  1.00201.60           C  
ANISOU 4855  CA  ALA B 385    21156  28424  27018  -7925  -5155   5150       C  
ATOM   4856  C   ALA B 385      43.983  12.525 -24.016  1.00202.74           C  
ANISOU 4856  C   ALA B 385    20834  28867  27331  -7841  -4795   5374       C  
ATOM   4857  O   ALA B 385      45.061  13.059 -24.286  1.00207.13           O  
ANISOU 4857  O   ALA B 385    21277  29447  27974  -8112  -4779   5535       O  
ATOM   4858  CB  ALA B 385      44.192  12.723 -21.528  1.00139.59           C  
ANISOU 4858  CB  ALA B 385    13093  20733  19210  -8020  -5451   5216       C  
ATOM   4859  N   CYS B 386      43.386  11.637 -24.808  1.00197.10           N  
ANISOU 4859  N   CYS B 386    19861  28375  26652  -7464  -4502   5380       N  
ATOM   4860  CA  CYS B 386      43.943  11.214 -26.092  1.00197.83           C  
ANISOU 4860  CA  CYS B 386    19520  28763  26883  -7328  -4126   5565       C  
ATOM   4861  C   CYS B 386      45.353  10.645 -25.953  1.00196.23           C  
ANISOU 4861  C   CYS B 386    19540  28394  26623  -7400  -3892   5558       C  
ATOM   4862  O   CYS B 386      45.606   9.789 -25.105  1.00194.24           O  
ANISOU 4862  O   CYS B 386    19776  27789  26236  -7524  -4018   5404       O  
ATOM   4863  CB  CYS B 386      43.927  12.368 -27.100  1.00143.99           C  
ATOM   4864  SG  CYS B 386      42.285  13.052 -27.431  1.00143.99           S  
TER    4865      CYS B 386                                                      
ATOM   4866  N   ARG C   8      18.293 -35.932 -47.347  1.00100.25           N  
ANISOU 4866  N   ARG C   8    15589   9910  12593   4019   2171  -1726       N  
ATOM   4867  CA  ARG C   8      17.391 -34.806 -47.555  1.00 93.50           C  
ANISOU 4867  CA  ARG C   8    14706   9274  11546   3594   2010  -1676       C  
ATOM   4868  C   ARG C   8      17.177 -34.022 -46.264  1.00 88.01           C  
ANISOU 4868  C   ARG C   8    13616   8798  11024   3370   1850  -1335       C  
ATOM   4869  O   ARG C   8      17.615 -34.440 -45.193  1.00 87.90           O  
ANISOU 4869  O   ARG C   8    13423   8695  11279   3486   1799  -1148       O  
ATOM   4870  CB  ARG C   8      16.050 -35.288 -48.109  1.00 68.96           C  
ATOM   4871  CG  ARG C   8      15.357 -36.315 -47.233  1.00 68.96           C  
ATOM   4872  CD  ARG C   8      14.022 -36.729 -47.826  1.00 68.96           C  
ATOM   4873  NE  ARG C   8      13.349 -37.737 -47.010  1.00 68.96           N  
ATOM   4874  CZ  ARG C   8      12.154 -38.248 -47.289  1.00 68.96           C  
ATOM   4875  NH1 ARG C   8      11.496 -37.846 -48.368  1.00 68.96           N  
ATOM   4876  NH2 ARG C   8      11.617 -39.160 -46.490  1.00 68.96           N  
ATOM   4877  N   ARG C   9      16.499 -32.885 -46.376  1.00 98.91           N  
ANISOU 4877  N   ARG C   9    14879  10459  12243   3055   1766  -1259       N  
ATOM   4878  CA  ARG C   9      16.268 -32.008 -45.235  1.00 96.23           C  
ANISOU 4878  CA  ARG C   9    14197  10335  12032   2830   1618   -964       C  
ATOM   4879  C   ARG C   9      14.776 -31.749 -45.051  1.00 93.75           C  
ANISOU 4879  C   ARG C   9    14021   9947  11652   2430   1347   -954       C  
ATOM   4880  O   ARG C   9      14.058 -31.530 -46.028  1.00 93.72           O  
ANISOU 4880  O   ARG C   9    14252   9933  11423   2282   1311  -1134       O  
ATOM   4881  CB  ARG C   9      17.006 -30.683 -45.441  1.00 78.29           C  
ANISOU 4881  CB  ARG C   9    11583   8509   9655   2846   1788   -842       C  
ATOM   4882  CG  ARG C   9      17.099 -29.801 -44.208  1.00 77.94           C  
ANISOU 4882  CG  ARG C   9    11172   8692   9749   2667   1664   -544       C  
