path: root/plip/test/pdb/4rdl.pdb

HEADER    VIRAL PROTEIN                           19-SEP-14   4RDL              
TITLE     CRYSTAL STRUCTURE OF NOROVIRUS BOXER P DOMAIN IN COMPLEX WITH LEWIS Y 
TITLE    2 TETRASACCHARIDE                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAPSID;                                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: PROTRUSION DOMAIN, UNP RESIDUES 227-526;                   
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HUMAN CALICIVIRUS NLV/BOXER/2001/US;            
SOURCE   3 ORGANISM_TAXID: 207658;                                              
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1                                 
KEYWDS    MIXED ALPHA/BETA STRUCTURE, RECEPTOR BINDING, HBGA, VIRUS CAPSID,     
KEYWDS   2 VIRAL PROTEIN                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.HAO,Y.CHEN,M.XIA,W.LIU,M.TAN,X.JIANG,X.LI                           
REVDAT   1   14-JAN-15 4RDL    0                                                
JRNL        AUTH   N.HAO,Y.CHEN,M.XIA,M.TAN,W.LIU,X.GUAN,X.JIANG,X.LI,Z.RAO     
JRNL        TITL   CRYSTAL STRUCTURES OF GI.8 BOXER VIRUS P DIMERS IN COMPLEX   
JRNL        TITL 2 WITH HBGAS, A NOVEL EVOLUTIONARY PATH SELECTED BY THE LEWIS  
JRNL        TITL 3 EPITOPE                                                      
JRNL        REF    PROTEIN CELL                               2014              
JRNL        REFN                   ESSN 1674-8018                               
JRNL        PMID   25547362                                                     
JRNL        DOI    10.1007/S13238-014-0126-0                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_650)                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.70                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 129411                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.131                           
REMARK   3   R VALUE            (WORKING SET) : 0.130                           
REMARK   3   FREE R VALUE                     : 0.151                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6496                            
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 47.7266 -  4.5013    1.00     4215   228  0.1669 0.1666        
REMARK   3     2  4.5013 -  3.5732    1.00     4159   217  0.1332 0.1392        
REMARK   3     3  3.5732 -  3.1216    1.00     4130   213  0.1385 0.1473        
REMARK   3     4  3.1216 -  2.8362    1.00     4125   211  0.1456 0.1668        
REMARK   3     5  2.8362 -  2.6330    1.00     4142   220  0.1482 0.1574        
REMARK   3     6  2.6330 -  2.4777    1.00     4087   216  0.1407 0.1605        
REMARK   3     7  2.4777 -  2.3536    1.00     4137   213  0.1335 0.1483        
REMARK   3     8  2.3536 -  2.2512    1.00     4067   217  0.1226 0.1546        
REMARK   3     9  2.2512 -  2.1645    1.00     4134   203  0.1246 0.1293        
REMARK   3    10  2.1645 -  2.0898    1.00     4082   216  0.1285 0.1517        
REMARK   3    11  2.0898 -  2.0245    1.00     4107   209  0.1233 0.1446        
REMARK   3    12  2.0245 -  1.9666    1.00     4103   207  0.1250 0.1678        
REMARK   3    13  1.9666 -  1.9148    1.00     4065   230  0.1196 0.1582        
REMARK   3    14  1.9148 -  1.8681    1.00     4088   236  0.1168 0.1467        
REMARK   3    15  1.8681 -  1.8257    1.00     4095   211  0.1045 0.1168        
REMARK   3    16  1.8257 -  1.7868    1.00     4117   201  0.0988 0.1366        
REMARK   3    17  1.7868 -  1.7511    1.00     4057   245  0.0995 0.1272        
REMARK   3    18  1.7511 -  1.7180    1.00     4032   238  0.0954 0.1247        
REMARK   3    19  1.7180 -  1.6873    1.00     4101   236  0.0950 0.1404        
REMARK   3    20  1.6873 -  1.6587    1.00     4055   229  0.0992 0.1537        
REMARK   3    21  1.6587 -  1.6320    1.00     4033   211  0.1037 0.1392        
REMARK   3    22  1.6320 -  1.6069    1.00     4174   183  0.1037 0.1389        
REMARK   3    23  1.6069 -  1.5832    1.00     4042   218  0.1086 0.1504        
REMARK   3    24  1.5832 -  1.5609    1.00     4070   228  0.1116 0.1621        
REMARK   3    25  1.5609 -  1.5398    1.00     4101   207  0.1111 0.1568        
REMARK   3    26  1.5398 -  1.5198    1.00     4095   193  0.1157 0.1512        
REMARK   3    27  1.5198 -  1.5008    1.00     4080   215  0.1188 0.1718        
REMARK   3    28  1.5008 -  1.4828    1.00     4073   213  0.1232 0.1458        
REMARK   3    29  1.4828 -  1.4655    1.00     4096   223  0.1307 0.1737        
REMARK   3    30  1.4655 -  1.4490    1.00     4053   209  0.1532 0.1929        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.83                                          
REMARK   3   K_SOL              : 0.33                                          
REMARK   3   B_SOL              : 38.40                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.140            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 12.430           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.62560                                              
REMARK   3    B22 (A**2) : 1.62560                                              
REMARK   3    B33 (A**2) : -3.25120                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  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           4822                                  
REMARK   3   ANGLE     :  1.140           6612                                  
REMARK   3   CHIRALITY :  0.075            746                                  
REMARK   3   PLANARITY :  0.005            870                                  
REMARK   3   DIHEDRAL  : 11.841           1702                                  
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 4RDL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-OCT-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB087213.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-AUG-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 129481                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.449                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 11.100                             
REMARK 200  R MERGE                    (I) : 0.09500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 27.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.48                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.00                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.47300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4RDJ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M LICL, 18%(W/V) PEG 3350, 10%(V/V)   
REMARK 280  MPD, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
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       21.67333            
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       43.34667            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       32.51000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       54.18333            
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       10.83667            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6210 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22860 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 4.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   219                                                      
REMARK 465     PRO A   220                                                      
REMARK 465     LEU A   221                                                      
REMARK 465     GLY A   222                                                      
REMARK 465     SER A   223                                                      
REMARK 465     PRO A   224                                                      
REMARK 465     GLU A   225                                                      
REMARK 465     PHE A   226                                                      
REMARK 465     GLN A   227                                                      
REMARK 465     ARG A   228                                                      
REMARK 465     THR A   229                                                      
REMARK 465     GLY B   219                                                      
REMARK 465     PRO B   220                                                      
REMARK 465     LEU B   221                                                      
REMARK 465     GLY B   222                                                      
REMARK 465     SER B   223                                                      
REMARK 465     PRO B   224                                                      
REMARK 465     GLU B   225                                                      
REMARK 465     PHE B   226                                                      
REMARK 465     GLN B   227                                                      
REMARK 465     ARG B   228                                                      
REMARK 465     THR B   229                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B  1060     O    HOH B  1104              1.87            
REMARK 500   O    HOH B  1024     O    HOH B  1051              1.88            
REMARK 500   O    HOH B  1039     O    HOH B  1047              1.89            
REMARK 500   O    HOH B  1107     O    HOH B  1111              1.89            
REMARK 500   O    HOH A   878     O    HOH A  1052              1.96            
REMARK 500   O    HOH A   737     O    HOH A   967              2.00            
REMARK 500   O    HOH A  1095     O    HOH A  1101              2.03            
REMARK 500   O    HOH B  1064     O    HOH B  1070              2.03            
REMARK 500   O    HOH A  1043     O    HOH A  1057              2.05            
REMARK 500   O    HOH B  1057     O    HOH B  1062              2.05            
REMARK 500   O    HOH B  1046     O    HOH B  1111              2.06            
REMARK 500   O    HOH B  1028     O    HOH B  1043              2.06            
REMARK 500   O    HOH B  1017     O    HOH B  1066              2.06            
REMARK 500   O    HOH B   758     O    HOH B  1104              2.13            
REMARK 500   O    HOH B  1034     O    HOH B  1067              2.15            
REMARK 500   OE1  GLU B   385     O    HOH B   976              2.17            
REMARK 500   O    HOH A  1082     O    HOH B  1101              2.17            
REMARK 500   O    HOH A  1078     O    HOH B  1081              2.17            
REMARK 500   O    HOH A   966     O    HOH A  1056              2.18            
REMARK 500   OE1  GLU A   377     O    HOH A   862              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 236       58.32    -93.38                                   
REMARK 500    GLN A 265       49.70   -141.79                                   
REMARK 500    THR A 282     -168.51   -130.00                                   
REMARK 500    SER A 358       53.71    -90.79                                   
REMARK 500    ASP A 360      158.65     74.59                                   
REMARK 500    SER A 411     -139.32     54.27                                   
REMARK 500    SER A 443      -15.51     91.05                                   
REMARK 500    ASN A 444       74.77   -156.62                                   
REMARK 500    PRO A 445       43.30    -83.29                                   
REMARK 500    ASN B 236       55.75    -90.67                                   
REMARK 500    GLN B 265       51.40   -143.07                                   
REMARK 500    ASP B 360      159.38     74.64                                   
REMARK 500    LEU B 413     -116.33     46.02                                   
REMARK 500    SER B 443       -6.74     91.47                                   
REMARK 500    ASN B 444       66.22   -162.92                                   
REMARK 500    PRO B 445       43.46    -84.12                                   
REMARK 500    ASN B 500     -159.18   -122.67                                   
REMARK 500    ALA B 501      -71.43    -55.33                                   
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 A1073        DISTANCE =  5.02 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF POLYSACCHARIDE         
REMARK 800  RESIDUES 601 TO 604                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF POLYSACCHARIDE         
REMARK 800  RESIDUES 601 TO 604                                                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4RDJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4RDK   RELATED DB: PDB                                   
DBREF  4RDL A  227   526  UNP    Q8BCA3   Q8BCA3_9CALI   227    526             
DBREF  4RDL B  227   526  UNP    Q8BCA3   Q8BCA3_9CALI   227    526             
SEQADV 4RDL GLY A  219  UNP  Q8BCA3              EXPRESSION TAG                 
SEQADV 4RDL PRO A  220  UNP  Q8BCA3              EXPRESSION TAG                 
SEQADV 4RDL LEU A  221  UNP  Q8BCA3              EXPRESSION TAG                 
SEQADV 4RDL GLY A  222  UNP  Q8BCA3              EXPRESSION TAG                 
SEQADV 4RDL SER A  223  UNP  Q8BCA3              EXPRESSION TAG                 
SEQADV 4RDL PRO A  224  UNP  Q8BCA3              EXPRESSION TAG                 
SEQADV 4RDL GLU A  225  UNP  Q8BCA3              EXPRESSION TAG                 
SEQADV 4RDL PHE A  226  UNP  Q8BCA3              EXPRESSION TAG                 
SEQADV 4RDL GLY B  219  UNP  Q8BCA3              EXPRESSION TAG                 
SEQADV 4RDL PRO B  220  UNP  Q8BCA3              EXPRESSION TAG                 
SEQADV 4RDL LEU B  221  UNP  Q8BCA3              EXPRESSION TAG                 
SEQADV 4RDL GLY B  222  UNP  Q8BCA3              EXPRESSION TAG                 
SEQADV 4RDL SER B  223  UNP  Q8BCA3              EXPRESSION TAG                 
SEQADV 4RDL PRO B  224  UNP  Q8BCA3              EXPRESSION TAG                 
SEQADV 4RDL GLU B  225  UNP  Q8BCA3              EXPRESSION TAG                 
SEQADV 4RDL PHE B  226  UNP  Q8BCA3              EXPRESSION TAG                 
SEQRES   1 A  308  GLY PRO LEU GLY SER PRO GLU PHE GLN ARG THR LYS PRO          
SEQRES   2 A  308  PHE SER VAL PRO ASN ILE PRO MET ASN LEU MET SER ASN          
SEQRES   3 A  308  SER ARG VAL PRO MET LEU ILE ASP GLY MET MET VAL SER          
SEQRES   4 A  308  ASN ASP GLN ASN GLN VAL PRO GLN PHE GLN ASN GLY ARG          
SEQRES   5 A  308  VAL THR LEU ASP GLY GLN LEU GLN GLY THR THR THR VAL          
SEQRES   6 A  308  SER ALA ALA CYS ILE ALA ARG MET ARG GLY ARG ILE PHE          
SEQRES   7 A  308  ASN ASN ASN GLY ASN TYR GLY VAL ASN LEU ALA GLU LEU          
SEQRES   8 A  308  ASP GLY ASN PRO TYR HIS ALA PHE ASP SER PRO ALA PRO          
SEQRES   9 A  308  LEU GLY PHE PRO ASP PHE GLY ASN CYS ASP LEU HIS MET          
SEQRES  10 A  308  THR PHE VAL LYS ILE ASN PRO THR GLU LEU SER THR GLY          
SEQRES  11 A  308  ASP PRO SER GLY LYS VAL VAL ILE HIS SER TYR ASP ALA          
SEQRES  12 A  308  THR PHE ALA PRO HIS LEU GLY THR VAL LYS LEU GLU ASP          
SEQRES  13 A  308  ASN ASN GLU LEU ASP GLN PHE VAL GLY LYS GLU VAL VAL          
SEQRES  14 A  308  LEU GLU LEU THR TRP VAL SER ASN ARG THR GLY ALA THR          
SEQRES  15 A  308  LEU ASN LEU TRP ALA VAL PRO ASN TYR GLY SER ASN LEU          
SEQRES  16 A  308  THR GLN ALA SER GLN LEU ALA PRO PRO ILE TYR PRO PRO          
SEQRES  17 A  308  GLY PHE GLY GLU ALA ILE VAL TYR PHE THR SER THR PHE          
SEQRES  18 A  308  PRO THR VAL SER ASN PRO LYS VAL PRO CYS THR LEU PRO          
SEQRES  19 A  308  GLN GLU PHE VAL SER HIS PHE VAL ASN GLU GLN ALA PRO          
SEQRES  20 A  308  THR ARG GLY ASP ALA ALA LEU LEU HIS TYR VAL ASP PRO          
SEQRES  21 A  308  ASP THR HIS ARG ASN LEU GLY GLU PHE LYS MET TYR PRO          
SEQRES  22 A  308  GLU GLY TYR MET THR CYS VAL PRO ASN ALA GLY GLY GLY          
SEQRES  23 A  308  PRO GLN THR LEU PRO ILE ASN GLY VAL PHE VAL PHE ILE          
SEQRES  24 A  308  SER TRP VAL SER ARG TYR TYR GLN LEU                          
SEQRES   1 B  308  GLY PRO LEU GLY SER PRO GLU PHE GLN ARG THR LYS PRO          
SEQRES   2 B  308  PHE SER VAL PRO ASN ILE PRO MET ASN LEU MET SER ASN          
SEQRES   3 B  308  SER ARG VAL PRO MET LEU ILE ASP GLY MET MET VAL SER          
SEQRES   4 B  308  ASN ASP GLN ASN GLN VAL PRO GLN PHE GLN ASN GLY ARG          
SEQRES   5 B  308  VAL THR LEU ASP GLY GLN LEU GLN GLY THR THR THR VAL          
SEQRES   6 B  308  SER ALA ALA CYS ILE ALA ARG MET ARG GLY ARG ILE PHE          
SEQRES   7 B  308  ASN ASN ASN GLY ASN TYR GLY VAL ASN LEU ALA GLU LEU          
SEQRES   8 B  308  ASP GLY ASN PRO TYR HIS ALA PHE ASP SER PRO ALA PRO          
SEQRES   9 B  308  LEU GLY PHE PRO ASP PHE GLY ASN CYS ASP LEU HIS MET          
SEQRES  10 B  308  THR PHE VAL LYS ILE ASN PRO THR GLU LEU SER THR GLY          
SEQRES  11 B  308  ASP PRO SER GLY LYS VAL VAL ILE HIS SER TYR ASP ALA          
SEQRES  12 B  308  THR PHE ALA PRO HIS LEU GLY THR VAL LYS LEU GLU ASP          
SEQRES  13 B  308  ASN ASN GLU LEU ASP GLN PHE VAL GLY LYS GLU VAL VAL          
SEQRES  14 B  308  LEU GLU LEU THR TRP VAL SER ASN ARG THR GLY ALA THR          
SEQRES  15 B  308  LEU ASN LEU TRP ALA VAL PRO ASN TYR GLY SER ASN LEU          
SEQRES  16 B  308  THR GLN ALA SER GLN LEU ALA PRO PRO ILE TYR PRO PRO          
SEQRES  17 B  308  GLY PHE GLY GLU ALA ILE VAL TYR PHE THR SER THR PHE          
SEQRES  18 B  308  PRO THR VAL SER ASN PRO LYS VAL PRO CYS THR LEU PRO          
SEQRES  19 B  308  GLN GLU PHE VAL SER HIS PHE VAL ASN GLU GLN ALA PRO          
SEQRES  20 B  308  THR ARG GLY ASP ALA ALA LEU LEU HIS TYR VAL ASP PRO          
SEQRES  21 B  308  ASP THR HIS ARG ASN LEU GLY GLU PHE LYS MET TYR PRO          
SEQRES  22 B  308  GLU GLY TYR MET THR CYS VAL PRO ASN ALA GLY GLY GLY          
SEQRES  23 B  308  PRO GLN THR LEU PRO ILE ASN GLY VAL PHE VAL PHE ILE          
SEQRES  24 B  308  SER TRP VAL SER ARG TYR TYR GLN LEU                          
HET    FUC  A 601      10                                                       
HET    GAL  A 602      11                                                       
HET    NDG  A 603      15                                                       
HET    FUC  A 604      10                                                       
HET    FUC  B 601      10                                                       
HET    GAL  B 602      11                                                       
HET    NDG  B 603      15                                                       
HET    FUC  B 604      10                                                       
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     GAL BETA-D-GALACTOSE                                                 
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE                        
FORMUL   3  FUC    4(C6 H12 O5)                                                 
FORMUL   3  GAL    2(C6 H12 O6)                                                 
FORMUL   3  NDG    2(C8 H15 N O6)                                               
FORMUL   5  HOH   *825(H2 O)                                                    
HELIX    1   1 PRO A  238  MET A  242  5                                   5    
HELIX    2   2 SER A  284  ILE A  288  5                                   5    
HELIX    3   3 ASN A  341  LEU A  345  5                                   5    
HELIX    4   4 PRO A  365  LEU A  367  5                                   3    
HELIX    5   5 LEU A  378  VAL A  382  5                                   5    
HELIX    6   6 PRO A  452  GLN A  463  1                                  12    
HELIX    7   7 PRO B  238  MET B  242  5                                   5    
HELIX    8   8 SER B  284  ILE B  288  5                                   5    
HELIX    9   9 ASN B  341  LEU B  345  5                                   5    
HELIX   10  10 PRO B  365  LEU B  367  5                                   3    
HELIX   11  11 LEU B  378  VAL B  382  5                                   5    
HELIX   12  12 PRO B  452  GLN B  463  1                                  12    
HELIX   13  13 GLY B  504  LEU B  508  5                                   5    
SHEET    1   A 3 GLY A 253  VAL A 256  0                                        
SHEET    2   A 3 ALA A 431  THR A 438 -1  O  TYR A 434   N  MET A 255           
SHEET    3   A 3 LYS A 446  CYS A 449 -1  O  VAL A 447   N  SER A 437           
SHEET    1   B 6 GLY A 253  VAL A 256  0                                        
SHEET    2   B 6 ALA A 431  THR A 438 -1  O  TYR A 434   N  MET A 255           
SHEET    3   B 6 TYR A 494  CYS A 497 -1  O  MET A 495   N  VAL A 433           
SHEET    4   B 6 ASN A 483  TYR A 490 -1  N  TYR A 490   O  TYR A 494           
SHEET    5   B 6 ALA A 470  VAL A 476 -1  N  TYR A 475   O  LEU A 484           
SHEET    6   B 6 VAL A 513  VAL A 520 -1  O  VAL A 513   N  VAL A 476           
SHEET    1   C 7 SER A 351  HIS A 357  0                                        
SHEET    2   C 7 CYS A 331  LYS A 339 -1  N  MET A 335   O  VAL A 354           
SHEET    3   C 7 GLU A 385  ASN A 395 -1  O  SER A 394   N  ASP A 332           
SHEET    4   C 7 ARG A 290  ASN A 298 -1  N  MET A 291   O  LEU A 388           
SHEET    5   C 7 ASN A 301  ALA A 307 -1  O  ASN A 301   N  ASN A 298           
SHEET    6   C 7 THR A 369  LEU A 372 -1  O  VAL A 370   N  VAL A 304           
SHEET    7   C 7 PHE A 363  ALA A 364 -1  N  ALA A 364   O  THR A 369           
SHEET    1   D 3 GLY B 253  MET B 255  0                                        
SHEET    2   D 3 TYR B 434  THR B 438 -1  O  TYR B 434   N  MET B 255           
SHEET    3   D 3 LYS B 446  CYS B 449 -1  O  VAL B 447   N  SER B 437           
SHEET    1   E 7 SER B 351  HIS B 357  0                                        
SHEET    2   E 7 CYS B 331  LYS B 339 -1  N  MET B 335   O  VAL B 354           
SHEET    3   E 7 GLU B 385  ASN B 395 -1  O  GLU B 389   N  THR B 336           
SHEET    4   E 7 ARG B 290  ASN B 298 -1  N  GLY B 293   O  VAL B 386           
SHEET    5   E 7 ASN B 301  ALA B 307 -1  O  ASN B 301   N  ASN B 298           
SHEET    6   E 7 THR B 369  LEU B 372 -1  O  LEU B 372   N  TYR B 302           
SHEET    7   E 7 PHE B 363  ALA B 364 -1  N  ALA B 364   O  THR B 369           
SHEET    1   F 5 ALA B 431  ILE B 432  0                                        
SHEET    2   F 5 TYR B 494  CYS B 497 -1  O  CYS B 497   N  ALA B 431           
SHEET    3   F 5 ASN B 483  TYR B 490 -1  N  LYS B 488   O  THR B 496           
SHEET    4   F 5 ALA B 470  VAL B 476 -1  N  TYR B 475   O  LEU B 484           
SHEET    5   F 5 VAL B 513  VAL B 520 -1  O  SER B 518   N  LEU B 472           
LINK         C1  FUC A 601                 O2  GAL A 602     1555   1555  1.39  
LINK         C1  FUC B 601                 O2  GAL B 602     1555   1555  1.43  
LINK         C1  GAL B 602                 O4  NDG B 603     1555   1555  1.37  
LINK         O3  NDG B 603                 C1  FUC B 604     1555   1555  1.39  
LINK         C1  GAL A 602                 O4  NDG A 603     1555   1555  1.40  
LINK         O3  NDG A 603                 C1  FUC A 604     1555   1555  1.41  
SITE     1 AC1 20 ASP A 332  HIS A 334  TRP A 392  SER A 394                    
SITE     2 AC1 20 ASN A 395  THR A 397  VAL A 442  ASP A 477                    
SITE     3 AC1 20 HOH A 716  HOH A 849  HOH A 855  HOH A 861                    
SITE     4 AC1 20 HOH A 901  HOH A 909  HOH A1053  HOH A1054                    
SITE     5 AC1 20 THR B 347  GLY B 348  ASP B 349  HOH B 805                    
SITE     1 AC2 17 THR A 347  GLY A 348  ASP A 349  HOH A 808                    
SITE     2 AC2 17 HOH A 957  ASP B 332  HIS B 334  SER B 394                    
SITE     3 AC2 17 ASN B 395  THR B 397  VAL B 442  HOH B 738                    
SITE     4 AC2 17 HOH B 800  HOH B 813  HOH B 824  HOH B 893                    
SITE     5 AC2 17 HOH B1081                                                     
CRYST1  140.390  140.390   65.020  90.00  90.00 120.00 P 61         12          
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      0.007123  0.004112  0.000000        0.00000                         
SCALE2      0.000000  0.008225  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015380        0.00000                         
ATOM      1  N   LYS A 230      32.874  -7.255  -1.930  1.00 43.09           N  
ANISOU    1  N   LYS A 230     4814   5458   6101   -327  -1881    756       N  
ATOM      2  CA  LYS A 230      34.227  -6.964  -2.393  1.00 41.33           C  
ANISOU    2  CA  LYS A 230     4705   5361   5636   -224  -2051    850       C  
ATOM      3  C   LYS A 230      35.262  -7.795  -1.640  1.00 36.05           C  
ANISOU    3  C   LYS A 230     4151   4780   4764   -702  -2164    586       C  
ATOM      4  O   LYS A 230      35.293  -7.787  -0.409  1.00 35.34           O  
ANISOU    4  O   LYS A 230     4033   4707   4687  -1009  -2109    446       O  
ATOM      5  CB  LYS A 230      34.538  -5.474  -2.242  1.00 43.87           C  
ANISOU    5  CB  LYS A 230     5131   5440   6097    235  -2144    793       C  
ATOM      6  CG  LYS A 230      35.816  -5.033  -2.942  1.00 47.80           C  
ANISOU    6  CG  LYS A 230     5532   5726   6905    714  -1985    480       C  
ATOM      7  CD  LYS A 230      35.925  -3.516  -2.993  1.00 51.37           C  
ANISOU    7  CD  LYS A 230     5906   5870   7742    956  -1738    -24       C  
ATOM      8  CE  LYS A 230      36.989  -3.072  -3.983  1.00 53.92           C  
ANISOU    8  CE  LYS A 230     6154   6008   8326   1237  -1728   -462       C  
ATOM      9  NZ  LYS A 230      37.100  -1.585  -4.074  1.00 54.82           N  
ANISOU    9  NZ  LYS A 230     6280   6026   8521   1384  -1867   -729       N  
ATOM     10  N   PRO A 231      36.109  -8.521  -2.382  1.00 31.74           N  
ANISOU   10  N   PRO A 231     3795   4132   4131   -877  -2114    270       N  
ATOM     11  CA  PRO A 231      37.158  -9.356  -1.790  1.00 28.40           C  
ANISOU   11  CA  PRO A 231     3467   3636   3686  -1082  -1686    522       C  
ATOM     12  C   PRO A 231      38.218  -8.528  -1.071  1.00 24.06           C  
ANISOU   12  C   PRO A 231     2903   3029   3208  -1165  -1426    852       C  
ATOM     13  O   PRO A 231      38.663  -7.495  -1.580  1.00 26.23           O  
ANISOU   13  O   PRO A 231     3088   3207   3672  -1053  -1424   1324       O  
ATOM     14  CB  PRO A 231      37.783 -10.051  -3.005  1.00 30.68           C  
ANISOU   14  CB  PRO A 231     3731   3817   4107   -923  -1627    103       C  
ATOM     15  CG  PRO A 231      36.752  -9.971  -4.070  1.00 32.27           C  
ANISOU   15  CG  PRO A 231     3947   4325   3988   -385  -1684    549       C  
ATOM     16  CD  PRO A 231      36.050  -8.671  -3.845  1.00 33.15           C  
ANISOU   16  CD  PRO A 231     3995   4341   4257   -431  -1563    669       C  
ATOM     17  N   PHE A 232      38.610  -8.989   0.110  1.00 20.43           N  
ANISOU   17  N   PHE A 232     2276   2627   2858  -1072  -1152    673       N  
ATOM     18  CA  PHE A 232      39.687  -8.369   0.866  1.00 17.97           C  
ANISOU   18  CA  PHE A 232     1930   2086   2812   -863   -869    491       C  
ATOM     19  C   PHE A 232      41.016  -8.547   0.137  1.00 16.47           C  
ANISOU   19  C   PHE A 232     2085   1603   2570   -631   -466    675       C  
ATOM     20  O   PHE A 232      41.208  -9.510  -0.603  1.00 17.79           O  
ANISOU   20  O   PHE A 232     2288   1445   3024   -499   -817    295       O  
ATOM     21  CB  PHE A 232      39.761  -8.990   2.266  1.00 16.61           C  
ANISOU   21  CB  PHE A 232     1862   1869   2579   -762   -552    719       C  
ATOM     22  CG  PHE A 232      40.836  -8.407   3.131  1.00 16.12           C  
ANISOU   22  CG  PHE A 232     1877   1646   2601   -786   -399    160       C  
ATOM     23  CD1 PHE A 232      40.678  -7.158   3.709  1.00 16.43           C  
ANISOU   23  CD1 PHE A 232     1944   1769   2528   -631    -49    197       C  
ATOM     24  CD2 PHE A 232      42.008  -9.109   3.367  1.00 15.42           C  
ANISOU   24  CD2 PHE A 232     1911   1538   2410   -661   -150    481       C  
ATOM     25  CE1 PHE A 232      41.677  -6.616   4.504  1.00 17.04           C  
ANISOU   25  CE1 PHE A 232     2135   1824   2516   -589    130    411       C  
ATOM     26  CE2 PHE A 232      43.006  -8.575   4.160  1.00 15.21           C  
ANISOU   26  CE2 PHE A 232     2070   1631   2076   -688   -434    184       C  
ATOM     27  CZ  PHE A 232      42.840  -7.326   4.730  1.00 15.16           C  
ANISOU   27  CZ  PHE A 232     2118   1456   2186   -726   -191    123       C  
ATOM     28  N   SER A 233      41.927  -7.605   0.341  1.00 14.62           N  
ANISOU   28  N   SER A 233     1659   1440   2454   -671   -461    448       N  
ATOM     29  CA  SER A 233      43.270  -7.693  -0.215  1.00 13.95           C  
ANISOU   29  CA  SER A 233     1845   1416   2039   -506   -290    202       C  
ATOM     30  C   SER A 233      44.175  -6.764   0.571  1.00 12.32           C  
ANISOU   30  C   SER A 233     1767   1256   1658   -269   -531    -53       C  
ATOM     31  O   SER A 233      43.700  -5.898   1.310  1.00 12.92           O  
ANISOU   31  O   SER A 233     1677   1244   1989   -233   -272    -53       O  
ATOM     32  CB  SER A 233      43.280  -7.297  -1.693  1.00 14.11           C  
ANISOU   32  CB  SER A 233     2292   1020   2050   -225   -470    -98       C  
ATOM     33  OG  SER A 233      42.938  -5.925  -1.841  1.00 14.80           O  
ANISOU   33  OG  SER A 233     2350   1084   2190   -279   -759    -13       O  
ATOM     34  N   VAL A 234      45.481  -6.967   0.436  1.00 12.92           N  
ANISOU   34  N   VAL A 234     1744   1111   2053   -305   -413     36       N  
ATOM     35  CA  VAL A 234      46.452  -6.027   0.988  1.00 11.94           C  
ANISOU   35  CA  VAL A 234     1698   1072   1767   -290   -349     -3       C  
ATOM     36  C   VAL A 234      47.284  -5.471  -0.164  1.00 12.23           C  
ANISOU   36  C   VAL A 234     1690   1098   1857    -41   -145   -179       C  
ATOM     37  O   VAL A 234      47.290  -6.045  -1.254  1.00 12.60           O  
ANISOU   37  O   VAL A 234     1767   1144   1876   -115   -410    166       O  
ATOM     38  CB  VAL A 234      47.351  -6.686   2.055  1.00 12.49           C  
ANISOU   38  CB  VAL A 234     1726   1284   1734    -11   -240    238       C  
ATOM     39  CG1 VAL A 234      46.503  -7.220   3.205  1.00 13.44           C  
ANISOU   39  CG1 VAL A 234     2015   1149   1942    -43     52    186       C  
ATOM     40  CG2 VAL A 234      48.215  -7.791   1.449  1.00 13.74           C  
ANISOU   40  CG2 VAL A 234     1610   1435   2175    -10   -200     61       C  
ATOM     41  N   PRO A 235      47.983  -4.347   0.059  1.00 12.26           N  
ANISOU   41  N   PRO A 235     1721    973   1964   -177     34    127       N  
ATOM     42  CA  PRO A 235      48.759  -3.787  -1.047  1.00 13.28           C  
ANISOU   42  CA  PRO A 235     1887    875   2283    -46     58     -4       C  
ATOM     43  C   PRO A 235      49.764  -4.768  -1.644  1.00 12.71           C  
ANISOU   43  C   PRO A 235     1832    978   2017   -131   -513    275       C  
ATOM     44  O   PRO A 235      50.415  -5.542  -0.932  1.00 13.01           O  
ANISOU   44  O   PRO A 235     1880   1217   1847    155   -453      5       O  
ATOM     45  CB  PRO A 235      49.491  -2.607  -0.401  1.00 15.46           C  
ANISOU   45  CB  PRO A 235     2246    927   2699   -365     87   -270       C  
ATOM     46  CG  PRO A 235      48.616  -2.205   0.736  1.00 15.85           C  
ANISOU   46  CG  PRO A 235     2267   1117   2639   -191    379    -74       C  
ATOM     47  CD  PRO A 235      48.045  -3.499   1.263  1.00 13.71           C  
ANISOU   47  CD  PRO A 235     2095    802   2310   -321    162   -346       C  
ATOM     48  N   ASN A 236      49.846  -4.712  -2.967  1.00 15.27           N  
ANISOU   48  N   ASN A 236     2105   1676   2022   -567    -13   -110       N  
ATOM     49  CA  ASN A 236      50.816  -5.410  -3.788  1.00 18.59           C  
ANISOU   49  CA  ASN A 236     2430   2313   2318   -616    342    284       C  
ATOM     50  C   ASN A 236      51.997  -4.472  -4.021  1.00 18.64           C  
ANISOU   50  C   ASN A 236     2450   2310   2321   -502    447    251       C  
ATOM     51  O   ASN A 236      52.313  -4.109  -5.162  1.00 24.37           O  
ANISOU   51  O   ASN A 236     3150   3077   3031     98    563    946       O  
ATOM     52  CB  ASN A 236      50.158  -5.751  -5.124  1.00 23.63           C  
ANISOU   52  CB  ASN A 236     3013   3235   2731   -356   -166   -636       C  
ATOM     53  CG  ASN A 236      51.070  -6.496  -6.055  1.00 27.55           C  
ANISOU   53  CG  ASN A 236     3509   4215   2744   -250   -522   -327       C  
ATOM     54  OD1 ASN A 236      51.867  -7.328  -5.626  1.00 31.61           O  
ANISOU   54  OD1 ASN A 236     3989   4323   3697    263   -249    -15       O  
ATOM     55  ND2 ASN A 236      50.954  -6.209  -7.348  1.00 31.68           N  
ANISOU   55  ND2 ASN A 236     3685   4611   3739   -317   -602   -491       N  
ATOM     56  N   ILE A 237      52.598  -4.044  -2.916  1.00 13.80           N  
ANISOU   56  N   ILE A 237     1612   1936   1693   -346   -126    225       N  
ATOM     57  CA  ILE A 237      53.772  -3.175  -2.901  1.00 13.91           C  
ANISOU   57  CA  ILE A 237     1721   1413   2150    126    -83    248       C  
ATOM     58  C   ILE A 237      54.809  -3.777  -1.959  1.00 12.34           C  
ANISOU   58  C   ILE A 237     1530   1088   2069     21     14    338       C  
ATOM     59  O   ILE A 237      54.476  -4.176  -0.838  1.00 11.85           O  
ANISOU   59  O   ILE A 237     1649   1046   1805   -107     80    139       O  
ATOM     60  CB  ILE A 237      53.420  -1.774  -2.356  1.00 14.60           C  
ANISOU   60  CB  ILE A 237     1879   1313   2354    149   -225    332       C  
ATOM     61  CG1 ILE A 237      52.350  -1.101  -3.214  1.00 18.09           C  
ANISOU   61  CG1 ILE A 237     2039   1641   3194    488   -166    212       C  
ATOM     62  CG2 ILE A 237      54.666  -0.887  -2.277  1.00 14.78           C  
ANISOU   62  CG2 ILE A 237     2120   1019   2477    -12   -335      1       C  
ATOM     63  CD1 ILE A 237      51.742   0.113  -2.577  1.00 22.80           C  
ANISOU   63  CD1 ILE A 237     2526   2006   4130    501    -35    193       C  
ATOM     64  N   PRO A 238      56.076  -3.844  -2.395  1.00 11.18           N  
ANISOU   64  N   PRO A 238     1453    937   1859    -65   -137    154       N  
ATOM     65  CA  PRO A 238      57.112  -4.359  -1.493  1.00 11.44           C  
ANISOU   65  CA  PRO A 238     1608   1095   1643     48     25    159       C  
ATOM     66  C   PRO A 238      57.177  -3.585  -0.181  1.00 10.43           C  
ANISOU   66  C   PRO A 238     1645    892   1426     14   -289     28       C  
ATOM     67  O   PRO A 238      57.000  -2.363  -0.148  1.00 11.05           O  
ANISOU   67  O   PRO A 238     1551    594   2052      3   -196    -32       O  
ATOM     68  CB  PRO A 238      58.401  -4.178  -2.297  1.00 12.91           C  
ANISOU   68  CB  PRO A 238     1782   1356   1768     99    173    -68       C  
ATOM     69  CG  PRO A 238      57.953  -4.230  -3.721  1.00 14.28           C  
ANISOU   69  CG  PRO A 238     1858   1735   1833    303    126    201       C  
ATOM     70  CD  PRO A 238      56.615  -3.531  -3.728  1.00 12.90           C  
ANISOU   70  CD  PRO A 238     1509   1500   1890    100    385    404       C  
ATOM     71  N   MET A 239      57.440  -4.304   0.901  1.00 10.87           N  
ANISOU   71  N   MET A 239     1553   1139   1436    -60   -142   -127       N  
ATOM     72  CA  MET A 239      57.399  -3.713   2.229  1.00 10.30           C  
ANISOU   72  CA  MET A 239     1716    785   1410    -32   -223     37       C  
ATOM     73  C   MET A 239      58.294  -2.482   2.343  1.00 10.39           C  
ANISOU   73  C   MET A 239     1372    725   1849   -218   -133   -109       C  
ATOM     74  O   MET A 239      57.907  -1.474   2.961  1.00 11.35           O  
ANISOU   74  O   MET A 239     1722    731   1857     14    -41   -138       O  
ATOM     75  CB  MET A 239      57.794  -4.745   3.290  1.00 10.65           C  
ANISOU   75  CB  MET A 239     1868    801   1375    -65    -74    122       C  
ATOM     76  CG  MET A 239      57.605  -4.231   4.713  1.00 11.66           C  
ANISOU   76  CG  MET A 239     1800    919   1709   -140    -37   -287       C  
ATOM     77  SD  MET A 239      58.102  -5.406   5.986  1.00 12.59           S  
ANISOU   77  SD  MET A 239     2147    846   1789    -27     76     65       S  
ATOM     78  CE  MET A 239      59.879  -5.430   5.736  1.00 13.31           C  
ANISOU   78  CE  MET A 239     1541   1192   2323   -147     34     29       C  
ATOM     79  N   ASN A 240      59.485  -2.564   1.752  1.00  9.87           N  
ANISOU   79  N   ASN A 240     1164    804   1780   -281    120    149       N  
ATOM     80  CA  ASN A 240      60.472  -1.491   1.873  1.00 10.35           C  
ANISOU   80  CA  ASN A 240     1178    748   2004   -139    139    213       C  
ATOM     81  C   ASN A 240      60.218  -0.267   0.992  1.00  9.63           C  
ANISOU   81  C   ASN A 240     1549    671   1439    166   -186    -22       C  
ATOM     82  O   ASN A 240      61.019   0.676   1.000  1.00 11.77           O  
ANISOU   82  O   ASN A 240     1458    719   2294   -104   -308     11       O  
ATOM     83  CB  ASN A 240      61.902  -2.009   1.697  1.00 12.36           C  
ANISOU   83  CB  ASN A 240     1475   1111   2109     47    315   -133       C  
ATOM     84  CG  ASN A 240      62.195  -2.470   0.282  1.00 13.81           C  
ANISOU   84  CG  ASN A 240     1744   1104   2398    -88    101   -265       C  
ATOM     85  OD1 ASN A 240      61.313  -2.956  -0.439  1.00 12.81           O  
ANISOU   85  OD1 ASN A 240     1776    998   2091    109    -11      0       O  
ATOM     86  ND2 ASN A 240      63.453  -2.339  -0.117  1.00 17.13           N  
ANISOU   86  ND2 ASN A 240     1830   1474   3205   -317    470   -489       N  
ATOM     87  N   LEU A 241      59.096  -0.275   0.270  1.00 10.16           N  
ANISOU   87  N   LEU A 241     1524    784   1550    235   -145    -89       N  
ATOM     88  CA  LEU A 241      58.635   0.906  -0.456  1.00 10.17           C  
ANISOU   88  CA  LEU A 241     1418    875   1571     64    114      0       C  
ATOM     89  C   LEU A 241      57.490   1.611   0.268  1.00  9.72           C  
ANISOU   89  C   LEU A 241     1275    912   1504     40    272      5       C  
ATOM     90  O   LEU A 241      57.046   2.670  -0.162  1.00 10.99           O  
ANISOU   90  O   LEU A 241     1398    824   1952    277    178    140       O  
ATOM     91  CB  LEU A 241      58.191   0.556  -1.879  1.00 11.01           C  
ANISOU   91  CB  LEU A 241     1778   1091   1315     -7    233   -125       C  
ATOM     92  CG  LEU A 241      59.267  -0.037  -2.792  1.00 14.78           C  
ANISOU   92  CG  LEU A 241     2084   1781   1750     91    384     39       C  
ATOM     93  CD1 LEU A 241      58.759  -0.186  -4.215  1.00 15.52           C  
ANISOU   93  CD1 LEU A 241     2616   2086   1193     44     44   -136       C  
ATOM     94  CD2 LEU A 241      60.519   0.805  -2.753  1.00 16.75           C  
ANISOU   94  CD2 LEU A 241     2103   2146   2113   -184    573    -69       C  
ATOM     95  N   MET A 242      57.003   1.020   1.355  1.00  9.79           N  
ANISOU   95  N   MET A 242     1089   1034   1595    -94    231    -41       N  
ATOM     96  CA  MET A 242      55.901   1.616   2.103  1.00  9.81           C  
ANISOU   96  CA  MET A 242     1295    944   1486   -185    300     79       C  
ATOM     97  C   MET A 242      56.406   2.412   3.299  1.00  8.91           C  
