CNRS Nantes University UFIP UFIP
home |  start a new run |  job status |  references&downloads |  examples |  help  

Should you encounter any unexpected behaviour,
please let us know.


***  teste-1  ***

elNémo ID: 22040117183546502

Job options:

ID        	=	 22040117183546502
JOBID     	=	 teste-1
USERID    	=	 si
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -10
DQMAX     	=	 10
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER teste-1

HEADER    HYDROLASE                               18-DEC-14   4XCT              
TITLE     CRYSTAL STRUCTURE OF A HYDROXAMATE BASED INHIBITOR ARP101 (EN73) IN   
TITLE    2 COMPLEX WITH THE MMP-9 CATALYTIC DOMAIN.                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MATRIX METALLOPROTEINASE-9,MATRIX METALLOPROTEINASE-9;     
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 113-216,UNP RESIDUES 392-444;                 
COMPND   5 SYNONYM: MMP-9,92 KDA GELATINASE,92 KDA TYPE IV COLLAGENASE,         
COMPND   6 GELATINASE B,GELB;                                                   
COMPND   7 EC: 3.4.24.35;                                                       
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 OTHER_DETAILS: N73 ZINC CHELATING INHIBITOR - HUMAN WILD-TYPE MMP-9  
COMPND  10 CATALYTIC DOMAIN UNP RESIDUES 107-215/391-443                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MMP9, CLG4B;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: STAR;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-14B                                   
KEYWDS    INHIBITOR-COMPLEX, METALLOPROTEASE, HYDROLASE                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.A.STURA,L.TEPSHI,E.NUTI,V.DIVE,E.CASSAR-LAJEUNESSE,L.VERA,          
AUTHOR   2 A.ROSSELLO                                                           
REVDAT   4   29-MAY-19 4XCT    1       COMPND REMARK HETNAM FORMUL              
REVDAT   4 2                   1       LINK   SITE   ATOM                       
REVDAT   3   07-OCT-15 4XCT    1       JRNL                                     
REVDAT   2   26-AUG-15 4XCT    1       JRNL                                     
REVDAT   1   22-APR-15 4XCT    0                                                
JRNL        AUTH   E.NUTI,A.R.CANTELMO,C.GALLO,A.BRUNO,B.BASSANI,C.CAMODECA,    
JRNL        AUTH 2 T.TUCCINARDI,L.VERA,E.ORLANDINI,S.NENCETTI,E.A.STURA,        
JRNL        AUTH 3 A.MARTINELLI,V.DIVE,A.ALBINI,A.ROSSELLO                      
JRNL        TITL   N-O-ISOPROPYL SULFONAMIDO-BASED HYDROXAMATES AS MATRIX       
JRNL        TITL 2 METALLOPROTEINASE INHIBITORS: HIT SELECTION AND IN VIVO      
JRNL        TITL 3 ANTIANGIOGENIC ACTIVITY.                                     
JRNL        REF    J.MED.CHEM.                   V.  58  7224 2015              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   26263024                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.5B00367                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.9_1692)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT 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) : 1.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.30                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 37897                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.170                           
REMARK   3   R VALUE            (WORKING SET) : 0.167                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1892                            
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 34.3065 -  3.1315    1.00     2803   148  0.1443 0.2063        
REMARK   3     2  3.1315 -  2.4858    1.00     2645   138  0.1680 0.2244        
REMARK   3     3  2.4858 -  2.1716    1.00     2627   138  0.1575 0.2219        
REMARK   3     4  2.1716 -  1.9731    1.00     2564   135  0.1529 0.2057        
REMARK   3     5  1.9731 -  1.8317    1.00     2589   137  0.1583 0.2284        
REMARK   3     6  1.8317 -  1.7237    1.00     2523   133  0.1653 0.2518        
REMARK   3     7  1.7237 -  1.6374    1.00     2574   135  0.1746 0.2284        
REMARK   3     8  1.6374 -  1.5661    1.00     2536   134  0.1856 0.2768        
REMARK   3     9  1.5661 -  1.5058    1.00     2572   135  0.2085 0.2735        
REMARK   3    10  1.5058 -  1.4539    1.00     2506   130  0.2258 0.3337        
REMARK   3    11  1.4539 -  1.4084    1.00     2525   133  0.2502 0.3349        
REMARK   3    12  1.4084 -  1.3681    1.00     2504   131  0.2631 0.3288        
REMARK   3    13  1.3681 -  1.3321    1.00     2564   134  0.2723 0.3198        
REMARK   3    14  1.3321 -  1.2996    0.98     2473   131  0.2760 0.3203        
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)     : 0.150            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.170           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
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      :  0.006           1497                                  
REMARK   3   ANGLE     :  1.049           2047                                  
REMARK   3   CHIRALITY :  0.053            198                                  
REMARK   3   PLANARITY :  0.005            273                                  
REMARK   3   DIHEDRAL  : 14.462            548                                  
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 : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4XCT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-DEC-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000205450.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-DEC-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0-8.5                            
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97857                            
REMARK 200  MONOCHROMATOR                  : CHANNEL CUT SI(111)                
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38007                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 52.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : 0.05500                            
REMARK 200   FOR THE DATA SET  : 14.6200                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.16                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.39200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.120                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 4H3X                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.47                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: HMMP-9-WT AT 337 MICRO-M WITH   
REMARK 280  120 MILLI-M ACETOHYDROXAMIC ACID. PRECIPITANT: 40.5% MPEG 5,000,    
REMARK 280  180 MM IMIDAZOLE PIPERIDINE, PH 8.5. CRYOPROTECTANT: 40%            
REMARK 280  CRYOPROTX-C1, 10% PEG 10K, 10% PCTP 50/50, VAPOR DIFFUSION,         
REMARK 280  SITTING DROP, TEMPERATURE 293.0K                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      109.30667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       54.65333            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       54.65333            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      109.30667            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1750 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8150 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 494  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 611  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 627  LIES ON A SPECIAL POSITION.                          
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    TYR A 160       66.28   -114.98                                   
REMARK 500    ALA A 173     -136.70     49.34                                   
REMARK 500    ASP A 185     -161.01     57.35                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 630        DISTANCE =  6.22 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 306  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 131   OD1                                                    
REMARK 620 2 ASP A 131   OD2  52.2                                              
REMARK 620 3 ASP A 206   O   151.5 149.3                                        
REMARK 620 4 ASP A 206   OD1  92.3  91.3  73.5                                  
REMARK 620 5 GLU A 208   O   126.3  77.4  82.0 107.6                            
REMARK 620 6 HOH A 512   O    87.1  93.3 104.3 173.7  77.7                      
REMARK 620 7 HOH A 515   O    78.6 130.6  75.9  86.1 149.6  87.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 305  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 165   O                                                      
REMARK 620 2 GLY A 197   O   172.8                                              
REMARK 620 3 GLN A 199   O   102.8  83.8                                        
REMARK 620 4 ASP A 201   OD1  86.2  96.2  96.0                                  
REMARK 620 5 HOH A 415   O    88.3  84.7 164.2  95.9                            
REMARK 620 6 HOH A 452   O    86.5  91.1  84.4 172.6  85.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 303  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 175   NE2                                                    
REMARK 620 2 ASP A 177   OD2 109.7                                              
REMARK 620 3 HIS A 190   NE2 114.0 114.0                                        
REMARK 620 4 HIS A 203   ND1 108.8  92.2 116.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 304  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 182   OD1                                                    
REMARK 620 2 GLY A 183   O    88.6                                              
REMARK 620 3 ASP A 185   O    84.0  85.1                                        
REMARK 620 4 LEU A 187   O    92.4 177.6  92.9                                  
REMARK 620 5 ASP A 205   OD2  91.6  88.1 171.9  94.1                            
REMARK 620 6 GLU A 208   OE2 170.1  94.3  86.8  84.4  97.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 302  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 226   NE2                                                    
REMARK 620 2 HIS A 230   NE2  93.6                                              
REMARK 620 3 HIS A 236   NE2 108.6  94.3                                        
REMARK 620 4 N73 A 301   O8  136.4 126.9  85.9                                  
REMARK 620 5 N73 A 301   OA8  98.2  88.6 152.7  70.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue N73 A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 306                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 308                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 309                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 310                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 311                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 312                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 313                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGO A 314                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGO A 315                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BUD A 316                 
DBREF  4XCT A  113   216  UNP    P14780   MMP9_HUMAN     113    216             
DBREF  4XCT A  217   269  UNP    P14780   MMP9_HUMAN     392    444             
SEQRES   1 A  157  ASP LEU LYS TRP HIS HIS HIS ASN ILE THR TYR TRP ILE          
SEQRES   2 A  157  GLN ASN TYR SER GLU ASP LEU PRO ARG ALA VAL ILE ASP          
SEQRES   3 A  157  ASP ALA PHE ALA ARG ALA PHE ALA LEU TRP SER ALA VAL          
SEQRES   4 A  157  THR PRO LEU THR PHE THR ARG VAL TYR SER ARG ASP ALA          
SEQRES   5 A  157  ASP ILE VAL ILE GLN PHE GLY VAL ALA GLU HIS GLY ASP          
SEQRES   6 A  157  GLY TYR PRO PHE ASP GLY LYS ASP GLY LEU LEU ALA HIS          
SEQRES   7 A  157  ALA PHE PRO PRO GLY PRO GLY ILE GLN GLY ASP ALA HIS          
SEQRES   8 A  157  PHE ASP ASP ASP GLU LEU TRP SER LEU GLY LYS GLY VAL          
SEQRES   9 A  157  GLY TYR SER LEU PHE LEU VAL ALA ALA HIS GLU PHE GLY          
SEQRES  10 A  157  HIS ALA LEU GLY LEU ASP HIS SER SER VAL PRO GLU ALA          
SEQRES  11 A  157  LEU MET TYR PRO MET TYR ARG PHE THR GLU GLY PRO PRO          
SEQRES  12 A  157  LEU HIS LYS ASP ASP VAL ASN GLY ILE ARG HIS LEU TYR          
SEQRES  13 A  157  GLY                                                          
HET    N73  A 301      28                                                       
HET     ZN  A 302       1                                                       
HET     ZN  A 303       1                                                       
HET     CA  A 304       1                                                       
HET     CA  A 305       1                                                       
HET     CA  A 306       1                                                       
HET    DMS  A 307       4                                                       
HET    DMS  A 308       4                                                       
HET    EDO  A 309       4                                                       
HET    EDO  A 310       4                                                       
HET    EDO  A 311       4                                                       
HET    EDO  A 312       4                                                       
HET    GOL  A 313       6                                                       
HET    PGO  A 314       5                                                       
HET    PGO  A 315       5                                                       
HET    BUD  A 316       6                                                       
HETNAM     N73 (2~{R})-3-METHYL-~{N}-OXIDANYLIDENE-2-[(4-                       
HETNAM   2 N73  PHENYLPHENYL)SULFONYL-PROPAN-2-YLOXY-AMINO]BUTANAMIDE           
HETNAM      ZN ZINC ION                                                         
HETNAM      CA CALCIUM ION                                                      
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     GOL GLYCEROL                                                         
HETNAM     PGO S-1,2-PROPANEDIOL                                                
HETNAM     BUD (2S,3S)-BUTANE-2,3-DIOL                                          
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  N73    C20 H24 N2 O5 S                                              
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   5   CA    3(CA 2+)                                                     
FORMUL   8  DMS    2(C2 H6 O S)                                                 
FORMUL  10  EDO    4(C2 H6 O2)                                                  
FORMUL  14  GOL    C3 H8 O3                                                     
FORMUL  15  PGO    2(C3 H8 O2)                                                  
FORMUL  17  BUD    C4 H10 O2                                                    
FORMUL  18  HOH   *230(H2 O)                                                    
HELIX    1 AA1 PRO A  133  ALA A  150  1                                  18    
HELIX    2 AA2 LEU A  220  LEU A  232  1                                  13    
HELIX    3 AA3 HIS A  257  GLY A  269  1                                  13    
SHEET    1 AA1 5 THR A 155  ARG A 158  0                                        
SHEET    2 AA1 5 ASN A 120  ILE A 125  1  N  ILE A 121   O  THR A 157           
SHEET    3 AA1 5 ILE A 166  GLY A 171  1  O  ILE A 168   N  TRP A 124           
SHEET    4 AA1 5 ALA A 202  ASP A 205  1  O  PHE A 204   N  GLN A 169           
SHEET    5 AA1 5 ALA A 189  ALA A 191 -1  N  HIS A 190   O  HIS A 203           
SHEET    1 AA2 2 TRP A 210  SER A 211  0                                        
SHEET    2 AA2 2 TYR A 218  SER A 219  1  O  TYR A 218   N  SER A 211           
LINK         OD1 ASP A 131                CA    CA A 306     1555   1555  2.62  
LINK         OD2 ASP A 131                CA    CA A 306     1555   1555  2.37  
LINK         O   ASP A 165                CA    CA A 305     1555   1555  2.34  
LINK         NE2 HIS A 175                ZN    ZN A 303     1555   1555  1.97  
LINK         OD2 ASP A 177                ZN    ZN A 303     1555   1555  1.99  
LINK         OD1 ASP A 182                CA    CA A 304     1555   1555  2.43  
LINK         O   GLY A 183                CA    CA A 304     1555   1555  2.28  
LINK         O   ASP A 185                CA    CA A 304     1555   1555  2.33  
LINK         O   LEU A 187                CA    CA A 304     1555   1555  2.27  
LINK         NE2 HIS A 190                ZN    ZN A 303     1555   1555  2.06  
LINK         O   GLY A 197                CA    CA A 305     1555   1555  2.31  
LINK         O   GLN A 199                CA    CA A 305     1555   1555  2.26  
LINK         OD1 ASP A 201                CA    CA A 305     1555   1555  2.34  
LINK         ND1 HIS A 203                ZN    ZN A 303     1555   1555  2.06  
LINK         OD2 ASP A 205                CA    CA A 304     1555   1555  2.31  
LINK         O   ASP A 206                CA    CA A 306     1555   1555  2.41  
LINK         OD1 ASP A 206                CA    CA A 306     1555   1555  2.42  
LINK         O   GLU A 208                CA    CA A 306     1555   1555  2.38  
LINK         OE2 GLU A 208                CA    CA A 304     1555   1555  2.34  
LINK         NE2 HIS A 226                ZN    ZN A 302     1555   1555  2.06  
LINK         NE2 HIS A 230                ZN    ZN A 302     1555   1555  2.11  
LINK         NE2 HIS A 236                ZN    ZN A 302     1555   1555  2.08  
LINK         O8  N73 A 301                ZN    ZN A 302     1555   1555  2.16  
LINK         OA8 N73 A 301                ZN    ZN A 302     1555   1555  2.31  
LINK        CA    CA A 305                 O   HOH A 415     1555   1555  2.29  
LINK        CA    CA A 305                 O   HOH A 452     1555   1555  2.31  
LINK        CA    CA A 306                 O   HOH A 512     1555   1555  2.35  
LINK        CA    CA A 306                 O   HOH A 515     1555   1555  2.42  
SITE     1 AC1 16 LEU A 187  LEU A 188  ALA A 189  LEU A 222                    
SITE     2 AC1 16 HIS A 226  GLU A 227  HIS A 230  HIS A 236                    
SITE     3 AC1 16 LEU A 243  TYR A 245  PRO A 246  MET A 247                    
SITE     4 AC1 16 TYR A 248   ZN A 302  PGO A 315  HOH A 501                    
SITE     1 AC2  4 HIS A 226  HIS A 230  HIS A 236  N73 A 301                    
SITE     1 AC3  4 HIS A 175  ASP A 177  HIS A 190  HIS A 203                    
SITE     1 AC4  6 ASP A 182  GLY A 183  ASP A 185  LEU A 187                    
SITE     2 AC4  6 ASP A 205  GLU A 208                                          
SITE     1 AC5  6 ASP A 165  GLY A 197  GLN A 199  ASP A 201                    
SITE     2 AC5  6 HOH A 415  HOH A 452                                          
SITE     1 AC6  5 ASP A 131  ASP A 206  GLU A 208  HOH A 512                    
SITE     2 AC6  5 HOH A 515                                                     
SITE     1 AC7  3 HIS A 190  ALA A 191  PHE A 192                               
SITE     1 AC8  2 THR A 157  ASP A 182                                          
SITE     1 AC9  6 ILE A 125  GLN A 126  TYR A 128  ALA A 173                    
SITE     2 AC9  6 GLU A 174  HOH A 460                                          
SITE     1 AD1  6 SER A 211  LEU A 212  GLY A 215  VAL A 216                    
SITE     2 AD1  6 HIS A 266  HOH A 495                                          
SITE     1 AD2  4 HIS A 118  HIS A 119  ASN A 120  HOH A 407                    
SITE     1 AD3  2 LEU A 187  ASN A 262                                          
SITE     1 AD4  8 ASP A 113  LYS A 115  TRP A 116  HIS A 117                    
SITE     2 AD4  8 HIS A 118  GLY A 195  HOH A 406  HOH A 436                    
SITE     1 AD5  5 ARG A 162  GLY A 183  LYS A 184  ASP A 207                    
SITE     2 AD5  5 HOH A 537                                                     
SITE     1 AD6  5 PRO A 240  ALA A 242  ARG A 249  N73 A 301                    
SITE     2 AD6  5 HOH A 429                                                     
SITE     1 AD7  4 HIS A 117  GLU A 130  LEU A 132  PRO A 133                    
CRYST1   39.600   39.600  163.960  90.00  90.00 120.00 P 32 2 1      6          
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      0.025253  0.014580  0.000000        0.00000                         
SCALE2      0.000000  0.029159  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006099        0.00000                         
ATOM      1  N   ASP A 113      34.746 -14.843  10.245  1.00 56.35           N  
ANISOU    1  N   ASP A 113     4826   6381  10203   2509    641    -68       N  
ATOM      2  CA  ASP A 113      35.711 -14.082  11.032  1.00 52.68           C  
ANISOU    2  CA  ASP A 113     4123   5831  10061    906    556   -216       C  
ATOM      3  C   ASP A 113      35.217 -13.842  12.456  1.00 47.15           C  
ANISOU    3  C   ASP A 113     3222   5420   9274    978    127   -715       C  
ATOM      4  O   ASP A 113      34.022 -13.955  12.740  1.00 44.92           O  
ANISOU    4  O   ASP A 113     2334   5755   8978    321    166   -828       O  
ATOM      5  CB  ASP A 113      36.020 -12.746  10.355  1.00 49.72           C  
ANISOU    5  CB  ASP A 113     3915   4150  10827   -813    969     61       C  
ATOM      6  CG  ASP A 113      36.734 -12.916   9.028  1.00 59.34           C  
ANISOU    6  CG  ASP A 113     4788   5890  11868   1189   1242    117       C  
ATOM      7  OD1 ASP A 113      37.365 -13.974   8.823  1.00 68.80           O  
ANISOU    7  OD1 ASP A 113     6555   7870  11717   3639   1497    245       O  
ATOM      8  OD2 ASP A 113      36.671 -11.989   8.192  1.00 52.89           O  
ANISOU    8  OD2 ASP A 113     3552   4829  11715    873   1255    138       O  
ATOM      9  N   LEU A 114      36.146 -13.507  13.345  1.00 41.67           N  
ANISOU    9  N   LEU A 114     3507   3998   8327   1305   -110  -1124       N  
ATOM     10  CA  LEU A 114      35.823 -13.278  14.746  1.00 34.31           C  
ANISOU   10  CA  LEU A 114     2290   3421   7325    182   -257  -1134       C  
ATOM     11  C   LEU A 114      35.189 -11.911  14.961  1.00 31.17           C  
ANISOU   11  C   LEU A 114     2097   3508   6240    951    -44   -674       C  
ATOM     12  O   LEU A 114      34.393 -11.730  15.877  1.00 30.32           O  
ANISOU   12  O   LEU A 114     2268   3056   6194    955    264   -533       O  
ATOM     13  CB  LEU A 114      37.076 -13.404  15.616  1.00 39.06           C  
ANISOU   13  CB  LEU A 114     3251   4292   7300   1603   -762   -903       C  
ATOM     14  CG  LEU A 114      37.699 -14.790  15.767  1.00 45.48           C  
ANISOU   14  CG  LEU A 114     4422   5408   7448   1666   -768   -396       C  
ATOM     15  CD1 LEU A 114      38.921 -14.698  16.657  1.00 42.49           C  
ANISOU   15  CD1 LEU A 114     3903   5042   7200   2530   -476    134       C  
ATOM     16  CD2 LEU A 114      36.695 -15.777  16.337  1.00 48.48           C  
ANISOU   16  CD2 LEU A 114     4941   6207   7273   1880   -837   -195       C  
ATOM     17  N  ALYS A 115      35.545 -10.958  14.105  0.33 28.58           N  
ANISOU   17  N  ALYS A 115     1643   3212   6006     32    -37   -875       N  
ATOM     18  N  BLYS A 115      35.552 -10.952  14.115  0.67 29.34           N  
ANISOU   18  N  BLYS A 115     1738   3339   6072    -36     60   -854       N  
ATOM     19  CA ALYS A 115      35.076  -9.585  14.235  0.33 27.20           C  
ANISOU   19  CA ALYS A 115     1677   3291   5369    645    -68   -918       C  
ATOM     20  CA BLYS A 115      35.080  -9.577  14.245  0.67 28.11           C  
ANISOU   20  CA BLYS A 115     1807   3465   5409    813    -12   -894       C  
ATOM     21  C  ALYS A 115      35.125  -8.867  12.894  0.33 25.86           C  
ANISOU   21  C  ALYS A 115     1544   2813   5470    359     -2   -889       C  
ATOM     22  C  BLYS A 115      35.147  -8.855  12.907  0.67 25.66           C  
ANISOU   22  C  BLYS A 115     1460   2763   5525    146     84   -804       C  
ATOM     23  O  ALYS A 115      35.736  -9.357  11.941  0.33 27.27           O  
ANISOU   23  O  ALYS A 115     1706   3317   5337    703    -54   -886       O  
ATOM     24  O  BLYS A 115      35.784  -9.338  11.966  0.67 28.17           O  
ANISOU   24  O  BLYS A 115     1730   3517   5457    715    -30   -903       O  
ATOM     25  CB ALYS A 115      35.923  -8.822  15.254  0.33 24.73           C  
ANISOU   25  CB ALYS A 115     1397   2892   5108    245     -7   -871       C  
ATOM     26  CB BLYS A 115      35.910  -8.814  15.281  0.67 24.92           C  
ANISOU   26  CB BLYS A 115     1452   2862   5156    342     96   -803       C  
ATOM     27  CG ALYS A 115      37.394  -8.728  14.860  0.33 26.38           C  
ANISOU   27  CG ALYS A 115     1414   3367   5242    195     56   -829       C  
ATOM     28  CG BLYS A 115      37.397  -8.732  14.932  0.67 28.47           C  
ANISOU   28  CG BLYS A 115     1629   3607   5579    435    235   -786       C  
ATOM     29  CD ALYS A 115      38.216  -7.925  15.860  0.33 23.91           C  
ANISOU   29  CD ALYS A 115     1344   2811   4929   -139    -38   -961       C  
ATOM     30  CD BLYS A 115      38.189  -7.872  15.919  0.67 24.44           C  
ANISOU   30  CD BLYS A 115     1401   2746   5138   -265    -42   -767       C  
ATOM     31  CE ALYS A 115      37.876  -6.445  15.803  0.33 23.69           C  
ANISOU   31  CE ALYS A 115     1554   2540   4908    177      7   -990       C  
ATOM     32  CE BLYS A 115      38.045  -6.387  15.617  0.67 25.63           C  
ANISOU   32  CE BLYS A 115     1504   2970   5264    471   -258   -627       C  
ATOM     33  NZ ALYS A 115      38.240  -5.840  14.497  0.33 25.84           N  
ANISOU   33  NZ ALYS A 115     1383   3648   4786    224    276   -665       N  
ATOM     34  NZ BLYS A 115      38.578  -5.531  16.713  0.67 27.91           N  
ANISOU   34  NZ BLYS A 115     1489   4066   5050    724    -59   -369       N  
ATOM     35  N   TRP A 116      34.475  -7.710  12.823  1.00 26.71           N  
ANISOU   35  N   TRP A 116     2164   2583   5401    902   -105   -762       N  
ATOM     36  CA  TRP A 116      34.579  -6.857  11.656  1.00 23.80           C  
ANISOU   36  CA  TRP A 116     1368   2818   4854   -383   -140   -575       C  
ATOM     37  C   TRP A 116      35.914  -6.169  11.748  1.00 26.00           C  
ANISOU   37  C   TRP A 116     1436   3207   5238    394     -7   -584       C  
ATOM     38  O   TRP A 116      36.353  -5.839  12.842  1.00 29.15           O  
ANISOU   38  O   TRP A 116     2158   3564   5354    -47   -167   -577       O  
ATOM     39  CB  TRP A 116      33.454  -5.820  11.602  1.00 24.54           C  
ANISOU   39  CB  TRP A 116     1255   3232   4838   -202    157   -346       C  
ATOM     40  CG  TRP A 116      32.096  -6.413  11.368  1.00 24.35           C  
ANISOU   40  CG  TRP A 116     1250   3277   4724    141    181   -534       C  
ATOM     41  CD1 TRP A 116      31.109  -6.599  12.291  1.00 26.24           C  
ANISOU   41  CD1 TRP A 116     1202   4077   4691    130     82   -241       C  
ATOM     42  CD2 TRP A 116      31.585  -6.909  10.127  1.00 28.00           C  
ANISOU   42  CD2 TRP A 116     1609   4199   4831    686   -210   -686       C  
ATOM     43  NE1 TRP A 116      30.005  -7.174  11.696  1.00 24.93           N  
ANISOU   43  NE1 TRP A 116     1275   3629   4568   -366     66   -606       N  
ATOM     44  CE2 TRP A 116      30.274  -7.371  10.367  1.00 26.28           C  
ANISOU   44  CE2 TRP A 116     1348   3961   4675   -237    -33   -899       C  
ATOM     45  CE3 TRP A 116      32.105  -7.001   8.833  1.00 26.21           C  
ANISOU   45  CE3 TRP A 116     1388   3939   4630    246   -297   -660       C  
ATOM     46  CZ2 TRP A 116      29.482  -7.927   9.361  1.00 26.23           C  
ANISOU   46  CZ2 TRP A 116     1385   3950   4632   -417      5   -865       C  
ATOM     47  CZ3 TRP A 116      31.322  -7.545   7.837  1.00 25.67           C  
ANISOU   47  CZ3 TRP A 116     1488   3598   4668    -62    -56   -852       C  
ATOM     48  CH2 TRP A 116      30.017  -8.002   8.105  1.00 26.10           C  
ANISOU   48  CH2 TRP A 116     1460   4124   4332   -826   -100   -520       C  
ATOM     49  N   HIS A 117      36.537  -5.928  10.605  1.00 27.27           N  
ANISOU   49  N   HIS A 117     1543   3334   5484    291    140  -1016       N  
ATOM     50  CA  HIS A 117      37.854  -5.304  10.605  1.00 25.94           C  
ANISOU   50  CA  HIS A 117     1401   3123   5331    -27     80   -812       C  
ATOM     51  C   HIS A 117      37.767  -3.800  10.396  1.00 24.90           C  
ANISOU   51  C   HIS A 117     1954   1911   5594   -491     -2   -465       C  
ATOM     52  O   HIS A 117      38.736  -3.087  10.640  1.00 28.73           O  
ANISOU   52  O   HIS A 117     2078   3063   5774    -63     62   -746       O  
ATOM     53  CB  HIS A 117      38.750  -5.956   9.546  1.00 29.00           C  
ANISOU   53  CB  HIS A 117     1837   3395   5787    427    585  -1034       C  
ATOM     54  CG  HIS A 117      38.921  -7.432   9.737  1.00 29.55           C  
ANISOU   54  CG  HIS A 117     1719   3992   5515   -657    593   -831       C  
ATOM     55  ND1 HIS A 117      39.040  -8.009  10.983  1.00 32.29           N  
ANISOU   55  ND1 HIS A 117     1784   4752   5732    514    671   -765       N  
ATOM     56  CD2 HIS A 117      38.977  -8.449   8.845  1.00 36.39           C  
ANISOU   56  CD2 HIS A 117     3591   4374   5861    471    301   -825       C  
ATOM     57  CE1 HIS A 117      39.167  -9.317  10.851  1.00 34.63           C  
ANISOU   57  CE1 HIS A 117     3378   3952   5828   1787    592   -999       C  
ATOM     58  NE2 HIS A 117      39.134  -9.610   9.564  1.00 39.69           N  
ANISOU   58  NE2 HIS A 117     5099   4139   5844   1460    509   -907       N  
ATOM     59  N   HIS A 118      36.609  -3.317   9.954  1.00 25.62           N  
ANISOU   59  N   HIS A 118     1693   2976   5066    835   -219   -200       N  
ATOM     60  CA  HIS A 118      36.328  -1.873   9.912  1.00 26.79           C  
ANISOU   60  CA  HIS A 118     1451   3309   5418   -127    295   -643       C  
ATOM     61  C   HIS A 118      35.261  -1.509  10.951  1.00 27.40           C  
ANISOU   61  C   HIS A 118     1854   3252   5304    193    465  -1075       C  
ATOM     62  O   HIS A 118      34.567  -2.388  11.464  1.00 28.45           O  
ANISOU   62  O   HIS A 118     1774   3583   5453    431    403   -813       O  
ATOM     63  CB  HIS A 118      35.900  -1.435   8.511  1.00 27.59           C  
ANISOU   63  CB  HIS A 118     1604   4027   4852   -887    427   -379       C  
ATOM     64  CG  HIS A 118      34.618  -2.053   8.047  1.00 26.73           C  
ANISOU   64  CG  HIS A 118     1598   3493   5067   -748    473   -258       C  
ATOM     65  ND1 HIS A 118      34.462  -3.413   7.896  1.00 28.12           N  
ANISOU   65  ND1 HIS A 118     1430   3974   5283   -318    334   -482       N  
ATOM     66  CD2 HIS A 118      33.444  -1.495   7.672  1.00 28.13           C  
ANISOU   66  CD2 HIS A 118     1451   4331   4907   -547    -36   -676       C  
ATOM     67  CE1 HIS A 118      33.237  -3.669   7.473  1.00 27.02           C  
ANISOU   67  CE1 HIS A 118     1575   3787   4903   -848    316   -377       C  
ATOM     68  NE2 HIS A 118      32.599  -2.521   7.325  1.00 29.58           N  
ANISOU   68  NE2 HIS A 118     1785   4136   5317   -996    141   -631       N  
ATOM     69  N  AHIS A 119      35.121  -0.225  11.280  0.20 28.69           N  
ANISOU   69  N  AHIS A 119     2213   3479   5207   -218    426  -1026       N  
ATOM     70  N  BHIS A 119      35.149  -0.217  11.250  0.35 27.29           N  
ANISOU   70  N  BHIS A 119     2152   3069   5149   -252    438  -1024       N  
ATOM     71  N  CHIS A 119      35.122  -0.217  11.234  0.45 25.64           N  
ANISOU   71  N  CHIS A 119     2072   2441   5229   -543    441  -1081       N  
ATOM     72  CA AHIS A 119      34.154   0.144  12.315  0.20 30.44           C  
ANISOU   72  CA AHIS A 119     2286   4111   5169   -434    414   -955       C  
ATOM     73  CA BHIS A 119      34.258   0.271  12.296  0.35 28.68           C  
ANISOU   73  CA BHIS A 119     1907   3919   5069   -285    388   -871       C  
ATOM     74  CA CHIS A 119      34.234   0.239  12.296  0.45 27.96           C  
ANISOU   74  CA CHIS A 119     1972   3372   5281   -825    280   -897       C  
ATOM     75  C  AHIS A 119      32.914   0.847  11.763  0.20 31.49           C  
ANISOU   75  C  AHIS A 119     2008   4818   5137  -1055    471   -803       C  
ATOM     76  C  BHIS A 119      32.933   0.791  11.744  0.35 27.60           C  
ANISOU   76  C  BHIS A 119     1813   3761   4914  -1035    449   -678       C  
ATOM     77  C  CHIS A 119      32.928   0.808  11.750  0.45 28.53           C  
ANISOU   77  C  CHIS A 119     1861   4016   4963  -1111    433   -658       C  
ATOM     78  O  AHIS A 119      31.940   1.046  12.487  0.20 34.42           O  
ANISOU   78  O  AHIS A 119     2250   5769   5058  -1052    573   -901       O  
ATOM     79  O  BHIS A 119      31.925   0.805  12.448  0.35 26.62           O  
ANISOU   79  O  BHIS A 119     2210   2958   4949  -1152    655   -672       O  
ATOM     80  O  CHIS A 119      31.928   0.878  12.464  0.45 29.64           O  
ANISOU   80  O  CHIS A 119     2215   4074   4971  -1378    719   -600       O  
ATOM     81  CB AHIS A 119      34.824   0.999  13.415  0.20 30.33           C  
ANISOU   81  CB AHIS A 119     2521   3837   5167   -284    350   -821       C  
ATOM     82  CB BHIS A 119      34.938   1.383  13.101  0.35 28.16           C  
ANISOU   82  CB BHIS A 119     1827   3943   4929   -151    365   -753       C  
ATOM     83  CB CHIS A 119      34.932   1.296  13.149  0.45 25.46           C  
ANISOU   83  CB CHIS A 119     2149   2606   4919  -1036    123   -663       C  
ATOM     84  CG AHIS A 119      35.135   2.415  13.023  0.20 31.34           C  
ANISOU   84  CG AHIS A 119     3184   3528   5195     67    280   -789       C  
ATOM     85  CG BHIS A 119      35.943   0.891  14.095  0.35 29.12           C  
ANISOU   85  CG BHIS A 119     2147   4057   4861    906    596   -628       C  
ATOM     86  CG CHIS A 119      34.810   2.683  12.599  0.45 27.57           C  
ANISOU   86  CG CHIS A 119     2853   2437   5185    -75    214   -592       C  
ATOM     87  ND1AHIS A 119      34.225   3.250  12.410  0.20 32.22           N  
ANISOU   87  ND1AHIS A 119     3521   3530   5190    375    333   -747       N  
ATOM     88  ND1BHIS A 119      36.238  -0.445  14.263  0.35 31.46           N  
ANISOU   88  ND1BHIS A 119     2696   4400   4858    341    494   -495       N  
ATOM     89  ND1CHIS A 119      35.567   3.133  11.539  0.45 23.50           N  
ANISOU   89  ND1CHIS A 119     1627   2063   5240   -431    181   -686       N  
ATOM     90  CD2AHIS A 119      36.255   3.155  13.203  0.20 32.16           C  
ANISOU   90  CD2AHIS A 119     3768   3219   5234    426    173   -775       C  
ATOM     91  CD2BHIS A 119      36.714   1.561  14.984  0.35 27.19           C  
ANISOU   91  CD2BHIS A 119     1369   4200   4762     99    520   -526       C  
ATOM     92  CD2CHIS A 119      34.006   3.713  12.952  0.45 24.78           C  
ANISOU   92  CD2CHIS A 119     2888   1471   5056   -433    189   -537       C  
ATOM     93  CE1AHIS A 119      34.779   4.432  12.205  0.20 33.36           C  
ANISOU   93  CE1AHIS A 119     3863   3599   5212    618    274   -719       C  
ATOM     94  CE1BHIS A 119      37.151  -0.576  15.209  0.35 32.03           C  
ANISOU   94  CE1BHIS A 119     2847   4482   4842    626    544   -496       C  
ATOM     95  CE1CHIS A 119      35.244   4.385  11.270  0.45 22.40           C  
ANISOU   95  CE1CHIS A 119     2344   1453   4713   -482    253   -486       C  
ATOM     96  NE2AHIS A 119      36.011   4.401  12.679  0.20 33.26           N  
ANISOU   96  NE2AHIS A 119     3985   3414   5239    634    192   -775       N  
ATOM     97  NE2BHIS A 119      37.457   0.627  15.662  0.35 32.34           N  
ANISOU   97  NE2BHIS A 119     2752   4690   4845    940    517   -569       N  
ATOM     98  NE2CHIS A 119      34.299   4.762  12.114  0.45 26.08           N  
ANISOU   98  NE2CHIS A 119     2917   1738   5253   -800    315   -237       N  
ATOM     99  N   ASN A 120      32.945   1.223  10.489  1.00 29.95           N  
ANISOU   99  N   ASN A 120     1945   4499   4936  -1288    430   -452       N  
ATOM    100  CA  ASN A 120      31.779   1.848   9.877  1.00 27.94           C  
ANISOU  100  CA  ASN A 120     2348   3403   4867  -1508    257   -300       C  
ATOM    101  C   ASN A 120      30.940   0.779   9.167  1.00 27.87           C  
ANISOU  101  C   ASN A 120     2087   3724   4778  -1474    243    102       C  
ATOM    102  O   ASN A 120      31.035   0.583   7.954  1.00 26.41           O  
ANISOU  102  O   ASN A 120     2254   3010   4771   -689    479    422       O  
ATOM    103  CB  ASN A 120      32.199   2.984   8.925  1.00 28.46           C  
ANISOU  103  CB  ASN A 120     2763   3102   4950  -1606    253   -408       C  
ATOM    104  CG  ASN A 120      33.190   2.533   7.863  1.00 40.22           C  
ANISOU  104  CG  ASN A 120     4539   5264   5480   -334    625    124       C  
ATOM    105  OD1 ASN A 120      34.067   1.706   8.119  1.00 38.18           O  
ANISOU  105  OD1 ASN A 120     3845   5191   5469  -2396    338   -204       O  