ATOM   4883  CD  ARG C   9      17.682 -28.440 -44.554  1.00 80.98           C  
ANISOU 4883  CD  ARG C   9    11271   9488  10007   2641   1816   -445       C  
ATOM   4884  NE  ARG C   9      18.038 -27.675 -43.363  1.00 77.78           N  
ANISOU 4884  NE  ARG C   9    10524   9283   9743   2500   1705   -173       N  
ATOM   4885  CZ  ARG C   9      19.256 -27.650 -42.831  1.00 77.02           C  
ANISOU 4885  CZ  ARG C   9    10102   9357   9803   2669   1801     -1       C  
ATOM   4886  NH1 ARG C   9      20.237 -28.348 -43.387  1.00 73.63           N  
ANISOU 4886  NH1 ARG C   9     9618   8932   9426   3004   2024    -64       N  
ATOM   4887  NH2 ARG C   9      19.494 -26.926 -41.745  1.00 78.14           N  
ANISOU 4887  NH2 ARG C   9     9973   9667  10049   2508   1672    230       N  
ATOM   4888  N   PRO C  10      14.302 -31.782 -43.794  1.00 84.23           N  
ANISOU 4888  N   PRO C  10    12666   8698  10639   2258   1155   -740       N  
ATOM   4889  CA  PRO C  10      12.897 -31.502 -43.478  1.00 81.38           C  
ANISOU 4889  CA  PRO C  10    12381   8297  10243   1888    912   -703       C  
ATOM   4890  C   PRO C  10      12.458 -30.123 -43.961  1.00 76.15           C  
ANISOU 4890  C   PRO C  10    11596   7963   9374   1680    901   -683       C  
ATOM   4891  O   PRO C  10      13.260 -29.189 -43.983  1.00 75.71           O  
ANISOU 4891  O   PRO C  10    11292   8206   9268   1764   1044   -590       O  
ATOM   4892  CB  PRO C  10      12.869 -31.551 -41.948  1.00 70.42           C  
ANISOU 4892  CB  PRO C  10    10773   6892   9090   1812    785   -440       C  
ATOM   4893  CG  PRO C  10      13.977 -32.466 -41.586  1.00 73.01           C  
ANISOU 4893  CG  PRO C  10    11081   7060   9598   2139    895   -406       C  
ATOM   4894  CD  PRO C  10      15.057 -32.205 -42.602  1.00 78.04           C  
ANISOU 4894  CD  PRO C  10    11670   7864  10118   2417   1150   -533       C  
ATOM   4895  N   TYR C  11      11.192 -30.007 -44.349  1.00 47.45           N  
ANISOU 4895  N   TYR C  11     8133   4265   5632   1406    723   -762       N  
ATOM   4896  CA  TYR C  11      10.639 -28.737 -44.803  1.00 46.86           C  
ANISOU 4896  CA  TYR C  11     7961   4467   5377   1196    672   -731       C  
ATOM   4897  C   TYR C  11       9.570 -28.238 -43.836  1.00 45.93           C  
ANISOU 4897  C   TYR C  11     7694   4388   5369    919    458   -556       C  
ATOM   4898  O   TYR C  11       9.061 -27.125 -43.973  1.00 42.26           O  
ANISOU 4898  O   TYR C  11     7125   4135   4798    741    387   -500       O  
ATOM   4899  CB  TYR C  11      10.061 -28.874 -46.216  1.00 39.10           C  
ANISOU 4899  CB  TYR C  11     7288   3426   4143   1120    642   -971       C  
ATOM   4900  CG  TYR C  11       9.049 -29.990 -46.370  1.00 41.71           C  
ANISOU 4900  CG  TYR C  11     7930   3410   4509    992    458  -1120       C  
ATOM   4901  CD1 TYR C  11       7.694 -29.761 -46.157  1.00 39.82           C  
ANISOU 4901  CD1 TYR C  11     7706   3142   4280    674    210  -1077       C  
ATOM   4902  CD2 TYR C  11       9.449 -31.272 -46.735  1.00 46.10           C  
ANISOU 4902  CD2 TYR C  11     8759   3661   5095   1188    530  -1301       C  
ATOM   4903  CE1 TYR C  11       6.766 -30.779 -46.297  1.00 42.14           C  
ANISOU 4903  CE1 TYR C  11     8269   3126   4617    526     29  -1198       C  
ATOM   4904  CE2 TYR C  11       8.529 -32.296 -46.879  1.00 49.10           C  
ANISOU 4904  CE2 TYR C  11     9443   3700   5514   1046    345  -1436       C  
ATOM   4905  CZ  TYR C  11       7.190 -32.043 -46.658  1.00 47.12           C  