ANISOU   97  C   MET A 242     1279    828   1276    123     51     90       C  
ATOM     98  O   MET A 242      57.540   2.226   3.744  1.00 11.01           O  
ANISOU   98  O   MET A 242     1358    956   1867    292    -98    -65       O  
ATOM     99  CB  MET A 242      54.891   0.548   2.540  1.00 11.75           C  
ANISOU   99  CB  MET A 242     1416    914   2133   -211    206      9       C  
ATOM    100  CG  MET A 242      54.097   0.004   1.358  1.00 12.10           C  
ANISOU  100  CG  MET A 242     1495   1193   1909   -637    227   -397       C  
ATOM    101  SD  MET A 242      52.847  -1.209   1.802  1.00 16.07           S  
ANISOU  101  SD  MET A 242     1677   1474   2956   -195    284   -469       S  
ATOM    102  CE  MET A 242      53.912  -2.584   2.239  1.00 19.12           C  
ANISOU  102  CE  MET A 242     1881   1824   3559   -265    -67    316       C  
ATOM    103  N   SER A 243      55.563   3.307   3.807  1.00  9.38           N  
ANISOU  103  N   SER A 243     1330    832   1402    183    149   -305       N  
ATOM    104  CA  SER A 243      55.920   4.154   4.931  1.00  9.05           C  
ANISOU  104  CA  SER A 243     1204    795   1440     73    168   -146       C  
ATOM    105  C   SER A 243      55.507   3.581   6.283  1.00  8.46           C  
ANISOU  105  C   SER A 243     1081    710   1422     79    -34     60       C  
ATOM    106  O   SER A 243      54.491   2.901   6.415  1.00  9.52           O  
ANISOU  106  O   SER A 243     1042    929   1647    -61   -142    -47       O  
ATOM    107  CB  SER A 243      55.245   5.525   4.762  1.00  9.86           C  
ANISOU  107  CB  SER A 243     1565    641   1541    231     12   -362       C  
ATOM    108  OG  SER A 243      55.596   6.420   5.819  1.00 10.51           O  
ANISOU  108  OG  SER A 243     1373    827   1794    126    188     91       O  
ATOM    109  N   ASN A 244      56.305   3.875   7.300  1.00  8.46           N  
ANISOU  109  N   ASN A 244     1181    760   1273    158   -159    -25       N  
ATOM    110  CA  ASN A 244      55.880   3.740   8.682  1.00  8.36           C  
ANISOU  110  CA  ASN A 244     1005    951   1219    174    -74   -224       C  
ATOM    111  C   ASN A 244      54.586   4.551   8.850  1.00  8.33           C  
ANISOU  111  C   ASN A 244      936    959   1269    -97     24    -24       C  
ATOM    112  O   ASN A 244      54.370   5.543   8.145  1.00  8.97           O  
ANISOU  112  O   ASN A 244     1074    831   1501     26    105    122       O  
ATOM    113  CB  ASN A 244      56.999   4.293   9.584  1.00  8.87           C  
ANISOU  113  CB  ASN A 244     1132    839   1398    -72   -325    -56       C  
ATOM    114  CG  ASN A 244      56.943   3.776  11.012  1.00  8.70           C  
ANISOU  114  CG  ASN A 244     1132    648   1523    106     22    -76       C  
ATOM    115  OD1 ASN A 244      56.104   4.189  11.815  1.00  9.39           O  
ANISOU  115  OD1 ASN A 244     1260    735   1571    205    -64   -179       O  
ATOM    116  ND2 ASN A 244      57.882   2.893  11.349  1.00  9.42           N  
ANISOU  116  ND2 ASN A 244     1240    578   1761    142   -437    -29       N  
ATOM    117  N   SER A 245      53.725   4.151   9.779  1.00  8.11           N  
ANISOU  117  N   SER A 245      758    857   1467     77     16   -191       N  
ATOM    118  CA  SER A 245      52.503   4.919  10.042  1.00  8.08           C  
ANISOU  118  CA  SER A 245      738    846   1485   -155     79   -124       C  
ATOM    119  C   SER A 245      52.617   5.904  11.208  1.00  8.03           C  
ANISOU  119  C   SER A 245      977    738   1334   -116   -272   -120       C  
ATOM    120  O   SER A 245      51.685   6.683  11.452  1.00  9.73           O  
ANISOU  120  O   SER A 245     1024    912   1759    171    -79   -192       O  
ATOM    121  CB  SER A 245      51.314   3.980  10.258  1.00  9.21           C  
ANISOU  121  CB  SER A 245     1088    780   1629    135    -17    256       C  
ATOM    122  OG  SER A 245      51.638   2.998  11.231  1.00 10.44           O  
ANISOU  122  OG  SER A 245     1040   1200   1725    109     -4    250       O  
ATOM    123  N   ARG A 246      53.752   5.895  11.908  1.00  8.18           N  
ANISOU  123  N   ARG A 246     1153    776   1179    -87   -197    -28       N  
ATOM    124  CA  ARG A 246      53.967   6.808  13.041  1.00  8.32           C  
ANISOU  124  CA  ARG A 246     1261    723   1175    -70   -320     66       C  
ATOM    125  C   ARG A 246      54.977   7.922  12.756  1.00  9.09           C  
ANISOU  125  C   ARG A 246     1170    731   1551     52   -245     20       C  
ATOM    126  O   ARG A 246      54.983   8.946  13.440  1.00  9.63           O  
ANISOU  126  O   ARG A 246     1256    703   1701    111   -135    -27       O  
ATOM    127  CB  ARG A 246      54.405   6.024  14.275  1.00  9.46           C  
ANISOU  127  CB  ARG A 246     1428    688   1478    -76    -55    123       C  
ATOM    128  CG  ARG A 246      53.332   5.090  14.796  1.00  9.96           C  
ANISOU  128  CG  ARG A 246     1640    780   1364   -135      2    150       C  
ATOM    129  CD  ARG A 246      53.821   4.335  16.018  1.00 10.75           C  
ANISOU  129  CD  ARG A 246     1894   1086   1105    280   -130     48       C  
ATOM    130  NE  ARG A 246      53.858   5.171  17.208  1.00 10.11           N  
ANISOU  130  NE  ARG A 246     1811   1017   1014     76   -107   -203       N  
ATOM    131  CZ  ARG A 246      54.603   4.914  18.279  1.00 10.59           C  
ANISOU  131  CZ  ARG A 246     1838    605   1579     33   -178   -164       C  
ATOM    132  NH1 ARG A 246      55.423   3.862  18.284  1.00 11.58           N  
ANISOU  132  NH1 ARG A 246     1805    916   1679    338    130   -136       N  
ATOM    133  NH2 ARG A 246      54.532   5.711  19.339  1.00 12.01           N  
ANISOU  133  NH2 ARG A 246     2007    877   1677     95     26   -227       N  
ATOM    134  N   VAL A 247      55.854   7.702  11.776  1.00  9.43           N  
ANISOU  134  N   VAL A 247     1132    904   1545     70     32     -6       N  
ATOM    135  CA  VAL A 247      56.716   8.752  11.228  1.00  9.44           C  
ANISOU  135  CA  VAL A 247     1225    978   1384    147   -198     59       C  
ATOM    136  C   VAL A 247      56.731   8.568   9.715  1.00  9.24           C  
ANISOU  136  C   VAL A 247     1239    683   1587    109   -251    110       C  
ATOM    137  O   VAL A 247      56.528   7.453   9.230  1.00  9.80           O  
ANISOU  137  O   VAL A 247     1477    625   1621     27   -118     48       O  
ATOM    138  CB  VAL A 247      58.166   8.672  11.766  1.00  9.55           C  
ANISOU  138  CB  VAL A 247     1143    830   1655    353   -398   -203       C  
ATOM    139  CG1 VAL A 247      58.222   9.071  13.239  1.00 11.97           C  
ANISOU  139  CG1 VAL A 247     1265   1364   1918    180   -558   -383       C  
ATOM    140  CG2 VAL A 247      58.737   7.277  11.560  1.00 10.49           C  
ANISOU  140  CG2 VAL A 247     1286    870   1830    230   -320    136       C  
ATOM    141  N   PRO A 248      56.927   9.655   8.955  1.00  9.78           N  
ANISOU  141  N   PRO A 248     1552    660   1502    322     -2   -118       N  
ATOM    142  CA  PRO A 248      56.981   9.521   7.495  1.00  9.78           C  
ANISOU  142  CA  PRO A 248     1493    665   1556    397     25      9       C  
ATOM    143  C   PRO A 248      58.376   9.079   7.050  1.00 10.45           C  
ANISOU  143  C   PRO A 248     1425    912   1633     26    155    -54       C  
ATOM    144  O   PRO A 248      59.220   9.894   6.663  1.00 14.55           O  
ANISOU  144  O   PRO A 248     1567    907   3052     58    182     38       O  
ATOM    145  CB  PRO A 248      56.635  10.930   7.009  1.00 11.32           C  
ANISOU  145  CB  PRO A 248     1845    537   1920    128    -32     21       C  
ATOM    146  CG  PRO A 248      57.181  11.808   8.088  1.00 11.43           C  
ANISOU  146  CG  PRO A 248     1943    520   1880    -54     10     85       C  
ATOM    147  CD  PRO A 248      56.928  11.069   9.382  1.00 11.14           C  
ANISOU  147  CD  PRO A 248     1854    514   1865     57     14     36       C  
ATOM    148  N   MET A 249      58.608   7.771   7.136  1.00 10.66           N  
ANISOU  148  N   MET A 249     1501    720   1829    182    166     27       N  
ATOM    149  CA  MET A 249      59.887   7.160   6.802  1.00 10.27           C  
ANISOU  149  CA  MET A 249     1558   1009   1336    275    -32   -448       C  
ATOM    150  C   MET A 249      59.606   5.811   6.192  1.00  9.51           C  
ANISOU  150  C   MET A 249     1178    994   1440    269      0   -335       C  
ATOM    151  O   MET A 249      58.696   5.110   6.630  1.00 11.22           O  
ANISOU  151  O   MET A 249     1132   1179   1951    -11    287     98       O  
ATOM    152  CB  MET A 249      60.734   6.921   8.055  1.00 12.42           C  
ANISOU  152  CB  MET A 249     2053   1052   1613    194   -503   -102       C  
ATOM    153  CG  MET A 249      61.150   8.146   8.819  1.00 19.50           C  
ANISOU  153  CG  MET A 249     2507   1884   3018   -119   -361     61       C  
ATOM    154  SD  MET A 249      62.226   9.224   7.870  1.00 19.55           S  
ANISOU  154  SD  MET A 249     2602   1981   2844   -757   -436     46       S  
ATOM    155  CE  MET A 249      63.450   8.102   7.256  1.00 21.78           C  
ANISOU  155  CE  MET A 249     2567   2399   3309   -371    446   1429       C  
ATOM    156  N   LEU A 250      60.402   5.432   5.199  1.00  9.33           N  
ANISOU  156  N   LEU A 250     1278    666   1602    173    -37   -190       N  
ATOM    157  CA  LEU A 250      60.296   4.088   4.646  1.00  9.75           C  
ANISOU  157  CA  LEU A 250     1384    609   1709    284    262    -12       C  
ATOM    158  C   LEU A 250      60.457   3.027   5.739  1.00  9.61           C  
ANISOU  158  C   LEU A 250     1214    574   1862     14    130     48       C  
ATOM    159  O   LEU A 250      61.234   3.187   6.689  1.00 10.42           O  
ANISOU  159  O   LEU A 250     1209    892   1856    133   -154   -107       O  
ATOM    160  CB  LEU A 250      61.357   3.879   3.571  1.00 10.96           C  
ANISOU  160  CB  LEU A 250     1615    855   1693    467    231    114       C  
ATOM    161  CG  LEU A 250      61.168   4.651   2.269  1.00 11.97           C  
ANISOU  161  CG  LEU A 250     2025   1121   1403     96    103    312       C  
ATOM    162  CD1 LEU A 250      62.425   4.530   1.417  1.00 15.47           C  
ANISOU  162  CD1 LEU A 250     2336   1692   1850    433    837     80       C  
ATOM    163  CD2 LEU A 250      59.947   4.147   1.518  1.00 14.28           C  
ANISOU  163  CD2 LEU A 250     2384   1091   1949     -4   -554    219       C  
ATOM    164  N   ILE A 251      59.719   1.937   5.587  1.00  9.78           N  
ANISOU  164  N   ILE A 251     1243    567   1907    111     72    187       N  
ATOM    165  CA  ILE A 251      59.913   0.766   6.432  1.00  9.15           C  
ANISOU  165  CA  ILE A 251     1264    490   1723     99     21    -71       C  
ATOM    166  C   ILE A 251      61.226   0.077   6.072  1.00  9.55           C  
ANISOU  166  C   ILE A 251     1416    592   1619     52    187   -316       C  
ATOM    167  O   ILE A 251      61.497  -0.168   4.894  1.00 10.55           O  
ANISOU  167  O   ILE A 251     1444    792   1771    166     17   -267       O  
ATOM    168  CB  ILE A 251      58.738  -0.208   6.271  1.00  9.18           C  
ANISOU  168  CB  ILE A 251     1384    466   1638     11   -123     54       C  
ATOM    169  CG1 ILE A 251      57.468   0.417   6.862  1.00 11.78           C  
ANISOU  169  CG1 ILE A 251     1199    922   2354     48    113    111       C  
ATOM    170  CG2 ILE A 251      59.059  -1.548   6.933  1.00 10.36           C  
ANISOU  170  CG2 ILE A 251     1652    540   1745    134   -125    -18       C  
ATOM    171  CD1 ILE A 251      56.192  -0.300   6.505  1.00 14.65           C  
ANISOU  171  CD1 ILE A 251     1571   1251   2744     23   -154    -51       C  
ATOM    172  N   ASP A 252      62.038  -0.233   7.081  1.00  9.91           N  
ANISOU  172  N   ASP A 252     1303    574   1888    185   -191      8       N  
ATOM    173  CA  ASP A 252      63.306  -0.933   6.836  1.00 10.58           C  
ANISOU  173  CA  ASP A 252     1330    687   2003    259   -143      5       C  
ATOM    174  C   ASP A 252      63.408  -2.291   7.522  1.00  9.90           C  
ANISOU  174  C   ASP A 252     1436    583   1741    -13   -352     96       C  
ATOM    175  O   ASP A 252      64.482  -2.896   7.569  1.00 12.23           O  
ANISOU  175  O   ASP A 252     1321    781   2544    231   -275    -28       O  
ATOM    176  CB  ASP A 252      64.517  -0.039   7.161  1.00 11.49           C  
ANISOU  176  CB  ASP A 252     1390   1000   1976    -75   -102    -40       C  
ATOM    177  CG  ASP A 252      64.660   0.263   8.642  1.00 14.16           C  
ANISOU  177  CG  ASP A 252     1820   1151   2409   -565   -154   -484       C  
ATOM    178  OD1 ASP A 252      63.852  -0.184   9.462  1.00 13.72           O  
ANISOU  178  OD1 ASP A 252     1621   1189   2404     31    -45    -77       O  
ATOM    179  OD2 ASP A 252      65.617   0.983   8.994  1.00 21.79           O  
ANISOU  179  OD2 ASP A 252     2741   2068   3469  -1124    431   -735       O  
ATOM    180  N   GLY A 253      62.285  -2.769   8.044  1.00  9.95           N  
ANISOU  180  N   GLY A 253     1383    526   1871    -48   -128     86       N  
ATOM    181  CA  GLY A 253      62.257  -4.087   8.643  1.00 10.53           C  
ANISOU  181  CA  GLY A 253     1397    590   2015     -1   -189    193       C  
ATOM    182  C   GLY A 253      60.965  -4.391   9.354  1.00  9.05           C  
ANISOU  182  C   GLY A 253     1263    514   1661    -85   -191    -37       C  
ATOM    183  O   GLY A 253      60.045  -3.560   9.412  1.00 10.00           O  
ANISOU  183  O   GLY A 253     1375    736   1686    252    -80    -12       O  
ATOM    184  N   MET A 254      60.891  -5.608   9.874  1.00  9.64           N  
ANISOU  184  N   MET A 254     1402    637   1622    -47   -247   -147       N  
ATOM    185  CA  MET A 254      59.840  -5.966  10.797  1.00  9.52           C  
ANISOU  185  CA  MET A 254     1503    627   1485   -328   -247     98       C  
ATOM    186  C   MET A 254      60.421  -6.852  11.878  1.00  9.11           C  
ANISOU  186  C   MET A 254     1333    730   1398    -72     36     42       C  
ATOM    187  O   MET A 254      61.466  -7.487  11.681  1.00 11.68           O  
ANISOU  187  O   MET A 254     1476    890   2071    261     16     15       O  
ATOM    188  CB  MET A 254      58.633  -6.604  10.092  1.00 14.67           C  
ANISOU  188  CB  MET A 254     1933   1271   2370   -234    358   -410       C  
ATOM    189  CG  MET A 254      58.933  -7.755   9.176  1.00 17.45           C  
ANISOU  189  CG  MET A 254     2209   1429   2992   -283   -110   -229       C  
ATOM    190  SD  MET A 254      57.393  -8.447   8.496  1.00 13.90           S  
ANISOU  190  SD  MET A 254     2304   1114   1862   -619   -279   -240       S  
ATOM    191  CE  MET A 254      58.072  -9.247   7.056  1.00 15.40           C  
ANISOU  191  CE  MET A 254     2175   1546   2128    163      1   -289       C  
ATOM    192  N   MET A 255      59.764  -6.861  13.033  1.00 10.32           N  
ANISOU  192  N   MET A 255     1497    973   1452     17   -207    180       N  
ATOM    193  CA  MET A 255      60.268  -7.582  14.194  1.00 10.89           C  
ANISOU  193  CA  MET A 255     1447   1144   1546   -107   -385    503       C  
ATOM    194  C   MET A 255      59.136  -7.802  15.182  1.00 10.28           C  
ANISOU  194  C   MET A 255     1263    954   1687   -207   -230    167       C  
ATOM    195  O   MET A 255      58.160  -7.050  15.188  1.00 11.37           O  
ANISOU  195  O   MET A 255     1297   1065   1958    199   -179    139       O  
ATOM    196  CB  MET A 255      61.381  -6.768  14.871  1.00 14.69           C  
ANISOU  196  CB  MET A 255     1666   1585   2330   -182   -398    509       C  
ATOM    197  CG  MET A 255      60.866  -5.506  15.560  1.00 15.53           C  
ANISOU  197  CG  MET A 255     1893   1455   2552   -718   -815    299       C  
ATOM    198  SD  MET A 255      62.144  -4.482  16.310  1.00 18.80           S  
ANISOU  198  SD  MET A 255     2504   1890   2750   -528   -958    382       S  
ATOM    199  CE  MET A 255      62.648  -5.516  17.683  1.00 25.16           C  
ANISOU  199  CE  MET A 255     3036   2663   3859   -127   -789    900       C  
ATOM    200  N   VAL A 256      59.272  -8.817  16.031  1.00 10.81           N  
ANISOU  200  N   VAL A 256     1481    921   1703   -194   -243    445       N  
ATOM    201  CA  VAL A 256      58.433  -8.903  17.212  1.00 11.31           C  
ANISOU  201  CA  VAL A 256     1483    788   2026   -353   -192    229       C  
ATOM    202  C   VAL A 256      59.178  -8.209  18.340  1.00 10.97           C  
ANISOU  202  C   VAL A 256     1301   1095   1770   -188   -310    129       C  
ATOM    203  O   VAL A 256      60.393  -8.020  18.268  1.00 12.30           O  
ANISOU  203  O   VAL A 256     1529   1018   2124     28   -260     99       O  
ATOM    204  CB  VAL A 256      58.082 -10.361  17.587  1.00 11.54           C  
ANISOU  204  CB  VAL A 256     1378    747   2260   -172   -642    216       C  
ATOM    205  CG1 VAL A 256      57.391 -11.038  16.413  1.00 13.31           C  
ANISOU  205  CG1 VAL A 256     1774    989   2295   -300   -520    -21       C  
ATOM    206  CG2 VAL A 256      59.328 -11.132  17.991  1.00 12.62           C  
ANISOU  206  CG2 VAL A 256     1650    812   2333     30   -674    157       C  
ATOM    207  N   SER A 257      58.458  -7.811  19.377  1.00 12.68           N  
ANISOU  207  N   SER A 257     1706   1508   1602    -48   -313    225       N  
ATOM    208  CA  SER A 257      59.101  -7.180  20.521  1.00 16.56           C  
ANISOU  208  CA  SER A 257     2244   2375   1673    364   -564   -463       C  
ATOM    209  C   SER A 257      59.797  -8.220  21.380  1.00 19.61           C  
ANISOU  209  C   SER A 257     2733   2645   2074    500  -1214   -571       C  
ATOM    210  O   SER A 257      59.335  -9.354  21.488  1.00 23.82           O  
ANISOU  210  O   SER A 257     3122   2594   3333    237  -1405    180       O  
ATOM    211  CB  SER A 257      58.063  -6.452  21.371  1.00 20.15           C  
ANISOU  211  CB  SER A 257     2665   3045   1945    774   -808   -862       C  
ATOM    212  OG  SER A 257      58.656  -6.015  22.576  1.00 26.07           O  
ANISOU  212  OG  SER A 257     3128   4025   2751   1069   -921   -733       O  
ATOM    213  N   ASN A 258      60.901  -7.825  22.008  1.00 22.65           N  
ANISOU  213  N   ASN A 258     2991   3178   2436    806  -1222   -372       N  
ATOM    214  CA  ASN A 258      61.503  -8.645  23.058  1.00 27.94           C  
ANISOU  214  CA  ASN A 258     3348   3940   3329   1249  -1464   -102       C  
ATOM    215  C   ASN A 258      60.704  -8.614  24.364  1.00 31.01           C  
ANISOU  215  C   ASN A 258     4095   4555   3133   1761  -1210   -126       C  
ATOM    216  O   ASN A 258      60.671  -9.599  25.103  1.00 35.41           O  
ANISOU  216  O   ASN A 258     4540   4879   4035   1957   -589    360       O  
ATOM    217  CB  ASN A 258      62.952  -8.238  23.315  1.00 30.21           C  
ANISOU  217  CB  ASN A 258     3176   4216   4086   1258   -618   -410       C  
ATOM    218  CG  ASN A 258      63.899  -8.795  22.279  1.00 28.24           C  
ANISOU  218  CG  ASN A 258     3038   4228   3463   1045   -528   -358       C  
ATOM    219  OD1 ASN A 258      63.539  -8.955  21.114  1.00 30.82           O  
ANISOU  219  OD1 ASN A 258     3305   4573   3830   1121   -810   -193       O  
ATOM    220  ND2 ASN A 258      65.114  -9.117  22.702  1.00 27.47           N  
ANISOU  220  ND2 ASN A 258     2853   4073   3510    987   -988   -341       N  
ATOM    221  N   ASP A 259      60.072  -7.481  24.654  1.00 31.25           N  
ANISOU  221  N   ASP A 259     4386   4568   2918   1691  -1445   -511       N  
ATOM    222  CA  ASP A 259      59.190  -7.382  25.814  1.00 33.27           C  
ANISOU  222  CA  ASP A 259     4790   4853   2996   1526   -773   -217       C  
ATOM    223  C   ASP A 259      57.754  -7.648  25.387  1.00 37.30           C  
ANISOU  223  C   ASP A 259     5085   5114   3971   1313   -468    130       C  
ATOM    224  O   ASP A 259      57.036  -6.731  24.994  1.00 38.54           O  
ANISOU  224  O   ASP A 259     5296   4889   4459   1269   -340    267       O  
ATOM    225  CB  ASP A 259      59.299  -6.006  26.476  1.00 35.33           C  
ANISOU  225  CB  ASP A 259     5048   5440   2935   1859   -408   -432       C  
ATOM    226  CG  ASP A 259      58.405  -5.870  27.712  1.00 38.84           C  
ANISOU  226  CG  ASP A 259     5430   5737   3588   2262   -498   -472       C  
ATOM    227  OD1 ASP A 259      58.333  -4.756  28.279  1.00 40.93           O  
ANISOU  227  OD1 ASP A 259     5761   5889   3901   2255   -946   -904       O  
ATOM    228  OD2 ASP A 259      57.775  -6.872  28.119  1.00 36.86           O  
ANISOU  228  OD2 ASP A 259     5395   5717   2891   2401   -484    -88       O  
ATOM    229  N   GLN A 260      57.340  -8.908  25.461  1.00 38.48           N  
ANISOU  229  N   GLN A 260     5162   5059   4398    864   -566    212       N  
ATOM    230  CA  GLN A 260      55.989  -9.291  25.058  1.00 40.85           C  
ANISOU  230  CA  GLN A 260     5430   5244   4848    753   -402    794       C  
ATOM    231  C   GLN A 260      54.925  -8.653  25.948  1.00 42.84           C  
ANISOU  231  C   GLN A 260     5686   5955   4636    987   -149   1589       C  
ATOM    232  O   GLN A 260      53.736  -8.649  25.612  1.00 41.78           O  
ANISOU  232  O   GLN A 260     5578   6068   4228    773   -242   1636       O  
ATOM    233  CB  GLN A 260      55.845 -10.813  25.053  1.00 40.26           C  
ANISOU  233  CB  GLN A 260     5374   4903   5019    376   -757    676       C  
ATOM    234  CG  GLN A 260      56.534 -11.481  23.875  1.00 37.32           C  
ANISOU  234  CG  GLN A 260     5267   4258   4654    152  -1278    564       C  
ATOM    235  CD  GLN A 260      55.877 -11.124  22.555  1.00 35.23           C  
ANISOU  235  CD  GLN A 260     5130   3742   4512    -25  -1686    667       C  
ATOM    236  OE1 GLN A 260      54.706 -11.438  22.331  1.00 32.87           O  
ANISOU  236  OE1 GLN A 260     5044   3270   4173   -161  -1991    442       O  
ATOM    237  NE2 GLN A 260      56.623 -10.453  21.677  1.00 33.23           N  
ANISOU  237  NE2 GLN A 260     4996   3230   4400   -364  -1779    933       N  
ATOM    238  N   ASN A 261      55.361  -8.105  27.078  1.00 42.42           N  
ANISOU  238  N   ASN A 261     6031   6163   3923   1333    -22   2499       N  
ATOM    239  CA  ASN A 261      54.445  -7.475  28.020  1.00 46.32           C  
ANISOU  239  CA  ASN A 261     6465   6579   4553   1709    134   2438       C  
ATOM    240  C   ASN A 261      54.145  -6.008  27.714  1.00 46.86           C  
ANISOU  240  C   ASN A 261     6570   6268   4967   1788    282   2236       C  
ATOM    241  O   ASN A 261      53.171  -5.458  28.223  1.00 48.04           O  
ANISOU  241  O   ASN A 261     6507   6611   5133   1797    363   2460       O  
ATOM    242  CB  ASN A 261      54.957  -7.623  29.455  1.00 48.38           C  
ANISOU  242  CB  ASN A 261     6697   6893   4792   1970    108   2399       C  
ATOM    243  CG  ASN A 261      54.947  -9.062  29.930  1.00 53.04           C  
ANISOU  243  CG  ASN A 261     6914   7283   5954   2209     69   1850       C  
ATOM    244  OD1 ASN A 261      55.944  -9.566  30.446  1.00 55.13           O  
ANISOU  244  OD1 ASN A 261     7030   7395   6523   2254     11   1548       O  
ATOM    245  ND2 ASN A 261      53.813  -9.735  29.753  1.00 54.01           N  
ANISOU  245  ND2 ASN A 261     6987   7342   6193   2337    160   1708       N  
ATOM    246  N   GLN A 262      54.977  -5.375  26.890  1.00 45.12           N  
ANISOU  246  N   GLN A 262     6710   5741   4691   1738    199   1571       N  
ATOM    247  CA  GLN A 262      54.741  -3.982  26.519  1.00 43.29           C  
ANISOU  247  CA  GLN A 262     6809   5116   4524   1633    -42    806       C  
ATOM    248  C   GLN A 262      53.665  -3.903  25.442  1.00 39.95           C  
ANISOU  248  C   GLN A 262     6488   4687   4002   1586   -141   -111       C  
ATOM    249  O   GLN A 262      53.852  -4.363  24.315  1.00 41.68           O  
ANISOU  249  O   GLN A 262     6556   4776   4503   1756    167   -740       O  
ATOM    250  CB  GLN A 262      56.030  -3.284  26.073  1.00 45.04           C  
ANISOU  250  CB  GLN A 262     7200   4881   5030   1354    -58    683       C  
ATOM    251  CG  GLN A 262      56.617  -3.796  24.775  1.00 45.96           C  
ANISOU  251  CG  GLN A 262     7590   4607   5266   1121   -267    947       C  
ATOM    252  CD  GLN A 262      57.888  -3.068  24.398  1.00 46.31           C  
ANISOU  252  CD  GLN A 262     7927   4312   5357    888   -387   1330       C  
ATOM    253  OE1 GLN A 262      58.230  -2.045  24.993  1.00 47.07           O  
ANISOU  253  OE1 GLN A 262     7993   4312   5579    654   -605   1245       O  
ATOM    254  NE2 GLN A 262      58.599  -3.591  23.407  1.00 46.51           N  
ANISOU  254  NE2 GLN A 262     8127   4181   5364    793   -419   1615       N  
ATOM    255  N   VAL A 263      52.535  -3.316  25.818  1.00 34.96           N  
ANISOU  255  N   VAL A 263     6064   3754   3466   1446   -680     68       N  
ATOM    256  CA  VAL A 263      51.328  -3.325  25.014  1.00 29.69           C  
ANISOU  256  CA  VAL A 263     5538   3098   2644   1375   -281    227       C  
ATOM    257  C   VAL A 263      51.321  -2.148  24.046  1.00 23.66           C  
ANISOU  257  C   VAL A 263     4869   1921   2198    885   -545    -65       C  
ATOM    258  O   VAL A 263      51.467  -1.001  24.460  1.00 26.63           O  
ANISOU  258  O   VAL A 263     5177   2380   2559    954   -916   -317       O  
ATOM    259  CB  VAL A 263      50.090  -3.235  25.930  1.00 26.63           C  
ANISOU  259  CB  VAL A 263     5429   2781   1909    719    -25    742       C  
ATOM    260  CG1 VAL A 263      48.800  -3.223  25.120  1.00 30.48           C  
ANISOU  260  CG1 VAL A 263     5827   2778   2976   1042    -69    604       C  
ATOM    261  CG2 VAL A 263      50.097  -4.382  26.941  1.00 29.34           C  
ANISOU  261  CG2 VAL A 263     5898   2744   2505   1191   -156    485       C  
ATOM    262  N   PRO A 264      51.170  -2.425  22.743  1.00 18.42           N  
ANISOU  262  N   PRO A 264     3653   1328   2016    180   -321    113       N  
ATOM    263  CA  PRO A 264      51.038  -1.296  21.818  1.00 17.12           C  
ANISOU  263  CA  PRO A 264     3028   1408   2070    -48   -281    170       C  
ATOM    264  C   PRO A 264      49.636  -0.695  21.869  1.00 16.25           C  
ANISOU  264  C   PRO A 264     2849   1225   2098   -232    154     87       C  
ATOM    265  O   PRO A 264      48.638  -1.424  21.871  1.00 16.07           O  
ANISOU  265  O   PRO A 264     2602   1358   2145   -486     96    142       O  
ATOM    266  CB  PRO A 264      51.292  -1.939  20.450  1.00 16.08           C  
ANISOU  266  CB  PRO A 264     2767   1466   1876   -420   -258     43       C  
ATOM    267  CG  PRO A 264      50.825  -3.339  20.616  1.00 15.84           C  
ANISOU  267  CG  PRO A 264     2808   1374   1837   -532      8     -4       C  
ATOM    268  CD  PRO A 264      51.166  -3.721  22.038  1.00 17.15           C  
ANISOU  268  CD  PRO A 264     3281   1067   2168   -157    177     98       C  
ATOM    269  N   GLN A 265      49.569   0.630  21.923  1.00 15.15           N  
ANISOU  269  N   GLN A 265     2749   1169   1838    -33    -40    -10       N  
ATOM    270  CA  GLN A 265      48.303   1.336  21.802  1.00 15.18           C  
ANISOU  270  CA  GLN A 265     2657   1617   1494   -179    105    154       C  
ATOM    271  C   GLN A 265      48.560   2.594  20.987  1.00 13.82           C  
ANISOU  271  C   GLN A 265     2289   1503   1457   -160    186     82       C  
ATOM    272  O   GLN A 265      48.187   3.707  21.374  1.00 13.97           O  
ANISOU  272  O   GLN A 265     2190   1498   1618   -140    327   -191       O  
ATOM    273  CB  GLN A 265      47.690   1.660  23.170  1.00 16.95           C  
ANISOU  273  CB  GLN A 265     2763   1871   1804   -328    392    217       C  
ATOM    274  CG  GLN A 265      46.275   2.220  23.053  1.00 18.15           C  
ANISOU  274  CG  GLN A 265     2945   2139   1811   -285    909     65       C  
ATOM    275  CD  GLN A 265      45.571   2.399  24.382  1.00 21.07           C  
ANISOU  275  CD  GLN A 265     3328   2152   2526   -358    633     -1       C  
ATOM    276  OE1 GLN A 265      46.142   2.161  25.446  1.00 22.22           O  
ANISOU  276  OE1 GLN A 265     3662   2514   2266   -265    756   -252       O  
ATOM    277  NE2 GLN A 265      44.312   2.824  24.323  1.00 21.20           N  
ANISOU  277  NE2 GLN A 265     3503   1837   2713   -251    861    198       N  
ATOM    278  N   PHE A 266      49.222   2.402  19.852  1.00 12.43           N  
ANISOU  278  N   PHE A 266     1860   1324   1538   -270    162     78       N  
ATOM    279  CA  PHE A 266      49.518   3.503  18.952  1.00 10.79           C  
ANISOU  279  CA  PHE A 266     1679   1080   1339     17     65    221       C  
ATOM    280  C   PHE A 266      48.208   4.140  18.507  1.00 10.60           C  
ANISOU  280  C   PHE A 266     1601    856   1568   -180    -91   -106       C  
ATOM    281  O   PHE A 266      47.177   3.463  18.429  1.00 11.80           O  
ANISOU  281  O   PHE A 266     1929    919   1633   -150    131     -6       O  
ATOM    282  CB  PHE A 266      50.317   3.009  17.746  1.00 11.28           C  
ANISOU  282  CB  PHE A 266     1702   1064   1518    206    255    122       C  
ATOM    283  CG  PHE A 266      51.532   2.209  18.119  1.00 11.31           C  
ANISOU  283  CG  PHE A 266     1639   1023   1636    -20      4     66       C  
ATOM    284  CD1 PHE A 266      52.271   2.538  19.244  1.00 11.93           C  
ANISOU  284  CD1 PHE A 266     1543   1252   1738    147   -127     64       C  
ATOM    285  CD2 PHE A 266      51.918   1.115  17.359  1.00 11.51           C  
ANISOU  285  CD2 PHE A 266     1579   1027   1766    268      5    128       C  
ATOM    286  CE1 PHE A 266      53.388   1.788  19.603  1.00 12.59           C  
ANISOU  286  CE1 PHE A 266     1667   1254   1863     98    165   -332       C  
ATOM    287  CE2 PHE A 266      53.030   0.374  17.703  1.00 11.38           C  
ANISOU  287  CE2 PHE A 266     1626   1093   1606    217    -27     38       C  
ATOM    288  CZ  PHE A 266      53.759   0.699  18.835  1.00 11.79           C  
ANISOU  288  CZ  PHE A 266     1625   1231   1624    -49    171     23       C  
ATOM    289  N   GLN A 267      48.238   5.442  18.236  1.00 10.76           N  
ANISOU  289  N   GLN A 267     1545    895   1648     37   -121    -50       N  
ATOM    290  CA  GLN A 267      47.043   6.135  17.781  1.00 10.30           C  
ANISOU  290  CA  GLN A 267     1493    894   1525    126     79   -120       C  
ATOM    291  C   GLN A 267      47.090   6.408  16.284  1.00 10.51           C  
ANISOU  291  C   GLN A 267     1455    861   1677     91    257    -61       C  
ATOM    292  O   GLN A 267      46.056   6.661  15.660  1.00 11.19           O  
ANISOU  292  O   GLN A 267     1409   1135   1708     97     47    -97       O  
ATOM    293  CB  GLN A 267      46.837   7.421  18.576  1.00 10.75           C  
ANISOU  293  CB  GLN A 267     1766   1010   1306    128    126   -348       C  
ATOM    294  CG  GLN A 267      46.579   7.144  20.043  1.00 11.78           C  
ANISOU  294  CG  GLN A 267     1804   1207   1463   -228    529   -136       C  
ATOM    295  CD  GLN A 267      45.390   6.226  20.235  1.00 13.45           C  
ANISOU  295  CD  GLN A 267     1974   1265   1869     52    253     32       C  
ATOM    296  OE1 GLN A 267      44.290   6.517  19.764  1.00 14.45           O  
ANISOU  296  OE1 GLN A 267     1965   1416   2108     36    411     37       O  
ATOM    297  NE2 GLN A 267      45.606   5.099  20.913  1.00 14.11           N  
ANISOU  297  NE2 GLN A 267     2380   1184   1795   -140    518      1       N  
ATOM    298  N   ASN A 268      48.296   6.364  15.723  1.00 10.10           N  
ANISOU  298  N   ASN A 268     1539    837   1459     33    157    -62       N  
ATOM    299  CA  ASN A 268      48.478   6.411  14.282  1.00 10.17           C  
ANISOU  299  CA  ASN A 268     1454    805   1605   -228    229   -138       C  
ATOM    300  C   ASN A 268      48.687   5.003  13.723  1.00 10.69           C  
ANISOU  300  C   ASN A 268     1415    869   1777    -27    -37   -526       C  
ATOM    301  O   ASN A 268      49.057   4.086  14.462  1.00 11.61           O  
ANISOU  301  O   ASN A 268     1526    982   1904    126    121     22       O  
ATOM    302  CB  ASN A 268      49.621   7.355  13.911  1.00 10.60           C  
ANISOU  302  CB  ASN A 268     1493    760   1772      5    119   -201       C  
ATOM    303  CG  ASN A 268      49.247   8.812  14.116  1.00  9.28           C  
ANISOU  303  CG  ASN A 268     1221    835   1468   -188      9   -292       C  
ATOM    304  OD1 ASN A 268      48.112   9.208  13.839  1.00 11.44           O  
ANISOU  304  OD1 ASN A 268     1144   1248   1954     76    165   -291       O  
ATOM    305  ND2 ASN A 268      50.183   9.609  14.617  1.00 10.43           N  
ANISOU  305  ND2 ASN A 268     1185    958   1821    -17     17   -234       N  
ATOM    306  N   GLY A 269      48.417   4.834  12.431  1.00  9.31           N  
ANISOU  306  N   GLY A 269      942    858   1738   -145    -40   -547       N  
ATOM    307  CA  GLY A 269      48.439   3.524  11.790  1.00  9.72           C  
ANISOU  307  CA  GLY A 269     1197    755   1740   -217    146   -316       C  
ATOM    308  C   GLY A 269      47.340   2.586  12.257  1.00  9.37           C  
ANISOU  308  C   GLY A 269     1143    749   1669    -10    253      8       C  
ATOM    309  O   GLY A 269      47.488   1.366  12.122  1.00 12.71           O  
ANISOU  309  O   GLY A 269     1535    770   2524      6    396   -113       O  
ATOM    310  N   ARG A 270      46.250   3.137  12.798  1.00 10.04           N  
ANISOU  310  N   ARG A 270     1092   1031   1692   -254    153     59       N  
ATOM    311  CA  ARG A 270      45.157   2.332  13.343  1.00  9.95           C  
ANISOU  311  CA  ARG A 270     1125   1136   1518    -88    147   -206       C  
ATOM    312  C   ARG A 270      43.927   2.369  12.437  1.00 10.03           C  
ANISOU  312  C   ARG A 270     1239    963   1607   -146    -35   -239       C  
ATOM    313  O   ARG A 270      43.393   3.444  12.141  1.00 11.50           O  
ANISOU  313  O   ARG A 270     1336   1167   1865     15    127    -86       O  
ATOM    314  CB  ARG A 270      44.775   2.813  14.748  1.00 11.49           C  
ANISOU  314  CB  ARG A 270     1252   1377   1737    -13    221   -135       C  
ATOM    315  CG  ARG A 270      45.930   2.846  15.744  1.00 10.97           C  
ANISOU  315  CG  ARG A 270     1222   1056   1888     70   -131    225       C  
ATOM    316  CD  ARG A 270      46.513   1.445  16.000  1.00 10.97           C  
ANISOU  316  CD  ARG A 270     1471    925   1770   -147    306    318       C  
ATOM    317  NE  ARG A 270      45.522   0.478  16.487  1.00 12.59           N  
ANISOU  317  NE  ARG A 270     1720   1111   1951   -161    230    215       N  
ATOM    318  CZ  ARG A 270      45.260   0.245  17.774  1.00 12.75           C  
ANISOU  318  CZ  ARG A 270     1871    939   2035   -295    -91    116       C  
ATOM    319  NH1 ARG A 270      45.922   0.897  18.721  1.00 12.64           N  
ANISOU  319  NH1 ARG A 270     1758   1209   1834   -139      3    147       N  
ATOM    320  NH2 ARG A 270      44.343  -0.656  18.117  1.00 14.15           N  
ANISOU  320  NH2 ARG A 270     1879   1132   2366   -238    387    161       N  
ATOM    321  N   VAL A 271      43.493   1.187  12.006  1.00 10.30           N  
ANISOU  321  N   VAL A 271      993   1308   1612   -297    -75   -214       N  
ATOM    322  CA  VAL A 271      42.350   1.028  11.110  1.00 10.96           C  
ANISOU  322  CA  VAL A 271     1049   1171   1943   -340     -2    -34       C  
ATOM    323  C   VAL A 271      41.890  -0.427  11.200  1.00 10.93           C  
ANISOU  323  C   VAL A 271     1068   1110   1973   -432     91   -206       C  
ATOM    324  O   VAL A 271      42.697  -1.321  11.427  1.00 12.77           O  
ANISOU  324  O   VAL A 271     1322   1100   2428     23    -85    -82       O  
ATOM    325  CB  VAL A 271      42.743   1.367   9.648  1.00 11.96           C  
ANISOU  325  CB  VAL A 271     1140   1397   2006    -30     46    219       C  
ATOM    326  CG1 VAL A 271      43.749   0.347   9.099  1.00 13.89           C  
ANISOU  326  CG1 VAL A 271     1298   1581   2396    236    367    -92       C  
ATOM    327  CG2 VAL A 271      41.522   1.472   8.746  1.00 13.89           C  
ANISOU  327  CG2 VAL A 271     1437   1576   2263     45   -280   -138       C  
ATOM    328  N   THR A 272      40.591  -0.661  11.059  1.00 11.98           N  
ANISOU  328  N   THR A 272     1166   1385   2001   -576    190    -35       N  
ATOM    329  CA  THR A 272      40.100  -2.026  10.972  1.00 12.46           C  
ANISOU  329  CA  THR A 272     1198   1249   2288   -521    134    -74       C  
ATOM    330  C   THR A 272      40.361  -2.575   9.568  1.00 12.25           C  
ANISOU  330  C   THR A 272     1325   1215   2114   -407   -103      4       C  
ATOM    331  O   THR A 272      40.592  -1.815   8.618  1.00 12.77           O  
ANISOU  331  O   THR A 272     1398   1259   2193   -384    -76     14       O  
ATOM    332  CB  THR A 272      38.601  -2.104  11.249  1.00 14.76           C  
ANISOU  332  CB  THR A 272     1477   1601   2529   -246    365     96       C  
ATOM    333  OG1 THR A 272      37.899  -1.310  10.282  1.00 15.34           O  
ANISOU  333  OG1 THR A 272     1336   1428   3063   -187     56     93       O  
ATOM    334  CG2 THR A 272      38.292  -1.589  12.646  1.00 15.70           C  
ANISOU  334  CG2 THR A 272     1586   1743   2636   -209    463   -290       C  
ATOM    335  N   LEU A 273      40.317  -3.895   9.422  1.00 13.03           N  
ANISOU  335  N   LEU A 273     1362   1326   2261   -331   -354   -194       N  
ATOM    336  CA  LEU A 273      40.511  -4.488   8.100  1.00 13.28           C  
ANISOU  336  CA  LEU A 273     1465   1335   2244    -19   -275   -206       C  
ATOM    337  C   LEU A 273      39.427  -4.068   7.113  1.00 14.20           C  
ANISOU  337  C   LEU A 273     1415   1450   2530   -191   -367    -60       C  
ATOM    338  O   LEU A 273      39.654  -4.075   5.895  1.00 15.16           O  
ANISOU  338  O   LEU A 273     1606   1746   2409    -47   -404     69       O  
ATOM    339  CB  LEU A 273      40.594  -6.015   8.178  1.00 13.11           C  
ANISOU  339  CB  LEU A 273     1269   1140   2570   -218   -377   -180       C  
ATOM    340  CG  LEU A 273      41.752  -6.549   9.018  1.00 14.14           C  
ANISOU  340  CG  LEU A 273     1223   1437   2710   -425   -420   -307       C  
ATOM    341  CD1 LEU A 273      41.829  -8.065   8.867  1.00 14.36           C  
ANISOU  341  CD1 LEU A 273     1714   1050   2691   -279   -215   -302       C  
ATOM    342  CD2 LEU A 273      43.076  -5.894   8.613  1.00 14.40           C  
ANISOU  342  CD2 LEU A 273     1251   1707   2512   -356     -4   -102       C  
ATOM    343  N   ASP A 274      38.250  -3.709   7.625  1.00 14.21           N  
ANISOU  343  N   ASP A 274     1133   1578   2687   -392   -587      1       N  
ATOM    344  CA  ASP A 274      37.188  -3.240   6.735  1.00 15.90           C  
ANISOU  344  CA  ASP A 274     1395   1741   2906   -408   -242     31       C  
ATOM    345  C   ASP A 274      37.185  -1.716   6.510  1.00 15.21           C  