ATOM    106  ND2 ASN A 120      33.045   3.070   6.659  1.00 40.15           N  
ANISOU  106  ND2 ASN A 120     5100   4810   5344    465   1088    528       N  
ATOM    107  N   ILE A 121      30.126   0.074   9.952  1.00 24.14           N  
ANISOU  107  N   ILE A 121     1724   2999   4448  -1065     28   -170       N  
ATOM    108  CA  ILE A 121      29.284  -1.010   9.450  1.00 24.12           C  
ANISOU  108  CA  ILE A 121     1462   3220   4481   -816     57   -285       C  
ATOM    109  C   ILE A 121      28.069  -0.461   8.709  1.00 22.67           C  
ANISOU  109  C   ILE A 121     1271   2639   4705   -266    176   -592       C  
ATOM    110  O   ILE A 121      27.467   0.522   9.139  1.00 25.04           O  
ANISOU  110  O   ILE A 121     1991   2465   5060   -726    507  -1139       O  
ATOM    111  CB  ILE A 121      28.819  -1.921  10.607  1.00 23.41           C  
ANISOU  111  CB  ILE A 121     1211   3278   4406   -459    149    111       C  
ATOM    112  CG1 ILE A 121      29.975  -2.257  11.549  1.00 24.02           C  
ANISOU  112  CG1 ILE A 121     1225   3460   4442   -512    -92      2       C  
ATOM    113  CG2 ILE A 121      28.141  -3.195  10.081  1.00 25.30           C  
ANISOU  113  CG2 ILE A 121     1203   3935   4473   -352     73   -315       C  
ATOM    114  CD1 ILE A 121      31.170  -2.918  10.872  1.00 26.31           C  
ANISOU  114  CD1 ILE A 121     1164   4296   4537   -206    -29    136       C  
ATOM    115  N   THR A 122      27.723  -1.088   7.589  1.00 23.39           N  
ANISOU  115  N   THR A 122     1633   2742   4513   -807    138   -666       N  
ATOM    116  CA  THR A 122      26.528  -0.709   6.839  1.00 22.49           C  
ANISOU  116  CA  THR A 122     1158   2862   4527    -97    164   -280       C  
ATOM    117  C   THR A 122      25.487  -1.821   6.849  1.00 20.10           C  
ANISOU  117  C   THR A 122     1235   1900   4503   -276     87   -299       C  
ATOM    118  O   THR A 122      25.823  -3.005   6.970  1.00 24.41           O  
ANISOU  118  O   THR A 122     1404   3199   4672   -523    233   -772       O  
ATOM    119  CB  THR A 122      26.848  -0.348   5.373  1.00 22.50           C  
ANISOU  119  CB  THR A 122     2321   1642   4585   -710    440   -407       C  
ATOM    120  OG1 THR A 122      27.538  -1.431   4.740  1.00 26.63           O  
ANISOU  120  OG1 THR A 122     3067   2408   4641  -1359    363   -741       O  
ATOM    121  CG2 THR A 122      27.698   0.913   5.307  1.00 25.78           C  
ANISOU  121  CG2 THR A 122     3102   2159   4532  -1302    570   -334       C  
ATOM    122  N   TYR A 123      24.223  -1.438   6.726  1.00 20.62           N  
ANISOU  122  N   TYR A 123     1622   1780   4433   -574    -82   -184       N  
ATOM    123  CA  TYR A 123      23.156  -2.431   6.687  1.00 22.31           C  
ANISOU  123  CA  TYR A 123     1990   2230   4258  -1028     97    136       C  
ATOM    124  C   TYR A 123      22.093  -2.077   5.661  1.00 22.24           C  
ANISOU  124  C   TYR A 123     1737   2509   4205   -984    -35    231       C  
ATOM    125  O   TYR A 123      21.826  -0.909   5.398  1.00 22.70           O  
ANISOU  125  O   TYR A 123     2384   1866   4374   -996     89    -31       O  
ATOM    126  CB  TYR A 123      22.544  -2.618   8.081  1.00 23.66           C  
ANISOU  126  CB  TYR A 123     2102   2282   4604   -114    292    -87       C  
ATOM    127  CG  TYR A 123      21.705  -1.482   8.642  1.00 21.68           C  
ANISOU  127  CG  TYR A 123     1677   2432   4128   -915    310    -22       C  
ATOM    128  CD1 TYR A 123      22.299  -0.443   9.369  1.00 21.42           C  
ANISOU  128  CD1 TYR A 123     1217   2693   4227   -509    -63    -27       C  
ATOM    129  CD2 TYR A 123      20.316  -1.478   8.497  1.00 25.55           C  
ANISOU  129  CD2 TYR A 123     1927   3063   4717   -231    489   -201       C  
ATOM    130  CE1 TYR A 123      21.528   0.576   9.908  1.00 20.55           C  
ANISOU  130  CE1 TYR A 123     1491   1551   4768   -234    333    396       C  
ATOM    131  CE2 TYR A 123      19.546  -0.463   9.025  1.00 23.04           C  
ANISOU  131  CE2 TYR A 123     1820   2698   4238  -1106      9    161       C  
ATOM    132  CZ  TYR A 123      20.155   0.563   9.730  1.00 23.72           C  
ANISOU  132  CZ  TYR A 123     1932   2204   4877   -803    282    152       C  
ATOM    133  OH  TYR A 123      19.345   1.552  10.256  1.00 24.96           O  
ANISOU  133  OH  TYR A 123     2775   1668   5039   -668     52   -224       O  
ATOM    134  N   TRP A 124      21.484  -3.118   5.092  1.00 20.60           N  
ANISOU  134  N   TRP A 124     1263   2452   4113   -557     65   -284       N  
ATOM    135  CA  TRP A 124      20.455  -2.994   4.060  1.00 20.48           C  
ANISOU  135  CA  TRP A 124     2037   1562   4182   -710    128   -126       C  
ATOM    136  C   TRP A 124      19.245  -3.826   4.436  1.00 22.43           C  
ANISOU  136  C   TRP A 124     1609   3070   3844  -1157    133     77       C  
ATOM    137  O   TRP A 124      19.365  -5.033   4.644  1.00 23.26           O  
ANISOU  137  O   TRP A 124     2014   2437   4387  -1070    138    296       O  
ATOM    138  CB  TRP A 124      20.979  -3.465   2.704  1.00 23.00           C  
ANISOU  138  CB  TRP A 124     1981   2324   4434   -866   -242   -657       C  
ATOM    139  CG  TRP A 124      19.994  -3.395   1.574  1.00 20.05           C  
ANISOU  139  CG  TRP A 124     1535   1956   4126   -671    170     38       C  
ATOM    140  CD1 TRP A 124      19.105  -2.383   1.310  1.00 22.48           C  
ANISOU  140  CD1 TRP A 124     1706   2314   4520   -762    494   -267       C  
ATOM    141  CD2 TRP A 124      19.767  -4.398   0.565  1.00 19.75           C  
ANISOU  141  CD2 TRP A 124     1852   1442   4208   -493    527     25       C  
ATOM    142  NE1 TRP A 124      18.366  -2.681   0.189  1.00 23.67           N  
ANISOU  142  NE1 TRP A 124     1911   2824   4260  -1157    393   -108       N  
ATOM    143  CE2 TRP A 124      18.749  -3.910  -0.283  1.00 21.50           C  
ANISOU  143  CE2 TRP A 124     1752   1906   4513   -691    150   -156       C  
ATOM    144  CE3 TRP A 124      20.339  -5.645   0.287  1.00 22.63           C  
ANISOU  144  CE3 TRP A 124     2110   2024   4463   -433    525   -230       C  
ATOM    145  CZ2 TRP A 124      18.291  -4.625  -1.386  1.00 23.19           C  
ANISOU  145  CZ2 TRP A 124     2204   2346   4262  -1071    487    333       C  
ATOM    146  CZ3 TRP A 124      19.870  -6.357  -0.803  1.00 24.44           C  
ANISOU  146  CZ3 TRP A 124     1998   2834   4453  -1152    341    -57       C  
ATOM    147  CH2 TRP A 124      18.860  -5.845  -1.626  1.00 21.19           C  
ANISOU  147  CH2 TRP A 124     2423   1251   4376   -355    186   -412       C  
ATOM    148  N   ILE A 125      18.092  -3.176   4.542  1.00 20.56           N  
ANISOU  148  N   ILE A 125     1185   2354   4272   -378     36   -187       N  
ATOM    149  CA  ILE A 125      16.837  -3.883   4.761  1.00 22.26           C  
ANISOU  149  CA  ILE A 125     1457   2807   4195   -806    286   -181       C  
ATOM    150  C   ILE A 125      16.326  -4.330   3.401  1.00 22.11           C  
ANISOU  150  C   ILE A 125     2393   1923   4085  -1085    235    118       C  
ATOM    151  O   ILE A 125      15.701  -3.558   2.676  1.00 21.21           O  
ANISOU  151  O   ILE A 125     2328   1240   4492    -81     55   -233       O  
ATOM    152  CB  ILE A 125      15.815  -2.992   5.490  1.00 23.33           C  
ANISOU  152  CB  ILE A 125     1951   2530   4382  -1037    485   -141       C  
ATOM    153  CG1 ILE A 125      16.393  -2.491   6.820  1.00 22.06           C  
ANISOU  153  CG1 ILE A 125     2529   1391   4462     30    198    -63       C  
ATOM    154  CG2 ILE A 125      14.503  -3.734   5.717  1.00 25.99           C  
ANISOU  154  CG2 ILE A 125     2752   2689   4433    126    386   -131       C  
ATOM    155  CD1 ILE A 125      15.559  -1.419   7.474  1.00 21.61           C  
ANISOU  155  CD1 ILE A 125     2030   1650   4529   -404    -18   -200       C  
ATOM    156  N   GLN A 126      16.590  -5.588   3.057  1.00 21.78           N  
ANISOU  156  N   GLN A 126     1897   2046   4333   -853    300     66       N  
ATOM    157  CA  GLN A 126      16.277  -6.075   1.717  1.00 20.80           C  
ANISOU  157  CA  GLN A 126     1904   1546   4454   -571    282   -173       C  
ATOM    158  C   GLN A 126      14.780  -6.187   1.468  1.00 20.16           C  
ANISOU  158  C   GLN A 126     1659   1718   4284   -576    332    101       C  
ATOM    159  O   GLN A 126      14.309  -5.930   0.362  1.00 22.73           O  
ANISOU  159  O   GLN A 126     2114   2182   4340   -652    129    146       O  
ATOM    160  CB  GLN A 126      16.937  -7.431   1.475  1.00 21.69           C  
ANISOU  160  CB  GLN A 126     1651   2258   4333   -740      6   -567       C  
ATOM    161  CG  GLN A 126      16.703  -7.978   0.088  1.00 24.75           C  
ANISOU  161  CG  GLN A 126     2343   2497   4563   -508    -75   -240       C  
ATOM    162  CD  GLN A 126      17.704  -9.043  -0.297  1.00 27.21           C  
ANISOU  162  CD  GLN A 126     2843   2867   4628   -334   -151   -244       C  
ATOM    163  OE1 GLN A 126      18.417  -9.572   0.553  1.00 26.29           O  
ANISOU  163  OE1 GLN A 126     2376   2944   4669   -201   -225   -545       O  
ATOM    164  NE2 GLN A 126      17.762  -9.364  -1.582  1.00 30.60           N  
ANISOU  164  NE2 GLN A 126     3188   3704   4733   -882   -635   -144       N  
ATOM    165  N  AASN A 127      14.043  -6.600   2.492  0.32 19.58           N  
ANISOU  165  N  AASN A 127     1657   1742   4041   -677    159     57       N  
ATOM    166  N  BASN A 127      14.035  -6.573   2.493  0.68 20.35           N  
ANISOU  166  N  BASN A 127     1742   1830   4160   -738    103     81       N  
ATOM    167  CA AASN A 127      12.599  -6.746   2.374  0.32 19.39           C  
ANISOU  167  CA AASN A 127     1593   1693   4081   -610   -101     43       C  
ATOM    168  CA BASN A 127      12.591  -6.662   2.360  0.68 21.79           C  
ANISOU  168  CA BASN A 127     1551   2438   4290   -333   -182   -224       C  
ATOM    169  C  AASN A 127      11.930  -6.585   3.729  0.32 20.37           C  
ANISOU  169  C  AASN A 127     1513   2313   3914   -834    -49    196       C  
ATOM    170  C  BASN A 127      11.934  -6.473   3.711  0.68 22.45           C  
ANISOU  170  C  BASN A 127     1988   2270   4273   -634   -128     87       C  
ATOM    171  O  AASN A 127      12.598  -6.578   4.767  0.32 21.81           O  
ANISOU  171  O  AASN A 127     1223   3017   4046   -396    210    425       O  
ATOM    172  O  BASN A 127      12.618  -6.315   4.728  0.68 21.47           O  
ANISOU  172  O  BASN A 127     1856   2055   4247   -745    226   -136       O  
ATOM    173  CB AASN A 127      12.231  -8.100   1.759  0.32 18.93           C  
ANISOU  173  CB AASN A 127     2333   1368   3493   -715   -246    530       C  
ATOM    174  CB BASN A 127      12.174  -7.995   1.721  0.68 25.37           C  
ANISOU  174  CB BASN A 127     2171   3107   4359    -19   -625      7       C  
ATOM    175  CG AASN A 127      12.470  -9.252   2.704  0.32 20.54           C  
ANISOU  175  CG AASN A 127     2628   1386   3789   -611   -295    514       C  
ATOM    176  CG BASN A 127      12.862  -9.190   2.347  0.68 22.17           C  
ANISOU  176  CG BASN A 127     1849   2228   4347   -885   -350    -95       C  
ATOM    177  OD1AASN A 127      13.287  -9.169   3.617  0.32 20.37           O  
ANISOU  177  OD1AASN A 127     2164   1883   3694   -558   -204    634       O  
ATOM    178  OD1BASN A 127      12.893  -9.341   3.569  0.68 23.86           O  
ANISOU  178  OD1BASN A 127     1330   3387   4350   -655    271    259       O  
ATOM    179  ND2AASN A 127      11.747 -10.340   2.491  0.32 20.31           N  
ANISOU  179  ND2AASN A 127     3190   1026   3503   -388   -434     18       N  
ATOM    180  ND2BASN A 127      13.417 -10.057   1.501  0.68 23.29           N  
ANISOU  180  ND2BASN A 127     3091   1264   4495   -482   -335     48       N  
ATOM    181  N   TYR A 128      10.607  -6.472   3.708  1.00 21.86           N  
ANISOU  181  N   TYR A 128     1232   2998   4074   -592     18    352       N  
ATOM    182  CA  TYR A 128       9.841  -6.178   4.902  1.00 23.50           C  
ANISOU  182  CA  TYR A 128     1889   2571   4469   -393    101    246       C  
ATOM    183  C   TYR A 128       8.814  -7.229   5.217  1.00 22.54           C  
ANISOU  183  C   TYR A 128     1729   2595   4239   -955   -190   -335       C  
ATOM    184  O   TYR A 128       8.188  -7.798   4.326  1.00 32.14           O  
ANISOU  184  O   TYR A 128     3348   4312   4550  -2221    362   -251       O  
ATOM    185  CB  TYR A 128       9.103  -4.844   4.763  1.00 23.27           C  
ANISOU  185  CB  TYR A 128     1992   2360   4490    -66   -212    105       C  
ATOM    186  CG  TYR A 128      10.010  -3.648   4.862  1.00 22.50           C  
ANISOU  186  CG  TYR A 128     2310   1790   4448    -24    -32     91       C  
ATOM    187  CD1 TYR A 128      10.688  -3.164   3.745  1.00 24.14           C  
ANISOU  187  CD1 TYR A 128     2620   2084   4468   -494   -128     66       C  
ATOM    188  CD2 TYR A 128      10.200  -2.997   6.075  1.00 24.43           C  
ANISOU  188  CD2 TYR A 128     2570   2266   4444    438   -104   -214       C  
ATOM    189  CE1 TYR A 128      11.526  -2.066   3.841  1.00 26.80           C  
ANISOU  189  CE1 TYR A 128     3226   2418   4538   -885   -172     97       C  
ATOM    190  CE2 TYR A 128      11.031  -1.900   6.174  1.00 24.67           C  
ANISOU  190  CE2 TYR A 128     2225   2612   4536   -724    -96   -311       C  
ATOM    191  CZ  TYR A 128      11.684  -1.447   5.056  1.00 25.92           C  
ANISOU  191  CZ  TYR A 128     3316   1911   4621   -546   -177    -17       C  
ATOM    192  OH  TYR A 128      12.506  -0.359   5.164  1.00 31.16           O  
ANISOU  192  OH  TYR A 128     5035   2045   4760  -1056     70   -173       O  
ATOM    193  N   SER A 129       8.611  -7.440   6.507  1.00 20.18           N  
ANISOU  193  N   SER A 129     1296   1789   4583     85    -89   -362       N  
ATOM    194  CA  SER A 129       7.449  -8.162   6.975  1.00 22.54           C  
ANISOU  194  CA  SER A 129     1257   2377   4929    -86    138   -364       C  
ATOM    195  C   SER A 129       6.253  -7.226   6.896  1.00 23.33           C  
ANISOU  195  C   SER A 129     1301   2530   5032   -206     45   -308       C  
ATOM    196  O   SER A 129       6.387  -6.023   7.115  1.00 25.27           O  
ANISOU  196  O   SER A 129     1327   3215   5058    331     92    159       O  
ATOM    197  CB  SER A 129       7.637  -8.649   8.403  1.00 20.62           C  
ANISOU  197  CB  SER A 129     1205   2001   4628   -185     78   -257       C  
ATOM    198  OG  SER A 129       6.374  -9.093   8.908  1.00 20.68           O  
ANISOU  198  OG  SER A 129     1191   2168   4496   -202    247   -333       O  
ATOM    199  N   GLU A 130       5.076  -7.770   6.597  1.00 24.78           N  
ANISOU  199  N   GLU A 130     1208   3405   4802    117     42    -75       N  
ATOM    200  CA  GLU A 130       3.852  -6.964   6.599  1.00 27.82           C  
ANISOU  200  CA  GLU A 130     1326   3982   5261      8   -181     39       C  
ATOM    201  C   GLU A 130       3.267  -6.877   7.999  1.00 24.46           C  
ANISOU  201  C   GLU A 130     1322   2700   5271     30    -25   -183       C  
ATOM    202  O   GLU A 130       2.226  -6.256   8.196  1.00 26.86           O  
ANISOU  202  O   GLU A 130     1375   3728   5102    443    224    147       O  
ATOM    203  CB  GLU A 130       2.831  -7.535   5.615  1.00 37.27           C  
ANISOU  203  CB  GLU A 130     2290   6109   5760   1620   -274    -41       C  
ATOM    204  CG  GLU A 130       3.258  -7.397   4.164  1.00 48.76           C  
ANISOU  204  CG  GLU A 130     4314   8191   6023    780    -57    419       C  
ATOM    205  CD  GLU A 130       2.312  -8.089   3.205  1.00 68.15           C  
ANISOU  205  CD  GLU A 130     8450  11026   6419   2292    467    934       C  
ATOM    206  OE1 GLU A 130       1.170  -8.392   3.609  1.00 72.99           O  
ANISOU  206  OE1 GLU A 130     8522  12598   6615   2189    734   1047       O  
ATOM    207  OE2 GLU A 130       2.711  -8.326   2.045  1.00 79.48           O  
ANISOU  207  OE2 GLU A 130    11419  12022   6758   3427    516    993       O  
ATOM    208  N   ASP A 131       3.913  -7.515   8.970  1.00 21.69           N  
ANISOU  208  N   ASP A 131     1216   2329   4697      1   -328   -174       N  
ATOM    209  CA  ASP A 131       3.408  -7.558  10.334  1.00 24.87           C  
ANISOU  209  CA  ASP A 131     1819   2542   5087    226     24   -414       C  
ATOM    210  C   ASP A 131       3.325  -6.170  10.956  1.00 21.55           C  
ANISOU  210  C   ASP A 131     1154   2431   4604    -38    -28   -117       C  
ATOM    211  O   ASP A 131       2.460  -5.925  11.792  1.00 23.39           O  
ANISOU  211  O   ASP A 131     1584   2127   5178    256    342    -29       O  
ATOM    212  CB  ASP A 131       4.274  -8.436  11.241  1.00 20.96           C  
ANISOU  212  CB  ASP A 131     1263   1818   4881   -159     27    -82       C  
ATOM    213  CG  ASP A 131       4.315  -9.897  10.818  1.00 20.31           C  
ANISOU  213  CG  ASP A 131     1306   2168   4243   -519     61   -103       C  
ATOM    214  OD1 ASP A 131       3.663 -10.299   9.822  1.00 24.31           O  
ANISOU  214  OD1 ASP A 131     1954   2254   5030   -790    -21   -446       O  
ATOM    215  OD2 ASP A 131       5.018 -10.650  11.522  1.00 22.02           O  
ANISOU  215  OD2 ASP A 131     1443   2243   4682   -312   -231   -523       O  
ATOM    216  N   LEU A 132       4.246  -5.290  10.555  1.00 21.84           N  
ANISOU  216  N   LEU A 132     1390   2010   4900   -336    231     40       N  
ATOM    217  CA  LEU A 132       4.410  -3.949  11.128  1.00 21.14           C  
ANISOU  217  CA  LEU A 132     1330   1544   5156    -74   -186    468       C  
ATOM    218  C   LEU A 132       4.600  -2.926  10.016  1.00 21.53           C  
ANISOU  218  C   LEU A 132     1378   1618   5182    -30   -482   -127       C  
ATOM    219  O   LEU A 132       5.015  -3.274   8.911  1.00 26.20           O  
ANISOU  219  O   LEU A 132     1701   3175   5079   -469   -355    212       O  
ATOM    220  CB  LEU A 132       5.604  -3.916  12.092  1.00 24.14           C  
ANISOU  220  CB  LEU A 132     1691   2316   5165   -190   -536    -96       C  
ATOM    221  CG  LEU A 132       5.484  -4.718  13.393  1.00 23.70           C  
ANISOU  221  CG  LEU A 132     1612   2304   5088    527   -451    -32       C  
ATOM    222  CD1 LEU A 132       6.868  -4.875  14.042  1.00 22.69           C  
ANISOU  222  CD1 LEU A 132     1253   2507   4862    -79   -284   -173       C  
ATOM    223  CD2 LEU A 132       4.507  -4.055  14.352  1.00 21.99           C  
ANISOU  223  CD2 LEU A 132     1678   1771   4908    289   -382   -456       C  
ATOM    224  N   PRO A 133       4.249  -1.660  10.286  1.00 25.04           N  
ANISOU  224  N   PRO A 133     2107   2050   5357    503   -220    -46       N  
ATOM    225  CA  PRO A 133       4.547  -0.602   9.319  1.00 26.04           C  
ANISOU  225  CA  PRO A 133     2867   1608   5417    583   -321    138       C  
ATOM    226  C   PRO A 133       6.039  -0.502   9.054  1.00 25.48           C  
ANISOU  226  C   PRO A 133     3360   1391   4931    272   -110    586       C  
ATOM    227  O   PRO A 133       6.828  -0.797   9.956  1.00 24.83           O  
ANISOU  227  O   PRO A 133     2041   1807   5586    214   -440    516       O  
ATOM    228  CB  PRO A 133       4.032   0.659  10.014  1.00 25.79           C  
ANISOU  228  CB  PRO A 133     2038   2590   5173    947   -284    165       C  
ATOM    229  CG  PRO A 133       2.953   0.166  10.916  1.00 28.70           C  
ANISOU  229  CG  PRO A 133     2206   3360   5338    462     88     82       C  
ATOM    230  CD  PRO A 133       3.453  -1.156  11.419  1.00 27.16           C  
ANISOU  230  CD  PRO A 133     2932   2205   5183    532    -88   -261       C  
ATOM    231  N   ARG A 134       6.414  -0.102   7.843  1.00 24.88           N  
ANISOU  231  N   ARG A 134     2752   1379   5321   -177   -455    180       N  
ATOM    232  CA  ARG A 134       7.818  -0.052   7.478  1.00 26.44           C  
ANISOU  232  CA  ARG A 134     3109   1571   5365   -108   -308    220       C  
ATOM    233  C   ARG A 134       8.615   0.884   8.389  1.00 22.60           C  
ANISOU  233  C   ARG A 134     2487   1433   4668    564    -48    239       C  
ATOM    234  O   ARG A 134       9.753   0.552   8.756  1.00 26.86           O  
ANISOU  234  O   ARG A 134     2880   2051   5276   1023   -117    355       O  
ATOM    235  CB  ARG A 134       7.975   0.356   6.011  1.00 27.37           C  
ANISOU  235  CB  ARG A 134     3357   1754   5287    723   -563    198       C  
ATOM    236  CG  ARG A 134       7.482  -0.691   5.023  1.00 33.75           C  
ANISOU  236  CG  ARG A 134     4052   3500   5273    331   -615     51       C  
ATOM    237  CD  ARG A 134       8.153  -0.528   3.668  1.00 39.76           C  
ANISOU  237  CD  ARG A 134     4563   5172   5373   1481   -806    -95       C  
ATOM    238  NE  ARG A 134       7.713  -1.535   2.707  1.00 40.99           N  
ANISOU  238  NE  ARG A 134     4782   5312   5481   1269   -837   -155       N  
ATOM    239  CZ  ARG A 134       8.207  -1.658   1.478  1.00 45.56           C  
ANISOU  239  CZ  ARG A 134     5665   6044   5600   1435   -669   -152       C  
ATOM    240  NH1 ARG A 134       7.750  -2.604   0.668  1.00 45.29           N  
ANISOU  240  NH1 ARG A 134     6004   5591   5615    738   -374    -31       N  
ATOM    241  NH2 ARG A 134       9.161  -0.835   1.058  1.00 41.15           N  
ANISOU  241  NH2 ARG A 134     5712   4260   5663    666   -570   -362       N  
ATOM    242  N   ALA A 135       8.032   2.034   8.749  1.00 24.87           N  
ANISOU  242  N   ALA A 135     2852   1417   5179    286   -593    224       N  
ATOM    243  CA  ALA A 135       8.721   2.992   9.614  1.00 23.38           C  
ANISOU  243  CA  ALA A 135     2717   1268   4898    115   -444   -215       C  
ATOM    244  C   ALA A 135       8.977   2.424  11.009  1.00 26.00           C  
ANISOU  244  C   ALA A 135     2221   2606   5053    468   -394    114       C  
ATOM    245  O   ALA A 135       9.964   2.768  11.660  1.00 25.09           O  
ANISOU  245  O   ALA A 135     1768   2695   5070    622   -261     -3       O  
ATOM    246  CB  ALA A 135       7.922   4.266   9.717  1.00 31.80           C  
ANISOU  246  CB  ALA A 135     4715   2367   5000    772   -560   -145       C  
ATOM    247  N   VAL A 136       8.085   1.548  11.463  1.00 25.13           N  
ANISOU  247  N   VAL A 136     2053   2442   5054    531   -223     65       N  
ATOM    248  CA  VAL A 136       8.226   0.901  12.766  1.00 22.36           C  
ANISOU  248  CA  VAL A 136     1597   2021   4877    518    179   -255       C  
ATOM    249  C   VAL A 136       9.325  -0.147  12.728  1.00 20.97           C  
ANISOU  249  C   VAL A 136     1261   1821   4885     98   -209   -424       C  
ATOM    250  O   VAL A 136      10.118  -0.276  13.658  1.00 22.14           O  
ANISOU  250  O   VAL A 136     1917   1372   5125    190   -340   -337       O  
ATOM    251  CB  VAL A 136       6.903   0.251  13.204  1.00 24.56           C  
ANISOU  251  CB  VAL A 136     1647   2637   5048    516    401   -640       C  
ATOM    252  CG1 VAL A 136       7.075  -0.490  14.518  1.00 26.99           C  
ANISOU  252  CG1 VAL A 136     3123   2144   4989    785    359   -416       C  
ATOM    253  CG2 VAL A 136       5.837   1.321  13.350  1.00 30.07           C  
ANISOU  253  CG2 VAL A 136     2038   4355   5031    520    366   -857       C  
ATOM    254  N   ILE A 137       9.346  -0.908  11.643  1.00 21.98           N  
ANISOU  254  N   ILE A 137     1355   2047   4948    205    403   -153       N  
ATOM    255  CA  ILE A 137      10.397  -1.885  11.428  1.00 21.60           C  
ANISOU  255  CA  ILE A 137     1366   1746   5096      2    108   -183       C  
ATOM    256  C   ILE A 137      11.751  -1.170  11.322  1.00 21.95           C  
ANISOU  256  C   ILE A 137     1263   2152   4925    168    -63     -8       C  
ATOM    257  O   ILE A 137      12.732  -1.580  11.957  1.00 20.44           O  
ANISOU  257  O   ILE A 137     1262   1513   4993    -22    -47   -362       O  
ATOM    258  CB  ILE A 137      10.116  -2.733  10.164  1.00 22.47           C  
ANISOU  258  CB  ILE A 137     1702   1847   4989     13    105   -245       C  
ATOM    259  CG1 ILE A 137       8.944  -3.694  10.426  1.00 19.89           C  
ANISOU  259  CG1 ILE A 137     1337   1374   4845    -80     46   -565       C  
ATOM    260  CG2 ILE A 137      11.344  -3.509   9.746  1.00 21.51           C  
ANISOU  260  CG2 ILE A 137     1680   1654   4840     54     71    -69       C  
ATOM    261  CD1 ILE A 137       8.429  -4.424   9.200  1.00 22.52           C  
ANISOU  261  CD1 ILE A 137     1875   1588   5095   -422     92   -251       C  
ATOM    262  N   ASP A 138      11.811  -0.104  10.521  1.00 21.51           N  
ANISOU  262  N   ASP A 138     1351   1688   5136   -158    125   -161       N  
ATOM    263  CA  ASP A 138      13.041   0.690  10.387  1.00 21.66           C  
ANISOU  263  CA  ASP A 138     1537   1548   5143   -169   -326   -407       C  
ATOM    264  C   ASP A 138      13.530   1.151  11.753  1.00 21.64           C  
ANISOU  264  C   ASP A 138     1368   1702   5153    171    -98   -313       C  
ATOM    265  O   ASP A 138      14.723   1.026  12.078  1.00 23.00           O  
ANISOU  265  O   ASP A 138     1586   1758   5394   -304    231   -233       O  
ATOM    266  CB  ASP A 138      12.811   1.913   9.493  1.00 28.13           C  
ANISOU  266  CB  ASP A 138     2947   2397   5342   -239   -319    240       C  
ATOM    267  CG  ASP A 138      12.559   1.549   8.040  1.00 26.17           C  
ANISOU  267  CG  ASP A 138     2921   1585   5438    354   -226    172       C  
ATOM    268  OD1 ASP A 138      12.728   0.360   7.679  1.00 26.95           O  
ANISOU  268  OD1 ASP A 138     2386   2436   5419   -410   -123    175       O  
ATOM    269  OD2 ASP A 138      12.193   2.469   7.263  1.00 28.05           O  
ANISOU  269  OD2 ASP A 138     2960   2191   5509    547   -119    142       O  
ATOM    270  N   ASP A 139      12.610   1.694  12.546  1.00 22.21           N  
ANISOU  270  N   ASP A 139     2221   1247   4971    -50     23    -79       N  
ATOM    271  CA  ASP A 139      12.960   2.195  13.868  1.00 24.38           C  
ANISOU  271  CA  ASP A 139     2103   1851   5309   -310    149   -420       C  
ATOM    272  C   ASP A 139      13.389   1.083  14.822  1.00 22.23           C  
ANISOU  272  C   ASP A 139     1860   1864   4722   -649   -129   -292       C  
ATOM    273  O   ASP A 139      14.299   1.272  15.630  1.00 23.53           O  
ANISOU  273  O   ASP A 139     2039   1948   4954   -703    141   -522       O  
ATOM    274  CB  ASP A 139      11.793   2.974  14.470  1.00 26.84           C  
ANISOU  274  CB  ASP A 139     2499   2347   5351     23    227   -430       C  
ATOM    275  CG  ASP A 139      12.033   3.349  15.915  1.00 35.77           C  
ANISOU  275  CG  ASP A 139     4816   3179   5596   1229    153   -278       C  
ATOM    276  OD1 ASP A 139      12.700   4.377  16.158  1.00 39.29           O  
ANISOU  276  OD1 ASP A 139     6405   2732   5791   2032    -32     91       O  
ATOM    277  OD2 ASP A 139      11.551   2.621  16.811  1.00 35.17           O  
ANISOU  277  OD2 ASP A 139     4853   2784   5728     90    274   -605       O  
ATOM    278  N   ALA A 140      12.734  -0.071  14.747  1.00 20.71           N  
ANISOU  278  N   ALA A 140     1378   1687   4803    263   -220   -519       N  
ATOM    279  CA  ALA A 140      13.133  -1.177  15.608  1.00 20.27           C  
ANISOU  279  CA  ALA A 140     1305   1688   4707    220   -346   -305       C  
ATOM    280  C   ALA A 140      14.577  -1.591  15.350  1.00 20.66           C  
ANISOU  280  C   ALA A 140     1236   2117   4498   -302   -165   -179       C  
ATOM    281  O   ALA A 140      15.329  -1.800  16.291  1.00 19.59           O  
ANISOU  281  O   ALA A 140     1193   1594   4655     40   -127   -533       O  
ATOM    282  CB  ALA A 140      12.206  -2.359  15.425  1.00 20.07           C  
ANISOU  282  CB  ALA A 140     1139   1948   4540    -52    -25     91       C  
ATOM    283  N   PHE A 141      14.931  -1.717  14.076  1.00 20.37           N  
ANISOU  283  N   PHE A 141     1217   1965   4558   -219    239   -185       N  
ATOM    284  CA  PHE A 141      16.308  -2.029  13.696  1.00 19.86           C  
ANISOU  284  CA  PHE A 141     1581   1664   4300   -541    131   -143       C  
ATOM    285  C   PHE A 141      17.298  -0.927  14.123  1.00 19.64           C  
ANISOU  285  C   PHE A 141     1253   1589   4622   -201    107   -166       C  
ATOM    286  O   PHE A 141      18.379  -1.243  14.633  1.00 21.12           O  
ANISOU  286  O   PHE A 141     1241   2214   4570   -308    158     37       O  
ATOM    287  CB  PHE A 141      16.394  -2.286  12.189  1.00 21.08           C  
ANISOU  287  CB  PHE A 141     1551   2123   4337   -683    217    -39       C  
ATOM    288  CG  PHE A 141      15.750  -3.594  11.753  1.00 19.34           C  
ANISOU  288  CG  PHE A 141     1364   1739   4244   -172    -49     18       C  
ATOM    289  CD1 PHE A 141      15.753  -4.697  12.591  1.00 20.96           C  
ANISOU  289  CD1 PHE A 141     1510   2171   4285   -321   -316   -284       C  
ATOM    290  CD2 PHE A 141      15.129  -3.717  10.511  1.00 18.33           C  
ANISOU  290  CD2 PHE A 141     1371   1536   4059   -406    280     13       C  
ATOM    291  CE1 PHE A 141      15.163  -5.885  12.201  1.00 17.85           C  
ANISOU  291  CE1 PHE A 141     1172   1615   3996    275    385    257       C  
ATOM    292  CE2 PHE A 141      14.538  -4.910  10.121  1.00 18.07           C  
ANISOU  292  CE2 PHE A 141     1071   1602   4192    -79    123   -281       C  
ATOM    293  CZ  PHE A 141      14.578  -5.991  10.964  1.00 19.42           C  
ANISOU  293  CZ  PHE A 141     1251   1756   4370    285    341    210       C  
ATOM    294  N   ALA A 142      16.933   0.343  13.925  1.00 21.44           N  
ANISOU  294  N   ALA A 142     1462   2010   4673   -140    152    193       N  
ATOM    295  CA  ALA A 142      17.776   1.472  14.336  1.00 22.99           C  
ANISOU  295  CA  ALA A 142     2538   1689   4507   -881   -196    110       C  
ATOM    296  C   ALA A 142      18.055   1.442  15.837  1.00 23.51           C  
ANISOU  296  C   ALA A 142     2257   1788   4887   -763    104   -106       C  
ATOM    297  O   ALA A 142      19.184   1.696  16.270  1.00 24.76           O  
ANISOU  297  O   ALA A 142     2189   2340   4878  -1001   -213   -275       O  
ATOM    298  CB  ALA A 142      17.115   2.779  13.943  1.00 22.78           C  
ANISOU  298  CB  ALA A 142     2488   1521   4646   -652   -457    146       C  
ATOM    299  N   ARG A 143      17.029   1.124  16.631  1.00 20.64           N  
ANISOU  299  N   ARG A 143     1778   1293   4771   -222    385   -109       N  
ATOM    300  CA  ARG A 143      17.195   1.062  18.078  1.00 22.00           C  
ANISOU  300  CA  ARG A 143     1950   1335   5075     26    447   -166       C  
ATOM    301  C   ARG A 143      18.079  -0.119  18.483  1.00 21.54           C  
ANISOU  301  C   ARG A 143     1385   1876   4921   -302    111   -342       C  
ATOM    302  O   ARG A 143      18.875  -0.013  19.414  1.00 21.61           O  
ANISOU  302  O   ARG A 143     1560   2002   4650   -537    423   -309       O  
ATOM    303  CB  ARG A 143      15.835   0.977  18.775  1.00 22.03           C  
ANISOU  303  CB  ARG A 143     1574   1760   5037   -318    565   -833       C  
ATOM    304  CG  ARG A 143      15.056   2.281  18.723  1.00 26.83           C  
ANISOU  304  CG  ARG A 143     2093   2609   5493    512    312   -691       C  
ATOM    305  CD  ARG A 143      13.766   2.237  19.523  1.00 28.05           C  
ANISOU  305  CD  ARG A 143     2902   2093   5663    673    467   -646       C  
ATOM    306  NE  ARG A 143      12.755   1.368  18.925  1.00 31.24           N  
ANISOU  306  NE  ARG A 143     2260   3879   5729   -454    730   -327       N  
ATOM    307  CZ  ARG A 143      12.200   0.328  19.537  1.00 40.99           C  
ANISOU  307  CZ  ARG A 143     4469   5419   5685   1439    673   -403       C  
ATOM    308  NH1 ARG A 143      12.558   0.018  20.775  1.00 43.41           N  
ANISOU  308  NH1 ARG A 143     5452   5300   5742   1549    465   -428       N  
ATOM    309  NH2 ARG A 143      11.282  -0.396  18.910  1.00 42.76           N  
ANISOU  309  NH2 ARG A 143     4229   6396   5624   2250    947   -378       N  
ATOM    310  N   ALA A 144      17.904  -1.256  17.811  1.00 20.18           N  
ANISOU  310  N   ALA A 144     1328   1676   4662   -222    451   -124       N  
ATOM    311  CA  ALA A 144      18.742  -2.419  18.062  1.00 20.21           C  
ANISOU  311  CA  ALA A 144     1301   2127   4252   -336    586    -96       C  
ATOM    312  C   ALA A 144      20.215  -2.108  17.777  1.00 22.83           C  
ANISOU  312  C   ALA A 144     1534   2630   4512    218    224    -83       C  
ATOM    313  O   ALA A 144      21.096  -2.454  18.561  1.00 22.62           O  
ANISOU  313  O   ALA A 144     1528   2525   4543   -586    326    -92       O  
ATOM    314  CB  ALA A 144      18.277  -3.592  17.220  1.00 18.86           C  
ANISOU  314  CB  ALA A 144     1127   1664   4374   -135     49   -134       C  
ATOM    315  N   PHE A 145      20.480  -1.485  16.636  1.00 20.56           N  
ANISOU  315  N   PHE A 145     1326   2019   4466   -403   -160   -230       N  
ATOM    316  CA  PHE A 145      21.841  -1.051  16.322  1.00 19.54           C  
ANISOU  316  CA  PHE A 145     1361   2311   3752   -729    240   -252       C  
ATOM    317  C   PHE A 145      22.345  -0.042  17.330  1.00 25.53           C  
ANISOU  317  C   PHE A 145     1369   3904   4426   -742    232   -287       C  
ATOM    318  O   PHE A 145      23.519  -0.095  17.691  1.00 24.52           O  
ANISOU  318  O   PHE A 145     1517   3384   4416   -904    108   -386       O  
ATOM    319  CB  PHE A 145      21.912  -0.467  14.914  1.00 23.31           C  
ANISOU  319  CB  PHE A 145     1528   3288   4042   -976    414   -116       C  
ATOM    320  CG  PHE A 145      21.978  -1.503  13.835  1.00 21.38           C  
ANISOU  320  CG  PHE A 145     1261   2537   4324    -60    143   -247       C  
ATOM    321  CD1 PHE A 145      22.956  -2.482  13.862  1.00 20.92           C  
ANISOU  321  CD1 PHE A 145     1822   1979   4146   -800    444   -455       C  
ATOM    322  CD2 PHE A 145      21.063  -1.506  12.795  1.00 21.98           C  
ANISOU  322  CD2 PHE A 145     1397   2947   4007   -871     -5    106       C  
ATOM    323  CE1 PHE A 145      23.031  -3.442  12.875  1.00 23.66           C  
ANISOU  323  CE1 PHE A 145     1740   2964   4287   -825    335   -148       C  
ATOM    324  CE2 PHE A 145      21.134  -2.464  11.796  1.00 20.81           C  
ANISOU  324  CE2 PHE A 145     1318   2528   4060   -665     50    168       C  
ATOM    325  CZ  PHE A 145      22.132  -3.433  11.837  1.00 23.46           C  
ANISOU  325  CZ  PHE A 145     1283   3430   4201   -670    306    101       C  
ATOM    326  N   ALA A 146      21.503   0.882  17.777  1.00 22.16           N  
ANISOU  326  N   ALA A 146     1423   2643   4354   -682    212   -366       N  
ATOM    327  CA  ALA A 146      21.988   1.930  18.686  1.00 24.78           C  
ANISOU  327  CA  ALA A 146     1959   2733   4724   -936    279   -761       C  
ATOM    328  C   ALA A 146      22.425   1.358  20.025  1.00 22.72           C  
ANISOU  328  C   ALA A 146     1438   2870   4324   -638    563   -370       C  
ATOM    329  O   ALA A 146      23.290   1.913  20.709  1.00 26.05           O  
ANISOU  329  O   ALA A 146     1777   3425   4696   -818   -124  -1112       O  
ATOM    330  CB  ALA A 146      20.916   2.986  18.896  1.00 23.96           C  
ANISOU  330  CB  ALA A 146     2060   2422   4623   -513    422   -848       C  
ATOM    331  N   LEU A 147      21.797   0.252  20.404  1.00 23.10           N  
ANISOU  331  N   LEU A 147     1416   2991   4370   -370    795   -400       N  
ATOM    332  CA  LEU A 147      22.191  -0.470  21.601  1.00 24.14           C  
ANISOU  332  CA  LEU A 147     1788   2922   4461   -595    785   -568       C  
ATOM    333  C   LEU A 147      23.668  -0.873  21.548  1.00 26.18           C  
ANISOU  333  C   LEU A 147     1767   3757   4424   -323    454   -857       C  
ATOM    334  O   LEU A 147      24.396  -0.712  22.526  1.00 26.35           O  
ANISOU  334  O   LEU A 147     1605   4029   4379   -757    555  -1019       O  
ATOM    335  CB  LEU A 147      21.315  -1.704  21.772  1.00 26.66           C  
ANISOU  335  CB  LEU A 147     2941   2726   4463   -747    245   -518       C  
ATOM    336  CG  LEU A 147      21.283  -2.358  23.146  1.00 26.55           C  
ANISOU  336  CG  LEU A 147     3385   2233   4472   -603   -255   -736       C  
ATOM    337  CD1 LEU A 147      20.607  -1.452  24.157  1.00 23.96           C  
ANISOU  337  CD1 LEU A 147     1684   3043   4379    -90    -41   -815       C  
ATOM    338  CD2 LEU A 147      20.570  -3.683  23.055  1.00 26.11           C  
ANISOU  338  CD2 LEU A 147     3475   1835   4611   -837   -284   -400       C  
ATOM    339  N   TRP A 148      24.102  -1.395  20.402  1.00 24.59           N  