ANISOU 4905  CZ  TYR C  11     9190   3439   5274    700     91  -1378       C  
ATOM   4906  OH  TYR C  11       6.271 -33.057 -46.799  1.00 51.13           O  
ANISOU 4906  OH  TYR C  11     9983   3614   5830    528   -105  -1498       O  
ATOM   4907  N   ILE C  12       9.238 -29.072 -42.856  1.00 60.99           N  
ANISOU 4907  N   ILE C  12     9596   6089   7486    893    364   -465       N  
ATOM   4908  CA  ILE C  12       8.224 -28.731 -41.865  1.00 55.10           C  
ANISOU 4908  CA  ILE C  12     8724   5363   6848    641    182   -302       C  
ATOM   4909  C   ILE C  12       8.849 -28.171 -40.591  1.00 51.49           C  
ANISOU 4909  C   ILE C  12     7970   5057   6534    692    218    -65       C  
ATOM   4910  O   ILE C  12       9.575 -28.869 -39.883  1.00 50.15           O  
ANISOU 4910  O   ILE C  12     7765   4788   6500    880    290      2       O  
ATOM   4911  CB  ILE C  12       7.350 -29.949 -41.510  1.00 48.18           C  
ANISOU 4911  CB  ILE C  12     8060   4154   6093    515     29   -343       C  
ATOM   4912  CG1 ILE C  12       6.579 -30.426 -42.743  1.00 49.60           C  
ANISOU 4912  CG1 ILE C  12     8548   4176   6124    419    -50   -583       C  
ATOM   4913  CG2 ILE C  12       6.394 -29.605 -40.373  1.00 48.88           C  
ANISOU 4913  CG2 ILE C  12     7986   4294   6292    262   -126   -156       C  
ATOM   4914  CD1 ILE C  12       5.685 -31.621 -42.486  1.00 49.25           C  
ANISOU 4914  CD1 ILE C  12     8739   3776   6198    278   -209   -637       C  
ATOM   4915  N   LEU C  13       8.567 -26.903 -40.309  1.00 47.78           N  
ANISOU 4915  N   LEU C  13     7300   4825   6031    530    158     58       N  
ATOM   4916  CA  LEU C  13       9.069 -26.255 -39.104  1.00 45.78           C  
ANISOU 4916  CA  LEU C  13     6792   4715   5889    534    161    272       C  
ATOM   4917  C   LEU C  13       8.048 -26.378 -37.977  1.00 43.87           C  
ANISOU 4917  C   LEU C  13     6517   4413   5740    318      8    388       C  
ATOM   4918  O   LEU C  13       6.844 -26.476 -38.217  1.00 43.77           O  
ANISOU 4918  O   LEU C  13     6618   4315   5698    135   -104    316       O  
ATOM   4919  CB  LEU C  13       9.381 -24.780 -39.378  1.00 50.21           C  
ANISOU 4919  CB  LEU C  13     7150   5584   6343    525    221    334       C  
ATOM   4920  CG  LEU C  13       9.937 -23.945 -38.221  1.00 50.45           C  
ANISOU 4920  CG  LEU C  13     7027   5755   6386    739    379    391       C  
ATOM   4921  CD1 LEU C  13      11.257 -24.514 -37.725  1.00 49.54           C  
ANISOU 4921  CD1 LEU C  13     6744   5920   6157    673    413    447       C  
ATOM   4922  CD2 LEU C  13      10.097 -22.490 -38.638  1.00 49.00           C  
ANISOU 4922  CD2 LEU C  13     6709   5531   6378    825    365    557       C  
ATOM   4923  OXT LEU C  13       8.393 -26.380 -36.795  1.00 50.72           O  
ANISOU 4923  OXT LEU C  13     7236   5327   6707    317     -6    559       O  
TER    4924      LEU C  13                                                      
ATOM   4925  N   ARG D   8      -8.112  24.960 -30.372  1.00 88.09           N  
ANISOU 4925  N   ARG D   8    15176   6168  12125   3739  -2275   -126       N  
ATOM   4926  CA  ARG D   8      -6.819  24.699 -30.992  1.00 83.32           C  
ANISOU 4926  CA  ARG D   8    14448   5761  11446   3297  -2382    123       C  
ATOM   4927  C   ARG D   8      -6.123  23.521 -30.320  1.00 77.72           C  
ANISOU 4927  C   ARG D   8    13682   5308  10539   2940  -2258     32       C  
ATOM   4928  O   ARG D   8      -6.006  23.477 -29.097  1.00 78.68           O  