ANISOU  345  C   ASP A 274     1561   1657   2560   -351   -278    -21       C  
ATOM    346  O   ASP A 274      36.233  -1.165   5.958  1.00 18.08           O  
ANISOU  346  O   ASP A 274     1718   2152   2997     -1   -555     76       O  
ATOM    347  CB  ASP A 274      35.805  -3.812   7.108  1.00 16.75           C  
ANISOU  347  CB  ASP A 274     1404   1989   2971   -456   -235   -106       C  
ATOM    348  CG  ASP A 274      35.244  -3.273   8.421  1.00 18.82           C  
ANISOU  348  CG  ASP A 274     1542   2247   3362   -626   -155     21       C  
ATOM    349  OD1 ASP A 274      35.805  -2.337   9.017  1.00 19.09           O  
ANISOU  349  OD1 ASP A 274     1549   2405   3297   -505   -144   -163       O  
ATOM    350  OD2 ASP A 274      34.187  -3.791   8.843  1.00 22.78           O  
ANISOU  350  OD2 ASP A 274     1975   2477   4202   -709    196   -249       O  
ATOM    351  N   GLY A 275      38.265  -1.049   6.920  1.00 13.90           N  
ANISOU  351  N   GLY A 275     1511   1481   2290   -272    -14     88       N  
ATOM    352  CA  GLY A 275      38.506   0.331   6.524  1.00 14.03           C  
ANISOU  352  CA  GLY A 275     1561   1445   2324    -73    -51     83       C  
ATOM    353  C   GLY A 275      38.002   1.443   7.434  1.00 14.70           C  
ANISOU  353  C   GLY A 275     1390   1849   2345   -145     49    -22       C  
ATOM    354  O   GLY A 275      37.818   2.574   6.976  1.00 17.17           O  
ANISOU  354  O   GLY A 275     1781   1953   2789      5   -100    191       O  
ATOM    355  N   GLN A 276      37.785   1.139   8.712  1.00 14.00           N  
ANISOU  355  N   GLN A 276     1272   1829   2216   -169   -116   -348       N  
ATOM    356  CA  GLN A 276      37.353   2.145   9.685  1.00 14.30           C  
ANISOU  356  CA  GLN A 276     1298   1626   2507   -269    147   -446       C  
ATOM    357  C   GLN A 276      38.553   2.727  10.424  1.00 13.64           C  
ANISOU  357  C   GLN A 276     1293   1425   2465    -99   -111   -245       C  
ATOM    358  O   GLN A 276      39.208   2.027  11.204  1.00 14.99           O  
ANISOU  358  O   GLN A 276     1646   1478   2569    282   -120    -97       O  
ATOM    359  CB  GLN A 276      36.381   1.539  10.701  1.00 17.16           C  
ANISOU  359  CB  GLN A 276     1479   1933   3106   -495    462   -452       C  
ATOM    360  CG  GLN A 276      35.121   0.940  10.102  1.00 22.96           C  
ANISOU  360  CG  GLN A 276     1927   2449   4347   -524    612   -523       C  
ATOM    361  CD  GLN A 276      34.272   0.218  11.139  1.00 29.06           C  
ANISOU  361  CD  GLN A 276     2830   2922   5289    -30    714   -533       C  
ATOM    362  OE1 GLN A 276      34.144  -1.010  11.113  1.00 32.12           O  
ANISOU  362  OE1 GLN A 276     3272   3218   5712     44    500   -677       O  
ATOM    363  NE2 GLN A 276      33.686   0.981  12.058  1.00 30.45           N  
ANISOU  363  NE2 GLN A 276     3108   2968   5491     23    894   -426       N  
ATOM    364  N   LEU A 277      38.850   3.998  10.166  1.00 13.04           N  
ANISOU  364  N   LEU A 277     1228   1389   2338    -41   -172   -415       N  
ATOM    365  CA  LEU A 277      39.966   4.670  10.819  1.00 12.85           C  
ANISOU  365  CA  LEU A 277     1317   1443   2123     22   -102   -148       C  
ATOM    366  C   LEU A 277      39.744   4.798  12.319  1.00 12.55           C  
ANISOU  366  C   LEU A 277     1334   1555   1878   -110    -29   -206       C  
ATOM    367  O   LEU A 277      38.619   5.031  12.769  1.00 14.67           O  
ANISOU  367  O   LEU A 277     1337   1931   2306    -83     72   -262       O  
ATOM    368  CB  LEU A 277      40.181   6.064  10.216  1.00 12.65           C  
ANISOU  368  CB  LEU A 277     1316   1238   2252     43     45    -22       C  
ATOM    369  CG  LEU A 277      40.662   6.072   8.762  1.00 12.31           C  
ANISOU  369  CG  LEU A 277     1110   1635   1933    108    -45    -47       C  
ATOM    370  CD1 LEU A 277      40.490   7.446   8.143  1.00 13.76           C  
ANISOU  370  CD1 LEU A 277     1485   1350   2392    295     72    215       C  
ATOM    371  CD2 LEU A 277      42.110   5.607   8.677  1.00 14.03           C  
ANISOU  371  CD2 LEU A 277     1084   1657   2590    -25   -226   -217       C  
ATOM    372  N   GLN A 278      40.830   4.682  13.081  1.00 12.18           N  
ANISOU  372  N   GLN A 278     1365   1514   1748   -180     58   -182       N  
ATOM    373  CA  GLN A 278      40.768   4.816  14.535  1.00 12.59           C  
ANISOU  373  CA  GLN A 278     1527   1339   1918   -309   -145   -152       C  
ATOM    374  C   GLN A 278      41.820   5.783  15.061  1.00 12.52           C  
ANISOU  374  C   GLN A 278     1435   1427   1895   -226    173   -349       C  
ATOM    375  O   GLN A 278      42.778   6.107  14.363  1.00 12.08           O  
ANISOU  375  O   GLN A 278     1356   1373   1859    -50    123     22       O  
ATOM    376  CB  GLN A 278      40.951   3.456  15.197  1.00 13.56           C  
ANISOU  376  CB  GLN A 278     1685   1231   2237   -418      4    171       C  
ATOM    377  CG  GLN A 278      39.889   2.444  14.813  1.00 15.07           C  
ANISOU  377  CG  GLN A 278     1684   1267   2773   -575    158    189       C  
ATOM    378  CD  GLN A 278      40.111   1.126  15.496  1.00 17.34           C  
ANISOU  378  CD  GLN A 278     1914   1734   2941   -506    255    -38       C  
ATOM    379  OE1 GLN A 278      41.217   0.836  15.936  1.00 19.32           O  
ANISOU  379  OE1 GLN A 278     2097   1938   3305   -385     84    -13       O  
ATOM    380  NE2 GLN A 278      39.060   0.314  15.591  1.00 18.58           N  
ANISOU  380  NE2 GLN A 278     2151   1703   3204   -527    282     54       N  
ATOM    381  N   GLY A 279      41.640   6.229  16.301  1.00 13.48           N  
ANISOU  381  N   GLY A 279     1687   1450   1984   -147     -8   -480       N  
ATOM    382  CA  GLY A 279      42.597   7.114  16.940  1.00 12.86           C  
ANISOU  382  CA  GLY A 279     1436   1353   2098   -477    146   -166       C  
ATOM    383  C   GLY A 279      42.772   8.408  16.177  1.00 12.48           C  
ANISOU  383  C   GLY A 279     1441   1384   1916   -341    -90   -200       C  
ATOM    384  O   GLY A 279      41.792   9.067  15.828  1.00 15.24           O  
ANISOU  384  O   GLY A 279     1638   1732   2420    -94    151   -160       O  
ATOM    385  N   THR A 280      44.025   8.771  15.918  1.00 11.43           N  
ANISOU  385  N   THR A 280     1545   1106   1692    -39    116    -35       N  
ATOM    386  CA  THR A 280      44.329   9.971  15.146  1.00 11.68           C  
ANISOU  386  CA  THR A 280     1460   1133   1845    211     71     13       C  
ATOM    387  C   THR A 280      44.733   9.622  13.713  1.00 10.18           C  
ANISOU  387  C   THR A 280     1397    907   1565    112    -48   -109       C  
ATOM    388  O   THR A 280      45.318  10.432  12.991  1.00 11.37           O  
ANISOU  388  O   THR A 280     1343   1100   1875    114    154    -82       O  
ATOM    389  CB  THR A 280      45.442  10.790  15.821  1.00 12.22           C  
ANISOU  389  CB  THR A 280     1218   1360   2065    199    -91   -421       C  
ATOM    390  OG1 THR A 280      46.591   9.954  16.023  1.00 11.27           O  
ANISOU  390  OG1 THR A 280     1355   1148   1780    295    -21   -274       O  
ATOM    391  CG2 THR A 280      44.962  11.307  17.169  1.00 14.26           C  
ANISOU  391  CG2 THR A 280     1558   1662   2197    304    348   -769       C  
ATOM    392  N   THR A 281      44.406   8.410  13.289  1.00 10.42           N  
ANISOU  392  N   THR A 281     1334   1125   1499     62    -78   -207       N  
ATOM    393  CA  THR A 281      44.857   7.936  11.989  1.00 10.38           C  
ANISOU  393  CA  THR A 281     1428    869   1645     72     -1   -176       C  
ATOM    394  C   THR A 281      44.082   8.542  10.830  1.00 11.54           C  
ANISOU  394  C   THR A 281     1664   1228   1492    197   -128    125       C  
ATOM    395  O   THR A 281      42.853   8.640  10.863  1.00 13.70           O  
ANISOU  395  O   THR A 281     1577   1616   2013    427    -12     22       O  
ATOM    396  CB  THR A 281      44.796   6.396  11.909  1.00 10.11           C  
ANISOU  396  CB  THR A 281     1419    807   1613    -59     87   -321       C  
ATOM    397  OG1 THR A 281      45.561   5.857  12.990  1.00 10.48           O  
ANISOU  397  OG1 THR A 281     1344   1151   1485     34   -249    -31       O  
ATOM    398  CG2 THR A 281      45.369   5.891  10.587  1.00 11.08           C  
ANISOU  398  CG2 THR A 281     1684    944   1583    284    259    -74       C  
ATOM    399  N   THR A 282      44.811   8.945   9.797  1.00 11.68           N  
ANISOU  399  N   THR A 282     1800   1089   1549    286   -284    152       N  
ATOM    400  CA  THR A 282      44.164   9.376   8.574  1.00 12.27           C  
ANISOU  400  CA  THR A 282     1804   1316   1543    389    -11    293       C  
ATOM    401  C   THR A 282      44.779   8.671   7.364  1.00 11.72           C  
ANISOU  401  C   THR A 282     1458   1289   1704    126    248    267       C  
ATOM    402  O   THR A 282      45.524   7.703   7.518  1.00 11.57           O  
ANISOU  402  O   THR A 282     1420   1307   1667    221    -89    146       O  
ATOM    403  CB  THR A 282      44.119  10.923   8.461  1.00 13.56           C  
ANISOU  403  CB  THR A 282     1633   1543   1977    457     -3    405       C  
ATOM    404  OG1 THR A 282      43.217  11.313   7.411  1.00 14.10           O  
ANISOU  404  OG1 THR A 282     1912   1422   2021    515    277    124       O  
ATOM    405  CG2 THR A 282      45.512  11.512   8.227  1.00 15.43           C  
ANISOU  405  CG2 THR A 282     1415   1529   2918   -152    244    510       C  
ATOM    406  N   VAL A 283      44.450   9.137   6.167  1.00 10.43           N  
ANISOU  406  N   VAL A 283     1450   1224   1288    133    255    -22       N  
ATOM    407  CA  VAL A 283      44.725   8.392   4.950  1.00 10.85           C  
ANISOU  407  CA  VAL A 283     1441   1321   1360    110    -22    143       C  
ATOM    408  C   VAL A 283      46.143   8.582   4.407  1.00 10.12           C  
ANISOU  408  C   VAL A 283     1193   1028   1624     17     80    214       C  
ATOM    409  O   VAL A 283      46.821   7.601   4.068  1.00 11.48           O  
ANISOU  409  O   VAL A 283     1408   1241   1714    258   -106    139       O  
ATOM    410  CB  VAL A 283      43.687   8.756   3.860  1.00 11.72           C  
ANISOU  410  CB  VAL A 283     1535   1755   1162    114     -2    -73       C  
ATOM    411  CG1 VAL A 283      44.037   8.119   2.529  1.00 15.13           C  
ANISOU  411  CG1 VAL A 283     1846   2123   1779    420   -435   -188       C  
ATOM    412  CG2 VAL A 283      42.283   8.354   4.301  1.00 15.66           C  
ANISOU  412  CG2 VAL A 283     1534   1735   2680     25    120    194       C  
ATOM    413  N   SER A 284      46.590   9.832   4.306  1.00 10.31           N  
ANISOU  413  N   SER A 284     1261   1092   1563   -130     87    252       N  
ATOM    414  CA  SER A 284      47.850  10.125   3.626  1.00 10.37           C  
ANISOU  414  CA  SER A 284     1286   1103   1550    -55    101    236       C  
ATOM    415  C   SER A 284      49.074  10.130   4.538  1.00 10.10           C  
ANISOU  415  C   SER A 284     1188   1234   1413     93     76    142       C  
ATOM    416  O   SER A 284      49.043  10.685   5.647  1.00 10.77           O  
ANISOU  416  O   SER A 284     1300   1322   1471    121     97    -18       O  
ATOM    417  CB  SER A 284      47.761  11.472   2.896  1.00 11.07           C  
ANISOU  417  CB  SER A 284     1391   1076   1738   -139    495    521       C  
ATOM    418  OG  SER A 284      48.981  11.763   2.222  1.00 10.38           O  
ANISOU  418  OG  SER A 284     1508    996   1439     37     48    235       O  
ATOM    419  N   ALA A 285      50.168   9.546   4.051  1.00 10.03           N  
ANISOU  419  N   ALA A 285     1038   1119   1653     38    108     54       N  
ATOM    420  CA  ALA A 285      51.436   9.606   4.773  1.00 10.22           C  
ANISOU  420  CA  ALA A 285      846   1152   1884    141      9   -134       C  
ATOM    421  C   ALA A 285      51.925  11.045   4.927  1.00 10.22           C  
ANISOU  421  C   ALA A 285     1249   1050   1582     65    -15    175       C  
ATOM    422  O   ALA A 285      52.746  11.328   5.791  1.00 11.92           O  
ANISOU  422  O   ALA A 285     1388   1323   1819    112   -103    -92       O  
ATOM    423  CB  ALA A 285      52.493   8.756   4.081  1.00 11.60           C  
ANISOU  423  CB  ALA A 285     1064   1405   1936    433    243    -57       C  
ATOM    424  N   ALA A 286      51.420  11.950   4.088  1.00 10.08           N  
ANISOU  424  N   ALA A 286     1704    744   1380    122     66     59       N  
ATOM    425  CA  ALA A 286      51.767  13.370   4.206  1.00 11.38           C  
ANISOU  425  CA  ALA A 286     1883    980   1462    119     73    240       C  
ATOM    426  C   ALA A 286      51.280  14.000   5.514  1.00 11.47           C  
ANISOU  426  C   ALA A 286     1865   1375   1118     94    248    -30       C  
ATOM    427  O   ALA A 286      51.716  15.091   5.876  1.00 14.39           O  
ANISOU  427  O   ALA A 286     2162   1212   2093   -289    214     19       O  
ATOM    428  CB  ALA A 286      51.224  14.168   3.009  1.00 11.98           C  
ANISOU  428  CB  ALA A 286     2016    930   1607    -61   -215    270       C  
ATOM    429  N   CYS A 287      50.401  13.313   6.236  1.00  9.89           N  
ANISOU  429  N   CYS A 287     1320   1353   1083    223    113    160       N  
ATOM    430  CA  CYS A 287      49.876  13.856   7.483  1.00  9.72           C  
ANISOU  430  CA  CYS A 287     1052   1409   1230    105    156    131       C  
ATOM    431  C   CYS A 287      50.582  13.348   8.738  1.00  9.55           C  
ANISOU  431  C   CYS A 287     1222   1138   1266    162   -290     -8       C  
ATOM    432  O   CYS A 287      50.341  13.846   9.834  1.00 10.61           O  
ANISOU  432  O   CYS A 287     1443   1064   1525    193   -143   -105       O  
ATOM    433  CB  CYS A 287      48.381  13.544   7.597  1.00 11.34           C  
ANISOU  433  CB  CYS A 287     1085   1521   1703    301   -106    238       C  
ATOM    434  SG  CYS A 287      47.404  14.282   6.272  1.00 14.31           S  
ANISOU  434  SG  CYS A 287     1576   2025   1837    500   -262     75       S  
ATOM    435  N   ILE A 288      51.427  12.333   8.593  1.00  8.97           N  
ANISOU  435  N   ILE A 288     1043    752   1612    132   -229    189       N  
ATOM    436  CA  ILE A 288      51.954  11.646   9.761  1.00  8.92           C  
ANISOU  436  CA  ILE A 288     1304    674   1410    213   -197   -112       C  
ATOM    437  C   ILE A 288      52.888  12.513  10.603  1.00  9.33           C  
ANISOU  437  C   ILE A 288     1453    678   1412    108   -403   -235       C  
ATOM    438  O   ILE A 288      53.851  13.091  10.085  1.00 10.54           O  
ANISOU  438  O   ILE A 288     1313    940   1750     93     12    -80       O  
ATOM    439  CB  ILE A 288      52.688  10.354   9.352  1.00  8.51           C  
ANISOU  439  CB  ILE A 288     1016    505   1711     45   -275   -106       C  
ATOM    440  CG1 ILE A 288      51.732   9.392   8.637  1.00  9.98           C  
ANISOU  440  CG1 ILE A 288     1288    735   1768   -113   -137   -217       C  
ATOM    441  CG2 ILE A 288      53.318   9.683  10.576  1.00 10.07           C  
ANISOU  441  CG2 ILE A 288     1283   1048   1493    414   -305    162       C  
ATOM    442  CD1 ILE A 288      52.462   8.252   7.946  1.00 12.27           C  
ANISOU  442  CD1 ILE A 288     1865   1036   1760    324   -248   -410       C  
ATOM    443  N   ALA A 289      52.578  12.596  11.899  1.00  9.32           N  
ANISOU  443  N   ALA A 289     1616    776   1149    248   -328   -341       N  
ATOM    444  CA  ALA A 289      53.420  13.276  12.883  1.00  9.25           C  
ANISOU  444  CA  ALA A 289     1310    725   1480    225   -420    -93       C  
ATOM    445  C   ALA A 289      53.551  14.768  12.611  1.00  9.26           C  
ANISOU  445  C   ALA A 289     1095    751   1671     40   -114     58       C  
ATOM    446  O   ALA A 289      54.593  15.368  12.849  1.00 14.64           O  
ANISOU  446  O   ALA A 289     1484   1064   3013     74   -915    200       O  
ATOM    447  CB  ALA A 289      54.795  12.603  12.986  1.00 11.11           C  
ANISOU  447  CB  ALA A 289     1194    899   2126    214   -597    -96       C  
ATOM    448  N   ARG A 290      52.470  15.358  12.118  1.00  9.46           N  
ANISOU  448  N   ARG A 290     1129    711   1752    297   -142    -70       N  
ATOM    449  CA  ARG A 290      52.412  16.795  11.887  1.00  9.12           C  
ANISOU  449  CA  ARG A 290     1233    815   1417    402     45    -67       C  
ATOM    450  C   ARG A 290      51.354  17.434  12.766  1.00  9.66           C  
ANISOU  450  C   ARG A 290     1124    925   1622    132    -63     23       C  
ATOM    451  O   ARG A 290      50.495  16.738  13.317  1.00  9.87           O  
ANISOU  451  O   ARG A 290     1350    858   1541    139   -116    -50       O  
ATOM    452  CB  ARG A 290      52.142  17.089  10.409  1.00 10.60           C  
ANISOU  452  CB  ARG A 290     1448   1242   1335    256     23   -193       C  
ATOM    453  CG  ARG A 290      53.303  16.666   9.512  1.00 12.25           C  
ANISOU  453  CG  ARG A 290     1717   1550   1385    292    133      4       C  
ATOM    454  CD  ARG A 290      53.068  17.008   8.054  1.00 16.38           C  
ANISOU  454  CD  ARG A 290     2254   2365   1604    233    163   -202       C  
ATOM    455  NE  ARG A 290      54.108  16.445   7.197  1.00 18.70           N  
ANISOU  455  NE  ARG A 290     2519   2501   2084   -198    461    -32       N  
ATOM    456  CZ  ARG A 290      55.060  17.155   6.598  1.00 21.97           C  
ANISOU  456  CZ  ARG A 290     2930   2572   2846    -40     97   -710       C  
ATOM    457  NH1 ARG A 290      55.121  18.469   6.765  1.00 24.12           N  
ANISOU  457  NH1 ARG A 290     3395   2307   3461     21   -474   -199       N  
ATOM    458  NH2 ARG A 290      55.956  16.546   5.825  1.00 21.98           N  
ANISOU  458  NH2 ARG A 290     2982   2955   2415   -165    -49   -264       N  
ATOM    459  N   MET A 291      51.441  18.755  12.900  1.00  9.52           N  
ANISOU  459  N   MET A 291     1282    764   1569    338    -42   -123       N  
ATOM    460  CA  MET A 291      50.447  19.556  13.606  1.00  8.98           C  
ANISOU  460  CA  MET A 291     1291    779   1342    369   -132   -137       C  
ATOM    461  C   MET A 291      50.174  20.815  12.808  1.00  9.55           C  
ANISOU  461  C   MET A 291     1473    863   1290    527   -204     33       C  
ATOM    462  O   MET A 291      50.969  21.213  11.950  1.00 10.20           O  
ANISOU  462  O   MET A 291     1481    871   1524    342   -122    -15       O  
ATOM    463  CB  MET A 291      50.953  19.979  14.986  1.00  9.57           C  
ANISOU  463  CB  MET A 291     1303   1003   1331    337   -190    195       C  
ATOM    464  CG  MET A 291      51.493  18.861  15.861  1.00  9.91           C  
ANISOU  464  CG  MET A 291     1466   1137   1161    259   -195    -22       C  
ATOM    465  SD  MET A 291      52.192  19.613  17.359  1.00 10.95           S  
ANISOU  465  SD  MET A 291     1438   1055   1667    303   -238   -155       S  
ATOM    466  CE  MET A 291      52.973  18.197  18.131  1.00 11.35           C  
ANISOU  466  CE  MET A 291     1519   1174   1620    474   -412     30       C  
ATOM    467  N   ARG A 292      49.058  21.459  13.122  1.00  9.38           N  
ANISOU  467  N   ARG A 292     1327    634   1601    397    -59    -61       N  
ATOM    468  CA  ARG A 292      48.738  22.756  12.547  1.00  9.23           C  
ANISOU  468  CA  ARG A 292     1362    737   1408    475   -198    -98       C  
ATOM    469  C   ARG A 292      48.023  23.591  13.589  1.00  8.97           C  
ANISOU  469  C   ARG A 292     1274    808   1326    442     -1   -247       C  
ATOM    470  O   ARG A 292      47.239  23.072  14.381  1.00 10.15           O  
ANISOU  470  O   ARG A 292     1256   1008   1593    287     -7    -67       O  
ATOM    471  CB  ARG A 292      47.856  22.609  11.303  1.00 10.16           C  
ANISOU  471  CB  ARG A 292     1396    971   1493    443   -429    203       C  
ATOM    472  CG  ARG A 292      47.477  23.942  10.655  1.00 10.38           C  
ANISOU  472  CG  ARG A 292     1301   1126   1517    362    -54    162       C  
ATOM    473  CD  ARG A 292      46.882  23.733   9.268  1.00 10.57           C  
ANISOU  473  CD  ARG A 292     1398   1293   1325    464   -360    185       C  
ATOM    474  NE  ARG A 292      46.470  25.000   8.666  1.00 11.76           N  
ANISOU  474  NE  ARG A 292     1396   1365   1707    320   -315    177       N  
ATOM    475  CZ  ARG A 292      46.325  25.199   7.363  1.00 12.33           C  
ANISOU  475  CZ  ARG A 292     1426   1658   1602    417   -266     79       C  
ATOM    476  NH1 ARG A 292      46.561  24.208   6.510  1.00 13.54           N  
ANISOU  476  NH1 ARG A 292     1539   1825   1779    151     62   -232       N  
ATOM    477  NH2 ARG A 292      45.949  26.393   6.914  1.00 14.33           N  
ANISOU  477  NH2 ARG A 292     1800   1573   2070    465   -239    150       N  
ATOM    478  N   GLY A 293      48.284  24.889  13.587  1.00 10.10           N  
ANISOU  478  N   GLY A 293     1337    903   1598    552    -11   -233       N  
ATOM    479  CA  GLY A 293      47.472  25.783  14.392  1.00 11.15           C  
ANISOU  479  CA  GLY A 293     1407    895   1932    546     53   -152       C  
ATOM    480  C   GLY A 293      48.069  27.159  14.527  1.00  9.97           C  
ANISOU  480  C   GLY A 293     1251    793   1745    294    -82   -185       C  
ATOM    481  O   GLY A 293      49.033  27.508  13.842  1.00 11.82           O  
ANISOU  481  O   GLY A 293     1631   1020   1839    366    320   -154       O  
ATOM    482  N   ARG A 294      47.492  27.944  15.431  1.00  9.77           N  
ANISOU  482  N   ARG A 294     1284    946   1483    301    -33   -433       N  
ATOM    483  CA  ARG A 294      47.896  29.332  15.606  1.00  9.82           C  
ANISOU  483  CA  ARG A 294     1371    816   1544    465   -211   -302       C  
ATOM    484  C   ARG A 294      48.718  29.456  16.871  1.00 10.08           C  
ANISOU  484  C   ARG A 294     1336    889   1605    315    184   -316       C  
ATOM    485  O   ARG A 294      48.303  29.011  17.938  1.00 10.90           O  
ANISOU  485  O   ARG A 294     1509   1162   1469    339    -54   -166       O  
ATOM    486  CB  ARG A 294      46.676  30.249  15.669  1.00 10.56           C  
ANISOU  486  CB  ARG A 294     1289   1007   1715    627    -12    -21       C  
ATOM    487  CG  ARG A 294      47.017  31.720  15.462  1.00 15.07           C  
ANISOU  487  CG  ARG A 294     1646   1090   2991    495    203     37       C  
ATOM    488  CD  ARG A 294      45.746  32.565  15.239  1.00 17.26           C  
ANISOU  488  CD  ARG A 294     1790   1484   3283    670    -35   -473       C  
ATOM    489  NE  ARG A 294      44.959  32.065  14.112  1.00 17.50           N  
ANISOU  489  NE  ARG A 294     2012   2174   2461   1122   -201   -195       N  
ATOM    490  CZ  ARG A 294      45.173  32.394  12.842  1.00 19.74           C  
ANISOU  490  CZ  ARG A 294     2320   2174   3004    889   -730     15       C  
ATOM    491  NH1 ARG A 294      46.128  33.258  12.529  1.00 20.72           N  
ANISOU  491  NH1 ARG A 294     2599   2161   3113    680   -523   -170       N  
ATOM    492  NH2 ARG A 294      44.427  31.864  11.881  1.00 20.11           N  
ANISOU  492  NH2 ARG A 294     2707   2276   2659   1284   -448   -377       N  
ATOM    493  N   ILE A 295      49.897  30.049  16.744  1.00 10.79           N  
ANISOU  493  N   ILE A 295     1542    898   1658    334   -174   -224       N  
ATOM    494  CA  ILE A 295      50.762  30.250  17.900  1.00 10.76           C  
ANISOU  494  CA  ILE A 295     1451   1060   1577    263    -64   -211       C  
ATOM    495  C   ILE A 295      50.219  31.387  18.761  1.00 11.16           C  
ANISOU  495  C   ILE A 295     1552   1117   1570    446   -347    -93       C  
ATOM    496  O   ILE A 295      49.822  32.438  18.249  1.00 11.82           O  
ANISOU  496  O   ILE A 295     1669   1009   1812    403   -197    -79       O  
ATOM    497  CB  ILE A 295      52.222  30.509  17.464  1.00 11.70           C  
ANISOU  497  CB  ILE A 295     1444   1148   1853    218   -278   -592       C  
ATOM    498  CG1 ILE A 295      52.806  29.211  16.887  1.00 12.32           C  
ANISOU  498  CG1 ILE A 295     1329   1346   2004    493    -58   -645       C  
ATOM    499  CG2 ILE A 295      53.069  30.999  18.637  1.00 13.28           C  
ANISOU  499  CG2 ILE A 295     1861   1137   2046    244   -480   -414       C  
ATOM    500  CD1 ILE A 295      54.199  29.346  16.290  1.00 13.35           C  
ANISOU  500  CD1 ILE A 295     1400   1632   2040    536     80   -315       C  
ATOM    501  N   PHE A 296      50.189  31.163  20.070  1.00 11.84           N  
ANISOU  501  N   PHE A 296     1713   1234   1552    416   -189   -376       N  
ATOM    502  CA  PHE A 296      49.741  32.177  21.012  1.00 11.13           C  
ANISOU  502  CA  PHE A 296     1510   1181   1536    273   -136   -360       C  
ATOM    503  C   PHE A 296      50.752  32.415  22.116  1.00 11.88           C  
ANISOU  503  C   PHE A 296     1644   1337   1534    458   -366   -301       C  
ATOM    504  O   PHE A 296      51.680  31.634  22.310  1.00 12.58           O  
ANISOU  504  O   PHE A 296     1526   1395   1860    501   -279   -240       O  
ATOM    505  CB  PHE A 296      48.379  31.803  21.612  1.00 12.85           C  
ANISOU  505  CB  PHE A 296     1767   1307   1808    564   -122    145       C  
ATOM    506  CG  PHE A 296      48.391  30.557  22.474  1.00 12.00           C  
ANISOU  506  CG  PHE A 296     1822   1236   1500    392   -397   -557       C  
ATOM    507  CD1 PHE A 296      48.824  30.603  23.796  1.00 12.76           C  
ANISOU  507  CD1 PHE A 296     1855   1350   1644    484   -343     53       C  
ATOM    508  CD2 PHE A 296      47.914  29.350  21.973  1.00 12.62           C  
ANISOU  508  CD2 PHE A 296     1659   1006   2131    455   -260   -165       C  
ATOM    509  CE1 PHE A 296      48.808  29.466  24.588  1.00 13.44           C  
ANISOU  509  CE1 PHE A 296     1890   1535   1679    454   -307   -200       C  
ATOM    510  CE2 PHE A 296      47.884  28.218  22.755  1.00 12.57           C  
ANISOU  510  CE2 PHE A 296     1745   1378   1654    585   -237   -308       C  
ATOM    511  CZ  PHE A 296      48.336  28.268  24.066  1.00 13.01           C  
ANISOU  511  CZ  PHE A 296     1692   1370   1880    494    175   -142       C  
ATOM    512  N   ASN A 297      50.558  33.511  22.836  1.00 13.56           N  
ANISOU  512  N   ASN A 297     2211   1182   1759    427   -418   -511       N  
ATOM    513  CA  ASN A 297      51.354  33.838  24.004  1.00 16.04           C  
ANISOU  513  CA  ASN A 297     2672   1587   1836    678   -409   -527       C  
ATOM    514  C   ASN A 297      50.388  34.384  25.031  1.00 17.14           C  
ANISOU  514  C   ASN A 297     2921   2016   1576    968   -217   -621       C  
ATOM    515  O   ASN A 297      49.740  35.406  24.806  1.00 18.48           O  
ANISOU  515  O   ASN A 297     2815   1844   2363   1080   -211   -417       O  
ATOM    516  CB  ASN A 297      52.423  34.883  23.655  1.00 19.86           C  
ANISOU  516  CB  ASN A 297     2968   1737   2841    268  -1209   -893       C  
ATOM    517  CG  ASN A 297      53.221  35.340  24.861  1.00 28.36           C  
ANISOU  517  CG  ASN A 297     3728   2478   4568    556  -1869   -869       C  
ATOM    518  OD1 ASN A 297      53.651  34.535  25.683  1.00 30.65           O  
ANISOU  518  OD1 ASN A 297     4359   2868   4416    372  -1706  -1191       O  
ATOM    519  ND2 ASN A 297      53.437  36.640  24.961  1.00 34.27           N  
ANISOU  519  ND2 ASN A 297     4221   3082   5716    771  -2035  -1338       N  
ATOM    520  N   ASN A 298      50.261  33.674  26.143  1.00 19.96           N  
ANISOU  520  N   ASN A 298     3260   2449   1873   1285      2   -661       N  
ATOM    521  CA  ASN A 298      49.325  34.061  27.185  1.00 26.60           C  
ANISOU  521  CA  ASN A 298     4293   3567   2245   2219    259   -106       C  
ATOM    522  C   ASN A 298      49.856  33.699  28.555  1.00 31.81           C  
ANISOU  522  C   ASN A 298     5259   4268   2560   2669    351    -92       C  
ATOM    523  O   ASN A 298      50.343  32.591  28.768  1.00 32.71           O  
ANISOU  523  O   ASN A 298     5473   4528   2426   2861    374     88       O  
ATOM    524  CB  ASN A 298      47.983  33.372  26.965  1.00 29.66           C  
ANISOU  524  CB  ASN A 298     4332   3857   3081   2273   1210    879       C  
ATOM    525  CG  ASN A 298      46.958  33.757  28.009  1.00 34.80           C  
ANISOU  525  CG  ASN A 298     4522   4469   4231   2418   1558   1544       C  
ATOM    526  OD1 ASN A 298      46.951  33.224  29.117  1.00 32.55           O  
ANISOU  526  OD1 ASN A 298     4527   4227   3614   2408   1421   1274       O  
ATOM    527  ND2 ASN A 298      46.082  34.688  27.658  1.00 39.55           N  
ANISOU  527  ND2 ASN A 298     4769   5118   5138   2589   1690   1971       N  
ATOM    528  N   ASN A 299      49.756  34.639  29.487  1.00 35.25           N  
ANISOU  528  N   ASN A 299     5688   4843   2861   2780    234   -534       N  
ATOM    529  CA  ASN A 299      50.151  34.387  30.864  1.00 38.41           C  
ANISOU  529  CA  ASN A 299     6258   5444   2890   3143     60   -570       C  
ATOM    530  C   ASN A 299      51.601  33.907  30.958  1.00 38.76           C  
ANISOU  530  C   ASN A 299     6205   5353   3168   3094   -229   -909       C  
ATOM    531  O   ASN A 299      51.926  33.042  31.769  1.00 39.88           O  
ANISOU  531  O   ASN A 299     6454   5445   3251   3252    -29   -691       O  
ATOM    532  CB  ASN A 299      49.198  33.369  31.498  1.00 41.05           C  
ANISOU  532  CB  ASN A 299     6858   6096   2641   3119    334   -259       C  
ATOM    533  CG  ASN A 299      49.291  33.342  33.012  1.00 45.98           C  
ANISOU  533  CG  ASN A 299     7446   6653   3372   3198    526    -83       C  
ATOM    534  OD1 ASN A 299      49.825  34.261  33.631  1.00 46.88           O  
ANISOU  534  OD1 ASN A 299     7720   6713   3377   3216    754   -480       O  
ATOM    535  ND2 ASN A 299      48.763  32.283  33.617  1.00 47.40           N  
ANISOU  535  ND2 ASN A 299     7601   6764   3646   3200    530    416       N  
ATOM    536  N   GLY A 300      52.465  34.469  30.114  1.00 38.47           N  
ANISOU  536  N   GLY A 300     5857   5187   3573   2761   -490  -1449       N  
ATOM    537  CA  GLY A 300      53.891  34.195  30.172  1.00 38.46           C  
ANISOU  537  CA  GLY A 300     5752   4833   4029   2721   -946  -1579       C  
ATOM    538  C   GLY A 300      54.351  32.916  29.491  1.00 36.67           C  
ANISOU  538  C   GLY A 300     5451   4588   3893   2714  -1234  -1385       C  
ATOM    539  O   GLY A 300      55.496  32.494  29.654  1.00 37.73           O  
ANISOU  539  O   GLY A 300     5439   4677   4218   2594   -999  -1557       O  
ATOM    540  N   ASN A 301      53.466  32.297  28.719  1.00 29.81           N  
ANISOU  540  N   ASN A 301     4825   3990   2511   2259  -1234  -1168       N  
ATOM    541  CA  ASN A 301      53.791  31.036  28.067  1.00 25.84           C  
ANISOU  541  CA  ASN A 301     4554   3303   1959   1919  -1008   -672       C  
ATOM    542  C   ASN A 301      53.262  30.964  26.646  1.00 19.09           C  
ANISOU  542  C   ASN A 301     3412   2249   1591   1291   -828   -272       C  
ATOM    543  O   ASN A 301      52.196  31.500  26.331  1.00 19.84           O  
ANISOU  543  O   ASN A 301     3319   2407   1811   1598   -435   -352       O  
ATOM    544  CB  ASN A 301      53.268  29.857  28.886  1.00 29.98           C  
ANISOU  544  CB  ASN A 301     5196   3582   2611   1671  -1134   -243       C  
ATOM    545  CG  ASN A 301      53.965  29.725  30.229  1.00 33.48           C  
ANISOU  545  CG  ASN A 301     5646   4007   3069   1672   -976   -121       C  
ATOM    546  OD1 ASN A 301      53.448  30.163  31.254  1.00 35.67           O  
ANISOU  546  OD1 ASN A 301     5896   3945   3710   1525   -838   -832       O  
ATOM    547  ND2 ASN A 301      55.149  29.125  30.224  1.00 35.64           N  
ANISOU  547  ND2 ASN A 301     5930   4128   3481   1840  -1033     85       N  
ATOM    548  N   TYR A 302      54.023  30.300  25.787  1.00 15.03           N  
ANISOU  548  N   TYR A 302     2584   1432   1695    430   -327   -521       N  
ATOM    549  CA  TYR A 302      53.638  30.143  24.394  1.00 12.71           C  
ANISOU  549  CA  TYR A 302     1924   1227   1676    412   -177   -614       C  
ATOM    550  C   TYR A 302      52.911  28.821  24.183  1.00 11.47           C  
ANISOU  550  C   TYR A 302     1580   1216   1560    371   -575   -447       C  
ATOM    551  O   TYR A 302      53.042  27.889  24.971  1.00 12.84           O  
ANISOU  551  O   TYR A 302     1864   1208   1806    719   -293   -257       O  
ATOM    552  CB  TYR A 302      54.870  30.215  23.490  1.00 13.64           C  
ANISOU  552  CB  TYR A 302     1695   1428   2060    226   -230   -405       C  
ATOM    553  CG  TYR A 302      55.614  31.531  23.585  1.00 14.85           C  
ANISOU  553  CG  TYR A 302     1961   1212   2468    338   -372   -543       C  
ATOM    554  CD1 TYR A 302      55.398  32.542  22.661  1.00 16.16           C  
ANISOU  554  CD1 TYR A 302     2217   1365   2559    220   -214   -328       C  
ATOM    555  CD2 TYR A 302      56.532  31.757  24.600  1.00 17.51           C  
ANISOU  555  CD2 TYR A 302     2249   1300   3105    181   -374   -540       C  
ATOM    556  CE1 TYR A 302      56.077  33.741  22.746  1.00 18.42           C  
ANISOU  556  CE1 TYR A 302     2468   1272   3259    167   -425   -180       C  
ATOM    557  CE2 TYR A 302      57.214  32.954  24.696  1.00 19.29           C  
ANISOU  557  CE2 TYR A 302     2505   1393   3432    172   -246    -16       C  
ATOM    558  CZ  TYR A 302      56.978  33.944  23.768  1.00 20.05           C  
ANISOU  558  CZ  TYR A 302     2594   1190   3833   -271   -306    -36       C  
ATOM    559  OH  TYR A 302      57.654  35.141  23.857  1.00 24.03           O  
ANISOU  559  OH  TYR A 302     3030   1536   4562   -340   -363   -171       O  
ATOM    560  N   GLY A 303      52.144  28.748  23.107  1.00 11.00           N  
ANISOU  560  N   GLY A 303     1423   1091   1663    384   -465   -407       N  
ATOM    561  CA  GLY A 303      51.434  27.531  22.783  1.00 11.15           C  
ANISOU  561  CA  GLY A 303     1448   1111   1676    364   -639   -383       C  
ATOM    562  C   GLY A 303      50.902  27.555  21.372  1.00 11.20           C  
ANISOU  562  C   GLY A 303     1435   1107   1713    398   -367   -171       C  
ATOM    563  O   GLY A 303      51.092  28.529  20.626  1.00 11.45           O  
ANISOU  563  O   GLY A 303     1590   1165   1595    388   -239   -177       O  
ATOM    564  N   VAL A 304      50.226  26.473  21.002  1.00 10.34           N  
ANISOU  564  N   VAL A 304     1463    968   1497    311   -248   -198       N  
ATOM    565  CA  VAL A 304      49.510  26.414  19.736  1.00 10.62           C  
ANISOU  565  CA  VAL A 304     1383   1249   1401    339   -229   -277       C  
ATOM    566  C   VAL A 304      48.049  26.040  19.979  1.00 10.79           C  
ANISOU  566  C   VAL A 304     1350   1078   1670    480    -75   -290       C  
ATOM    567  O   VAL A 304      47.760  25.087  20.723  1.00 11.39           O  
ANISOU  567  O   VAL A 304     1488   1089   1749    396   -147   -192       O  
ATOM    568  CB  VAL A 304      50.159  25.399  18.753  1.00 11.58           C  
ANISOU  568  CB  VAL A 304     1470   1470   1459    325   -336   -397       C  
ATOM    569  CG1 VAL A 304      49.278  25.205  17.528  1.00 13.97           C  
ANISOU  569  CG1 VAL A 304     1877   1985   1444    856   -212   -318       C  
ATOM    570  CG2 VAL A 304      51.549  25.865  18.349  1.00 14.74           C  
ANISOU  570  CG2 VAL A 304     1488   1641   2469     45     -4   -149       C  
ATOM    571  N   ASN A 305      47.141  26.811  19.372  1.00 10.42           N  
ANISOU  571  N   ASN A 305      994   1215   1750    485   -148   -152       N  
ATOM    572  CA  ASN A 305      45.742  26.425  19.249  1.00 10.61           C  
ANISOU  572  CA  ASN A 305     1230   1127   1675    602    -96   -316       C  
ATOM    573  C   ASN A 305      45.602  25.553  18.019  1.00  9.52           C  
ANISOU  573  C   ASN A 305     1227    899   1491    280      1   -462       C  
ATOM    574  O   ASN A 305      45.767  26.031  16.895  1.00 10.53           O  
ANISOU  574  O   ASN A 305     1414   1049   1539    393     95    -88       O  
ATOM    575  CB  ASN A 305      44.844  27.664  19.111  1.00 11.34           C  
ANISOU  575  CB  ASN A 305     1563   1142   1603    651     46   -362       C  
ATOM    576  CG  ASN A 305      44.767  28.468  20.385  1.00 11.34           C  
ANISOU  576  CG  ASN A 305     1732   1159   1418    664    -61   -269       C  
ATOM    577  OD1 ASN A 305      44.506  27.925  21.453  1.00 13.76           O  
ANISOU  577  OD1 ASN A 305     2208   1376   1644    727    183   -241       O  
ATOM    578  ND2 ASN A 305      45.022  29.777  20.282  1.00 12.58           N  
ANISOU  578  ND2 ASN A 305     1727   1165   1886    721   -191   -325       N  
ATOM    579  N   LEU A 306      45.297  24.277  18.231  1.00 10.38           N  
ANISOU  579  N   LEU A 306     1342    861   1742    317    -96   -478       N  
ATOM    580  CA  LEU A 306      45.355  23.280  17.168  1.00  9.88           C  
ANISOU  580  CA  LEU A 306     1346    869   1540    231   -107   -188       C  
ATOM    581  C   LEU A 306      44.166  23.304  16.216  1.00  9.64           C  
ANISOU  581  C   LEU A 306     1244   1034   1383    102   -298   -160       C  
ATOM    582  O   LEU A 306      43.038  23.627  16.600  1.00 12.18           O  
ANISOU  582  O   LEU A 306     1191   1482   1955    373    204   -239       O  
ATOM    583  CB  LEU A 306      45.487  21.882  17.774  1.00 11.03           C  
ANISOU  583  CB  LEU A 306     1711    917   1564    423   -203   -131       C  
ATOM    584  CG  LEU A 306      46.763  21.585  18.566  1.00 11.98           C  
ANISOU  584  CG  LEU A 306     1742   1199   1611    573   -123   -101       C  
ATOM    585  CD1 LEU A 306      46.606  20.314  19.407  1.00 14.07           C  
ANISOU  585  CD1 LEU A 306     2116   1311   1920    443    155    326       C  
ATOM    586  CD2 LEU A 306      47.958  21.473  17.621  1.00 11.96           C  
ANISOU  586  CD2 LEU A 306     1657   1373   1515    435    401    -51       C  
ATOM    587  N   ALA A 307      44.452  22.950  14.967  1.00 10.24           N  
ANISOU  587  N   ALA A 307     1546   1118   1226    179   -296   -345       N  
ATOM    588  CA  ALA A 307      43.446  22.710  13.949  1.00 10.58           C  
ANISOU  588  CA  ALA A 307     1693    952   1375    282   -244   -236       C  
ATOM    589  C   ALA A 307      43.797  21.414  13.220  1.00 10.07           C  
ANISOU  589  C   ALA A 307     1321    877   1627    143    203   -213       C  
ATOM    590  O   ALA A 307      44.876  20.841  13.433  1.00 11.11           O  
ANISOU  590  O   ALA A 307     1276   1231   1715    499   -118   -256       O  
ATOM    591  CB  ALA A 307      43.399  23.885  12.963  1.00 13.11           C  
ANISOU  591  CB  ALA A 307     1896   1265   1818    339   -274    -28       C  
ATOM    592  N   GLU A 308      42.906  20.945  12.350  1.00 10.46           N  
ANISOU  592  N   GLU A 308     1390    949   1636    171    -68   -333       N  