ANISOU  339  N   TRP A 148     1531   3552   4259   -561      7   -637       N  
ATOM    340  CA  TRP A 148      25.477  -1.866  20.249  1.00 24.36           C  
ANISOU  340  CA  TRP A 148     1514   3456   4287   -848    225   -423       C  
ATOM    341  C   TRP A 148      26.453  -0.754  19.944  1.00 26.73           C  
ANISOU  341  C   TRP A 148     1577   4169   4410      7   -195   -409       C  
ATOM    342  O   TRP A 148      27.608  -0.812  20.354  1.00 24.49           O  
ANISOU  342  O   TRP A 148     1714   3108   4483     97   -216   -491       O  
ATOM    343  CB  TRP A 148      25.562  -2.909  19.142  1.00 25.98           C  
ANISOU  343  CB  TRP A 148     1315   4308   4248    183    216   -453       C  
ATOM    344  CG  TRP A 148      24.906  -4.179  19.511  1.00 23.90           C  
ANISOU  344  CG  TRP A 148     1346   3632   4104   -839     37   -260       C  
ATOM    345  CD1 TRP A 148      23.772  -4.707  18.949  1.00 22.11           C  
ANISOU  345  CD1 TRP A 148     1458   2645   4299   -721     95   -474       C  
ATOM    346  CD2 TRP A 148      25.292  -5.083  20.553  1.00 24.64           C  
ANISOU  346  CD2 TRP A 148     1205   4088   4068    -98   -164   -678       C  
ATOM    347  NE1 TRP A 148      23.451  -5.889  19.558  1.00 24.01           N  
ANISOU  347  NE1 TRP A 148     1133   3687   4304     18     32   -434       N  
ATOM    348  CE2 TRP A 148      24.366  -6.148  20.544  1.00 24.55           C  
ANISOU  348  CE2 TRP A 148     1240   3911   4177   -202   -106   -804       C  
ATOM    349  CE3 TRP A 148      26.350  -5.113  21.474  1.00 24.69           C  
ANISOU  349  CE3 TRP A 148     1174   4006   4200    187     -4   -531       C  
ATOM    350  CZ2 TRP A 148      24.450  -7.217  21.434  1.00 26.43           C  
ANISOU  350  CZ2 TRP A 148     1405   4386   4249    510   -106   -907       C  
ATOM    351  CZ3 TRP A 148      26.423  -6.171  22.357  1.00 26.93           C  
ANISOU  351  CZ3 TRP A 148     1478   4385   4369    681     67   -796       C  
ATOM    352  CH2 TRP A 148      25.490  -7.214  22.324  1.00 24.09           C  
ANISOU  352  CH2 TRP A 148     1190   3604   4358     20    -32   -669       C  
ATOM    353  N   SER A 149      26.010   0.255  19.207  1.00 21.23           N  
ANISOU  353  N   SER A 149     1290   2536   4242   -510    -76   -469       N  
ATOM    354  CA  SER A 149      26.937   1.335  18.884  1.00 25.56           C  
ANISOU  354  CA  SER A 149     1606   3777   4328   -940   -109   -689       C  
ATOM    355  C   SER A 149      27.294   2.151  20.120  1.00 26.25           C  
ANISOU  355  C   SER A 149     1763   3831   4381  -1096    270   -766       C  
ATOM    356  O   SER A 149      28.363   2.749  20.172  1.00 30.32           O  
ANISOU  356  O   SER A 149     2339   4625   4558  -1611    151   -838       O  
ATOM    357  CB  SER A 149      26.365   2.250  17.802  1.00 30.40           C  
ANISOU  357  CB  SER A 149     3061   3614   4875    638    -66   -142       C  
ATOM    358  OG  SER A 149      25.264   2.992  18.276  1.00 28.11           O  
ANISOU  358  OG  SER A 149     2440   3238   5003  -1192    117     86       O  
ATOM    359  N   ALA A 150      26.427   2.172  21.128  1.00 24.38           N  
ANISOU  359  N   ALA A 150     1300   3751   4214   -263    113  -1062       N  
ATOM    360  CA  ALA A 150      26.733   2.952  22.326  1.00 26.16           C  
ANISOU  360  CA  ALA A 150     1631   3801   4508   -617    152  -1188       C  
ATOM    361  C   ALA A 150      27.913   2.358  23.079  1.00 24.95           C  
ANISOU  361  C   ALA A 150     1968   3138   4375  -1116    204   -918       C  
ATOM    362  O   ALA A 150      28.641   3.067  23.772  1.00 28.69           O  
ANISOU  362  O   ALA A 150     1780   4552   4568   -923    -58   -979       O  
ATOM    363  CB  ALA A 150      25.529   3.035  23.233  1.00 24.26           C  
ANISOU  363  CB  ALA A 150     1473   3502   4244   -589    578   -990       C  
ATOM    364  N   VAL A 151      28.120   1.058  22.921  1.00 27.31           N  
ANISOU  364  N   VAL A 151     1516   4440   4419   -752    174   -791       N  
ATOM    365  CA  VAL A 151      29.130   0.364  23.709  1.00 28.91           C  
ANISOU  365  CA  VAL A 151     1793   4579   4614    603    177  -1016       C  
ATOM    366  C   VAL A 151      30.313  -0.176  22.889  1.00 29.62           C  
ANISOU  366  C   VAL A 151     1660   4809   4786    657     30   -770       C  
ATOM    367  O   VAL A 151      31.083  -0.999  23.378  1.00 31.41           O  
ANISOU  367  O   VAL A 151     1681   5572   4680    793    -33   -721       O  
ATOM    368  CB  VAL A 151      28.469  -0.785  24.495  1.00 29.99           C  
ANISOU  368  CB  VAL A 151     2172   4803   4420    404    325  -1018       C  
ATOM    369  CG1 VAL A 151      27.521  -0.220  25.546  1.00 31.43           C  
ANISOU  369  CG1 VAL A 151     2273   5341   4327   -245    614  -1097       C  
ATOM    370  CG2 VAL A 151      27.699  -1.705  23.553  1.00 26.86           C  
ANISOU  370  CG2 VAL A 151     1451   4373   4380    -48     41  -1224       C  
ATOM    371  N   THR A 152      30.452   0.289  21.650  1.00 26.53           N  
ANISOU  371  N   THR A 152     1461   3849   4770   -637    450   -457       N  
ATOM    372  CA  THR A 152      31.546  -0.131  20.769  1.00 28.28           C  
ANISOU  372  CA  THR A 152     1595   4313   4839   -861    264   -608       C  
ATOM    373  C   THR A 152      32.086   1.069  19.994  1.00 29.10           C  
ANISOU  373  C   THR A 152     1752   4289   5015   -623    318   -713       C  
ATOM    374  O   THR A 152      31.485   2.145  20.020  1.00 28.38           O  
ANISOU  374  O   THR A 152     1667   4077   5040   -473    267  -1416       O  
ATOM    375  CB  THR A 152      31.090  -1.207  19.754  1.00 32.49           C  
ANISOU  375  CB  THR A 152     1966   5481   4896   -509    263   -937       C  
ATOM    376  OG1 THR A 152      30.099  -0.651  18.886  1.00 30.73           O  
ANISOU  376  OG1 THR A 152     1563   5401   4711   -331     37  -1001       O  
ATOM    377  CG2 THR A 152      30.523  -2.416  20.450  1.00 35.00           C  
ANISOU  377  CG2 THR A 152     2013   6421   4865   1102    118   -725       C  
ATOM    378  N   PRO A 153      33.230   0.901  19.302  1.00 27.94           N  
ANISOU  378  N   PRO A 153     1677   3906   5032    326    205   -761       N  
ATOM    379  CA  PRO A 153      33.662   1.966  18.392  1.00 30.54           C  
ANISOU  379  CA  PRO A 153     1982   4516   5106    -91    358   -649       C  
ATOM    380  C   PRO A 153      32.951   1.903  17.051  1.00 27.86           C  
ANISOU  380  C   PRO A 153     1714   3930   4939   -929    421   -698       C  
ATOM    381  O   PRO A 153      33.303   2.630  16.120  1.00 31.91           O  
ANISOU  381  O   PRO A 153     2348   4658   5119  -1602    174   -754       O  
ATOM    382  CB  PRO A 153      35.156   1.691  18.202  1.00 29.99           C  
ANISOU  382  CB  PRO A 153     1360   5059   4976    158    435   -171       C  
ATOM    383  CG  PRO A 153      35.515   0.652  19.218  1.00 32.06           C  
ANISOU  383  CG  PRO A 153     2094   4974   5111    801    214   -109       C  
ATOM    384  CD  PRO A 153      34.273  -0.125  19.462  1.00 27.14           C  
ANISOU  384  CD  PRO A 153     1762   3486   5064   -553    -11   -610       C  
ATOM    385  N   LEU A 154      31.952   1.030  16.951  1.00 26.97           N  
ANISOU  385  N   LEU A 154     1350   4109   4787    -72    -21   -878       N  
ATOM    386  CA  LEU A 154      31.288   0.804  15.683  1.00 26.24           C  
ANISOU  386  CA  LEU A 154     1719   3396   4854    -92     40   -636       C  
ATOM    387  C   LEU A 154      30.181   1.804  15.432  1.00 25.65           C  
ANISOU  387  C   LEU A 154     1509   3718   4520    665     16   -960       C  
ATOM    388  O   LEU A 154      29.535   2.294  16.366  1.00 28.27           O  
ANISOU  388  O   LEU A 154     1678   4414   4651   -410     12  -1002       O  
ATOM    389  CB  LEU A 154      30.685  -0.593  15.625  1.00 25.14           C  
ANISOU  389  CB  LEU A 154     1702   2949   4901    352     78   -745       C  
ATOM    390  CG  LEU A 154      31.595  -1.789  15.904  1.00 23.52           C  
ANISOU  390  CG  LEU A 154     1167   3140   4628     10     92   -204       C  
ATOM    391  CD1 LEU A 154      30.735  -3.046  15.906  1.00 27.21           C  
ANISOU  391  CD1 LEU A 154     1273   4068   4998     10    165   -237       C  
ATOM    392  CD2 LEU A 154      32.711  -1.897  14.874  1.00 24.51           C  
ANISOU  392  CD2 LEU A 154     1280   3111   4922    221   -111   -390       C  
ATOM    393  N  ATHR A 155      29.977   2.131  14.164  0.72 25.51           N  
ANISOU  393  N  ATHR A 155     1572   3690   4429   -564    193   -758       N  
ATOM    394  N  BTHR A 155      29.941   2.081  14.158  0.28 26.30           N  
ANISOU  394  N  BTHR A 155     1576   4030   4389   -618    -18   -960       N  
ATOM    395  CA ATHR A 155      28.801   2.891  13.763  0.72 25.24           C  
ANISOU  395  CA ATHR A 155     1792   3321   4475    158    115   -688       C  
ATOM    396  CA BTHR A 155      28.807   2.899  13.763  0.28 26.91           C  
ANISOU  396  CA BTHR A 155     2023   3882   4321   -409    -31   -943       C  
ATOM    397  C  ATHR A 155      27.983   2.030  12.822  0.72 22.64           C  
ANISOU  397  C  ATHR A 155     1633   2482   4488   -756    271   -643       C  
ATOM    398  C  BTHR A 155      28.007   2.178  12.679  0.28 24.81           C  
ANISOU  398  C  BTHR A 155     2153   2897   4376  -1039    114   -782       C  
ATOM    399  O  ATHR A 155      28.513   1.108  12.196  0.72 23.82           O  
ANISOU  399  O  ATHR A 155     1469   3291   4289   -711    281   -868       O  
ATOM    400  O  BTHR A 155      28.572   1.502  11.818  0.28 27.73           O  
ANISOU  400  O  BTHR A 155     2621   3599   4317  -1297    242   -853       O  
ATOM    401  CB ATHR A 155      29.159   4.212  13.069  0.72 26.31           C  
ANISOU  401  CB ATHR A 155     2771   2699   4527   -450   -136   -590       C  
ATOM    402  CB BTHR A 155      29.253   4.278  13.268  0.28 30.11           C  
ANISOU  402  CB BTHR A 155     2678   4492   4270    177   -178  -1046       C  
ATOM    403  OG1ATHR A 155      29.944   3.944  11.899  0.72 23.73           O  
ANISOU  403  OG1ATHR A 155     1931   2716   4370   -701     28   -774       O  
ATOM    404  OG1BTHR A 155      29.943   4.960  14.323  0.28 34.23           O  
ANISOU  404  OG1BTHR A 155     3706   5049   4251    937   -225   -939       O  
ATOM    405  CG2ATHR A 155      29.940   5.127  14.013  0.72 27.23           C  
ANISOU  405  CG2ATHR A 155     2901   2869   4578  -1700   -239   -209       C  
ATOM    406  CG2BTHR A 155      28.055   5.096  12.863  0.28 27.36           C  
ANISOU  406  CG2BTHR A 155     1676   4472   4247   -763   -115  -1220       C  
ATOM    407  N   PHE A 156      26.689   2.315  12.735  1.00 23.88           N  
ANISOU  407  N   PHE A 156     1502   3160   4413   -769    -34   -643       N  
ATOM    408  CA  PHE A 156      25.803   1.567  11.843  1.00 22.35           C  
ANISOU  408  CA  PHE A 156     1577   2713   4201   -932     57     74       C  
ATOM    409  C   PHE A 156      25.015   2.494  10.936  1.00 24.98           C  
ANISOU  409  C   PHE A 156     2037   2955   4499   -866   -299    -18       C  
ATOM    410  O   PHE A 156      24.201   3.286  11.395  1.00 28.66           O  
ANISOU  410  O   PHE A 156     2873   3609   4407   -164    536   -239       O  
ATOM    411  CB  PHE A 156      24.855   0.673  12.654  1.00 22.65           C  
ANISOU  411  CB  PHE A 156     1446   3131   4029   -958    -64     78       C  
ATOM    412  CG  PHE A 156      25.575  -0.324  13.496  1.00 23.35           C  
ANISOU  412  CG  PHE A 156     1550   3006   4317   -918     13    303       C  
ATOM    413  CD1 PHE A 156      26.025  -1.515  12.947  1.00 22.66           C  
ANISOU  413  CD1 PHE A 156     1264   3294   4054   -725   -172   -113       C  
ATOM    414  CD2 PHE A 156      25.858  -0.050  14.823  1.00 24.37           C  
ANISOU  414  CD2 PHE A 156     2040   3030   4189   -545    138    232       C  
ATOM    415  CE1 PHE A 156      26.736  -2.424  13.723  1.00 23.14           C  
ANISOU  415  CE1 PHE A 156     1028   3760   4004   -164     41    142       C  
ATOM    416  CE2 PHE A 156      26.555  -0.949  15.596  1.00 21.30           C  
ANISOU  416  CE2 PHE A 156     1684   2258   4150   -849   -266   -150       C  
ATOM    417  CZ  PHE A 156      26.981  -2.151  15.046  1.00 22.94           C  
ANISOU  417  CZ  PHE A 156     1895   2584   4237   -451   -264     -3       C  
ATOM    418  N   THR A 157      25.272   2.397   9.638  1.00 26.76           N  
ANISOU  418  N   THR A 157     3001   2613   4555   -640   -608     83       N  
ATOM    419  CA  THR A 157      24.625   3.269   8.672  1.00 22.37           C  
ANISOU  419  CA  THR A 157     2556   1565   4378   -750   -523    -77       C  
ATOM    420  C   THR A 157      23.750   2.494   7.691  1.00 25.83           C  
ANISOU  420  C   THR A 157     2794   2445   4576  -1449    132    158       C  
ATOM    421  O   THR A 157      24.188   1.508   7.095  1.00 25.08           O  
ANISOU  421  O   THR A 157     2561   2339   4628   -841    287   -292       O  
ATOM    422  CB  THR A 157      25.666   4.086   7.867  1.00 25.87           C  
ANISOU  422  CB  THR A 157     3644   1850   4334  -1351     71   -151       C  
ATOM    423  OG1 THR A 157      26.571   4.771   8.753  1.00 30.58           O  
ANISOU  423  OG1 THR A 157     4506   2231   4883  -1663    -93   -142       O  
ATOM    424  CG2 THR A 157      24.958   5.090   6.974  1.00 31.19           C  
ANISOU  424  CG2 THR A 157     4142   2885   4825  -1185   -121    580       C  
ATOM    425  N   ARG A 158      22.510   2.945   7.523  1.00 22.74           N  
ANISOU  425  N   ARG A 158     2211   1900   4528   -874   -390    311       N  
ATOM    426  CA  ARG A 158      21.581   2.315   6.595  1.00 23.68           C  
ANISOU  426  CA  ARG A 158     1819   2513   4665   -256   -214   -280       C  
ATOM    427  C   ARG A 158      21.945   2.695   5.172  1.00 21.91           C  
ANISOU  427  C   ARG A 158     2598   1250   4477   -430     15   -128       C  
ATOM    428  O   ARG A 158      22.175   3.878   4.874  1.00 26.10           O  
ANISOU  428  O   ARG A 158     3549   1850   4517   -593     20    157       O  
ATOM    429  CB  ARG A 158      20.135   2.729   6.893  1.00 22.49           C  
ANISOU  429  CB  ARG A 158     1777   1961   4806    575   -532   -603       C  
ATOM    430  CG  ARG A 158      19.125   2.038   5.985  1.00 22.86           C  
ANISOU  430  CG  ARG A 158     1965   1836   4884    669      7   -176       C  
ATOM    431  CD  ARG A 158      17.699   2.351   6.349  1.00 26.01           C  
ANISOU  431  CD  ARG A 158     2027   2837   5017    824    211   -302       C  
ATOM    432  NE  ARG A 158      16.774   1.612   5.497  1.00 24.58           N  
ANISOU  432  NE  ARG A 158     1588   2713   5039   -293    387    120       N  
ATOM    433  CZ  ARG A 158      15.463   1.816   5.483  1.00 24.43           C  
ANISOU  433  CZ  ARG A 158     1993   2285   5005   -365    413    335       C  
ATOM    434  NH1 ARG A 158      14.933   2.738   6.276  0.84 26.54           N  
ANISOU  434  NH1 ARG A 158     3172   1900   5011    165    555    586       N  
ATOM    435  NH2 ARG A 158      14.686   1.107   4.678  1.00 29.51           N  
ANISOU  435  NH2 ARG A 158     3539   2686   4987   -848    309    226       N  
ATOM    436  N   VAL A 159      22.011   1.692   4.303  1.00 21.94           N  
ANISOU  436  N   VAL A 159     2227   1484   4625   -465   -180    127       N  
ATOM    437  CA  VAL A 159      22.250   1.926   2.889  1.00 22.33           C  
ANISOU  437  CA  VAL A 159     2012   1825   4646   -646   -205   -125       C  
ATOM    438  C   VAL A 159      21.197   1.206   2.058  1.00 23.26           C  
ANISOU  438  C   VAL A 159     2522   1636   4679   -471   -146   -127       C  
ATOM    439  O   VAL A 159      20.475   0.336   2.555  1.00 22.90           O  
ANISOU  439  O   VAL A 159     2361   1761   4581   -851      0    212       O  
ATOM    440  CB  VAL A 159      23.653   1.464   2.464  1.00 22.42           C  
ANISOU  440  CB  VAL A 159     2323   1612   4585   -420    -10    297       C  
ATOM    441  CG1 VAL A 159      24.712   2.368   3.077  1.00 26.75           C  
ANISOU  441  CG1 VAL A 159     2279   3254   4630   -618   -392   -306       C  
ATOM    442  CG2 VAL A 159      23.882   0.032   2.860  1.00 23.26           C  
ANISOU  442  CG2 VAL A 159     2067   2192   4578   -657    -41    226       C  
ATOM    443  N   TYR A 160      21.098   1.592   0.793  1.00 25.10           N  
ANISOU  443  N   TYR A 160     2970   2014   4552  -1266    -12      9       N  
ATOM    444  CA  TYR A 160      20.163   0.976  -0.131  1.00 26.39           C  
ANISOU  444  CA  TYR A 160     3053   2507   4467  -1616    172     99       C  
ATOM    445  C   TYR A 160      20.954   0.267  -1.220  1.00 27.79           C  
ANISOU  445  C   TYR A 160     2898   2978   4682  -1004    254    -59       C  
ATOM    446  O   TYR A 160      20.916   0.630  -2.392  1.00 28.30           O  
ANISOU  446  O   TYR A 160     3914   2116   4723  -1364    674    216       O  
ATOM    447  CB  TYR A 160      19.211   2.028  -0.702  1.00 28.37           C  
ANISOU  447  CB  TYR A 160     3209   2751   4818  -1121    236    672       C  
ATOM    448  CG  TYR A 160      18.396   2.720   0.374  1.00 26.81           C  
ANISOU  448  CG  TYR A 160     3437   2216   4536  -1527    211    290       C  
ATOM    449  CD1 TYR A 160      17.230   2.136   0.863  1.00 28.10           C  
ANISOU  449  CD1 TYR A 160     4016   1586   5074   -800    319   -424       C  
ATOM    450  CD2 TYR A 160      18.790   3.950   0.903  1.00 30.43           C  
ANISOU  450  CD2 TYR A 160     3911   2593   5061  -1545    698    529       C  
ATOM    451  CE1 TYR A 160      16.479   2.749   1.845  1.00 27.44           C  
ANISOU  451  CE1 TYR A 160     4273   1298   4853   -130    509    103       C  
ATOM    452  CE2 TYR A 160      18.038   4.569   1.893  1.00 31.39           C  
ANISOU  452  CE2 TYR A 160     4451   2412   5064   -794    963    339       C  
ATOM    453  CZ  TYR A 160      16.883   3.965   2.352  1.00 30.51           C  
ANISOU  453  CZ  TYR A 160     4619   1883   5091   -622    702     91       C  
ATOM    454  OH  TYR A 160      16.123   4.555   3.331  1.00 32.09           O  
ANISOU  454  OH  TYR A 160     4503   2546   5144    220    899     24       O  
ATOM    455  N   SER A 161      21.665  -0.772  -0.804  1.00 28.23           N  
ANISOU  455  N   SER A 161     2766   3287   4674  -1632    475   -344       N  
ATOM    456  CA  SER A 161      22.695  -1.375  -1.629  1.00 28.29           C  
ANISOU  456  CA  SER A 161     2971   3098   4681   -906    353   -799       C  
ATOM    457  C   SER A 161      22.961  -2.815  -1.202  1.00 28.58           C  
ANISOU  457  C   SER A 161     2338   3839   4683   -641    286   -754       C  
ATOM    458  O   SER A 161      23.016  -3.119  -0.010  1.00 27.34           O  
ANISOU  458  O   SER A 161     2614   3159   4614  -1223    296   -463       O  
ATOM    459  CB  SER A 161      23.980  -0.547  -1.539  1.00 28.51           C  
ANISOU  459  CB  SER A 161     3252   2817   4763   -872    434   -640       C  
ATOM    460  OG  SER A 161      25.093  -1.252  -2.053  1.00 34.07           O  
ANISOU  460  OG  SER A 161     3808   4291   4846   -658    608   -496       O  
ATOM    461  N   ARG A 162      23.145  -3.696  -2.180  1.00 24.68           N  
ANISOU  461  N   ARG A 162     1928   2670   4780   -191     91   -661       N  
ATOM    462  CA  ARG A 162      23.477  -5.088  -1.907  1.00 27.64           C  
ANISOU  462  CA  ARG A 162     2142   3521   4840   -420    189   -359       C  
ATOM    463  C   ARG A 162      24.875  -5.228  -1.321  1.00 32.59           C  
ANISOU  463  C   ARG A 162     2259   5102   5023    -63    327   -224       C  
ATOM    464  O   ARG A 162      25.256  -6.303  -0.859  1.00 41.66           O  
ANISOU  464  O   ARG A 162     5194   5591   5043   1472   -170   -145       O  
ATOM    465  CB  ARG A 162      23.371  -5.918  -3.186  1.00 24.41           C  
ANISOU  465  CB  ARG A 162     1909   2611   4753   -640      9   -303       C  
ATOM    466  CG  ARG A 162      22.019  -5.820  -3.840  1.00 26.57           C  
ANISOU  466  CG  ARG A 162     2412   3079   4605   -519    -57   -233       C  
ATOM    467  CD  ARG A 162      21.888  -6.722  -5.057  1.00 26.68           C  
ANISOU  467  CD  ARG A 162     3049   2444   4645    715     93   -258       C  
ATOM    468  NE  ARG A 162      20.681  -6.360  -5.788  1.00 23.91           N  
ANISOU  468  NE  ARG A 162     2600   1821   4663   -371     91    182       N  
ATOM    469  CZ  ARG A 162      19.465  -6.829  -5.510  1.00 24.40           C  
ANISOU  469  CZ  ARG A 162     3060   1601   4611     57    243    246       C  
ATOM    470  NH1 ARG A 162      19.290  -7.700  -4.523  1.00 27.21           N  
ANISOU  470  NH1 ARG A 162     3576   2274   4488   -695    373    198       N  
ATOM    471  NH2 ARG A 162      18.419  -6.415  -6.221  1.00 23.91           N  
ANISOU  471  NH2 ARG A 162     2846   1447   4791    212     76    485       N  
ATOM    472  N  AASP A 163      25.630  -4.132  -1.340  0.47 35.59           N  
ANISOU  472  N  AASP A 163     2588   5622   5313   -696    519    170       N  
ATOM    473  N  BASP A 163      25.642  -4.142  -1.344  0.53 34.80           N  
ANISOU  473  N  BASP A 163     2503   5751   4970   -552    372    -22       N  
ATOM    474  CA AASP A 163      27.017  -4.118  -0.885  0.47 39.86           C  
ANISOU  474  CA AASP A 163     3160   6373   5611  -1350    652    437       C  
ATOM    475  CA BASP A 163      27.022  -4.166  -0.876  0.53 39.18           C  
ANISOU  475  CA BASP A 163     2987   6906   4992   -960    405    -58       C  
ATOM    476  C  AASP A 163      27.133  -3.964   0.631  0.47 34.03           C  
ANISOU  476  C  AASP A 163     2511   5209   5211  -1812    500   -139       C  
ATOM    477  C  BASP A 163      27.129  -3.861   0.618  0.53 32.81           C  
ANISOU  477  C  BASP A 163     2509   5074   4884  -1818    445   -287       C  
ATOM    478  O  AASP A 163      28.237  -3.935   1.175  0.47 37.08           O  
ANISOU  478  O  AASP A 163     2921   5975   5194   -955    387   -681       O  
ATOM    479  O  BASP A 163      28.222  -3.631   1.136  0.53 36.90           O  
ANISOU  479  O  BASP A 163     3194   5885   4941   -962    518   -651       O  
ATOM    480  CB AASP A 163      27.781  -2.984  -1.574  0.47 44.54           C  
ANISOU  480  CB AASP A 163     3860   6944   6119  -1859    952   1305       C  
ATOM    481  CB BASP A 163      27.864  -3.173  -1.679  0.53 43.32           C  
ANISOU  481  CB BASP A 163     3347   8056   5058  -1311    330    269       C  
ATOM    482  CG AASP A 163      27.506  -2.913  -3.066  0.47 51.88           C  
ANISOU  482  CG AASP A 163     5029   8154   6530   -738    994   1852       C  
ATOM    483  CG BASP A 163      27.842  -3.463  -3.170  0.53 49.02           C  
ANISOU  483  CG BASP A 163     4136   9369   5119    471     63    245       C  
ATOM    484  OD1AASP A 163      27.170  -3.958  -3.664  0.47 53.37           O  
ANISOU  484  OD1AASP A 163     5721   7605   6951  -1827   1156   2048       O  
ATOM    485  OD1BASP A 163      28.593  -4.355  -3.616  0.53 47.36           O  
ANISOU  485  OD1BASP A 163     4396   8457   5142   1424    -17    145       O  
ATOM    486  OD2AASP A 163      27.620  -1.809  -3.641  0.47 51.16           O  
ANISOU  486  OD2AASP A 163     4875   7638   6925    -96    973   2056       O  
ATOM    487  OD2BASP A 163      27.070  -2.801  -3.896  0.53 54.96           O  
ANISOU  487  OD2BASP A 163     4509  11227   5147   1811    -64    305       O  
ATOM    488  N   ALA A 164      25.992  -3.871   1.308  1.00 30.38           N  
ANISOU  488  N   ALA A 164     1928   4655   4958  -1273    530   -268       N  
ATOM    489  CA  ALA A 164      25.968  -3.632   2.750  1.00 28.14           C  
ANISOU  489  CA  ALA A 164     1917   4012   4763  -1253    587    -27       C  
ATOM    490  C   ALA A 164      26.604  -4.780   3.521  1.00 29.43           C  
ANISOU  490  C   ALA A 164     1588   4833   4763   -462    552   -194       C  
ATOM    491  O   ALA A 164      26.534  -5.931   3.094  1.00 30.44           O  
ANISOU  491  O   ALA A 164     2586   4257   4725   -710    -60   -368       O  
ATOM    492  CB  ALA A 164      24.540  -3.412   3.225  1.00 25.67           C  
ANISOU  492  CB  ALA A 164     2285   2901   4567  -1307    563   -259       C  
ATOM    493  N   ASP A 165      27.232  -4.464   4.651  1.00 23.92           N  
ANISOU  493  N   ASP A 165     1555   3050   4485   -850    330   -321       N  
ATOM    494  CA  ASP A 165      27.847  -5.497   5.482  1.00 24.57           C  
ANISOU  494  CA  ASP A 165     1607   3254   4476   -984    226   -211       C  
ATOM    495  C   ASP A 165      26.769  -6.431   6.024  1.00 19.63           C  
ANISOU  495  C   ASP A 165     1307   1635   4514   -298    -98     27       C  
ATOM    496  O   ASP A 165      26.875  -7.657   5.931  1.00 21.70           O  
ANISOU  496  O   ASP A 165     1223   2192   4829   -111    -15    188       O  
ATOM    497  CB  ASP A 165      28.642  -4.882   6.651  1.00 25.25           C  
ANISOU  497  CB  ASP A 165     1865   3221   4510  -1193    156   -325       C  
ATOM    498  CG  ASP A 165      29.798  -4.010   6.198  1.00 26.27           C  
ANISOU  498  CG  ASP A 165     1696   3232   5053   -769    428   -835       C  
ATOM    499  OD1 ASP A 165      30.576  -4.453   5.332  1.00 27.58           O  
ANISOU  499  OD1 ASP A 165     1902   3552   5024   -959    705   -918       O  
ATOM    500  OD2 ASP A 165      29.920  -2.889   6.728  1.00 27.36           O  
ANISOU  500  OD2 ASP A 165     2159   3170   5065   -477    734   -917       O  
ATOM    501  N   ILE A 166      25.764  -5.833   6.644  1.00 22.56           N  
ANISOU  501  N   ILE A 166     1296   2632   4646   -354   -230   -363       N  
ATOM    502  CA  ILE A 166      24.692  -6.614   7.244  1.00 21.95           C  
ANISOU  502  CA  ILE A 166     1746   1898   4695   -585   -130   -321       C  
ATOM    503  C   ILE A 166      23.415  -6.501   6.404  1.00 22.74           C  
ANISOU  503  C   ILE A 166     1508   2704   4428   -746    351   -292       C  
ATOM    504  O   ILE A 166      22.708  -5.498   6.444  1.00 21.60           O  
ANISOU  504  O   ILE A 166     1360   2239   4607   -372    -24   -446       O  
ATOM    505  CB  ILE A 166      24.428  -6.165   8.696  1.00 21.64           C  
ANISOU  505  CB  ILE A 166     1422   2497   4303   -659    -37   -388       C  
ATOM    506  CG1 ILE A 166      25.696  -6.314   9.551  1.00 22.98           C  
ANISOU  506  CG1 ILE A 166     1441   2936   4354   -631   -165   -691       C  
ATOM    507  CG2 ILE A 166      23.215  -6.914   9.293  1.00 21.54           C  
ANISOU  507  CG2 ILE A 166     1192   2727   4265   -424    -93   -242       C  
ATOM    508  CD1 ILE A 166      25.542  -5.767  10.950  1.00 23.76           C  
ANISOU  508  CD1 ILE A 166     1318   3308   4403   -531    -50   -616       C  
ATOM    509  N   VAL A 167      23.122  -7.532   5.623  1.00 20.39           N  
ANISOU  509  N   VAL A 167     1113   2418   4215   -130    116   -588       N  
ATOM    510  CA  VAL A 167      21.885  -7.526   4.860  1.00 21.16           C  
ANISOU  510  CA  VAL A 167     1416   2435   4191   -650    392   -319       C  
ATOM    511  C   VAL A 167      20.818  -8.183   5.715  1.00 18.98           C  
ANISOU  511  C   VAL A 167     1350   1777   4083   -490    164   -210       C  
ATOM    512  O   VAL A 167      21.037  -9.258   6.267  1.00 22.40           O  
ANISOU  512  O   VAL A 167     1348   2625   4536   -237    646    -63       O  
ATOM    513  CB  VAL A 167      22.043  -8.253   3.505  1.00 27.70           C  
ANISOU  513  CB  VAL A 167     2292   3854   4380  -1047      2   -531       C  
ATOM    514  CG1 VAL A 167      20.695  -8.387   2.803  1.00 25.49           C  
ANISOU  514  CG1 VAL A 167     2163   3289   4234  -1494   -300   -236       C  
ATOM    515  CG2 VAL A 167      23.044  -7.509   2.626  1.00 27.25           C  
ANISOU  515  CG2 VAL A 167     1657   4452   4244  -1103    429    129       C  
ATOM    516  N   ILE A 168      19.679  -7.502   5.836  1.00 20.63           N  
ANISOU  516  N   ILE A 168     1214   2671   3954   -566    287    -85       N  
ATOM    517  CA  ILE A 168      18.551  -7.938   6.648  1.00 20.07           C  
ANISOU  517  CA  ILE A 168     1412   1713   4501   -346    177   -670       C  
ATOM    518  C   ILE A 168      17.424  -8.443   5.762  1.00 19.25           C  
ANISOU  518  C   ILE A 168     1337   2038   3941   -578    243   -329       C  
ATOM    519  O   ILE A 168      17.030  -7.768   4.817  1.00 19.74           O  
ANISOU  519  O   ILE A 168     1429   1626   4446   -397    179   -206       O  
ATOM    520  CB  ILE A 168      18.003  -6.792   7.509  1.00 19.60           C  
ANISOU  520  CB  ILE A 168     1335   1847   4264   -418    310     44       C  
ATOM    521  CG1 ILE A 168      19.032  -6.324   8.536  1.00 22.31           C  
ANISOU  521  CG1 ILE A 168     1780   2602   4096   -853     25   -205       C  
ATOM    522  CG2 ILE A 168      16.710  -7.238   8.200  1.00 20.00           C  
ANISOU  522  CG2 ILE A 168     1240   2299   4059   -389    510    -58       C  
ATOM    523  CD1 ILE A 168      18.675  -4.999   9.165  1.00 22.26           C  
ANISOU  523  CD1 ILE A 168     2647   1733   4079   -315     62   -480       C  
ATOM    524  N   GLN A 169      16.927  -9.644   6.058  1.00 20.10           N  
ANISOU  524  N   GLN A 169     1292   2202   4141   -496    333   -344       N  
ATOM    525  CA  GLN A 169      15.825 -10.266   5.320  1.00 21.52           C  
ANISOU  525  CA  GLN A 169     1792   2375   4011  -1031    103   -154       C  
ATOM    526  C   GLN A 169      14.778 -10.808   6.267  1.00 19.81           C  
ANISOU  526  C   GLN A 169     1590   1791   4143   -632    195   -277       C  
ATOM    527  O   GLN A 169      15.109 -11.293   7.347  1.00 19.74           O  
ANISOU  527  O   GLN A 169     1365   1740   4397   -398    157   -318       O  
ATOM    528  CB  GLN A 169      16.320 -11.437   4.477  1.00 21.65           C  
ANISOU  528  CB  GLN A 169     1757   1718   4750   -474    -37   -471       C  
ATOM    529  CG  GLN A 169      17.269 -11.088   3.352  1.00 25.96           C  
ANISOU  529  CG  GLN A 169     2263   3030   4569   -546    225   -235       C  
ATOM    530  CD  GLN A 169      17.792 -12.332   2.654  1.00 29.97           C  
ANISOU  530  CD  GLN A 169     3716   3144   4525   1021   -128   -671       C  
ATOM    531  OE1 GLN A 169      17.557 -13.457   3.108  1.00 31.11           O  
ANISOU  531  OE1 GLN A 169     3895   3327   4600   1135    -40   -562       O  
ATOM    532  NE2 GLN A 169      18.497 -12.141   1.545  1.00 36.90           N  
ANISOU  532  NE2 GLN A 169     6102   3378   4539   1202   -661   -764       N  
ATOM    533  N   PHE A 170      13.517 -10.704   5.850  1.00 17.91           N  
ANISOU  533  N   PHE A 170     1255   1485   4066   -326     51   -225       N  
ATOM    534  CA  PHE A 170      12.438 -11.540   6.388  1.00 17.95           C  
ANISOU  534  CA  PHE A 170     1166   1235   4420     57   -305   -540       C  
ATOM    535  C   PHE A 170      12.170 -12.684   5.415  1.00 18.21           C  
ANISOU  535  C   PHE A 170     1488   1434   3998   -438     -7   -284       C  
ATOM    536  O   PHE A 170      12.091 -12.464   4.210  1.00 23.67           O  
ANISOU  536  O   PHE A 170     2810   1609   4576   -621   -213   -397       O  
ATOM    537  CB  PHE A 170      11.175 -10.711   6.599  1.00 18.31           C  
ANISOU  537  CB  PHE A 170     1391   1145   4422   -100    214    -50       C  
ATOM    538  CG  PHE A 170      11.297  -9.689   7.685  1.00 19.50           C  
ANISOU  538  CG  PHE A 170     1597   1363   4450   -327   -117   -202       C  
ATOM    539  CD1 PHE A 170      11.776  -8.425   7.406  1.00 18.70           C  
ANISOU  539  CD1 PHE A 170     1254   1447   4406    220     10   -132       C  
ATOM    540  CD2 PHE A 170      10.921  -9.988   8.982  1.00 18.56           C  
ANISOU  540  CD2 PHE A 170     1072   1751   4229    -42   -127   -222       C  
ATOM    541  CE1 PHE A 170      11.866  -7.466   8.412  1.00 20.29           C  
ANISOU  541  CE1 PHE A 170     1320   1973   4417    222   -525   -414       C  
ATOM    542  CE2 PHE A 170      11.019  -9.075   9.987  1.00 18.04           C  
ANISOU  542  CE2 PHE A 170     1095   1432   4329    -54     92   -178       C  
ATOM    543  CZ  PHE A 170      11.480  -7.796   9.711  1.00 20.15           C  
ANISOU  543  CZ  PHE A 170     1298   1850   4507    143    -70   -591       C  
ATOM    544  N   GLY A 171      12.014 -13.906   5.928  1.00 19.53           N  
ANISOU  544  N   GLY A 171     1694   1530   4198   -538    142   -300       N  
ATOM    545  CA  GLY A 171      11.747 -15.070   5.089  1.00 22.71           C  
ANISOU  545  CA  GLY A 171     2716   1423   4488   -669    316    -83       C  
ATOM    546  C   GLY A 171      11.072 -16.188   5.845  1.00 21.32           C  
ANISOU  546  C   GLY A 171     2010   1791   4300   -783    314    102       C  
ATOM    547  O   GLY A 171      10.989 -16.156   7.060  1.00 20.60           O  
ANISOU  547  O   GLY A 171     2055   1388   4386   -489    474    -84       O  
ATOM    548  N   VAL A 172      10.590 -17.181   5.111  1.00 21.52           N  
ANISOU  548  N   VAL A 172     1380   2661   4134   -729    156   -238       N  
ATOM    549  CA  VAL A 172       9.960 -18.337   5.737  1.00 22.56           C  
ANISOU  549  CA  VAL A 172     2144   1874   4554   -832    377   -187       C  
ATOM    550  C   VAL A 172      10.634 -19.584   5.183  1.00 21.13           C  
ANISOU  550  C   VAL A 172     1882   1818   4327   -742    358   -160       C  
ATOM    551  O   VAL A 172      11.176 -19.555   4.072  1.00 20.71           O  
ANISOU  551  O   VAL A 172     1571   1591   4707   -158     18   -328       O  
ATOM    552  CB  VAL A 172       8.428 -18.384   5.501  1.00 22.97           C  
ANISOU  552  CB  VAL A 172     2073   2501   4154  -1165    307   -380       C  
ATOM    553  CG1 VAL A 172       7.773 -17.114   6.048  1.00 24.57           C  
ANISOU  553  CG1 VAL A 172     2803   2005   4526   -418    673   -570       C  
ATOM    554  CG2 VAL A 172       8.110 -18.549   4.030  1.00 23.40           C  
ANISOU  554  CG2 VAL A 172     2065   2440   4385     88    229   -380       C  
ATOM    555  N   ALA A 173      10.605 -20.669   5.961  1.00 21.17           N  
ANISOU  555  N   ALA A 173     1970   1671   4404   -698    101   -158       N  
ATOM    556  CA  ALA A 173      11.114 -21.970   5.528  1.00 22.19           C  
ANISOU  556  CA  ALA A 173     2648   1202   4582   -191    268   -269       C  
ATOM    557  C   ALA A 173      12.518 -21.879   4.925  1.00 23.84           C  
ANISOU  557  C   ALA A 173     2317   1949   4792    654     15    -42       C  
ATOM    558  O   ALA A 173      13.374 -21.168   5.456  1.00 23.86           O  
ANISOU  558  O   ALA A 173     2136   2086   4843   -172   -272   -625       O  
ATOM    559  CB  ALA A 173      10.148 -22.599   4.544  1.00 25.22           C  
ANISOU  559  CB  ALA A 173     3083   2041   4460  -1292    -80   -369       C  
ATOM    560  N   GLU A 174      12.753 -22.574   3.815  1.00 26.09           N  
ANISOU  560  N   GLU A 174     3288   1946   4679     -7    289   -403       N  
ATOM    561  CA  GLU A 174      14.055 -22.484   3.148  1.00 24.13           C  
ANISOU  561  CA  GLU A 174     2989   1447   4734   -180    275   -598       C  
ATOM    562  C   GLU A 174      14.079 -21.210   2.325  1.00 25.02           C  
ANISOU  562  C   GLU A 174     2546   2185   4773    606   -176   -729       C  
ATOM    563  O   GLU A 174      13.317 -21.079   1.366  1.00 24.32           O  
ANISOU  563  O   GLU A 174     2552   1850   4837   -670     10   -542       O  
ATOM    564  CB  GLU A 174      14.335 -23.696   2.257  1.00 27.80           C  
ANISOU  564  CB  GLU A 174     3518   2290   4756   1082    306   -341       C  
ATOM    565  CG  GLU A 174      15.537 -23.509   1.331  1.00 27.59           C  
ANISOU  565  CG  GLU A 174     3222   2376   4884   1108    127   -826       C  
ATOM    566  CD  GLU A 174      16.836 -23.208   2.075  0.81 26.62           C  
ANISOU  566  CD  GLU A 174     3451   1658   5007     54    375   -236       C  
ATOM    567  OE1 GLU A 174      17.028 -23.720   3.197  0.87 31.63           O  
ANISOU  567  OE1 GLU A 174     3746   3241   5029    124     86   -501       O  
ATOM    568  OE2 GLU A 174      17.664 -22.435   1.545  1.00 32.44           O  
ANISOU  568  OE2 GLU A 174     3262   3994   5071   -347    296   -504       O  
ATOM    569  N   HIS A 175      14.964 -20.285   2.694  1.00 24.18           N  
ANISOU  569  N   HIS A 175     1690   2687   4811   -201    -17   -764       N  
ATOM    570  CA  HIS A 175      14.919 -18.933   2.152  1.00 24.51           C  
ANISOU  570  CA  HIS A 175     2642   1903   4766   -414    -93   -107       C  
ATOM    571  C   HIS A 175      16.215 -18.553   1.449  1.00 23.35           C  
ANISOU  571  C   HIS A 175     2199   1798   4874   -502     57   -117       C  
ATOM    572  O   HIS A 175      16.548 -17.371   1.326  1.00 25.13           O  
ANISOU  572  O   HIS A 175     2385   2274   4890   -651    242   -419       O  