ANISOU 4928  O   ARG D   8    14070   5262  10561   2876  -2219   -173       O  
ATOM   4929  CB  ARG D   8      -5.930  25.941 -30.923  1.00 85.29           C  
ANISOU 4929  CB  ARG D   8    15046   5616  11745   3095  -2652    320       C  
ATOM   4930  CG  ARG D   8      -4.605  25.789 -31.644  1.00 89.75           C  
ANISOU 4930  CG  ARG D   8    16111   5686  12305   3093  -2743    153       C  
ATOM   4931  CD  ARG D   8      -3.727  27.008 -31.438  1.00 87.09           C  
ANISOU 4931  CD  ARG D   8    15943   5348  11797   2614  -2769    124       C  
ATOM   4932  NE  ARG D   8      -2.453  26.882 -32.139  1.00 87.13           N  
ANISOU 4932  NE  ARG D   8    16052   5250  11801   2226  -2970    410       N  
ATOM   4933  CZ  ARG D   8      -1.459  27.759 -32.047  1.00 91.17           C  
ANISOU 4933  CZ  ARG D   8    16977   5333  12328   2014  -3163    456       C  
ATOM   4934  NH1 ARG D   8      -1.587  28.830 -31.277  1.00 96.84           N  
ANISOU 4934  NH1 ARG D   8    18067   5665  13062   2155  -3196    216       N  
ATOM   4935  NH2 ARG D   8      -0.336  27.564 -32.721  1.00 91.12           N  
ANISOU 4935  NH2 ARG D   8    17021   5285  12314   1653  -3319    741       N  
ATOM   4936  N   ARG D   9      -5.662  22.569 -31.125  1.00 92.86           N  
ANISOU 4936  N   ARG D   9    15261   7624  12398   2715  -2207    182       N  
ATOM   4937  CA  ARG D   9      -5.053  21.354 -30.596  1.00 87.83           C  
ANISOU 4937  CA  ARG D   9    14519   7261  11589   2402  -2088    122       C  
ATOM   4938  C   ARG D   9      -3.654  21.134 -31.168  1.00 83.73           C  
ANISOU 4938  C   ARG D   9    14088   6725  10999   1952  -2234    320       C  
ATOM   4939  O   ARG D   9      -3.437  21.304 -32.368  1.00 84.81           O  
ANISOU 4939  O   ARG D   9    14195   6830  11199   1871  -2369    551       O  
ATOM   4940  CB  ARG D   9      -5.941  20.146 -30.907  1.00 86.73           C  
ANISOU 4940  CB  ARG D   9    13932   7591  11430   2477  -1897    125       C  
ATOM   4941  CG  ARG D   9      -5.795  18.995 -29.929  1.00 90.31           C  
ANISOU 4941  CG  ARG D   9    14108   8266  11938   2377  -1972    377       C  
ATOM   4942  CD  ARG D   9      -6.696  17.830 -30.298  1.00 91.57           C  
ANISOU 4942  CD  ARG D   9    13845   8850  12098   2471  -1796    361       C  
ATOM   4943  NE  ARG D   9      -6.901  16.928 -29.169  1.00 91.03           N  
ANISOU 4943  NE  ARG D   9    13694   9008  11884   2295  -1626    238       N  
ATOM   4944  CZ  ARG D   9      -6.075  15.941 -28.838  1.00 91.16           C  
ANISOU 4944  CZ  ARG D   9    13653   9123  11861   2480  -1436     37       C  
ATOM   4945  NH1 ARG D   9      -4.978  15.724 -29.551  1.00 92.35           N  
ANISOU 4945  NH1 ARG D   9    13801   9174  12114   2861  -1371    -75       N  
ATOM   4946  NH2 ARG D   9      -6.345  15.171 -27.793  1.00 93.58           N  
ANISOU 4946  NH2 ARG D   9    13900   9633  12022   2294  -1304    -44       N  
ATOM   4947  N   PRO D  10      -2.696  20.761 -30.304  1.00 65.55           N  
ANISOU 4947  N   PRO D  10    11895   4451   8562   1662  -2209    237       N  
ATOM   4948  CA  PRO D  10      -1.319  20.476 -30.722  1.00 64.67           C  
ANISOU 4948  CA  PRO D  10    11832   4357   8382   1227  -2321    414       C  
ATOM   4949  C   PRO D  10      -1.242  19.330 -31.726  1.00 62.29           C  
ANISOU 4949  C   PRO D  10    11182   4422   8066   1088  -2275    619       C  
ATOM   4950  O   PRO D  10      -2.094  18.440 -31.718  1.00 60.04           O  
ANISOU 4950  O   PRO D  10    10596   4436   7780   1251  -2130    580       O  