ATOM    593  CA  GLU A 308      43.280  19.854  11.450  1.00 10.95           C  
ANISOU  593  CA  GLU A 308     1377   1196   1588    295   -212   -375       C  
ATOM    594  C   GLU A 308      44.310  20.363  10.437  1.00 11.07           C  
ANISOU  594  C   GLU A 308     1402   1342   1463    498   -211   -136       C  
ATOM    595  O   GLU A 308      44.418  21.573  10.201  1.00 11.27           O  
ANISOU  595  O   GLU A 308     1359   1271   1650    467     -4   -184       O  
ATOM    596  CB  GLU A 308      42.054  19.291  10.740  1.00 10.63           C  
ANISOU  596  CB  GLU A 308     1183   1188   1667     12   -215   -356       C  
ATOM    597  CG  GLU A 308      40.973  18.781  11.685  1.00 11.30           C  
ANISOU  597  CG  GLU A 308     1389   1137   1765    302     12    -86       C  
ATOM    598  CD  GLU A 308      41.347  17.481  12.403  1.00 13.22           C  
ANISOU  598  CD  GLU A 308     1680   1547   1796    348    -99   -664       C  
ATOM    599  OE1 GLU A 308      42.266  16.766  11.945  1.00 14.33           O  
ANISOU  599  OE1 GLU A 308     1736   1400   2307    423     33     75       O  
ATOM    600  OE2 GLU A 308      40.717  17.173  13.439  1.00 15.47           O  
ANISOU  600  OE2 GLU A 308     2148   1843   1886    473    101   -174       O  
ATOM    601  N   LEU A 309      45.054  19.444   9.826  1.00 11.13           N  
ANISOU  601  N   LEU A 309     1407   1310   1512    410   -228   -263       N  
ATOM    602  CA  LEU A 309      46.161  19.824   8.949  1.00 11.67           C  
ANISOU  602  CA  LEU A 309     1438   1230   1765    640    -45   -260       C  
ATOM    603  C   LEU A 309      45.732  20.615   7.708  1.00 11.33           C  
ANISOU  603  C   LEU A 309     1338   1432   1535    540    -87   -205       C  
ATOM    604  O   LEU A 309      46.534  21.338   7.124  1.00 12.55           O  
ANISOU  604  O   LEU A 309     1547   1571   1649    468    -70    -65       O  
ATOM    605  CB  LEU A 309      46.971  18.593   8.550  1.00 12.74           C  
ANISOU  605  CB  LEU A 309     1473   1260   2106    662   -391   -376       C  
ATOM    606  CG  LEU A 309      47.720  17.935   9.712  1.00 13.38           C  
ANISOU  606  CG  LEU A 309     1530   1240   2314    532   -825   -497       C  
ATOM    607  CD1 LEU A 309      48.386  16.630   9.247  1.00 16.47           C  
ANISOU  607  CD1 LEU A 309     1797   1461   2998    626   -637   -722       C  
ATOM    608  CD2 LEU A 309      48.747  18.872  10.298  1.00 13.98           C  
ANISOU  608  CD2 LEU A 309     1536   1417   2358    460   -684   -450       C  
ATOM    609  N   ASP A 310      44.471  20.487   7.305  1.00 12.64           N  
ANISOU  609  N   ASP A 310     1466   1692   1644    688   -274    155       N  
ATOM    610  CA  ASP A 310      43.972  21.259   6.165  1.00 13.56           C  
ANISOU  610  CA  ASP A 310     1553   1705   1894    453    -63     37       C  
ATOM    611  C   ASP A 310      43.497  22.658   6.567  1.00 14.50           C  
ANISOU  611  C   ASP A 310     1728   1914   1867    452    -27    -56       C  
ATOM    612  O   ASP A 310      43.061  23.448   5.722  1.00 16.83           O  
ANISOU  612  O   ASP A 310     1849   2299   2247    590   -197    464       O  
ATOM    613  CB  ASP A 310      42.874  20.497   5.411  1.00 14.26           C  
ANISOU  613  CB  ASP A 310     1383   2016   2017    146    -66    -52       C  
ATOM    614  CG  ASP A 310      41.600  20.310   6.227  1.00 15.76           C  
ANISOU  614  CG  ASP A 310     1519   2230   2239    262   -423   -275       C  
ATOM    615  OD1 ASP A 310      41.572  20.676   7.423  1.00 15.22           O  
ANISOU  615  OD1 ASP A 310     1614   1972   2195    541   -107   -228       O  
ATOM    616  OD2 ASP A 310      40.618  19.776   5.650  1.00 16.19           O  
ANISOU  616  OD2 ASP A 310     1575   2568   2008     49   -378    -37       O  
ATOM    617  N   GLY A 311      43.593  22.966   7.857  1.00 13.36           N  
ANISOU  617  N   GLY A 311     1429   1607   2040    549    -15      2       N  
ATOM    618  CA  GLY A 311      43.205  24.278   8.350  1.00 14.70           C  
ANISOU  618  CA  GLY A 311     1465   1646   2473    783    -45     43       C  
ATOM    619  C   GLY A 311      41.769  24.363   8.847  1.00 14.36           C  
ANISOU  619  C   GLY A 311     1488   1568   2401    476   -123    -78       C  
ATOM    620  O   GLY A 311      41.380  25.351   9.460  1.00 16.43           O  
ANISOU  620  O   GLY A 311     1619   1611   3013    529    278   -244       O  
ATOM    621  N   ASN A 312      40.980  23.333   8.576  1.00 14.01           N  
ANISOU  621  N   ASN A 312     1340   1884   2099    634     50     87       N  
ATOM    622  CA  ASN A 312      39.650  23.234   9.150  1.00 14.49           C  
ANISOU  622  CA  ASN A 312     1669   1912   1924    570    -51   -254       C  
ATOM    623  C   ASN A 312      39.735  22.937  10.645  1.00 14.05           C  
ANISOU  623  C   ASN A 312     1607   1700   2031    619     69   -308       C  
ATOM    624  O   ASN A 312      40.752  22.447  11.130  1.00 14.44           O  
ANISOU  624  O   ASN A 312     1705   1665   2115    765   -360   -332       O  
ATOM    625  CB  ASN A 312      38.824  22.189   8.407  1.00 17.30           C  
ANISOU  625  CB  ASN A 312     1749   2578   2247    596   -509   -611       C  
ATOM    626  CG  ASN A 312      38.365  22.686   7.051  1.00 21.75           C  
ANISOU  626  CG  ASN A 312     2292   3462   2510   1321   -701   -764       C  
ATOM    627  OD1 ASN A 312      37.759  23.755   6.947  1.00 27.36           O  
ANISOU  627  OD1 ASN A 312     3185   3875   3336   1823  -1045   -534       O  
ATOM    628  ND2 ASN A 312      38.666  21.927   6.004  1.00 22.92           N  
ANISOU  628  ND2 ASN A 312     2390   3771   2548   1352   -469   -597       N  
ATOM    629  N   PRO A 313      38.677  23.262  11.387  1.00 13.83           N  
ANISOU  629  N   PRO A 313     1341   1741   2172    666   -139   -152       N  
ATOM    630  CA  PRO A 313      38.773  23.201  12.846  1.00 14.85           C  
ANISOU  630  CA  PRO A 313     1608   1867   2166    985    115   -125       C  
ATOM    631  C   PRO A 313      38.898  21.788  13.380  1.00 15.33           C  
ANISOU  631  C   PRO A 313     1780   1739   2304    512   -195   -260       C  
ATOM    632  O   PRO A 313      38.317  20.845  12.830  1.00 14.31           O  
ANISOU  632  O   PRO A 313     1686   1837   1914    472    -30     14       O  
ATOM    633  CB  PRO A 313      37.455  23.824  13.317  1.00 16.86           C  
ANISOU  633  CB  PRO A 313     1695   2237   2474   1028    217   -115       C  
ATOM    634  CG  PRO A 313      36.548  23.781  12.140  1.00 17.43           C  
ANISOU  634  CG  PRO A 313     1570   2295   2758    663     42   -499       C  
ATOM    635  CD  PRO A 313      37.417  23.876  10.933  1.00 16.04           C  
ANISOU  635  CD  PRO A 313     1341   2021   2733    684    146    258       C  
ATOM    636  N   TYR A 314      39.666  21.654  14.456  1.00 15.35           N  
ANISOU  636  N   TYR A 314     1812   1972   2048    851   -213    -37       N  
ATOM    637  CA  TYR A 314      39.714  20.413  15.198  1.00 16.15           C  
ANISOU  637  CA  TYR A 314     1840   2330   1966    741    178     14       C  
ATOM    638  C   TYR A 314      38.505  20.411  16.109  1.00 18.55           C  
ANISOU  638  C   TYR A 314     1955   2432   2662    714     64   -376       C  
ATOM    639  O   TYR A 314      38.275  21.365  16.861  1.00 19.98           O  
ANISOU  639  O   TYR A 314     2241   2627   2724    693    272   -539       O  
ATOM    640  CB  TYR A 314      40.995  20.316  16.028  1.00 16.10           C  
ANISOU  640  CB  TYR A 314     1867   2448   1802    772   -523    -32       C  
ATOM    641  CG  TYR A 314      40.938  19.229  17.077  1.00 15.79           C  
ANISOU  641  CG  TYR A 314     1816   2439   1745    890     50     84       C  
ATOM    642  CD1 TYR A 314      40.734  17.900  16.719  1.00 16.66           C  
ANISOU  642  CD1 TYR A 314     1889   2461   1980   1186     83     71       C  
ATOM    643  CD2 TYR A 314      41.082  19.531  18.426  1.00 15.39           C  
ANISOU  643  CD2 TYR A 314     1626   2421   1799    439     54    266       C  
ATOM    644  CE1 TYR A 314      40.674  16.900  17.678  1.00 16.59           C  
ANISOU  644  CE1 TYR A 314     2007   2542   1755   1115    157     -7       C  
ATOM    645  CE2 TYR A 314      41.034  18.538  19.391  1.00 16.58           C  
ANISOU  645  CE2 TYR A 314     1851   2417   2031    696   -137   -117       C  
ATOM    646  CZ  TYR A 314      40.825  17.225  19.009  1.00 16.05           C  
ANISOU  646  CZ  TYR A 314     1993   2653   1451    984   -131    -34       C  
ATOM    647  OH  TYR A 314      40.763  16.238  19.961  1.00 17.57           O  
ANISOU  647  OH  TYR A 314     1982   2917   1776    817   -150     68       O  
ATOM    648  N   HIS A 315      37.718  19.349  16.021  1.00 18.04           N  
ANISOU  648  N   HIS A 315     2068   2443   2341    466    370    155       N  
ATOM    649  CA  HIS A 315      36.559  19.210  16.875  1.00 22.15           C  
ANISOU  649  CA  HIS A 315     2625   2781   3010    450     79    324       C  
ATOM    650  C   HIS A 315      37.018  18.664  18.210  1.00 22.25           C  
ANISOU  650  C   HIS A 315     2847   2731   2877    178    253    156       C  
ATOM    651  O   HIS A 315      37.128  17.452  18.398  1.00 24.63           O  
ANISOU  651  O   HIS A 315     2992   2487   3880    218     12   1163       O  
ATOM    652  CB  HIS A 315      35.511  18.313  16.217  1.00 26.64           C  
ANISOU  652  CB  HIS A 315     3050   3312   3761    446   -171    347       C  
ATOM    653  CG  HIS A 315      34.902  18.912  14.988  1.00 35.11           C  
ANISOU  653  CG  HIS A 315     3854   4125   5360    809   -870    102       C  
ATOM    654  ND1 HIS A 315      34.254  18.160  14.033  1.00 39.44           N  
ANISOU  654  ND1 HIS A 315     4307   4564   6112   1117  -1001      1       N  
ATOM    655  CD2 HIS A 315      34.845  20.195  14.559  1.00 39.36           C  
ANISOU  655  CD2 HIS A 315     4227   4575   6154    988  -1280   -106       C  
ATOM    656  CE1 HIS A 315      33.824  18.954  13.068  1.00 40.91           C  
ANISOU  656  CE1 HIS A 315     4451   4747   6346   1233  -1255   -145       C  
ATOM    657  NE2 HIS A 315      34.171  20.194  13.362  1.00 40.53           N  
ANISOU  657  NE2 HIS A 315     4433   4703   6263   1110  -1344   -168       N  
ATOM    658  N   ALA A 316      37.300  19.585  19.131  1.00 24.73           N  
ANISOU  658  N   ALA A 316     2915   3086   3396     18    294   -379       N  
ATOM    659  CA  ALA A 316      37.802  19.227  20.451  1.00 25.92           C  
ANISOU  659  CA  ALA A 316     3042   3240   3564    377    741   -638       C  
ATOM    660  C   ALA A 316      36.872  18.229  21.126  1.00 25.64           C  
ANISOU  660  C   ALA A 316     2678   3452   3613     39    684   -463       C  
ATOM    661  O   ALA A 316      35.653  18.277  20.946  1.00 26.24           O  
ANISOU  661  O   ALA A 316     2517   3908   3543    332    637   -373       O  
ATOM    662  CB  ALA A 316      37.984  20.477  21.324  1.00 28.06           C  
ANISOU  662  CB  ALA A 316     3522   2860   4279    709   1209   -734       C  
ATOM    663  N   PHE A 317      37.468  17.319  21.887  1.00 24.40           N  
ANISOU  663  N   PHE A 317     2714   3321   3234   -266    440   -423       N  
ATOM    664  CA  PHE A 317      36.735  16.288  22.612  1.00 25.83           C  
ANISOU  664  CA  PHE A 317     2951   3564   3297   -417    549   -351       C  
ATOM    665  C   PHE A 317      36.057  15.240  21.715  1.00 25.98           C  
ANISOU  665  C   PHE A 317     3016   3522   3331  -1057   -159   -698       C  
ATOM    666  O   PHE A 317      35.169  14.532  22.182  1.00 29.43           O  
ANISOU  666  O   PHE A 317     3553   3703   3925   -664    147     26       O  
ATOM    667  CB  PHE A 317      35.710  16.922  23.570  1.00 27.75           C  
ANISOU  667  CB  PHE A 317     3309   3862   3372   -258    692   -525       C  
ATOM    668  CG  PHE A 317      36.308  17.926  24.522  1.00 30.61           C  
ANISOU  668  CG  PHE A 317     3699   4242   3687      0    690   -521       C  
ATOM    669  CD1 PHE A 317      36.198  19.286  24.277  1.00 31.04           C  
ANISOU  669  CD1 PHE A 317     3918   4152   3722    -42    764   -899       C  
ATOM    670  CD2 PHE A 317      36.984  17.507  25.657  1.00 32.89           C  
ANISOU  670  CD2 PHE A 317     3911   4431   4155    197    422   -632       C  
ATOM    671  CE1 PHE A 317      36.755  20.215  25.150  1.00 33.23           C  
ANISOU  671  CE1 PHE A 317     4063   4469   4094    289    626   -765       C  
ATOM    672  CE2 PHE A 317      37.540  18.423  26.531  1.00 34.15           C  
ANISOU  672  CE2 PHE A 317     4016   4479   4481    251    386   -691       C  
ATOM    673  CZ  PHE A 317      37.423  19.782  26.276  1.00 33.76           C  
ANISOU  673  CZ  PHE A 317     4022   4418   4385    186    452   -825       C  
ATOM    674  N   ASP A 318      36.489  15.119  20.456  1.00 24.12           N  
ANISOU  674  N   ASP A 318     3046   3656   2460  -1446    489   -556       N  
ATOM    675  CA  ASP A 318      35.805  14.249  19.480  1.00 33.05           C  
ANISOU  675  CA  ASP A 318     3852   4075   4630   -700    471     70       C  
ATOM    676  C   ASP A 318      36.655  13.178  18.774  1.00 36.01           C  
ANISOU  676  C   ASP A 318     4063   3786   5834   -592      7    -80       C  
ATOM    677  O   ASP A 318      36.111  12.221  18.213  1.00 42.11           O  
ANISOU  677  O   ASP A 318     4603   4289   7106   -513   -436   -617       O  
ATOM    678  CB  ASP A 318      35.073  15.090  18.436  1.00 37.80           C  
ANISOU  678  CB  ASP A 318     4412   4880   5071   -361    182    504       C  
ATOM    679  CG  ASP A 318      33.605  15.265  18.762  1.00 42.15           C  
ANISOU  679  CG  ASP A 318     5005   5649   5361    103     73    577       C  
ATOM    680  OD1 ASP A 318      32.885  15.898  17.958  1.00 44.44           O  
ANISOU  680  OD1 ASP A 318     5168   5931   5785    246   -176    479       O  
ATOM    681  OD2 ASP A 318      33.167  14.755  19.818  1.00 41.27           O  
ANISOU  681  OD2 ASP A 318     5243   5858   4580    300    204    772       O  
ATOM    682  N   SER A 319      37.967  13.380  18.740  1.00 30.19           N  
ANISOU  682  N   SER A 319     3389   3192   4889   -807   -273    578       N  
ATOM    683  CA  SER A 319      38.941  12.314  18.486  1.00 26.84           C  
ANISOU  683  CA  SER A 319     3285   2745   4166   -650    126    612       C  
ATOM    684  C   SER A 319      40.104  12.694  19.392  1.00 19.02           C  
ANISOU  684  C   SER A 319     2450   1976   2801   -556    -54    382       C  
ATOM    685  O   SER A 319      40.097  13.793  19.936  1.00 21.15           O  
ANISOU  685  O   SER A 319     2352   2649   3033    202    595    526       O  
ATOM    686  CB  SER A 319      39.342  12.220  17.009  1.00 29.54           C  
ANISOU  686  CB  SER A 319     3524   2883   4815   -583   -422   -121       C  
ATOM    687  OG  SER A 319      40.168  13.296  16.605  1.00 28.47           O  
ANISOU  687  OG  SER A 319     3364   3547   3904   -585  -1324   -646       O  
ATOM    688  N   PRO A 320      41.088  11.798  19.605  1.00 14.37           N  
ANISOU  688  N   PRO A 320     2147   1199   2115    -26    217     16       N  
ATOM    689  CA  PRO A 320      42.005  12.133  20.705  1.00 13.98           C  
ANISOU  689  CA  PRO A 320     2082   1245   1984    185    137   -106       C  
ATOM    690  C   PRO A 320      42.782  13.425  20.468  1.00 13.47           C  
ANISOU  690  C   PRO A 320     2103   1291   1723    340    144   -458       C  
ATOM    691  O   PRO A 320      43.125  14.111  21.428  1.00 13.27           O  
ANISOU  691  O   PRO A 320     2087   1294   1659    345    238   -143       O  
ATOM    692  CB  PRO A 320      42.957  10.935  20.746  1.00 16.50           C  
ANISOU  692  CB  PRO A 320     2141   1433   2693    391     47      0       C  
ATOM    693  CG  PRO A 320      42.184   9.819  20.123  1.00 16.80           C  
ANISOU  693  CG  PRO A 320     2263   1305   2814    148     85   -402       C  
ATOM    694  CD  PRO A 320      41.349  10.457  19.057  1.00 15.66           C  
ANISOU  694  CD  PRO A 320     2206   1416   2328    201   -153     61       C  
ATOM    695  N   ALA A 321      43.052  13.740  19.205  1.00 12.36           N  
ANISOU  695  N   ALA A 321     1753   1321   1621    189    444     59       N  
ATOM    696  CA  ALA A 321      43.778  14.940  18.831  1.00 11.39           C  
ANISOU  696  CA  ALA A 321     1352   1387   1587    141    183    212       C  
ATOM    697  C   ALA A 321      43.541  15.101  17.343  1.00 11.05           C  
ANISOU  697  C   ALA A 321     1278   1326   1592    298    266     18       C  
ATOM    698  O   ALA A 321      42.928  14.229  16.722  1.00 12.02           O  
ANISOU  698  O   ALA A 321     1218   1435   1912    -79    220   -277       O  
ATOM    699  CB  ALA A 321      45.281  14.768  19.126  1.00 12.65           C  
ANISOU  699  CB  ALA A 321     1464   1370   1971    424   -347   -258       C  
ATOM    700  N   PRO A 322      43.998  16.216  16.754  1.00 11.02           N  
ANISOU  700  N   PRO A 322     1472   1189   1527    216    -70   -277       N  
ATOM    701  CA  PRO A 322      43.841  16.331  15.300  1.00 11.27           C  
ANISOU  701  CA  PRO A 322     1557   1040   1684     83    -35   -415       C  
ATOM    702  C   PRO A 322      44.460  15.136  14.569  1.00  9.42           C  
ANISOU  702  C   PRO A 322     1162   1088   1330    -96    -99   -128       C  
ATOM    703  O   PRO A 322      45.437  14.541  15.046  1.00 10.19           O  
ANISOU  703  O   PRO A 322     1105   1297   1470    210    -66   -103       O  
ATOM    704  CB  PRO A 322      44.613  17.608  14.975  1.00 11.18           C  
ANISOU  704  CB  PRO A 322     1527   1183   1539    -48    120   -155       C  
ATOM    705  CG  PRO A 322      44.519  18.425  16.236  1.00 12.22           C  
ANISOU  705  CG  PRO A 322     1673   1361   1607    218     97   -160       C  
ATOM    706  CD  PRO A 322      44.611  17.418  17.350  1.00 11.44           C  
ANISOU  706  CD  PRO A 322     1639   1112   1595    -11   -107   -227       C  
ATOM    707  N   LEU A 323      43.909  14.787  13.411  1.00  9.81           N  
ANISOU  707  N   LEU A 323     1221   1027   1480    225      5   -371       N  
ATOM    708  CA  LEU A 323      44.433  13.646  12.670  1.00  9.97           C  
ANISOU  708  CA  LEU A 323     1084   1095   1608    116   -125   -426       C  
ATOM    709  C   LEU A 323      45.906  13.846  12.316  1.00  8.69           C  
ANISOU  709  C   LEU A 323     1057    722   1522   -227     32    -14       C  
ATOM    710  O   LEU A 323      46.326  14.954  11.962  1.00 10.03           O  
ANISOU  710  O   LEU A 323     1056    944   1809     80    -23   -163       O  
ATOM    711  CB  LEU A 323      43.606  13.383  11.412  1.00 11.70           C  
ANISOU  711  CB  LEU A 323      956   1403   2087    -94   -264   -513       C  
ATOM    712  CG  LEU A 323      42.116  13.171  11.679  1.00 12.27           C  
ANISOU  712  CG  LEU A 323      907   1409   2347   -254   -183   -401       C  
ATOM    713  CD1 LEU A 323      41.396  12.793  10.386  1.00 16.31           C  
ANISOU  713  CD1 LEU A 323     1134   2113   2948    -49   -323  -1111       C  
ATOM    714  CD2 LEU A 323      41.913  12.089  12.739  1.00 15.04           C  
ANISOU  714  CD2 LEU A 323     1234   1269   3212    -49    290   -183       C  
ATOM    715  N   GLY A 324      46.693  12.776  12.428  1.00  9.70           N  
ANISOU  715  N   GLY A 324     1048   1035   1602    118     53   -128       N  
ATOM    716  CA  GLY A 324      48.120  12.823  12.128  1.00 10.53           C  
ANISOU  716  CA  GLY A 324     1178   1141   1683    107    113    -70       C  
ATOM    717  C   GLY A 324      49.002  13.253  13.297  1.00  9.38           C  
ANISOU  717  C   GLY A 324     1253    931   1378    216    133    -50       C  
ATOM    718  O   GLY A 324      50.219  13.111  13.244  1.00 10.68           O  
ANISOU  718  O   GLY A 324     1329   1196   1531    300     58   -208       O  
ATOM    719  N   PHE A 325      48.397  13.780  14.357  1.00  9.71           N  
ANISOU  719  N   PHE A 325     1315    931   1444    142   -302   -140       N  
ATOM    720  CA  PHE A 325      49.150  14.293  15.499  1.00 10.04           C  
ANISOU  720  CA  PHE A 325     1239   1078   1496    356    -12   -230       C  
ATOM    721  C   PHE A 325      50.139  13.231  16.009  1.00  8.67           C  
ANISOU  721  C   PHE A 325     1037    898   1359    107   -115    -47       C  
ATOM    722  O   PHE A 325      49.782  12.066  16.124  1.00 10.16           O  
ANISOU  722  O   PHE A 325     1403    898   1560    143     28     15       O  
ATOM    723  CB  PHE A 325      48.173  14.685  16.614  1.00 10.45           C  
ANISOU  723  CB  PHE A 325     1366   1239   1363    197   -150   -463       C  
ATOM    724  CG  PHE A 325      48.774  15.570  17.674  1.00  9.02           C  
ANISOU  724  CG  PHE A 325     1119    964   1344    -46    137    -94       C  
ATOM    725  CD1 PHE A 325      48.705  16.959  17.568  1.00 10.23           C  
ANISOU  725  CD1 PHE A 325     1365    793   1727     36    193   -198       C  
ATOM    726  CD2 PHE A 325      49.390  15.024  18.786  1.00 10.16           C  
ANISOU  726  CD2 PHE A 325     1238   1268   1353    102    -67   -169       C  
ATOM    727  CE1 PHE A 325      49.253  17.778  18.547  1.00 11.13           C  
ANISOU  727  CE1 PHE A 325     1561   1028   1640    228      6   -198       C  
ATOM    728  CE2 PHE A 325      49.937  15.837  19.775  1.00 11.75           C  
ANISOU  728  CE2 PHE A 325     1514   1309   1641    330    -39   -223       C  
ATOM    729  CZ  PHE A 325      49.867  17.215  19.658  1.00 11.31           C  
ANISOU  729  CZ  PHE A 325     1625    957   1715    384    104   -163       C  
ATOM    730  N   PRO A 326      51.386  13.628  16.319  1.00  9.10           N  
ANISOU  730  N   PRO A 326     1355    574   1529    217   -253     20       N  
ATOM    731  CA  PRO A 326      52.362  12.645  16.816  1.00  9.80           C  
ANISOU  731  CA  PRO A 326     1303    725   1696     -3   -302    167       C  
ATOM    732  C   PRO A 326      51.819  11.830  17.992  1.00  9.90           C  
ANISOU  732  C   PRO A 326     1557    701   1502    202   -170    -28       C  
ATOM    733  O   PRO A 326      51.205  12.395  18.910  1.00 11.02           O  
ANISOU  733  O   PRO A 326     1797    913   1475    405     31   -185       O  
ATOM    734  CB  PRO A 326      53.530  13.521  17.286  1.00 11.84           C  
ANISOU  734  CB  PRO A 326     1365   1017   2117    -53   -543     11       C  
ATOM    735  CG  PRO A 326      53.450  14.731  16.430  1.00 12.08           C  
ANISOU  735  CG  PRO A 326     1503    937   2148    389   -295    327       C  
ATOM    736  CD  PRO A 326      51.959  14.987  16.265  1.00  9.87           C  
ANISOU  736  CD  PRO A 326     1133    616   2002    177   -187     -7       C  
ATOM    737  N   ASP A 327      52.050  10.516  17.978  1.00 10.30           N  
ANISOU  737  N   ASP A 327     1663    711   1538     14   -119    249       N  
ATOM    738  CA  ASP A 327      51.600   9.667  19.086  1.00 10.92           C  
ANISOU  738  CA  ASP A 327     1544    843   1763    -85   -245     13       C  
ATOM    739  C   ASP A 327      52.752   9.176  19.966  1.00 10.97           C  
ANISOU  739  C   ASP A 327     1676   1032   1459    281   -394    -77       C  
ATOM    740  O   ASP A 327      52.698   8.093  20.549  1.00 12.27           O  
ANISOU  740  O   ASP A 327     1797   1069   1795     98   -282     42       O  
ATOM    741  CB  ASP A 327      50.686   8.523  18.609  1.00 11.58           C  
ANISOU  741  CB  ASP A 327     1564    905   1929    107     13   -216       C  
ATOM    742  CG  ASP A 327      51.419   7.452  17.816  1.00 10.43           C  
ANISOU  742  CG  ASP A 327     1647    765   1550    -99    -23     54       C  
ATOM    743  OD1 ASP A 327      52.609   7.634  17.491  1.00 11.37           O  
ANISOU  743  OD1 ASP A 327     1495   1067   1759     45    163    -98       O  
ATOM    744  OD2 ASP A 327      50.780   6.415  17.503  1.00 11.68           O  
ANISOU  744  OD2 ASP A 327     1536   1057   1846     92      7   -198       O  
ATOM    745  N   PHE A 328      53.780  10.006  20.081  1.00 10.94           N  
ANISOU  745  N   PHE A 328     1467   1032   1657    170   -402   -175       N  
ATOM    746  CA  PHE A 328      54.884   9.757  20.997  1.00 10.31           C  
ANISOU  746  CA  PHE A 328     1353   1094   1470    117    -76    -41       C  
ATOM    747  C   PHE A 328      54.619  10.485  22.305  1.00 11.04           C  
ANISOU  747  C   PHE A 328     1774   1143   1276    279   -142   -191       C  
ATOM    748  O   PHE A 328      54.493  11.716  22.328  1.00 11.85           O  
ANISOU  748  O   PHE A 328     1667   1069   1764    230   -159   -345       O  
ATOM    749  CB  PHE A 328      56.210  10.190  20.370  1.00 11.10           C  
ANISOU  749  CB  PHE A 328     1407   1149   1661    181   -194   -290       C  
ATOM    750  CG  PHE A 328      56.511   9.469  19.089  1.00 10.95           C  
ANISOU  750  CG  PHE A 328     1711    969   1479    111   -250   -371       C  
ATOM    751  CD1 PHE A 328      56.922   8.148  19.111  1.00 13.04           C  
ANISOU  751  CD1 PHE A 328     1985   1116   1851    437     69   -285       C  
ATOM    752  CD2 PHE A 328      56.323  10.087  17.865  1.00 11.28           C  
ANISOU  752  CD2 PHE A 328     1648   1225   1413    172     77   -164       C  
ATOM    753  CE1 PHE A 328      57.165   7.465  17.927  1.00 12.40           C  
ANISOU  753  CE1 PHE A 328     2064   1125   1523    498    199   -181       C  
ATOM    754  CE2 PHE A 328      56.559   9.408  16.677  1.00 12.44           C  
ANISOU  754  CE2 PHE A 328     1749    922   2055    255    -95   -299       C  
ATOM    755  CZ  PHE A 328      56.979   8.096  16.711  1.00 12.09           C  
ANISOU  755  CZ  PHE A 328     1995   1172   1426    321     67   -247       C  
ATOM    756  N   GLY A 329      54.517   9.715  23.385  1.00 11.82           N  
ANISOU  756  N   GLY A 329     1993   1264   1232    404     -7     37       N  
ATOM    757  CA  GLY A 329      54.132  10.248  24.675  1.00 12.50           C  
ANISOU  757  CA  GLY A 329     2060   1444   1246    521   -152   -110       C  
ATOM    758  C   GLY A 329      55.273  10.379  25.662  1.00 11.52           C  
ANISOU  758  C   GLY A 329     2018    984   1373    215    -46   -305       C  
ATOM    759  O   GLY A 329      56.249   9.627  25.596  1.00 13.73           O  
ANISOU  759  O   GLY A 329     2049   1197   1970    512     67    -37       O  
ATOM    760  N   ASN A 330      55.131  11.337  26.575  1.00 11.43           N  
ANISOU  760  N   ASN A 330     1976   1032   1336    406   -221     57       N  
ATOM    761  CA  ASN A 330      56.082  11.549  27.662  1.00 11.94           C  
ANISOU  761  CA  ASN A 330     2046   1249   1242    340   -377    164       C  
ATOM    762  C   ASN A 330      57.494  11.854  27.195  1.00 12.54           C  
ANISOU  762  C   ASN A 330     2034   1310   1419    445   -227   -322       C  
ATOM    763  O   ASN A 330      58.461  11.414  27.812  1.00 14.10           O  
ANISOU  763  O   ASN A 330     1856   1717   1783    478   -406    -83       O  
ATOM    764  CB  ASN A 330      56.111  10.362  28.635  1.00 13.34           C  
ANISOU  764  CB  ASN A 330     2225   1306   1537    511   -211    148       C  
ATOM    765  CG  ASN A 330      56.578  10.774  30.018  1.00 13.69           C  
ANISOU  765  CG  ASN A 330     2372   1366   1463    611   -126     20       C  
ATOM    766  OD1 ASN A 330      56.148  11.800  30.539  1.00 15.42           O  
ANISOU  766  OD1 ASN A 330     2712   1708   1438    815   -117    -40       O  
ATOM    767  ND2 ASN A 330      57.469   9.989  30.612  1.00 15.16           N  
ANISOU  767  ND2 ASN A 330     2430   1719   1612    600   -255    424       N  
ATOM    768  N   CYS A 331      57.607  12.623  26.115  1.00 11.91           N  
ANISOU  768  N   CYS A 331     1790   1320   1413    258   -383   -318       N  
ATOM    769  CA  CYS A 331      58.909  12.932  25.549  1.00 10.96           C  
ANISOU  769  CA  CYS A 331     1662    996   1504    267     31     -1       C  
ATOM    770  C   CYS A 331      58.939  14.322  24.929  1.00 10.54           C  
ANISOU  770  C   CYS A 331     1510   1009   1485     55   -355     73       C  
ATOM    771  O   CYS A 331      57.930  15.034  24.924  1.00 11.80           O  
ANISOU  771  O   CYS A 331     1407   1358   1717    390   -293   -184       O  
ATOM    772  CB  CYS A 331      59.313  11.864  24.528  1.00 13.16           C  
ANISOU  772  CB  CYS A 331     1920   1350   1728    422   -252   -234       C  
ATOM    773  SG  CYS A 331      58.108  11.655  23.183  1.00 13.44           S  
ANISOU  773  SG  CYS A 331     1877   1462   1765    211   -350   -232       S  
ATOM    774  N   ASP A 332      60.109  14.708  24.435  1.00 11.37           N  
ANISOU  774  N   ASP A 332     1745    973   1603   -114   -170    -60       N  
ATOM    775  CA  ASP A 332      60.292  16.024  23.843  1.00 10.51           C  
ANISOU  775  CA  ASP A 332     1577   1006   1409     35   -304   -210       C  
ATOM    776  C   ASP A 332      60.210  15.921  22.327  1.00 10.06           C  
ANISOU  776  C   ASP A 332     1533   1143   1145    508   -213   -259       C  
ATOM    777  O   ASP A 332      61.026  15.241  21.693  1.00 13.09           O  
ANISOU  777  O   ASP A 332     1655   1493   1826    697   -148   -271       O  
ATOM    778  CB  ASP A 332      61.641  16.619  24.245  1.00 12.47           C  
ANISOU  778  CB  ASP A 332     1695   1169   1874     76   -371   -513       C  
ATOM    779  CG  ASP A 332      61.696  17.038  25.709  1.00 13.88           C  
ANISOU  779  CG  ASP A 332     1789   1267   2216   -104   -505   -342       C  
ATOM    780  OD1 ASP A 332      60.736  16.775  26.472  1.00 14.12           O  
ANISOU  780  OD1 ASP A 332     2158   1545   1660    251   -427   -227       O  
ATOM    781  OD2 ASP A 332      62.721  17.639  26.092  1.00 15.56           O  
ANISOU  781  OD2 ASP A 332     1893   1627   2391    229   -503   -717       O  
ATOM    782  N   LEU A 333      59.201  16.573  21.763  1.00 10.50           N  
ANISOU  782  N   LEU A 333     1462   1021   1504    335   -457     -8       N  
ATOM    783  CA  LEU A 333      59.003  16.617  20.322  1.00 10.32           C  
ANISOU  783  CA  LEU A 333     1231   1059   1629    263   -205    -59       C  
ATOM    784  C   LEU A 333      59.685  17.852  19.759  1.00  9.52           C  
ANISOU  784  C   LEU A 333     1269   1030   1319    226   -107     11       C  
ATOM    785  O   LEU A 333      59.288  18.984  20.057  1.00 12.18           O  
ANISOU  785  O   LEU A 333     1607    922   2100    344     87   -238       O  
ATOM    786  CB  LEU A 333      57.512  16.665  19.984  1.00 10.57           C  
ANISOU  786  CB  LEU A 333     1246   1024   1746     92   -109     77       C  
ATOM    787  CG  LEU A 333      56.626  15.634  20.690  1.00 10.54           C  
ANISOU  787  CG  LEU A 333     1260    879   1865    344    -78     -9       C  
ATOM    788  CD1 LEU A 333      55.159  15.918  20.385  1.00 12.13           C  
ANISOU  788  CD1 LEU A 333     1161   1259   2190    281   -460     63       C  
ATOM    789  CD2 LEU A 333      57.011  14.210  20.271  1.00 12.66           C  
ANISOU  789  CD2 LEU A 333     1647    913   2250    471    175   -225       C  
ATOM    790  N   HIS A 334      60.714  17.634  18.953  1.00  9.69           N  
ANISOU  790  N   HIS A 334     1267    943   1472    301   -203   -215       N  
ATOM    791  CA  HIS A 334      61.443  18.738  18.341  1.00  9.89           C  
ANISOU  791  CA  HIS A 334      977   1099   1680    125   -199    136       C  
ATOM    792  C   HIS A 334      60.855  18.983  16.969  1.00  9.84           C  
ANISOU  792  C   HIS A 334     1257    975   1506    274     62   -142       C  
ATOM    793  O   HIS A 334      61.055  18.186  16.045  1.00 10.11           O  
ANISOU  793  O   HIS A 334     1329    943   1567    353   -199   -257       O  
ATOM    794  CB  HIS A 334      62.936  18.411  18.255  1.00 10.83           C  
ANISOU  794  CB  HIS A 334     1154   1295   1666    221   -362    -22       C  
ATOM    795  CG  HIS A 334      63.559  18.160  19.591  1.00 11.49           C  
ANISOU  795  CG  HIS A 334     1286   1312   1768    266   -471   -232       C  
ATOM    796  ND1 HIS A 334      64.196  19.151  20.310  1.00 12.56           N  
ANISOU  796  ND1 HIS A 334     1452   1310   2009    308   -480   -154       N  
ATOM    797  CD2 HIS A 334      63.597  17.048  20.362  1.00 12.01           C  
ANISOU  797  CD2 HIS A 334     1479   1320   1764    318   -556   -171       C  
ATOM    798  CE1 HIS A 334      64.623  18.650  21.456  1.00 13.73           C  
ANISOU  798  CE1 HIS A 334     1520   1366   2329    277   -481    -99       C  
ATOM    799  NE2 HIS A 334      64.263  17.379  21.517  1.00 13.34           N  
ANISOU  799  NE2 HIS A 334     1488   1498   2082    397   -439    -81       N  
ATOM    800  N   MET A 335      60.113  20.081  16.855  1.00 10.71           N  
ANISOU  800  N   MET A 335     1268   1146   1653    276   -331    -71       N  
ATOM    801  CA  MET A 335      59.333  20.370  15.659  1.00 10.10           C  
ANISOU  801  CA  MET A 335     1338    977   1520    159   -183   -199       C  
ATOM    802  C   MET A 335      60.010  21.419  14.803  1.00 10.74           C  
ANISOU  802  C   MET A 335     1453    964   1662     56   -441   -277       C  
ATOM    803  O   MET A 335      60.631  22.361  15.309  1.00 12.91           O  
ANISOU  803  O   MET A 335     2016   1209   1679     84   -400   -326       O  
ATOM    804  CB  MET A 335      57.936  20.883  16.032  1.00 12.09           C  
ANISOU  804  CB  MET A 335     1377   1165   2050    239    -28    110       C  
ATOM    805  CG  MET A 335      57.189  20.050  17.066  1.00 12.33           C  
ANISOU  805  CG  MET A 335     1592   1068   2024    151   -171     65       C  
ATOM    806  SD  MET A 335      56.793  18.377  16.535  1.00 11.92           S  
ANISOU  806  SD  MET A 335     1427   1127   1974    439   -113    164       S  
ATOM    807  CE  MET A 335      55.555  18.664  15.282  1.00 11.88           C  
ANISOU  807  CE  MET A 335     1247   1282   1983    563   -204    -95       C  
ATOM    808  N   THR A 336      59.861  21.269  13.497  1.00 10.06           N  
ANISOU  808  N   THR A 336     1276    858   1688    277   -216    -62       N  
ATOM    809  CA  THR A 336      60.191  22.333  12.570  1.00 10.12           C  
ANISOU  809  CA  THR A 336     1118   1025   1702    287    -27    -62       C  
ATOM    810  C   THR A 336      58.864  22.879  12.064  1.00  9.85           C  
ANISOU  810  C   THR A 336     1264    805   1674     54   -238      7       C  
ATOM    811  O   THR A 336      57.924  22.117  11.859  1.00 12.70           O  
ANISOU  811  O   THR A 336     1475    795   2554     42   -482   -196       O  
ATOM    812  CB  THR A 336      61.045  21.802  11.417  1.00 11.98           C  
ANISOU  812  CB  THR A 336     1440   1476   1636    546    300    371       C  
ATOM    813  OG1 THR A 336      62.346  21.469  11.917  1.00 12.82           O  
ANISOU  813  OG1 THR A 336     1186   1517   2167    401      4     37       O  
ATOM    814  CG2 THR A 336      61.188  22.844  10.317  1.00 13.95           C  
ANISOU  814  CG2 THR A 336     1604   1716   1980    512     47    135       C  
ATOM    815  N   PHE A 337      58.758  24.190  11.875  1.00  9.72           N  
ANISOU  815  N   PHE A 337     1207    791   1695    111    -73    248       N  
ATOM    816  CA  PHE A 337      57.490  24.735  11.412  1.00  9.86           C  
ANISOU  816  CA  PHE A 337     1179    986   1581    308    -56     93       C  
ATOM    817  C   PHE A 337      57.645  25.845  10.388  1.00  9.33           C  
ANISOU  817  C   PHE A 337     1397    614   1535    372    -62    128       C  
ATOM    818  O   PHE A 337      58.706  26.468  10.271  1.00 10.31           O  
ANISOU  818  O   PHE A 337     1275    833   1807      8     17     53       O  
ATOM    819  CB  PHE A 337      56.605  25.199  12.580  1.00 10.27           C  
ANISOU  819  CB  PHE A 337     1194   1174   1533    290   -119   -155       C  
ATOM    820  CG  PHE A 337      57.147  26.385  13.340  1.00 11.57           C  
ANISOU  820  CG  PHE A 337     1353   1377   1665    334   -212     34       C  
ATOM    821  CD1 PHE A 337      56.931  27.684  12.887  1.00 11.47           C  
ANISOU  821  CD1 PHE A 337     1396   1066   1896    351      8   -159       C  
ATOM    822  CD2 PHE A 337      57.854  26.203  14.519  1.00 12.77           C  
ANISOU  822  CD2 PHE A 337     1555   1433   1864    148   -377   -150       C  
ATOM    823  CE1 PHE A 337      57.419  28.768  13.595  1.00 13.11           C  
ANISOU  823  CE1 PHE A 337     1579   1395   2008    385   -297   -576       C  
ATOM    824  CE2 PHE A 337      58.334  27.284  15.235  1.00 13.92           C  
ANISOU  824  CE2 PHE A 337     1561   1555   2173    384   -236   -387       C  
ATOM    825  CZ  PHE A 337      58.120  28.564  14.770  1.00 14.04           C  
ANISOU  825  CZ  PHE A 337     1677   1404   2252    568    -68   -478       C  
ATOM    826  N   VAL A 338      56.565  26.082   9.649  1.00  9.41           N  
ANISOU  826  N   VAL A 338     1306    760   1508    431   -270    102       N  
ATOM    827  CA  VAL A 338      56.501  27.181   8.699  1.00 10.03           C  
ANISOU  827  CA  VAL A 338     1401    812   1596    456    -78    -20       C  
ATOM    828  C   VAL A 338      55.148  27.873   8.797  1.00  9.99           C  
ANISOU  828  C   VAL A 338     1380    687   1727    321    -17    -76       C  
ATOM    829  O   VAL A 338      54.122  27.226   9.039  1.00 10.48           O  
ANISOU  829  O   VAL A 338     1329    765   1887    213    -52    175       O  
ATOM    830  CB  VAL A 338      56.709  26.690   7.244  1.00 10.57           C  
ANISOU  830  CB  VAL A 338     1420   1068   1528    181     28   -326       C  
ATOM    831  CG1 VAL A 338      58.140  26.162   7.049  1.00 11.70           C  
ANISOU  831  CG1 VAL A 338     1041   1299   2104    299    319   -279       C  
ATOM    832  CG2 VAL A 338      55.676  25.634   6.849  1.00 12.58           C  
ANISOU  832  CG2 VAL A 338     1552   1422   1805    123    -88   -416       C  
ATOM    833  N   LYS A 339      55.145  29.189   8.607  1.00 10.02           N  
ANISOU  833  N   LYS A 339     1253    756   1797    345   -115   -107       N  
ATOM    834  CA  LYS A 339      53.886  29.899   8.419  1.00 10.68           C  
ANISOU  834  CA  LYS A 339     1255    755   2046    292   -439   -228       C  
ATOM    835  C   LYS A 339      53.173  29.333   7.194  1.00 10.86           C  
ANISOU  835  C   LYS A 339     1256    921   1949    372     91    -58       C  
ATOM    836  O   LYS A 339      53.824  28.949   6.214  1.00 10.93           O  
ANISOU  836  O   LYS A 339     1436   1068   1650    459    188     95       O  
ATOM    837  CB  LYS A 339      54.146  31.400   8.248  1.00 12.51           C  
ANISOU  837  CB  LYS A 339     1780    698   2273    287    -88     36       C  
ATOM    838  CG  LYS A 339      54.704  32.054   9.501  1.00 13.09           C  
ANISOU  838  CG  LYS A 339     2034    728   2211    111   -203   -351       C  
ATOM    839  CD  LYS A 339      54.692  33.583   9.403  1.00 14.85           C  
ANISOU  839  CD  LYS A 339     2327    721   2595    124    131     10       C  
ATOM    840  CE  LYS A 339      55.617  34.075   8.305  1.00 17.32           C  
ANISOU  840  CE  LYS A 339     2576    838   3166     98     -3     11       C  