ATOM    573  CB  HIS A 175      14.609 -17.922   3.265  1.00 23.31           C  
ANISOU  573  CB  HIS A 175     3016   1267   4572    482    -11      9       C  
ATOM    574  CG  HIS A 175      15.501 -18.059   4.460  1.00 22.67           C  
ANISOU  574  CG  HIS A 175     2190   1970   4452    107   -468     84       C  
ATOM    575  ND1 HIS A 175      15.220 -18.919   5.498  1.00 21.52           N  
ANISOU  575  ND1 HIS A 175     2563   1227   4386    226    210    107       N  
ATOM    576  CD2 HIS A 175      16.673 -17.457   4.774  1.00 23.54           C  
ANISOU  576  CD2 HIS A 175     2229   2313   4401   -102    387     19       C  
ATOM    577  CE1 HIS A 175      16.177 -18.838   6.406  1.00 24.26           C  
ANISOU  577  CE1 HIS A 175     3073   1773   4374    713    138   -218       C  
ATOM    578  NE2 HIS A 175      17.071 -17.957   5.990  1.00 21.37           N  
ANISOU  578  NE2 HIS A 175     2624   1268   4227   -455    675   -226       N  
ATOM    579  N   GLY A 176      16.935 -19.565   0.983  1.00 26.67           N  
ANISOU  579  N   GLY A 176     2206   2996   4930    787    381   -413       N  
ATOM    580  CA  GLY A 176      18.049 -19.344   0.088  1.00 29.34           C  
ANISOU  580  CA  GLY A 176     2553   3740   4856    490    286   -505       C  
ATOM    581  C   GLY A 176      19.437 -19.542   0.661  1.00 30.09           C  
ANISOU  581  C   GLY A 176     2655   3923   4857    156    653   -125       C  
ATOM    582  O   GLY A 176      20.421 -19.358  -0.060  1.00 34.18           O  
ANISOU  582  O   GLY A 176     4162   4113   4711    545    570    109       O  
ATOM    583  N   ASP A 177      19.547 -19.911   1.935  1.00 26.46           N  
ANISOU  583  N   ASP A 177     1727   3273   5054     33    606   -706       N  
ATOM    584  CA  ASP A 177      20.887 -20.086   2.494  1.00 24.19           C  
ANISOU  584  CA  ASP A 177     1559   2972   4660    692    176   -668       C  
ATOM    585  C   ASP A 177      21.156 -21.465   3.103  1.00 30.38           C  
ANISOU  585  C   ASP A 177     2806   3576   5161   1061    138   -985       C  
ATOM    586  O   ASP A 177      22.210 -21.685   3.692  1.00 32.59           O  
ANISOU  586  O   ASP A 177     2483   4784   5114    607    303  -1267       O  
ATOM    587  CB  ASP A 177      21.192 -19.003   3.532  1.00 27.42           C  
ANISOU  587  CB  ASP A 177     1599   3734   5084    198    192   -717       C  
ATOM    588  CG  ASP A 177      20.248 -19.020   4.716  1.00 27.19           C  
ANISOU  588  CG  ASP A 177     2053   3292   4987    469    349   -450       C  
ATOM    589  OD1 ASP A 177      19.514 -20.005   4.917  1.00 29.05           O  
ANISOU  589  OD1 ASP A 177     2357   3762   4920   1428    620   -190       O  
ATOM    590  OD2 ASP A 177      20.267 -18.026   5.465  1.00 23.85           O  
ANISOU  590  OD2 ASP A 177     1874   2258   4932    364    634   -738       O  
ATOM    591  N   GLY A 178      20.216 -22.392   2.965  1.00 29.28           N  
ANISOU  591  N   GLY A 178     3030   2896   5200    999    529   -593       N  
ATOM    592  CA  GLY A 178      20.456 -23.748   3.425  1.00 30.76           C  
ANISOU  592  CA  GLY A 178     3425   3004   5257   1545    635   -256       C  
ATOM    593  C   GLY A 178      20.283 -23.937   4.921  1.00 31.97           C  
ANISOU  593  C   GLY A 178     3904   2854   5388   1278    395   -124       C  
ATOM    594  O   GLY A 178      20.581 -25.001   5.457  1.00 35.98           O  
ANISOU  594  O   GLY A 178     5565   2521   5584   1767    476   -197       O  
ATOM    595  N   TYR A 179      19.796 -22.903   5.597  1.00 27.88           N  
ANISOU  595  N   TYR A 179     2106   3104   5382    607    128   -345       N  
ATOM    596  CA  TYR A 179      19.430 -22.997   7.007  1.00 27.89           C  
ANISOU  596  CA  TYR A 179     2830   2285   5482    530   -254   -192       C  
ATOM    597  C   TYR A 179      17.967 -22.613   7.147  1.00 29.01           C  
ANISOU  597  C   TYR A 179     3115   2586   5320    947   -278   -151       C  
ATOM    598  O   TYR A 179      17.659 -21.461   7.447  1.00 24.38           O  
ANISOU  598  O   TYR A 179     2218   1716   5328    209   -122   -654       O  
ATOM    599  CB  TYR A 179      20.298 -22.080   7.870  1.00 26.91           C  
ANISOU  599  CB  TYR A 179     2733   2063   5430    942   -424     83       C  
ATOM    600  CG  TYR A 179      21.752 -22.469   7.876  1.00 28.18           C  
ANISOU  600  CG  TYR A 179     2748   2238   5721    974   -298    319       C  
ATOM    601  CD1 TYR A 179      22.231 -23.436   8.755  1.00 30.68           C  
ANISOU  601  CD1 TYR A 179     2408   3496   5755   1210   -606    407       C  
ATOM    602  CD2 TYR A 179      22.651 -21.883   6.996  1.00 29.90           C  
ANISOU  602  CD2 TYR A 179     3122   2556   5683   1260   -306    585       C  
ATOM    603  CE1 TYR A 179      23.561 -23.805   8.761  1.00 33.62           C  
ANISOU  603  CE1 TYR A 179     2575   4381   5819   1460   -787    253       C  
ATOM    604  CE2 TYR A 179      23.996 -22.252   6.995  1.00 28.88           C  
ANISOU  604  CE2 TYR A 179     3168   2171   5635   1128   -243    193       C  
ATOM    605  CZ  TYR A 179      24.439 -23.209   7.880  1.00 36.62           C  
ANISOU  605  CZ  TYR A 179     2958   4870   6086   1690   -195    247       C  
ATOM    606  OH  TYR A 179      25.768 -23.572   7.882  1.00 38.47           O  
ANISOU  606  OH  TYR A 179     2438   6171   6008    770    115    304       O  
ATOM    607  N   PRO A 180      17.058 -23.571   6.913  1.00 26.79           N  
ANISOU  607  N   PRO A 180     3390   1926   4864   1166   -221   -430       N  
ATOM    608  CA  PRO A 180      15.625 -23.258   6.845  1.00 24.85           C  
ANISOU  608  CA  PRO A 180     3026   1375   5041    395    301   -163       C  
ATOM    609  C   PRO A 180      15.005 -22.870   8.183  1.00 24.04           C  
ANISOU  609  C   PRO A 180     2182   1883   5070    -14     81   -413       C  
ATOM    610  O   PRO A 180      15.428 -23.352   9.236  1.00 24.42           O  
ANISOU  610  O   PRO A 180     2035   2221   5024    247    389   -590       O  
ATOM    611  CB  PRO A 180      15.011 -24.557   6.325  1.00 26.78           C  
ANISOU  611  CB  PRO A 180     4029   1278   4868    -77    295   -323       C  
ATOM    612  CG  PRO A 180      15.975 -25.640   6.740  1.00 28.36           C  
ANISOU  612  CG  PRO A 180     3963   1741   5073   1008    155   -480       C  
ATOM    613  CD  PRO A 180      17.338 -25.005   6.697  1.00 28.05           C  
ANISOU  613  CD  PRO A 180     3155   2242   5260    967    154   -402       C  
ATOM    614  N   PHE A 181      14.015 -21.982   8.124  1.00 24.44           N  
ANISOU  614  N   PHE A 181     2606   1810   4869    505    244     -9       N  
ATOM    615  CA  PHE A 181      13.174 -21.678   9.276  1.00 20.33           C  
ANISOU  615  CA  PHE A 181     1964   1311   4449   -382    237   -297       C  
ATOM    616  C   PHE A 181      12.094 -22.758   9.371  1.00 24.32           C  
ANISOU  616  C   PHE A 181     2906   1649   4685   -331    280   -597       C  
ATOM    617  O   PHE A 181      12.052 -23.661   8.537  1.00 25.07           O  
ANISOU  617  O   PHE A 181     2877   2033   4614   -395    441   -555       O  
ATOM    618  CB  PHE A 181      12.583 -20.261   9.160  1.00 20.88           C  
ANISOU  618  CB  PHE A 181     2375   1149   4407   -207    308   -104       C  
ATOM    619  CG  PHE A 181      13.602 -19.151   9.384  1.00 20.41           C  
ANISOU  619  CG  PHE A 181     2101   1342   4312   -458    480   -376       C  
ATOM    620  CD1 PHE A 181      14.530 -19.250  10.406  1.00 22.36           C  
ANISOU  620  CD1 PHE A 181     1996   1988   4513   -807    273   -535       C  
ATOM    621  CD2 PHE A 181      13.617 -18.019   8.578  1.00 20.73           C  
ANISOU  621  CD2 PHE A 181     1848   1625   4402   -565    616   -391       C  
ATOM    622  CE1 PHE A 181      15.470 -18.254  10.620  1.00 20.86           C  
ANISOU  622  CE1 PHE A 181     1747   1633   4548   -310    236   -388       C  
ATOM    623  CE2 PHE A 181      14.551 -17.001   8.791  1.00 22.24           C  
ANISOU  623  CE2 PHE A 181     1852   2047   4551   -686    742   -214       C  
ATOM    624  CZ  PHE A 181      15.477 -17.123   9.811  1.00 21.00           C  
ANISOU  624  CZ  PHE A 181     1881   1542   4559    217    535   -306       C  
ATOM    625  N   ASP A 182      11.236 -22.670  10.382  1.00 22.54           N  
ANISOU  625  N   ASP A 182     2434   1373   4759     62    409   -286       N  
ATOM    626  CA  ASP A 182      10.443 -23.824  10.799  1.00 25.26           C  
ANISOU  626  CA  ASP A 182     3153   1689   4756   -963    251   -205       C  
ATOM    627  C   ASP A 182       8.970 -23.526  11.088  1.00 24.84           C  
ANISOU  627  C   ASP A 182     2812   2050   4577  -1207    122   -243       C  
ATOM    628  O   ASP A 182       8.299 -24.286  11.796  1.00 26.30           O  
ANISOU  628  O   ASP A 182     2729   2056   5209   -726    378    292       O  
ATOM    629  CB  ASP A 182      11.086 -24.441  12.040  1.00 24.56           C  
ANISOU  629  CB  ASP A 182     3001   1426   4903   -433    -89      2       C  
ATOM    630  CG  ASP A 182      11.251 -23.444  13.169  1.00 27.45           C  
ANISOU  630  CG  ASP A 182     3342   2258   4829    -75      3     40       C  
ATOM    631  OD1 ASP A 182      10.903 -22.258  12.974  1.00 25.07           O  
ANISOU  631  OD1 ASP A 182     2780   1894   4850   -525    380     71       O  
ATOM    632  OD2 ASP A 182      11.730 -23.849  14.251  1.00 27.64           O  
ANISOU  632  OD2 ASP A 182     3558   2158   4784   -852    -77   -197       O  
ATOM    633  N   GLY A 183       8.447 -22.444  10.529  1.00 23.39           N  
ANISOU  633  N   GLY A 183     2195   1498   5194     40    319    -12       N  
ATOM    634  CA  GLY A 183       7.070 -22.089  10.800  1.00 23.12           C  
ANISOU  634  CA  GLY A 183     1933   1660   5192   -382    290   -144       C  
ATOM    635  C   GLY A 183       6.937 -21.357  12.122  1.00 25.64           C  
ANISOU  635  C   GLY A 183     2515   1882   5344   -355     95    108       C  
ATOM    636  O   GLY A 183       7.929 -20.888  12.674  1.00 23.32           O  
ANISOU  636  O   GLY A 183     1790   1861   5209   -493     14    379       O  
ATOM    637  N   LYS A 184       5.716 -21.261  12.636  1.00 27.45           N  
ANISOU  637  N   LYS A 184     2798   2322   5311  -1004    515    565       N  
ATOM    638  CA  LYS A 184       5.456 -20.477  13.841  1.00 32.36           C  
ANISOU  638  CA  LYS A 184     2786   4074   5436     23    527    542       C  
ATOM    639  C   LYS A 184       6.216 -21.010  15.056  1.00 28.08           C  
ANISOU  639  C   LYS A 184     1886   3490   5293   -524    598    500       C  
ATOM    640  O   LYS A 184       6.297 -22.224  15.271  1.00 28.88           O  
ANISOU  640  O   LYS A 184     2560   3074   5339   -842    597    478       O  
ATOM    641  CB  LYS A 184       3.953 -20.432  14.140  1.00 35.86           C  
ANISOU  641  CB  LYS A 184     3064   4869   5691   -620    725    715       C  
ATOM    642  CG  LYS A 184       3.529 -19.216  14.962  1.00 43.15           C  
ANISOU  642  CG  LYS A 184     3686   6707   6000  -1002    750    460       C  
ATOM    643  CD  LYS A 184       2.044 -19.235  15.295  1.00 51.48           C  
ANISOU  643  CD  LYS A 184     4919   8363   6277   -641    703    277       C  
ATOM    644  CE  LYS A 184       1.763 -20.074  16.532  1.00 59.88           C  
ANISOU  644  CE  LYS A 184     6328   9999   6425    769    603     75       C  
ATOM    645  NZ  LYS A 184       2.314 -19.447  17.768  1.00 64.56           N  
ANISOU  645  NZ  LYS A 184     7217  10698   6614   1895    762    -63       N  
ATOM    646  N   ASP A 185       6.771 -20.079  15.832  1.00 26.25           N  
ANISOU  646  N   ASP A 185     1970   2873   5129   -925    126    260       N  
ATOM    647  CA  ASP A 185       7.589 -20.367  17.006  1.00 27.53           C  
ANISOU  647  CA  ASP A 185     1693   3810   4959    195    404    184       C  
ATOM    648  C   ASP A 185       8.794 -21.244  16.653  1.00 27.35           C  
ANISOU  648  C   ASP A 185     2206   3218   4968   -884   -181    -46       C  
ATOM    649  O   ASP A 185       9.191 -21.322  15.492  1.00 25.81           O  
ANISOU  649  O   ASP A 185     2772   2094   4939    -49    386    383       O  
ATOM    650  CB  ASP A 185       6.730 -21.003  18.098  1.00 28.76           C  
ANISOU  650  CB  ASP A 185     2771   3244   4912   1117    437    211       C  
ATOM    651  CG  ASP A 185       5.550 -20.125  18.481  1.00 27.57           C  
ANISOU  651  CG  ASP A 185     3534   2046   4895  -1288    339   -119       C  
ATOM    652  OD1 ASP A 185       5.777 -18.934  18.811  1.00 29.09           O  
ANISOU  652  OD1 ASP A 185     3321   2831   4900  -1143    500    448       O  
ATOM    653  OD2 ASP A 185       4.398 -20.611  18.410  1.00 32.74           O  
ANISOU  653  OD2 ASP A 185     3811   3644   4985  -2107    457     -8       O  
ATOM    654  N   GLY A 186       9.385 -21.888  17.648  1.00 26.48           N  
ANISOU  654  N   GLY A 186     2665   2375   5023   -378    -13    306       N  
ATOM    655  CA  GLY A 186      10.658 -22.544  17.426  1.00 23.29           C  
ANISOU  655  CA  GLY A 186     2164   1608   5075    106    149    126       C  
ATOM    656  C   GLY A 186      11.722 -21.511  17.075  1.00 23.32           C  
ANISOU  656  C   GLY A 186     2068   1861   4929     94     58    -35       C  
ATOM    657  O   GLY A 186      11.868 -20.514  17.782  1.00 26.26           O  
ANISOU  657  O   GLY A 186     2760   2207   5008    780     93     85       O  
ATOM    658  N   LEU A 187      12.455 -21.739  15.985  1.00 23.55           N  
ANISOU  658  N   LEU A 187     2870   1217   4861    -19     83    -29       N  
ATOM    659  CA  LEU A 187      13.467 -20.791  15.511  1.00 22.22           C  
ANISOU  659  CA  LEU A 187     2330   1355   4756     93   -262   -278       C  
ATOM    660  C   LEU A 187      12.824 -19.457  15.219  1.00 23.50           C  
ANISOU  660  C   LEU A 187     2012   2045   4871   -119   -335   -630       C  
ATOM    661  O   LEU A 187      11.775 -19.414  14.598  1.00 23.77           O  
ANISOU  661  O   LEU A 187     2782   1680   4568   -916   -162   -172       O  
ATOM    662  CB  LEU A 187      14.145 -21.308  14.246  1.00 28.23           C  
ANISOU  662  CB  LEU A 187     4151   1995   4580    743   -223    268       C  
ATOM    663  CG  LEU A 187      14.891 -22.628  14.373  1.00 32.31           C  
ANISOU  663  CG  LEU A 187     5254   2427   4595   1673   -243    541       C  
ATOM    664  CD1 LEU A 187      15.466 -23.048  13.024  1.00 36.86           C  
ANISOU  664  CD1 LEU A 187     5981   3484   4538   1516     45    224       C  
ATOM    665  CD2 LEU A 187      15.967 -22.488  15.413  1.00 30.14           C  
ANISOU  665  CD2 LEU A 187     4163   2657   4634   1613   -432    158       C  
ATOM    666  N   LEU A 188      13.468 -18.377  15.652  1.00 21.25           N  
ANISOU  666  N   LEU A 188     1460   2037   4578   -145     83    130       N  
ATOM    667  CA  LEU A 188      12.957 -17.026  15.438  1.00 20.68           C  
ANISOU  667  CA  LEU A 188     2291   1184   4383   -265     95    253       C  
ATOM    668  C   LEU A 188      13.728 -16.266  14.373  1.00 20.17           C  
ANISOU  668  C   LEU A 188     1368   1836   4460   -402   -252    -43       C  
ATOM    669  O   LEU A 188      13.160 -15.496  13.603  1.00 20.12           O  
ANISOU  669  O   LEU A 188     1526   1686   4433   -155   -201     39       O  
ATOM    670  CB  LEU A 188      13.019 -16.224  16.736  1.00 23.23           C  
ANISOU  670  CB  LEU A 188     2207   2331   4286    464     93     53       C  
ATOM    671  CG  LEU A 188      12.328 -16.833  17.949  1.00 20.32           C  
ANISOU  671  CG  LEU A 188     1190   2310   4220    396    139    181       C  
ATOM    672  CD1 LEU A 188      12.530 -15.942  19.160  1.00 24.43           C  
ANISOU  672  CD1 LEU A 188     2414   2739   4129    249    227   -276       C  
ATOM    673  CD2 LEU A 188      10.864 -17.012  17.649  1.00 21.01           C  
ANISOU  673  CD2 LEU A 188     1532   2254   4197    757     72    159       C  
ATOM    674  N   ALA A 189      15.039 -16.468  14.358  1.00 19.03           N  
ANISOU  674  N   ALA A 189     1383   1325   4521   -219    130    -42       N  
ATOM    675  CA  ALA A 189      15.925 -15.646  13.544  1.00 20.52           C  
ANISOU  675  CA  ALA A 189     1170   2051   4576    148    -14   -145       C  
ATOM    676  C   ALA A 189      17.316 -16.222  13.623  1.00 20.16           C  
ANISOU  676  C   ALA A 189     1099   2196   4365     64    101    -20       C  
ATOM    677  O   ALA A 189      17.625 -16.966  14.554  1.00 20.88           O  
ANISOU  677  O   ALA A 189     1711   1461   4761    370    166     -7       O  
ATOM    678  CB  ALA A 189      15.935 -14.174  14.020  1.00 20.58           C  
ANISOU  678  CB  ALA A 189     1531   1768   4520    -45     39   -430       C  
ATOM    679  N   HIS A 190      18.153 -15.874  12.657  1.00 18.91           N  
ANISOU  679  N   HIS A 190     1193   1402   4591     68    267    -25       N  
ATOM    680  CA  HIS A 190      19.566 -16.211  12.769  1.00 23.50           C  
ANISOU  680  CA  HIS A 190     1534   2784   4612    643    563    -39       C  
ATOM    681  C   HIS A 190      20.425 -15.185  12.064  1.00 20.44           C  
ANISOU  681  C   HIS A 190     1645   1711   4409    538     63   -352       C  
ATOM    682  O   HIS A 190      19.948 -14.411  11.236  1.00 20.76           O  
ANISOU  682  O   HIS A 190     1255   2102   4530    306    125   -306       O  
ATOM    683  CB  HIS A 190      19.853 -17.649  12.266  1.00 26.14           C  
ANISOU  683  CB  HIS A 190     1724   3432   4777    986    271   -415       C  
ATOM    684  CG  HIS A 190      19.481 -17.925  10.836  1.00 21.84           C  
ANISOU  684  CG  HIS A 190     1513   1788   4998   -259    143   -220       C  
ATOM    685  ND1 HIS A 190      19.013 -19.158  10.436  1.00 24.48           N  
ANISOU  685  ND1 HIS A 190     2476   1770   5056    221    -22   -376       N  
ATOM    686  CD2 HIS A 190      19.576 -17.180   9.707  1.00 22.18           C  
ANISOU  686  CD2 HIS A 190     1265   2278   4883     80     99   -585       C  
ATOM    687  CE1 HIS A 190      18.797 -19.150   9.133  1.00 28.76           C  
ANISOU  687  CE1 HIS A 190     2977   2875   5075   1654    -59    -45       C  
ATOM    688  NE2 HIS A 190      19.129 -17.960   8.665  1.00 20.97           N  
ANISOU  688  NE2 HIS A 190     1435   1319   5213     40   -188    -60       N  
ATOM    689  N   ALA A 191      21.702 -15.166  12.433  1.00 22.61           N  
ANISOU  689  N   ALA A 191     1316   2701   4574    428    310   -231       N  
ATOM    690  CA  ALA A 191      22.644 -14.216  11.866  1.00 21.39           C  
ANISOU  690  CA  ALA A 191     1226   2574   4326    434    195    -74       C  
ATOM    691  C   ALA A 191      24.025 -14.838  11.737  1.00 23.28           C  
ANISOU  691  C   ALA A 191     1518   2567   4759    624     -4   -477       C  
ATOM    692  O   ALA A 191      24.457 -15.615  12.584  1.00 28.56           O  
ANISOU  692  O   ALA A 191     1988   4088   4777   1423    238   -277       O  
ATOM    693  CB  ALA A 191      22.718 -12.952  12.712  1.00 24.36           C  
ANISOU  693  CB  ALA A 191     1634   2906   4717    787     29   -625       C  
ATOM    694  N   PHE A 192      24.700 -14.469  10.664  1.00 23.36           N  
ANISOU  694  N   PHE A 192     1301   2599   4975    145    119   -564       N  
ATOM    695  CA  PHE A 192      26.025 -14.990  10.373  1.00 26.44           C  
ANISOU  695  CA  PHE A 192     1410   3832   4804    534    -29   -680       C  
ATOM    696  C   PHE A 192      27.127 -14.120  10.976  1.00 29.87           C  
ANISOU  696  C   PHE A 192     1642   4527   5179    786     80   -736       C  
ATOM    697  O   PHE A 192      26.999 -12.907  11.031  1.00 26.63           O  
ANISOU  697  O   PHE A 192     1495   3451   5171    353    297   -837       O  
ATOM    698  CB  PHE A 192      26.199 -15.101   8.864  1.00 27.06           C  
ANISOU  698  CB  PHE A 192     1435   3683   5163    194     83   -968       C  
ATOM    699  CG  PHE A 192      25.253 -16.064   8.226  1.00 25.13           C  
ANISOU  699  CG  PHE A 192     1547   2666   5336    474   -153   -617       C  
ATOM    700  CD1 PHE A 192      23.969 -15.678   7.899  1.00 28.28           C  
ANISOU  700  CD1 PHE A 192     1889   3442   5414    299   -416   -454       C  
ATOM    701  CD2 PHE A 192      25.637 -17.369   7.981  1.00 26.58           C  
ANISOU  701  CD2 PHE A 192     1985   2703   5412    193    -87   -554       C  
ATOM    702  CE1 PHE A 192      23.094 -16.568   7.322  1.00 25.01           C  
ANISOU  702  CE1 PHE A 192     2372   1753   5379    556   -843   -514       C  
ATOM    703  CE2 PHE A 192      24.762 -18.268   7.400  1.00 30.38           C  
ANISOU  703  CE2 PHE A 192     2622   3404   5515    248   -550   -467       C  
ATOM    704  CZ  PHE A 192      23.487 -17.865   7.073  1.00 28.57           C  
ANISOU  704  CZ  PHE A 192     3010   2243   5600    545   -748   -182       C  
ATOM    705  N   PRO A 193      28.236 -14.744  11.418  1.00 25.34           N  
ANISOU  705  N   PRO A 193     1368   3040   5222     80   -227   -645       N  
ATOM    706  CA  PRO A 193      29.365 -13.989  11.970  1.00 27.03           C  
ANISOU  706  CA  PRO A 193     1815   3174   5282    846    151   -633       C  
ATOM    707  C   PRO A 193      30.002 -13.107  10.893  1.00 28.18           C  
ANISOU  707  C   PRO A 193     1808   3450   5450    441    435   -746       C  
ATOM    708  O   PRO A 193      29.744 -13.328   9.713  1.00 25.60           O  
ANISOU  708  O   PRO A 193     1541   2902   5285    360    431   -617       O  
ATOM    709  CB  PRO A 193      30.320 -15.088  12.449  1.00 29.11           C  
ANISOU  709  CB  PRO A 193     1552   4409   5100    708    -96   -650       C  
ATOM    710  CG  PRO A 193      29.968 -16.276  11.638  1.00 34.50           C  
ANISOU  710  CG  PRO A 193     2498   5154   5456   1324   -317   -732       C  
ATOM    711  CD  PRO A 193      28.494 -16.195  11.414  1.00 29.52           C  
ANISOU  711  CD  PRO A 193     1442   4498   5278    214   -111   -707       C  
ATOM    712  N   PRO A 194      30.804 -12.105  11.296  1.00 28.24           N  
ANISOU  712  N   PRO A 194     2156   3230   5343    771    343   -780       N  
ATOM    713  CA  PRO A 194      31.400 -11.140  10.364  1.00 27.81           C  
ANISOU  713  CA  PRO A 194     1668   3603   5295   -581     44   -984       C  
ATOM    714  C   PRO A 194      32.192 -11.771   9.218  1.00 26.97           C  
ANISOU  714  C   PRO A 194     1470   3544   5233     77    499   -741       C  
ATOM    715  O   PRO A 194      32.734 -12.874   9.353  1.00 31.45           O  
ANISOU  715  O   PRO A 194     1569   5036   5344    633    417   -374       O  
ATOM    716  CB  PRO A 194      32.332 -10.328  11.265  1.00 27.19           C  
ANISOU  716  CB  PRO A 194     2104   2999   5227    183   -344   -922       C  
ATOM    717  CG  PRO A 194      31.681 -10.405  12.608  1.00 26.80           C  
ANISOU  717  CG  PRO A 194     2328   2581   5274    -59    229   -403       C  
ATOM    718  CD  PRO A 194      31.171 -11.807  12.691  1.00 26.47           C  
ANISOU  718  CD  PRO A 194     2118   2709   5232    940    275   -597       C  
ATOM    719  N   GLY A 195      32.252 -11.063   8.096  1.00 29.60           N  
ANISOU  719  N   GLY A 195     1828   4138   5282   -854    790   -610       N  
ATOM    720  CA  GLY A 195      32.964 -11.529   6.917  1.00 27.55           C  
ANISOU  720  CA  GLY A 195     1470   3869   5129   -251    637   -462       C  
ATOM    721  C   GLY A 195      32.220 -11.108   5.666  1.00 31.97           C  
ANISOU  721  C   GLY A 195     1773   4836   5536     62    768   -591       C  
ATOM    722  O   GLY A 195      31.215 -10.405   5.759  1.00 30.21           O  
ANISOU  722  O   GLY A 195     2273   3678   5528     28   1044   -677       O  
ATOM    723  N   PRO A 196      32.687 -11.554   4.493  1.00 31.82           N  
ANISOU  723  N   PRO A 196     2023   4569   5500   -191    745   -625       N  
ATOM    724  CA  PRO A 196      32.046 -11.148   3.235  1.00 34.16           C  
ANISOU  724  CA  PRO A 196     1867   5622   5489    312    786   -358       C  
ATOM    725  C   PRO A 196      30.786 -11.937   2.872  1.00 30.14           C  
ANISOU  725  C   PRO A 196     1740   4169   5542   -588    773   -305       C  
ATOM    726  O   PRO A 196      30.523 -13.008   3.427  1.00 31.12           O  
ANISOU  726  O   PRO A 196     1722   4530   5571    186    756   -300       O  
ATOM    727  CB  PRO A 196      33.143 -11.403   2.204  1.00 34.38           C  
ANISOU  727  CB  PRO A 196     1872   5717   5475    933    751   -313       C  
ATOM    728  CG  PRO A 196      33.900 -12.578   2.767  1.00 37.49           C  
ANISOU  728  CG  PRO A 196     2852   5819   5572   1796   1080   -396       C  
ATOM    729  CD  PRO A 196      33.886 -12.387   4.266  1.00 35.92           C  
ANISOU  729  CD  PRO A 196     2495   5698   5455   1363   1236   -456       C  
ATOM    730  N   GLY A 197      30.016 -11.398   1.931  1.00 29.67           N  
ANISOU  730  N   GLY A 197     1616   4253   5404    248    862   -188       N  
ATOM    731  CA  GLY A 197      28.823 -12.066   1.434  1.00 29.51           C  
ANISOU  731  CA  GLY A 197     1553   4387   5273    -79    791   -384       C  
ATOM    732  C   GLY A 197      27.783 -12.306   2.505  1.00 27.50           C  
ANISOU  732  C   GLY A 197     1730   3234   5485   -549    721   -983       C  
ATOM    733  O   GLY A 197      27.423 -11.396   3.232  1.00 27.41           O  
ANISOU  733  O   GLY A 197     1618   3438   5360    -54    431  -1263       O  
ATOM    734  N   ILE A 198      27.315 -13.548   2.603  1.00 27.27           N  
ANISOU  734  N   ILE A 198     1594   3769   4997   -618    570   -844       N  
ATOM    735  CA  ILE A 198      26.287 -13.933   3.571  1.00 26.04           C  
ANISOU  735  CA  ILE A 198     1947   2503   5443   -444    840   -548       C  
ATOM    736  C   ILE A 198      26.741 -13.694   5.017  1.00 24.93           C  
ANISOU  736  C   ILE A 198     1458   2725   5291    149    419   -683       C  
ATOM    737  O   ILE A 198      25.917 -13.541   5.922  1.00 26.48           O  
ANISOU  737  O   ILE A 198     1500   3113   5446   -152    358  -1017       O  
ATOM    738  CB  ILE A 198      25.891 -15.422   3.392  1.00 29.56           C  
ANISOU  738  CB  ILE A 198     3008   2911   5312   -353    767   -601       C  
ATOM    739  CG1 ILE A 198      24.567 -15.723   4.094  1.00 40.29           C  
ANISOU  739  CG1 ILE A 198     4099   6030   5181    952    880   -761       C  
ATOM    740  CG2 ILE A 198      26.990 -16.355   3.886  1.00 30.70           C  
ANISOU  740  CG2 ILE A 198     4003   2335   5326    160    490   -567       C  
ATOM    741  CD1 ILE A 198      23.483 -14.762   3.741  1.00 44.26           C  
ANISOU  741  CD1 ILE A 198     4180   7497   5139    612    436   -817       C  
ATOM    742  N   GLN A 199      28.054 -13.657   5.236  1.00 25.00           N  
ANISOU  742  N   GLN A 199     1649   2635   5214    512    129   -872       N  
ATOM    743  CA  GLN A 199      28.579 -13.370   6.564  1.00 26.15           C  
ANISOU  743  CA  GLN A 199     1368   3670   4896     42    281   -870       C  
ATOM    744  C   GLN A 199      28.108 -11.981   7.014  1.00 25.63           C  
ANISOU  744  C   GLN A 199     1373   3295   5068    -83    176   -902       C  
ATOM    745  O   GLN A 199      28.009 -11.062   6.210  1.00 27.60           O  
ANISOU  745  O   GLN A 199     1262   4398   4826    -73     95   -357       O  
ATOM    746  CB  GLN A 199      30.111 -13.482   6.566  1.00 28.07           C  
ANISOU  746  CB  GLN A 199     1483   4154   5027    159    462   -865       C  
ATOM    747  CG  GLN A 199      30.628 -14.807   6.029  1.00 32.71           C  
ANISOU  747  CG  GLN A 199     2082   4982   5363    802    819   -541       C  
ATOM    748  CD  GLN A 199      30.229 -15.995   6.886  1.00 33.48           C  
ANISOU  748  CD  GLN A 199     2618   4685   5416   1689    880   -488       C  
ATOM    749  OE1 GLN A 199      30.014 -15.865   8.092  1.00 33.38           O  
ANISOU  749  OE1 GLN A 199     1937   5256   5488    907    483   -915       O  
ATOM    750  NE2 GLN A 199      30.167 -17.172   6.270  1.00 33.78           N  
ANISOU  750  NE2 GLN A 199     3447   3999   5387   1987    688   -566       N  
ATOM    751  N   GLY A 200      27.786 -11.847   8.293  1.00 24.43           N  
ANISOU  751  N   GLY A 200     1368   2967   4948   -208    358   -821       N  
ATOM    752  CA  GLY A 200      27.179 -10.620   8.797  1.00 22.46           C  
ANISOU  752  CA  GLY A 200     1255   2608   4670     73    125   -827       C  
ATOM    753  C   GLY A 200      25.681 -10.442   8.614  1.00 24.49           C  
ANISOU  753  C   GLY A 200     1389   3151   4764   -293    477   -862       C  
ATOM    754  O   GLY A 200      25.092  -9.578   9.255  1.00 26.22           O  
ANISOU  754  O   GLY A 200     1436   3671   4857   -592    -76   -582       O  
ATOM    755  N   ASP A 201      25.053 -11.237   7.756  1.00 21.62           N  
ANISOU  755  N   ASP A 201     1284   2144   4786   -110    345   -551       N  
ATOM    756  CA  ASP A 201      23.649 -10.975   7.446  1.00 23.20           C  
ANISOU  756  CA  ASP A 201     1277   3078   4460   -517    165   -307       C  
ATOM    757  C   ASP A 201      22.733 -11.499   8.536  1.00 21.08           C  
ANISOU  757  C   ASP A 201     1236   2625   4147    485   -232   -474       C  
ATOM    758  O   ASP A 201      23.108 -12.380   9.316  1.00 23.14           O  
ANISOU  758  O   ASP A 201     1609   2918   4267    952     53   -362       O  
ATOM    759  CB  ASP A 201      23.270 -11.574   6.098  1.00 21.80           C  
ANISOU  759  CB  ASP A 201     1171   2735   4379   -236    292   -316       C  
ATOM    760  CG  ASP A 201      24.074 -10.985   4.950  1.00 23.35           C  
ANISOU  760  CG  ASP A 201     1270   3302   4299   -534    220   -476       C  
ATOM    761  OD1 ASP A 201      24.902 -10.062   5.190  1.00 22.69           O  
ANISOU  761  OD1 ASP A 201     1241   2808   4572   -245    305   -523       O  
ATOM    762  OD2 ASP A 201      23.882 -11.433   3.800  1.00 25.66           O  
ANISOU  762  OD2 ASP A 201     1456   3678   4617   -640    339   -728       O  
ATOM    763  N   ALA A 202      21.528 -10.931   8.585  1.00 21.83           N  
ANISOU  763  N   ALA A 202     1150   2606   4539     75    -85   -266       N  
ATOM    764  CA  ALA A 202      20.559 -11.257   9.631  1.00 19.24           C  
ANISOU  764  CA  ALA A 202     1026   2197   4087     71    -13    -64       C  
ATOM    765  C   ALA A 202      19.210 -11.543   9.013  1.00 17.46           C  
ANISOU  765  C   ALA A 202     1152   1103   4381      3    308     22       C  
ATOM    766  O   ALA A 202      18.695 -10.720   8.265  1.00 19.80           O  
ANISOU  766  O   ALA A 202     1427   1436   4661    141     45   -343       O  
ATOM    767  CB  ALA A 202      20.444 -10.118  10.628  1.00 21.32           C  
ANISOU  767  CB  ALA A 202     1346   2136   4619    258    360   -278       C  
ATOM    768  N   HIS A 203      18.668 -12.724   9.307  1.00 19.11           N  
ANISOU  768  N   HIS A 203     1182   1709   4369   -214    215   -228       N  
ATOM    769  CA  HIS A 203      17.392 -13.178   8.757  1.00 18.72           C  
ANISOU  769  CA  HIS A 203     1161   1631   4322   -176    115   -470       C  
ATOM    770  C   HIS A 203      16.375 -13.424   9.851  1.00 19.12           C  
ANISOU  770  C   HIS A 203     1221   1807   4238    263    243   -381       C  
ATOM    771  O   HIS A 203      16.691 -14.031  10.875  1.00 20.10           O  
ANISOU  771  O   HIS A 203     1275   1700   4660     87    426   -350       O  
ATOM    772  CB  HIS A 203      17.579 -14.463   7.958  1.00 21.40           C  
ANISOU  772  CB  HIS A 203     1573   2092   4466   -423    144   -707       C  
ATOM    773  CG  HIS A 203      18.556 -14.346   6.835  1.00 22.66           C  
ANISOU  773  CG  HIS A 203     1272   3111   4229    431    466   -317       C  
ATOM    774  ND1 HIS A 203      19.150 -15.444   6.246  1.00 23.31           N  
ANISOU  774  ND1 HIS A 203     1168   3398   4290    212    152   -532       N  
ATOM    775  CD2 HIS A 203      19.044 -13.261   6.192  1.00 22.19           C  
ANISOU  775  CD2 HIS A 203     1204   2952   4276    147    560     74       C  
ATOM    776  CE1 HIS A 203      19.959 -15.036   5.286  1.00 23.18           C  
ANISOU  776  CE1 HIS A 203     1688   2731   4389   -575    660     12       C  
ATOM    777  NE2 HIS A 203      19.920 -13.714   5.237  1.00 23.09           N  
ANISOU  777  NE2 HIS A 203     1386   3137   4250   -519    203   -257       N  
ATOM    778  N   PHE A 204      15.150 -12.946   9.627  1.00 17.93           N  
ANISOU  778  N   PHE A 204     1080   1574   4161   -127    148   -190       N  
ATOM    779  CA  PHE A 204      14.052 -13.109  10.588  1.00 16.72           C  
ANISOU  779  CA  PHE A 204     1095   1236   4022   -127    217    -16       C  
ATOM    780  C   PHE A 204      12.920 -13.968  10.044  1.00 18.15           C  
ANISOU  780  C   PHE A 204     1251   1361   4285   -163    336    218       C  
ATOM    781  O   PHE A 204      12.527 -13.817   8.895  1.00 18.08           O  
ANISOU  781  O   PHE A 204     1295   1201   4372   -133    283   -275       O  
ATOM    782  CB  PHE A 204      13.527 -11.743  11.004  1.00 17.23           C  
ANISOU  782  CB  PHE A 204     1066   1284   4197    -12    -91   -361       C  
ATOM    783  CG  PHE A 204      14.590 -10.897  11.626  1.00 17.51           C  
ANISOU  783  CG  PHE A 204     1091   1308   4255    -70   -148     77       C  
ATOM    784  CD1 PHE A 204      15.476 -10.169  10.833  1.00 18.82           C  
ANISOU  784  CD1 PHE A 204     1809   1367   3976   -546     52     90       C  
ATOM    785  CD2 PHE A 204      14.730 -10.843  12.998  1.00 18.95           C  
ANISOU  785  CD2 PHE A 204     1050   1969   4182    -60    -25     -8       C  
ATOM    786  CE1 PHE A 204      16.498  -9.408  11.411  1.00 18.18           C  
ANISOU  786  CE1 PHE A 204     1208   1438   4262   -227     47     80       C  
ATOM    787  CE2 PHE A 204      15.730 -10.086  13.574  1.00 20.30           C  
ANISOU  787  CE2 PHE A 204     1825   1755   4133    237   -236   -107       C  
ATOM    788  CZ  PHE A 204      16.602  -9.360  12.771  1.00 18.50           C  
ANISOU  788  CZ  PHE A 204     1026   2001   4000    120   -155   -173       C  
ATOM    789  N   ASP A 205      12.459 -14.903  10.864  1.00 17.31           N  
ANISOU  789  N   ASP A 205     1110   1113   4355     -6    222      9       N  
ATOM    790  CA  ASP A 205      11.418 -15.836  10.433  1.00 18.33           C  
ANISOU  790  CA  ASP A 205     1397   1267   4302   -230      0   -246       C  
ATOM    791  C   ASP A 205      10.072 -15.139  10.372  1.00 21.89           C  
ANISOU  791  C   ASP A 205     1854   1692   4770   -151    204     -5       C  
ATOM    792  O   ASP A 205       9.517 -14.775  11.405  1.00 20.45           O  
ANISOU  792  O   ASP A 205     1322   1915   4532   -183     -3   -186       O  
ATOM    793  CB  ASP A 205      11.354 -17.053  11.388  1.00 19.85           C  
ANISOU  793  CB  ASP A 205     1987   1261   4294   -382    370     23       C  
ATOM    794  CG  ASP A 205      10.444 -18.174  10.885  1.00 22.11           C  
ANISOU  794  CG  ASP A 205     2376   1303   4723   -349    282    111       C  
ATOM    795  OD1 ASP A 205       9.776 -18.024   9.849  1.00 19.96           O  
ANISOU  795  OD1 ASP A 205     1288   1362   4934    -16    158    -63       O  
ATOM    796  OD2 ASP A 205      10.403 -19.216  11.547  1.00 20.15           O  
ANISOU  796  OD2 ASP A 205     1783   1358   4516   -380    209    -13       O  
ATOM    797  N   ASP A 206       9.538 -14.954   9.171  1.00 18.63           N  
ANISOU  797  N   ASP A 206     1185   1433   4460     56    302   -325       N  
ATOM    798  CA  ASP A 206       8.287 -14.186   9.079  1.00 17.67           C  
ANISOU  798  CA  ASP A 206     1076   1734   3902   -222    300   -242       C  
ATOM    799  C   ASP A 206       7.061 -15.050   9.354  1.00 19.97           C  
ANISOU  799  C   ASP A 206     1632   1559   4397    483    148    -99       C  
ATOM    800  O   ASP A 206       5.929 -14.576   9.302  1.00 19.67           O  
ANISOU  800  O   ASP A 206     1425   1474   4576   -301   -153     95       O  
ATOM    801  CB  ASP A 206       8.160 -13.500   7.718  1.00 20.83           C  
ANISOU  801  CB  ASP A 206     1162   2223   4529     36    233   -264       C  
ATOM    802  CG  ASP A 206       7.259 -12.262   7.763  1.00 22.45           C  
ANISOU  802  CG  ASP A 206     1250   2909   4370   -522    122   -131       C  
ATOM    803  OD1 ASP A 206       6.807 -11.858   8.866  1.00 20.27           O  
ANISOU  803  OD1 ASP A 206     1318   2060   4325   -473    -13    204       O  
ATOM    804  OD2 ASP A 206       7.038 -11.663   6.691  1.00 24.38           O  
ANISOU  804  OD2 ASP A 206     2521   2485   4258     82    451   -194       O  
ATOM    805  N   ASP A 207       7.287 -16.313   9.686  1.00 19.68           N  
ANISOU  805  N   ASP A 207     1521   1558   4400   -403    251    181       N  
ATOM    806  CA  ASP A 207       6.169 -17.098  10.181  1.00 19.88           C  