ATOM   4951  CB  PRO D  10      -0.636  20.069 -29.413  1.00 55.36           C  
ANISOU 4951  CB  PRO D  10    10720   3253   7062   1030  -2251    246       C  
ATOM   4952  CG  PRO D  10      -1.427  20.741 -28.355  1.00 58.10           C  
ANISOU 4952  CG  PRO D  10    11260   3413   7403   1337  -2183    -24       C  
ATOM   4953  CD  PRO D  10      -2.846  20.708 -28.840  1.00 58.63           C  
ANISOU 4953  CD  PRO D  10    11117   3577   7582   1741  -2078    -35       C  
ATOM   4954  N   TYR D  11      -0.225  19.360 -32.581  1.00 74.41           N  
ANISOU 4954  N   TYR D  11    12766   5925   9582    785  -2394    836       N  
ATOM   4955  CA  TYR D  11      -0.025  18.318 -33.581  1.00 70.20           C  
ANISOU 4955  CA  TYR D  11    11946   5719   9009    636  -2351   1022       C  
ATOM   4956  C   TYR D  11       1.330  17.643 -33.396  1.00 68.64           C  
ANISOU 4956  C   TYR D  11    11669   5715   8699    274  -2302   1063       C  
ATOM   4957  O   TYR D  11       1.628  16.637 -34.041  1.00 66.15           O  
ANISOU 4957  O   TYR D  11    11122   5681   8334    137  -2242   1191       O  
ATOM   4958  CB  TYR D  11      -0.138  18.899 -34.993  1.00 54.33           C  
ANISOU 4958  CB  TYR D  11    10020   3571   7050    601  -2504   1263       C  
ATOM   4959  CG  TYR D  11       0.748  20.103 -35.239  1.00 58.53           C  
ANISOU 4959  CG  TYR D  11    10895   3749   7594    382  -2672   1368       C  
ATOM   4960  CD1 TYR D  11       2.058  19.949 -35.679  1.00 58.33           C  
ANISOU 4960  CD1 TYR D  11    10878   3796   7489     -6  -2702   1535       C  
ATOM   4961  CD2 TYR D  11       0.272  21.392 -35.035  1.00 63.19           C  
ANISOU 4961  CD2 TYR D  11    11798   3927   8283    563  -2797   1303       C  
ATOM   4962  CE1 TYR D  11       2.869  21.045 -35.906  1.00 62.58           C  
ANISOU 4962  CE1 TYR D  11    11715   4016   8045   -237  -2857   1650       C  
ATOM   4963  CE2 TYR D  11       1.075  22.494 -35.259  1.00 67.51           C  
ANISOU 4963  CE2 TYR D  11    12677   4125   8850    341  -2964   1406       C  
ATOM   4964  CZ  TYR D  11       2.373  22.315 -35.695  1.00 67.14           C  
ANISOU 4964  CZ  TYR D  11    12620   4168   8722    -73  -2996   1586       C  
ATOM   4965  OH  TYR D  11       3.176  23.410 -35.918  1.00 71.83           O  
ANISOU 4965  OH  TYR D  11    13530   4420   9342   -325  -3163   1707       O  
ATOM   4966  N   ILE D  12       2.145  18.206 -32.510  1.00 61.12           N  
ANISOU 4966  N   ILE D  12    10910   4606   7707    128  -2335    952       N  
ATOM   4967  CA  ILE D  12       3.479  17.679 -32.245  1.00 61.17           C  
ANISOU 4967  CA  ILE D  12    10837   4784   7622   -208  -2310    992       C  
ATOM   4968  C   ILE D  12       3.461  16.648 -31.121  1.00 58.67           C  
ANISOU 4968  C   ILE D  12    10395   4668   7228   -151  -2175    791       C  
ATOM   4969  O   ILE D  12       3.026  16.937 -30.007  1.00 59.14           O  
ANISOU 4969  O   ILE D  12    10636   4563   7272    -16  -2177    593       O  
ATOM   4970  CB  ILE D  12       4.465  18.806 -31.880  1.00 50.34           C  
ANISOU 4970  CB  ILE D  12     9761   3116   6253   -487  -2477   1043       C  
ATOM   4971  CG1 ILE D  12       4.580  19.806 -33.033  1.00 54.35           C  
ANISOU 4971  CG1 ILE D  12    10405   3421   6824   -581  -2611   1274       C  
ATOM   4972  CG2 ILE D  12       5.826  18.229 -31.526  1.00 48.51           C  
ANISOU 4972  CG2 ILE D  12     9405   3086   5939   -825  -2456   1086       C  
ATOM   4973  CD1 ILE D  12       5.490  20.979 -32.739  1.00 58.91           C  