ATOM    841  NZ  LYS A 339      55.712  35.581   8.315  1.00 18.41           N  
ANISOU  841  NZ  LYS A 339     2798    889   3306    142    115     92       N  
ATOM    842  N   ILE A 340      51.846  29.253   7.252  1.00  9.72           N  
ANISOU  842  N   ILE A 340     1105    814   1773    238   -123   -158       N  
ATOM    843  CA  ILE A 340      51.089  28.587   6.189  1.00 10.83           C  
ANISOU  843  CA  ILE A 340     1335    696   2084    218   -360     68       C  
ATOM    844  C   ILE A 340      50.011  29.469   5.532  1.00 10.66           C  
ANISOU  844  C   ILE A 340     1611    665   1775    346     23    -54       C  
ATOM    845  O   ILE A 340      49.412  29.076   4.544  1.00 12.71           O  
ANISOU  845  O   ILE A 340     1838   1241   1751    423   -217    -39       O  
ATOM    846  CB  ILE A 340      50.507  27.229   6.693  1.00 11.16           C  
ANISOU  846  CB  ILE A 340     1381   1007   1851    184    -18    140       C  
ATOM    847  CG1 ILE A 340      50.137  26.299   5.527  1.00 11.79           C  
ANISOU  847  CG1 ILE A 340     1415   1141   1923    279     24   -359       C  
ATOM    848  CG2 ILE A 340      49.351  27.447   7.663  1.00 11.64           C  
ANISOU  848  CG2 ILE A 340      947   1562   1912    276    259     59       C  
ATOM    849  CD1 ILE A 340      51.310  25.955   4.627  1.00 12.73           C  
ANISOU  849  CD1 ILE A 340     1663   1126   2048    306     40   -305       C  
ATOM    850  N   ASN A 341      49.771  30.656   6.080  1.00 11.26           N  
ANISOU  850  N   ASN A 341     1669    783   1825    500    -14    209       N  
ATOM    851  CA  ASN A 341      48.881  31.615   5.430  1.00 12.66           C  
ANISOU  851  CA  ASN A 341     1869   1204   1737    799    128    218       C  
ATOM    852  C   ASN A 341      49.579  32.201   4.202  1.00 11.88           C  
ANISOU  852  C   ASN A 341     1841   1140   1534    719    -39     95       C  
ATOM    853  O   ASN A 341      50.674  32.749   4.314  1.00 12.67           O  
ANISOU  853  O   ASN A 341     1765   1011   2037    487     22    178       O  
ATOM    854  CB  ASN A 341      48.509  32.725   6.420  1.00 13.83           C  
ANISOU  854  CB  ASN A 341     1907   1305   2041    875    111      6       C  
ATOM    855  CG  ASN A 341      47.421  33.654   5.900  1.00 17.67           C  
ANISOU  855  CG  ASN A 341     2523   1879   2312   1224    315    181       C  
ATOM    856  OD1 ASN A 341      47.239  33.821   4.701  1.00 15.95           O  
ANISOU  856  OD1 ASN A 341     2328   1588   2142   1012     88     37       O  
ATOM    857  ND2 ASN A 341      46.710  34.286   6.823  1.00 22.67           N  
ANISOU  857  ND2 ASN A 341     3184   2625   2803   1674    278    156       N  
ATOM    858  N   PRO A 342      48.949  32.097   3.022  1.00 12.30           N  
ANISOU  858  N   PRO A 342     1733   1134   1804    386   -135   -114       N  
ATOM    859  CA  PRO A 342      49.606  32.621   1.817  1.00 13.05           C  
ANISOU  859  CA  PRO A 342     1973   1332   1652    477    -35   -128       C  
ATOM    860  C   PRO A 342      50.024  34.091   1.939  1.00 13.56           C  
ANISOU  860  C   PRO A 342     2205   1302   1643    769    -45   -101       C  
ATOM    861  O   PRO A 342      51.027  34.480   1.338  1.00 15.43           O  
ANISOU  861  O   PRO A 342     2380   1541   1940    671   -148     51       O  
ATOM    862  CB  PRO A 342      48.543  32.454   0.725  1.00 15.73           C  
ANISOU  862  CB  PRO A 342     2322   1692   1963    398   -120    123       C  
ATOM    863  CG  PRO A 342      47.657  31.388   1.213  1.00 17.84           C  
ANISOU  863  CG  PRO A 342     2364   1789   2624    101   -419    143       C  
ATOM    864  CD  PRO A 342      47.685  31.404   2.716  1.00 13.81           C  
ANISOU  864  CD  PRO A 342     2188   1584   1473    424   -390     21       C  
ATOM    865  N   THR A 343      49.288  34.898   2.700  1.00 13.22           N  
ANISOU  865  N   THR A 343     2124   1007   1893    664    159    254       N  
ATOM    866  CA  THR A 343      49.653  36.307   2.832  1.00 15.00           C  
ANISOU  866  CA  THR A 343     2407   1070   2222    689    167    136       C  
ATOM    867  C   THR A 343      50.935  36.496   3.640  1.00 15.67           C  
ANISOU  867  C   THR A 343     2522   1208   2224    515    112    424       C  
ATOM    868  O   THR A 343      51.534  37.577   3.627  1.00 18.28           O  
ANISOU  868  O   THR A 343     2776   1257   2912    345   -148    256       O  
ATOM    869  CB  THR A 343      48.520  37.140   3.463  1.00 17.23           C  
ANISOU  869  CB  THR A 343     2525   1449   2573    883    282    -34       C  
ATOM    870  OG1 THR A 343      48.302  36.717   4.817  1.00 20.11           O  
ANISOU  870  OG1 THR A 343     2911   1661   3067    828    599    -57       O  
ATOM    871  CG2 THR A 343      47.241  36.972   2.671  1.00 19.27           C  
ANISOU  871  CG2 THR A 343     2353   1711   3256    921     12   -179       C  
ATOM    872  N   GLU A 344      51.348  35.442   4.341  1.00 14.25           N  
ANISOU  872  N   GLU A 344     2389   1262   1763    573    -60    117       N  
ATOM    873  CA  GLU A 344      52.576  35.457   5.132  1.00 13.21           C  
ANISOU  873  CA  GLU A 344     2252   1138   1630    353     -9     42       C  
ATOM    874  C   GLU A 344      53.724  34.811   4.365  1.00 14.50           C  
ANISOU  874  C   GLU A 344     2236   1151   2120    216     55    -71       C  
ATOM    875  O   GLU A 344      54.819  34.629   4.902  1.00 15.35           O  
ANISOU  875  O   GLU A 344     2332   1443   2058     83    -44   -231       O  
ATOM    876  CB  GLU A 344      52.369  34.720   6.459  1.00 14.54           C  
ANISOU  876  CB  GLU A 344     2386   1207   1929    518    -45     27       C  
ATOM    877  CG  GLU A 344      51.369  35.389   7.384  1.00 16.17           C  
ANISOU  877  CG  GLU A 344     2559   1384   2201    570    139   -541       C  
ATOM    878  CD  GLU A 344      51.919  36.633   8.044  1.00 17.98           C  
ANISOU  878  CD  GLU A 344     2813   1545   2473    811   -284   -107       C  
ATOM    879  OE1 GLU A 344      53.161  36.771   8.124  1.00 18.02           O  
ANISOU  879  OE1 GLU A 344     3256   1350   2239    807   -486   -309       O  
ATOM    880  OE2 GLU A 344      51.105  37.471   8.488  1.00 20.68           O  
ANISOU  880  OE2 GLU A 344     2847   1997   3011    844   -174   -469       O  
ATOM    881  N   LEU A 345      53.466  34.470   3.108  1.00 12.29           N  
ANISOU  881  N   LEU A 345     2023    767   1878    210     64   -115       N  
ATOM    882  CA  LEU A 345      54.427  33.724   2.298  1.00 12.42           C  
ANISOU  882  CA  LEU A 345     2070    652   1998    131     92    -84       C  
ATOM    883  C   LEU A 345      54.803  34.447   0.997  1.00 13.49           C  
ANISOU  883  C   LEU A 345     2253    745   2126    193   -166     18       C  
ATOM    884  O   LEU A 345      55.109  33.805  -0.014  1.00 13.64           O  
ANISOU  884  O   LEU A 345     2159    991   2031    299     25     83       O  
ATOM    885  CB  LEU A 345      53.887  32.316   1.993  1.00 12.34           C  
ANISOU  885  CB  LEU A 345     1860    959   1870    238    343    246       C  
ATOM    886  CG  LEU A 345      53.691  31.397   3.203  1.00 11.66           C  
ANISOU  886  CG  LEU A 345     1680   1007   1744    107   -173      0       C  
ATOM    887  CD1 LEU A 345      52.948  30.110   2.831  1.00 12.65           C  
ANISOU  887  CD1 LEU A 345     1539   1062   2206     -9     87   -104       C  
ATOM    888  CD2 LEU A 345      55.027  31.084   3.881  1.00 12.99           C  
ANISOU  888  CD2 LEU A 345     1676   1354   1903     47   -480     18       C  
ATOM    889  N   SER A 346      54.794  35.780   1.019  1.00 15.09           N  
ANISOU  889  N   SER A 346     2468   1012   2251    332     12    239       N  
ATOM    890  CA  SER A 346      55.197  36.540  -0.160  1.00 15.90           C  
ANISOU  890  CA  SER A 346     2591   1192   2257    437    138    464       C  
ATOM    891  C   SER A 346      56.684  36.886  -0.136  1.00 16.39           C  
ANISOU  891  C   SER A 346     2653   1211   2362    431      7    298       C  
ATOM    892  O   SER A 346      57.307  37.062  -1.183  1.00 17.34           O  
ANISOU  892  O   SER A 346     2789   1343   2456    193     54    134       O  
ATOM    893  CB  SER A 346      54.373  37.820  -0.292  1.00 19.36           C  
ANISOU  893  CB  SER A 346     2925   1705   2725    884   -125   -243       C  
ATOM    894  OG  SER A 346      54.691  38.729   0.740  1.00 23.20           O  
ANISOU  894  OG  SER A 346     3317   2241   3257    970    261    401       O  
ATOM    895  N   THR A 347      57.242  36.976   1.066  1.00 15.58           N  
ANISOU  895  N   THR A 347     2453    941   2526    296     84    356       N  
ATOM    896  CA  THR A 347      58.623  37.399   1.249  1.00 15.97           C  
ANISOU  896  CA  THR A 347     2722    906   2441    197   -231    273       C  
ATOM    897  C   THR A 347      59.139  36.919   2.598  1.00 16.91           C  
ANISOU  897  C   THR A 347     2693   1049   2681    246   -171    151       C  
ATOM    898  O   THR A 347      58.360  36.716   3.533  1.00 18.03           O  
ANISOU  898  O   THR A 347     2759   1326   2764    124   -134    219       O  
ATOM    899  CB  THR A 347      58.754  38.950   1.177  1.00 18.49           C  
ANISOU  899  CB  THR A 347     2924    992   3110    197     85    246       C  
ATOM    900  OG1 THR A 347      60.134  39.332   1.266  1.00 21.01           O  
ANISOU  900  OG1 THR A 347     2924   1068   3992     88    198    194       O  
ATOM    901  CG2 THR A 347      57.977  39.623   2.316  1.00 19.28           C  
ANISOU  901  CG2 THR A 347     3044   1012   3268    449     90   -255       C  
ATOM    902  N   GLY A 348      60.452  36.730   2.692  1.00 15.90           N  
ANISOU  902  N   GLY A 348     2613    856   2570     99   -496     73       N  
ATOM    903  CA  GLY A 348      61.087  36.433   3.961  1.00 15.33           C  
ANISOU  903  CA  GLY A 348     2508    873   2444     64   -207    171       C  
ATOM    904  C   GLY A 348      61.088  34.964   4.340  1.00 14.68           C  
ANISOU  904  C   GLY A 348     2351    733   2492    -86      7    144       C  
ATOM    905  O   GLY A 348      60.476  34.131   3.675  1.00 16.17           O  
ANISOU  905  O   GLY A 348     2483   1030   2631     44   -132    -65       O  
ATOM    906  N   ASP A 349      61.778  34.664   5.434  1.00 13.77           N  
ANISOU  906  N   ASP A 349     2212    837   2183     -5    -74    172       N  
ATOM    907  CA  ASP A 349      61.915  33.300   5.946  1.00 12.65           C  
ANISOU  907  CA  ASP A 349     1802    811   2192   -156      1    232       C  
ATOM    908  C   ASP A 349      60.702  32.975   6.820  1.00 12.28           C  
ANISOU  908  C   ASP A 349     1807    793   2064   -127   -298   -121       C  
ATOM    909  O   ASP A 349      60.505  33.590   7.865  1.00 14.27           O  
ANISOU  909  O   ASP A 349     2070   1084   2269    -21    -32   -265       O  
ATOM    910  CB  ASP A 349      63.212  33.209   6.755  1.00 14.04           C  
ANISOU  910  CB  ASP A 349     1705   1187   2443    -21   -273    115       C  
ATOM    911  CG  ASP A 349      63.512  31.803   7.259  1.00 13.01           C  
ANISOU  911  CG  ASP A 349     1580    943   2420   -180   -328    -93       C  
ATOM    912  OD1 ASP A 349      62.604  30.945   7.265  1.00 12.65           O  
ANISOU  912  OD1 ASP A 349     1604    972   2230   -109     15   -233       O  
ATOM    913  OD2 ASP A 349      64.671  31.560   7.671  1.00 16.26           O  
ANISOU  913  OD2 ASP A 349     1691   1429   3056     71   -273      4       O  
ATOM    914  N   PRO A 350      59.874  32.007   6.390  1.00 10.70           N  
ANISOU  914  N   PRO A 350     1547    795   1724    -96     17     55       N  
ATOM    915  CA  PRO A 350      58.642  31.690   7.118  1.00 11.77           C  
ANISOU  915  CA  PRO A 350     1602    971   1897    -17    -54     44       C  
ATOM    916  C   PRO A 350      58.848  30.628   8.189  1.00 11.38           C  
ANISOU  916  C   PRO A 350     1417    797   2111   -326   -224    -29       C  
ATOM    917  O   PRO A 350      57.869  30.200   8.806  1.00 12.08           O  
ANISOU  917  O   PRO A 350     1465    926   2200     53   -168    -74       O  
ATOM    918  CB  PRO A 350      57.760  31.108   6.022  1.00 13.15           C  
ANISOU  918  CB  PRO A 350     1619   1305   2072     68     80   -164       C  
ATOM    919  CG  PRO A 350      58.743  30.345   5.160  1.00 13.85           C  
ANISOU  919  CG  PRO A 350     1787   1238   2238     11     78   -272       C  
ATOM    920  CD  PRO A 350      60.017  31.189   5.172  1.00 11.67           C  
ANISOU  920  CD  PRO A 350     1640    975   1817   -311    141   -291       C  
ATOM    921  N   SER A 351      60.091  30.212   8.412  1.00 11.02           N  
ANISOU  921  N   SER A 351     1659    723   1805    -82   -395    -80       N  
ATOM    922  CA  SER A 351      60.348  28.986   9.175  1.00 10.39           C  
ANISOU  922  CA  SER A 351     1550    744   1654     57    -23     -5       C  
ATOM    923  C   SER A 351      60.877  29.210  10.590  1.00 10.55           C  
ANISOU  923  C   SER A 351     1585    890   1533   -104    -84      9       C  
ATOM    924  O   SER A 351      61.482  30.241  10.901  1.00 12.16           O  
ANISOU  924  O   SER A 351     1749    857   2014   -141   -242    -90       O  
ATOM    925  CB  SER A 351      61.315  28.070   8.409  1.00 11.60           C  
ANISOU  925  CB  SER A 351     1540    949   1917     35    118    -28       C  
ATOM    926  OG  SER A 351      62.654  28.549   8.442  1.00 13.03           O  
ANISOU  926  OG  SER A 351     1468   1259   2222      6     -1    -74       O  
ATOM    927  N   GLY A 352      60.666  28.205  11.431  1.00 12.02           N  
ANISOU  927  N   GLY A 352     1577   1032   1959    104   -260    153       N  
ATOM    928  CA  GLY A 352      61.220  28.204  12.766  1.00 12.39           C  
ANISOU  928  CA  GLY A 352     1812    980   1916     -1   -286    423       C  
ATOM    929  C   GLY A 352      61.295  26.793  13.302  1.00 10.97           C  
ANISOU  929  C   GLY A 352     1482    827   1859   -128   -423     46       C  
ATOM    930  O   GLY A 352      61.075  25.824  12.567  1.00 11.41           O  
ANISOU  930  O   GLY A 352     1316   1092   1928    -55   -260   -268       O  
ATOM    931  N   LYS A 353      61.624  26.673  14.581  1.00 12.86           N  
ANISOU  931  N   LYS A 353     1736   1144   2006     99   -321    186       N  
ATOM    932  CA  LYS A 353      61.652  25.380  15.238  1.00 11.75           C  
ANISOU  932  CA  LYS A 353     1858   1056   1550    146   -159    123       C  
ATOM    933  C   LYS A 353      61.252  25.584  16.681  1.00 11.60           C  
ANISOU  933  C   LYS A 353     1860    875   1671     13   -169    -17       C  
ATOM    934  O   LYS A 353      61.368  26.692  17.217  1.00 14.58           O  
ANISOU  934  O   LYS A 353     2389   1003   2146    -71   -245   -247       O  
ATOM    935  CB  LYS A 353      63.040  24.763  15.155  1.00 15.21           C  
ANISOU  935  CB  LYS A 353     2025   1253   2501    216   -388     46       C  
ATOM    936  CG  LYS A 353      64.113  25.640  15.761  1.00 18.73           C  
ANISOU  936  CG  LYS A 353     1984   1823   3309    283   -509   -153       C  
ATOM    937  CD  LYS A 353      65.498  25.103  15.474  1.00 21.85           C  
ANISOU  937  CD  LYS A 353     2114   2244   3942    442   -726   -119       C  
ATOM    938  CE  LYS A 353      65.733  23.777  16.172  1.00 21.54           C  
ANISOU  938  CE  LYS A 353     2148   2055   3979    678   -443     49       C  
ATOM    939  NZ  LYS A 353      67.166  23.377  16.064  1.00 20.47           N  
ANISOU  939  NZ  LYS A 353     2204   1923   3649    634   -634   -311       N  
ATOM    940  N   VAL A 354      60.771  24.524  17.314  1.00 10.73           N  
ANISOU  940  N   VAL A 354     1469   1073   1536     69    -62    125       N  
ATOM    941  CA  VAL A 354      60.294  24.630  18.682  1.00 10.50           C  
ANISOU  941  CA  VAL A 354     1486    923   1579    -33     76     45       C  
ATOM    942  C   VAL A 354      60.183  23.243  19.295  1.00 10.22           C  
ANISOU  942  C   VAL A 354     1520    781   1582    144   -188     19       C  
ATOM    943  O   VAL A 354      60.016  22.254  18.580  1.00 12.94           O  
ANISOU  943  O   VAL A 354     2094    883   1939    221   -209   -371       O  
ATOM    944  CB  VAL A 354      58.933  25.364  18.730  1.00 11.92           C  
ANISOU  944  CB  VAL A 354     1521   1485   1522    331   -400   -500       C  
ATOM    945  CG1 VAL A 354      57.832  24.507  18.146  1.00 13.08           C  
ANISOU  945  CG1 VAL A 354     1363   1577   2028    313   -601   -315       C  
ATOM    946  CG2 VAL A 354      58.591  25.800  20.155  1.00 13.77           C  
ANISOU  946  CG2 VAL A 354     1532   1519   2180    194   -404   -395       C  
ATOM    947  N   VAL A 355      60.313  23.173  20.614  1.00 10.95           N  
ANISOU  947  N   VAL A 355     1556    884   1719    440   -313    131       N  
ATOM    948  CA  VAL A 355      60.141  21.926  21.341  1.00 10.92           C  
ANISOU  948  CA  VAL A 355     1439   1168   1540    311   -249    124       C  
ATOM    949  C   VAL A 355      58.748  21.909  21.962  1.00 10.61           C  
ANISOU  949  C   VAL A 355     1439   1109   1482    343   -182   -357       C  
ATOM    950  O   VAL A 355      58.297  22.912  22.535  1.00 10.97           O  
ANISOU  950  O   VAL A 355     1594   1000   1573    455   -132   -354       O  
ATOM    951  CB  VAL A 355      61.198  21.777  22.451  1.00 11.76           C  
ANISOU  951  CB  VAL A 355     1649   1186   1633    258   -316    100       C  
ATOM    952  CG1 VAL A 355      60.983  20.487  23.225  1.00 14.53           C  
ANISOU  952  CG1 VAL A 355     1810   1609   2100    280   -489    237       C  
ATOM    953  CG2 VAL A 355      62.599  21.838  21.856  1.00 13.69           C  
ANISOU  953  CG2 VAL A 355     1730   1333   2137    331     -8   -155       C  
ATOM    954  N   ILE A 356      58.063  20.779  21.826  1.00 10.70           N  
ANISOU  954  N   ILE A 356     1392   1052   1621    140   -151   -196       N  
ATOM    955  CA  ILE A 356      56.779  20.564  22.482  1.00 10.30           C  
ANISOU  955  CA  ILE A 356     1493   1130   1288    295   -217    -62       C  
ATOM    956  C   ILE A 356      56.863  19.324  23.370  1.00 10.04           C  
ANISOU  956  C   ILE A 356     1531    890   1392    168   -184    -93       C  
ATOM    957  O   ILE A 356      57.154  18.220  22.892  1.00 11.63           O  
ANISOU  957  O   ILE A 356     1906    823   1688    372   -267   -213       O  
ATOM    958  CB  ILE A 356      55.641  20.390  21.448  1.00 10.82           C  
ANISOU  958  CB  ILE A 356     1565   1082   1463    224   -169   -107       C  
ATOM    959  CG1 ILE A 356      55.539  21.644  20.562  1.00 11.53           C  
ANISOU  959  CG1 ILE A 356     1885    927   1570    477   -512     32       C  
ATOM    960  CG2 ILE A 356      54.303  20.099  22.141  1.00 11.88           C  
ANISOU  960  CG2 ILE A 356     1382   1444   1687     29     15   -102       C  
ATOM    961  CD1 ILE A 356      54.509  21.529  19.461  1.00 11.41           C  
ANISOU  961  CD1 ILE A 356     1725   1111   1499    399   -431    -34       C  
ATOM    962  N   HIS A 357      56.604  19.505  24.658  1.00 10.69           N  
ANISOU  962  N   HIS A 357     1580   1245   1235    299   -312      6       N  
ATOM    963  CA  HIS A 357      56.543  18.390  25.600  1.00 10.70           C  
ANISOU  963  CA  HIS A 357     1685   1120   1259    275   -472   -122       C  
ATOM    964  C   HIS A 357      55.227  17.649  25.441  1.00 10.08           C  
ANISOU  964  C   HIS A 357     1550    879   1399    187   -484    -58       C  
ATOM    965  O   HIS A 357      54.160  18.259  25.528  1.00 11.52           O  
ANISOU  965  O   HIS A 357     1504   1059   1815    377   -348    -14       O  
ATOM    966  CB  HIS A 357      56.619  18.911  27.039  1.00 12.11           C  
ANISOU  966  CB  HIS A 357     1789   1394   1416    158   -605   -249       C  
ATOM    967  CG  HIS A 357      57.927  19.547  27.385  1.00 12.68           C  
ANISOU  967  CG  HIS A 357     1870   1391   1557    246   -814   -281       C  
ATOM    968  ND1 HIS A 357      58.124  20.249  28.557  1.00 13.95           N  
ANISOU  968  ND1 HIS A 357     2267   1582   1452    452   -599   -471       N  
ATOM    969  CD2 HIS A 357      59.105  19.582  26.722  1.00 14.36           C  
ANISOU  969  CD2 HIS A 357     1823   1510   2123    417   -596    276       C  
ATOM    970  CE1 HIS A 357      59.370  20.687  28.598  1.00 15.69           C  
ANISOU  970  CE1 HIS A 357     2105   1497   2357    240   -754   -276       C  
ATOM    971  NE2 HIS A 357      59.989  20.295  27.500  1.00 14.45           N  
ANISOU  971  NE2 HIS A 357     1942   1378   2168    225   -525   -102       N  
ATOM    972  N   SER A 358      55.283  16.334  25.235  1.00 10.61           N  
ANISOU  972  N   SER A 358     1673   1032   1326     94   -120    165       N  
ATOM    973  CA  SER A 358      54.055  15.536  25.243  1.00 10.37           C  
ANISOU  973  CA  SER A 358     1690   1055   1196    128    -45   -115       C  
ATOM    974  C   SER A 358      53.782  15.022  26.662  1.00 11.68           C  
ANISOU  974  C   SER A 358     1805   1186   1448    319    -29     42       C  
ATOM    975  O   SER A 358      53.616  13.818  26.899  1.00 12.61           O  
ANISOU  975  O   SER A 358     1897   1119   1776    404   -110     -1       O  
ATOM    976  CB  SER A 358      54.087  14.401  24.213  1.00 10.67           C  
ANISOU  976  CB  SER A 358     1502    965   1587    430   -248   -239       C  
ATOM    977  OG  SER A 358      55.219  13.576  24.387  1.00 10.68           O  
ANISOU  977  OG  SER A 358     1347   1055   1657    463   -221   -104       O  
ATOM    978  N   TYR A 359      53.754  15.961  27.602  1.00 11.91           N  
ANISOU  978  N   TYR A 359     1847   1484   1193    440   -102   -249       N  
ATOM    979  CA  TYR A 359      53.536  15.671  29.015  1.00 11.78           C  
ANISOU  979  CA  TYR A 359     1879   1418   1178    688     19   -108       C  
ATOM    980  C   TYR A 359      53.251  16.975  29.741  1.00 13.60           C  
ANISOU  980  C   TYR A 359     2081   1354   1732    595   -188   -368       C  
ATOM    981  O   TYR A 359      53.408  18.050  29.153  1.00 12.96           O  
ANISOU  981  O   TYR A 359     1979   1322   1621    383   -167   -201       O  
ATOM    982  CB  TYR A 359      54.739  14.935  29.636  1.00 13.04           C  
ANISOU  982  CB  TYR A 359     1871   1482   1602    547   -239     29       C  
ATOM    983  CG  TYR A 359      56.091  15.598  29.446  1.00 12.64           C  
ANISOU  983  CG  TYR A 359     1924   1443   1434    377   -464    -61       C  
ATOM    984  CD1 TYR A 359      56.597  16.482  30.397  1.00 14.78           C  
ANISOU  984  CD1 TYR A 359     2210   1654   1751    457   -405     41       C  
ATOM    985  CD2 TYR A 359      56.870  15.328  28.317  1.00 12.87           C  
ANISOU  985  CD2 TYR A 359     1948   1445   1497    504   -190    271       C  
ATOM    986  CE1 TYR A 359      57.837  17.080  30.233  1.00 14.09           C  
ANISOU  986  CE1 TYR A 359     2210   1548   1593    499   -442   -240       C  
ATOM    987  CE2 TYR A 359      58.112  15.925  28.139  1.00 13.29           C  
ANISOU  987  CE2 TYR A 359     2034   1083   1931    298   -545      3       C  
ATOM    988  CZ  TYR A 359      58.591  16.794  29.103  1.00 12.94           C  
ANISOU  988  CZ  TYR A 359     2031   1206   1677    216   -304   -158       C  
ATOM    989  OH  TYR A 359      59.820  17.386  28.943  1.00 13.85           O  
ANISOU  989  OH  TYR A 359     1972   1374   1916    470   -264    -50       O  
ATOM    990  N   ASP A 360      52.846  16.854  31.010  1.00 14.17           N  
ANISOU  990  N   ASP A 360     2250   1732   1403    732    -69   -411       N  
ATOM    991  CA  ASP A 360      52.366  17.955  31.859  1.00 14.10           C  
ANISOU  991  CA  ASP A 360     2206   1739   1411    621   -103   -384       C  
ATOM    992  C   ASP A 360      50.955  18.395  31.472  1.00 13.03           C  
ANISOU  992  C   ASP A 360     2136   1501   1314    489   -153     86       C  
ATOM    993  O   ASP A 360      50.499  18.146  30.355  1.00 13.72           O  
ANISOU  993  O   ASP A 360     2321   1350   1543    449   -160    -54       O  
ATOM    994  CB  ASP A 360      53.327  19.155  31.874  1.00 16.74           C  
ANISOU  994  CB  ASP A 360     2172   2030   2158    407   -365   -746       C  
ATOM    995  CG  ASP A 360      54.653  18.838  32.534  1.00 16.96           C  
ANISOU  995  CG  ASP A 360     2670   2179   1593    434   -370   -549       C  
ATOM    996  OD1 ASP A 360      54.715  17.904  33.369  1.00 20.01           O  
ANISOU  996  OD1 ASP A 360     3045   2390   2166    643   -420   -110       O  
ATOM    997  OD2 ASP A 360      55.637  19.533  32.223  1.00 18.56           O  
ANISOU  997  OD2 ASP A 360     2727   2259   2066    173   -382   -375       O  
ATOM    998  N   ALA A 361      50.268  19.043  32.406  1.00 14.70           N  
ANISOU  998  N   ALA A 361     2433   1618   1533    778    426     69       N  
ATOM    999  CA  ALA A 361      48.875  19.430  32.205  1.00 15.39           C  
ANISOU  999  CA  ALA A 361     2222   1791   1833    705    377     63       C  
ATOM   1000  C   ALA A 361      48.706  20.365  31.009  1.00 14.52           C  
ANISOU 1000  C   ALA A 361     1978   1639   1899    518    302   -198       C  
ATOM   1001  O   ALA A 361      47.631  20.431  30.412  1.00 15.39           O  
ANISOU 1001  O   ALA A 361     1827   1697   2322    307     92   -225       O  
ATOM   1002  CB  ALA A 361      48.318  20.069  33.465  1.00 17.85           C  
ANISOU 1002  CB  ALA A 361     2612   2370   1800    861    345   -506       C  
ATOM   1003  N   THR A 362      49.772  21.090  30.671  1.00 13.08           N  
ANISOU 1003  N   THR A 362     2084   1500   1385    700     60   -102       N  
ATOM   1004  CA  THR A 362      49.746  22.027  29.553  1.00 13.35           C  
ANISOU 1004  CA  THR A 362     1996   1506   1571    532   -211   -254       C  
ATOM   1005  C   THR A 362      49.842  21.331  28.189  1.00 12.12           C  
ANISOU 1005  C   THR A 362     1890   1369   1344    475   -172    -35       C  
ATOM   1006  O   THR A 362      49.719  21.974  27.147  1.00 13.37           O  
ANISOU 1006  O   THR A 362     1898   1620   1562    621     41   -152       O  
ATOM   1007  CB  THR A 362      50.855  23.075  29.679  1.00 14.17           C  
ANISOU 1007  CB  THR A 362     1970   1280   2135    348   -272   -795       C  
ATOM   1008  OG1 THR A 362      52.086  22.431  30.036  1.00 14.15           O  
ANISOU 1008  OG1 THR A 362     1977   1475   1924    405    -91   -482       O  
ATOM   1009  CG2 THR A 362      50.499  24.081  30.763  1.00 16.79           C  
ANISOU 1009  CG2 THR A 362     2340   1423   2616    377    207   -844       C  
ATOM   1010  N   PHE A 363      50.080  20.022  28.190  1.00 11.79           N  
ANISOU 1010  N   PHE A 363     1791   1280   1408    507     -9   -244       N  
ATOM   1011  CA  PHE A 363      49.938  19.230  26.972  1.00 11.65           C  
ANISOU 1011  CA  PHE A 363     1633   1181   1612    503   -148   -243       C  
ATOM   1012  C   PHE A 363      48.488  18.755  26.932  1.00 11.43           C  
ANISOU 1012  C   PHE A 363     1558   1139   1646    444     51     90       C  
ATOM   1013  O   PHE A 363      48.119  17.804  27.620  1.00 12.63           O  
ANISOU 1013  O   PHE A 363     1838   1414   1546    537   -108    -19       O  
ATOM   1014  CB  PHE A 363      50.924  18.051  26.969  1.00 11.16           C  
ANISOU 1014  CB  PHE A 363     1642   1004   1592    513    -21   -354       C  
ATOM   1015  CG  PHE A 363      50.787  17.135  25.778  1.00 10.70           C  
ANISOU 1015  CG  PHE A 363     1529   1055   1480    398    -28    -52       C  
ATOM   1016  CD1 PHE A 363      51.214  17.537  24.519  1.00 11.25           C  
ANISOU 1016  CD1 PHE A 363     1624   1259   1389    601   -193   -139       C  
ATOM   1017  CD2 PHE A 363      50.236  15.870  25.920  1.00 11.78           C  
ANISOU 1017  CD2 PHE A 363     1631   1386   1459    595    -41   -158       C  
ATOM   1018  CE1 PHE A 363      51.090  16.693  23.419  1.00 12.47           C  
ANISOU 1018  CE1 PHE A 363     1657   1181   1898    598    -74     77       C  
ATOM   1019  CE2 PHE A 363      50.111  15.019  24.827  1.00 12.07           C  
ANISOU 1019  CE2 PHE A 363     1546   1381   1658    494    -73   -262       C  
ATOM   1020  CZ  PHE A 363      50.536  15.432  23.572  1.00 12.07           C  
ANISOU 1020  CZ  PHE A 363     1595   1504   1485    439    151    184       C  
ATOM   1021  N   ALA A 364      47.659  19.443  26.147  1.00 10.86           N  
ANISOU 1021  N   ALA A 364     1419   1159   1548    518   -136     -5       N  
ATOM   1022  CA  ALA A 364      46.223  19.195  26.166  1.00 11.01           C  
ANISOU 1022  CA  ALA A 364     1384   1438   1359    413      9   -319       C  
ATOM   1023  C   ALA A 364      45.619  19.195  24.754  1.00 10.66           C  
ANISOU 1023  C   ALA A 364     1541   1222   1287    312    101    -52       C  
ATOM   1024  O   ALA A 364      44.635  19.894  24.490  1.00 11.61           O  
ANISOU 1024  O   ALA A 364     1400   1382   1630    525     31     12       O  
ATOM   1025  CB  ALA A 364      45.521  20.237  27.059  1.00 12.45           C  
ANISOU 1025  CB  ALA A 364     1603   1561   1565    425    -73   -487       C  
ATOM   1026  N   PRO A 365      46.195  18.400  23.839  1.00 10.54           N  
ANISOU 1026  N   PRO A 365     1586   1046   1371    557    190   -132       N  
ATOM   1027  CA  PRO A 365      45.741  18.496  22.445  1.00 11.13           C  
ANISOU 1027  CA  PRO A 365     1568   1271   1391    230     29   -242       C  
ATOM   1028  C   PRO A 365      44.258  18.151  22.269  1.00 11.25           C  
ANISOU 1028  C   PRO A 365     1481   1402   1390    -52    243     -9       C  
ATOM   1029  O   PRO A 365      43.601  18.711  21.396  1.00 12.85           O  
ANISOU 1029  O   PRO A 365     1687   1753   1441    279    -63    -21       O  
ATOM   1030  CB  PRO A 365      46.641  17.493  21.708  1.00 12.33           C  
ANISOU 1030  CB  PRO A 365     1688   1106   1890    473    175   -214       C  
ATOM   1031  CG  PRO A 365      47.102  16.523  22.784  1.00 12.33           C  
ANISOU 1031  CG  PRO A 365     1830   1051   1805    431     -2   -266       C  
ATOM   1032  CD  PRO A 365      47.276  17.411  24.005  1.00 11.64           C  
ANISOU 1032  CD  PRO A 365     1748    823   1851    359     71   -419       C  
ATOM   1033  N   HIS A 366      43.737  17.252  23.099  1.00 11.33           N  
ANISOU 1033  N   HIS A 366     1466   1454   1386     85    251   -167       N  
ATOM   1034  CA  HIS A 366      42.327  16.881  23.037  1.00 12.03           C  
ANISOU 1034  CA  HIS A 366     1526   1291   1753    139    215    -48       C  
ATOM   1035  C   HIS A 366      41.443  18.082  23.374  1.00 11.92           C  
ANISOU 1035  C   HIS A 366     1388   1464   1675    180    -15   -154       C  
ATOM   1036  O   HIS A 366      40.295  18.162  22.926  1.00 13.94           O  
ANISOU 1036  O   HIS A 366     1469   1991   1835    289    -77   -241       O  
ATOM   1037  CB  HIS A 366      42.049  15.732  24.009  1.00 12.95           C  
ANISOU 1037  CB  HIS A 366     1626   1507   1786   -189    133    -40       C  
ATOM   1038  CG  HIS A 366      40.674  15.150  23.899  1.00 15.01           C  
ANISOU 1038  CG  HIS A 366     1730   2178   1794     52    231   -133       C  
ATOM   1039  ND1 HIS A 366      40.170  14.645  22.719  1.00 16.84           N  
ANISOU 1039  ND1 HIS A 366     1745   2632   2022   -182     65     43       N  
ATOM   1040  CD2 HIS A 366      39.712  14.957  24.831  1.00 16.75           C  
ANISOU 1040  CD2 HIS A 366     1715   2622   2028     22    103   -246       C  
ATOM   1041  CE1 HIS A 366      38.952  14.179  22.926  1.00 18.10           C  
ANISOU 1041  CE1 HIS A 366     1926   3233   1718      1     53   -141       C  
ATOM   1042  NE2 HIS A 366      38.649  14.356  24.199  1.00 19.24           N  
ANISOU 1042  NE2 HIS A 366     1763   3152   2394   -263     65    -79       N  
ATOM   1043  N   LEU A 367      41.981  18.999  24.177  1.00 11.80           N  
ANISOU 1043  N   LEU A 367     1605   1252   1627    405    123   -339       N  
ATOM   1044  CA  LEU A 367      41.283  20.230  24.554  1.00 11.81           C  
ANISOU 1044  CA  LEU A 367     1641   1468   1377    511   -118    -95       C  
ATOM   1045  C   LEU A 367      41.560  21.345  23.551  1.00 12.75           C  
ANISOU 1045  C   LEU A 367     1606   1519   1718    558   -132    104       C  
ATOM   1046  O   LEU A 367      40.988  22.429  23.643  1.00 14.49           O  
ANISOU 1046  O   LEU A 367     1914   1889   1700    727     95    121       O  
ATOM   1047  CB  LEU A 367      41.711  20.694  25.950  1.00 11.66           C  
ANISOU 1047  CB  LEU A 367     1626   1680   1125    522    -51    -98       C  
ATOM   1048  CG  LEU A 367      41.216  19.898  27.154  1.00 13.95           C  
ANISOU 1048  CG  LEU A 367     1941   1893   1464    436    153    114       C  
ATOM   1049  CD1 LEU A 367      41.687  18.456  27.092  1.00 17.38           C  
ANISOU 1049  CD1 LEU A 367     2431   2134   2036    445    120    102       C  
ATOM   1050  CD2 LEU A 367      41.682  20.557  28.443  1.00 14.13           C  
ANISOU 1050  CD2 LEU A 367     1922   2013   1433    416    -27   -108       C  
ATOM   1051  N   GLY A 368      42.470  21.085  22.616  1.00 11.89           N  
ANISOU 1051  N   GLY A 368     1422   1411   1685    106     30    176       N  
ATOM   1052  CA  GLY A 368      42.776  22.032  21.560  1.00 11.78           C  
ANISOU 1052  CA  GLY A 368     1483   1221   1771     65    -13     95       C  
ATOM   1053  C   GLY A 368      44.064  22.830  21.698  1.00 11.11           C  
ANISOU 1053  C   GLY A 368     1311   1384   1526    288   -191   -123       C  
ATOM   1054  O   GLY A 368      44.350  23.673  20.836  1.00 12.48           O  
ANISOU 1054  O   GLY A 368     1702   1427   1612    286    137     -6       O  
ATOM   1055  N   THR A 369      44.842  22.584  22.754  1.00 11.37           N  
ANISOU 1055  N   THR A 369     1182   1415   1724    312   -101   -137       N  
ATOM   1056  CA  THR A 369      46.050  23.378  22.991  1.00 11.52           C  
ANISOU 1056  CA  THR A 369     1466   1422   1489    608   -145   -205       C  
ATOM   1057  C   THR A 369      47.251  22.563  23.466  1.00 11.02           C  
ANISOU 1057  C   THR A 369     1445   1387   1354    494   -149     47       C  
ATOM   1058  O   THR A 369      47.100  21.595  24.219  1.00 13.09           O  
ANISOU 1058  O   THR A 369     1662   1425   1887    387   -171    196       O  
ATOM   1059  CB  THR A 369      45.812  24.527  24.009  1.00 13.80           C  
ANISOU 1059  CB  THR A 369     2063   1537   1642    797    -84   -267       C  
ATOM   1060  OG1 THR A 369      45.522  23.983  25.302  1.00 16.72           O  
ANISOU 1060  OG1 THR A 369     2317   2068   1966    844    -75   -229       O  
ATOM   1061  CG2 THR A 369      44.660  25.422  23.565  1.00 14.57           C  
ANISOU 1061  CG2 THR A 369     2002   1259   2275    770   -440   -235       C  
ATOM   1062  N   VAL A 370      48.441  22.969  23.032  1.00 11.05           N  
ANISOU 1062  N   VAL A 370     1086   1440   1672    155    -69   -201       N  
ATOM   1063  CA  VAL A 370      49.685  22.453  23.602  1.00 11.03           C  
ANISOU 1063  CA  VAL A 370     1156   1343   1690    223   -306   -252       C  
ATOM   1064  C   VAL A 370      50.637  23.606  23.894  1.00 10.85           C  
ANISOU 1064  C   VAL A 370     1268   1075   1778    323   -269   -148       C  
ATOM   1065  O   VAL A 370      50.653  24.616  23.178  1.00 11.61           O  
ANISOU 1065  O   VAL A 370     1549   1196   1664    336   -412     77       O  
ATOM   1066  CB  VAL A 370      50.385  21.415  22.681  1.00 11.45           C  
ANISOU 1066  CB  VAL A 370     1694   1207   1450    285     30   -256       C  
ATOM   1067  CG1 VAL A 370      49.510  20.185  22.509  1.00 13.29           C  
ANISOU 1067  CG1 VAL A 370     1835   1260   1954     52   -212   -146       C  
ATOM   1068  CG2 VAL A 370      50.748  22.040  21.332  1.00 13.39           C  
ANISOU 1068  CG2 VAL A 370     1807   1346   1933    267    119   -219       C  
ATOM   1069  N   LYS A 371      51.422  23.455  24.951  1.00 12.23           N  
ANISOU 1069  N   LYS A 371     1476   1355   1817    180   -688   -456       N  
ATOM   1070  CA  LYS A 371      52.431  24.446  25.293  1.00 11.66           C  
ANISOU 1070  CA  LYS A 371     1609   1273   1548    305   -770   -502       C  
ATOM   1071  C   LYS A 371      53.667  24.268  24.411  1.00 11.48           C  
ANISOU 1071  C   LYS A 371     1464   1314   1585    566   -190   -378       C  
ATOM   1072  O   LYS A 371      54.091  23.136  24.130  1.00 12.17           O  
ANISOU 1072  O   LYS A 371     1524   1313   1785    469   -232   -372       O  
ATOM   1073  CB  LYS A 371      52.827  24.342  26.776  1.00 12.33           C  
ANISOU 1073  CB  LYS A 371     1911   1327   1447    238   -810   -212       C  
ATOM   1074  CG  LYS A 371      54.005  25.229  27.150  1.00 13.09           C  
ANISOU 1074  CG  LYS A 371     2049   1576   1346     20   -807   -391       C  
ATOM   1075  CD  LYS A 371      54.362  25.119  28.625  1.00 16.11           C  
ANISOU 1075  CD  LYS A 371     2262   1897   1963     69   -922   -759       C  
ATOM   1076  CE  LYS A 371      55.546  26.009  28.962  1.00 16.85           C  
ANISOU 1076  CE  LYS A 371     2548   1948   1905    119  -1055   -592       C  
ATOM   1077  NZ  LYS A 371      55.949  25.889  30.394  1.00 19.08           N  
ANISOU 1077  NZ  LYS A 371     2892   2297   2060    518   -735   -277       N  
ATOM   1078  N   LEU A 372      54.234  25.393  23.981  1.00 11.11           N  
ANISOU 1078  N   LEU A 372     1290   1336   1595    229   -148   -116       N  
ATOM   1079  CA  LEU A 372      55.520  25.425  23.293  1.00 11.96           C  
ANISOU 1079  CA  LEU A 372     1438   1226   1881    334   -367   -250       C  
ATOM   1080  C   LEU A 372      56.596  25.900  24.260  1.00 13.44           C  
ANISOU 1080  C   LEU A 372     1446   1407   2253    347   -473   -120       C  
ATOM   1081  O   LEU A 372      56.387  26.867  24.989  1.00 15.33           O  
ANISOU 1081  O   LEU A 372     1831   1398   2595    356   -470   -639       O  
ATOM   1082  CB  LEU A 372      55.457  26.393  22.111  1.00 13.14           C  
ANISOU 1082  CB  LEU A 372     1653   1534   1803    100   -365   -148       C  
ATOM   1083  CG  LEU A 372      54.984  25.804  20.772  1.00 16.50           C  
ANISOU 1083  CG  LEU A 372     1872   2120   2278   -368   -489    716       C  
ATOM   1084  CD1 LEU A 372      53.768  24.883  20.913  1.00 19.01           C  
ANISOU 1084  CD1 LEU A 372     2491   1887   2845    119   -541   -129       C  
ATOM   1085  CD2 LEU A 372      54.728  26.931  19.773  1.00 17.79           C  
ANISOU 1085  CD2 LEU A 372     1855   2367   2537   -114   -310    787       C  
ATOM   1086  N   GLU A 373      57.749  25.237  24.262  1.00 12.10           N  
ANISOU 1086  N   GLU A 373     1415   1307   1876    370   -412   -374       N  
ATOM   1087  CA  GLU A 373      58.876  25.711  25.063  1.00 12.49           C  
ANISOU 1087  CA  GLU A 373     1521   1107   2116    186   -733   -224       C  
ATOM   1088  C   GLU A 373      59.409  27.007  24.462  1.00 14.55           C  