ANISOU  806  CA  ASP A 207     2197   1154   4202   -325    281    -65       C  
ATOM    807  C   ASP A 207       5.914 -16.717  11.646  1.00 22.43           C  
ANISOU  807  C   ASP A 207     1771   2111   4642    345     57    112       C  
ATOM    808  O   ASP A 207       4.932 -17.134  12.235  1.00 21.19           O  
ANISOU  808  O   ASP A 207     1618   1788   4647   -481    544   -270       O  
ATOM    809  CB  ASP A 207       6.413 -18.597   9.999  1.00 21.89           C  
ANISOU  809  CB  ASP A 207     2009   2033   4274   -890    149    392       C  
ATOM    810  CG  ASP A 207       6.026 -19.078   8.606  1.00 22.08           C  
ANISOU  810  CG  ASP A 207     1313   2244   4831   -250   -352    -36       C  
ATOM    811  OD1 ASP A 207       5.129 -18.457   7.983  1.00 21.74           O  
ANISOU  811  OD1 ASP A 207     1635   1833   4793   -343   -150   -213       O  
ATOM    812  OD2 ASP A 207       6.595 -20.087   8.135  1.00 22.88           O  
ANISOU  812  OD2 ASP A 207     1896   1957   4840   -622     47   -485       O  
ATOM    813  N   GLU A 208       6.781 -15.893  12.228  1.00 22.21           N  
ANISOU  813  N   GLU A 208     2259   1648   4533    112    -68   -495       N  
ATOM    814  CA  GLU A 208       6.467 -15.275  13.511  1.00 19.62           C  
ANISOU  814  CA  GLU A 208     1555   1293   4607   -180   -175    -67       C  
ATOM    815  C   GLU A 208       5.640 -14.048  13.291  1.00 21.14           C  
ANISOU  815  C   GLU A 208     1601   2003   4427   -645   -221    -78       C  
ATOM    816  O   GLU A 208       5.711 -13.447  12.225  1.00 21.08           O  
ANISOU  816  O   GLU A 208     1327   1759   4924   -171    298     -6       O  
ATOM    817  CB  GLU A 208       7.716 -14.868  14.289  1.00 22.93           C  
ANISOU  817  CB  GLU A 208     1359   2670   4684    257   -360   -535       C  
ATOM    818  CG  GLU A 208       8.773 -15.920  14.366  1.00 21.96           C  
ANISOU  818  CG  GLU A 208     1535   1870   4938   -283   -356   -302       C  
ATOM    819  CD  GLU A 208       8.248 -17.249  14.863  1.00 22.34           C  
ANISOU  819  CD  GLU A 208     1441   1807   5239    192   -439   -202       C  
ATOM    820  OE1 GLU A 208       7.198 -17.326  15.538  1.00 23.02           O  
ANISOU  820  OE1 GLU A 208     1542   1951   5252    -82    242     -8       O  
ATOM    821  OE2 GLU A 208       8.903 -18.255  14.574  1.00 22.01           O  
ANISOU  821  OE2 GLU A 208     1560   1391   5414     13   -175     78       O  
ATOM    822  N   LEU A 209       4.862 -13.678  14.301  1.00 21.03           N  
ANISOU  822  N   LEU A 209     1306   2021   4664   -154    495    275       N  
ATOM    823  CA  LEU A 209       4.267 -12.363  14.338  1.00 20.00           C  
ANISOU  823  CA  LEU A 209     1187   2271   4143   -424     78   -176       C  
ATOM    824  C   LEU A 209       5.244 -11.401  15.016  1.00 21.45           C  
ANISOU  824  C   LEU A 209     1259   2092   4800      6    285   -319       C  
ATOM    825  O   LEU A 209       5.501 -11.517  16.215  1.00 22.08           O  
ANISOU  825  O   LEU A 209     1498   2258   4634   -337    207    -89       O  
ATOM    826  CB  LEU A 209       2.923 -12.399  15.075  1.00 20.71           C  
ANISOU  826  CB  LEU A 209     1186   2425   4258   -371    169   -301       C  
ATOM    827  CG  LEU A 209       2.235 -11.043  15.196  1.00 24.48           C  
ANISOU  827  CG  LEU A 209     1807   2894   4601    292    295   -388       C  
ATOM    828  CD1 LEU A 209       1.830 -10.516  13.825  1.00 23.48           C  
ANISOU  828  CD1 LEU A 209     1211   3229   4482    -33    289   -593       C  
ATOM    829  CD2 LEU A 209       1.038 -11.176  16.093  1.00 31.06           C  
ANISOU  829  CD2 LEU A 209     2907   4499   4395   1031    689    101       C  
ATOM    830  N   TRP A 210       5.782 -10.464  14.237  1.00 18.83           N  
ANISOU  830  N   TRP A 210     1142   1493   4519      6   -118   -298       N  
ATOM    831  CA  TRP A 210       6.686  -9.455  14.758  1.00 19.78           C  
ANISOU  831  CA  TRP A 210     1279   1720   4518    290   -147   -184       C  
ATOM    832  C   TRP A 210       5.909  -8.294  15.319  1.00 21.03           C  
ANISOU  832  C   TRP A 210     1259   2012   4718    256     29    -51       C  
ATOM    833  O   TRP A 210       4.995  -7.778  14.686  1.00 21.22           O  
ANISOU  833  O   TRP A 210     1221   2247   4594    243    -28   -395       O  
ATOM    834  CB  TRP A 210       7.652  -9.005  13.668  1.00 20.77           C  
ANISOU  834  CB  TRP A 210     1544   1758   4591     30    519     10       C  
ATOM    835  CG  TRP A 210       8.491 -10.170  13.292  1.00 17.70           C  
ANISOU  835  CG  TRP A 210     1296   1135   4297    -99    -28   -191       C  
ATOM    836  CD1 TRP A 210       8.404 -10.925  12.153  1.00 18.03           C  
ANISOU  836  CD1 TRP A 210     1176   1165   4512    -25    237   -291       C  
ATOM    837  CD2 TRP A 210       9.492 -10.788  14.108  1.00 18.63           C  
ANISOU  837  CD2 TRP A 210     1129   1718   4231   -195    182      0       C  
ATOM    838  NE1 TRP A 210       9.313 -11.959  12.202  1.00 18.87           N  
ANISOU  838  NE1 TRP A 210     1152   1725   4291   -204    190   -273       N  
ATOM    839  CE2 TRP A 210       9.990 -11.899  13.395  1.00 19.04           C  
ANISOU  839  CE2 TRP A 210     1136   1776   4322   -187    120   -129       C  
ATOM    840  CE3 TRP A 210      10.014 -10.506  15.374  1.00 19.75           C  
ANISOU  840  CE3 TRP A 210     1233   1897   4374   -325     58    157       C  
ATOM    841  CZ2 TRP A 210      10.993 -12.727  13.906  1.00 20.51           C  
ANISOU  841  CZ2 TRP A 210     1318   2157   4319   -487    217   -236       C  
ATOM    842  CZ3 TRP A 210      11.007 -11.332  15.881  1.00 18.26           C  
ANISOU  842  CZ3 TRP A 210     1376   1233   4330   -193    175   -289       C  
ATOM    843  CH2 TRP A 210      11.483 -12.431  15.150  1.00 20.13           C  
ANISOU  843  CH2 TRP A 210     1632   1650   4364   -532    314   -237       C  
ATOM    844  N   SER A 211       6.266  -7.913  16.536  1.00 21.09           N  
ANISOU  844  N   SER A 211     1159   2412   4443    141    -35   -522       N  
ATOM    845  CA  SER A 211       5.563  -6.864  17.241  1.00 23.37           C  
ANISOU  845  CA  SER A 211     1433   2930   4516    594     31   -726       C  
ATOM    846  C   SER A 211       6.531  -6.088  18.104  1.00 19.99           C  
ANISOU  846  C   SER A 211     1233   1922   4441   -238    -63   -572       C  
ATOM    847  O   SER A 211       7.769  -6.235  17.981  1.00 20.05           O  
ANISOU  847  O   SER A 211     1208   1901   4509    105   -345   -601       O  
ATOM    848  CB  SER A 211       4.459  -7.460  18.111  1.00 24.54           C  
ANISOU  848  CB  SER A 211     1780   2786   4759    849    172   -562       C  
ATOM    849  OG  SER A 211       5.023  -8.287  19.116  1.00 24.53           O  
ANISOU  849  OG  SER A 211     1687   2951   4683   -392     86   -406       O  
ATOM    850  N  ALEU A 212       6.002  -5.253  18.989  0.62 25.53           N  
ANISOU  850  N  ALEU A 212     2722   2231   4749   -446    -93   -634       N  
ATOM    851  N  BLEU A 212       5.953  -5.281  18.982  0.38 24.59           N  
ANISOU  851  N  BLEU A 212     2196   2393   4754     25    175   -596       N  
ATOM    852  CA ALEU A 212       6.850  -4.589  19.969  0.62 31.84           C  
ANISOU  852  CA ALEU A 212     4027   3342   4727    310   -130   -543       C  
ATOM    853  CA BLEU A 212       6.669  -4.529  19.995  0.38 26.91           C  
ANISOU  853  CA BLEU A 212     2531   2958   4735    806    196   -506       C  
ATOM    854  C  ALEU A 212       6.867  -5.381  21.276  0.62 35.61           C  
ANISOU  854  C  ALEU A 212     4045   4672   4814   -591    -90   -657       C  
ATOM    855  C  BLEU A 212       6.960  -5.417  21.211  0.38 31.89           C  
ANISOU  855  C  BLEU A 212     2969   4327   4821    -62     82   -648       C  
ATOM    856  O  ALEU A 212       7.281  -4.876  22.320  0.62 39.14           O  
ANISOU  856  O  ALEU A 212     4409   5674   4789  -1204   -134   -803       O  
ATOM    857  O  BLEU A 212       7.676  -5.017  22.128  0.38 33.56           O  
ANISOU  857  O  BLEU A 212     2743   5180   4829   -228    -59   -676       O  
ATOM    858  CB ALEU A 212       6.398  -3.146  20.205  0.62 37.93           C  
ANISOU  858  CB ALEU A 212     5899   3822   4690   1490   -328   -587       C  
ATOM    859  CB BLEU A 212       5.863  -3.278  20.393  0.38 27.64           C  
ANISOU  859  CB BLEU A 212     3282   2519   4700   1153    361   -556       C  
ATOM    860  CG ALEU A 212       6.865  -2.128  19.153  0.62 40.36           C  
ANISOU  860  CG ALEU A 212     6053   4669   4615    765   -197   -619       C  
ATOM    861  CG BLEU A 212       4.431  -3.287  20.966  0.38 30.26           C  
ANISOU  861  CG BLEU A 212     3413   3404   4679    191    256   -679       C  
ATOM    862  CD1ALEU A 212       8.133  -2.596  18.443  0.62 36.13           C  
ANISOU  862  CD1ALEU A 212     5209   3926   4591     94   -175   -521       C  
ATOM    863  CD1BLEU A 212       3.436  -4.226  20.266  0.38 31.86           C  
ANISOU  863  CD1BLEU A 212     3649   3777   4680    281    544   -467       C  
ATOM    864  CD2ALEU A 212       5.771  -1.810  18.147  0.62 42.25           C  
ANISOU  864  CD2ALEU A 212     6511   4969   4572    779   -233   -668       C  
ATOM    865  CD2BLEU A 212       4.446  -3.540  22.457  0.38 31.43           C  
ANISOU  865  CD2BLEU A 212     3048   4225   4669    780    235   -407       C  
ATOM    866  N   GLY A 213       6.400  -6.625  21.204  1.00 34.58           N  
ANISOU  866  N   GLY A 213     3269   4906   4962   -376     97   -629       N  
ATOM    867  CA  GLY A 213       6.656  -7.609  22.244  1.00 34.46           C  
ANISOU  867  CA  GLY A 213     1971   5778   5344   -392    517   -576       C  
ATOM    868  C   GLY A 213       5.848  -7.682  23.530  1.00 39.21           C  
ANISOU  868  C   GLY A 213     2312   6783   5802   -433    401   -827       C  
ATOM    869  O   GLY A 213       5.783  -8.748  24.149  1.00 43.63           O  
ANISOU  869  O   GLY A 213     2641   8079   5859    841     84   -700       O  
ATOM    870  N  ALYS A 214       5.235  -6.580  23.948  0.42 35.20           N  
ANISOU  870  N  ALYS A 214     1705   5938   5731   -161    461   -727       N  
ATOM    871  N  BLYS A 214       5.254  -6.564  23.940  0.58 35.80           N  
ANISOU  871  N  BLYS A 214     1767   6077   5758   -299    508   -781       N  
ATOM    872  CA ALYS A 214       4.552  -6.574  25.242  0.42 37.32           C  
ANISOU  872  CA ALYS A 214     1964   6120   6097   -615    834   -677       C  
ATOM    873  CA BLYS A 214       4.523  -6.495  25.207  0.58 38.86           C  
ANISOU  873  CA BLYS A 214     2281   6347   6137   -900    937   -752       C  
ATOM    874  C  ALYS A 214       3.290  -7.432  25.240  0.42 41.95           C  
ANISOU  874  C  ALYS A 214     2988   6826   6122    387    939   -457       C  
ATOM    875  C  BLYS A 214       3.310  -7.418  25.227  0.58 41.98           C  
ANISOU  875  C  BLYS A 214     3101   6692   6158   -529    907   -548       C  
ATOM    876  O  ALYS A 214       2.952  -8.056  26.246  0.42 45.87           O  
ANISOU  876  O  ALYS A 214     3773   7569   6088   1071   1173   -518       O  
ATOM    877  O  BLYS A 214       3.030  -8.071  26.230  0.58 39.54           O  
ANISOU  877  O  BLYS A 214     3419   5532   6072  -2306    817   -652       O  
ATOM    878  CB ALYS A 214       4.206  -5.152  25.674  0.42 39.92           C  
ANISOU  878  CB ALYS A 214     2383   6538   6247    680    720   -859       C  
ATOM    879  CB BLYS A 214       4.086  -5.057  25.488  0.58 43.60           C  
ANISOU  879  CB BLYS A 214     3638   6678   6250   1005    958   -940       C  
ATOM    880  CG ALYS A 214       3.819  -5.074  27.141  0.42 42.07           C  
ANISOU  880  CG ALYS A 214     3403   6204   6378    929    710   -989       C  
ATOM    881  CG BLYS A 214       3.243  -4.875  26.736  0.58 45.48           C  
ANISOU  881  CG BLYS A 214     4479   6437   6364   1532   1107  -1117       C  
ATOM    882  CD ALYS A 214       3.497  -3.664  27.584  0.42 44.69           C  
ANISOU  882  CD ALYS A 214     4631   5863   6487   1116    704   -902       C  
ATOM    883  CD BLYS A 214       4.025  -5.230  27.985  0.58 47.10           C  
ANISOU  883  CD BLYS A 214     4852   6581   6461   1426   1084  -1194       C  
ATOM    884  CE ALYS A 214       3.201  -3.631  29.075  0.42 48.81           C  
ANISOU  884  CE ALYS A 214     5651   6341   6554    716    644   -732       C  
ATOM    885  CE BLYS A 214       3.249  -4.857  29.233  0.58 49.45           C  
ANISOU  885  CE BLYS A 214     5363   6893   6534   1680    962  -1276       C  
ATOM    886  NZ ALYS A 214       2.169  -4.637  29.455  0.42 52.20           N  
ANISOU  886  NZ ALYS A 214     6249   6998   6584    716    671   -627       N  
ATOM    887  NZ BLYS A 214       1.922  -5.531  29.278  0.58 50.43           N  
ANISOU  887  NZ BLYS A 214     5722   6873   6567   2019    927  -1338       N  
ATOM    888  N   GLY A 215       2.595  -7.464  24.111  1.00 35.92           N  
ANISOU  888  N   GLY A 215     1740   6024   5886   -221    844   -189       N  
ATOM    889  CA  GLY A 215       1.451  -8.340  23.974  1.00 30.48           C  
ANISOU  889  CA  GLY A 215     1627   4224   5730   -296    644   -596       C  
ATOM    890  C   GLY A 215       1.820  -9.535  23.120  1.00 27.90           C  
ANISOU  890  C   GLY A 215     1534   3641   5424    308    416   -701       C  
ATOM    891  O   GLY A 215       2.837 -10.212  23.353  1.00 30.97           O  
ANISOU  891  O   GLY A 215     1723   4290   5752    533    218  -1033       O  
ATOM    892  N   VAL A 216       0.996  -9.784  22.109  1.00 29.58           N  
ANISOU  892  N   VAL A 216     1519   4298   5423   -506    202   -589       N  
ATOM    893  CA  VAL A 216       1.199 -10.906  21.210  1.00 26.56           C  
ANISOU  893  CA  VAL A 216     1477   3256   5359   -343    243   -775       C  
ATOM    894  C   VAL A 216       2.470 -10.728  20.382  1.00 24.27           C  
ANISOU  894  C   VAL A 216     2184   1724   5313   -305     78   -308       C  
ATOM    895  O   VAL A 216       2.889  -9.605  20.097  1.00 29.49           O  
ANISOU  895  O   VAL A 216     2015   3975   5215   -166    124   -119       O  
ATOM    896  CB  VAL A 216      -0.021 -11.088  20.272  1.00 29.09           C  
ANISOU  896  CB  VAL A 216     1882   3759   5413    104    -49   -578       C  
ATOM    897  CG1 VAL A 216      -0.086  -9.957  19.251  1.00 31.03           C  
ANISOU  897  CG1 VAL A 216     1399   5128   5263    399   -338    -20       C  
ATOM    898  CG2 VAL A 216       0.009 -12.452  19.591  1.00 30.35           C  
ANISOU  898  CG2 VAL A 216     2158   3982   5392   -417   -130   -880       C  
ATOM    899  N   GLY A 217       3.083 -11.851  20.026  1.00 23.31           N  
ANISOU  899  N   GLY A 217     1286   2631   4939   -167    201   -452       N  
ATOM    900  CA  GLY A 217       4.200 -11.874  19.106  1.00 23.97           C  
ANISOU  900  CA  GLY A 217     1265   3113   4729     19    339   -532       C  
ATOM    901  C   GLY A 217       5.547 -11.758  19.790  1.00 21.63           C  
ANISOU  901  C   GLY A 217     1335   2273   4609   -336    396   -708       C  
ATOM    902  O   GLY A 217       5.640 -11.787  21.020  1.00 29.03           O  
ANISOU  902  O   GLY A 217     1440   5006   4584    -43    547   -520       O  
ATOM    903  N   TYR A 218       6.594 -11.606  18.979  1.00 19.21           N  
ANISOU  903  N   TYR A 218     1219   1781   4299   -215    470   -448       N  
ATOM    904  CA  TYR A 218       7.955 -11.457  19.465  1.00 18.58           C  
ANISOU  904  CA  TYR A 218     1217   1582   4261   -257    254   -340       C  
ATOM    905  C   TYR A 218       8.412 -10.046  19.190  1.00 18.33           C  
ANISOU  905  C   TYR A 218     1231   1399   4334   -187    231   -483       C  
ATOM    906  O   TYR A 218       8.142  -9.507  18.122  1.00 21.07           O  
ANISOU  906  O   TYR A 218     1226   2188   4593    259    -18   -328       O  
ATOM    907  CB  TYR A 218       8.881 -12.455  18.791  1.00 17.97           C  
ANISOU  907  CB  TYR A 218     1200   1192   4435    -56    287   -426       C  
ATOM    908  CG  TYR A 218       8.593 -13.893  19.145  1.00 19.30           C  
ANISOU  908  CG  TYR A 218     1304   1506   4523   -212    440   -427       C  
ATOM    909  CD1 TYR A 218       9.132 -14.464  20.288  1.00 23.62           C  
ANISOU  909  CD1 TYR A 218     2176   2197   4602   -709    705   -247       C  
ATOM    910  CD2 TYR A 218       7.766 -14.677  18.343  1.00 21.34           C  
ANISOU  910  CD2 TYR A 218     2487   1137   4482     57    278    119       C  
ATOM    911  CE1 TYR A 218       8.860 -15.770  20.619  1.00 23.82           C  
ANISOU  911  CE1 TYR A 218     2173   2148   4728   -725    640     32       C  
ATOM    912  CE2 TYR A 218       7.499 -15.995  18.665  1.00 22.62           C  
ANISOU  912  CE2 TYR A 218     2328   1702   4565     71    168      2       C  
ATOM    913  CZ  TYR A 218       8.048 -16.525  19.807  1.00 22.27           C  
ANISOU  913  CZ  TYR A 218     2395   1307   4760   -112    515    204       C  
ATOM    914  OH  TYR A 218       7.804 -17.836  20.139  1.00 24.38           O  
ANISOU  914  OH  TYR A 218     2706   1533   5022   -137    124    234       O  
ATOM    915  N   SER A 219       9.117  -9.468  20.153  1.00 18.61           N  
ANISOU  915  N   SER A 219     1181   1460   4431   -148    192   -174       N  
ATOM    916  CA  SER A 219       9.688  -8.150  19.962  1.00 18.11           C  
ANISOU  916  CA  SER A 219     1232   1503   4147   -271    353   -286       C  
ATOM    917  C   SER A 219      10.767  -8.152  18.879  1.00 18.56           C  
ANISOU  917  C   SER A 219     1030   2066   3955   -137    192   -292       C  
ATOM    918  O   SER A 219      11.832  -8.784  19.027  1.00 18.50           O  
ANISOU  918  O   SER A 219     1207   1468   4353   -195    253   -258       O  
ATOM    919  CB  SER A 219      10.290  -7.628  21.258  1.00 20.73           C  
ANISOU  919  CB  SER A 219     1383   1906   4588   -376    408   -377       C  
ATOM    920  OG  SER A 219      11.089  -6.505  20.977  1.00 19.12           O  
ANISOU  920  OG  SER A 219     1191   1632   4443    168    193   -185       O  
ATOM    921  N   LEU A 220      10.491  -7.442  17.793  1.00 18.90           N  
ANISOU  921  N   LEU A 220     1091   1945   4147   -105    271    247       N  
ATOM    922  CA  LEU A 220      11.455  -7.312  16.715  1.00 17.19           C  
ANISOU  922  CA  LEU A 220     1084   1165   4282    -30     71   -187       C  
ATOM    923  C   LEU A 220      12.687  -6.578  17.213  1.00 19.10           C  
ANISOU  923  C   LEU A 220     1324   1395   4537   -202     29   -331       C  
ATOM    924  O   LEU A 220      13.795  -6.899  16.806  1.00 17.91           O  
ANISOU  924  O   LEU A 220     1098   1341   4367    -27     55   -195       O  
ATOM    925  CB  LEU A 220      10.852  -6.603  15.508  1.00 17.26           C  
ANISOU  925  CB  LEU A 220     1040   1519   4000   -111     95    265       C  
ATOM    926  CG  LEU A 220      11.764  -6.468  14.275  1.00 17.27           C  
ANISOU  926  CG  LEU A 220     1266   1096   4199    -92    249    -52       C  
ATOM    927  CD1 LEU A 220      12.195  -7.838  13.747  1.00 18.53           C  
ANISOU  927  CD1 LEU A 220     1422   1324   4296   -293     76     28       C  
ATOM    928  CD2 LEU A 220      11.075  -5.641  13.198  1.00 20.56           C  
ANISOU  928  CD2 LEU A 220     1252   2117   4443   -317    288    131       C  
ATOM    929  N   PHE A 221      12.494  -5.629  18.121  1.00 18.62           N  
ANISOU  929  N   PHE A 221     1183   1529   4363    -91   -208   -549       N  
ATOM    930  CA  PHE A 221      13.619  -4.898  18.687  1.00 18.85           C  
ANISOU  930  CA  PHE A 221     1193   1780   4187    260    -33   -598       C  
ATOM    931  C   PHE A 221      14.580  -5.845  19.434  1.00 17.74           C  
ANISOU  931  C   PHE A 221     1188   1313   4237    100     -4   -619       C  
ATOM    932  O   PHE A 221      15.797  -5.841  19.190  1.00 18.57           O  
ANISOU  932  O   PHE A 221     1068   1801   4188    106    -18   -236       O  
ATOM    933  CB  PHE A 221      13.136  -3.772  19.616  1.00 18.54           C  
ANISOU  933  CB  PHE A 221     1238   1291   4515    -70     16   -544       C  
ATOM    934  CG  PHE A 221      14.203  -3.272  20.553  1.00 17.54           C  
ANISOU  934  CG  PHE A 221     1357   1088   4219    -93    -27   -105       C  
ATOM    935  CD1 PHE A 221      15.253  -2.495  20.080  1.00 19.49           C  
ANISOU  935  CD1 PHE A 221     1706   1240   4459    270   -116      0       C  
ATOM    936  CD2 PHE A 221      14.150  -3.568  21.903  1.00 20.41           C  
ANISOU  936  CD2 PHE A 221     1626   1888   4240    658    -95   -368       C  
ATOM    937  CE1 PHE A 221      16.235  -2.037  20.943  1.00 20.27           C  
ANISOU  937  CE1 PHE A 221     1707   1517   4477   -325   -324    -87       C  
ATOM    938  CE2 PHE A 221      15.134  -3.133  22.766  1.00 21.93           C  
ANISOU  938  CE2 PHE A 221     2386   1513   4433    -62   -471   -208       C  
ATOM    939  CZ  PHE A 221      16.170  -2.355  22.288  1.00 21.44           C  
ANISOU  939  CZ  PHE A 221     2144   1630   4372   -696   -248   -275       C  
ATOM    940  N   LEU A 222      14.058  -6.657  20.347  1.00 17.76           N  
ANISOU  940  N   LEU A 222     1132   1163   4452    -17    152   -357       N  
ATOM    941  CA  LEU A 222      14.921  -7.514  21.164  1.00 17.46           C  
ANISOU  941  CA  LEU A 222     1126   1111   4397     -4    182     93       C  
ATOM    942  C   LEU A 222      15.574  -8.605  20.330  1.00 18.71           C  
ANISOU  942  C   LEU A 222     1425   1315   4367    250    402    137       C  
ATOM    943  O   LEU A 222      16.750  -8.913  20.495  1.00 19.55           O  
ANISOU  943  O   LEU A 222     1186   1737   4504    153    198    393       O  
ATOM    944  CB  LEU A 222      14.135  -8.156  22.305  1.00 18.79           C  
ANISOU  944  CB  LEU A 222     1095   1784   4262     67    232    -86       C  
ATOM    945  CG  LEU A 222      13.674  -7.216  23.422  1.00 22.96           C  
ANISOU  945  CG  LEU A 222     1803   2570   4349   -229    178   -178       C  
ATOM    946  CD1 LEU A 222      12.754  -7.938  24.399  1.00 24.10           C  
ANISOU  946  CD1 LEU A 222     2293   2557   4305   -445    211   -209       C  
ATOM    947  CD2 LEU A 222      14.872  -6.620  24.152  1.00 26.09           C  
ANISOU  947  CD2 LEU A 222     2901   2657   4354     51   -313   -364       C  
ATOM    948  N   VAL A 223      14.819  -9.203  19.424  1.00 17.60           N  
ANISOU  948  N   VAL A 223     1084   1350   4254    -70    -90     79       N  
ATOM    949  CA  VAL A 223      15.375 -10.297  18.637  1.00 17.75           C  
ANISOU  949  CA  VAL A 223     1150   1135   4458      4   -286   -118       C  
ATOM    950  C   VAL A 223      16.413  -9.727  17.693  1.00 17.44           C  
ANISOU  950  C   VAL A 223     1170   1156   4303     37    -75    372       C  
ATOM    951  O   VAL A 223      17.483 -10.306  17.547  1.00 19.50           O  
ANISOU  951  O   VAL A 223     1473   1628   4309    457   -194    -17       O  
ATOM    952  CB  VAL A 223      14.300 -11.092  17.852  1.00 19.95           C  
ANISOU  952  CB  VAL A 223     1356   1628   4595    246    291   -312       C  
ATOM    953  CG1 VAL A 223      14.961 -12.167  16.985  1.00 19.51           C  
ANISOU  953  CG1 VAL A 223     1205   1978   4228   -346    227   -183       C  
ATOM    954  CG2 VAL A 223      13.348 -11.773  18.818  1.00 18.71           C  
ANISOU  954  CG2 VAL A 223     1431   1319   4359    267    310    156       C  
ATOM    955  N   ALA A 224      16.154  -8.559  17.112  1.00 17.89           N  
ANISOU  955  N   ALA A 224     1152   1153   4494     17    256    144       N  
ATOM    956  CA  ALA A 224      17.170  -7.965  16.249  1.00 17.79           C  
ANISOU  956  CA  ALA A 224     1028   1700   4034     69   -151    122       C  
ATOM    957  C   ALA A 224      18.405  -7.576  17.048  1.00 19.52           C  
ANISOU  957  C   ALA A 224     1126   2130   4159   -103   -363   -347       C  
ATOM    958  O   ALA A 224      19.544  -7.719  16.563  1.00 19.14           O  
ANISOU  958  O   ALA A 224     1070   1948   4255     54    -42   -166       O  
ATOM    959  CB  ALA A 224      16.646  -6.764  15.520  1.00 18.85           C  
ANISOU  959  CB  ALA A 224     1129   1638   4393     93    199    124       C  
ATOM    960  N   ALA A 225      18.231  -7.121  18.280  1.00 17.55           N  
ANISOU  960  N   ALA A 225     1106   1415   4146    125   -158    247       N  
ATOM    961  CA  ALA A 225      19.411  -6.758  19.071  1.00 19.31           C  
ANISOU  961  CA  ALA A 225     1192   2031   4115    211   -551   -274       C  
ATOM    962  C   ALA A 225      20.262  -7.993  19.353  1.00 20.35           C  
ANISOU  962  C   ALA A 225     1063   2442   4227    -71    -78    -51       C  
ATOM    963  O   ALA A 225      21.493  -7.918  19.292  1.00 20.49           O  
ANISOU  963  O   ALA A 225     1093   2604   4090    206   -144   -499       O  
ATOM    964  CB  ALA A 225      19.009  -6.072  20.365  1.00 20.58           C  
ANISOU  964  CB  ALA A 225     1458   2200   4162   -363   -544   -316       C  
ATOM    965  N   HIS A 226      19.632  -9.117  19.662  1.00 19.31           N  
ANISOU  965  N   HIS A 226     1190   2106   4041    444     12    -28       N  
ATOM    966  CA  HIS A 226      20.327 -10.394  19.830  1.00 20.65           C  
ANISOU  966  CA  HIS A 226     1471   2224   4150    699    127   -166       C  
ATOM    967  C   HIS A 226      21.013 -10.796  18.532  1.00 21.34           C  
ANISOU  967  C   HIS A 226     1299   2487   4322    497     25   -457       C  
ATOM    968  O   HIS A 226      22.180 -11.196  18.547  1.00 21.83           O  
ANISOU  968  O   HIS A 226     1586   2097   4610    539    -86   -755       O  
ATOM    969  CB  HIS A 226      19.306 -11.447  20.278  1.00 20.52           C  
ANISOU  969  CB  HIS A 226     1372   2017   4408    491      5   -161       C  
ATOM    970  CG  HIS A 226      19.854 -12.837  20.381  1.00 20.77           C  
ANISOU  970  CG  HIS A 226     1611   1900   4381    610   -398   -172       C  
ATOM    971  ND1 HIS A 226      20.270 -13.384  21.576  1.00 21.91           N  
ANISOU  971  ND1 HIS A 226     1975   2086   4265    933   -339    -83       N  
ATOM    972  CD2 HIS A 226      20.028 -13.802  19.446  1.00 21.34           C  
ANISOU  972  CD2 HIS A 226     1447   2263   4398    513   -289    137       C  
ATOM    973  CE1 HIS A 226      20.694 -14.621  21.369  1.00 22.71           C  
ANISOU  973  CE1 HIS A 226     1913   2182   4534    595   -520    399       C  
ATOM    974  NE2 HIS A 226      20.556 -14.899  20.085  1.00 23.16           N  
ANISOU  974  NE2 HIS A 226     2321   2105   4374    773   -464    295       N  
ATOM    975  N   GLU A 227      20.317 -10.714  17.404  1.00 20.55           N  
ANISOU  975  N   GLU A 227     1306   2067   4434    364   -301   -636       N  
ATOM    976  CA  GLU A 227      20.887 -11.157  16.140  1.00 21.53           C  
ANISOU  976  CA  GLU A 227     1393   2071   4716    356   -194   -473       C  
ATOM    977  C   GLU A 227      22.035 -10.265  15.712  1.00 22.43           C  
ANISOU  977  C   GLU A 227     1316   2523   4683    397    110   -349       C  
ATOM    978  O   GLU A 227      23.036 -10.749  15.173  1.00 25.53           O  
ANISOU  978  O   GLU A 227     1380   3826   4493    443    141   -870       O  
ATOM    979  CB  GLU A 227      19.842 -11.194  15.024  1.00 20.58           C  
ANISOU  979  CB  GLU A 227     1565   1896   4357    599   -206   -335       C  
ATOM    980  CG  GLU A 227      18.728 -12.191  15.217  1.00 21.52           C  
ANISOU  980  CG  GLU A 227     1294   2127   4754   -204    422    -66       C  
ATOM    981  CD  GLU A 227      19.245 -13.559  15.610  1.00 23.56           C  
ANISOU  981  CD  GLU A 227     1786   2348   4819    614    634   -366       C  
ATOM    982  OE1 GLU A 227      20.236 -14.018  15.009  1.00 22.89           O  
ANISOU  982  OE1 GLU A 227     1947   1817   4932     -1    421   -398       O  
ATOM    983  OE2 GLU A 227      18.646 -14.177  16.514  1.00 22.50           O  
ANISOU  983  OE2 GLU A 227     1652   2077   4820    211    -69   -245       O  
ATOM    984  N   PHE A 228      21.909  -8.968  15.951  1.00 18.47           N  
ANISOU  984  N   PHE A 228     1091   1674   4254     83    -93   -393       N  
ATOM    985  CA  PHE A 228      22.978  -8.054  15.594  1.00 21.01           C  
ANISOU  985  CA  PHE A 228     1184   2338   4462   -221   -125   -369       C  
ATOM    986  C   PHE A 228      24.204  -8.368  16.445  1.00 23.46           C  
ANISOU  986  C   PHE A 228     1214   3108   4591    208   -289   -325       C  
ATOM    987  O   PHE A 228      25.318  -8.245  15.961  1.00 26.06           O  
ANISOU  987  O   PHE A 228     1264   4036   4602    217     15   -597       O  
ATOM    988  CB  PHE A 228      22.532  -6.595  15.740  1.00 19.51           C  
ANISOU  988  CB  PHE A 228     1312   1629   4473   -287   -198   -167       C  
ATOM    989  CG  PHE A 228      21.436  -6.193  14.761  1.00 22.06           C  
ANISOU  989  CG  PHE A 228     1249   2761   4372   -419    -48   -517       C  
ATOM    990  CD1 PHE A 228      21.152  -6.988  13.661  1.00 22.37           C  
ANISOU  990  CD1 PHE A 228     1132   3058   4310   -249     46   -340       C  
ATOM    991  CD2 PHE A 228      20.714  -5.018  14.937  1.00 19.67           C  
ANISOU  991  CD2 PHE A 228     1108   1996   4368    -24    129   -302       C  
ATOM    992  CE1 PHE A 228      20.144  -6.640  12.758  1.00 19.75           C  
ANISOU  992  CE1 PHE A 228     1614   1475   4414    -43    -28   -446       C  
ATOM    993  CE2 PHE A 228      19.723  -4.656  14.035  1.00 20.48           C  
ANISOU  993  CE2 PHE A 228     1511   2284   3984   -775    315      2       C  
ATOM    994  CZ  PHE A 228      19.434  -5.471  12.944  1.00 19.14           C  
ANISOU  994  CZ  PHE A 228     1257   1807   4209   -389    107    -24       C  
ATOM    995  N   GLY A 229      24.021  -8.831  17.678  1.00 24.69           N  
ANISOU  995  N   GLY A 229     1372   3582   4429    567   -468   -499       N  
ATOM    996  CA  GLY A 229      25.143  -9.346  18.456  1.00 24.01           C  
ANISOU  996  CA  GLY A 229     1272   3176   4673    227   -197   -692       C  
ATOM    997  C   GLY A 229      25.871 -10.496  17.771  1.00 23.73           C  
ANISOU  997  C   GLY A 229     1265   3424   4329    546    -25   -449       C  
ATOM    998  O   GLY A 229      27.106 -10.509  17.740  1.00 23.53           O  
ANISOU  998  O   GLY A 229     1332   2727   4881    302   -297   -528       O  
ATOM    999  N   HIS A 230      25.146 -11.470  17.225  1.00 26.49           N  
ANISOU  999  N   HIS A 230     1514   3928   4622    749   -260   -739       N  
ATOM   1000  CA  HIS A 230      25.782 -12.552  16.469  1.00 26.85           C  
ANISOU 1000  CA  HIS A 230     1717   3764   4721   1033    -24   -607       C  
ATOM   1001  C   HIS A 230      26.515 -11.977  15.269  1.00 24.50           C  
ANISOU 1001  C   HIS A 230     1360   3324   4625    591     24   -431       C  
ATOM   1002  O   HIS A 230      27.626 -12.418  14.943  1.00 26.29           O  
ANISOU 1002  O   HIS A 230     1644   3642   4702    848   -214   -895       O  
ATOM   1003  CB  HIS A 230      24.768 -13.584  15.973  1.00 22.88           C  
ANISOU 1003  CB  HIS A 230     1802   2295   4596    757   -670   -282       C  
ATOM   1004  CG  HIS A 230      24.204 -14.474  17.037  1.00 25.02           C  
ANISOU 1004  CG  HIS A 230     2233   2609   4665    755   -450   -342       C  
ATOM   1005  ND1 HIS A 230      24.984 -15.175  17.929  1.00 23.17           N  
ANISOU 1005  ND1 HIS A 230     1731   2396   4676    674     16    184       N  
ATOM   1006  CD2 HIS A 230      22.922 -14.806  17.320  1.00 19.95           C  
ANISOU 1006  CD2 HIS A 230     1134   1963   4484     78   -121    -69       C  
ATOM   1007  CE1 HIS A 230      24.208 -15.893  18.724  1.00 26.16           C  
ANISOU 1007  CE1 HIS A 230     1538   3699   4701    647   -398    -88       C  
ATOM   1008  NE2 HIS A 230      22.951 -15.683  18.377  1.00 23.13           N  
ANISOU 1008  NE2 HIS A 230     2191   1927   4671    845    -21   -251       N  
ATOM   1009  N   ALA A 231      25.905 -10.992  14.615  1.00 22.63           N  
ANISOU 1009  N   ALA A 231     1170   2896   4531     72     64   -477       N  
ATOM   1010  CA  ALA A 231      26.440 -10.399  13.393  1.00 24.20           C  
ANISOU 1010  CA  ALA A 231     1442   3052   4703    618    287   -314       C  
ATOM   1011  C   ALA A 231      27.726  -9.611  13.645  1.00 26.18           C  
ANISOU 1011  C   ALA A 231     1275   3921   4752    238     27   -525       C  
ATOM   1012  O   ALA A 231      28.457  -9.305  12.705  1.00 26.89           O  
ANISOU 1012  O   ALA A 231     1441   3978   4799   -471    343   -818       O  
ATOM   1013  CB  ALA A 231      25.403  -9.504  12.739  1.00 23.80           C  
ANISOU 1013  CB  ALA A 231     1459   2941   4643    290    153   -394       C  
ATOM   1014  N   LEU A 232      27.976  -9.265  14.907  1.00 23.58           N  
ANISOU 1014  N   LEU A 232     1241   3139   4579   -243    336   -443       N  
ATOM   1015  CA  LEU A 232      29.221  -8.614  15.301  1.00 25.45           C  
ANISOU 1015  CA  LEU A 232     1318   3419   4933   -159   -254   -555       C  
ATOM   1016  C   LEU A 232      30.215  -9.629  15.830  1.00 26.90           C  
ANISOU 1016  C   LEU A 232     1552   3281   5388    -18   -112   -492       C  
ATOM   1017  O   LEU A 232      31.361  -9.275  16.096  1.00 28.77           O  
ANISOU 1017  O   LEU A 232     1693   4211   5025   1035   -211   -378       O  
ATOM   1018  CB  LEU A 232      28.943  -7.535  16.354  1.00 23.34           C  
ANISOU 1018  CB  LEU A 232     1333   2750   4786    279   -162   -865       C  
ATOM   1019  CG  LEU A 232      27.932  -6.447  15.988  1.00 24.80           C  
ANISOU 1019  CG  LEU A 232     1725   2869   4831    818    -80   -724       C  
ATOM   1020  CD1 LEU A 232      27.705  -5.516  17.166  1.00 24.90           C  
ANISOU 1020  CD1 LEU A 232     1647   2932   4881     -6    209   -503       C  
ATOM   1021  CD2 LEU A 232      28.370  -5.681  14.751  1.00 23.80           C  
ANISOU 1021  CD2 LEU A 232     1813   2421   4807    -90     70   -907       C  
ATOM   1022  N   GLY A 233      29.802 -10.877  16.011  1.00 25.22           N  
ANISOU 1022  N   GLY A 233     1517   3226   4838    632   -184   -817       N  
ATOM   1023  CA  GLY A 233      30.762 -11.913  16.367  1.00 27.23           C  
ANISOU 1023  CA  GLY A 233     1860   3285   5201    339   -190   -738       C  
ATOM   1024  C   GLY A 233      30.530 -12.543  17.723  1.00 29.44           C  
ANISOU 1024  C   GLY A 233     2437   3793   4957   1510   -451   -851       C  
ATOM   1025  O   GLY A 233      31.314 -13.380  18.165  1.00 28.83           O  
ANISOU 1025  O   GLY A 233     1757   3929   5268    709   -542   -339       O  
ATOM   1026  N   LEU A 234      29.442 -12.165  18.387  1.00 27.34           N  
ANISOU 1026  N   LEU A 234     1510   3966   4912    515   -466   -848       N  
ATOM   1027  CA  LEU A 234      29.166 -12.716  19.702  1.00 29.63           C  
ANISOU 1027  CA  LEU A 234     2073   3965   5220   1072   -364  -1007       C  
ATOM   1028  C   LEU A 234      28.510 -14.090  19.613  1.00 29.59           C  
ANISOU 1028  C   LEU A 234     2368   3810   5064   1519   -488   -483       C  
ATOM   1029  O   LEU A 234      27.725 -14.370  18.703  1.00 29.85           O  
ANISOU 1029  O   LEU A 234     2122   4065   5153   1384   -475   -347       O  
ATOM   1030  CB  LEU A 234      28.283 -11.764  20.514  1.00 29.37           C  
ANISOU 1030  CB  LEU A 234     1964   4007   5188    802    -35  -1117       C  
ATOM   1031  CG  LEU A 234      28.836 -10.363  20.780  1.00 26.44           C  
ANISOU 1031  CG  LEU A 234     1387   3918   4741    417    -17   -824       C  
ATOM   1032  CD1 LEU A 234      27.881  -9.589  21.688  1.00 27.91           C  
ANISOU 1032  CD1 LEU A 234     1511   3845   5249    359    -87  -1048       C  
ATOM   1033  CD2 LEU A 234      30.250 -10.425  21.380  1.00 30.40           C  
ANISOU 1033  CD2 LEU A 234     1554   4752   5245    175   -177  -1124       C  
ATOM   1034  N  AASP A 235      28.872 -14.967  20.544  0.64 32.42           N  
ANISOU 1034  N  AASP A 235     2971   3900   5449   1924   -328   -218       N  
ATOM   1035  N  BASP A 235      28.861 -14.952  20.559  0.36 30.32           N  
ANISOU 1035  N  BASP A 235     2661   3612   5247   1661   -476   -236       N  
ATOM   1036  CA AASP A 235      28.209 -16.255  20.672  0.64 34.83           C  
ANISOU 1036  CA AASP A 235     3305   4209   5721   2161   -366    -29       C  
ATOM   1037  CA BASP A 235      28.220 -16.249  20.700  0.36 31.46           C  
ANISOU 1037  CA BASP A 235     2821   3832   5299   1800   -563     -8       C  
ATOM   1038  C  AASP A 235      27.193 -16.155  21.805  0.64 35.35           C  
ANISOU 1038  C  AASP A 235     3536   4349   5547   2184   -804     67       C  
ATOM   1039  C  BASP A 235      27.103 -16.132  21.726  0.36 32.85           C  