ANISOU 4973  CD1 ILE D  12    11289   3673   7423   -866  -2788   1343       C  
ATOM   4974  N   LEU D  13       3.935  15.443 -31.422  1.00 69.03           N  
ANISOU 4974  N   LEU D  13    11415   6328   8485   -247  -2056    843       N  
ATOM   4975  CA  LEU D  13       3.993  14.374 -30.433  1.00 69.24           C  
ANISOU 4975  CA  LEU D  13    11326   6554   8428   -240  -1941    692       C  
ATOM   4976  C   LEU D  13       5.423  14.181 -29.932  1.00 68.15           C  
ANISOU 4976  C   LEU D  13    11141   6530   8225   -576  -1977    768       C  
ATOM   4977  O   LEU D  13       5.654  13.741 -28.805  1.00 68.58           O  
ANISOU 4977  O   LEU D  13    11156   6702   8200   -624  -1932    660       O  
ATOM   4978  CB  LEU D  13       3.456  13.068 -31.026  1.00 60.21           C  
ANISOU 4978  CB  LEU D  13     9881   5713   7281    -56  -1772    673       C  
ATOM   4979  CG  LEU D  13       3.422  11.841 -30.110  1.00 57.38           C  
ANISOU 4979  CG  LEU D  13     9248   5649   6902   -208  -1702    822       C  
ATOM   4980  CD1 LEU D  13       2.606  12.127 -28.856  1.00 56.71           C  
ANISOU 4980  CD1 LEU D  13     8920   5808   6819    -13  -1550    761       C  
ATOM   4981  CD2 LEU D  13       2.864  10.638 -30.854  1.00 56.00           C  
ANISOU 4981  CD2 LEU D  13     9077   5429   6772   -303  -1782   1019       C  
ATOM   4982  OXT LEU D  13       6.389  14.463 -30.643  1.00 62.16           O  
ANISOU 4982  OXT LEU D  13    10369   5758   7489   -805  -2051    949       O  
TER    4983      LEU D  13                                                      
HETATM 4984  N   GLY A1385      12.541 -11.046 -45.867  1.00 67.79           N  
HETATM 4985  CA  GLY A1385      13.236 -10.573 -44.684  1.00 67.79           C  
HETATM 4986  C   GLY A1385      12.676 -11.164 -43.404  1.00 67.79           C  
HETATM 4987  O   GLY A1385      11.512 -11.560 -43.346  1.00 67.79           O  
HETATM 4988  OXT GLY A1385      13.372 -11.260 -42.393  1.00 80.91           O  
HETATM 4989  N   GLY A1386     -11.468 -11.881 -17.481  1.00102.99           N  
HETATM 4990  CA  GLY A1386     -12.112 -12.206 -18.740  1.00102.99           C  
HETATM 4991  C   GLY A1386     -11.176 -12.069 -19.926  1.00102.99           C  
HETATM 4992  O   GLY A1386     -10.131 -11.423 -19.838  1.00102.99           O  
HETATM 4993  OXT GLY A1386     -11.438 -12.601 -21.005  1.00 90.22           O  
HETATM 4994  N   GLY A1387       1.647  -3.518 -14.296  1.00 92.58           N  
HETATM 4995  CA  GLY A1387       1.084  -2.582 -15.251  1.00 92.58           C  
HETATM 4996  C   GLY A1387      -0.424  -2.471 -15.138  1.00 92.58           C  
HETATM 4997  O   GLY A1387      -1.023  -1.494 -15.589  1.00 92.58           O  
HETATM 4998  OXT GLY A1387      -1.087  -3.354 -14.592  1.00125.09           O  
HETATM 4999  N   GLY A1388      -3.712  -9.416 -31.147  1.00 98.67           N  
HETATM 5000  CA  GLY A1388      -4.513 -10.620 -31.033  1.00 98.67           C  
HETATM 5001  C   GLY A1388      -3.978 -11.759 -31.878  1.00 98.67           C  
HETATM 5002  O   GLY A1388      -3.159 -11.552 -32.774  1.00 98.67           O  
HETATM 5003  OXT GLY A1388      -4.350 -12.918 -31.690  1.00 76.64           O  
HETATM 5004  N   GLY A1389      15.965 -24.658 -25.493  1.00 89.24           N  
HETATM 5005  CA  GLY A1389      16.839 -23.567 -25.104  1.00 89.24           C  
HETATM 5006  C   GLY A1389      18.249 -23.739 -25.632  1.00 89.24           C  
HETATM 5007  O   GLY A1389      18.674 -24.849 -25.952  1.00 89.24           O  
HETATM 5008  OXT GLY A1389      19.003 -22.773 -25.753  1.00107.17           O  