ANISOU 1088  C   GLU A 373     1773   1422   2331     69   -684   -448       C  
ATOM   1089  O   GLU A 373      59.622  27.099  23.253  1.00 15.52           O  
ANISOU 1089  O   GLU A 373     2051   1455   2392    -18   -530   -378       O  
ATOM   1090  CB  GLU A 373      59.979  24.650  25.136  1.00 13.21           C  
ANISOU 1090  CB  GLU A 373     1631   1200   2188    478   -487     97       C  
ATOM   1091  CG  GLU A 373      59.515  23.371  25.811  1.00 14.34           C  
ANISOU 1091  CG  GLU A 373     1916   1510   2020    518   -344   -181       C  
ATOM   1092  CD  GLU A 373      58.995  23.636  27.215  1.00 14.16           C  
ANISOU 1092  CD  GLU A 373     1983   1555   1842    139   -598   -438       C  
ATOM   1093  OE1 GLU A 373      59.790  24.102  28.056  1.00 17.31           O  
ANISOU 1093  OE1 GLU A 373     2337   1973   2268    220   -743   -645       O  
ATOM   1094  OE2 GLU A 373      57.789  23.409  27.466  1.00 14.44           O  
ANISOU 1094  OE2 GLU A 373     2025   1447   2012    190   -664   -222       O  
ATOM   1095  N   ASP A 374      59.630  28.009  25.303  1.00 14.29           N  
ANISOU 1095  N   ASP A 374     1828   1224   2378     86   -707   -497       N  
ATOM   1096  CA  ASP A 374      60.126  29.282  24.810  1.00 15.78           C  
ANISOU 1096  CA  ASP A 374     1961   1309   2725    -56   -701   -496       C  
ATOM   1097  C   ASP A 374      61.595  29.166  24.430  1.00 16.81           C  
ANISOU 1097  C   ASP A 374     2027   1851   2509   -227   -674   -391       C  
ATOM   1098  O   ASP A 374      62.433  28.854  25.268  1.00 21.31           O  
ANISOU 1098  O   ASP A 374     2261   2823   3011    125   -565    241       O  
ATOM   1099  CB  ASP A 374      59.935  30.367  25.871  1.00 17.36           C  
ANISOU 1099  CB  ASP A 374     2516   1306   2772    103   -515   -855       C  
ATOM   1100  CG  ASP A 374      60.277  31.760  25.365  1.00 21.17           C  
ANISOU 1100  CG  ASP A 374     2865   1638   3541    196   -820   -770       C  
ATOM   1101  OD1 ASP A 374      60.521  31.924  24.151  1.00 21.77           O  
ANISOU 1101  OD1 ASP A 374     2903   1625   3744     63   -753   -693       O  
ATOM   1102  OD2 ASP A 374      60.292  32.698  26.191  1.00 23.84           O  
ANISOU 1102  OD2 ASP A 374     3203   1953   3903    306   -724   -823       O  
ATOM   1103  N   ASN A 375      61.904  29.412  23.161  1.00 18.15           N  
ANISOU 1103  N   ASN A 375     2013   2148   2735   -216   -399   -579       N  
ATOM   1104  CA  ASN A 375      63.289  29.416  22.700  1.00 19.16           C  
ANISOU 1104  CA  ASN A 375     2423   2202   2653   -419   -272   -443       C  
ATOM   1105  C   ASN A 375      63.753  30.810  22.290  1.00 21.53           C  
ANISOU 1105  C   ASN A 375     2661   2643   2877   -296   -451   -281       C  
ATOM   1106  O   ASN A 375      64.770  30.957  21.613  1.00 22.28           O  
ANISOU 1106  O   ASN A 375     2609   2687   3167   -380   -435   -198       O  
ATOM   1107  CB  ASN A 375      63.483  28.428  21.548  1.00 20.19           C  
ANISOU 1107  CB  ASN A 375     2583   2259   2830   -424   -434   -818       C  
ATOM   1108  CG  ASN A 375      62.619  28.752  20.345  1.00 21.50           C  
ANISOU 1108  CG  ASN A 375     2811   2506   2853   -403   -446   -592       C  
ATOM   1109  OD1 ASN A 375      62.063  29.846  20.238  1.00 22.99           O  
ANISOU 1109  OD1 ASN A 375     2621   2841   3272   -581   -911   -668       O  
ATOM   1110  ND2 ASN A 375      62.504  27.799  19.430  1.00 22.95           N  
ANISOU 1110  ND2 ASN A 375     3097   2405   3217   -329   -465   -712       N  
ATOM   1111  N   ASN A 376      62.994  31.821  22.708  1.00 21.62           N  
ANISOU 1111  N   ASN A 376     2701   2429   3085   -289   -659   -399       N  
ATOM   1112  CA  ASN A 376      63.308  33.224  22.436  1.00 23.37           C  
ANISOU 1112  CA  ASN A 376     2780   2550   3550   -547   -946   -395       C  
ATOM   1113  C   ASN A 376      63.180  33.610  20.963  1.00 23.80           C  
ANISOU 1113  C   ASN A 376     2688   2796   3558   -662   -868   -222       C  
ATOM   1114  O   ASN A 376      63.604  34.691  20.555  1.00 26.07           O  
ANISOU 1114  O   ASN A 376     2846   3029   4028   -549   -606    157       O  
ATOM   1115  CB  ASN A 376      64.702  33.584  22.957  1.00 27.28           C  
ANISOU 1115  CB  ASN A 376     3181   3152   4033   -257  -1134   -829       C  
ATOM   1116  CG  ASN A 376      64.799  33.504  24.469  1.00 33.27           C  
ANISOU 1116  CG  ASN A 376     3559   3811   5269     16  -1209   -833       C  
ATOM   1117  OD1 ASN A 376      63.831  33.770  25.182  1.00 35.85           O  
ANISOU 1117  OD1 ASN A 376     3926   3993   5703    374  -1013  -1079       O  
ATOM   1118  ND2 ASN A 376      65.974  33.138  24.967  1.00 37.15           N  
ANISOU 1118  ND2 ASN A 376     3873   4361   5879    533  -1083   -495       N  
ATOM   1119  N   GLU A 377      62.585  32.731  20.167  1.00 23.20           N  
ANISOU 1119  N   GLU A 377     2455   3177   3181   -655   -953    -18       N  
ATOM   1120  CA  GLU A 377      62.415  33.012  18.747  1.00 24.65           C  
ANISOU 1120  CA  GLU A 377     2589   3461   3315   -388   -910   -160       C  
ATOM   1121  C   GLU A 377      60.994  32.714  18.273  1.00 20.87           C  
ANISOU 1121  C   GLU A 377     2384   2979   2565   -507   -851   -570       C  
ATOM   1122  O   GLU A 377      60.775  32.344  17.115  1.00 24.00           O  
ANISOU 1122  O   GLU A 377     2397   3916   2804   -287   -450   -225       O  
ATOM   1123  CB  GLU A 377      63.462  32.251  17.933  1.00 30.61           C  
ANISOU 1123  CB  GLU A 377     2924   4393   4314   -252  -1063   -292       C  
ATOM   1124  CG  GLU A 377      64.880  32.710  18.277  1.00 36.50           C  
ANISOU 1124  CG  GLU A 377     3141   5030   5697   -237  -1543   -784       C  
ATOM   1125  CD  GLU A 377      65.968  31.880  17.635  1.00 44.34           C  
ANISOU 1125  CD  GLU A 377     3672   5894   7280    160  -1537   -945       C  
ATOM   1126  OE1 GLU A 377      65.642  30.954  16.869  1.00 47.80           O  
ANISOU 1126  OE1 GLU A 377     3943   6282   7936    519  -1456  -1041       O  
ATOM   1127  OE2 GLU A 377      67.158  32.155  17.902  1.00 47.29           O  
ANISOU 1127  OE2 GLU A 377     3872   6353   7741    278  -1708   -914       O  
ATOM   1128  N   LEU A 378      60.032  32.891  19.175  1.00 19.20           N  
ANISOU 1128  N   LEU A 378     2448   2249   2598   -209   -372    202       N  
ATOM   1129  CA  LEU A 378      58.628  32.619  18.864  1.00 17.34           C  
ANISOU 1129  CA  LEU A 378     2407   1790   2390   -255   -558   -228       C  
ATOM   1130  C   LEU A 378      57.800  33.884  18.670  1.00 18.26           C  
ANISOU 1130  C   LEU A 378     2672   1489   2778   -468   -398     19       C  
ATOM   1131  O   LEU A 378      56.708  33.830  18.109  1.00 18.20           O  
ANISOU 1131  O   LEU A 378     2512   1783   2618   -541   -338     37       O  
ATOM   1132  CB  LEU A 378      57.985  31.758  19.957  1.00 17.12           C  
ANISOU 1132  CB  LEU A 378     2446   1651   2409     52   -444    -42       C  
ATOM   1133  CG  LEU A 378      58.559  30.355  20.163  1.00 15.55           C  
ANISOU 1133  CG  LEU A 378     2361   1390   2156    136   -299   -343       C  
ATOM   1134  CD1 LEU A 378      57.875  29.649  21.318  1.00 15.19           C  
ANISOU 1134  CD1 LEU A 378     1866   1587   2317   -140    -13   -155       C  
ATOM   1135  CD2 LEU A 378      58.429  29.542  18.887  1.00 18.75           C  
ANISOU 1135  CD2 LEU A 378     2935   1589   2598     12   -185   -357       C  
ATOM   1136  N   ASP A 379      58.310  35.022  19.133  1.00 21.55           N  
ANISOU 1136  N   ASP A 379     2898   1774   3517   -436   -864   -153       N  
ATOM   1137  CA  ASP A 379      57.517  36.247  19.138  1.00 22.05           C  
ANISOU 1137  CA  ASP A 379     3136   1707   3535   -556   -842   -315       C  
ATOM   1138  C   ASP A 379      56.980  36.642  17.769  1.00 20.21           C  
ANISOU 1138  C   ASP A 379     2816   1639   3225   -316   -407   -540       C  
ATOM   1139  O   ASP A 379      55.831  37.083  17.652  1.00 19.58           O  
ANISOU 1139  O   ASP A 379     2641   1758   3038   -250    144   -259       O  
ATOM   1140  CB  ASP A 379      58.300  37.409  19.750  1.00 25.15           C  
ANISOU 1140  CB  ASP A 379     3769   1971   3816   -676  -1445   -321       C  
ATOM   1141  CG  ASP A 379      58.343  37.340  21.259  1.00 31.71           C  
ANISOU 1141  CG  ASP A 379     4467   2896   4686   -778  -1455   -122       C  
ATOM   1142  OD1 ASP A 379      57.368  36.833  21.855  1.00 31.92           O  
ANISOU 1142  OD1 ASP A 379     4727   2889   4511   -802  -1506    -73       O  
ATOM   1143  OD2 ASP A 379      59.346  37.787  21.848  1.00 36.34           O  
ANISOU 1143  OD2 ASP A 379     4774   3721   5310   -598  -1411    173       O  
ATOM   1144  N   GLN A 380      57.805  36.494  16.736  1.00 19.44           N  
ANISOU 1144  N   GLN A 380     2696   1288   3403   -270    -87    -38       N  
ATOM   1145  CA  GLN A 380      57.405  36.933  15.405  1.00 20.13           C  
ANISOU 1145  CA  GLN A 380     2655   1432   3559      8    299    314       C  
ATOM   1146  C   GLN A 380      56.254  36.088  14.881  1.00 17.10           C  
ANISOU 1146  C   GLN A 380     2401   1210   2885     99    154    157       C  
ATOM   1147  O   GLN A 380      55.599  36.460  13.904  1.00 20.44           O  
ANISOU 1147  O   GLN A 380     2702   1694   3370    341      2    312       O  
ATOM   1148  CB  GLN A 380      58.578  36.886  14.421  1.00 23.51           C  
ANISOU 1148  CB  GLN A 380     2700   1781   4450    280    505    472       C  
ATOM   1149  CG  GLN A 380      59.046  35.484  14.059  1.00 25.26           C  
ANISOU 1149  CG  GLN A 380     2759   2258   4581    366    725    403       C  
ATOM   1150  CD  GLN A 380      59.749  35.440  12.708  1.00 28.91           C  
ANISOU 1150  CD  GLN A 380     3115   3217   4650    681    471    572       C  
ATOM   1151  OE1 GLN A 380      59.211  35.903  11.699  1.00 31.41           O  
ANISOU 1151  OE1 GLN A 380     3436   3608   4888    667    536    137       O  
ATOM   1152  NE2 GLN A 380      60.955  34.889  12.686  1.00 29.89           N  
ANISOU 1152  NE2 GLN A 380     3054   3654   4647    405    394    604       N  
ATOM   1153  N   PHE A 381      56.013  34.950  15.531  1.00 14.71           N  
ANISOU 1153  N   PHE A 381     2101   1117   2370     66    197   -118       N  
ATOM   1154  CA  PHE A 381      54.981  34.021  15.072  1.00 14.37           C  
ANISOU 1154  CA  PHE A 381     1971    904   2584    305     87   -131       C  
ATOM   1155  C   PHE A 381      53.688  34.083  15.872  1.00 13.36           C  
ANISOU 1155  C   PHE A 381     2054   1248   1774    534     76     27       C  
ATOM   1156  O   PHE A 381      52.705  33.431  15.520  1.00 14.43           O  
ANISOU 1156  O   PHE A 381     2071   1250   2161    441   -167   -225       O  
ATOM   1157  CB  PHE A 381      55.516  32.584  15.067  1.00 14.34           C  
ANISOU 1157  CB  PHE A 381     1945   1154   2349    619     47   -135       C  
ATOM   1158  CG  PHE A 381      56.693  32.390  14.163  1.00 14.71           C  
ANISOU 1158  CG  PHE A 381     1891   1343   2353    386   -186   -328       C  
ATOM   1159  CD1 PHE A 381      56.530  32.419  12.786  1.00 15.74           C  
ANISOU 1159  CD1 PHE A 381     2021   1556   2402    417     30   -353       C  
ATOM   1160  CD2 PHE A 381      57.960  32.190  14.683  1.00 15.80           C  
ANISOU 1160  CD2 PHE A 381     1914   1567   2522    383    -28   -293       C  
ATOM   1161  CE1 PHE A 381      57.603  32.249  11.936  1.00 14.92           C  
ANISOU 1161  CE1 PHE A 381     1700   1613   2355    151   -203   -301       C  
ATOM   1162  CE2 PHE A 381      59.048  32.016  13.839  1.00 15.44           C  
ANISOU 1162  CE2 PHE A 381     1700   1557   2609    189   -110   -626       C  
ATOM   1163  CZ  PHE A 381      58.871  32.047  12.467  1.00 16.51           C  
ANISOU 1163  CZ  PHE A 381     1952   1817   2502    236    -29   -489       C  
ATOM   1164  N   VAL A 382      53.676  34.864  16.944  1.00 13.75           N  
ANISOU 1164  N   VAL A 382     2148   1301   1773    303     35   -226       N  
ATOM   1165  CA  VAL A 382      52.466  34.982  17.745  1.00 13.29           C  
ANISOU 1165  CA  VAL A 382     2103   1365   1579    245   -126   -444       C  
ATOM   1166  C   VAL A 382      51.350  35.566  16.886  1.00 13.90           C  
ANISOU 1166  C   VAL A 382     2185   1146   1949    395   -137   -260       C  
ATOM   1167  O   VAL A 382      51.517  36.608  16.252  1.00 16.41           O  
ANISOU 1167  O   VAL A 382     2467   1262   2507    361     -3     10       O  
ATOM   1168  CB  VAL A 382      52.687  35.824  19.016  1.00 14.19           C  
ANISOU 1168  CB  VAL A 382     2067   1411   1911    228   -126   -353       C  
ATOM   1169  CG1 VAL A 382      51.364  36.098  19.710  1.00 16.20           C  
ANISOU 1169  CG1 VAL A 382     2130   1774   2249    475    279   -638       C  
ATOM   1170  CG2 VAL A 382      53.649  35.100  19.954  1.00 16.74           C  
ANISOU 1170  CG2 VAL A 382     2405   1954   2001    369   -488   -388       C  
ATOM   1171  N   GLY A 383      50.223  34.863  16.856  1.00 12.97           N  
ANISOU 1171  N   GLY A 383     1923   1303   1702    389    -74   -507       N  
ATOM   1172  CA  GLY A 383      49.090  35.255  16.041  1.00 13.12           C  
ANISOU 1172  CA  GLY A 383     1877   1369   1739    572   -302   -390       C  
ATOM   1173  C   GLY A 383      49.091  34.643  14.653  1.00 13.81           C  
ANISOU 1173  C   GLY A 383     2045   1462   1740    672   -157     23       C  
ATOM   1174  O   GLY A 383      48.124  34.806  13.914  1.00 16.35           O  
ANISOU 1174  O   GLY A 383     2390   1893   1930    907   -399   -226       O  
ATOM   1175  N   LYS A 384      50.166  33.937  14.299  1.00 12.39           N  
ANISOU 1175  N   LYS A 384     1902    953   1852    384   -138   -101       N  
ATOM   1176  CA  LYS A 384      50.302  33.374  12.958  1.00 13.42           C  
ANISOU 1176  CA  LYS A 384     2076   1201   1822    449    -76   -287       C  
ATOM   1177  C   LYS A 384      49.958  31.889  12.928  1.00 11.06           C  
ANISOU 1177  C   LYS A 384     1728   1007   1466    555   -104    113       C  
ATOM   1178  O   LYS A 384      50.252  31.157  13.874  1.00 11.60           O  
ANISOU 1178  O   LYS A 384     1698   1156   1553    273   -106     11       O  
ATOM   1179  CB  LYS A 384      51.730  33.537  12.431  1.00 14.87           C  
ANISOU 1179  CB  LYS A 384     2379   1400   1870     46     -7   -321       C  
ATOM   1180  CG  LYS A 384      52.314  34.931  12.558  1.00 19.37           C  
ANISOU 1180  CG  LYS A 384     3170   1450   2739     -7   -334   -658       C  
ATOM   1181  CD  LYS A 384      51.602  35.924  11.689  1.00 20.40           C  
ANISOU 1181  CD  LYS A 384     3734   1245   2770    -25   -277   -354       C  
ATOM   1182  CE  LYS A 384      52.393  37.236  11.635  1.00 22.18           C  
ANISOU 1182  CE  LYS A 384     4214   1446   2768     36   -244   -266       C  
ATOM   1183  NZ  LYS A 384      51.619  38.338  11.017  1.00 26.79           N  
ANISOU 1183  NZ  LYS A 384     4522   1882   3775    245    -65   -219       N  
ATOM   1184  N   GLU A 385      49.348  31.454  11.830  1.00 11.21           N  
ANISOU 1184  N   GLU A 385     1543   1061   1656    349     60   -323       N  
ATOM   1185  CA  GLU A 385      49.065  30.039  11.631  1.00 10.49           C  
ANISOU 1185  CA  GLU A 385     1423    965   1598    417    -39   -341       C  
ATOM   1186  C   GLU A 385      50.278  29.341  11.041  1.00 10.33           C  
ANISOU 1186  C   GLU A 385     1276   1065   1583    455     11   -166       C  
ATOM   1187  O   GLU A 385      50.888  29.819  10.081  1.00 10.64           O  
ANISOU 1187  O   GLU A 385     1278   1017   1748    385    193    -21       O  
ATOM   1188  CB  GLU A 385      47.858  29.822  10.721  1.00 12.37           C  
ANISOU 1188  CB  GLU A 385     1603   1138   1957    337   -196   -302       C  
ATOM   1189  CG  GLU A 385      47.299  28.412  10.839  1.00 16.00           C  
ANISOU 1189  CG  GLU A 385     1834   1104   3142    279   -345   -435       C  
ATOM   1190  CD  GLU A 385      46.205  28.102   9.848  1.00 20.65           C  
ANISOU 1190  CD  GLU A 385     2042   1785   4018    643    -95   -540       C  
ATOM   1191  OE1 GLU A 385      46.093  28.814   8.833  1.00 21.96           O  
ANISOU 1191  OE1 GLU A 385     2321   2623   3400    243   -225   -682       O  
ATOM   1192  OE2 GLU A 385      45.458  27.126  10.085  1.00 23.54           O  
ANISOU 1192  OE2 GLU A 385     2026   1780   5136    404   -239   -864       O  
ATOM   1193  N   VAL A 386      50.631  28.211  11.640  1.00  9.80           N  
ANISOU 1193  N   VAL A 386     1222    887   1615    538   -125    -16       N  
ATOM   1194  CA  VAL A 386      51.784  27.438  11.182  1.00  9.95           C  
ANISOU 1194  CA  VAL A 386     1197    863   1718    371   -326      8       C  
ATOM   1195  C   VAL A 386      51.426  25.971  11.005  1.00  8.35           C  
ANISOU 1195  C   VAL A 386     1210    615   1347    114    168     73       C  
ATOM   1196  O   VAL A 386      50.461  25.480  11.591  1.00  9.87           O  
ANISOU 1196  O   VAL A 386     1270    886   1595    132    220      5       O  
ATOM   1197  CB  VAL A 386      52.988  27.556  12.166  1.00 10.18           C  
ANISOU 1197  CB  VAL A 386     1365    892   1609    164   -287     19       C  
ATOM   1198  CG1 VAL A 386      53.426  29.016  12.331  1.00 11.43           C  
ANISOU 1198  CG1 VAL A 386     1579    684   2081     81   -143   -221       C  
ATOM   1199  CG2 VAL A 386      52.669  26.921  13.529  1.00 11.15           C  
ANISOU 1199  CG2 VAL A 386     1602   1105   1530    193     -1    -24       C  
ATOM   1200  N   VAL A 387      52.206  25.285  10.175  1.00  8.93           N  
ANISOU 1200  N   VAL A 387     1171    573   1650    206    -24    -50       N  
ATOM   1201  CA  VAL A 387      52.210  23.830  10.163  1.00  9.01           C  
ANISOU 1201  CA  VAL A 387     1155    725   1541    166   -358   -116       C  
ATOM   1202  C   VAL A 387      53.537  23.352  10.736  1.00  8.80           C  
ANISOU 1202  C   VAL A 387     1020    804   1519    134   -139   -132       C  
ATOM   1203  O   VAL A 387      54.602  23.928  10.453  1.00 10.22           O  
ANISOU 1203  O   VAL A 387     1128    955   1801    150   -207     44       O  
ATOM   1204  CB  VAL A 387      51.954  23.258   8.755  1.00 10.05           C  
ANISOU 1204  CB  VAL A 387     1410    788   1621    237   -277   -216       C  
ATOM   1205  CG1 VAL A 387      50.519  23.513   8.336  1.00 12.31           C  
ANISOU 1205  CG1 VAL A 387     1352   1393   1931    436   -618   -512       C  
ATOM   1206  CG2 VAL A 387      52.908  23.832   7.744  1.00 15.75           C  
ANISOU 1206  CG2 VAL A 387     1738   1450   2795     81    245    143       C  
ATOM   1207  N   LEU A 388      53.459  22.334  11.587  1.00  9.63           N  
ANISOU 1207  N   LEU A 388     1159    915   1586    511   -267   -132       N  
ATOM   1208  CA  LEU A 388      54.626  21.813  12.287  1.00  9.16           C  
ANISOU 1208  CA  LEU A 388     1170    799   1509    334    -84    -94       C  
ATOM   1209  C   LEU A 388      54.858  20.371  11.879  1.00  9.08           C  
ANISOU 1209  C   LEU A 388     1121    755   1575    253   -132   -122       C  
ATOM   1210  O   LEU A 388      53.909  19.617  11.650  1.00 11.37           O  
ANISOU 1210  O   LEU A 388     1097    961   2261     45     56   -265       O  
ATOM   1211  CB  LEU A 388      54.420  21.893  13.800  1.00 10.11           C  
ANISOU 1211  CB  LEU A 388     1399   1024   1417    374     19   -148       C  
ATOM   1212  CG  LEU A 388      54.053  23.271  14.374  1.00 10.01           C  
ANISOU 1212  CG  LEU A 388     1392    775   1634    268   -148   -366       C  
ATOM   1213  CD1 LEU A 388      52.561  23.335  14.698  1.00 11.39           C  
ANISOU 1213  CD1 LEU A 388     1351    958   2019    223     63      0       C  
ATOM   1214  CD2 LEU A 388      54.875  23.534  15.616  1.00 12.62           C  
ANISOU 1214  CD2 LEU A 388     1777   1198   1818    284   -481   -226       C  
ATOM   1215  N   GLU A 389      56.129  19.995  11.778  1.00  9.28           N  
ANISOU 1215  N   GLU A 389     1319    657   1551    402   -106   -130       N  
ATOM   1216  CA  GLU A 389      56.491  18.620  11.468  1.00 11.87           C  
ANISOU 1216  CA  GLU A 389     1833   1185   1490    559   -500   -285       C  
ATOM   1217  C   GLU A 389      57.489  18.110  12.496  1.00  9.67           C  
ANISOU 1217  C   GLU A 389     1199    924   1550    308   -362   -131       C  
ATOM   1218  O   GLU A 389      58.328  18.859  12.996  1.00  9.83           O  
ANISOU 1218  O   GLU A 389     1082    867   1785    135   -325   -141       O  
ATOM   1219  CB  GLU A 389      57.080  18.502  10.068  1.00 15.81           C  
ANISOU 1219  CB  GLU A 389     2578   1761   1666   1154   -475   -407       C  
ATOM   1220  CG  GLU A 389      57.189  17.046   9.631  1.00 23.38           C  
ANISOU 1220  CG  GLU A 389     3296   2509   3077   1107     15   -377       C  
ATOM   1221  CD  GLU A 389      58.121  16.838   8.464  1.00 26.06           C  
ANISOU 1221  CD  GLU A 389     3564   2791   3547    691    677   -144       C  
ATOM   1222  OE1 GLU A 389      58.378  15.655   8.134  1.00 25.93           O  
ANISOU 1222  OE1 GLU A 389     3672   3161   3019   1239    791   -308       O  
ATOM   1223  OE2 GLU A 389      58.586  17.845   7.879  1.00 25.43           O  
ANISOU 1223  OE2 GLU A 389     3346   2691   3626   -245    763     76       O  
ATOM   1224  N   LEU A 390      57.393  16.827  12.811  1.00 10.05           N  
ANISOU 1224  N   LEU A 390     1249    720   1848    246   -420    103       N  
ATOM   1225  CA  LEU A 390      58.279  16.213  13.785  1.00  9.87           C  
ANISOU 1225  CA  LEU A 390     1259    958   1534    356   -157    142       C  
ATOM   1226  C   LEU A 390      59.656  15.956  13.180  1.00  9.38           C  
ANISOU 1226  C   LEU A 390     1067   1053   1444     69   -242   -260       C  
ATOM   1227  O   LEU A 390      59.819  15.083  12.331  1.00 14.52           O  
ANISOU 1227  O   LEU A 390     1648   1692   2175    -71     24   -960       O  
ATOM   1228  CB  LEU A 390      57.664  14.905  14.287  1.00 10.37           C  
ANISOU 1228  CB  LEU A 390     1500    677   1762    174   -380    244       C  
ATOM   1229  CG  LEU A 390      58.458  14.221  15.401  1.00 10.26           C  
ANISOU 1229  CG  LEU A 390     1576    621   1700    227   -399   -166       C  
ATOM   1230  CD1 LEU A 390      58.536  15.109  16.645  1.00 11.78           C  
ANISOU 1230  CD1 LEU A 390     1782    844   1848    182   -285   -528       C  
ATOM   1231  CD2 LEU A 390      57.830  12.872  15.735  1.00 11.48           C  
ANISOU 1231  CD2 LEU A 390     1598    634   2130    -42   -355   -118       C  
ATOM   1232  N   THR A 391      60.655  16.711  13.622  1.00  9.43           N  
ANISOU 1232  N   THR A 391      779   1133   1671    231   -228   -184       N  
ATOM   1233  CA  THR A 391      62.010  16.561  13.085  1.00 10.06           C  
ANISOU 1233  CA  THR A 391      952    924   1946     51   -117   -100       C  
ATOM   1234  C   THR A 391      62.796  15.490  13.832  1.00 10.02           C  
ANISOU 1234  C   THR A 391     1189    986   1633    267   -297   -156       C  
ATOM   1235  O   THR A 391      63.453  14.642  13.219  1.00 10.48           O  
ANISOU 1235  O   THR A 391     1182    978   1821    180   -289   -345       O  
ATOM   1236  CB  THR A 391      62.769  17.893  13.124  1.00 10.16           C  
ANISOU 1236  CB  THR A 391      958   1020   1883      7     16    137       C  
ATOM   1237  OG1 THR A 391      62.022  18.851  12.367  1.00 13.27           O  
ANISOU 1237  OG1 THR A 391     1489   1029   2522    488   -193     83       O  
ATOM   1238  CG2 THR A 391      64.167  17.763  12.526  1.00 12.13           C  
ANISOU 1238  CG2 THR A 391     1157   1271   2179    -37    135   -228       C  
ATOM   1239  N   TRP A 392      62.736  15.534  15.155  1.00 10.53           N  
ANISOU 1239  N   TRP A 392     1269   1130   1601    185   -345     63       N  
ATOM   1240  CA  TRP A 392      63.360  14.506  15.971  1.00  9.33           C  
ANISOU 1240  CA  TRP A 392     1012   1036   1495     34   -309     89       C  
ATOM   1241  C   TRP A 392      62.727  14.475  17.365  1.00  9.54           C  
ANISOU 1241  C   TRP A 392     1373    984   1266     36   -286    -60       C  
ATOM   1242  O   TRP A 392      61.926  15.355  17.715  1.00 11.44           O  
ANISOU 1242  O   TRP A 392     1372    999   1974    362    -84   -362       O  
ATOM   1243  CB  TRP A 392      64.894  14.663  16.017  1.00 11.50           C  
ANISOU 1243  CB  TRP A 392     1112   1036   2221     40   -228   -399       C  
ATOM   1244  CG  TRP A 392      65.422  15.918  16.678  1.00 10.00           C  
ANISOU 1244  CG  TRP A 392      945    925   1929    148   -238    -56       C  
ATOM   1245  CD1 TRP A 392      65.391  17.193  16.180  1.00 11.92           C  
ANISOU 1245  CD1 TRP A 392     1048   1212   2268     98   -212   -499       C  
ATOM   1246  CD2 TRP A 392      66.108  15.993  17.933  1.00 10.85           C  
ANISOU 1246  CD2 TRP A 392     1073   1131   1919    158   -288   -352       C  
ATOM   1247  NE1 TRP A 392      65.991  18.062  17.068  1.00 12.54           N  
ANISOU 1247  NE1 TRP A 392     1141   1346   2277    292   -538   -229       N  
ATOM   1248  CE2 TRP A 392      66.450  17.347  18.148  1.00 11.86           C  
ANISOU 1248  CE2 TRP A 392     1159   1367   1980    145   -463   -517       C  
ATOM   1249  CE3 TRP A 392      66.465  15.045  18.902  1.00 13.05           C  
ANISOU 1249  CE3 TRP A 392     1342   1598   2016    236   -531    123       C  
ATOM   1250  CZ2 TRP A 392      67.127  17.779  19.290  1.00 13.14           C  
ANISOU 1250  CZ2 TRP A 392     1384   1502   2106    114   -389    -96       C  
ATOM   1251  CZ3 TRP A 392      67.147  15.473  20.029  1.00 12.99           C  
ANISOU 1251  CZ3 TRP A 392     1399   1551   1986    122   -480    -15       C  
ATOM   1252  CH2 TRP A 392      67.463  16.831  20.218  1.00 14.79           C  
ANISOU 1252  CH2 TRP A 392     1674   1532   2414    113   -534   -494       C  
ATOM   1253  N   VAL A 393      63.064  13.444  18.136  1.00 10.13           N  
ANISOU 1253  N   VAL A 393     1323   1086   1440    222   -347     58       N  
ATOM   1254  CA  VAL A 393      62.480  13.203  19.445  1.00 10.93           C  
ANISOU 1254  CA  VAL A 393     1230   1236   1685    150   -677   -157       C  
ATOM   1255  C   VAL A 393      63.597  12.896  20.432  1.00 11.96           C  
ANISOU 1255  C   VAL A 393     1510   1335   1700    284   -269   -332       C  
ATOM   1256  O   VAL A 393      64.565  12.214  20.086  1.00 12.96           O  
ANISOU 1256  O   VAL A 393     1368   1406   2150    535   -461   -249       O  
ATOM   1257  CB  VAL A 393      61.492  12.003  19.402  1.00 11.51           C  
ANISOU 1257  CB  VAL A 393     1472   1254   1647    204   -440    -99       C  
ATOM   1258  CG1 VAL A 393      60.928  11.707  20.792  1.00 12.78           C  
ANISOU 1258  CG1 VAL A 393     1654   1769   1434    319   -152     58       C  
ATOM   1259  CG2 VAL A 393      60.370  12.264  18.401  1.00 12.36           C  
ANISOU 1259  CG2 VAL A 393     1343   1577   1774    198   -441   -160       C  
ATOM   1260  N   SER A 394      63.471  13.417  21.645  1.00 11.89           N  
ANISOU 1260  N   SER A 394     1548   1379   1591    439   -517   -160       N  
ATOM   1261  CA  SER A 394      64.376  13.032  22.722  1.00 13.03           C  
ANISOU 1261  CA  SER A 394     1747   1393   1811    504   -702   -264       C  
ATOM   1262  C   SER A 394      63.602  12.743  24.008  1.00 12.72           C  
ANISOU 1262  C   SER A 394     1890   1353   1589    474   -650      3       C  
ATOM   1263  O   SER A 394      62.408  13.055  24.115  1.00 12.85           O  
ANISOU 1263  O   SER A 394     1716   1396   1770    532   -544     66       O  
ATOM   1264  CB  SER A 394      65.433  14.113  22.966  1.00 13.43           C  
ANISOU 1264  CB  SER A 394     1756   1294   2052    564   -430   -516       C  
ATOM   1265  OG  SER A 394      64.819  15.319  23.370  1.00 13.77           O  
ANISOU 1265  OG  SER A 394     1832   1361   2040    258   -515   -168       O  
ATOM   1266  N   ASN A 395      64.278  12.137  24.979  1.00 13.84           N  
ANISOU 1266  N   ASN A 395     2038   1481   1739    439   -842    -29       N  
ATOM   1267  CA  ASN A 395      63.628  11.815  26.242  1.00 14.52           C  
ANISOU 1267  CA  ASN A 395     2377   1682   1459    565   -846     69       C  
ATOM   1268  C   ASN A 395      63.333  13.045  27.087  1.00 15.46           C  
ANISOU 1268  C   ASN A 395     2629   1672   1572    555   -683    -78       C  
ATOM   1269  O   ASN A 395      64.024  14.066  27.010  1.00 17.41           O  
ANISOU 1269  O   ASN A 395     2642   1842   2131    406   -597    -49       O  
ATOM   1270  CB  ASN A 395      64.471  10.829  27.053  1.00 16.85           C  
ANISOU 1270  CB  ASN A 395     2395   2012   1993    605  -1140    -74       C  
ATOM   1271  CG  ASN A 395      65.773  11.439  27.537  1.00 19.08           C  
ANISOU 1271  CG  ASN A 395     2762   2370   2117    939  -1086    -10       C  
ATOM   1272  OD1 ASN A 395      66.663  11.726  26.740  1.00 21.50           O  
ANISOU 1272  OD1 ASN A 395     2827   3000   2342    713  -1034    -42       O  
ATOM   1273  ND2 ASN A 395      65.899  11.620  28.852  1.00 19.99           N  
ANISOU 1273  ND2 ASN A 395     2877   2308   2411   1095  -1176   -246       N  
ATOM   1274  N   ARG A 396      62.284  12.936  27.890  1.00 15.95           N  
ANISOU 1274  N   ARG A 396     2566   1781   1712    441   -703    -19       N  
ATOM   1275  CA  ARG A 396      62.019  13.887  28.958  1.00 16.32           C  
ANISOU 1275  CA  ARG A 396     2598   1941   1662    300   -907   -433       C  
ATOM   1276  C   ARG A 396      63.085  13.715  30.028  1.00 17.50           C  
ANISOU 1276  C   ARG A 396     2861   1780   2008    400   -888   -622       C  
ATOM   1277  O   ARG A 396      63.434  12.589  30.381  1.00 18.27           O  
ANISOU 1277  O   ARG A 396     2944   1834   2162    892   -845   -330       O  
ATOM   1278  CB  ARG A 396      60.644  13.586  29.551  1.00 19.52           C  
ANISOU 1278  CB  ARG A 396     2627   2646   2143    753   -521   -990       C  
ATOM   1279  CG  ARG A 396      60.318  14.323  30.816  1.00 22.39           C  
ANISOU 1279  CG  ARG A 396     3073   2905   2527    776   -504    -92       C  
ATOM   1280  CD  ARG A 396      58.989  13.848  31.359  1.00 21.33           C  
ANISOU 1280  CD  ARG A 396     3116   2804   2184    638   -577    633       C  
ATOM   1281  NE  ARG A 396      58.599  14.628  32.524  1.00 22.54           N  
ANISOU 1281  NE  ARG A 396     3662   2632   2268    862   -890    409       N  
ATOM   1282  CZ  ARG A 396      57.425  14.534  33.133  1.00 24.97           C  
ANISOU 1282  CZ  ARG A 396     4126   2698   2663   1153   -747    -70       C  
ATOM   1283  NH1 ARG A 396      56.513  13.682  32.686  1.00 21.80           N  
ANISOU 1283  NH1 ARG A 396     4194   2393   1697   1169   -564   -172       N  
ATOM   1284  NH2 ARG A 396      57.165  15.296  34.189  1.00 27.80           N  
ANISOU 1284  NH2 ARG A 396     4503   2913   3145   1349   -916  -1096       N  
ATOM   1285  N   THR A 397      63.606  14.824  30.534  1.00 19.24           N  
ANISOU 1285  N   THR A 397     3041   2192   2075    256  -1235   -488       N  
ATOM   1286  CA  THR A 397      64.563  14.754  31.629  1.00 22.39           C  
ANISOU 1286  CA  THR A 397     3301   2634   2570    115  -1381   -904       C  
ATOM   1287  C   THR A 397      64.029  13.874  32.752  1.00 23.14           C  
ANISOU 1287  C   THR A 397     3445   2981   2364    530  -1368   -582       C  
ATOM   1288  O   THR A 397      62.896  14.040  33.197  1.00 23.08           O  
ANISOU 1288  O   THR A 397     3454   3036   2277    541  -1006   -502       O  
ATOM   1289  CB  THR A 397      64.876  16.145  32.192  1.00 25.47           C  
ANISOU 1289  CB  THR A 397     3489   3111   3077   -414  -1489   -941       C  
ATOM   1290  OG1 THR A 397      65.452  16.955  31.161  1.00 28.78           O  
ANISOU 1290  OG1 THR A 397     3881   3129   3924   -236  -1326   -816       O  
ATOM   1291  CG2 THR A 397      65.856  16.039  33.359  1.00 27.17           C  
ANISOU 1291  CG2 THR A 397     3661   3174   3489   -235  -1709   -815       C  
ATOM   1292  N   GLY A 398      64.854  12.935  33.207  1.00 24.83           N  
ANISOU 1292  N   GLY A 398     3613   3230   2589    652  -1449   -394       N  
ATOM   1293  CA  GLY A 398      64.473  12.053  34.295  1.00 24.74           C  
ANISOU 1293  CA  GLY A 398     3736   3212   2450    589  -1216   -178       C  
ATOM   1294  C   GLY A 398      63.747  10.796  33.852  1.00 24.45           C  
ANISOU 1294  C   GLY A 398     3939   3109   2243    687  -1187     55       C  
ATOM   1295  O   GLY A 398      63.417   9.950  34.680  1.00 28.35           O  
ANISOU 1295  O   GLY A 398     4516   3473   2781    602   -865    537       O  
ATOM   1296  N   ALA A 399      63.496  10.670  32.552  1.00 22.38           N  
ANISOU 1296  N   ALA A 399     3531   2740   2231    742  -1136   -278       N  
ATOM   1297  CA  ALA A 399      62.785   9.511  32.027  1.00 21.97           C  
ANISOU 1297  CA  ALA A 399     3375   2597   2375    852   -853    305       C  
ATOM   1298  C   ALA A 399      63.529   8.898  30.851  1.00 21.43           C  
ANISOU 1298  C   ALA A 399     3356   2183   2601    891   -915   -188       C  
ATOM   1299  O   ALA A 399      64.360   9.552  30.222  1.00 23.84           O  
ANISOU 1299  O   ALA A 399     3632   2039   3385   1053   -745    326       O  
ATOM   1300  CB  ALA A 399      61.372   9.906  31.602  1.00 22.33           C  
ANISOU 1300  CB  ALA A 399     3243   2766   2473    905   -601    112       C  
ATOM   1301  N   THR A 400      63.232   7.637  30.551  1.00 21.21           N  
ANISOU 1301  N   THR A 400     3365   2449   2244   1134  -1084   -220       N  
ATOM   1302  CA  THR A 400      63.731   7.032  29.321  1.00 21.51           C  
ANISOU 1302  CA  THR A 400     3304   2288   2582   1018  -1196     10       C  
ATOM   1303  C   THR A 400      62.740   7.326  28.200  1.00 19.30           C  
ANISOU 1303  C   THR A 400     2719   2148   2464    697   -999     21       C  
ATOM   1304  O   THR A 400      61.570   7.628  28.456  1.00 19.38           O  
ANISOU 1304  O   THR A 400     2719   2111   2532    622   -951   -231       O  
ATOM   1305  CB  THR A 400      63.902   5.517  29.455  1.00 27.49           C  
ANISOU 1305  CB  THR A 400     3941   2678   3824   1088  -1189    405       C  
ATOM   1306  OG1 THR A 400      62.636   4.916  29.752  1.00 28.93           O  
ANISOU 1306  OG1 THR A 400     4310   2519   4161    814   -893    267       O  
ATOM   1307  CG2 THR A 400      64.884   5.197  30.567  1.00 29.73           C  
ANISOU 1307  CG2 THR A 400     4176   3068   4050   1564  -1128    624       C  
ATOM   1308  N   LEU A 401      63.212   7.253  26.962  1.00 17.86           N  
ANISOU 1308  N   LEU A 401     2542   1960   2284    636  -1077    -67       N  
ATOM   1309  CA  LEU A 401      62.332   7.424  25.814  1.00 17.09           C  
ANISOU 1309  CA  LEU A 401     2513   1745   2234    441   -750   -325       C  
ATOM   1310  C   LEU A 401      61.563   6.134  25.573  1.00 17.21           C  
ANISOU 1310  C   LEU A 401     2560   1551   2426    548   -438   -352       C  
ATOM   1311  O   LEU A 401      62.154   5.093  25.263  1.00 22.38           O  
ANISOU 1311  O   LEU A 401     2763   1733   4005    630   -283   -616       O  
ATOM   1312  CB  LEU A 401      63.130   7.825  24.573  1.00 16.86           C  
ANISOU 1312  CB  LEU A 401     2445   1869   2091    603   -647   -212       C  
ATOM   1313  CG  LEU A 401      62.318   8.068  23.297  1.00 15.97           C  
ANISOU 1313  CG  LEU A 401     2300   1897   1870    519   -399   -194       C  
ATOM   1314  CD1 LEU A 401      61.249   9.149  23.507  1.00 16.24           C  
ANISOU 1314  CD1 LEU A 401     2278   1624   2267    787   -301   -315       C  
ATOM   1315  CD2 LEU A 401      63.242   8.444  22.148  1.00 17.54           C  
ANISOU 1315  CD2 LEU A 401     2269   2343   2050    360   -292   -377       C  
ATOM   1316  N   ASN A 402      60.249   6.200  25.746  1.00 14.70           N  
ANISOU 1316  N   ASN A 402     2449   1286   1848    170   -498    146       N  
ATOM   1317  CA  ASN A 402      59.386   5.028  25.633  1.00 15.02           C  
ANISOU 1317  CA  ASN A 402     2367   1606   1735    177   -604    125       C  
ATOM   1318  C   ASN A 402      58.469   5.162  24.424  1.00 13.59           C  
ANISOU 1318  C   ASN A 402     2165   1398   1600    190   -499    -80       C  
ATOM   1319  O   ASN A 402      57.494   5.920  24.447  1.00 14.85           O  
ANISOU 1319  O   ASN A 402     2464   1424   1753    668   -237     90       O  
ATOM   1320  CB  ASN A 402      58.567   4.864  26.918  1.00 16.50           C  
ANISOU 1320  CB  ASN A 402     2569   1923   1778    242   -422     70       C  
ATOM   1321  CG  ASN A 402      57.592   3.705  26.854  1.00 17.11           C  
ANISOU 1321  CG  ASN A 402     2915   1856   1729    262   -287    338       C  
ATOM   1322  OD1 ASN A 402      57.583   2.933  25.899  1.00 16.75           O  
ANISOU 1322  OD1 ASN A 402     2950   1630   1782    208   -441    119       O  
ATOM   1323  ND2 ASN A 402      56.765   3.574  27.888  1.00 19.96           N  
ANISOU 1323  ND2 ASN A 402     3089   2109   2387    141    -65    326       N  
ATOM   1324  N   LEU A 403      58.794   4.431  23.362  1.00 13.12           N  
ANISOU 1324  N   LEU A 403     2085   1374   1526    134   -427    -48       N  
ATOM   1325  CA  LEU A 403      58.052   4.530  22.110  1.00 13.79           C  
ANISOU 1325  CA  LEU A 403     2035   1401   1801    180    -86   -137       C  
ATOM   1326  C   LEU A 403      56.690   3.829  22.149  1.00 12.78           C  
ANISOU 1326  C   LEU A 403     2000   1222   1633    259   -130    120       C  
ATOM   1327  O   LEU A 403      55.944   3.860  21.163  1.00 13.13           O  
ANISOU 1327  O   LEU A 403     2019   1396   1573    252   -237    -96       O  
ATOM   1328  CB  LEU A 403      58.903   4.025  20.942  1.00 14.73           C  
ANISOU 1328  CB  LEU A 403     1940   1691   1965     61    251   -311       C  
ATOM   1329  CG  LEU A 403      60.245   4.742  20.770  1.00 15.24           C  
ANISOU 1329  CG  LEU A 403     1845   1688   2257    -73     92   -497       C  
ATOM   1330  CD1 LEU A 403      60.929   4.260  19.495  1.00 17.91           C  
ANISOU 1330  CD1 LEU A 403     2013   2154   2636   -165    278   -687       C  
ATOM   1331  CD2 LEU A 403      60.063   6.258  20.744  1.00 15.12           C  
ANISOU 1331  CD2 LEU A 403     1928   1887   1930    -82   -163   -409       C  
ATOM   1332  N   TRP A 404      56.375   3.216  23.289  1.00 13.15           N  
ANISOU 1332  N   TRP A 404     2146   1155   1694    166   -117     81       N  
ATOM   1333  CA  TRP A 404      55.076   2.586  23.527  1.00 13.31           C  
ANISOU 1333  CA  TRP A 404     2408    861   1787    229   -105    257       C  
ATOM   1334  C   TRP A 404      54.181   3.411  24.465  1.00 12.68           C  
ANISOU 1334  C   TRP A 404     2383    748   1687      9   -258    -46       C  
ATOM   1335  O   TRP A 404      53.027   3.051  24.702  1.00 14.82           O  
ANISOU 1335  O   TRP A 404     2352   1238   2040    -38     11     -1       O  
ATOM   1336  CB  TRP A 404      55.263   1.179  24.108  1.00 15.89           C  