ANISOU 1039  C  BASP A 235     3158   3907   5415   1670   -954   -200       C  
ATOM   1040  O  AASP A 235      27.008 -15.084  22.383  0.64 38.04           O  
ANISOU 1040  O  AASP A 235     3526   5287   5640   2305   -981   -111       O  
ATOM   1041  O  BASP A 235      26.766 -15.032  22.158  0.36 35.14           O  
ANISOU 1041  O  BASP A 235     3756   4186   5408   1387  -1083   -297       O  
ATOM   1042  CB AASP A 235      29.222 -17.376  20.932  0.64 38.75           C  
ANISOU 1042  CB AASP A 235     3707   4893   6123   2477   -317   -214       C  
ATOM   1043  CB BASP A 235      29.236 -17.308  21.125  0.36 32.15           C  
ANISOU 1043  CB BASP A 235     3055   3871   5291   1973   -454    222       C  
ATOM   1044  CG AASP A 235      30.108 -17.658  19.727  0.64 40.15           C  
ANISOU 1044  CG AASP A 235     3714   5217   6322   2471   -535   -537       C  
ATOM   1045  CG BASP A 235      29.930 -16.952  22.423  0.36 31.85           C  
ANISOU 1045  CG BASP A 235     3107   3805   5189   1873   -749    255       C  
ATOM   1046  OD1AASP A 235      29.632 -17.502  18.582  0.64 45.53           O  
ANISOU 1046  OD1AASP A 235     5435   5350   6514   3165   -420   -757       O  
ATOM   1047  OD1BASP A 235      29.971 -15.750  22.766  0.36 30.00           O  
ANISOU 1047  OD1BASP A 235     2418   3943   5038   1518   -776     72       O  
ATOM   1048  OD2AASP A 235      31.283 -18.041  19.925  0.64 37.87           O  
ANISOU 1048  OD2AASP A 235     2375   5360   6653    119   -763   -953       O  
ATOM   1049  OD2BASP A 235      30.441 -17.870  23.098  0.36 34.33           O  
ANISOU 1049  OD2BASP A 235     3363   4360   5321   2059   -881    341       O  
ATOM   1050  N   HIS A 236      26.536 -17.264  22.125  1.00 35.63           N  
ANISOU 1050  N   HIS A 236     3619   4398   5521   2214   -889   -268       N  
ATOM   1051  CA  HIS A 236      25.540 -17.264  23.187  1.00 33.94           C  
ANISOU 1051  CA  HIS A 236     3626   3863   5407   2093   -803    -76       C  
ATOM   1052  C   HIS A 236      26.171 -17.193  24.571  1.00 35.50           C  
ANISOU 1052  C   HIS A 236     3883   4106   5501   2223   -948   -493       C  
ATOM   1053  O   HIS A 236      27.181 -17.839  24.848  1.00 38.59           O  
ANISOU 1053  O   HIS A 236     3651   5412   5599   2307  -1227   -495       O  
ATOM   1054  CB  HIS A 236      24.648 -18.490  23.079  1.00 34.47           C  
ANISOU 1054  CB  HIS A 236     4155   3489   5452   2178   -579    245       C  
ATOM   1055  CG  HIS A 236      23.650 -18.403  21.973  1.00 29.75           C  
ANISOU 1055  CG  HIS A 236     3465   2740   5099   1605   -735    105       C  
ATOM   1056  ND1 HIS A 236      23.172 -19.511  21.309  1.00 32.53           N  
ANISOU 1056  ND1 HIS A 236     4139   2862   5360   1858   -634    208       N  
ATOM   1057  CD2 HIS A 236      23.020 -17.336  21.429  1.00 31.83           C  
ANISOU 1057  CD2 HIS A 236     3297   3537   5260   1990   -396    329       C  
ATOM   1058  CE1 HIS A 236      22.301 -19.130  20.393  1.00 30.37           C  
ANISOU 1058  CE1 HIS A 236     3818   2676   5045   1749   -497    276       C  
ATOM   1059  NE2 HIS A 236      22.188 -17.815  20.448  1.00 30.88           N  
ANISOU 1059  NE2 HIS A 236     4295   2334   5105   1312   -911    597       N  
ATOM   1060  N   SER A 237      25.563 -16.386  25.432  1.00 37.85           N  
ANISOU 1060  N   SER A 237     4521   4300   5561   2443  -1211   -779       N  
ATOM   1061  CA  SER A 237      26.033 -16.195  26.792  1.00 40.98           C  
ANISOU 1061  CA  SER A 237     5469   4471   5631   2069  -1386   -281       C  
ATOM   1062  C   SER A 237      25.447 -17.245  27.726  1.00 42.23           C  
ANISOU 1062  C   SER A 237     5937   4411   5699   2002  -1657   -254       C  
ATOM   1063  O   SER A 237      24.443 -17.880  27.408  1.00 36.28           O  
ANISOU 1063  O   SER A 237     5285   2767   5731   1615  -1835   -685       O  
ATOM   1064  CB  SER A 237      25.666 -14.793  27.280  1.00 41.70           C  
ANISOU 1064  CB  SER A 237     5846   4419   5579   2772  -1507   -517       C  
ATOM   1065  OG  SER A 237      25.910 -14.651  28.667  1.00 46.81           O  
ANISOU 1065  OG  SER A 237     6889   5311   5585   3004  -1576   -690       O  
ATOM   1066  N  ASER A 238      26.083 -17.416  28.881  0.24 40.71           N  
ANISOU 1066  N  ASER A 238     5297   4505   5665   1585  -1585     43       N  
ATOM   1067  N  BSER A 238      26.079 -17.432  28.881  0.76 40.10           N  
ANISOU 1067  N  BSER A 238     5084   4500   5652   2051  -1790     97       N  
ATOM   1068  CA ASER A 238      25.611 -18.357  29.888  0.24 41.12           C  
ANISOU 1068  CA ASER A 238     5650   4297   5678   1420  -1390    439       C  
ATOM   1069  CA BSER A 238      25.571 -18.370  29.875  0.76 39.45           C  
ANISOU 1069  CA BSER A 238     5529   3802   5658   1784  -1457    593       C  
ATOM   1070  C  ASER A 238      24.822 -17.635  30.977  0.24 44.85           C  
ANISOU 1070  C  ASER A 238     6814   4529   5697   2104  -1287    691       C  
ATOM   1071  C  BSER A 238      24.816 -17.636  30.980  0.76 43.86           C  
ANISOU 1071  C  BSER A 238     6657   4304   5702   2041  -1278    730       C  
ATOM   1072  O  ASER A 238      24.226 -18.267  31.849  0.24 50.63           O  
ANISOU 1072  O  ASER A 238     7987   5560   5692   2691  -1308    757       O  
ATOM   1073  O  BSER A 238      24.237 -18.259  31.870  0.76 48.77           O  
ANISOU 1073  O  BSER A 238     7771   5041   5720   2710  -1298    899       O  
ATOM   1074  CB ASER A 238      26.786 -19.118  30.502  0.24 42.66           C  
ANISOU 1074  CB ASER A 238     5425   5070   5714   1629  -1194    458       C  
ATOM   1075  CB BSER A 238      26.712 -19.201  30.469  0.76 39.81           C  
ANISOU 1075  CB BSER A 238     4823   4635   5667   2625   -983    345       C  
ATOM   1076  OG ASER A 238      26.328 -20.180  31.317  0.24 44.32           O  
ANISOU 1076  OG ASER A 238     5769   5336   5736   2185  -1049    514       O  
ATOM   1077  OG BSER A 238      27.189 -20.157  29.536  0.76 37.91           O  
ANISOU 1077  OG BSER A 238     4254   4479   5672   2408   -920    429       O  
ATOM   1078  N   VAL A 239      24.827 -16.307  30.917  1.00 42.33           N  
ANISOU 1078  N   VAL A 239     6575   3784   5725   2437  -1090    632       N  
ATOM   1079  CA  VAL A 239      24.084 -15.478  31.865  1.00 43.13           C  
ANISOU 1079  CA  VAL A 239     6444   4256   5689   1735   -998    457       C  
ATOM   1080  C   VAL A 239      22.657 -15.245  31.373  1.00 41.33           C  
ANISOU 1080  C   VAL A 239     6538   3444   5720   1417   -698    475       C  
ATOM   1081  O   VAL A 239      22.449 -14.591  30.350  1.00 41.15           O  
ANISOU 1081  O   VAL A 239     6364   3614   5656   1093   -990    228       O  
ATOM   1082  CB  VAL A 239      24.772 -14.113  32.086  1.00 40.83           C  
ANISOU 1082  CB  VAL A 239     5408   4464   5642   1090  -1194    345       C  
ATOM   1083  CG1 VAL A 239      23.945 -13.238  33.021  1.00 39.62           C  
ANISOU 1083  CG1 VAL A 239     5537   3849   5668   2195  -1068    145       C  
ATOM   1084  CG2 VAL A 239      26.177 -14.304  32.631  1.00 39.84           C  
ANISOU 1084  CG2 VAL A 239     5473   4057   5607   -814  -1367    464       C  
ATOM   1085  N   PRO A 240      21.665 -15.777  32.103  1.00 46.10           N  
ANISOU 1085  N   PRO A 240     7033   4652   5830   1626   -229    612       N  
ATOM   1086  CA  PRO A 240      20.255 -15.700  31.696  1.00 43.99           C  
ANISOU 1086  CA  PRO A 240     6152   4539   6022   1444     44    540       C  
ATOM   1087  C   PRO A 240      19.696 -14.281  31.546  1.00 41.49           C  
ANISOU 1087  C   PRO A 240     5278   4050   6437   1263    370    795       C  
ATOM   1088  O   PRO A 240      18.694 -14.109  30.852  1.00 44.74           O  
ANISOU 1088  O   PRO A 240     6126   4451   6421    836    630    915       O  
ATOM   1089  CB  PRO A 240      19.524 -16.447  32.821  1.00 48.29           C  
ANISOU 1089  CB  PRO A 240     6676   5784   5887   1137     33    649       C  
ATOM   1090  CG  PRO A 240      20.489 -16.503  33.955  1.00 52.07           C  
ANISOU 1090  CG  PRO A 240     7079   6871   5832   1446    -50    538       C  
ATOM   1091  CD  PRO A 240      21.841 -16.565  33.333  1.00 49.04           C  
ANISOU 1091  CD  PRO A 240     6635   6183   5814   2132   -164    560       C  
ATOM   1092  N   GLU A 241      20.321 -13.288  32.172  1.00 42.67           N  
ANISOU 1092  N   GLU A 241     4544   4665   7002   1365    397    827       N  
ATOM   1093  CA  GLU A 241      19.838 -11.912  32.070  1.00 45.91           C  
ANISOU 1093  CA  GLU A 241     5217   4626   7600   1751    571    412       C  
ATOM   1094  C   GLU A 241      20.494 -11.164  30.915  1.00 36.79           C  
ANISOU 1094  C   GLU A 241     3967   3643   6370   2198     28    128       C  
ATOM   1095  O   GLU A 241      20.154 -10.010  30.643  1.00 40.82           O  
ANISOU 1095  O   GLU A 241     5151   3832   6526   2347    300    186       O  
ATOM   1096  CB  GLU A 241      20.079 -11.147  33.376  1.00 57.69           C  
ANISOU 1096  CB  GLU A 241     6501   6375   9043   1874   1116    846       C  
ATOM   1097  CG  GLU A 241      19.308 -11.674  34.577  1.00 67.03           C  
ANISOU 1097  CG  GLU A 241     7113   8031  10326   1631   1699   1016       C  
ATOM   1098  CD  GLU A 241      19.938 -12.912  35.182  1.00 78.90           C  
ANISOU 1098  CD  GLU A 241     8087  10032  11861   2038   2111   1291       C  
ATOM   1099  OE1 GLU A 241      21.128 -13.173  34.908  1.00 81.84           O  
ANISOU 1099  OE1 GLU A 241     8095  10514  12485   1527   2242   1167       O  
ATOM   1100  OE2 GLU A 241      19.240 -13.626  35.932  1.00 86.64           O  
ANISOU 1100  OE2 GLU A 241     9198  10671  13051   2826   2232   1667       O  
ATOM   1101  N   ALA A 242      21.442 -11.821  30.251  1.00 36.27           N  
ANISOU 1101  N   ALA A 242     3980   3788   6012   2133   -565    179       N  
ATOM   1102  CA  ALA A 242      22.156 -11.200  29.143  1.00 31.59           C  
ANISOU 1102  CA  ALA A 242     3069   3453   5482   1355   -590    279       C  
ATOM   1103  C   ALA A 242      21.361 -11.285  27.849  1.00 31.03           C  
ANISOU 1103  C   ALA A 242     3533   3194   5062   1042   -449     86       C  
ATOM   1104  O   ALA A 242      20.552 -12.196  27.655  1.00 32.41           O  
ANISOU 1104  O   ALA A 242     4955   2372   4988   1730   -366    169       O  
ATOM   1105  CB  ALA A 242      23.517 -11.837  28.961  1.00 32.43           C  
ANISOU 1105  CB  ALA A 242     3270   3778   5274   1951   -678    399       C  
ATOM   1106  N   LEU A 243      21.603 -10.328  26.965  1.00 27.07           N  
ANISOU 1106  N   LEU A 243     2533   2926   4826    804   -335   -186       N  
ATOM   1107  CA  LEU A 243      20.898 -10.272  25.698  1.00 26.85           C  
ANISOU 1107  CA  LEU A 243     2743   2770   4688   1544   -283    -94       C  
ATOM   1108  C   LEU A 243      21.257 -11.473  24.842  1.00 26.72           C  
ANISOU 1108  C   LEU A 243     2873   2421   4859   1145   -465      9       C  
ATOM   1109  O   LEU A 243      20.418 -11.992  24.106  1.00 22.67           O  
ANISOU 1109  O   LEU A 243     1725   1960   4929    365   -355    141       O  
ATOM   1110  CB  LEU A 243      21.228  -8.984  24.958  1.00 22.29           C  
ANISOU 1110  CB  LEU A 243     2310   1745   4416    868    -19    176       C  
ATOM   1111  CG  LEU A 243      20.655  -8.868  23.548  1.00 23.72           C  
ANISOU 1111  CG  LEU A 243     2127   2519   4369   1194   -206    107       C  
ATOM   1112  CD1 LEU A 243      19.134  -8.893  23.566  1.00 23.05           C  
ANISOU 1112  CD1 LEU A 243     1270   3113   4374    563   -223    -21       C  
ATOM   1113  CD2 LEU A 243      21.165  -7.598  22.899  1.00 23.64           C  
ANISOU 1113  CD2 LEU A 243     1323   3150   4508    546    -94    437       C  
ATOM   1114  N   MET A 244      22.505 -11.921  24.959  1.00 27.13           N  
ANISOU 1114  N   MET A 244     2349   3035   4925   1215   -880   -404       N  
ATOM   1115  CA  MET A 244      23.009 -13.001  24.119  1.00 30.34           C  
ANISOU 1115  CA  MET A 244     3144   3511   4872   1874   -578   -400       C  
ATOM   1116  C   MET A 244      22.710 -14.393  24.678  1.00 31.58           C  
ANISOU 1116  C   MET A 244     3601   3262   5137   1933   -620   -281       C  
ATOM   1117  O   MET A 244      23.204 -15.395  24.156  1.00 34.93           O  
ANISOU 1117  O   MET A 244     3283   4710   5280   2130   -855   -574       O  
ATOM   1118  CB  MET A 244      24.519 -12.842  23.901  1.00 27.90           C  
ANISOU 1118  CB  MET A 244     2040   3628   4932   1251   -430   -573       C  
ATOM   1119  CG  MET A 244      24.889 -11.632  23.064  1.00 29.39           C  
ANISOU 1119  CG  MET A 244     2140   3893   5132    936   -437   -367       C  
ATOM   1120  SD  MET A 244      23.824 -11.458  21.607  1.00 27.36           S  
ANISOU 1120  SD  MET A 244     1993   3428   4975   1125   -593   -572       S  
ATOM   1121  CE  MET A 244      24.197 -12.999  20.751  1.00 27.71           C  
ANISOU 1121  CE  MET A 244     2423   3142   4963   1438   -260   -392       C  
ATOM   1122  N   TYR A 245      21.906 -14.464  25.733  1.00 33.56           N  
ANISOU 1122  N   TYR A 245     3963   2928   5860   1567   -817   -146       N  
ATOM   1123  CA  TYR A 245      21.402 -15.742  26.232  1.00 37.44           C  
ANISOU 1123  CA  TYR A 245     4325   3758   6142   2284   -668    156       C  
ATOM   1124  C   TYR A 245      20.503 -16.401  25.186  1.00 35.90           C  
ANISOU 1124  C   TYR A 245     3649   3948   6044   2087   -704    399       C  
ATOM   1125  O   TYR A 245      19.688 -15.732  24.566  1.00 32.77           O  
ANISOU 1125  O   TYR A 245     3228   3211   6011   1028   -730   1048       O  
ATOM   1126  CB  TYR A 245      20.634 -15.538  27.536  1.00 41.12           C  
ANISOU 1126  CB  TYR A 245     5120   3363   7141   1384   -981    533       C  
ATOM   1127  CG  TYR A 245      20.600 -16.755  28.420  1.00 43.59           C  
ANISOU 1127  CG  TYR A 245     5632   2820   8108    -96  -1295    604       C  
ATOM   1128  CD1 TYR A 245      21.770 -17.274  28.955  1.00 48.90           C  
ANISOU 1128  CD1 TYR A 245     6685   3426   8469   1394  -1335    888       C  
ATOM   1129  CD2 TYR A 245      19.402 -17.387  28.725  1.00 43.10           C  
ANISOU 1129  CD2 TYR A 245     5411   3072   7895  -1709  -1267    424       C  
ATOM   1130  CE1 TYR A 245      21.751 -18.381  29.769  1.00 52.52           C  
ANISOU 1130  CE1 TYR A 245     7269   3981   8705    603  -1402    855       C  
ATOM   1131  CE2 TYR A 245      19.374 -18.501  29.542  1.00 51.59           C  
ANISOU 1131  CE2 TYR A 245     6287   4382   8935  -1057  -1484    441       C  
ATOM   1132  CZ  TYR A 245      20.553 -18.991  30.059  1.00 56.14           C  
ANISOU 1132  CZ  TYR A 245     7229   4809   9292   -552  -1460    674       C  
ATOM   1133  OH  TYR A 245      20.546 -20.095  30.875  1.00 59.30           O  
ANISOU 1133  OH  TYR A 245     7312   4939  10279  -2644  -1568    381       O  
ATOM   1134  N   PRO A 246      20.640 -17.720  24.993  1.00 37.32           N  
ANISOU 1134  N   PRO A 246     4579   3594   6008   2161  -1031    138       N  
ATOM   1135  CA  PRO A 246      19.986 -18.419  23.877  1.00 32.99           C  
ANISOU 1135  CA  PRO A 246     3452   3094   5987   1254   -913     98       C  
ATOM   1136  C   PRO A 246      18.480 -18.678  24.006  1.00 37.55           C  
ANISOU 1136  C   PRO A 246     4015   4280   5973   1630   -470    410       C  
ATOM   1137  O   PRO A 246      17.952 -19.542  23.306  1.00 32.78           O  
ANISOU 1137  O   PRO A 246     3160   3272   6023    619    -52    546       O  
ATOM   1138  CB  PRO A 246      20.742 -19.750  23.828  1.00 34.94           C  
ANISOU 1138  CB  PRO A 246     4477   2835   5965   1299   -763     35       C  
ATOM   1139  CG  PRO A 246      21.194 -19.963  25.218  1.00 35.30           C  
ANISOU 1139  CG  PRO A 246     4543   2884   5985   1347  -1005    -23       C  
ATOM   1140  CD  PRO A 246      21.548 -18.607  25.739  1.00 36.10           C  
ANISOU 1140  CD  PRO A 246     4149   3607   5962   2046  -1023    103       C  
ATOM   1141  N  AMET A 247      17.786 -17.966  24.883  0.49 35.29           N  
ANISOU 1141  N  AMET A 247     3421   4102   5886    767   -551    633       N  
ATOM   1142  N  BMET A 247      17.806 -17.931  24.873  0.51 34.69           N  
ANISOU 1142  N  BMET A 247     3299   3864   6016    837   -505    406       N  
ATOM   1143  CA AMET A 247      16.336 -18.100  24.900  0.49 35.79           C  
ANISOU 1143  CA AMET A 247     3848   3925   5827   1143   -336   1182       C  
ATOM   1144  CA BMET A 247      16.362 -18.062  25.022  0.51 34.28           C  
ANISOU 1144  CA BMET A 247     3555   3457   6012   1582   -226    793       C  
ATOM   1145  C  AMET A 247      15.636 -16.770  25.112  0.49 32.01           C  
ANISOU 1145  C  AMET A 247     2671   3787   5703    776   -212    652       C  
ATOM   1146  C  BMET A 247      15.689 -16.697  25.062  0.51 31.19           C  
ANISOU 1146  C  BMET A 247     2473   3625   5752   1125   -204    500       C  
ATOM   1147  O  AMET A 247      16.015 -15.967  25.965  0.49 36.36           O  
ANISOU 1147  O  AMET A 247     2689   5355   5772    286   -317    537       O  
ATOM   1148  O  BMET A 247      16.143 -15.788  25.758  0.51 32.94           O  
ANISOU 1148  O  BMET A 247     1959   4830   5726   -549   -427    349       O  
ATOM   1149  CB AMET A 247      15.886 -19.117  25.954  0.49 45.54           C  
ANISOU 1149  CB AMET A 247     6105   5257   5940   1664   -387   1947       C  
ATOM   1150  CB BMET A 247      16.019 -18.862  26.280  0.51 43.01           C  
ANISOU 1150  CB BMET A 247     5611   4507   6224   1986   -108   1180       C  
ATOM   1151  CG AMET A 247      16.646 -19.100  27.261  0.49 56.13           C  
ANISOU 1151  CG AMET A 247     8712   6526   6090   1726   -261   2457       C  
ATOM   1152  CG BMET A 247      15.924 -20.364  26.045  0.51 52.80           C  
ANISOU 1152  CG BMET A 247     7858   5792   6413   1868    200   1265       C  
ATOM   1153  SD AMET A 247      16.649 -20.747  28.001  0.49 63.21           S  
ANISOU 1153  SD AMET A 247    10333   7496   6187   2185   -204   2911       S  
ATOM   1154  SD BMET A 247      14.276 -21.028  26.357  0.51 59.70           S  
ANISOU 1154  SD BMET A 247     9303   6835   6547   1170    287   1379       S  
ATOM   1155  CE AMET A 247      14.964 -21.268  27.681  0.49 60.75           C  
ANISOU 1155  CE AMET A 247    10618   6259   6205    676   -290   3437       C  
ATOM   1156  CE BMET A 247      14.375 -21.357  28.115  0.51 56.58           C  
ANISOU 1156  CE BMET A 247     9385   5544   6569   -244    410   1841       C  
ATOM   1157  N   TYR A 248      14.610 -16.556  24.301  1.00 32.83           N  
ANISOU 1157  N   TYR A 248     2614   4311   5550   1649    211    349       N  
ATOM   1158  CA  TYR A 248      13.873 -15.310  24.281  1.00 32.23           C  
ANISOU 1158  CA  TYR A 248     2712   4224   5312   1646    309    384       C  
ATOM   1159  C   TYR A 248      12.979 -15.157  25.490  1.00 36.97           C  
ANISOU 1159  C   TYR A 248     3918   4844   5284   1349    163    473       C  
ATOM   1160  O   TYR A 248      12.212 -16.055  25.835  1.00 36.55           O  
ANISOU 1160  O   TYR A 248     3742   4826   5321   1199    636    708       O  
ATOM   1161  CB  TYR A 248      13.023 -15.214  23.014  1.00 29.82           C  
ANISOU 1161  CB  TYR A 248     2527   3683   5120    973    298    235       C  
ATOM   1162  CG  TYR A 248      12.120 -13.996  22.955  1.00 24.62           C  
ANISOU 1162  CG  TYR A 248     1454   2955   4945   -156    171    357       C  
ATOM   1163  CD1 TYR A 248      10.810 -14.044  23.443  1.00 22.75           C  
ANISOU 1163  CD1 TYR A 248     1536   2246   4863    266    -10    396       C  
ATOM   1164  CD2 TYR A 248      12.565 -12.809  22.390  1.00 24.37           C  
ANISOU 1164  CD2 TYR A 248     1577   2755   4927      0    257    293       C  
ATOM   1165  CE1 TYR A 248       9.984 -12.941  23.381  1.00 23.43           C  
ANISOU 1165  CE1 TYR A 248     1617   2535   4750    738    187    332       C  
ATOM   1166  CE2 TYR A 248      11.734 -11.699  22.320  1.00 21.82           C  
ANISOU 1166  CE2 TYR A 248     1253   2276   4761     15    357    415       C  
ATOM   1167  CZ  TYR A 248      10.448 -11.778  22.818  1.00 22.58           C  
ANISOU 1167  CZ  TYR A 248     1381   2312   4886   -407    157   -147       C  
ATOM   1168  OH  TYR A 248       9.626 -10.684  22.757  1.00 21.68           O  
ANISOU 1168  OH  TYR A 248     1897   1646   4694   -550    484   -224       O  
ATOM   1169  N  AARG A 249      13.090 -14.021  26.161  0.59 32.23           N  
ANISOU 1169  N  AARG A 249     3056   3904   5286    831     16    191       N  
ATOM   1170  N  BARG A 249      13.074 -13.985  26.104  0.41 32.81           N  
ANISOU 1170  N  BARG A 249     3433   3782   5249    565    127    343       N  
ATOM   1171  CA AARG A 249      12.090 -13.648  27.143  0.59 37.84           C  
ANISOU 1171  CA AARG A 249     4249   4817   5312   1137      1    129       C  
ATOM   1172  CA BARG A 249      12.212 -13.587  27.202  0.41 36.40           C  
ANISOU 1172  CA BARG A 249     4138   4440   5254    577    225    250       C  
ATOM   1173  C  AARG A 249      11.895 -12.146  27.052  0.59 33.63           C  
ANISOU 1173  C  AARG A 249     3545   3949   5285    330    248    -56       C  
ATOM   1174  C  BARG A 249      11.914 -12.105  27.045  0.41 32.28           C  
ANISOU 1174  C  BARG A 249     3327   3688   5248    -51    335     10       C  
ATOM   1175  O  AARG A 249      12.858 -11.379  27.003  0.59 36.70           O  
ANISOU 1175  O  AARG A 249     4188   4404   5351    758    331   -219       O  
ATOM   1176  O  BARG A 249      12.839 -11.297  26.955  0.41 34.27           O  
ANISOU 1176  O  BARG A 249     3804   3911   5307    324    373    -79       O  
ATOM   1177  CB AARG A 249      12.479 -14.083  28.561  0.59 46.09           C  
ANISOU 1177  CB AARG A 249     5501   6636   5375   1967   -228    126       C  
ATOM   1178  CB BARG A 249      12.882 -13.863  28.547  0.41 44.03           C  
ANISOU 1178  CB BARG A 249     5513   5917   5300   1519    224    378       C  
ATOM   1179  CG AARG A 249      13.715 -13.424  29.137  0.59 49.81           C  
ANISOU 1179  CG AARG A 249     6340   7164   5421   1603   -261    243       C  
ATOM   1180  CG BARG A 249      11.925 -13.936  29.718  0.41 48.27           C  
ANISOU 1180  CG BARG A 249     6148   6847   5345   2090    243    501       C  
ATOM   1181  CD AARG A 249      13.439 -12.899  30.540  0.59 52.67           C  
ANISOU 1181  CD AARG A 249     7069   7486   5459   1573   -341    201       C  
ATOM   1182  CD BARG A 249      12.674 -14.152  31.020  0.41 50.65           C  
ANISOU 1182  CD BARG A 249     6424   7431   5391   1506    220    539       C  
ATOM   1183  NE AARG A 249      14.085 -13.696  31.578  0.59 53.71           N  
ANISOU 1183  NE AARG A 249     7692   7198   5517   1552   -266    244       N  
ATOM   1184  NE BARG A 249      11.757 -14.322  32.143  0.41 50.03           N  
ANISOU 1184  NE BARG A 249     6361   7199   5447    794    252    589       N  
ATOM   1185  CZ AARG A 249      14.898 -13.198  32.504  0.59 52.81           C  
ANISOU 1185  CZ AARG A 249     7867   6609   5590   1362   -265    197       C  
ATOM   1186  CZ BARG A 249      11.404 -13.348  32.974  0.41 49.73           C  
ANISOU 1186  CZ BARG A 249     6258   7131   5507    800    313    562       C  
ATOM   1187  NH1AARG A 249      15.162 -11.899  32.530  0.59 52.99           N  
ANISOU 1187  NH1AARG A 249     8177   6306   5652   1707   -236    183       N  
ATOM   1188  NH1BARG A 249      11.895 -12.127  32.813  0.41 51.96           N  
ANISOU 1188  NH1BARG A 249     6624   7557   5561   1432    281    607       N  
ATOM   1189  NH2AARG A 249      15.443 -13.997  33.411  0.59 50.81           N  
ANISOU 1189  NH2AARG A 249     7458   6255   5592    648   -306    243       N  
ATOM   1190  NH2BARG A 249      10.561 -13.594  33.968  0.41 48.28           N  
ANISOU 1190  NH2BARG A 249     5913   6931   5500    794    341    656       N  
ATOM   1191  N   PHE A 250      10.637 -11.734  26.990  1.00 30.64           N  
ANISOU 1191  N   PHE A 250     2486   3947   5210    183    442   -118       N  
ATOM   1192  CA  PHE A 250      10.319 -10.332  26.822  1.00 30.54           C  
ANISOU 1192  CA  PHE A 250     2213   4181   5210    331    718   -225       C  
ATOM   1193  C   PHE A 250      10.655  -9.556  28.084  1.00 26.93           C  
ANISOU 1193  C   PHE A 250     1614   3159   5460   -558    436   -581       C  
ATOM   1194  O   PHE A 250      10.425 -10.019  29.200  1.00 33.03           O  
ANISOU 1194  O   PHE A 250     3466   3680   5402    190    247   -643       O  
ATOM   1195  CB  PHE A 250       8.855 -10.119  26.459  1.00 29.79           C  
ANISOU 1195  CB  PHE A 250     2405   3924   4992    -26    344   -368       C  
ATOM   1196  CG  PHE A 250       8.490  -8.672  26.350  1.00 24.19           C  
ANISOU 1196  CG  PHE A 250     1810   2512   4870   -264    184   -425       C  
ATOM   1197  CD1 PHE A 250       8.861  -7.942  25.237  1.00 27.68           C  
ANISOU 1197  CD1 PHE A 250     1615   4051   4853    119    197   -386       C  
ATOM   1198  CD2 PHE A 250       7.829  -8.028  27.380  1.00 27.52           C  
ANISOU 1198  CD2 PHE A 250     2314   3312   4832    234     72   -459       C  
ATOM   1199  CE1 PHE A 250       8.555  -6.601  25.137  1.00 28.26           C  
ANISOU 1199  CE1 PHE A 250     2469   3409   4861   -319    -11   -457       C  
ATOM   1200  CE2 PHE A 250       7.519  -6.687  27.287  1.00 30.30           C  
ANISOU 1200  CE2 PHE A 250     2810   3883   4819    858   -199   -616       C  
ATOM   1201  CZ  PHE A 250       7.891  -5.970  26.162  1.00 27.41           C  
ANISOU 1201  CZ  PHE A 250     1419   4326   4670    436   -446   -650       C  
ATOM   1202  N   THR A 251      11.220  -8.373  27.884  1.00 28.80           N  
ANISOU 1202  N   THR A 251     1754   3562   5626   -723     75   -852       N  
ATOM   1203  CA  THR A 251      11.483  -7.434  28.964  1.00 35.51           C  
ANISOU 1203  CA  THR A 251     2495   4856   6142   -226   -214  -1206       C  
ATOM   1204  C   THR A 251      11.319  -6.016  28.440  1.00 32.81           C  
ANISOU 1204  C   THR A 251     2688   3491   6287  -1124     26  -1428       C  
ATOM   1205  O   THR A 251      11.482  -5.769  27.243  1.00 35.16           O  
ANISOU 1205  O   THR A 251     2881   4047   6429    465   -135  -1768       O  
ATOM   1206  CB  THR A 251      12.899  -7.607  29.552  1.00 40.05           C  
ANISOU 1206  CB  THR A 251     3924   5247   6046     91   -450  -1241       C  
ATOM   1207  OG1 THR A 251      13.095  -6.667  30.616  1.00 42.23           O  
ANISOU 1207  OG1 THR A 251     4794   5260   5991     48   -441   -899       O  
ATOM   1208  CG2 THR A 251      13.962  -7.386  28.480  1.00 41.01           C  
ANISOU 1208  CG2 THR A 251     4264   5324   5993    233   -635  -1401       C  
ATOM   1209  N   GLU A 252      10.977  -5.092  29.331  1.00 32.58           N  
ANISOU 1209  N   GLU A 252     2584   3164   6629   -905    199  -1453       N  
ATOM   1210  CA  GLU A 252      10.863  -3.684  28.965  1.00 36.85           C  
ANISOU 1210  CA  GLU A 252     2253   4598   7152   -695    446  -1554       C  
ATOM   1211  C   GLU A 252      12.064  -2.908  29.488  1.00 41.29           C  
ANISOU 1211  C   GLU A 252     3261   5318   7110    185    524  -1344       C  
ATOM   1212  O   GLU A 252      12.243  -1.731  29.174  1.00 41.60           O  
ANISOU 1212  O   GLU A 252     3596   5161   7050    891    538  -1147       O  
ATOM   1213  CB  GLU A 252       9.565  -3.088  29.510  1.00 44.86           C  
ANISOU 1213  CB  GLU A 252     3637   5986   7422   -489   1058  -1034       C  
ATOM   1214  CG  GLU A 252       8.320  -3.805  29.016  1.00 53.26           C  
ANISOU 1214  CG  GLU A 252     5054   7466   7717     69   1485  -1165       C  
ATOM   1215  CD  GLU A 252       7.037  -3.224  29.574  1.00 65.00           C  
ANISOU 1215  CD  GLU A 252     7317   9445   7935   1433   1698  -1224       C  
ATOM   1216  OE1 GLU A 252       6.506  -3.790  30.553  1.00 72.25           O  
ANISOU 1216  OE1 GLU A 252     8963  10458   8029   2891   1745  -1022       O  
ATOM   1217  OE2 GLU A 252       6.552  -2.210  29.028  1.00 64.72           O  
ANISOU 1217  OE2 GLU A 252     7033   9572   7987    734   1821   -945       O  
ATOM   1218  N   GLY A 253      12.884  -3.580  30.291  1.00 36.26           N  
ANISOU 1218  N   GLY A 253     2048   4946   6785   -510    403  -1663       N  
ATOM   1219  CA  GLY A 253      14.047  -2.959  30.897  1.00 38.85           C  
ANISOU 1219  CA  GLY A 253     2213   5779   6768   -132    411  -2326       C  
ATOM   1220  C   GLY A 253      15.276  -3.027  30.015  1.00 41.59           C  
ANISOU 1220  C   GLY A 253     2621   6841   6339    587    705  -2269       C  
ATOM   1221  O   GLY A 253      15.199  -3.510  28.885  1.00 42.81           O  
ANISOU 1221  O   GLY A 253     2602   7371   6294    510    701  -2199       O  
ATOM   1222  N   PRO A 254      16.418  -2.534  30.526  1.00 37.51           N  
ANISOU 1222  N   PRO A 254     3056   5181   6015   -513    704  -2211       N  
ATOM   1223  CA  PRO A 254      17.691  -2.541  29.802  1.00 35.40           C  
ANISOU 1223  CA  PRO A 254     2953   4638   5860    122    488  -1823       C  
ATOM   1224  C   PRO A 254      18.127  -3.944  29.385  1.00 28.57           C  
ANISOU 1224  C   PRO A 254     2022   3358   5475     69    494  -1338       C  
ATOM   1225  O   PRO A 254      18.336  -4.809  30.241  1.00 34.64           O  
ANISOU 1225  O   PRO A 254     4156   3584   5422    -58    813  -1115       O  
ATOM   1226  CB  PRO A 254      18.670  -1.948  30.816  1.00 32.78           C  
ANISOU 1226  CB  PRO A 254     2245   4495   5717  -1037    747  -1866       C  
ATOM   1227  CG  PRO A 254      17.841  -1.144  31.736  1.00 37.58           C  
ANISOU 1227  CG  PRO A 254     3147   5108   6023   -575    808  -1991       C  
ATOM   1228  CD  PRO A 254      16.544  -1.889  31.845  1.00 35.22           C  
ANISOU 1228  CD  PRO A 254     2901   4633   5847  -1600    894  -1827       C  
ATOM   1229  N   PRO A 255      18.268  -4.171  28.073  1.00 26.73           N  
ANISOU 1229  N   PRO A 255     2231   2799   5127   -172    153   -545       N  
ATOM   1230  CA  PRO A 255      18.616  -5.508  27.582  1.00 23.52           C  
ANISOU 1230  CA  PRO A 255     1924   2020   4991   -192     64   -650       C  
ATOM   1231  C   PRO A 255      20.087  -5.905  27.814  1.00 20.82           C  
ANISOU 1231  C   PRO A 255     1124   2549   4239   -109   -162   -547       C  
ATOM   1232  O   PRO A 255      20.332  -7.087  28.059  1.00 29.47           O  
ANISOU 1232  O   PRO A 255     2730   3296   5172   1221    -43   -450       O  
ATOM   1233  CB  PRO A 255      18.317  -5.423  26.075  1.00 26.21           C  
ANISOU 1233  CB  PRO A 255     2132   2840   4985    624     27   -736       C  
ATOM   1234  CG  PRO A 255      17.512  -4.166  25.891  1.00 29.74           C  
ANISOU 1234  CG  PRO A 255     3166   3204   4931    727    105   -347       C  
ATOM   1235  CD  PRO A 255      17.961  -3.244  26.974  1.00 26.45           C  
ANISOU 1235  CD  PRO A 255     2619   2448   4982    172     77   -314       C  
ATOM   1236  N   LEU A 256      21.037  -4.964  27.739  1.00 21.88           N  
ANISOU 1236  N   LEU A 256     1292   2188   4832    224    -57   -560       N  
ATOM   1237  CA  LEU A 256      22.459  -5.306  27.861  1.00 24.64           C  
ANISOU 1237  CA  LEU A 256     1680   3009   4673    800    -83    -34       C  
ATOM   1238  C   LEU A 256      22.861  -5.629  29.296  1.00 25.02           C  
ANISOU 1238  C   LEU A 256     1865   3012   4631   1035   -355   -425       C  
ATOM   1239  O   LEU A 256      22.459  -4.950  30.245  1.00 28.48           O  
ANISOU 1239  O   LEU A 256     2311   4023   4489   1007   -294   -562       O  
ATOM   1240  CB  LEU A 256      23.345  -4.170  27.336  1.00 25.84           C  
ANISOU 1240  CB  LEU A 256     2397   2906   4517   1008    -43   -391       C  
ATOM   1241  CG  LEU A 256      23.415  -3.885  25.834  1.00 25.93           C  
ANISOU 1241  CG  LEU A 256     1573   3724   4556    382   -271   -712       C  
ATOM   1242  CD1 LEU A 256      24.504  -2.875  25.552  1.00 28.35           C  
ANISOU 1242  CD1 LEU A 256     1856   4350   4567  -1327    -24   -340       C  
ATOM   1243  CD2 LEU A 256      23.632  -5.151  25.019  1.00 29.15           C  
ANISOU 1243  CD2 LEU A 256     2479   4080   4515   1567   -118  -1056       C  
ATOM   1244  N   HIS A 257      23.663  -6.680  29.429  1.00 26.32           N  
ANISOU 1244  N   HIS A 257     2170   3414   4415   1373   -559   -497       N  
ATOM   1245  CA  HIS A 257      24.207  -7.115  30.708  1.00 31.05           C  
ANISOU 1245  CA  HIS A 257     2361   4762   4674   1536   -357   -528       C  
ATOM   1246  C   HIS A 257      25.715  -6.929  30.653  1.00 31.85           C  
ANISOU 1246  C   HIS A 257     2938   4501   4662   1996   -451   -720       C  
ATOM   1247  O   HIS A 257      26.276  -6.774  29.570  1.00 31.19           O  
ANISOU 1247  O   HIS A 257     2173   4993   4685   1461   -417   -856       O  
ATOM   1248  CB  HIS A 257      23.833  -8.578  30.970  1.00 30.52           C  
ANISOU 1248  CB  HIS A 257     2658   4332   4607   1863   -472   -198       C  
ATOM   1249  CG  HIS A 257      24.292  -9.112  32.293  1.00 33.18           C  
ANISOU 1249  CG  HIS A 257     4055   3932   4621   1715   -660   -188       C  
ATOM   1250  ND1 HIS A 257      25.547  -9.649  32.485  1.00 37.19           N  
ANISOU 1250  ND1 HIS A 257     5014   4468   4646   2706   -774   -425       N  
ATOM   1251  CD2 HIS A 257      23.646  -9.232  33.477  1.00 33.56           C  
ANISOU 1251  CD2 HIS A 257     3959   4095   4696   1778   -873   -163       C  
ATOM   1252  CE1 HIS A 257      25.663 -10.053  33.737  1.00 37.93           C  
ANISOU 1252  CE1 HIS A 257     5465   4233   4712   2817   -476   -416       C  
ATOM   1253  NE2 HIS A 257      24.522  -9.816  34.359  1.00 35.64           N  
ANISOU 1253  NE2 HIS A 257     4518   4260   4764   2501   -597   -362       N  
ATOM   1254  N   LYS A 258      26.356  -6.903  31.815  1.00 32.46           N  
ANISOU 1254  N   LYS A 258     2902   4770   4660   1924   -763  -1059       N  
ATOM   1255  CA  LYS A 258      27.817  -6.843  31.887  1.00 32.16           C  
ANISOU 1255  CA  LYS A 258     2408   5094   4715    862   -871  -1299       C  
ATOM   1256  C   LYS A 258      28.486  -7.818  30.915  1.00 32.71           C  
ANISOU 1256  C   LYS A 258     2663   4905   4861   1577   -733  -1314       C  
ATOM   1257  O   LYS A 258      29.455  -7.471  30.242  1.00 33.27           O  
ANISOU 1257  O   LYS A 258     2305   5508   4828   1469   -630  -1134       O  
ATOM   1258  CB  LYS A 258      28.291  -7.138  33.311  1.00 37.24           C  
ANISOU 1258  CB  LYS A 258     3364   6167   4618   1510  -1048  -1259       C  
ATOM   1259  CG  LYS A 258      28.762  -5.919  34.090  1.00 40.74           C  
ANISOU 1259  CG  LYS A 258     4173   6656   4650   2227   -961  -1094       C  
ATOM   1260  CD  LYS A 258      29.457  -6.337  35.380  1.00 36.58           C  
ANISOU 1260  CD  LYS A 258     3554   5555   4789   2276  -1079   -721       C  
ATOM   1261  CE  LYS A 258      29.408  -5.241  36.438  1.00 31.53           C  
ANISOU 1261  CE  LYS A 258     2314   4757   4908   1626   -478   -457       C  
ATOM   1262  NZ  LYS A 258      30.073  -3.975  36.002  1.00 31.83           N  
ANISOU 1262  NZ  LYS A 258     3248   3751   5096   1964   -632   -373       N  
ATOM   1263  N   ASP A 259      27.943  -9.027  30.829  1.00 29.23           N  
ANISOU 1263  N   ASP A 259     2449   3862   4797   1365  -1052  -1253       N  
ATOM   1264  CA  ASP A 259      28.515 -10.073  29.982  1.00 32.77           C  
ANISOU 1264  CA  ASP A 259     2438   4962   5049   1614   -721   -789       C  
ATOM   1265  C   ASP A 259      28.491  -9.702  28.500  1.00 31.87           C  
ANISOU 1265  C   ASP A 259     1850   5225   5034   1198   -270   -382       C  
ATOM   1266  O   ASP A 259      29.461  -9.943  27.771  1.00 32.72           O  
ANISOU 1266  O   ASP A 259     1774   5579   5079    819   -306   -885       O  
ATOM   1267  CB  ASP A 259      27.771 -11.389  30.197  1.00 33.37           C  
ANISOU 1267  CB  ASP A 259     3081   4474   5123   2041   -551   -664       C  
ATOM   1268  CG  ASP A 259      28.470 -12.563  29.544  1.00 39.02           C  
ANISOU 1268  CG  ASP A 259     4162   5431   5233   2655  -1053   -581       C  
ATOM   1269  OD1 ASP A 259      29.512 -12.999  30.075  1.00 43.64           O  
ANISOU 1269  OD1 ASP A 259     4767   6402   5413   3144   -951   -553       O  
ATOM   1270  OD2 ASP A 259      27.984 -13.049  28.504  1.00 41.33           O  
ANISOU 1270  OD2 ASP A 259     4631   5807   5266   2889  -1163   -523       O  
ATOM   1271  N   ASP A 260      27.377  -9.117  28.062  1.00 31.51           N  
ANISOU 1271  N   ASP A 260     2314   4662   4997   1686   -265   -263       N  
ATOM   1272  CA  ASP A 260      27.228  -8.673  26.680  1.00 30.92           C  
ANISOU 1272  CA  ASP A 260     2284   4522   4942   1435   -581    -13       C  