HETATM 5009  N   GLY A1390      -2.471 -13.581 -41.903  1.00 72.53           N  
HETATM 5010  CA  GLY A1390      -2.046 -13.915 -43.250  1.00 72.53           C  
HETATM 5011  C   GLY A1390      -1.640 -12.688 -44.045  1.00 72.53           C  
HETATM 5012  O   GLY A1390      -1.547 -12.729 -45.273  1.00 72.53           O  
HETATM 5013  OXT GLY A1390      -1.399 -11.618 -43.483  1.00144.30           O  
HETATM 5014  N   GLY A1391      10.216  -8.214 -40.224  1.00 89.54           N  
HETATM 5015  CA  GLY A1391       9.574  -7.095 -40.888  1.00 89.54           C  
HETATM 5016  C   GLY A1391       9.479  -7.282 -42.390  1.00 89.54           C  
HETATM 5017  O   GLY A1391      10.162  -8.132 -42.965  1.00 89.54           O  
HETATM 5018  OXT GLY A1391       8.718  -6.589 -43.069  1.00101.46           O  
HETATM 5019  N   GLY A1392       4.066 -29.680 -13.083  1.00 77.23           N  
HETATM 5020  CA  GLY A1392       4.890 -29.119 -12.029  1.00 77.23           C  
HETATM 5021  C   GLY A1392       5.422 -30.176 -11.080  1.00 77.23           C  
HETATM 5022  O   GLY A1392       4.911 -31.295 -11.025  1.00 77.23           O  
HETATM 5023  OXT GLY A1392       6.379 -29.942 -10.341  1.00 68.96           O  
HETATM 5024  N   GLY B1387      20.165  -0.164 -34.327  1.00 94.64           N  
HETATM 5025  CA  GLY B1387      19.062   0.742 -34.593  1.00 94.64           C  
HETATM 5026  C   GLY B1387      17.751   0.010 -34.808  1.00 94.64           C  
HETATM 5027  O   GLY B1387      17.702  -1.222 -34.797  1.00 94.64           O  
HETATM 5028  OXT GLY B1387      16.702   0.628 -34.999  1.00 79.73           O  
HETATM 5029  N   GLY B1388      36.439  -1.882 -13.651  1.00104.40           N  
HETATM 5030  CA  GLY B1388      35.825  -1.937 -12.338  1.00104.40           C  
HETATM 5031  C   GLY B1388      34.333  -2.201 -12.408  1.00104.40           C  
HETATM 5032  O   GLY B1388      33.806  -2.598 -13.448  1.00104.40           O  
HETATM 5033  OXT GLY B1388      33.611  -2.028 -11.427  1.00 96.81           O  
HETATM 5034  N   GLY B1389      17.996 -13.115 -20.235  1.00108.73           N  
HETATM 5035  CA  GLY B1389      19.014 -14.117 -20.490  1.00108.73           C  
HETATM 5036  C   GLY B1389      18.471 -15.317 -21.241  1.00108.73           C  
HETATM 5037  O   GLY B1389      17.717 -15.172 -22.205  1.00108.73           O  
HETATM 5038  OXT GLY B1389      18.769 -16.463 -20.905  1.00143.49           O  
CONECT  685 1321                                                                
CONECT 1321  685                                                                
CONECT 4984 4985                                                                
CONECT 4985 4984 4986                                                           
CONECT 4986 4985 4987 4988                                                      
CONECT 4987 4986                                                                
CONECT 4988 4986                                                                
CONECT 4989 4990                                                                
CONECT 4990 4989 4991                                                           
CONECT 4991 4990 4992 4993                                                      
CONECT 4992 4991                                                                
CONECT 4993 4991                                                                
CONECT 4994 4995                                                                
CONECT 4995 4994 4996                                                           
CONECT 4996 4995 4997 4998                                                      