ANISOU 1336  CB  TRP A 404     2856   1025   2157    591    -30    265       C  
ATOM   1337  CG  TRP A 404      55.450   0.086  23.072  1.00 19.83           C  
ANISOU 1337  CG  TRP A 404     2956   1649   2930    332   -447    342       C  
ATOM   1338  CD1 TRP A 404      54.505  -0.796  22.622  1.00 18.71           C  
ANISOU 1338  CD1 TRP A 404     2882   1732   2496    588   -483    288       C  
ATOM   1339  CD2 TRP A 404      56.661  -0.239  22.380  1.00 17.97           C  
ANISOU 1339  CD2 TRP A 404     2643   1499   2685      3   -705    239       C  
ATOM   1340  NE1 TRP A 404      55.055  -1.647  21.692  1.00 20.03           N  
ANISOU 1340  NE1 TRP A 404     2570   2049   2992    180   -487   1001       N  
ATOM   1341  CE2 TRP A 404      56.375  -1.326  21.524  1.00 21.78           C  
ANISOU 1341  CE2 TRP A 404     2852   2262   3160    594   -216   1010       C  
ATOM   1342  CE3 TRP A 404      57.961   0.280  22.402  1.00 20.15           C  
ANISOU 1342  CE3 TRP A 404     2413   1782   3460   -127   -371    986       C  
ATOM   1343  CZ2 TRP A 404      57.338  -1.901  20.700  1.00 17.99           C  
ANISOU 1343  CZ2 TRP A 404     2691   1992   2150   1005     -6    766       C  
ATOM   1344  CZ3 TRP A 404      58.909  -0.285  21.580  1.00 20.88           C  
ANISOU 1344  CZ3 TRP A 404     2785   1711   3438    574   -638    148       C  
ATOM   1345  CH2 TRP A 404      58.593  -1.368  20.737  1.00 20.31           C  
ANISOU 1345  CH2 TRP A 404     2938   2008   2772    952   -238     78       C  
ATOM   1346  N   ALA A 405      54.702   4.516  24.999  1.00 13.20           N  
ANISOU 1346  N   ALA A 405     2371    933   1709    400   -226     46       N  
ATOM   1347  CA  ALA A 405      53.887   5.384  25.847  1.00 12.84           C  
ANISOU 1347  CA  ALA A 405     2242    925   1710    256   -152   -101       C  
ATOM   1348  C   ALA A 405      52.758   6.008  25.046  1.00 13.38           C  
ANISOU 1348  C   ALA A 405     2171   1158   1753    285    -97    173       C  
ATOM   1349  O   ALA A 405      52.959   6.434  23.909  1.00 14.01           O  
ANISOU 1349  O   ALA A 405     1993   1313   2017    307    -21    235       O  
ATOM   1350  CB  ALA A 405      54.737   6.477  26.477  1.00 14.70           C  
ANISOU 1350  CB  ALA A 405     2279   1120   2187    243   -322   -303       C  
ATOM   1351  N   VAL A 406      51.573   6.065  25.645  1.00 13.18           N  
ANISOU 1351  N   VAL A 406     1910   1152   1946    316    -10   -105       N  
ATOM   1352  CA  VAL A 406      50.436   6.731  25.025  1.00 12.92           C  
ANISOU 1352  CA  VAL A 406     1883   1184   1841    278    221    -47       C  
ATOM   1353  C   VAL A 406      50.375   8.164  25.538  1.00 13.15           C  
ANISOU 1353  C   VAL A 406     1984   1196   1817    299     82    160       C  
ATOM   1354  O   VAL A 406      50.349   8.389  26.747  1.00 14.71           O  
ANISOU 1354  O   VAL A 406     2268   1467   1854    523     -9     94       O  
ATOM   1355  CB  VAL A 406      49.111   6.014  25.355  1.00 14.24           C  
ANISOU 1355  CB  VAL A 406     2104   1134   2170    295    167   -132       C  
ATOM   1356  CG1 VAL A 406      47.956   6.696  24.644  1.00 16.07           C  
ANISOU 1356  CG1 VAL A 406     2078   1433   2594    275    142    -94       C  
ATOM   1357  CG2 VAL A 406      49.178   4.551  24.956  1.00 15.34           C  
ANISOU 1357  CG2 VAL A 406     2299   1247   2280    254    263   -115       C  
ATOM   1358  N   PRO A 407      50.367   9.146  24.621  1.00 12.18           N  
ANISOU 1358  N   PRO A 407     1846   1236   1545    156   -154   -142       N  
ATOM   1359  CA  PRO A 407      50.286  10.540  25.084  1.00 11.03           C  
ANISOU 1359  CA  PRO A 407     1726   1044   1422    215     77    -87       C  
ATOM   1360  C   PRO A 407      49.033  10.767  25.927  1.00 12.01           C  
ANISOU 1360  C   PRO A 407     1939   1096   1528    265   -135   -187       C  
ATOM   1361  O   PRO A 407      47.981  10.199  25.629  1.00 13.11           O  
ANISOU 1361  O   PRO A 407     1846   1347   1789    219    107   -147       O  
ATOM   1362  CB  PRO A 407      50.204  11.343  23.775  1.00 11.61           C  
ANISOU 1362  CB  PRO A 407     1845   1193   1374    282     41    208       C  
ATOM   1363  CG  PRO A 407      50.829  10.436  22.739  1.00 11.65           C  
ANISOU 1363  CG  PRO A 407     1598   1265   1561    411    116   -376       C  
ATOM   1364  CD  PRO A 407      50.420   9.046  23.153  1.00 10.91           C  
ANISOU 1364  CD  PRO A 407     1740    875   1529     65   -127    -35       C  
ATOM   1365  N   ASN A 408      49.144  11.601  26.959  1.00 12.40           N  
ANISOU 1365  N   ASN A 408     2078   1123   1508    469    147   -141       N  
ATOM   1366  CA  ASN A 408      47.994  11.968  27.780  1.00 13.25           C  
ANISOU 1366  CA  ASN A 408     2080   1549   1406    358    -48    -58       C  
ATOM   1367  C   ASN A 408      47.217  13.110  27.121  1.00 12.24           C  
ANISOU 1367  C   ASN A 408     1978   1269   1403    291    197     -6       C  
ATOM   1368  O   ASN A 408      47.264  14.260  27.566  1.00 13.36           O  
ANISOU 1368  O   ASN A 408     2021   1401   1654    252    146   -221       O  
ATOM   1369  CB  ASN A 408      48.457  12.356  29.183  1.00 15.03           C  
ANISOU 1369  CB  ASN A 408     2406   2097   1208    411   -142   -282       C  
ATOM   1370  CG  ASN A 408      47.317  12.464  30.159  1.00 21.54           C  
ANISOU 1370  CG  ASN A 408     3005   2879   2298    401   -350   -482       C  
ATOM   1371  OD1 ASN A 408      46.331  11.740  30.056  1.00 25.64           O  
ANISOU 1371  OD1 ASN A 408     3291   3151   3298    272    -54   -486       O  
ATOM   1372  ND2 ASN A 408      47.441  13.375  31.118  1.00 26.89           N  
ANISOU 1372  ND2 ASN A 408     3365   3416   3437    589   -370   -775       N  
ATOM   1373  N   TYR A 409      46.496  12.782  26.052  1.00 12.55           N  
ANISOU 1373  N   TYR A 409     1842   1389   1537    282      7     -3       N  
ATOM   1374  CA  TYR A 409      45.885  13.791  25.187  1.00 12.65           C  
ANISOU 1374  CA  TYR A 409     1824   1628   1352    403    108   -145       C  
ATOM   1375  C   TYR A 409      44.909  14.735  25.883  1.00 12.15           C  
ANISOU 1375  C   TYR A 409     1733   1645   1239    431    223    102       C  
ATOM   1376  O   TYR A 409      44.799  15.902  25.508  1.00 12.58           O  
ANISOU 1376  O   TYR A 409     1850   1481   1448    391     19    178       O  
ATOM   1377  CB  TYR A 409      45.141  13.119  24.038  1.00 13.46           C  
ANISOU 1377  CB  TYR A 409     1877   1764   1471    521     25   -268       C  
ATOM   1378  CG  TYR A 409      45.986  12.280  23.108  1.00 11.70           C  
ANISOU 1378  CG  TYR A 409     1680   1250   1513    297     49   -189       C  
ATOM   1379  CD1 TYR A 409      46.682  12.860  22.048  1.00 12.70           C  
ANISOU 1379  CD1 TYR A 409     1722   1481   1623    375     48   -225       C  
ATOM   1380  CD2 TYR A 409      46.039  10.902  23.254  1.00 12.02           C  
ANISOU 1380  CD2 TYR A 409     1592   1034   1941    102     62   -262       C  
ATOM   1381  CE1 TYR A 409      47.436  12.087  21.181  1.00 12.40           C  
ANISOU 1381  CE1 TYR A 409     1824   1142   1743    243   -227   -417       C  
ATOM   1382  CE2 TYR A 409      46.787  10.125  22.396  1.00 11.14           C  
ANISOU 1382  CE2 TYR A 409     1634   1137   1460    117    236   -109       C  
ATOM   1383  CZ  TYR A 409      47.478  10.716  21.363  1.00 11.20           C  
ANISOU 1383  CZ  TYR A 409     1672   1016   1565    197    210   -422       C  
ATOM   1384  OH  TYR A 409      48.204   9.921  20.517  1.00 11.32           O  
ANISOU 1384  OH  TYR A 409     1704    902   1695    144    112    -88       O  
ATOM   1385  N   GLY A 410      44.173  14.212  26.865  1.00 13.27           N  
ANISOU 1385  N   GLY A 410     1839   1617   1587    325    274   -100       N  
ATOM   1386  CA  GLY A 410      43.156  14.980  27.563  1.00 13.90           C  
ANISOU 1386  CA  GLY A 410     1754   1919   1607    486    302   -480       C  
ATOM   1387  C   GLY A 410      43.638  15.643  28.839  1.00 13.74           C  
ANISOU 1387  C   GLY A 410     1839   1805   1576    458    399    137       C  
ATOM   1388  O   GLY A 410      42.828  16.094  29.655  1.00 14.15           O  
ANISOU 1388  O   GLY A 410     1859   1907   1608    484    375     70       O  
ATOM   1389  N   SER A 411      44.954  15.716  29.017  1.00 14.22           N  
ANISOU 1389  N   SER A 411     1954   1834   1614    325    -59   -197       N  
ATOM   1390  CA  SER A 411      45.522  16.395  30.179  1.00 15.17           C  
ANISOU 1390  CA  SER A 411     2179   1871   1714    142    183     17       C  
ATOM   1391  C   SER A 411      44.922  15.813  31.469  1.00 15.50           C  
ANISOU 1391  C   SER A 411     2333   1997   1559    324     87   -253       C  
ATOM   1392  O   SER A 411      44.738  14.597  31.571  1.00 17.09           O  
ANISOU 1392  O   SER A 411     2691   1922   1878    395    358     78       O  
ATOM   1393  CB  SER A 411      45.293  17.908  30.064  1.00 16.09           C  
ANISOU 1393  CB  SER A 411     2421   1787   1905    -89    391   -160       C  
ATOM   1394  OG  SER A 411      45.859  18.621  31.150  1.00 17.24           O  
ANISOU 1394  OG  SER A 411     2608   2213   1729   -160    470   -488       O  
ATOM   1395  N   ASN A 412      44.610  16.661  32.448  1.00 16.05           N  
ANISOU 1395  N   ASN A 412     2239   2378   1482    400    253     58       N  
ATOM   1396  CA  ASN A 412      43.975  16.173  33.679  1.00 17.25           C  
ANISOU 1396  CA  ASN A 412     2419   2438   1696    342    172   -255       C  
ATOM   1397  C   ASN A 412      42.452  16.287  33.654  1.00 17.59           C  
ANISOU 1397  C   ASN A 412     2476   2733   1474    127    511     32       C  
ATOM   1398  O   ASN A 412      41.784  16.012  34.658  1.00 21.25           O  
ANISOU 1398  O   ASN A 412     2803   3553   1717    304    450    100       O  
ATOM   1399  CB  ASN A 412      44.524  16.892  34.917  1.00 18.37           C  
ANISOU 1399  CB  ASN A 412     2502   2507   1970    211     42     71       C  
ATOM   1400  CG  ASN A 412      46.010  16.649  35.126  1.00 19.88           C  
ANISOU 1400  CG  ASN A 412     2743   2484   2324    278   -139    207       C  
ATOM   1401  OD1 ASN A 412      46.560  15.644  34.674  1.00 22.39           O  
ANISOU 1401  OD1 ASN A 412     2911   2723   2874    464   -293    -95       O  
ATOM   1402  ND2 ASN A 412      46.670  17.575  35.814  1.00 21.30           N  
ANISOU 1402  ND2 ASN A 412     3078   2436   2580    422    -84     68       N  
ATOM   1403  N   LEU A 413      41.902  16.674  32.506  1.00 16.98           N  
ANISOU 1403  N   LEU A 413     2373   2424   1653    270    162     77       N  
ATOM   1404  CA  LEU A 413      40.465  16.938  32.402  1.00 17.89           C  
ANISOU 1404  CA  LEU A 413     2392   2380   2024    211    127    -97       C  
ATOM   1405  C   LEU A 413      39.654  15.682  32.119  1.00 17.56           C  
ANISOU 1405  C   LEU A 413     2566   2435   1672    152    337    -59       C  
ATOM   1406  O   LEU A 413      38.643  15.418  32.774  1.00 19.16           O  
ANISOU 1406  O   LEU A 413     2693   2576   2011    136    489    332       O  
ATOM   1407  CB  LEU A 413      40.178  17.992  31.329  1.00 17.94           C  
ANISOU 1407  CB  LEU A 413     2224   2399   2193    539    109     81       C  
ATOM   1408  CG  LEU A 413      38.695  18.295  31.087  1.00 19.42           C  
ANISOU 1408  CG  LEU A 413     2233   2506   2640    643    502    -31       C  
ATOM   1409  CD1 LEU A 413      38.029  18.855  32.351  1.00 22.19           C  
ANISOU 1409  CD1 LEU A 413     2476   2721   3234    802    793   -192       C  
ATOM   1410  CD2 LEU A 413      38.525  19.258  29.918  1.00 20.73           C  
ANISOU 1410  CD2 LEU A 413     2338   2535   3001    642    363    533       C  
ATOM   1411  N   THR A 414      40.093  14.909  31.136  1.00 16.63           N  
ANISOU 1411  N   THR A 414     2514   2167   1636   -133    279    -59       N  
ATOM   1412  CA  THR A 414      39.331  13.743  30.719  1.00 18.03           C  
ANISOU 1412  CA  THR A 414     2764   2354   1730   -241    289     12       C  
ATOM   1413  C   THR A 414      40.214  12.749  29.985  1.00 18.66           C  
ANISOU 1413  C   THR A 414     2997   2134   1957   -279    509     97       C  
ATOM   1414  O   THR A 414      41.263  13.109  29.449  1.00 18.75           O  
ANISOU 1414  O   THR A 414     2927   1993   2204   -126    582    154       O  
ATOM   1415  CB  THR A 414      38.179  14.159  29.793  1.00 20.29           C  
ANISOU 1415  CB  THR A 414     2994   2799   1915   -403    199    369       C  
ATOM   1416  OG1 THR A 414      37.364  13.020  29.496  1.00 24.32           O  
ANISOU 1416  OG1 THR A 414     3174   2957   3107   -501    344   -114       O  
ATOM   1417  CG2 THR A 414      38.723  14.748  28.498  1.00 21.82           C  
ANISOU 1417  CG2 THR A 414     3130   3141   2017    -85    250    196       C  
ATOM   1418  N   GLN A 415      39.806  11.488  29.968  1.00 20.43           N  
ANISOU 1418  N   GLN A 415     3331   2212   2219   -335    591     15       N  
ATOM   1419  CA  GLN A 415      40.443  10.542  29.070  1.00 22.61           C  
ANISOU 1419  CA  GLN A 415     3599   2458   2534   -333    760    227       C  
ATOM   1420  C   GLN A 415      39.953  10.871  27.671  1.00 21.78           C  
ANISOU 1420  C   GLN A 415     3147   2718   2411   -363    910   -181       C  
ATOM   1421  O   GLN A 415      38.748  10.989  27.438  1.00 23.89           O  
ANISOU 1421  O   GLN A 415     3092   3213   2770    -49    802   -625       O  
ATOM   1422  CB  GLN A 415      40.091   9.100  29.422  1.00 26.32           C  
ANISOU 1422  CB  GLN A 415     4402   2471   3127    132    948    603       C  
ATOM   1423  CG  GLN A 415      40.811   8.085  28.548  1.00 31.56           C  
ANISOU 1423  CG  GLN A 415     5102   2693   4196    625    926    692       C  
ATOM   1424  CD  GLN A 415      40.409   6.657  28.853  1.00 39.03           C  
ANISOU 1424  CD  GLN A 415     5680   3335   5814    971   1036    653       C  
ATOM   1425  OE1 GLN A 415      41.260   5.785  29.031  1.00 42.32           O  
ANISOU 1425  OE1 GLN A 415     6000   3615   6463   1266    989    764       O  
ATOM   1426  NE2 GLN A 415      39.106   6.408  28.908  1.00 42.18           N  
ANISOU 1426  NE2 GLN A 415     5909   3585   6531   1020    939    459       N  
ATOM   1427  N   ALA A 416      40.886  11.037  26.742  1.00 20.55           N  
ANISOU 1427  N   ALA A 416     2881   2755   2172   -146    608     13       N  
ATOM   1428  CA  ALA A 416      40.523  11.420  25.390  1.00 21.74           C  
ANISOU 1428  CA  ALA A 416     2630   3223   2405    -93    513   -512       C  
ATOM   1429  C   ALA A 416      39.538  10.414  24.824  1.00 24.68           C  
ANISOU 1429  C   ALA A 416     2540   3645   3193     61    289   -959       C  
ATOM   1430  O   ALA A 416      39.673   9.207  25.026  1.00 24.77           O  
ANISOU 1430  O   ALA A 416     2633   3715   3064    -55    475  -1122       O  
ATOM   1431  CB  ALA A 416      41.755  11.518  24.509  1.00 22.02           C  
ANISOU 1431  CB  ALA A 416     2607   3501   2257     66    844   -134       C  
ATOM   1432  N   SER A 417      38.526  10.912  24.127  1.00 25.89           N  
ANISOU 1432  N   SER A 417     2520   3810   3506    180     72  -1530       N  
ATOM   1433  CA  SER A 417      37.563  10.020  23.505  1.00 25.39           C  
ANISOU 1433  CA  SER A 417     2413   3459   3776    -57     89  -1286       C  
ATOM   1434  C   SER A 417      38.124   9.433  22.210  1.00 21.47           C  
ANISOU 1434  C   SER A 417     2095   2914   3147   -256    631   -647       C  
ATOM   1435  O   SER A 417      39.053   9.982  21.610  1.00 21.86           O  
ANISOU 1435  O   SER A 417     2270   2498   3537   -183    463   -592       O  
ATOM   1436  CB  SER A 417      36.231  10.734  23.260  1.00 27.39           C  
ANISOU 1436  CB  SER A 417     2632   3582   4192    -18    -60   -750       C  
ATOM   1437  OG  SER A 417      36.430  12.016  22.694  1.00 27.19           O  
ANISOU 1437  OG  SER A 417     2631   3488   4212   -388   -325    184       O  
ATOM   1438  N   GLN A 418      37.574   8.296  21.808  1.00 20.85           N  
ANISOU 1438  N   GLN A 418     2076   2525   3322   -181    278   -857       N  
ATOM   1439  CA  GLN A 418      37.932   7.671  20.541  1.00 18.81           C  
ANISOU 1439  CA  GLN A 418     2064   2548   2534    -57    773   -699       C  
ATOM   1440  C   GLN A 418      39.397   7.246  20.439  1.00 16.67           C  
ANISOU 1440  C   GLN A 418     1921   1990   2421   -257    409   -276       C  
ATOM   1441  O   GLN A 418      39.968   7.218  19.349  1.00 17.35           O  
ANISOU 1441  O   GLN A 418     2038   2293   2262   -179    657   -307       O  
ATOM   1442  CB  GLN A 418      37.557   8.592  19.376  1.00 24.13           C  
ANISOU 1442  CB  GLN A 418     2516   3470   3181    592    467   -597       C  
ATOM   1443  CG  GLN A 418      36.064   8.866  19.295  1.00 31.32           C  
ANISOU 1443  CG  GLN A 418     3055   4307   4536   1077    356   -477       C  
ATOM   1444  CD  GLN A 418      35.250   7.589  19.187  1.00 41.96           C  
ANISOU 1444  CD  GLN A 418     3818   5459   6666   1759    452   -468       C  
ATOM   1445  OE1 GLN A 418      35.565   6.703  18.392  1.00 45.40           O  
ANISOU 1445  OE1 GLN A 418     4301   5634   7316   1905    415   -490       O  
ATOM   1446  NE2 GLN A 418      34.202   7.485  19.996  1.00 45.80           N  
ANISOU 1446  NE2 GLN A 418     4103   5852   7447   1983    399   -470       N  
ATOM   1447  N   LEU A 419      40.002   6.903  21.571  1.00 16.60           N  
ANISOU 1447  N   LEU A 419     1886   2027   2394    -90    467    -95       N  
ATOM   1448  CA  LEU A 419      41.323   6.295  21.537  1.00 17.75           C  
ANISOU 1448  CA  LEU A 419     2171   2068   2506   -136    590   -315       C  
ATOM   1449  C   LEU A 419      41.231   4.936  20.857  1.00 18.65           C  
ANISOU 1449  C   LEU A 419     2218   1813   3055   -220   1048     50       C  
ATOM   1450  O   LEU A 419      40.323   4.147  21.131  1.00 21.46           O  
ANISOU 1450  O   LEU A 419     2292   1820   4040   -437   1225   -126       O  
ATOM   1451  CB  LEU A 419      41.883   6.109  22.945  1.00 17.84           C  
ANISOU 1451  CB  LEU A 419     2380   2268   2130   -322    504    121       C  
ATOM   1452  CG  LEU A 419      42.435   7.314  23.699  1.00 19.13           C  
ANISOU 1452  CG  LEU A 419     2814   2325   2127   -174    419   -265       C  
ATOM   1453  CD1 LEU A 419      42.640   6.950  25.163  1.00 20.66           C  
ANISOU 1453  CD1 LEU A 419     3136   2536   2178   -304    417    311       C  
ATOM   1454  CD2 LEU A 419      43.739   7.790  23.068  1.00 17.53           C  
ANISOU 1454  CD2 LEU A 419     2540   1982   2139   -359    429   -119       C  
ATOM   1455  N   ALA A 420      42.169   4.661  19.962  1.00 17.66           N  
ANISOU 1455  N   ALA A 420     2171   1716   2824   -119    848    -96       N  
ATOM   1456  CA  ALA A 420      42.304   3.322  19.428  1.00 16.66           C  
ANISOU 1456  CA  ALA A 420     2216   1570   2544    -54    792    -78       C  
ATOM   1457  C   ALA A 420      42.700   2.425  20.602  1.00 18.65           C  
ANISOU 1457  C   ALA A 420     2576   1588   2923   -278    942     32       C  
ATOM   1458  O   ALA A 420      43.487   2.832  21.451  1.00 17.96           O  
ANISOU 1458  O   ALA A 420     2533   1522   2770   -462    961    -21       O  
ATOM   1459  CB  ALA A 420      43.350   3.301  18.338  1.00 16.16           C  
ANISOU 1459  CB  ALA A 420     1947   1642   2550   -255    586     82       C  
ATOM   1460  N   PRO A 421      42.141   1.209  20.669  1.00 20.31           N  
ANISOU 1460  N   PRO A 421     2816   1554   3345   -481    968    -52       N  
ATOM   1461  CA  PRO A 421      42.356   0.359  21.846  1.00 20.45           C  
ANISOU 1461  CA  PRO A 421     3042   1746   2981   -499   1124    544       C  
ATOM   1462  C   PRO A 421      43.747  -0.269  21.928  1.00 19.07           C  
ANISOU 1462  C   PRO A 421     3232   1610   2403   -555    959    428       C  
ATOM   1463  O   PRO A 421      44.462  -0.339  20.926  1.00 17.69           O  
ANISOU 1463  O   PRO A 421     3170   1428   2122   -485    740    318       O  
ATOM   1464  CB  PRO A 421      41.302  -0.741  21.670  1.00 22.11           C  
ANISOU 1464  CB  PRO A 421     3202   1790   3409   -599   1279    390       C  
ATOM   1465  CG  PRO A 421      41.114  -0.839  20.197  1.00 23.76           C  
ANISOU 1465  CG  PRO A 421     3229   1818   3979   -602    892    125       C  
ATOM   1466  CD  PRO A 421      41.253   0.576  19.680  1.00 22.02           C  
ANISOU 1466  CD  PRO A 421     3040   1455   3870   -673    671   -157       C  
ATOM   1467  N   PRO A 422      44.135  -0.729  23.123  1.00 19.58           N  
ANISOU 1467  N   PRO A 422     3705   1784   1950   -395    878    195       N  
ATOM   1468  CA  PRO A 422      45.375  -1.497  23.276  1.00 19.56           C  
ANISOU 1468  CA  PRO A 422     3793   1753   1887   -442    327     -9       C  
ATOM   1469  C   PRO A 422      45.271  -2.814  22.511  1.00 18.95           C  
ANISOU 1469  C   PRO A 422     3628   1638   1935   -533    182     73       C  
ATOM   1470  O   PRO A 422      44.162  -3.327  22.343  1.00 19.78           O  
ANISOU 1470  O   PRO A 422     3546   1599   2369   -544    472   -104       O  
ATOM   1471  CB  PRO A 422      45.433  -1.781  24.786  1.00 22.16           C  
ANISOU 1471  CB  PRO A 422     4178   2134   2107   -106    159     87       C  
ATOM   1472  CG  PRO A 422      44.422  -0.878  25.405  1.00 24.71           C  
ANISOU 1472  CG  PRO A 422     4177   2922   2289     14    471    327       C  
ATOM   1473  CD  PRO A 422      43.370  -0.664  24.377  1.00 22.13           C  
ANISOU 1473  CD  PRO A 422     3973   2386   2050   -297    786     75       C  
ATOM   1474  N   ILE A 423      46.399  -3.347  22.051  1.00 17.76           N  
ANISOU 1474  N   ILE A 423     3416   1491   1840   -600     91   -183       N  
ATOM   1475  CA  ILE A 423      46.404  -4.637  21.360  1.00 16.98           C  
ANISOU 1475  CA  ILE A 423     3234   1375   1841   -676    -38    218       C  
ATOM   1476  C   ILE A 423      47.157  -5.707  22.140  1.00 18.52           C  
ANISOU 1476  C   ILE A 423     3477   1379   2180   -847   -190    388       C  
ATOM   1477  O   ILE A 423      48.257  -5.473  22.637  1.00 18.76           O  
ANISOU 1477  O   ILE A 423     3194   1542   2393   -890   -205    143       O  
ATOM   1478  CB  ILE A 423      47.031  -4.546  19.952  1.00 16.85           C  
ANISOU 1478  CB  ILE A 423     3069   1445   1886   -288    -79     31       C  
ATOM   1479  CG1 ILE A 423      46.369  -3.430  19.137  1.00 16.76           C  
ANISOU 1479  CG1 ILE A 423     2929   1649   1788   -295   -216    329       C  
ATOM   1480  CG2 ILE A 423      46.923  -5.898  19.244  1.00 17.78           C  
ANISOU 1480  CG2 ILE A 423     3077   1448   2231   -183   -369   -349       C  
ATOM   1481  CD1 ILE A 423      47.074  -3.127  17.833  1.00 17.75           C  
ANISOU 1481  CD1 ILE A 423     2804   2101   1837   -383      8    109       C  
ATOM   1482  N   TYR A 424      46.547  -6.887  22.227  1.00 23.77           N  
ANISOU 1482  N   TYR A 424     4114   1593   3324   -751    141    742       N  
ATOM   1483  CA  TYR A 424      47.150  -8.054  22.873  1.00 24.82           C  
ANISOU 1483  CA  TYR A 424     4357   1849   3223   -937    481    678       C  
ATOM   1484  C   TYR A 424      47.205  -9.220  21.901  1.00 26.39           C  
ANISOU 1484  C   TYR A 424     4526   1991   3511   -491    532    719       C  
ATOM   1485  O   TYR A 424      46.288  -9.406  21.097  1.00 27.56           O  
ANISOU 1485  O   TYR A 424     4757   2192   3520   -262    518    644       O  
ATOM   1486  CB  TYR A 424      46.339  -8.465  24.100  1.00 28.77           C  
ANISOU 1486  CB  TYR A 424     5453   2107   3370   -441    530    274       C  
ATOM   1487  CG  TYR A 424      46.172  -7.357  25.105  1.00 31.50           C  
ANISOU 1487  CG  TYR A 424     6079   2435   3452   -299    841    315       C  
ATOM   1488  CD1 TYR A 424      47.183  -7.055  26.009  1.00 33.15           C  
ANISOU 1488  CD1 TYR A 424     6378   2887   3328    -86   1070    214       C  
ATOM   1489  CD2 TYR A 424      45.008  -6.605  25.147  1.00 33.46           C  
ANISOU 1489  CD2 TYR A 424     6259   2890   3563   -115   1102    286       C  
ATOM   1490  CE1 TYR A 424      47.034  -6.036  26.927  1.00 33.22           C  
ANISOU 1490  CE1 TYR A 424     6560   2952   3109     57   1153   -289       C  
ATOM   1491  CE2 TYR A 424      44.853  -5.587  26.058  1.00 33.98           C  
ANISOU 1491  CE2 TYR A 424     6495   3001   3413    193   1277    203       C  
ATOM   1492  CZ  TYR A 424      45.867  -5.305  26.945  1.00 34.75           C  
ANISOU 1492  CZ  TYR A 424     6653   2996   3553    148   1207    -19       C  
ATOM   1493  OH  TYR A 424      45.710  -4.289  27.856  1.00 37.69           O  
ANISOU 1493  OH  TYR A 424     6869   3282   4170    329   1293     -6       O  
ATOM   1494  N   PRO A 425      48.277 -10.020  21.982  1.00 26.39           N  
ANISOU 1494  N   PRO A 425     4531   1694   3802   -625    162    290       N  
ATOM   1495  CA  PRO A 425      48.433 -11.186  21.106  1.00 27.49           C  
ANISOU 1495  CA  PRO A 425     4529   1845   4072   -574    175    -59       C  
ATOM   1496  C   PRO A 425      47.396 -12.258  21.447  1.00 23.91           C  
ANISOU 1496  C   PRO A 425     4384   2062   2637   -661    643    833       C  
ATOM   1497  O   PRO A 425      46.981 -12.368  22.600  1.00 24.62           O  
ANISOU 1497  O   PRO A 425     4341   2133   2881   -640    116    282       O  
ATOM   1498  CB  PRO A 425      49.850 -11.663  21.418  1.00 28.71           C  
ANISOU 1498  CB  PRO A 425     4435   1765   4709   -700    306   -174       C  
ATOM   1499  CG  PRO A 425      50.061 -11.258  22.838  1.00 31.21           C  
ANISOU 1499  CG  PRO A 425     4509   2120   5229   -390    179   -143       C  
ATOM   1500  CD  PRO A 425      49.341  -9.948  22.999  1.00 28.47           C  
ANISOU 1500  CD  PRO A 425     4451   1719   4645   -695    165   -242       C  
ATOM   1501  N   PRO A 426      46.967 -13.033  20.442  1.00 25.78           N  
ANISOU 1501  N   PRO A 426     4464   2551   2781   -609    726    235       N  
ATOM   1502  CA  PRO A 426      45.828 -13.954  20.573  1.00 27.83           C  
ANISOU 1502  CA  PRO A 426     4495   2886   3193   -582    558   -145       C  
ATOM   1503  C   PRO A 426      46.141 -15.330  21.164  1.00 29.57           C  
ANISOU 1503  C   PRO A 426     4473   3197   3563   -362    734   -160       C  
ATOM   1504  O   PRO A 426      45.219 -15.998  21.631  1.00 33.58           O  
ANISOU 1504  O   PRO A 426     4635   3386   4739   -219    623   -125       O  
ATOM   1505  CB  PRO A 426      45.352 -14.112  19.127  1.00 28.84           C  
ANISOU 1505  CB  PRO A 426     4587   3136   3233   -440    269   -585       C  
ATOM   1506  CG  PRO A 426      46.592 -13.933  18.316  1.00 29.51           C  
ANISOU 1506  CG  PRO A 426     4599   3219   3393   -407    484   -429       C  
ATOM   1507  CD  PRO A 426      47.424 -12.908  19.047  1.00 27.17           C  
ANISOU 1507  CD  PRO A 426     4585   2719   3017   -384    769     78       C  
ATOM   1508  N   GLY A 427      47.401 -15.751  21.141  1.00 29.28           N  
ANISOU 1508  N   GLY A 427     4455   3057   3613    -82    327   -345       N  
ATOM   1509  CA  GLY A 427      47.756 -17.095  21.568  1.00 27.03           C  
ANISOU 1509  CA  GLY A 427     4278   2713   3280   -154    152   -741       C  
ATOM   1510  C   GLY A 427      48.365 -17.895  20.431  1.00 23.58           C  
ANISOU 1510  C   GLY A 427     3995   2046   2918   -684   -153   -722       C  
ATOM   1511  O   GLY A 427      48.832 -17.323  19.450  1.00 23.37           O  
ANISOU 1511  O   GLY A 427     3889   2141   2849   -668    -54    -42       O  
ATOM   1512  N   PHE A 428      48.372 -19.219  20.563  1.00 21.51           N  
ANISOU 1512  N   PHE A 428     3942   1755   2475   -800    -69   -415       N  
ATOM   1513  CA  PHE A 428      48.895 -20.101  19.524  1.00 21.65           C  
ANISOU 1513  CA  PHE A 428     3794   2073   2357   -753   -125   -248       C  
ATOM   1514  C   PHE A 428      50.336 -19.779  19.152  1.00 20.83           C  
ANISOU 1514  C   PHE A 428     3794   1788   2333   -630   -509     75       C  
ATOM   1515  O   PHE A 428      50.767 -20.008  18.009  1.00 19.91           O  
ANISOU 1515  O   PHE A 428     3834   1431   2300   -664   -809     76       O  
ATOM   1516  CB  PHE A 428      47.987 -20.088  18.287  1.00 24.21           C  
ANISOU 1516  CB  PHE A 428     3634   2501   3063  -1184    166   -248       C  
ATOM   1517  CG  PHE A 428      46.532 -20.216  18.620  1.00 25.24           C  
ANISOU 1517  CG  PHE A 428     3561   2812   3216  -1467    170   -589       C  
ATOM   1518  CD1 PHE A 428      45.687 -19.124  18.527  1.00 25.69           C  
ANISOU 1518  CD1 PHE A 428     3592   3088   3079  -1472     80   -265       C  
ATOM   1519  CD2 PHE A 428      46.012 -21.425  19.054  1.00 29.07           C  
ANISOU 1519  CD2 PHE A 428     3578   3222   4243  -1251    289   -245       C  
ATOM   1520  CE1 PHE A 428      44.347 -19.233  18.842  1.00 26.19           C  
ANISOU 1520  CE1 PHE A 428     3630   3012   3310  -1537    319      4       C  
ATOM   1521  CE2 PHE A 428      44.673 -21.542  19.373  1.00 29.30           C  
ANISOU 1521  CE2 PHE A 428     3556   3272   4304  -1378    315   -216       C  
ATOM   1522  CZ  PHE A 428      43.840 -20.445  19.267  1.00 28.13           C  
ANISOU 1522  CZ  PHE A 428     3578   3191   3920  -1538    444   -156       C  
ATOM   1523  N   GLY A 429      51.079 -19.262  20.130  1.00 22.09           N  
ANISOU 1523  N   GLY A 429     3537   1427   3428   -654   -729    619       N  
ATOM   1524  CA  GLY A 429      52.489 -18.972  19.957  1.00 22.00           C  
ANISOU 1524  CA  GLY A 429     3253   1649   3458   -330  -1078    197       C  
ATOM   1525  C   GLY A 429      52.723 -17.655  19.251  1.00 18.85           C  
ANISOU 1525  C   GLY A 429     2771   1565   2826   -369  -1296     34       C  
ATOM   1526  O   GLY A 429      53.859 -17.312  18.927  1.00 19.85           O  
ANISOU 1526  O   GLY A 429     2934   1966   2643    -66  -1028     10       O  
ATOM   1527  N   GLU A 430      51.647 -16.910  19.019  1.00 16.21           N  
ANISOU 1527  N   GLU A 430     2492   1060   2607   -507   -638    372       N  
ATOM   1528  CA  GLU A 430      51.722 -15.724  18.175  1.00 14.54           C  
ANISOU 1528  CA  GLU A 430     2301    917   2306   -449   -553     19       C  
ATOM   1529  C   GLU A 430      52.229 -14.483  18.897  1.00 13.31           C  
ANISOU 1529  C   GLU A 430     2256    906   1894   -500   -408    -81       C  
ATOM   1530  O   GLU A 430      52.011 -14.290  20.098  1.00 16.60           O  
ANISOU 1530  O   GLU A 430     2755   1417   2136   -511    -49    -59       O  
ATOM   1531  CB  GLU A 430      50.377 -15.448  17.501  1.00 14.26           C  
ANISOU 1531  CB  GLU A 430     2089    932   2395   -456   -577    180       C  
ATOM   1532  CG  GLU A 430      49.959 -16.590  16.575  1.00 15.01           C  
ANISOU 1532  CG  GLU A 430     2039   1059   2603   -448   -529   -269       C  
ATOM   1533  CD  GLU A 430      48.578 -16.426  15.976  1.00 14.05           C  
ANISOU 1533  CD  GLU A 430     1979    904   2454   -505   -280    119       C  
ATOM   1534  OE1 GLU A 430      48.082 -15.284  15.872  1.00 16.09           O  
ANISOU 1534  OE1 GLU A 430     2058   1142   2912   -454   -330   -118       O  
ATOM   1535  OE2 GLU A 430      47.989 -17.463  15.600  1.00 14.80           O  
ANISOU 1535  OE2 GLU A 430     2176   1217   2231   -602   -492     62       O  
ATOM   1536  N   ALA A 431      52.917 -13.650  18.130  1.00 12.12           N  
ANISOU 1536  N   ALA A 431     1822    846   1937   -494   -371    171       N  
ATOM   1537  CA  ALA A 431      53.452 -12.385  18.622  1.00 11.80           C  
ANISOU 1537  CA  ALA A 431     1734    869   1881   -463   -529     78       C  
ATOM   1538  C   ALA A 431      53.104 -11.280  17.637  1.00 10.52           C  
ANISOU 1538  C   ALA A 431     1618    924   1453   -301   -564    240       C  
ATOM   1539  O   ALA A 431      53.127 -11.485  16.424  1.00 11.55           O  
ANISOU 1539  O   ALA A 431     1731    966   1689   -191   -524     34       O  
ATOM   1540  CB  ALA A 431      54.965 -12.483  18.797  1.00 12.96           C  
ANISOU 1540  CB  ALA A 431     1628   1166   2128   -263   -623    316       C  
ATOM   1541  N   ILE A 432      52.793 -10.102  18.166  1.00 11.45           N  
ANISOU 1541  N   ILE A 432     1615    740   1995   -146   -439     72       N  
ATOM   1542  CA  ILE A 432      52.498  -8.944  17.336  1.00 10.40           C  
ANISOU 1542  CA  ILE A 432     1567    722   1662    -65   -161    216       C  
ATOM   1543  C   ILE A 432      53.723  -8.549  16.515  1.00  9.54           C  
ANISOU 1543  C   ILE A 432     1494    808   1322    -28   -140    178       C  
ATOM   1544  O   ILE A 432      54.859  -8.533  17.023  1.00 11.48           O  
ANISOU 1544  O   ILE A 432     1433   1154   1773    -63   -455    211       O  
ATOM   1545  CB  ILE A 432      52.042  -7.760  18.208  1.00 10.61           C  
ANISOU 1545  CB  ILE A 432     1472    935   1622     28     79    201       C  
ATOM   1546  CG1 ILE A 432      50.737  -8.118  18.940  1.00 14.08           C  
ANISOU 1546  CG1 ILE A 432     1528   1558   2264    -16    346    -46       C  
ATOM   1547  CG2 ILE A 432      51.880  -6.495  17.381  1.00 12.03           C  
ANISOU 1547  CG2 ILE A 432     1669   1139   1761    144   -272    315       C  
ATOM   1548  CD1 ILE A 432      50.350  -7.145  20.025  1.00 15.50           C  
ANISOU 1548  CD1 ILE A 432     1939   1805   2144    184    530   -249       C  
ATOM   1549  N   VAL A 433      53.488  -8.246  15.241  1.00  9.52           N  
ANISOU 1549  N   VAL A 433     1478    796   1343   -234     47     86       N  
ATOM   1550  CA  VAL A 433      54.538  -7.788  14.340  1.00  9.53           C  
ANISOU 1550  CA  VAL A 433     1564    660   1396   -189    -80    -97       C  
ATOM   1551  C   VAL A 433      54.585  -6.267  14.279  1.00  9.94           C  
ANISOU 1551  C   VAL A 433     1461    669   1645   -152   -129    -13       C  
ATOM   1552  O   VAL A 433      53.558  -5.606  14.119  1.00 10.61           O  
ANISOU 1552  O   VAL A 433     1231    832   1968    -25   -192     91       O  
ATOM   1553  CB  VAL A 433      54.296  -8.342  12.919  1.00 10.72           C  
ANISOU 1553  CB  VAL A 433     1635   1036   1402   -277     44   -101       C  
ATOM   1554  CG1 VAL A 433      55.309  -7.770  11.932  1.00 12.07           C  
ANISOU 1554  CG1 VAL A 433     1634   1329   1622   -379     66   -184       C  
ATOM   1555  CG2 VAL A 433      54.343  -9.888  12.933  1.00 12.43           C  
ANISOU 1555  CG2 VAL A 433     2012    666   2044   -284    -47   -253       C  
ATOM   1556  N   TYR A 434      55.790  -5.729  14.417  1.00  8.99           N  
ANISOU 1556  N   TYR A 434     1324    534   1557   -263   -116    -85       N  
ATOM   1557  CA  TYR A 434      56.039  -4.293  14.266  1.00  8.89           C  
ANISOU 1557  CA  TYR A 434     1198    700   1479   -175   -144   -122       C  
ATOM   1558  C   TYR A 434      56.839  -4.026  13.009  1.00  8.97           C  
ANISOU 1558  C   TYR A 434     1301    644   1464     30    -99   -130       C  
ATOM   1559  O   TYR A 434      57.819  -4.718  12.717  1.00 10.36           O  
ANISOU 1559  O   TYR A 434     1274    902   1760    196    -19     12       O  
ATOM   1560  CB  TYR A 434      56.788  -3.749  15.483  1.00  9.78           C  
ANISOU 1560  CB  TYR A 434     1108   1094   1512   -191   -349   -284       C  
ATOM   1561  CG  TYR A 434      56.004  -3.934  16.748  1.00 10.48           C  
ANISOU 1561  CG  TYR A 434     1423   1275   1282    -90     62   -115       C  
ATOM   1562  CD1 TYR A 434      54.966  -3.070  17.065  1.00 12.73           C  
ANISOU 1562  CD1 TYR A 434     1692   1456   1689    180      9   -103       C  
ATOM   1563  CD2 TYR A 434      56.262  -5.003  17.598  1.00 11.50           C  
ANISOU 1563  CD2 TYR A 434     1603   1321   1446   -105   -241     33       C  
ATOM   1564  CE1 TYR A 434      54.229  -3.238  18.208  1.00 14.36           C  
ANISOU 1564  CE1 TYR A 434     2086   1852   1517    525    -41    392       C  
ATOM   1565  CE2 TYR A 434      55.532  -5.179  18.750  1.00 13.87           C  
ANISOU 1565  CE2 TYR A 434     1864   1911   1494    275   -150    137       C  
ATOM   1566  CZ  TYR A 434      54.517  -4.289  19.051  1.00 15.10           C  
ANISOU 1566  CZ  TYR A 434     1964   2167   1604    662     95    355       C  
ATOM   1567  OH  TYR A 434      53.776  -4.448  20.199  1.00 19.62           O  
ANISOU 1567  OH  TYR A 434     2572   2950   1933   1021    327    774       O  
ATOM   1568  N   PHE A 435      56.389  -3.038  12.249  1.00  9.28           N  
ANISOU 1568  N   PHE A 435     1280    693   1552    152   -174    156       N  
ATOM   1569  CA  PHE A 435      57.143  -2.540  11.120  1.00  9.37           C  
ANISOU 1569  CA  PHE A 435     1124    821   1614     64   -261    185       C  
ATOM   1570  C   PHE A 435      58.012  -1.413  11.630  1.00  9.83           C  
ANISOU 1570  C   PHE A 435     1134    756   1846   -149   -258    269       C  
ATOM   1571  O   PHE A 435      57.536  -0.545  12.361  1.00 11.28           O  
ANISOU 1571  O   PHE A 435     1403    929   1954    197     -1   -285       O  
ATOM   1572  CB  PHE A 435      56.172  -2.091  10.031  1.00  9.49           C  
ANISOU 1572  CB  PHE A 435     1266    627   1711    -34   -156   -244       C  
ATOM   1573  CG  PHE A 435      55.283  -3.202   9.569  1.00  8.90           C  
ANISOU 1573  CG  PHE A 435     1432    491   1459   -203   -121   -103       C  
ATOM   1574  CD1 PHE A 435      55.705  -4.062   8.566  1.00 10.85           C  
ANISOU 1574  CD1 PHE A 435     1864    663   1593    112   -267   -258       C  
ATOM   1575  CD2 PHE A 435      54.062  -3.432  10.183  1.00 10.80           C  
ANISOU 1575  CD2 PHE A 435     1412    858   1832   -285   -321    172       C  
ATOM   1576  CE1 PHE A 435      54.912  -5.122   8.174  1.00 12.69           C  
ANISOU 1576  CE1 PHE A 435     1903    849   2070   -273   -286   -310       C  
ATOM   1577  CE2 PHE A 435      53.263  -4.492   9.796  1.00 12.94           C  
ANISOU 1577  CE2 PHE A 435     1775   1038   2101   -112   -258   -138       C  
ATOM   1578  CZ  PHE A 435      53.682  -5.331   8.787  1.00 13.44           C  
ANISOU 1578  CZ  PHE A 435     1941   1051   2114   -354    109   -198       C  
ATOM   1579  N   THR A 436      59.289  -1.434  11.255  1.00  9.15           N  
ANISOU 1579  N   THR A 436     1148    632   1695    -76   -216    -24       N  
ATOM   1580  CA  THR A 436      60.271  -0.512  11.816  1.00  9.20           C  
ANISOU 1580  CA  THR A 436     1140    742   1611   -220   -200    -46       C  
ATOM   1581  C   THR A 436      60.796   0.467  10.794  1.00  9.42           C  
ANISOU 1581  C   THR A 436     1178    759   1641    -15     63    -88       C  
ATOM   1582  O   THR A 436      60.887   0.166   9.598  1.00 11.00           O  
ANISOU 1582  O   THR A 436     1449   1044   1686    -32     29   -228       O  
ATOM   1583  CB  THR A 436      61.496  -1.271  12.381  1.00 12.83           C  
ANISOU 1583  CB  THR A 436     1495   1253   2127    284   -365     75       C  
ATOM   1584  OG1 THR A 436      62.165  -1.964  11.319  1.00 15.81           O  