ATOM   1273  C   ASP A 260      28.290  -7.631  26.340  1.00 30.31           C  
ANISOU 1273  C   ASP A 260     1717   5046   4754   1008   -165   -621       C  
ATOM   1274  O   ASP A 260      28.948  -7.716  25.300  1.00 30.83           O  
ANISOU 1274  O   ASP A 260     1678   5323   4714    831   -195   -761       O  
ATOM   1275  CB  ASP A 260      25.830  -8.080  26.438  1.00 27.21           C  
ANISOU 1275  CB  ASP A 260     1700   4029   4608   1100   -490    -78       C  
ATOM   1276  CG  ASP A 260      24.704  -9.071  26.697  1.00 29.62           C  
ANISOU 1276  CG  ASP A 260     2075   4259   4920   1407   -368   -477       C  
ATOM   1277  OD1 ASP A 260      24.723 -10.188  26.140  1.00 30.75           O  
ANISOU 1277  OD1 ASP A 260     2014   4771   4898   1380   -366   -469       O  
ATOM   1278  OD2 ASP A 260      23.784  -8.712  27.460  1.00 30.95           O  
ANISOU 1278  OD2 ASP A 260     3346   3479   4934   2035     35   -199       O  
ATOM   1279  N   VAL A 261      28.456  -6.652  27.226  1.00 30.28           N  
ANISOU 1279  N   VAL A 261     1904   4890   4710   1271     -6   -607       N  
ATOM   1280  CA  VAL A 261      29.412  -5.570  27.011  1.00 28.85           C  
ANISOU 1280  CA  VAL A 261     1474   4815   4674    647   -145   -576       C  
ATOM   1281  C   VAL A 261      30.849  -6.078  27.090  1.00 29.98           C  
ANISOU 1281  C   VAL A 261     1567   4883   4942    251   -443   -866       C  
ATOM   1282  O   VAL A 261      31.692  -5.678  26.295  1.00 32.98           O  
ANISOU 1282  O   VAL A 261     1744   5905   4883   -195    -45  -1433       O  
ATOM   1283  CB  VAL A 261      29.217  -4.434  28.024  1.00 25.66           C  
ANISOU 1283  CB  VAL A 261     1471   3723   4554    609   -153   -974       C  
ATOM   1284  CG1 VAL A 261      30.220  -3.319  27.773  1.00 29.21           C  
ANISOU 1284  CG1 VAL A 261     2043   4217   4839    341      4   -902       C  
ATOM   1285  CG2 VAL A 261      27.793  -3.896  27.927  1.00 27.42           C  
ANISOU 1285  CG2 VAL A 261     1616   3941   4861    781   -107   -903       C  
ATOM   1286  N  AASN A 262      31.124  -6.955  28.049  0.65 29.48           N  
ANISOU 1286  N  AASN A 262     2102   4387   4713   1454   -240   -604       N  
ATOM   1287  N  BASN A 262      31.101  -6.943  28.070  0.35 29.86           N  
ANISOU 1287  N  BASN A 262     2002   4567   4776   1260   -293   -953       N  
ATOM   1288  CA AASN A 262      32.447  -7.564  28.154  0.65 29.58           C  
ANISOU 1288  CA AASN A 262     2170   4314   4756   1481   -369   -620       C  
ATOM   1289  CA BASN A 262      32.371  -7.648  28.221  0.35 30.74           C  
ANISOU 1289  CA BASN A 262     2328   4552   4799   1475   -321  -1197       C  
ATOM   1290  C  AASN A 262      32.751  -8.410  26.930  0.65 30.50           C  
ANISOU 1290  C  AASN A 262     1854   4817   4915   1144   -391   -657       C  
ATOM   1291  C  BASN A 262      32.727  -8.388  26.946  0.35 31.81           C  
ANISOU 1291  C  BASN A 262     1894   5296   4897    660   -473  -1465       C  
ATOM   1292  O  AASN A 262      33.889  -8.443  26.463  0.65 28.88           O  
ANISOU 1292  O  AASN A 262     1949   4154   4868   1408    -40   -199       O  
ATOM   1293  O  BASN A 262      33.859  -8.324  26.461  0.35 32.78           O  
ANISOU 1293  O  BASN A 262     2191   5343   4920   -213   -348  -1623       O  
ATOM   1294  CB AASN A 262      32.555  -8.406  29.423  0.65 32.41           C  
ANISOU 1294  CB AASN A 262     2149   5320   4845   1379   -667   -658       C  
ATOM   1295  CB BASN A 262      32.285  -8.634  29.391  0.35 31.86           C  
ANISOU 1295  CB BASN A 262     2715   4643   4746   1789   -279  -1111       C  
ATOM   1296  CG AASN A 262      32.727  -7.561  30.670  0.65 33.72           C  
ANISOU 1296  CG AASN A 262     2583   5380   4851    347   -619   -530       C  
ATOM   1297  CG BASN A 262      33.630  -9.212  29.776  0.35 31.14           C  
ANISOU 1297  CG BASN A 262     2613   4437   4781   1313    -56  -1042       C  
ATOM   1298  OD1AASN A 262      33.225  -6.432  30.610  0.65 33.63           O  
ANISOU 1298  OD1AASN A 262     3163   4720   4896   -560   -573    -27       O  
ATOM   1299  OD1BASN A 262      34.650  -8.529  29.726  0.35 33.30           O  
ANISOU 1299  OD1BASN A 262     2246   5604   4802   1413   -146  -1203       O  
ATOM   1300  ND2AASN A 262      32.326  -8.107  31.812  0.65 37.23           N  
ANISOU 1300  ND2AASN A 262     3626   5687   4832   1337   -837   -479       N  
ATOM   1301  ND2BASN A 262      33.637 -10.485  30.159  0.35 26.54           N  
ANISOU 1301  ND2BASN A 262     1926   3418   4742    -30     11   -962       N  
ATOM   1302  N   GLY A 263      31.739  -9.094  26.409  1.00 35.35           N  
ANISOU 1302  N   GLY A 263     2858   5616   4956   1525   -675  -1202       N  
ATOM   1303  CA  GLY A 263      31.911  -9.878  25.207  1.00 35.18           C  
ANISOU 1303  CA  GLY A 263     3221   5143   5004   2205   -370   -927       C  
ATOM   1304  C   GLY A 263      32.234  -8.995  24.020  1.00 31.62           C  
ANISOU 1304  C   GLY A 263     2130   4669   5214   1149   -105  -1116       C  
ATOM   1305  O   GLY A 263      33.116  -9.314  23.231  1.00 28.99           O  
ANISOU 1305  O   GLY A 263     1688   4049   5280    721   -120  -1023       O  
ATOM   1306  N   ILE A 264      31.536  -7.871  23.897  1.00 31.53           N  
ANISOU 1306  N   ILE A 264     2402   4451   5129   1464    310   -976       N  
ATOM   1307  CA  ILE A 264      31.705  -7.038  22.718  1.00 25.97           C  
ANISOU 1307  CA  ILE A 264     1354   3879   4634    444    -26   -736       C  
ATOM   1308  C   ILE A 264      32.985  -6.200  22.825  1.00 30.60           C  
ANISOU 1308  C   ILE A 264     1558   5167   4903    213    -41  -1129       C  
ATOM   1309  O   ILE A 264      33.612  -5.908  21.810  1.00 32.86           O  
ANISOU 1309  O   ILE A 264     1766   5709   5012    213    147  -1538       O  
ATOM   1310  CB  ILE A 264      30.438  -6.150  22.458  1.00 27.24           C  
ANISOU 1310  CB  ILE A 264     1953   3172   5226    821    306   -961       C  
ATOM   1311  CG1 ILE A 264      30.336  -5.788  20.973  1.00 26.16           C  
ANISOU 1311  CG1 ILE A 264     1335   3826   4779    -75    284   -793       C  
ATOM   1312  CG2 ILE A 264      30.385  -4.909  23.365  1.00 27.30           C  
ANISOU 1312  CG2 ILE A 264     1727   3855   4789    971     70   -756       C  
ATOM   1313  CD1 ILE A 264      30.107  -6.970  20.056  1.00 27.01           C  
ANISOU 1313  CD1 ILE A 264     1337   4098   4829    111    -46   -782       C  
ATOM   1314  N  AARG A 265      33.359  -5.827  24.045  0.63 30.05           N  
ANISOU 1314  N  AARG A 265     1594   4804   5020    167    -10  -1418       N  
ATOM   1315  N  BARG A 265      33.379  -5.836  24.043  0.37 30.43           N  
ANISOU 1315  N  BARG A 265     1616   4906   5041    231      8  -1402       N  
ATOM   1316  CA AARG A 265      34.607  -5.100  24.254  0.63 28.96           C  
ANISOU 1316  CA AARG A 265     1529   4573   4900   -193   -149  -1250       C  
ATOM   1317  CA BARG A 265      34.624  -5.091  24.232  0.37 29.40           C  
ANISOU 1317  CA BARG A 265     1503   4735   4933     50     29  -1167       C  
ATOM   1318  C  AARG A 265      35.812  -6.000  23.999  0.63 29.68           C  
ANISOU 1318  C  AARG A 265     1552   4520   5203    -80    -26  -1290       C  
ATOM   1319  C  BARG A 265      35.849  -5.989  24.087  0.37 30.92           C  
ANISOU 1319  C  BARG A 265     1645   4878   5227    481     81  -1148       C  
ATOM   1320  O  AARG A 265      36.859  -5.533  23.548  0.63 33.28           O  
ANISOU 1320  O  AARG A 265     1673   5577   5394   -205    209  -1115       O  
ATOM   1321  O  BARG A 265      36.947  -5.510  23.808  0.37 33.57           O  
ANISOU 1321  O  BARG A 265     1767   5643   5345    550    376   -959       O  
ATOM   1322  CB AARG A 265      34.674  -4.514  25.670  0.63 30.88           C  
ANISOU 1322  CB AARG A 265     1913   4926   4893    878    -74  -1529       C  
ATOM   1323  CB BARG A 265      34.651  -4.397  25.597  0.37 29.94           C  
ANISOU 1323  CB BARG A 265     1699   4897   4779    578    232  -1257       C  
ATOM   1324  CG AARG A 265      33.803  -3.271  25.873  0.63 31.39           C  
ANISOU 1324  CG AARG A 265     2380   4821   4724   1429   -146  -1444       C  
ATOM   1325  CG BARG A 265      33.762  -3.164  25.681  0.37 29.94           C  
ANISOU 1325  CG BARG A 265     1708   4963   4703    678    324  -1056       C  
ATOM   1326  CD AARG A 265      33.972  -2.668  27.269  0.63 33.47           C  
ANISOU 1326  CD AARG A 265     2512   5362   4843    788   -111  -1719       C  
ATOM   1327  CD BARG A 265      34.012  -2.371  26.958  0.37 28.68           C  
ANISOU 1327  CD BARG A 265     1501   4709   4689   -281    520   -868       C  
ATOM   1328  NE AARG A 265      33.065  -1.541  27.489  0.63 31.62           N  
ANISOU 1328  NE AARG A 265     2399   4897   4717   1285   -377  -1691       N  
ATOM   1329  NE BARG A 265      35.236  -1.572  26.905  0.37 26.90           N  
ANISOU 1329  NE BARG A 265     1401   4301   4520    223    477   -735       N  
ATOM   1330  CZ AARG A 265      32.711  -1.078  28.686  0.63 30.95           C  
ANISOU 1330  CZ AARG A 265     2081   5018   4661    326   -454  -1799       C  
ATOM   1331  CZ BARG A 265      35.707  -0.870  27.932  0.37 23.05           C  
ANISOU 1331  CZ BARG A 265     1311   3060   4389   -422    222   -866       C  
ATOM   1332  NH1AARG A 265      31.868  -0.052  28.788  0.63 27.41           N  
ANISOU 1332  NH1AARG A 265     1507   4518   4389   -148    167  -1518       N  
ATOM   1333  NH1BARG A 265      36.823  -0.167  27.805  0.37 24.85           N  
ANISOU 1333  NH1BARG A 265     1698   3238   4506    149    283   -782       N  
ATOM   1334  NH2AARG A 265      33.183  -1.650  29.786  0.63 28.94           N  
ANISOU 1334  NH2AARG A 265     1936   4454   4604   -465   -705  -1453       N  
ATOM   1335  NH2BARG A 265      35.060  -0.873  29.090  0.37 26.57           N  
ANISOU 1335  NH2BARG A 265     2211   3429   4455    489    199   -997       N  
ATOM   1336  N   HIS A 266      35.663  -7.288  24.288  1.00 30.54           N  
ANISOU 1336  N   HIS A 266     1703   4675   5225    784    -23   -942       N  
ATOM   1337  CA  HIS A 266      36.738  -8.243  24.042  1.00 28.76           C  
ANISOU 1337  CA  HIS A 266     1486   3829   5611    -19    126   -811       C  
ATOM   1338  C   HIS A 266      37.048  -8.274  22.551  1.00 29.80           C  
ANISOU 1338  C   HIS A 266     1566   4174   5585    -34     45  -1187       C  
ATOM   1339  O   HIS A 266      38.218  -8.345  22.156  1.00 32.80           O  
ANISOU 1339  O   HIS A 266     1730   5088   5644    565    400   -852       O  
ATOM   1340  CB  HIS A 266      36.364  -9.636  24.546  1.00 30.21           C  
ANISOU 1340  CB  HIS A 266     1726   3920   5832    726     20   -569       C  
ATOM   1341  CG  HIS A 266      37.450 -10.647  24.377  1.00 43.15           C  
ANISOU 1341  CG  HIS A 266     3952   6123   6319   2790    118   -406       C  
ATOM   1342  ND1 HIS A 266      38.599 -10.636  25.137  1.00 48.94           N  
ANISOU 1342  ND1 HIS A 266     5040   7195   6359   3487    255   -194       N  
ATOM   1343  CD2 HIS A 266      37.561 -11.703  23.538  1.00 46.69           C  
ANISOU 1343  CD2 HIS A 266     4646   6768   6327   2281    516   -264       C  
ATOM   1344  CE1 HIS A 266      39.374 -11.641  24.772  1.00 50.97           C  
ANISOU 1344  CE1 HIS A 266     5322   7631   6414   3595    730   -216       C  
ATOM   1345  NE2 HIS A 266      38.767 -12.304  23.804  1.00 46.57           N  
ANISOU 1345  NE2 HIS A 266     3985   7347   6364   2333    873   -264       N  
ATOM   1346  N   LEU A 267      36.009  -8.198  21.726  1.00 29.77           N  
ANISOU 1346  N   LEU A 267     1705   3993   5615    282   -199  -1670       N  
ATOM   1347  CA  LEU A 267      36.174  -8.163  20.279  1.00 28.52           C  
ANISOU 1347  CA  LEU A 267     1546   4024   5266     63   -145  -1377       C  
ATOM   1348  C   LEU A 267      36.594  -6.789  19.771  1.00 31.38           C  
ANISOU 1348  C   LEU A 267     1696   4800   5428    -38   -151  -1597       C  
ATOM   1349  O   LEU A 267      37.433  -6.693  18.874  1.00 37.33           O  
ANISOU 1349  O   LEU A 267     2388   6435   5362    867    629  -1393       O  
ATOM   1350  CB  LEU A 267      34.877  -8.604  19.578  1.00 27.34           C  
ANISOU 1350  CB  LEU A 267     1569   3383   5436    160   -427  -1270       C  
ATOM   1351  CG  LEU A 267      34.464 -10.057  19.802  1.00 32.54           C  
ANISOU 1351  CG  LEU A 267     1751   4972   5640    490   -427  -1211       C  
ATOM   1352  CD1 LEU A 267      33.189 -10.349  19.037  1.00 32.37           C  
ANISOU 1352  CD1 LEU A 267     1896   4762   5640   -517   -425  -1256       C  
ATOM   1353  CD2 LEU A 267      35.579 -11.014  19.386  1.00 36.38           C  
ANISOU 1353  CD2 LEU A 267     2947   5280   5597   2078    -94   -699       C  
ATOM   1354  N   TYR A 268      36.064  -5.726  20.369  1.00 29.76           N  
ANISOU 1354  N   TYR A 268     1571   4413   5324    -55     86  -1328       N  
ATOM   1355  CA  TYR A 268      36.209  -4.402  19.768  1.00 27.62           C  
ANISOU 1355  CA  TYR A 268     1591   3755   5147   -716    287   -675       C  
ATOM   1356  C   TYR A 268      36.887  -3.335  20.645  1.00 31.47           C  
ANISOU 1356  C   TYR A 268     1549   4869   5538     25    -88   -926       C  
ATOM   1357  O   TYR A 268      37.183  -2.244  20.162  1.00 35.79           O  
ANISOU 1357  O   TYR A 268     1953   5671   5973   -230   -618  -1367       O  
ATOM   1358  CB  TYR A 268      34.831  -3.904  19.306  1.00 31.99           C  
ANISOU 1358  CB  TYR A 268     1689   4898   5569    442    101   -739       C  
ATOM   1359  CG  TYR A 268      34.262  -4.768  18.205  1.00 29.87           C  
ANISOU 1359  CG  TYR A 268     1501   4679   5167    627    -53   -510       C  
ATOM   1360  CD1 TYR A 268      34.686  -4.618  16.898  1.00 27.45           C  
ANISOU 1360  CD1 TYR A 268     1403   3740   5284   -133    281   -608       C  
ATOM   1361  CD2 TYR A 268      33.267  -5.711  18.466  1.00 25.57           C  
ANISOU 1361  CD2 TYR A 268     1347   3380   4989    272   -259   -587       C  
ATOM   1362  CE1 TYR A 268      34.190  -5.404  15.882  1.00 28.63           C  
ANISOU 1362  CE1 TYR A 268     1422   4422   5035    492   -103   -531       C  
ATOM   1363  CE2 TYR A 268      32.749  -6.505  17.444  1.00 24.70           C  
ANISOU 1363  CE2 TYR A 268     1443   2698   5243     13   -433   -868       C  
ATOM   1364  CZ  TYR A 268      33.213  -6.339  16.151  1.00 30.71           C  
ANISOU 1364  CZ  TYR A 268     1964   4297   5407   1095   -225   -955       C  
ATOM   1365  OH  TYR A 268      32.724  -7.107  15.115  1.00 29.55           O  
ANISOU 1365  OH  TYR A 268     1521   4413   5295     70     24  -1135       O  
ATOM   1366  N   GLY A 269      37.126  -3.636  21.917  1.00 32.41           N  
ANISOU 1366  N   GLY A 269     1763   4902   5650    323   -255  -1556       N  
ATOM   1367  CA  GLY A 269      37.873  -2.716  22.764  1.00 37.33           C  
ANISOU 1367  CA  GLY A 269     2084   6208   5891   -610   -136  -1725       C  
ATOM   1368  C   GLY A 269      37.012  -1.738  23.539  1.00 47.31           C  
ANISOU 1368  C   GLY A 269     2766   8841   6370    -10   -146  -1911       C  
ATOM   1369  O   GLY A 269      37.504  -1.002  24.396  1.00 48.68           O  
ANISOU 1369  O   GLY A 269     2766   9439   6293  -1105    184  -1702       O  
ATOM   1370  OXT GLY A 269      35.802  -1.651  23.332  1.00 43.30           O  
ANISOU 1370  OXT GLY A 269     2260   7883   6310    183     35  -1736       O  
TER    1371      GLY A 269                                                      
HETATM 1372  OSB N73 A 301      15.642 -20.336  18.402  1.00 39.64           O  
ANISOU 1372  OSB N73 A 301     3080   5801   6182   1354   -329    355       O  
HETATM 1373  S2  N73 A 301      16.579 -19.345  17.877  1.00 28.46           S  
ANISOU 1373  S2  N73 A 301     2392   2342   6080    215    141     67       S  
HETATM 1374  OSA N73 A 301      16.203 -18.927  16.520  1.00 33.62           O  
ANISOU 1374  OSA N73 A 301     3708   2967   6097    852    198    293       O  
HETATM 1375  N1  N73 A 301      17.964 -19.879  17.956  1.00 41.19           N  
ANISOU 1375  N1  N73 A 301     4315   4921   6414   1318   -340    -19       N  
HETATM 1376  ON2 N73 A 301      18.035 -21.078  18.363  1.00 53.04           O  
ANISOU 1376  ON2 N73 A 301     6575   6883   6696   2175   -525    516       O  
HETATM 1377  C13 N73 A 301      18.321 -21.332  19.745  1.00 51.77           C  
ANISOU 1377  C13 N73 A 301     6597   6187   6888   2138   -742    994       C  
HETATM 1378  C44 N73 A 301      17.360 -22.386  20.319  1.00 49.47           C  
ANISOU 1378  C44 N73 A 301     6992   4855   6950   2375   -744   1306       C  
HETATM 1379  C15 N73 A 301      19.760 -21.815  19.928  1.00 47.21           C  
ANISOU 1379  C15 N73 A 301     5188   5813   6935   2192   -714   1064       C  
HETATM 1380  C16 N73 A 301      18.806 -19.561  16.908  1.00 36.86           C  
ANISOU 1380  C16 N73 A 301     4072   3543   6391    487   -612   -568       C  
HETATM 1381  C18 N73 A 301      19.866 -20.660  16.575  1.00 35.03           C  
ANISOU 1381  C18 N73 A 301     3470   3325   6514   -441   -355   -551       C  
HETATM 1382  C19 N73 A 301      19.324 -21.779  15.671  1.00 37.66           C  
ANISOU 1382  C19 N73 A 301     4817   2989   6504   1275   -302   -458       C  
HETATM 1383  C20 N73 A 301      21.065 -20.057  15.844  1.00 32.13           C  
ANISOU 1383  C20 N73 A 301     2211   3414   6584     36   -274   -384       C  
HETATM 1384  C17 N73 A 301      19.606 -18.334  17.394  1.00 32.69           C  
ANISOU 1384  C17 N73 A 301     2799   3349   6273   -554   -541   -626       C  
HETATM 1385  O8  N73 A 301      20.280 -18.411  18.369  1.00 35.79           O  
ANISOU 1385  O8  N73 A 301     4803   2438   6359    -66   -508   -954       O  
HETATM 1386  N8  N73 A 301      19.562 -17.085  16.667  1.00 32.13           N  
ANISOU 1386  N8  N73 A 301     1725   4315   6168    355   -556     39       N  
HETATM 1387  OA8 N73 A 301      20.205 -16.178  17.055  1.00 30.63           O  
ANISOU 1387  OA8 N73 A 301     2172   3754   5712    562  -1390     88       O  
HETATM 1388  C1  N73 A 301      16.629 -17.853  18.956  1.00 25.07           C  
ANISOU 1388  C1  N73 A 301     1492   2585   5450    395    -56     58       C  
HETATM 1389  C2  N73 A 301      16.756 -16.555  18.368  1.00 27.08           C  
ANISOU 1389  C2  N73 A 301     2078   2455   5755    681   -232     52       C  
HETATM 1390  C3  N73 A 301      16.819 -15.386  19.249  1.00 24.03           C  
ANISOU 1390  C3  N73 A 301     1829   2254   5046    738   -202     42       C  
HETATM 1391  C4  N73 A 301      16.753 -15.551  20.672  1.00 24.32           C  
ANISOU 1391  C4  N73 A 301     2034   1786   5420    366   -345    468       C  
HETATM 1392  C11 N73 A 301      16.641 -16.846  21.260  1.00 29.30           C  
ANISOU 1392  C11 N73 A 301     3137   2502   5494   1143   -116    -49       C  
HETATM 1393  C12 N73 A 301      16.574 -18.015  20.382  1.00 28.68           C  
ANISOU 1393  C12 N73 A 301     2639   2621   5639    583   -148     82       C  
HETATM 1394  C5  N73 A 301      16.824 -14.291  21.571  1.00 24.50           C  
ANISOU 1394  C5  N73 A 301     2036   2020   5251   -286   -191    323       C  
HETATM 1395  C6  N73 A 301      17.518 -14.345  22.942  1.00 26.22           C  
ANISOU 1395  C6  N73 A 301     2264   2496   5201    802   -330     31       C  
HETATM 1396  C7  N73 A 301      17.547 -13.223  23.747  1.00 26.82           C  
ANISOU 1396  C7  N73 A 301     2656   2295   5240   -770   -396   -726       C  
HETATM 1397  C8  N73 A 301      16.845 -11.930  23.274  1.00 29.29           C  
ANISOU 1397  C8  N73 A 301     2278   3624   5229     11   -195     90       C  
HETATM 1398  C9  N73 A 301      16.207 -11.895  22.086  1.00 23.19           C  
ANISOU 1398  C9  N73 A 301     1553   2123   5135    315    117    294       C  
HETATM 1399  C10 N73 A 301      16.172 -13.166  21.174  1.00 24.09           C  
ANISOU 1399  C10 N73 A 301     1395   2674   5086    287    -53    722       C  
HETATM 1400 ZN    ZN A 302      21.189 -16.597  19.098  1.00 26.22          ZN  
ANISOU 1400 ZN    ZN A 302     2251   2346   5367    933   -336    -66      ZN  
HETATM 1401 ZN    ZN A 303      18.825 -17.422   6.703  1.00 23.52          ZN  
ANISOU 1401 ZN    ZN A 303     1544   2224   5167    213    200   -588      ZN  
HETATM 1402 CA    CA A 304       9.878 -20.149  13.596  1.00 21.43          CA  
ANISOU 1402 CA    CA A 304     2111   1659   4372   -182    355    119      CA  
HETATM 1403 CA    CA A 305      27.143  -9.627   4.690  1.00 26.06          CA  
ANISOU 1403 CA    CA A 305     1686   2674   5541   -411    724   -948      CA  
HETATM 1404 CA    CA A 306       4.894 -12.582  10.164  1.00 20.12          CA  
ANISOU 1404 CA    CA A 306     1205   1980   4460   -267    -54   -184      CA  
HETATM 1405  S   DMS A 307      23.200 -19.573  10.750  1.00 69.22           S  
ANISOU 1405  S   DMS A 307     8825   5978  11496   2308   1620  -1427       S  
HETATM 1406  O   DMS A 307      23.412 -18.322  11.537  1.00 64.12           O  
ANISOU 1406  O   DMS A 307     8293   4653  11418   1253   1801  -1759       O  
HETATM 1407  C1  DMS A 307      24.822 -20.261  10.324  1.00 66.74           C  
ANISOU 1407  C1  DMS A 307     8239   5591  11529   2261   1683  -1332       C  
HETATM 1408  C2  DMS A 307      22.597 -20.883  11.851  1.00 72.14           C  
ANISOU 1408  C2  DMS A 307     9557   6310  11542   1998   1697  -1321       C  
HETATM 1409  S   DMS A 308      13.780  -5.919  -7.507  1.00 67.79           S  
ANISOU 1409  S   DMS A 308     8057   8372   9329    824     54     32       S  
HETATM 1410  O   DMS A 308      14.708  -6.560  -6.523  1.00 66.32           O  
ANISOU 1410  O   DMS A 308     8271   7580   9349   -496   -144   -215       O  
HETATM 1411  C1  DMS A 308      13.547  -7.038  -8.910  1.00 62.54           C  
ANISOU 1411  C1  DMS A 308     7436   7045   9282   -862     23     31       C  
HETATM 1412  C2  DMS A 308      12.095  -5.940  -6.839  1.00 61.86           C  
ANISOU 1412  C2  DMS A 308     7179   6987   9338   -822     25   -111       C  
HETATM 1413  C1  EDO A 309      13.665  -2.870  -0.057  1.00 32.50           C  
ANISOU 1413  C1  EDO A 309     3824   2531   5993   1479    253    -66       C  
HETATM 1414  O1  EDO A 309      12.475  -2.879   0.739  1.00 38.86           O  
ANISOU 1414  O1  EDO A 309     4142   4784   5839    -73    396    -48       O  
HETATM 1415  C2  EDO A 309      13.331  -3.416  -1.436  1.00 26.08           C  
ANISOU 1415  C2  EDO A 309     2727   1943   5240   -944    121    -61       C  
HETATM 1416  O2  EDO A 309      12.534  -2.472  -2.154  1.00 36.15           O  
ANISOU 1416  O2  EDO A 309     4985   2935   5817   -371    515    321       O  
HETATM 1417  C1 AEDO A 310       1.360  -5.305  19.684  0.99 59.00           C  
ANISOU 1417  C1 AEDO A 310     8075   6069   8273   2954   -663  -1124       C  
HETATM 1418  O1 AEDO A 310       1.820  -4.051  20.203  0.99 57.90           O  
ANISOU 1418  O1 AEDO A 310     7742   5944   8315   2246   -697  -1188       O  
HETATM 1419  C2 AEDO A 310       1.303  -6.336  20.803  0.99 57.75           C  
ANISOU 1419  C2 AEDO A 310     7988   5744   8208   3457   -631  -1024       C  
HETATM 1420  O2 AEDO A 310       2.631  -6.748  21.147  0.99 60.30           O  
ANISOU 1420  O2 AEDO A 310     8530   6262   8120   3365   -461  -1124       O  
HETATM 1421  C1  EDO A 311      38.763   1.738  11.435  1.00 63.75           C  
ANISOU 1421  C1  EDO A 311     6519   9139   8563    242    720    630       C  
HETATM 1422  O1  EDO A 311      38.737   0.624  12.334  1.00 61.60           O  
ANISOU 1422  O1  EDO A 311     5307   9549   8549  -1186   1060    855       O  
HETATM 1423  C2  EDO A 311      38.059   1.357  10.139  1.00 65.44           C  
ANISOU 1423  C2  EDO A 311     7869   8452   8542    902    483    406       C  
HETATM 1424  O2  EDO A 311      37.035   2.315   9.846  1.00 65.73           O  
ANISOU 1424  O2  EDO A 311     8364   8058   8553    101    303    343       O  
HETATM 1425  C1  EDO A 312      12.923 -25.109  19.381  1.00 60.65           C  
ANISOU 1425  C1  EDO A 312     7811   6773   8461     34    659    844       C  
HETATM 1426  O1  EDO A 312      12.319 -25.167  20.677  1.00 58.29           O  
ANISOU 1426  O1  EDO A 312     8078   5584   8486   -839    608    667       O  
HETATM 1427  C2  EDO A 312      14.142 -24.195  19.429  1.00 60.65           C  
ANISOU 1427  C2  EDO A 312     7239   7381   8423   -512    657    800       C  
HETATM 1428  O2  EDO A 312      14.820 -24.245  18.169  1.00 60.89           O  
ANISOU 1428  O2  EDO A 312     7025   7694   8415   -683    627    738       O  
HETATM 1429  C1  GOL A 313      35.231  -6.492   7.586  1.00 54.73           C  
ANISOU 1429  C1  GOL A 313     3189   7280  10325     78   1495    780       C  
HETATM 1430  O1  GOL A 313      36.190  -5.614   7.049  1.00 55.81           O  
ANISOU 1430  O1  GOL A 313     3546   7282  10378   1380   1332    561       O  
HETATM 1431  C2  GOL A 313      35.665  -7.943   7.443  1.00 58.66           C  
ANISOU 1431  C2  GOL A 313     5392   6593  10305    588   1150    526       C  
HETATM 1432  O2  GOL A 313      35.167  -8.456   6.227  1.00 62.01           O  
ANISOU 1432  O2  GOL A 313     6743   6544  10275   -134   1311    934       O  
HETATM 1433  C3  GOL A 313      35.071  -8.727   8.606  1.00 58.26           C  
ANISOU 1433  C3  GOL A 313     5381   6472  10283   1369    663   -173       C  
HETATM 1434  O3  GOL A 313      35.682  -9.989   8.702  1.00 52.81           O  
ANISOU 1434  O3  GOL A 313     5402   4395  10268   1569   -293   -426       O  
HETATM 1435  C1  PGO A 314      18.388  -7.950  -9.815  1.00 70.49           C  
ANISOU 1435  C1  PGO A 314     9807   7802   9174   -134    387     44       C  
HETATM 1436  C2  PGO A 314      19.623  -8.737  -9.399  1.00 74.85           C  
ANISOU 1436  C2  PGO A 314    10447   8833   9159    128    306   -548       C  
HETATM 1437  C3  PGO A 314      19.430  -9.349  -8.018  1.00 74.82           C  
ANISOU 1437  C3  PGO A 314    10480   8810   9137   -632    328   -551       C  
HETATM 1438  O1  PGO A 314      18.067  -8.226 -11.183  1.00 64.37           O  
ANISOU 1438  O1  PGO A 314     9424   5844   9189   -897    428    262       O  
HETATM 1439  O2  PGO A 314      20.760  -7.865  -9.390  1.00 74.95           O  
ANISOU 1439  O2  PGO A 314    10822   8488   9166    946    357   -349       O  
HETATM 1440  C1  PGO A 315      15.998 -10.527  27.511  1.00 62.93           C  
HETATM 1441  C2  PGO A 315      16.445 -11.288  28.754  1.00 86.13           C  
HETATM 1442  C3  PGO A 315      16.493 -10.369  29.968  1.00 61.05           C  
HETATM 1443  O1  PGO A 315      16.523 -11.171  26.345  1.00 85.42           O  
HETATM 1444  O2  PGO A 315      17.739 -11.864  28.533  1.00 83.53           O  
HETATM 1445  C1  BUD A 316       0.006  -1.516   5.768  1.00 80.09           C  
ANISOU 1445  C1  BUD A 316     9679  10023  10727    639    101    564       C  
HETATM 1446  O1  BUD A 316       0.445  -1.001   8.059  1.00 76.25           O  
ANISOU 1446  O1  BUD A 316     9037   9210  10725    -57     59    532       O  
HETATM 1447  C2  BUD A 316       0.052  -2.036   7.187  1.00 75.47           C  
ANISOU 1447  C2  BUD A 316     8543   9418  10714    388     24    602       C  
HETATM 1448  O2  BUD A 316       2.106  -2.951   6.381  1.00 63.28           O  
ANISOU 1448  O2  BUD A 316     5293   7988  10761   2335   -418    214       O  
HETATM 1449  C3  BUD A 316       1.043  -3.171   7.278  1.00 67.65           C  
ANISOU 1449  C3  BUD A 316     6534   8467  10703   1015   -193    355       C  
HETATM 1450  C4  BUD A 316       1.579  -3.229   8.687  1.00 64.93           C  
ANISOU 1450  C4  BUD A 316     5826   8136  10710    392   -181    355       C  
HETATM 1451  O   HOH A 401      28.414 -20.303  27.655  1.00 39.18           O  
ANISOU 1451  O   HOH A 401     3535   5682   5672     58   -484    753       O  
HETATM 1452  O   HOH A 402       9.622 -10.859   3.126  1.00 47.01           O  
ANISOU 1452  O   HOH A 402     6216   6179   5467   2597    -78   -372       O  
HETATM 1453  O   HOH A 403      24.912 -19.342  33.772  1.00 57.33           O  
ANISOU 1453  O   HOH A 403     5836   5048  10898    -64  -2885   2600       O  
HETATM 1454  O   HOH A 404      19.153 -19.767  32.674  1.00 58.31           O  
ANISOU 1454  O   HOH A 404     9947   3248   8960  -1900    612    681       O  
HETATM 1455  O   HOH A 405      34.625   4.515  15.957  1.00 70.30           O  
ANISOU 1455  O   HOH A 405     5560   8713  12439   1165   1495   -703       O  
HETATM 1456  O   HOH A 406      37.070  -3.831   5.808  1.00 67.24           O  
ANISOU 1456  O   HOH A 406     8248   7507   9793  -2955   4107  -3998       O  
HETATM 1457  O   HOH A 407      36.493   2.716   7.597  1.00 85.65           O  
ANISOU 1457  O   HOH A 407     7916  10648  13978   -750  -1519   6722       O  
HETATM 1458  O   HOH A 408       8.619 -26.608  11.463  1.00 53.84           O  
ANISOU 1458  O   HOH A 408     5432   3705  11321   -943   -263  -1778       O  
HETATM 1459  O   HOH A 409      14.039   5.732  17.570  1.00 64.51           O  
ANISOU 1459  O   HOH A 409     9781   4627  10101   -711  -2070  -1897       O  
HETATM 1460  O   HOH A 410      31.721 -11.574  31.158  1.00 62.88           O  
ANISOU 1460  O   HOH A 410     4903   9786   9201   1465  -3265    831       O  
HETATM 1461  O   HOH A 411      16.875 -14.165  35.726  1.00 87.61           O  
HETATM 1462  O   HOH A 412      12.558 -10.043  31.712  1.00 61.81           O  
ANISOU 1462  O   HOH A 412     6098   8955   8431  -2068   -666   3859       O  
HETATM 1463  O   HOH A 413      36.165  -7.959  27.852  1.00 65.56           O  
ANISOU 1463  O   HOH A 413     3336  12997   8578     89     48   1274       O  
HETATM 1464  O   HOH A 414      33.234   7.009  12.276  1.00 48.24           O  
ANISOU 1464  O   HOH A 414     5362   3144   9825   -247   1902   -524       O  
HETATM 1465  O   HOH A 415      26.727  -8.408   2.793  1.00 30.38           O  
ANISOU 1465  O   HOH A 415     2194   2243   7106   -402    592   -171       O  
HETATM 1466  O   HOH A 416      12.951 -26.021  14.528  1.00 39.52           O  
ANISOU 1466  O   HOH A 416     7101   1969   5948    776   -540     -3       O  
HETATM 1467  O   HOH A 417       1.973 -10.418   7.967  1.00 42.33           O  
ANISOU 1467  O   HOH A 417     3423   4922   7739    220  -2320  -1077       O  
HETATM 1468  O   HOH A 418      30.515 -17.443   3.781  1.00 51.60           O  
ANISOU 1468  O   HOH A 418     4552   6651   8402   1678   1941    935       O  
HETATM 1469  O   HOH A 419      18.936 -15.999  36.758  1.00 61.67           O  
ANISOU 1469  O   HOH A 419     7136   6759   9537    102   1083   2657       O  
HETATM 1470  O   HOH A 420      33.708 -13.926  17.432  1.00 41.79           O  
ANISOU 1470  O   HOH A 420     4283   3679   7917   1972    185    -35       O  
HETATM 1471  O   HOH A 421       8.040 -12.516   4.482  1.00 39.76           O  
ANISOU 1471  O   HOH A 421     4659   5908   4542   1565    221   -637       O  
HETATM 1472  O   HOH A 422      10.156  -4.305  22.324  1.00 28.59           O  
ANISOU 1472  O   HOH A 422     2197   2483   6182   -456   1364  -1442       O  
HETATM 1473  O   HOH A 423       0.559  -6.992  13.191  1.00 62.82           O  
ANISOU 1473  O   HOH A 423     7497   7707   8665   -150  -1663   2132       O  
HETATM 1474  O   HOH A 424      28.105  -1.168  -6.104  1.00 28.91           O  
ANISOU 1474  O   HOH A 424     3519   1774   5691     56     30    593       O  
HETATM 1475  O   HOH A 425      28.557   3.004   9.707  1.00 24.05           O  
ANISOU 1475  O   HOH A 425     1382   2256   5501    -63     87      3       O  
HETATM 1476  O   HOH A 426      28.272 -14.811  15.739  1.00 39.88           O  
ANISOU 1476  O   HOH A 426     3483   5403   6267   2217    756   -712       O  
HETATM 1477  O   HOH A 427      30.798  -6.685   4.007  1.00 34.97           O  
ANISOU 1477  O   HOH A 427     1796   5818   5673   -545    419   -963       O  
HETATM 1478  O   HOH A 428      26.242 -16.507  14.261  1.00 38.30           O  
ANISOU 1478  O   HOH A 428     2333   5359   6859    794   -465  -1678       O  
HETATM 1479  O   HOH A 429      18.803  -9.210  28.106  1.00 36.47           O  
ANISOU 1479  O   HOH A 429     4691   2747   6419    777   1210    879       O  
HETATM 1480  O   HOH A 430       9.838   0.697  16.329  1.00 29.38           O  
ANISOU 1480  O   HOH A 430     2528   2052   6585    504    416   -106       O  
HETATM 1481  O   HOH A 431       7.064 -10.982  23.251  1.00 25.07           O  
ANISOU 1481  O   HOH A 431     1523   2958   5042   -193    237    -49       O  
HETATM 1482  O   HOH A 432      16.359 -15.214  30.310  1.00 57.29           O  
HETATM 1483  O   HOH A 433      21.073   3.198  15.147  1.00 34.51           O  
ANISOU 1483  O   HOH A 433     3612   3883   5618  -1913    582   -174       O  
HETATM 1484  O   HOH A 434      27.863   0.745  -2.927  1.00 44.22           O  
ANISOU 1484  O   HOH A 434     4415   4338   8049    578    408   1346       O  
HETATM 1485  O   HOH A 435      11.478   4.845  10.950  1.00 38.56           O  
ANISOU 1485  O   HOH A 435     2957   3186   8510   -386    141   -136       O  
HETATM 1486  O   HOH A 436      33.604  -7.745   4.178  1.00 46.73           O  
ANISOU 1486  O   HOH A 436     3637   6519   7600   2389   1159   -625       O  
HETATM 1487  O   HOH A 437       6.069  -3.419   6.439  1.00 29.61           O  
ANISOU 1487  O   HOH A 437     4004   2596   4650   -377     52     97       O  
HETATM 1488  O   HOH A 438       2.385 -14.170  21.200  1.00 56.54           O  
ANISOU 1488  O   HOH A 438     6933   4748   9801   1360   2376   1196       O  
HETATM 1489  O   HOH A 439       9.247 -20.354   8.516  1.00 20.83           O  
ANISOU 1489  O   HOH A 439     1537   1512   4866   -263    512    -98       O  
HETATM 1490  O   HOH A 440      11.666 -25.757   6.887  1.00 67.39           O  
ANISOU 1490  O   HOH A 440     9285   3832  12488   -941   2103  -1650       O  
HETATM 1491  O   HOH A 441       5.620  -3.999  33.090  1.00 71.04           O  
ANISOU 1491  O   HOH A 441     9504   8240   9247     88   2840    823       O  
HETATM 1492  O   HOH A 442       2.438  -6.946  14.925  1.00 33.10           O  
ANISOU 1492  O   HOH A 442     1752   4711   6114    765   -153   -425       O  
HETATM 1493  O   HOH A 443      16.792 -26.410   3.175  1.00 47.72           O  
ANISOU 1493  O   HOH A 443     8735   3506   5892   1965   1653    -35       O  
HETATM 1494  O   HOH A 444      13.419 -13.191   1.963  1.00 32.12           O  
ANISOU 1494  O   HOH A 444     3000   4480   4726   -299    453    -52       O  
HETATM 1495  O   HOH A 445      29.312  -4.921  -6.169  1.00 54.72           O  
ANISOU 1495  O   HOH A 445     9327   3931   7534   -156   2025   1532       O  
HETATM 1496  O   HOH A 446      16.635   1.487  10.108  1.00 26.21           O  
ANISOU 1496  O   HOH A 446     2564   1509   5886   -143    -18   -255       O  
HETATM 1497  O   HOH A 447      10.782   2.713   4.952  1.00 54.88           O  
ANISOU 1497  O   HOH A 447     8323   3789   8740    146   1123   1669       O  
HETATM 1498  O   HOH A 448      30.646   6.332  10.805  1.00 44.60           O  
ANISOU 1498  O   HOH A 448     5618   4573   6757  -2638   1783  -1450       O  
HETATM 1499  O   HOH A 449      21.335 -12.534   3.237  1.00 29.65           O  
ANISOU 1499  O   HOH A 449     1838   4244   5183  -1112    354   -512       O  
HETATM 1500  O   HOH A 450      34.384  -0.734  32.048  1.00 59.59           O  
ANISOU 1500  O   HOH A 450     4172  13385   5085   2387      6  -1209       O  
HETATM 1501  O   HOH A 451      23.811   0.496  24.899  1.00 27.80           O  
ANISOU 1501  O   HOH A 451     1785   3811   4965   -850    486  -1169       O  
HETATM 1502  O   HOH A 452      29.335  -8.975   4.393  1.00 28.94           O  
ANISOU 1502  O   HOH A 452     1713   4159   5124   -408    762  -1273       O  
HETATM 1503  O   HOH A 453      30.985 -16.825  25.565  1.00 53.23           O  
ANISOU 1503  O   HOH A 453     4335   6529   9362   2014  -1708  -1584       O  
HETATM 1504  O   HOH A 454       5.128 -15.783  16.442  1.00 27.44           O  
ANISOU 1504  O   HOH A 454     2729   2639   5059   -363    763    306       O  
HETATM 1505  O   HOH A 455      22.738   3.642   0.024  1.00 32.89           O  
ANISOU 1505  O   HOH A 455     3090   3651   5755  -1610   -448   1249       O  
HETATM 1506  O   HOH A 456      28.111 -13.570  24.377  1.00 41.14           O  
ANISOU 1506  O   HOH A 456     3747   4498   7388   2012   -807  -1132       O  
HETATM 1507  O   HOH A 457      17.752 -22.700  -1.180  1.00 58.24           O  
ANISOU 1507  O   HOH A 457    11381   3711   7036   -838   2766   -829       O  
HETATM 1508  O   HOH A 458      21.961  -2.271  30.557  1.00 30.28           O  
ANISOU 1508  O   HOH A 458     2825   3568   5113    980    766   -348       O  
HETATM 1509  O   HOH A 459       3.997 -23.237  17.727  1.00 53.50           O  
ANISOU 1509  O   HOH A 459     8827   6574   4927  -4097   -725   1111       O  
HETATM 1510  O  AHOH A 460       9.934  -1.976  -1.423  0.53 36.66           O  