CONECT 4997 4996                                                                
CONECT 4998 4996                                                                
CONECT 4999 5000                                                                
CONECT 5000 4999 5001                                                           
CONECT 5001 5000 5002 5003                                                      
CONECT 5002 5001                                                                
CONECT 5003 5001                                                                
CONECT 5004 5005                                                                
CONECT 5005 5004 5006                                                           
CONECT 5006 5005 5007 5008                                                      
CONECT 5007 5006                                                                
CONECT 5008 5006                                                                
CONECT 5009 5010                                                                
CONECT 5010 5009 5011                                                           
CONECT 5011 5010 5012 5013                                                      
CONECT 5012 5011                                                                
CONECT 5013 5011                                                                
CONECT 5014 5015                                                                
CONECT 5015 5014 5016                                                           
CONECT 5016 5015 5017 5018                                                      
CONECT 5017 5016                                                                
CONECT 5018 5016                                                                
CONECT 5019 5020                                                                
CONECT 5020 5019 5021                                                           
CONECT 5021 5020 5022 5023                                                      
CONECT 5022 5021                                                                
CONECT 5023 5021                                                                
CONECT 3073 3709                                                                
CONECT 3709 3073                                                                
CONECT 5024 5025                                                                
CONECT 5025 5024 5026                                                           
CONECT 5026 5025 5027 5028                                                      
CONECT 5027 5026                                                                
CONECT 5028 5026                                                                
CONECT 5029 5030                                                                
CONECT 5030 5029 5031                                                           
CONECT 5031 5030 5032 5033                                                      
CONECT 5032 5031                                                                
CONECT 5033 5031                                                                
CONECT 5034 5035                                                                
CONECT 5035 5034 5036                                                           
CONECT 5036 5035 5037 5038                                                      
CONECT 5037 5036                                                                
CONECT 5038 5036                                                                
MASTER      393    0   11   23    4    0   10    9 5034    4   59   54          
END