ANISOU 1510  O  AHOH A 460     2314   5150   6464  -1457    402   -409       O  
HETATM 1511  O  BHOH A 460       9.097  -1.637  -2.997  0.47 50.45           O  
ANISOU 1511  O  BHOH A 460     5802   4157   9211  -1805   1675    318       O  
HETATM 1512  O   HOH A 461      17.051 -21.107   4.397  1.00 34.54           O  
ANISOU 1512  O   HOH A 461     3940   3863   5319   1989    717    -80       O  
HETATM 1513  O   HOH A 462      29.660 -12.099  26.076  1.00 82.74           O  
ANISOU 1513  O   HOH A 462     7727   8888  14823  -3013  -4881   5910       O  
HETATM 1514  O   HOH A 463      20.196   3.923  11.375  1.00 38.54           O  
ANISOU 1514  O   HOH A 463     4010   3397   7235  -1398   1032  -1779       O  
HETATM 1515  O   HOH A 464      24.509 -10.419   1.313  1.00 41.45           O  
ANISOU 1515  O   HOH A 464     2412   8097   5242   -954    777   -675       O  
HETATM 1516  O   HOH A 465       9.992  -5.940  31.764  1.00 56.15           O  
ANISOU 1516  O   HOH A 465     6609   8504   6223  -2361   1951  -2077       O  
HETATM 1517  O   HOH A 466      26.892 -12.066  26.162  1.00 38.04           O  
ANISOU 1517  O   HOH A 466     3510   5929   5016   2394   -906  -1184       O  
HETATM 1518  O   HOH A 467      10.084 -10.773   0.325  1.00 36.80           O  
ANISOU 1518  O   HOH A 467     5239   2651   6094  -1928   -306     31       O  
HETATM 1519  O   HOH A 468      10.515  -1.780  21.271  1.00 41.61           O  
ANISOU 1519  O   HOH A 468     4996   4820   5995    695   1469    148       O  
HETATM 1520  O   HOH A 469      31.103   4.553   5.343  1.00 94.67           O  
HETATM 1521  O   HOH A 470      37.821 -11.366   5.743  1.00 64.86           O  
ANISOU 1521  O   HOH A 470     5021   7651  11973  -1985    596   -562       O  
HETATM 1522  O   HOH A 471      15.656  -0.780   2.558  1.00 26.31           O  
ANISOU 1522  O   HOH A 471     2501   2114   5382   -778   -549    239       O  
HETATM 1523  O   HOH A 472      40.462  -3.691  12.738  1.00 43.64           O  
ANISOU 1523  O   HOH A 472     3265   3329   9987    165  -1815    733       O  
HETATM 1524  O   HOH A 473      19.118 -21.578  11.814  1.00 45.01           O  
ANISOU 1524  O   HOH A 473     6562   5693   4845    153   -205   -143       O  
HETATM 1525  O   HOH A 474      10.681 -20.090   1.369  1.00 33.43           O  
ANISOU 1525  O   HOH A 474     4295   3913   4493   1289    414   -203       O  
HETATM 1526  O   HOH A 475      20.826 -10.267  -0.721  1.00 50.18           O  
ANISOU 1526  O   HOH A 475     4069   6018   8979   1948   1616   -431       O  
HETATM 1527  O   HOH A 476      24.675 -20.327   3.739  1.00 48.94           O  
ANISOU 1527  O   HOH A 476     3254   5700   9641    582   -104  -2488       O  
HETATM 1528  O   HOH A 477       3.901 -16.833  18.727  1.00 39.56           O  
ANISOU 1528  O   HOH A 477     4530   4483   6017   -174   1462    819       O  
HETATM 1529  O   HOH A 478      15.535   5.178   7.556  1.00 50.12           O  
ANISOU 1529  O   HOH A 478     5112   4437   9493    149    -90    371       O  
HETATM 1530  O   HOH A 479      13.171 -22.359  -1.145  1.00 31.54           O  
ANISOU 1530  O   HOH A 479     4616   2181   5185   -190   -352   -814       O  
HETATM 1531  O   HOH A 480      18.012  -0.299   3.827  1.00 22.92           O  
ANISOU 1531  O   HOH A 480     1804   1613   5292   -282    162     48       O  
HETATM 1532  O   HOH A 481      41.331  -5.107  16.192  1.00 38.06           O  
ANISOU 1532  O   HOH A 481     2205   4957   7298   -700    663  -1355       O  
HETATM 1533  O   HOH A 482      13.942  -3.336  26.345  1.00 47.52           O  
ANISOU 1533  O   HOH A 482     4079   7286   6689   2841    276    325       O  
HETATM 1534  O   HOH A 483      11.575   5.095   8.153  1.00 43.86           O  
ANISOU 1534  O   HOH A 483     7272   2987   6406    592  -1272     25       O  
HETATM 1535  O   HOH A 484       2.414 -15.953  11.646  1.00 51.24           O  
ANISOU 1535  O   HOH A 484     4543   5376   9549  -1867    733   1525       O  
HETATM 1536  O   HOH A 485       5.741  -3.351   3.666  1.00 46.23           O  
ANISOU 1536  O   HOH A 485     5614   5598   6354    433  -1578    991       O  
HETATM 1537  O   HOH A 486      33.375  -2.632  22.211  1.00 45.43           O  
ANISOU 1537  O   HOH A 486     2520   8537   6204    448    123  -2163       O  
HETATM 1538  O   HOH A 487      23.608 -22.102  22.427  1.00 45.53           O  
ANISOU 1538  O   HOH A 487     5349   4677   7274   2592  -1513    158       O  
HETATM 1539  O   HOH A 488       7.801  -3.832  -1.925  1.00 64.58           O  
ANISOU 1539  O   HOH A 488     8182   8028   8326  -1591    153    957       O  
HETATM 1540  O   HOH A 489      21.150  -9.254  -2.967  1.00 47.13           O  
ANISOU 1540  O   HOH A 489     7276   4616   6016    519   2699   1352       O  
HETATM 1541  O   HOH A 490      21.544   5.235   8.984  1.00 43.41           O  
ANISOU 1541  O   HOH A 490     6201   3756   6538   1374  -1045  -1570       O  
HETATM 1542  O   HOH A 491      18.870 -15.779   1.959  1.00 38.03           O  
ANISOU 1542  O   HOH A 491     3482   4331   6636     31    256   -684       O  
HETATM 1543  O  AHOH A 492       8.661 -12.080  30.190  0.56 42.62           O  
ANISOU 1543  O  AHOH A 492     5632   5263   5301  -1596    647   1782       O  
HETATM 1544  O  BHOH A 492      27.918 -20.720  23.935  0.44 45.26           O  
ANISOU 1544  O  BHOH A 492     5184   4534   7480   2113  -1005    889       O  
HETATM 1545  O   HOH A 493      14.028  -0.145  23.256  1.00 72.45           O  
ANISOU 1545  O   HOH A 493     9057   5802  12669   1827   4267  -1099       O  
HETATM 1546  O   HOH A 494      10.849   0.000  27.327  0.40 39.82           O  
ANISOU 1546  O   HOH A 494     5028   4093   6007     -4      7    911       O  
HETATM 1547  O  AHOH A 495       3.249  -3.638  17.718  0.40 40.22           O  
ANISOU 1547  O  AHOH A 495     3956   6398   4928    662    649  -1933       O  
HETATM 1548  O  BHOH A 495       9.766  -4.134  18.437  0.60 29.21           O  
ANISOU 1548  O  BHOH A 495     1696   4770   4632   -943    131   -844       O  
HETATM 1549  O   HOH A 496      32.594  -5.188  36.772  1.00 50.04           O  
ANISOU 1549  O   HOH A 496     2264   8207   8544    747   -392    -39       O  
HETATM 1550  O   HOH A 497      31.617   0.481   5.111  1.00 50.87           O  
ANISOU 1550  O   HOH A 497     5019   6660   7650  -1472   -437   -964       O  
HETATM 1551  O   HOH A 498      17.419 -19.606  13.356  1.00 75.82           O  
ANISOU 1551  O   HOH A 498     8948  10009   9851   2665  -1873    995       O  
HETATM 1552  O   HOH A 499      28.349 -15.468   0.679  1.00 46.96           O  
ANISOU 1552  O   HOH A 499     4904   5766   7173  -1997   2465  -2883       O  
HETATM 1553  O   HOH A 500      18.137 -23.784  10.211  1.00 38.86           O  
ANISOU 1553  O   HOH A 500     6655   2958   5151   1320    384    132       O  
HETATM 1554  O   HOH A 501      22.013 -16.778  14.838  1.00 29.06           O  
ANISOU 1554  O   HOH A 501     2213   3748   5080   1197   -103   -820       O  
HETATM 1555  O   HOH A 502      29.850 -15.700  31.111  1.00 70.37           O  
ANISOU 1555  O   HOH A 502     7673   7770  11296   3763   2967   3267       O  
HETATM 1556  O   HOH A 503      33.340 -16.802   8.593  1.00 84.94           O  
ANISOU 1556  O   HOH A 503     6038  10760  15475   2583  -2735  -4657       O  
HETATM 1557  O   HOH A 504       4.379  -8.390  28.811  1.00 63.80           O  
ANISOU 1557  O   HOH A 504     5575  10790   7878  -2541    897   -501       O  
HETATM 1558  O   HOH A 505       8.113  -9.737  30.988  1.00 67.43           O  
ANISOU 1558  O   HOH A 505     9443   8543   7635  -4007   -149   3235       O  
HETATM 1559  O   HOH A 506      38.665   5.484  13.339  1.00 59.02           O  
ANISOU 1559  O   HOH A 506     6342   8470   7613  -2013  -1600   -803       O  
HETATM 1560  O   HOH A 507      11.155  -4.001  24.914  1.00 49.51           O  
ANISOU 1560  O   HOH A 507     6851   5017   6943    249   -300   2008       O  
HETATM 1561  O   HOH A 508      18.800 -11.582  -3.214  1.00 55.52           O  
ANISOU 1561  O   HOH A 508     7559   5325   8211   -157   1285  -1024       O  
HETATM 1562  O   HOH A 509       9.362  -6.190   1.054  1.00 34.40           O  
ANISOU 1562  O   HOH A 509     3216   3989   5866   1517  -1331   -846       O  
HETATM 1563  O  AHOH A 510      31.466   3.799  23.341  0.48 37.23           O  
ANISOU 1563  O  AHOH A 510     3401   6445   4298   -815   -251   -490       O  
HETATM 1564  O  BHOH A 510      32.949  -3.231  30.543  0.52 31.59           O  
ANISOU 1564  O  BHOH A 510     2442   4195   5367    233    784   -787       O  
HETATM 1565  O   HOH A 511      13.180   4.298   3.112  1.00 61.42           O  
ANISOU 1565  O   HOH A 511     4232  10542   8561  -1189   -376   3570       O  
HETATM 1566  O   HOH A 512       2.931 -13.349  11.199  1.00 27.63           O  
ANISOU 1566  O   HOH A 512     1593   3492   5413   -669   -308    162       O  
HETATM 1567  O   HOH A 513      30.018 -14.574  25.488  1.00 68.66           O  
ANISOU 1567  O   HOH A 513     5358   8785  11947   2781  -2407    359       O  
HETATM 1568  O  AHOH A 514      13.714 -18.956  22.802  0.48 30.21           O  
ANISOU 1568  O  AHOH A 514     4997   1832   4649    -97   -389   -316       O  
HETATM 1569  O  BHOH A 514      12.940 -19.245  21.093  0.52 29.87           O  
ANISOU 1569  O  BHOH A 514     3664   2609   5077   -308    -92   1476       O  
HETATM 1570  O   HOH A 515       3.796 -12.943   8.033  1.00 28.06           O  
ANISOU 1570  O   HOH A 515     1408   4395   4858   -568   -415   -265       O  
HETATM 1571  O   HOH A 516      24.810  -5.830  34.127  1.00 43.88           O  
ANISOU 1571  O   HOH A 516     3736   8062   4874   1370     11    243       O  
HETATM 1572  O   HOH A 517       4.176   0.680   6.030  1.00 39.34           O  
ANISOU 1572  O   HOH A 517     3341   5080   6527    292   -652   1097       O  
HETATM 1573  O   HOH A 518       9.137 -22.883  20.452  1.00 44.80           O  
ANISOU 1573  O   HOH A 518     5668   6171   5183  -1951   1139    774       O  
HETATM 1574  O   HOH A 519      25.530   4.426  14.511  1.00 32.34           O  
ANISOU 1574  O   HOH A 519     2466   3735   6087  -1076   1225  -1285       O  
HETATM 1575  O   HOH A 520      38.991 -13.473  12.415  1.00 48.96           O  
ANISOU 1575  O   HOH A 520     5326   6068   7207     37   -577   -540       O  
HETATM 1576  O   HOH A 521      19.965  -7.227  31.730  1.00 53.00           O  
ANISOU 1576  O   HOH A 521     6733   5056   8350    563    253   1103       O  
HETATM 1577  O   HOH A 522      -0.334  -6.320  31.088  1.00 66.48           O  
ANISOU 1577  O   HOH A 522    10630   5213   9418   2266    624   1656       O  
HETATM 1578  O   HOH A 523      20.805  -1.980  27.959  1.00 23.43           O  
ANISOU 1578  O   HOH A 523     1274   2563   5064     85    -65    -92       O  
HETATM 1579  O   HOH A 524       5.155 -10.535  26.478  1.00 58.51           O  
ANISOU 1579  O   HOH A 524     6957   7385   7890  -1838   -335  -1367       O  
HETATM 1580  O   HOH A 525      14.633 -25.989  10.447  1.00 34.11           O  
ANISOU 1580  O   HOH A 525     3790   2595   6575   -851    392    282       O  
HETATM 1581  O   HOH A 526       8.252 -24.470  14.800  1.00 45.71           O  
ANISOU 1581  O   HOH A 526     5582   2820   8966   -411   -359  -1268       O  
HETATM 1582  O   HOH A 527      23.904  -2.585  -4.873  1.00 28.06           O  
ANISOU 1582  O   HOH A 527     3478   2286   4899   -396   -106    429       O  
HETATM 1583  O   HOH A 528      20.791   6.258   6.097  1.00 73.23           O  
ANISOU 1583  O   HOH A 528    13641   3471  10713    134    809   -206       O  
HETATM 1584  O   HOH A 529       4.198 -15.751   7.035  1.00 30.89           O  
ANISOU 1584  O   HOH A 529     3545   2569   5623   -658    343   -272       O  
HETATM 1585  O   HOH A 530      30.075  -6.283   1.621  1.00 42.31           O  
ANISOU 1585  O   HOH A 530     2648   6998   6431   -180   -371  -1303       O  
HETATM 1586  O   HOH A 531      13.988  -9.941  -1.465  1.00 51.98           O  
ANISOU 1586  O   HOH A 531     4357   7862   7529  -1889    328  -2962       O  
HETATM 1587  O   HOH A 532       9.927  -9.823  32.838  1.00 86.60           O  
ANISOU 1587  O   HOH A 532     7402  14181  11321    916  -2316   4842       O  
HETATM 1588  O   HOH A 533      14.958  -5.976  -2.615  1.00 63.19           O  
ANISOU 1588  O   HOH A 533     4062  10751   9198    568    503   5924       O  
HETATM 1589  O   HOH A 534      38.930  -5.181  26.099  1.00 52.92           O  
ANISOU 1589  O   HOH A 534     3631   6700   9775   -143  -2465   1224       O  
HETATM 1590  O   HOH A 535      31.032 -15.783   2.273  1.00 56.94           O  
ANISOU 1590  O   HOH A 535    10632   3854   7150   1585    648    713       O  
HETATM 1591  O   HOH A 536      20.588 -26.769   7.950  1.00 49.46           O  
ANISOU 1591  O   HOH A 536     8189   3895   6708   2379    757   1371       O  
HETATM 1592  O   HOH A 537      15.107  -8.257 -11.965  1.00 57.37           O  
ANISOU 1592  O   HOH A 537     5788   6006  10004  -2639   -990  -1215       O  
HETATM 1593  O   HOH A 538      26.447 -26.395   8.871  1.00 46.58           O  
ANISOU 1593  O   HOH A 538     5789   4232   7676     18    391    632       O  
HETATM 1594  O   HOH A 539      24.126 -20.870  26.759  1.00 47.60           O  
ANISOU 1594  O   HOH A 539     5704   5039   7344    200  -1514    925       O  
HETATM 1595  O   HOH A 540      33.398 -12.359  22.887  1.00 48.27           O  
ANISOU 1595  O   HOH A 540     3667   5906   8768   2138   1016    448       O  
HETATM 1596  O   HOH A 541      29.604 -18.698   9.258  1.00 59.32           O  
ANISOU 1596  O   HOH A 541     4906  10923   6710    595     34    887       O  
HETATM 1597  O   HOH A 542      10.386 -19.460  20.718  1.00 56.90           O  
ANISOU 1597  O   HOH A 542     9386   5419   6814  -1847   -927   2009       O  
HETATM 1598  O   HOH A 543       5.351   3.147   7.641  1.00 35.04           O  
ANISOU 1598  O   HOH A 543     3851   2318   7145    927   -608    178       O  
HETATM 1599  O   HOH A 544      37.840 -10.331  28.139  1.00 99.99           O  
ANISOU 1599  O   HOH A 544    10115  12548  15329   4902  -4756  -6926       O  
HETATM 1600  O   HOH A 545      23.676   2.940  15.600  1.00 49.15           O  
ANISOU 1600  O   HOH A 545     3744   6689   8241  -2752   -209    -89       O  
HETATM 1601  O   HOH A 546      19.429 -14.448  -0.332  1.00 55.65           O  
ANISOU 1601  O   HOH A 546     6149   9336   5660    799    210  -2369       O  
HETATM 1602  O   HOH A 547      34.890 -15.166   7.142  1.00 52.15           O  
ANISOU 1602  O   HOH A 547     4348   8504   6962    986     56    337       O  
HETATM 1603  O   HOH A 548      15.580  -9.298  -9.627  1.00 58.93           O  
ANISOU 1603  O   HOH A 548     7741   3999  10652  -2219    718      5       O  
HETATM 1604  O   HOH A 549      22.418  -5.096  33.367  1.00 47.75           O  
ANISOU 1604  O   HOH A 549     5729   6069   6346   3174   1097   -806       O  
HETATM 1605  O   HOH A 550       9.663   4.417  18.541  1.00 67.73           O  
ANISOU 1605  O   HOH A 550    10167   6717   8849   -397   1878  -4034       O  
HETATM 1606  O  AHOH A 551      37.896  -3.063  17.196  0.59 43.59           O  
ANISOU 1606  O  AHOH A 551     3495   4675   8392    812   -552  -1943       O  
HETATM 1607  O  BHOH A 551      33.318   5.266  14.280  0.41 67.62           O  
ANISOU 1607  O  BHOH A 551     6653  12455   6583   -996  -3312   -673       O  
HETATM 1608  O   HOH A 552       3.050  -7.729  31.263  1.00 77.87           O  
ANISOU 1608  O   HOH A 552    15148   4703   9737   2848    -32     43       O  
HETATM 1609  O   HOH A 553       6.094  -6.934  30.593  1.00 73.06           O  
ANISOU 1609  O   HOH A 553     9255  10613   7889     50   4392   1575       O  
HETATM 1610  O   HOH A 554      40.105 -12.575  10.349  1.00 54.16           O  
ANISOU 1610  O   HOH A 554     3400   7630   9548  -1771   -627   -645       O  
HETATM 1611  O   HOH A 555      19.611 -18.976  -3.165  1.00 63.73           O  
HETATM 1612  O   HOH A 556      15.921  -7.806  -3.786  1.00 38.73           O  
ANISOU 1612  O   HOH A 556     5675   3334   5706   -598    118   -295       O  
HETATM 1613  O   HOH A 557      38.900   1.365  18.474  1.00 65.20           O  
ANISOU 1613  O   HOH A 557     3828   8634  12310   -876   -623    828       O  
HETATM 1614  O   HOH A 558      23.204  -8.821  -0.858  1.00 46.18           O  
ANISOU 1614  O   HOH A 558     7308   4374   5865   1576   -259    435       O  
HETATM 1615  O   HOH A 559      22.023   5.847   2.283  1.00 51.09           O  
ANISOU 1615  O   HOH A 559     8260   4457   6695  -1659   -708   1170       O  
HETATM 1616  O   HOH A 560      38.744  -7.809  26.800  1.00 69.91           O  
ANISOU 1616  O   HOH A 560     8618   9405   8538   2315   3612  -1589       O  
HETATM 1617  O   HOH A 561      25.157   6.448  11.211  1.00 63.63           O  
ANISOU 1617  O   HOH A 561     8755   5684   9736    743  -1710  -3918       O  
HETATM 1618  O   HOH A 562      15.982   0.278  28.836  1.00 50.03           O  
ANISOU 1618  O   HOH A 562     8525   3958   6528  -2717   -763     66       O  
HETATM 1619  O  AHOH A 563      31.779 -14.365  22.049  0.89 51.68           O  
ANISOU 1619  O  AHOH A 563     7512   4577   7546    236  -3589  -1018       O  
HETATM 1620  O  BHOH A 563      30.813 -16.891  17.681  0.11 16.05           O  
ANISOU 1620  O  BHOH A 563     1437   1472   3189    616    174    374       O  
HETATM 1621  O   HOH A 564      19.019 -11.911  38.800  1.00 62.69           O  
ANISOU 1621  O   HOH A 564     6439   7986   9396   1464   -743   1663       O  
HETATM 1622  O   HOH A 565      36.905   1.628  22.408  1.00 54.43           O  
ANISOU 1622  O   HOH A 565     6396   5723   8563    393    216  -2870       O  
HETATM 1623  O   HOH A 566      15.737  -4.952  32.746  1.00 57.38           O  
ANISOU 1623  O   HOH A 566     8868   4596   8337   1355  -2188   -792       O  
HETATM 1624  O   HOH A 567      11.557   1.172   2.332  1.00 55.30           O  
ANISOU 1624  O   HOH A 567     8162   7154   5694   3843    925   1409       O  
HETATM 1625  O   HOH A 568      13.898   4.708  11.784  1.00 45.23           O  
ANISOU 1625  O   HOH A 568     8094   2816   6275  -1544  -1835    452       O  
HETATM 1626  O   HOH A 569      26.424 -18.928  19.160  1.00 55.93           O  
ANISOU 1626  O   HOH A 569     6268   5652   9329   -375   3484  -1534       O  
HETATM 1627  O   HOH A 570      41.258   2.106  14.104  1.00 62.06           O  
ANISOU 1627  O   HOH A 570     6748   9618   7213   3376    493  -2422       O  
HETATM 1628  O   HOH A 571      24.048  -7.191  36.606  1.00 60.37           O  
ANISOU 1628  O   HOH A 571     6742   8310   7884   2621   -659  -2956       O  
HETATM 1629  O   HOH A 572      27.176   0.649   0.007  1.00 52.92           O  
ANISOU 1629  O   HOH A 572     5058   8698   6350   -790    246   -682       O  
HETATM 1630  O   HOH A 573      27.199 -22.770   4.795  1.00107.20           O  
ANISOU 1630  O   HOH A 573     5581  15754  19394  -1868    305  -2275       O  
HETATM 1631  O   HOH A 574      28.781 -20.227   7.275  1.00 61.98           O  
ANISOU 1631  O   HOH A 574    10722   4839   7990   -933   2384  -1102       O  
HETATM 1632  O   HOH A 575      28.658   7.829  15.906  1.00 48.71           O  
ANISOU 1632  O   HOH A 575     3012   4836  10658    730    758   -141       O  
HETATM 1633  O   HOH A 576      18.505 -14.677  39.247  1.00 72.85           O  
ANISOU 1633  O   HOH A 576     7761   8739  11180   3299   -131   2327       O  
HETATM 1634  O   HOH A 577      11.750 -26.666  16.450  1.00 46.15           O  
ANISOU 1634  O   HOH A 577     4354   4521   8660  -1806    207  -1677       O  
HETATM 1635  O   HOH A 578      36.017 -14.341  22.602  1.00 55.70           O  
ANISOU 1635  O   HOH A 578     8379   5940   6844    562   1207    794       O  
HETATM 1636  O   HOH A 579      10.808  -3.917  33.251  1.00 55.43           O  
ANISOU 1636  O   HOH A 579     5962   6223   8877   -688   2024    -88       O  
HETATM 1637  O   HOH A 580       2.619 -11.636  26.801  1.00 46.83           O  
ANISOU 1637  O   HOH A 580     5003   6574   6217   1303   -301   1462       O  
HETATM 1638  O  AHOH A 581      37.233  -1.474  14.895  0.34 27.98           O  
ANISOU 1638  O  AHOH A 581     3774   2087   4771   1493   -165    144       O  
HETATM 1639  O  BHOH A 581      36.586  -3.204  13.943  0.19 24.72           O  
ANISOU 1639  O  BHOH A 581     2608   2632   4152   -947   1451   -507       O  
HETATM 1640  O  CHOH A 581      38.149  -2.693  15.010  0.46 39.83           O  
ANISOU 1640  O  CHOH A 581     2299   5446   7388    158    735  -1824       O  
HETATM 1641  O   HOH A 582      33.752 -17.090   5.549  1.00 65.67           O  
ANISOU 1641  O   HOH A 582     5353   8115  11485   3128   -241   -830       O  
HETATM 1642  O   HOH A 583      23.241  -9.425  -7.116  1.00 51.30           O  
ANISOU 1642  O   HOH A 583     7087   5707   6700    925   1450   1521       O  
HETATM 1643  O   HOH A 584      24.461 -17.996  15.560  1.00 37.84           O  
ANISOU 1643  O   HOH A 584     2852   4934   6592   1907     24   -488       O  
HETATM 1644  O   HOH A 585      36.972   5.287   7.600  1.00 68.82           O  
ANISOU 1644  O   HOH A 585     9128   5972  11050  -1243  -1407   4128       O  
HETATM 1645  O   HOH A 586      18.559 -11.989 -10.970  1.00 71.75           O  
ANISOU 1645  O   HOH A 586     6983   9027  11252   -728  -2640   2184       O  
HETATM 1646  O   HOH A 587      37.098   0.546   6.052  1.00106.33           O  
ANISOU 1646  O   HOH A 587    14485   8865  17051  -3616   3014   4321       O  
HETATM 1647  O   HOH A 588       9.059  -1.958  26.106  1.00 67.10           O  
ANISOU 1647  O   HOH A 588     5745  10003   9747  -2752  -2414  -2037       O  
HETATM 1648  O   HOH A 589       8.967  -0.120  22.243  1.00 54.62           O  
ANISOU 1648  O   HOH A 589     6223   7161   7368   1141   2110   -185       O  
HETATM 1649  O   HOH A 590      25.257 -12.306  -0.448  1.00 60.58           O  
ANISOU 1649  O   HOH A 590     6796   9181   7039   2397   1999   -950       O  
HETATM 1650  O   HOH A 591      12.633   6.030  19.683  1.00 57.84           O  
ANISOU 1650  O   HOH A 591     5110   7137   9728   1374   -114    538       O  
HETATM 1651  O   HOH A 592      24.253 -25.982   4.569  1.00 52.65           O  
ANISOU 1651  O   HOH A 592     7470   5686   6849   1325    489   1894       O  
HETATM 1652  O   HOH A 593      17.450   5.119  17.114  1.00 58.16           O  
ANISOU 1652  O   HOH A 593     5120   8331   8646  -1091    668   -769       O  
HETATM 1653  O   HOH A 594      32.796   6.759   5.322  1.00 60.06           O  
ANISOU 1653  O   HOH A 594     5479   7129  10211   1646  -1440   -429       O  
HETATM 1654  O   HOH A 595       8.167   4.442  14.741  1.00 51.05           O  
ANISOU 1654  O   HOH A 595     6682   5353   7363   1190   -361   -576       O  
HETATM 1655  O   HOH A 596      16.058   4.175   9.778  1.00 38.91           O  
ANISOU 1655  O   HOH A 596     2996   3586   8202   -996   1008    264       O  
HETATM 1656  O   HOH A 597      23.920 -26.978   7.041  1.00 69.23           O  
ANISOU 1656  O   HOH A 597     8000   6607  11696   -256    268   -662       O  
HETATM 1657  O   HOH A 598       7.638   2.162  17.321  1.00 44.97           O  
ANISOU 1657  O   HOH A 598     4383   4885   7819   2419    115  -1082       O  
HETATM 1658  O   HOH A 599       7.963  -3.137  34.200  1.00 78.08           O  
ANISOU 1658  O   HOH A 599     9745   7980  11942   3480  -1288  -2662       O  
HETATM 1659  O   HOH A 600      26.715   6.259  16.258  1.00 59.33           O  
ANISOU 1659  O   HOH A 600     3957   6706  11879   -636  -2175  -1046       O  
HETATM 1660  O   HOH A 601      30.665   5.864   8.473  1.00 56.72           O  
HETATM 1661  O   HOH A 602      28.493   4.723   5.226  1.00 75.73           O  
HETATM 1662  O   HOH A 603      18.783 -26.779   1.253  1.00 56.25           O  
ANISOU 1662  O   HOH A 603     6979   5993   8402     84    707   -689       O  
HETATM 1663  O   HOH A 604      24.462  -9.356  -3.417  1.00 64.94           O  
ANISOU 1663  O   HOH A 604     7512   9066   8095   -206   1951  -3238       O  
HETATM 1664  O   HOH A 605      21.107 -15.314   1.547  1.00 47.89           O  
ANISOU 1664  O   HOH A 605     3585   7087   7523    366   1111   -942       O  
HETATM 1665  O   HOH A 606      15.465 -11.427 -10.372  1.00 94.00           O  
ANISOU 1665  O   HOH A 606    13958   6627  15129  -3499   4249    422       O  
HETATM 1666  O   HOH A 607      17.875 -28.236   5.226  1.00 85.36           O  
ANISOU 1666  O   HOH A 607    11226   7003  14205   4849     78  -1150       O  
HETATM 1667  O   HOH A 608      23.256 -25.775   2.278  1.00 61.80           O  
ANISOU 1667  O   HOH A 608     7494   6855   9133   -362   -432   -652       O  
HETATM 1668  O   HOH A 609      17.755 -11.446  -5.785  1.00 71.90           O  
ANISOU 1668  O   HOH A 609     9970   6742  10605  -3364  -1958  -1451       O  
HETATM 1669  O   HOH A 610      19.764   5.870  15.687  1.00 52.29           O  
ANISOU 1669  O   HOH A 610     5865   5488   8517    202   -854   -358       O  
HETATM 1670  O   HOH A 611      18.703   0.000  27.325  0.42 24.23           O  
ANISOU 1670  O   HOH A 611     2481   1460   5267    -13     33    -30       O  
HETATM 1671  O   HOH A 612      35.138 -14.793  19.672  1.00 54.41           O  
ANISOU 1671  O   HOH A 612     5657   6211   8804    697  -1001   2579       O  
HETATM 1672  O   HOH A 613       6.188   5.339  12.524  1.00 71.46           O  
HETATM 1673  O   HOH A 614      27.074 -20.355   5.188  1.00 55.59           O  
ANISOU 1673  O   HOH A 614     5769   6438   8916   2342   2453   1432       O  
HETATM 1674  O   HOH A 615      22.111   6.702  13.295  1.00 57.89           O  
ANISOU 1674  O   HOH A 615    10487   4479   7030  -2969    510   -868       O  
HETATM 1675  O   HOH A 616      37.073   4.672  17.441  1.00 67.23           O  
ANISOU 1675  O   HOH A 616     7140   8212  10191  -1480   -205    261       O  
HETATM 1676  O   HOH A 617       5.988 -10.107  29.367  1.00 55.47           O  
ANISOU 1676  O   HOH A 617     5712   7294   8069  -1026    849   2918       O  
HETATM 1677  O   HOH A 618      17.944   5.545  11.732  1.00 49.09           O  
ANISOU 1677  O   HOH A 618     7817   3875   6960  -2610  -1295   1201       O  
HETATM 1678  O   HOH A 619       9.837  -8.468  -1.121  1.00 54.72           O  
ANISOU 1678  O   HOH A 619     7412   5810   7569   1589  -3248  -1713       O  
HETATM 1679  O   HOH A 620      21.253 -26.255   0.813  1.00 58.91           O  
ANISOU 1679  O   HOH A 620     6347   7838   8197    176     50   -898       O  
HETATM 1680  O   HOH A 621      26.951 -17.448   0.021  1.00 49.13           O  
ANISOU 1680  O   HOH A 621     6238   4997   7435    307    710  -2156       O  
HETATM 1681  O   HOH A 622      21.445 -24.682  -1.039  1.00 59.62           O  
ANISOU 1681  O   HOH A 622     5495   7689   9468   1667   1865   2359       O  
HETATM 1682  O   HOH A 623      42.315  -0.705  15.214  1.00 55.22           O  
ANISOU 1682  O   HOH A 623     6511   6211   8258  -1781   3148  -2767       O  
HETATM 1683  O   HOH A 624      23.079 -10.643  -5.093  1.00 68.85           O  
ANISOU 1683  O   HOH A 624     7857   8447   9857   -222   2775  -1997       O  
HETATM 1684  O   HOH A 625      37.898   8.635  14.089  1.00 55.39           O  
ANISOU 1684  O   HOH A 625     7090   5342   8615   1548   2236    813       O  
HETATM 1685  O   HOH A 626      16.785   6.483  14.500  1.00 57.71           O  
ANISOU 1685  O   HOH A 626     7611   4767   9550    809   1186    199       O  
HETATM 1686  O   HOH A 627      22.694   0.001  27.327  0.50 24.21           O  
ANISOU 1686  O   HOH A 627     1787   3114   4298    -11     -1   -777       O  
HETATM 1687  O   HOH A 628      18.909 -12.610  -8.356  1.00 59.87           O  
ANISOU 1687  O   HOH A 628     3905   7654  11189   -927   1617  -1837       O  
HETATM 1688  O   HOH A 629      34.142 -20.159   8.778  1.00 70.57           O  
ANISOU 1688  O   HOH A 629     6866   8449  11498   1384   2029   2867       O  
HETATM 1689  O   HOH A 630      23.773 -12.701  -6.901  1.00 67.80           O  
ANISOU 1689  O   HOH A 630     7016   9422   9322    826    602   1536       O  
CONECT  214 1404                                                                
CONECT  215 1404                                                                
CONECT  496 1403                                                                
CONECT  578 1401                                                                
CONECT  590 1401                                                                
CONECT  631 1402                                                                
CONECT  636 1402                                                                
CONECT  649 1402                                                                
CONECT  661 1402                                                                
CONECT  688 1401                                                                
CONECT  733 1403                                                                
CONECT  745 1403                                                                
CONECT  761 1403                                                                
CONECT  774 1401                                                                
CONECT  796 1402                                                                
CONECT  800 1404                                                                
CONECT  803 1404                                                                
CONECT  816 1404                                                                
CONECT  821 1402                                                                
CONECT  974 1400                                                                
CONECT 1008 1400                                                                
CONECT 1059 1400                                                                
CONECT 1372 1373                                                                
CONECT 1373 1372 1374 1375 1388                                                 
CONECT 1374 1373                                                                
CONECT 1375 1373 1376 1380                                                      
CONECT 1376 1375 1377                                                           
CONECT 1377 1376 1378 1379                                                      
CONECT 1378 1377                                                                
CONECT 1379 1377                                                                
CONECT 1380 1375 1381 1384                                                      
CONECT 1381 1380 1382 1383                                                      
CONECT 1382 1381                                                                
CONECT 1383 1381                                                                
CONECT 1384 1380 1385 1386                                                      
CONECT 1385 1384 1400                                                           
CONECT 1386 1384 1387                                                           
CONECT 1387 1386 1400                                                           
CONECT 1388 1373 1389 1393                                                      
CONECT 1389 1388 1390                                                           
CONECT 1390 1389 1391                                                           
CONECT 1391 1390 1392 1394                                                      
CONECT 1392 1391 1393                                                           
CONECT 1393 1388 1392                                                           
CONECT 1394 1391 1395 1399                                                      
CONECT 1395 1394 1396                                                           
CONECT 1396 1395 1397                                                           
CONECT 1397 1396 1398                                                           
CONECT 1398 1397 1399                                                           
CONECT 1399 1394 1398                                                           
CONECT 1400  974 1008 1059 1385                                                 
CONECT 1400 1387                                                                
CONECT 1401  578  590  688  774                                                 
CONECT 1402  631  636  649  661                                                 
CONECT 1402  796  821                                                           
CONECT 1403  496  733  745  761                                                 
CONECT 1403 1465 1502                                                           
CONECT 1404  214  215  800  803                                                 
CONECT 1404  816 1566 1570                                                      
CONECT 1405 1406 1407 1408                                                      
CONECT 1406 1405                                                                
CONECT 1407 1405                                                                
CONECT 1408 1405                                                                
CONECT 1409 1410 1411 1412                                                      
CONECT 1410 1409                                                                
CONECT 1411 1409                                                                
CONECT 1412 1409                                                                
CONECT 1413 1414 1415                                                           
CONECT 1414 1413                                                                
CONECT 1415 1413 1416                                                           
CONECT 1416 1415                                                                
CONECT 1417 1418 1419                                                           
CONECT 1418 1417                                                                
CONECT 1419 1417 1420                                                           
CONECT 1420 1419                                                                
CONECT 1421 1422 1423                                                           
CONECT 1422 1421                                                                
CONECT 1423 1421 1424                                                           
CONECT 1424 1423                                                                
CONECT 1425 1426 1427                                                           
CONECT 1426 1425                                                                
CONECT 1427 1425 1428                                                           
CONECT 1428 1427                                                                
CONECT 1429 1430 1431                                                           
CONECT 1430 1429                                                                
CONECT 1431 1429 1432 1433                                                      
CONECT 1432 1431                                                                
CONECT 1433 1431 1434                                                           
CONECT 1434 1433                                                                
CONECT 1435 1436 1438                                                           
CONECT 1436 1435 1437 1439                                                      
CONECT 1437 1436                                                                
CONECT 1438 1435                                                                
CONECT 1439 1436                                                                
CONECT 1440 1441 1443                                                           
CONECT 1441 1440 1442 1444                                                      
CONECT 1442 1441                                                                
CONECT 1443 1440                                                                
CONECT 1444 1441                                                                
CONECT 1445 1447                                                                
CONECT 1446 1447                                                                
CONECT 1447 1445 1446 1449                                                      
CONECT 1448 1449                                                                
CONECT 1449 1447 1448 1450                                                      
CONECT 1450 1449                                                                
CONECT 1465 1403                                                                
CONECT 1502 1403                                                                
CONECT 1566 1404                                                                
CONECT 1570 1404                                                                
MASTER      381    0   16    3    7    0   27    6 1558    1  109   13          
END                                                                             



If you find results from this site helpful for your research, please cite one of our papers:

elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.