ANISOU 1584  OG1 THR A 436     1566   1361   3080    309   -689   -469       O  
ATOM   1585  CG2 THR A 436      61.067  -2.270  13.459  1.00 16.31           C  
ANISOU 1585  CG2 THR A 436     1948   1370   2880    -12  -1000    558       C  
ATOM   1586  N   SER A 437      61.157   1.655  11.289  1.00 10.09           N  
ANISOU 1586  N   SER A 437     1310    550   1974     43   -120    -96       N  
ATOM   1587  CA  SER A 437      61.936   2.616  10.520  1.00  9.73           C  
ANISOU 1587  CA  SER A 437     1094    672   1931   -104   -338     15       C  
ATOM   1588  C   SER A 437      63.046   3.178  11.382  1.00  9.12           C  
ANISOU 1588  C   SER A 437      872    822   1772   -178    140    101       C  
ATOM   1589  O   SER A 437      62.848   3.461  12.569  1.00 11.72           O  
ANISOU 1589  O   SER A 437     1302   1434   1715      7     36   -157       O  
ATOM   1590  CB  SER A 437      61.063   3.787  10.047  1.00 11.80           C  
ANISOU 1590  CB  SER A 437     1299    849   2333    322   -382      9       C  
ATOM   1591  OG  SER A 437      60.021   3.343   9.199  1.00 11.00           O  
ANISOU 1591  OG  SER A 437     1079   1011   2090     83   -296   -104       O  
ATOM   1592  N   THR A 438      64.206   3.378  10.772  1.00  9.83           N  
ANISOU 1592  N   THR A 438      939    604   2192     -6   -130    -90       N  
ATOM   1593  CA  THR A 438      65.259   4.132  11.432  1.00  9.83           C  
ANISOU 1593  CA  THR A 438      838    802   2096     72    -58   -233       C  
ATOM   1594  C   THR A 438      64.901   5.614  11.360  1.00 10.93           C  
ANISOU 1594  C   THR A 438     1245    911   1995    222   -137   -202       C  
ATOM   1595  O   THR A 438      64.600   6.144  10.291  1.00 11.30           O  
ANISOU 1595  O   THR A 438     1418    933   1942    174   -256   -165       O  
ATOM   1596  CB  THR A 438      66.622   3.865  10.790  1.00 11.99           C  
ANISOU 1596  CB  THR A 438      959    951   2645     -1    -96   -316       C  
ATOM   1597  OG1 THR A 438      66.953   2.480  10.974  1.00 13.91           O  
ANISOU 1597  OG1 THR A 438     1428   1142   2713    433   -129   -136       O  
ATOM   1598  CG2 THR A 438      67.688   4.716  11.445  1.00 13.06           C  
ANISOU 1598  CG2 THR A 438     1120   1209   2632   -179    -36   -237       C  
ATOM   1599  N   PHE A 439      64.906   6.264  12.515  1.00 10.73           N  
ANISOU 1599  N   PHE A 439     1233    769   2075    206    -70   -420       N  
ATOM   1600  CA  PHE A 439      64.401   7.624  12.645  1.00 10.59           C  
ANISOU 1600  CA  PHE A 439     1058    830   2134    117   -358   -522       C  
ATOM   1601  C   PHE A 439      65.070   8.221  13.878  1.00 11.29           C  
ANISOU 1601  C   PHE A 439     1168    948   2173     63   -257   -527       C  
ATOM   1602  O   PHE A 439      65.415   7.492  14.807  1.00 12.34           O  
ANISOU 1602  O   PHE A 439     1507   1103   2078    364   -205   -230       O  
ATOM   1603  CB  PHE A 439      62.878   7.583  12.825  1.00 10.57           C  
ANISOU 1603  CB  PHE A 439      965    740   2310    130   -102   -154       C  
ATOM   1604  CG  PHE A 439      62.251   8.935  13.033  1.00  8.82           C  
ANISOU 1604  CG  PHE A 439     1006    679   1665      3   -373   -114       C  
ATOM   1605  CD1 PHE A 439      61.786   9.674  11.957  1.00 10.86           C  
ANISOU 1605  CD1 PHE A 439      987    963   2175    203    -13    -82       C  
ATOM   1606  CD2 PHE A 439      62.122   9.457  14.306  1.00 10.52           C  
ANISOU 1606  CD2 PHE A 439     1076   1034   1888     46    -98   -570       C  
ATOM   1607  CE1 PHE A 439      61.217  10.922  12.153  1.00 11.55           C  
ANISOU 1607  CE1 PHE A 439     1000   1365   2022    285    129    113       C  
ATOM   1608  CE2 PHE A 439      61.551  10.696  14.513  1.00 11.67           C  
ANISOU 1608  CE2 PHE A 439     1131   1100   2201    175   -200   -225       C  
ATOM   1609  CZ  PHE A 439      61.101  11.432  13.433  1.00 12.39           C  
ANISOU 1609  CZ  PHE A 439     1195   1143   2370    204    108    -31       C  
ATOM   1610  N   PRO A 440      65.274   9.547  13.893  1.00 10.26           N  
ANISOU 1610  N   PRO A 440     1350    940   1606    131   -477   -463       N  
ATOM   1611  CA  PRO A 440      65.957  10.182  15.033  1.00 11.29           C  
ANISOU 1611  CA  PRO A 440     1499    888   1903    248    -15   -263       C  
ATOM   1612  C   PRO A 440      65.093  10.318  16.301  1.00 11.26           C  
ANISOU 1612  C   PRO A 440     1372    887   2020    194   -464   -527       C  
ATOM   1613  O   PRO A 440      64.898  11.426  16.820  1.00 11.97           O  
ANISOU 1613  O   PRO A 440     1370   1136   2040    255   -278   -214       O  
ATOM   1614  CB  PRO A 440      66.341  11.563  14.484  1.00 11.96           C  
ANISOU 1614  CB  PRO A 440     1589    781   2175    116    -75   -392       C  
ATOM   1615  CG  PRO A 440      65.282  11.839  13.459  1.00 11.03           C  
ANISOU 1615  CG  PRO A 440     1262   1192   1735    260   -578   -116       C  
ATOM   1616  CD  PRO A 440      65.066  10.495  12.785  1.00 10.78           C  
ANISOU 1616  CD  PRO A 440     1453    845   1799    305   -325   -148       C  
ATOM   1617  N   THR A 441      64.576   9.189  16.777  1.00 10.63           N  
ANISOU 1617  N   THR A 441     1375   1170   1492    144   -247    -69       N  
ATOM   1618  CA  THR A 441      64.127   9.066  18.157  1.00 11.18           C  
ANISOU 1618  CA  THR A 441     1263   1031   1954    142   -372     -4       C  
ATOM   1619  C   THR A 441      65.400   8.768  18.954  1.00 11.30           C  
ANISOU 1619  C   THR A 441     1680    912   1702    378   -369   -274       C  
ATOM   1620  O   THR A 441      65.824   7.608  19.099  1.00 12.61           O  
ANISOU 1620  O   THR A 441     1679   1037   2073    391   -376   -209       O  
ATOM   1621  CB  THR A 441      63.072   7.949  18.328  1.00 11.33           C  
ANISOU 1621  CB  THR A 441     1140   1097   2069    251   -118   -210       C  
ATOM   1622  OG1 THR A 441      63.352   6.890  17.410  1.00 12.46           O  
ANISOU 1622  OG1 THR A 441     1456   1202   2077    350    -79   -536       O  
ATOM   1623  CG2 THR A 441      61.647   8.478  18.058  1.00 11.98           C  
ANISOU 1623  CG2 THR A 441      992   1275   2285    372   -172   -140       C  
ATOM   1624  N   VAL A 442      66.045   9.831  19.418  1.00 11.62           N  
ANISOU 1624  N   VAL A 442     1478   1210   1727    488   -528   -354       N  
ATOM   1625  CA  VAL A 442      67.388   9.722  19.976  1.00 13.25           C  
ANISOU 1625  CA  VAL A 442     1522   1361   2149    413   -761   -296       C  
ATOM   1626  C   VAL A 442      67.383   8.885  21.252  1.00 13.76           C  
ANISOU 1626  C   VAL A 442     1651   1805   1770    392   -702     78       C  
ATOM   1627  O   VAL A 442      66.556   9.097  22.141  1.00 16.31           O  
ANISOU 1627  O   VAL A 442     1850   2225   2120    539   -408   -130       O  
ATOM   1628  CB  VAL A 442      67.993  11.122  20.185  1.00 12.83           C  
ANISOU 1628  CB  VAL A 442     1386   1463   2027    182   -905   -297       C  
ATOM   1629  CG1 VAL A 442      69.334  11.051  20.907  1.00 14.99           C  
ANISOU 1629  CG1 VAL A 442     1476   1771   2446    279   -973   -545       C  
ATOM   1630  CG2 VAL A 442      68.141  11.820  18.837  1.00 14.18           C  
ANISOU 1630  CG2 VAL A 442     1641   1481   2265    507   -715      1       C  
ATOM   1631  N   SER A 443      68.318   7.932  21.305  1.00 14.46           N  
ANISOU 1631  N   SER A 443     1575   1608   2312    401   -849    149       N  
ATOM   1632  CA  SER A 443      68.435   6.871  22.326  1.00 15.08           C  
ANISOU 1632  CA  SER A 443     2035   1835   1860    404   -527    238       C  
ATOM   1633  C   SER A 443      67.699   5.568  21.980  1.00 16.99           C  
ANISOU 1633  C   SER A 443     2355   1667   2431    214   -699   -242       C  
ATOM   1634  O   SER A 443      67.957   4.524  22.584  1.00 20.40           O  
ANISOU 1634  O   SER A 443     2914   1969   2869    481   -777    363       O  
ATOM   1635  CB  SER A 443      68.105   7.341  23.755  1.00 16.35           C  
ANISOU 1635  CB  SER A 443     2109   2401   1703    699   -376     79       C  
ATOM   1636  OG  SER A 443      66.712   7.298  24.026  1.00 17.97           O  
ANISOU 1636  OG  SER A 443     2065   2597   2166    698   -218    148       O  
ATOM   1637  N   ASN A 444      66.798   5.628  20.999  1.00 16.40           N  
ANISOU 1637  N   ASN A 444     2398   1739   2094    422   -689   -134       N  
ATOM   1638  CA  ASN A 444      66.142   4.428  20.481  1.00 15.60           C  
ANISOU 1638  CA  ASN A 444     2308   1766   1851     61   -343    142       C  
ATOM   1639  C   ASN A 444      65.648   4.687  19.067  1.00 13.49           C  
ANISOU 1639  C   ASN A 444     1893   1483   1749    126   -441     38       C  
ATOM   1640  O   ASN A 444      64.450   4.877  18.844  1.00 13.89           O  
ANISOU 1640  O   ASN A 444     1630   1469   2179    -69   -298     66       O  
ATOM   1641  CB  ASN A 444      64.974   4.005  21.370  1.00 18.88           C  
ANISOU 1641  CB  ASN A 444     2789   1963   2421    -50   -330    330       C  
ATOM   1642  CG  ASN A 444      64.535   2.575  21.105  1.00 22.68           C  
ANISOU 1642  CG  ASN A 444     3363   2166   3087   -115    242    578       C  
ATOM   1643  OD1 ASN A 444      64.796   2.025  20.036  1.00 25.09           O  
ANISOU 1643  OD1 ASN A 444     3442   2182   3908   -391   -305    265       O  
ATOM   1644  ND2 ASN A 444      63.871   1.966  22.079  1.00 27.91           N  
ANISOU 1644  ND2 ASN A 444     3784   2672   4149    114    610    213       N  
ATOM   1645  N   PRO A 445      66.580   4.711  18.104  1.00 12.61           N  
ANISOU 1645  N   PRO A 445     1501   1265   2025    204   -351     36       N  
ATOM   1646  CA  PRO A 445      66.280   5.201  16.755  1.00 12.11           C  
ANISOU 1646  CA  PRO A 445     1588   1242   1771    274    -35    136       C  
ATOM   1647  C   PRO A 445      65.636   4.144  15.860  1.00 12.27           C  
ANISOU 1647  C   PRO A 445     1683   1179   1801    240   -321     72       C  
ATOM   1648  O   PRO A 445      65.979   4.019  14.685  1.00 14.61           O  
ANISOU 1648  O   PRO A 445     1830   1606   2115    -56    -98    106       O  
ATOM   1649  CB  PRO A 445      67.656   5.610  16.224  1.00 13.26           C  
ANISOU 1649  CB  PRO A 445     1295   1246   2495    374      8     12       C  
ATOM   1650  CG  PRO A 445      68.601   4.675  16.922  1.00 13.20           C  
ANISOU 1650  CG  PRO A 445     1429   1180   2406    481   -329    218       C  
ATOM   1651  CD  PRO A 445      68.022   4.489  18.310  1.00 13.22           C  
ANISOU 1651  CD  PRO A 445     1440   1576   2006    365   -428     83       C  
ATOM   1652  N   LYS A 446      64.686   3.406  16.420  1.00 12.17           N  
ANISOU 1652  N   LYS A 446     1326   1141   2155   -132   -273     76       N  
ATOM   1653  CA  LYS A 446      63.957   2.399  15.665  1.00 11.30           C  
ANISOU 1653  CA  LYS A 446     1287   1072   1932    249   -476    122       C  
ATOM   1654  C   LYS A 446      62.485   2.531  16.034  1.00 11.63           C  
ANISOU 1654  C   LYS A 446     1189   1088   2141    131   -290    169       C  
ATOM   1655  O   LYS A 446      62.065   2.089  17.102  1.00 14.29           O  
ANISOU 1655  O   LYS A 446     1447   1669   2314    291   -151    324       O  
ATOM   1656  CB  LYS A 446      64.491   0.993  15.987  1.00 12.98           C  
ANISOU 1656  CB  LYS A 446     1571   1261   2100    121   -521   -141       C  
ATOM   1657  CG  LYS A 446      63.813  -0.144  15.210  1.00 15.72           C  
ANISOU 1657  CG  LYS A 446     1980   1317   2675    248   -464   -142       C  
ATOM   1658  CD  LYS A 446      64.404  -1.515  15.557  1.00 18.66           C  
ANISOU 1658  CD  LYS A 446     2295   1607   3188    229   -441    -78       C  
ATOM   1659  CE  LYS A 446      65.837  -1.652  15.065  1.00 19.88           C  
ANISOU 1659  CE  LYS A 446     2736   2264   2552    701   -799    -36       C  
ATOM   1660  NZ  LYS A 446      65.926  -1.937  13.600  1.00 23.16           N  
ANISOU 1660  NZ  LYS A 446     2972   2571   3257    717   -738    -96       N  
ATOM   1661  N   VAL A 447      61.711   3.169  15.159  1.00 10.40           N  
ANISOU 1661  N   VAL A 447     1124   1018   1807    152   -323   -188       N  
ATOM   1662  CA  VAL A 447      60.304   3.438  15.442  1.00 10.47           C  
ANISOU 1662  CA  VAL A 447     1207    936   1835     87   -116     67       C  
ATOM   1663  C   VAL A 447      59.429   2.276  14.988  1.00 10.02           C  
ANISOU 1663  C   VAL A 447     1292    776   1738     29   -146    -95       C  
ATOM   1664  O   VAL A 447      59.421   1.926  13.810  1.00 10.09           O  
ANISOU 1664  O   VAL A 447     1417    807   1610    191   -132    -90       O  
ATOM   1665  CB  VAL A 447      59.825   4.730  14.752  1.00 10.18           C  
ANISOU 1665  CB  VAL A 447     1257    896   1716    -48   -367    -68       C  
ATOM   1666  CG1 VAL A 447      58.303   4.892  14.894  1.00 10.97           C  
ANISOU 1666  CG1 VAL A 447     1063   1154   1949     64   -130    -61       C  
ATOM   1667  CG2 VAL A 447      60.563   5.940  15.318  1.00 10.67           C  
ANISOU 1667  CG2 VAL A 447     1606    755   1691   -171   -339   -217       C  
ATOM   1668  N   PRO A 448      58.713   1.654  15.937  1.00  9.90           N  
ANISOU 1668  N   PRO A 448     1526    796   1437     91   -328   -252       N  
ATOM   1669  CA  PRO A 448      57.812   0.538  15.631  1.00  9.81           C  
ANISOU 1669  CA  PRO A 448     1281    724   1720    -19   -445     46       C  
ATOM   1670  C   PRO A 448      56.393   1.037  15.355  1.00  9.11           C  
ANISOU 1670  C   PRO A 448     1217    635   1610     70   -149     -7       C  
ATOM   1671  O   PRO A 448      55.938   1.980  16.007  1.00 10.69           O  
ANISOU 1671  O   PRO A 448     1426    849   1786    114    -27   -184       O  
ATOM   1672  CB  PRO A 448      57.829  -0.262  16.927  1.00 11.25           C  
ANISOU 1672  CB  PRO A 448     1707    957   1608    165   -115     60       C  
ATOM   1673  CG  PRO A 448      57.927   0.815  17.990  1.00 11.93           C  
ANISOU 1673  CG  PRO A 448     1712    768   2052   -221   -220   -360       C  
ATOM   1674  CD  PRO A 448      58.797   1.914  17.388  1.00 11.04           C  
ANISOU 1674  CD  PRO A 448     1724    765   1705   -311    -97    -24       C  
ATOM   1675  N   CYS A 449      55.710   0.416  14.395  1.00  9.31           N  
ANISOU 1675  N   CYS A 449     1126    893   1519   -133   -305     11       N  
ATOM   1676  CA  CYS A 449      54.297   0.681  14.148  1.00  9.60           C  
ANISOU 1676  CA  CYS A 449     1233    842   1572      0   -243     -2       C  
ATOM   1677  C   CYS A 449      53.603  -0.648  13.829  1.00  9.06           C  
ANISOU 1677  C   CYS A 449     1252    658   1530   -197      5   -191       C  
ATOM   1678  O   CYS A 449      54.268  -1.644  13.534  1.00  9.54           O  
ANISOU 1678  O   CYS A 449     1323    634   1668      9     96    -40       O  
ATOM   1679  CB  CYS A 449      54.107   1.701  13.016  1.00 10.87           C  
ANISOU 1679  CB  CYS A 449     1522    999   1608     63   -101    -32       C  
ATOM   1680  SG  CYS A 449      54.492   1.084  11.374  1.00 10.06           S  
ANISOU 1680  SG  CYS A 449     1504    642   1674     52    -60    -37       S  
ATOM   1681  N   THR A 450      52.280  -0.681  13.919  1.00  9.78           N  
ANISOU 1681  N   THR A 450     1287    730   1700   -307    -71    160       N  
ATOM   1682  CA  THR A 450      51.566  -1.942  13.735  1.00 10.01           C  
ANISOU 1682  CA  THR A 450     1322    896   1584   -195    -25    211       C  
ATOM   1683  C   THR A 450      51.004  -2.152  12.321  1.00  9.88           C  
ANISOU 1683  C   THR A 450     1382   1007   1363   -125   -141    403       C  
ATOM   1684  O   THR A 450      50.569  -3.249  11.983  1.00 12.10           O  
ANISOU 1684  O   THR A 450     1714    893   1989   -228   -305    228       O  
ATOM   1685  CB  THR A 450      50.495  -2.166  14.830  1.00 12.21           C  
ANISOU 1685  CB  THR A 450     1553   1108   1977    -38    273    124       C  
ATOM   1686  OG1 THR A 450      49.806  -0.937  15.100  1.00 14.18           O  
ANISOU 1686  OG1 THR A 450     1611   1159   2618    -51    473    -71       O  
ATOM   1687  CG2 THR A 450      51.151  -2.660  16.129  1.00 13.27           C  
ANISOU 1687  CG2 THR A 450     2065   1274   1704    129     53    254       C  
ATOM   1688  N   LEU A 451      51.029  -1.108  11.492  1.00 10.23           N  
ANISOU 1688  N   LEU A 451     1469   1161   1257    154      0    161       N  
ATOM   1689  CA  LEU A 451      50.705  -1.255  10.066  1.00 10.75           C  
ANISOU 1689  CA  LEU A 451     1240   1119   1724    200     41    400       C  
ATOM   1690  C   LEU A 451      51.470  -0.246   9.217  1.00 10.21           C  
ANISOU 1690  C   LEU A 451     1513   1071   1294    119      9    312       C  
ATOM   1691  O   LEU A 451      51.642   0.903   9.624  1.00 11.75           O  
ANISOU 1691  O   LEU A 451     1755    875   1834     55   -182    -96       O  
ATOM   1692  CB  LEU A 451      49.215  -1.018   9.803  1.00 12.86           C  
ANISOU 1692  CB  LEU A 451     1350   1339   2197    206   -194     21       C  
ATOM   1693  CG  LEU A 451      48.153  -2.037  10.194  1.00 13.99           C  
ANISOU 1693  CG  LEU A 451     1449   1259   2606    -97   -133     39       C  
ATOM   1694  CD1 LEU A 451      46.754  -1.467   9.927  1.00 14.14           C  
ANISOU 1694  CD1 LEU A 451     1359   1566   2448    -47   -204    163       C  
ATOM   1695  CD2 LEU A 451      48.372  -3.360   9.450  1.00 13.37           C  
ANISOU 1695  CD2 LEU A 451     1618    995   2467   -229   -190   -388       C  
ATOM   1696  N   PRO A 452      51.886  -0.656   8.008  1.00 10.26           N  
ANISOU 1696  N   PRO A 452     1569    673   1656    173    -48     14       N  
ATOM   1697  CA  PRO A 452      52.388   0.325   7.040  1.00 10.04           C  
ANISOU 1697  CA  PRO A 452     1535    728   1550    252    -12    225       C  
ATOM   1698  C   PRO A 452      51.281   1.320   6.691  1.00  9.07           C  
ANISOU 1698  C   PRO A 452     1302    611   1532    -49   -307     88       C  
ATOM   1699  O   PRO A 452      50.104   0.939   6.630  1.00  9.98           O  
ANISOU 1699  O   PRO A 452     1453    737   1602   -129   -136      9       O  
ATOM   1700  CB  PRO A 452      52.719  -0.528   5.810  1.00 11.98           C  
ANISOU 1700  CB  PRO A 452     1775    847   1931    496    248    131       C  
ATOM   1701  CG  PRO A 452      52.871  -1.935   6.345  1.00 13.28           C  
ANISOU 1701  CG  PRO A 452     1842   1021   2181    364    293    259       C  
ATOM   1702  CD  PRO A 452      51.870  -2.024   7.458  1.00 12.14           C  
ANISOU 1702  CD  PRO A 452     1668   1057   1888    134    479    -74       C  
ATOM   1703  N   GLN A 453      51.644   2.575   6.459  1.00  9.21           N  
ANISOU 1703  N   GLN A 453     1281    551   1668     84    -20    101       N  
ATOM   1704  CA  GLN A 453      50.629   3.571   6.151  1.00  9.19           C  
ANISOU 1704  CA  GLN A 453     1403    521   1566     94   -164    161       C  
ATOM   1705  C   GLN A 453      49.815   3.189   4.910  1.00  9.68           C  
ANISOU 1705  C   GLN A 453     1386    815   1478    140     21    -66       C  
ATOM   1706  O   GLN A 453      48.606   3.410   4.847  1.00  9.65           O  
ANISOU 1706  O   GLN A 453     1071    841   1754      4    -51     78       O  
ATOM   1707  CB  GLN A 453      51.255   4.947   5.949  1.00  9.96           C  
ANISOU 1707  CB  GLN A 453     1475    570   1738     75    127    220       C  
ATOM   1708  CG  GLN A 453      50.213   6.033   5.702  1.00  9.22           C  
ANISOU 1708  CG  GLN A 453     1316    748   1439    353    -92     18       C  
ATOM   1709  CD  GLN A 453      49.250   6.177   6.867  1.00 10.26           C  
ANISOU 1709  CD  GLN A 453     1484    932   1480    294   -372     23       C  
ATOM   1710  OE1 GLN A 453      49.602   5.896   8.012  1.00 10.65           O  
ANISOU 1710  OE1 GLN A 453     1341   1042   1664    285   -100    -80       O  
ATOM   1711  NE2 GLN A 453      48.028   6.634   6.583  1.00 11.19           N  
ANISOU 1711  NE2 GLN A 453     1422    919   1910    138   -301    -78       N  
ATOM   1712  N   GLU A 454      50.474   2.611   3.914  1.00  9.20           N  
ANISOU 1712  N   GLU A 454     1418    783   1294    -90   -201   -100       N  
ATOM   1713  CA  GLU A 454      49.766   2.300   2.684  1.00 10.00           C  
ANISOU 1713  CA  GLU A 454     1430   1091   1279   -282    245    -18       C  
ATOM   1714  C   GLU A 454      48.774   1.143   2.877  1.00  9.50           C  
ANISOU 1714  C   GLU A 454     1352    753   1502   -357    247     75       C  
ATOM   1715  O   GLU A 454      47.837   1.008   2.101  1.00 10.87           O  
ANISOU 1715  O   GLU A 454     1313   1068   1747   -188   -183   -127       O  
ATOM   1716  CB  GLU A 454      50.728   2.066   1.520  1.00 10.78           C  
ANISOU 1716  CB  GLU A 454     1484   1272   1338   -441    184   -176       C  
ATOM   1717  CG  GLU A 454      51.392   3.348   0.996  1.00 11.99           C  
ANISOU 1717  CG  GLU A 454     1244   1454   1857   -561     23     57       C  
ATOM   1718  CD  GLU A 454      52.561   3.829   1.855  1.00 11.57           C  
ANISOU 1718  CD  GLU A 454     1430   1046   1918   -228    181     12       C  
ATOM   1719  OE1 GLU A 454      53.088   4.933   1.571  1.00 12.08           O  
ANISOU 1719  OE1 GLU A 454     1304   1253   2031   -276     39    225       O  
ATOM   1720  OE2 GLU A 454      52.963   3.117   2.808  1.00 11.23           O  
ANISOU 1720  OE2 GLU A 454     1167   1415   1683     -5     66    228       O  
ATOM   1721  N   PHE A 455      48.957   0.327   3.917  1.00  9.90           N  
ANISOU 1721  N   PHE A 455     1293    753   1713   -191    256     99       N  
ATOM   1722  CA  PHE A 455      47.904  -0.634   4.271  1.00 10.30           C  
ANISOU 1722  CA  PHE A 455     1334    695   1885    -69    122    232       C  
ATOM   1723  C   PHE A 455      46.667   0.125   4.745  1.00  9.85           C  
ANISOU 1723  C   PHE A 455     1384    647   1712    -64     55   -114       C  
ATOM   1724  O   PHE A 455      45.537  -0.248   4.418  1.00 11.66           O  
ANISOU 1724  O   PHE A 455     1426   1077   1928   -188    -59   -121       O  
ATOM   1725  CB  PHE A 455      48.339  -1.580   5.398  1.00 10.55           C  
ANISOU 1725  CB  PHE A 455     1627    700   1680     85     31    140       C  
ATOM   1726  CG  PHE A 455      49.053  -2.823   4.933  1.00 11.08           C  
ANISOU 1726  CG  PHE A 455     1552    710   1949   -258    -65     68       C  
ATOM   1727  CD1 PHE A 455      50.140  -2.749   4.074  1.00 13.36           C  
ANISOU 1727  CD1 PHE A 455     1559   1037   2481    -77    432   -328       C  
ATOM   1728  CD2 PHE A 455      48.670  -4.067   5.413  1.00 11.73           C  
ANISOU 1728  CD2 PHE A 455     1700    685   2070    -39   -187   -108       C  
ATOM   1729  CE1 PHE A 455      50.809  -3.900   3.678  1.00 15.09           C  
ANISOU 1729  CE1 PHE A 455     1744   1029   2960   -322    155   -228       C  
ATOM   1730  CE2 PHE A 455      49.340  -5.224   5.021  1.00 13.17           C  
ANISOU 1730  CE2 PHE A 455     1820    843   2340    -31   -301    -85       C  
ATOM   1731  CZ  PHE A 455      50.402  -5.139   4.154  1.00 14.84           C  
ANISOU 1731  CZ  PHE A 455     1615   1374   2648   -153   -327   -460       C  
ATOM   1732  N   VAL A 456      46.877   1.169   5.542  1.00 10.10           N  
ANISOU 1732  N   VAL A 456     1222    787   1827    -31    112   -122       N  
ATOM   1733  CA  VAL A 456      45.753   1.946   6.063  1.00 11.47           C  
ANISOU 1733  CA  VAL A 456     1482   1035   1839    107    306   -428       C  
ATOM   1734  C   VAL A 456      44.922   2.532   4.918  1.00 11.99           C  
ANISOU 1734  C   VAL A 456     1503   1101   1952    -12     32    -38       C  
ATOM   1735  O   VAL A 456      43.698   2.353   4.864  1.00 12.80           O  
ANISOU 1735  O   VAL A 456     1325   1521   2016   -187     11   -229       O  
ATOM   1736  CB  VAL A 456      46.217   3.083   7.012  1.00 11.09           C  
ANISOU 1736  CB  VAL A 456     1388   1126   1699     50    136    -81       C  
ATOM   1737  CG1 VAL A 456      45.021   3.918   7.466  1.00 13.06           C  
ANISOU 1737  CG1 VAL A 456     1445   1315   2200    309    107   -506       C  
ATOM   1738  CG2 VAL A 456      46.972   2.512   8.206  1.00 12.91           C  
ANISOU 1738  CG2 VAL A 456     1412   1442   2052   -123   -158    -81       C  
ATOM   1739  N   SER A 457      45.574   3.242   3.999  1.00 11.47           N  
ANISOU 1739  N   SER A 457     1494   1096   1768   -150    -57    -48       N  
ATOM   1740  CA  SER A 457      44.833   3.861   2.900  1.00 12.04           C  
ANISOU 1740  CA  SER A 457     1601   1184   1790    -34   -230    111       C  
ATOM   1741  C   SER A 457      44.195   2.796   2.012  1.00 11.74           C  
ANISOU 1741  C   SER A 457     1455   1082   1922   -162   -268    -34       C  
ATOM   1742  O   SER A 457      43.110   3.001   1.472  1.00 14.43           O  
ANISOU 1742  O   SER A 457     1450   1358   2674   -110   -496     40       O  
ATOM   1743  CB  SER A 457      45.710   4.814   2.086  1.00 13.62           C  
ANISOU 1743  CB  SER A 457     1495   1175   2504   -130     16    277       C  
ATOM   1744  OG  SER A 457      46.907   4.196   1.666  1.00 13.06           O  
ANISOU 1744  OG  SER A 457     1591   1226   2145     92     12    221       O  
ATOM   1745  N   HIS A 458      44.859   1.651   1.884  1.00 11.20           N  
ANISOU 1745  N   HIS A 458     1549    920   1786   -184   -242    -66       N  
ATOM   1746  CA  HIS A 458      44.309   0.551   1.104  1.00 11.46           C  
ANISOU 1746  CA  HIS A 458     1438   1088   1829   -243    100     85       C  
ATOM   1747  C   HIS A 458      42.975   0.091   1.690  1.00 11.48           C  
ANISOU 1747  C   HIS A 458     1326   1279   1758   -403   -253    -14       C  
ATOM   1748  O   HIS A 458      41.988  -0.047   0.967  1.00 12.82           O  
ANISOU 1748  O   HIS A 458     1498   1364   2007   -290   -441    181       O  
ATOM   1749  CB  HIS A 458      45.297  -0.611   1.043  1.00 11.80           C  
ANISOU 1749  CB  HIS A 458     1626    977   1878   -197   -211   -304       C  
ATOM   1750  CG  HIS A 458      44.900  -1.689   0.085  1.00 12.94           C  
ANISOU 1750  CG  HIS A 458     2006   1230   1681   -256   -134     57       C  
ATOM   1751  ND1 HIS A 458      45.038  -1.556  -1.281  1.00 16.99           N  
ANISOU 1751  ND1 HIS A 458     2879   1414   2160   -176     58   -254       N  
ATOM   1752  CD2 HIS A 458      44.375  -2.922   0.292  1.00 13.37           C  
ANISOU 1752  CD2 HIS A 458     1874   1261   1945   -345   -366     39       C  
ATOM   1753  CE1 HIS A 458      44.618  -2.661  -1.872  1.00 17.21           C  
ANISOU 1753  CE1 HIS A 458     2891   1405   2241    -71   -136   -222       C  
ATOM   1754  NE2 HIS A 458      44.209  -3.505  -0.940  1.00 14.67           N  
ANISOU 1754  NE2 HIS A 458     2176   1280   2118   -315   -448    166       N  
ATOM   1755  N   PHE A 459      42.943  -0.150   2.999  1.00 12.27           N  
ANISOU 1755  N   PHE A 459     1382   1288   1992   -274      3    100       N  
ATOM   1756  CA  PHE A 459      41.716  -0.634   3.631  1.00 12.02           C  
ANISOU 1756  CA  PHE A 459     1326   1260   1982   -295   -117     29       C  
ATOM   1757  C   PHE A 459      40.616   0.431   3.582  1.00 13.18           C  
ANISOU 1757  C   PHE A 459     1406   1297   2303   -109   -271    170       C  
ATOM   1758  O   PHE A 459      39.447   0.111   3.397  1.00 15.11           O  
ANISOU 1758  O   PHE A 459     1271   1723   2745   -218   -294     -5       O  
ATOM   1759  CB  PHE A 459      41.985  -1.087   5.071  1.00 12.84           C  
ANISOU 1759  CB  PHE A 459     1548   1382   1947    -46   -102    132       C  
ATOM   1760  CG  PHE A 459      42.992  -2.205   5.181  1.00 12.81           C  
ANISOU 1760  CG  PHE A 459     1488   1004   2373   -223    121   -100       C  
ATOM   1761  CD1 PHE A 459      43.184  -3.099   4.135  1.00 13.39           C  
ANISOU 1761  CD1 PHE A 459     1581    947   2557   -191     -2   -133       C  
ATOM   1762  CD2 PHE A 459      43.747  -2.360   6.334  1.00 12.53           C  
ANISOU 1762  CD2 PHE A 459     1546   1238   1977   -221    -27    127       C  
ATOM   1763  CE1 PHE A 459      44.114  -4.122   4.235  1.00 13.81           C  
ANISOU 1763  CE1 PHE A 459     1506   1457   2283   -339   -165    112       C  
ATOM   1764  CE2 PHE A 459      44.678  -3.380   6.441  1.00 13.02           C  
ANISOU 1764  CE2 PHE A 459     1466   1148   2333   -315   -216    115       C  
ATOM   1765  CZ  PHE A 459      44.857  -4.268   5.391  1.00 12.82           C  
ANISOU 1765  CZ  PHE A 459     1517   1222   2131   -336   -161   -210       C  
ATOM   1766  N   VAL A 460      40.985   1.698   3.741  1.00 13.15           N  
ANISOU 1766  N   VAL A 460     1386   1322   2288     37   -182    166       N  
ATOM   1767  CA  VAL A 460      40.000   2.770   3.651  1.00 14.23           C  
ANISOU 1767  CA  VAL A 460     1581   1310   2514     99   -395     81       C  
ATOM   1768  C   VAL A 460      39.403   2.807   2.246  1.00 14.81           C  
ANISOU 1768  C   VAL A 460     1607   1572   2448     12   -145    142       C  
ATOM   1769  O   VAL A 460      38.185   2.940   2.065  1.00 17.80           O  
ANISOU 1769  O   VAL A 460     1488   2275   2998    227   -507    -51       O  
ATOM   1770  CB  VAL A 460      40.610   4.141   4.008  1.00 13.69           C  
ANISOU 1770  CB  VAL A 460     1591   1415   2194    209   -429     61       C  
ATOM   1771  CG1 VAL A 460      39.628   5.267   3.667  1.00 16.65           C  
ANISOU 1771  CG1 VAL A 460     1769   1496   3061    395   -548     31       C  
ATOM   1772  CG2 VAL A 460      40.971   4.178   5.481  1.00 15.33           C  
ANISOU 1772  CG2 VAL A 460     1702   1740   2383    391   -144   -290       C  
ATOM   1773  N   ASN A 461      40.269   2.672   1.250  1.00 14.55           N  
ANISOU 1773  N   ASN A 461     1925   1439   2163   -121   -567    136       N  
ATOM   1774  CA  ASN A 461      39.833   2.646  -0.138  1.00 15.62           C  
ANISOU 1774  CA  ASN A 461     2124   1556   2253   -403   -401    226       C  
ATOM   1775  C   ASN A 461      38.888   1.483  -0.455  1.00 16.22           C  
ANISOU 1775  C   ASN A 461     2013   1482   2668   -254   -629    244       C  
ATOM   1776  O   ASN A 461      37.859   1.658  -1.109  1.00 19.37           O  
ANISOU 1776  O   ASN A 461     2131   1857   3371   -162   -996    505       O  
ATOM   1777  CB  ASN A 461      41.050   2.562  -1.055  1.00 16.66           C  
ANISOU 1777  CB  ASN A 461     2337   1913   2080   -387   -684    420       C  
ATOM   1778  CG  ASN A 461      40.717   2.894  -2.480  1.00 19.31           C  
ANISOU 1778  CG  ASN A 461     2748   1937   2650   -520   -671     86       C  
ATOM   1779  OD1 ASN A 461      40.632   4.063  -2.841  1.00 21.25           O  
ANISOU 1779  OD1 ASN A 461     3029   2063   2983   -512   -896    539       O  
ATOM   1780  ND2 ASN A 461      40.511   1.872  -3.299  1.00 21.36           N  
ANISOU 1780  ND2 ASN A 461     3050   2215   2851   -382   -611    488       N  
ATOM   1781  N   GLU A 462      39.249   0.292   0.011  1.00 15.70           N  
ANISOU 1781  N   GLU A 462     1804   1330   2831   -283   -512    267       N  
ATOM   1782  CA  GLU A 462      38.541  -0.930  -0.359  1.00 15.83           C  
ANISOU 1782  CA  GLU A 462     1725   1296   2993   -487   -503    309       C  
ATOM   1783  C   GLU A 462      37.241  -1.153   0.405  1.00 16.42           C  
ANISOU 1783  C   GLU A 462     1794   1738   2705   -249   -611    629       C  
ATOM   1784  O   GLU A 462      36.250  -1.584  -0.176  1.00 18.31           O  
ANISOU 1784  O   GLU A 462     1772   2056   3130   -268   -803    369       O  
ATOM   1785  CB  GLU A 462      39.461  -2.145  -0.183  1.00 17.00           C  
ANISOU 1785  CB  GLU A 462     1825   1597   3037   -278   -359    299       C  
ATOM   1786  CG  GLU A 462      40.651  -2.135  -1.108  1.00 18.07           C  
ANISOU 1786  CG  GLU A 462     2272   1813   2781   -607   -667    141       C  
ATOM   1787  CD  GLU A 462      40.237  -2.159  -2.559  1.00 21.88           C  
ANISOU 1787  CD  GLU A 462     3116   2215   2980   -129   -679    275       C  
ATOM   1788  OE1 GLU A 462      39.831  -3.237  -3.047  1.00 23.65           O  
ANISOU 1788  OE1 GLU A 462     3302   2331   3354    -85   -990   -175       O  
ATOM   1789  OE2 GLU A 462      40.294  -1.095  -3.208  1.00 24.76           O  
ANISOU 1789  OE2 GLU A 462     3737   2361   3309    106   -689    356       O  
ATOM   1790  N   GLN A 463      37.254  -0.882   1.707  1.00 16.95           N  
ANISOU 1790  N   GLN A 463     1988   1759   2691   -293   -622    296       N  
ATOM   1791  CA  GLN A 463      36.093  -1.150   2.550  1.00 18.69           C  
ANISOU 1791  CA  GLN A 463     1911   1939   3251   -504   -495    495       C  
ATOM   1792  C   GLN A 463      35.594  -2.585   2.353  1.00 17.80           C  
ANISOU 1792  C   GLN A 463     1784   1853   3125   -477   -683    405       C  
ATOM   1793  O   GLN A 463      34.386  -2.829   2.246  1.00 21.37           O  
ANISOU 1793  O   GLN A 463     1772   2141   4207   -483   -679    529       O  
ATOM   1794  CB  GLN A 463      34.964  -0.167   2.230  1.00 22.73           C  
ANISOU 1794  CB  GLN A 463     2349   2174   4113   -572   -164    463       C  
ATOM   1795  CG  GLN A 463      35.347   1.294   2.394  1.00 26.03           C  
ANISOU 1795  CG  GLN A 463     2611   2751   4527   -745    144    576       C  
ATOM   1796  CD  GLN A 463      35.317   1.741   3.836  1.00 26.92           C  
ANISOU 1796  CD  GLN A 463     2625   3197   4406   -921    256    579       C  
ATOM   1797  OE1 GLN A 463      34.311   1.568   4.531  1.00 29.21           O  
ANISOU 1797  OE1 GLN A 463     2648   3655   4795  -1088    123   -114       O  
ATOM   1798  NE2 GLN A 463      36.416   2.316   4.301  1.00 28.83           N  
ANISOU 1798  NE2 GLN A 463     2743   3673   4538   -485    141    672       N  
ATOM   1799  N   ALA A 464      36.522  -3.535   2.295  1.00 17.38           N  
ANISOU 1799  N   ALA A 464     1722   1646   3236   -380   -640    300       N  
ATOM   1800  CA  ALA A 464      36.154  -4.935   2.104  1.00 17.30           C  
ANISOU 1800  CA  ALA A 464     1674   1780   3118   -244   -637    305       C  
ATOM   1801  C   ALA A 464      35.618  -5.523   3.401  1.00 18.04           C  
ANISOU 1801  C   ALA A 464     1506   1873   3474   -610   -492    410       C  
ATOM   1802  O   ALA A 464      36.257  -5.414   4.443  1.00 18.03           O  
ANISOU 1802  O   ALA A 464     1547   2156   3148   -538   -453    368       O  
ATOM   1803  CB  ALA A 464      37.347  -5.740   1.611  1.00 17.77           C  
ANISOU 1803  CB  ALA A 464     1696   2047   3007      5   -296    702       C  
ATOM   1804  N   PRO A 465      34.430  -6.142   3.347  1.00 19.28           N  
ANISOU 1804  N   PRO A 465     1650   2343   3330   -682   -908    151       N  
ATOM   1805  CA  PRO A 465      33.895  -6.764   4.560  1.00 20.06           C  
ANISOU 1805  CA  PRO A 465     1670   2277   3676   -765   -691    850       C  
ATOM   1806  C   PRO A 465      34.826  -7.840   5.114  1.00 19.49           C  
ANISOU 1806  C   PRO A 465     1812   2418   3175   -647   -482    464       C  
ATOM   1807  O   PRO A 465      35.454  -8.582   4.355  1.00 18.64           O  
ANISOU 1807  O   PRO A 465     1732   2233   3117   -731   -557    311       O  
ATOM   1808  CB  PRO A 465      32.585  -7.390   4.073  1.00 21.60           C  
ANISOU 1808  CB  PRO A 465     1686   2564   3956   -690   -882   1005       C  
ATOM   1809  CG  PRO A 465      32.170  -6.505   2.939  1.00 23.42           C  
ANISOU 1809  CG  PRO A 465     1938   2716   4244   -522   -941    802       C  
ATOM   1810  CD  PRO A 465      33.454  -6.153   2.243  1.00 21.18           C  
ANISOU 1810  CD  PRO A 465     1765   2437   3846   -737   -943    433       C  
ATOM   1811  N   THR A 466      34.913  -7.902   6.438  1.00 17.97           N  
ANISOU 1811  N   THR A 466     1809   2263   2754   -601   -627    550       N  
ATOM   1812  CA  THR A 466      35.699  -8.919   7.130  1.00 17.47           C  
ANISOU 1812  CA  THR A 466     1973   2144   2521   -761   -618    421       C  
ATOM   1813  C   THR A 466      34.884 -10.208   7.200  1.00 18.66           C  
ANISOU 1813  C   THR A 466     1978   2155   2957  -1111   -401    353       C  
ATOM   1814  O   THR A 466      33.747 -10.202   7.664  1.00 22.47           O  
ANISOU 1814  O   THR A 466     2088   2587   3860   -881    282    268       O  
ATOM   1815  CB  THR A 466      36.066  -8.440   8.545  1.00 18.43           C  
ANISOU 1815  CB  THR A 466     1888   2330   2783   -991   -724    274       C  
ATOM   1816  OG1 THR A 466      36.896  -7.274   8.447  1.00 20.18           O  
ANISOU 1816  OG1 THR A 466     1858   2548   3262  -1008   -399     57       O  
ATOM   1817  CG2 THR A 466      36.806  -9.524   9.328  1.00 20.21           C  
ANISOU 1817  CG2 THR A 466     2206   2732   2740   -260   -589    624       C  
ATOM   1818  N   ARG A 467      35.461 -11.310   6.731  1.00 18.39           N  
ANISOU 1818  N   ARG A 467     2029   2048   2911   -965   -780    126       N  
ATOM   1819  CA  ARG A 467      34.691 -12.542   6.574  1.00 20.24           C  
ANISOU 1819  CA  ARG A 467     2271   2126   3292  -1121   -669    184       C  
ATOM   1820  C   ARG A 467      35.283 -13.751   7.304  1.00 19.80           C  
ANISOU 1820  C   ARG A 467     2393   2065   3066   -915   -591    198       C  
ATOM   1821  O   ARG A 467      34.967 -14.896   6.981  1.00 22.50           O  
ANISOU 1821  O   ARG A 467     2848   1946   3756   -861   -846     99       O  
ATOM   1822  CB  ARG A 467      34.500 -12.841   5.081  1.00 22.23           C  
ANISOU 1822  CB  ARG A 467     2710   2298   3439  -1197  -1029    307       C  
ATOM   1823  CG  ARG A 467      33.739 -11.743   4.328  1.00 25.57           C  
ANISOU 1823  CG  ARG A 467     3055   2927   3732   -831  -1418    639       C  
ATOM   1824  CD  ARG A 467      33.798 -11.929   2.814  1.00 33.34           C  
ANISOU 1824  CD  ARG A 467     3252   3752   5664   -614   -983    646       C  
ATOM   1825  NE  ARG A 467      35.176 -11.946   2.319  1.00 36.46           N  
ANISOU 1825  NE  ARG A 467     3421   4297   6134   -637   -890   1047       N  
ATOM   1826  CZ  ARG A 467      35.833 -10.897   1.819  1.00 32.67           C  
ANISOU 1826  CZ  ARG A 467     3398   3892   5122   -773  -1445   1646       C  
ATOM   1827  NH1 ARG A 467      35.251  -9.695   1.721  1.00 29.57           N  
ANISOU 1827  NH1 ARG A 467     3310   4005   3918   -897  -1649   1374       N  
ATOM   1828  NH2 ARG A 467      37.089 -11.060   1.411  1.00 26.28           N  
ANISOU 1828  NH2 ARG A 467     2857   3413   3716  -1394  -1531   1902       N  
ATOM   1829  N   GLY A 468      36.135 -13.499   8.293  1.00 17.94           N  
ANISOU 1829  N   GLY A 468     2036   2009   2772   -890   -535    376       N  
ATOM   1830  CA  GLY A 468      36.715 -14.575   9.082  1.00 17.55           C  
ANISOU 1830  CA  GLY A 468     1929   2056   2681   -759   -521    521       C  
ATOM   1831  C   GLY A 468      37.412 -14.040  10.315  1.00 16.40           C  
ANISOU 1831  C   GLY A 468     1814   1844   2574   -755   -457    183       C  
ATOM   1832  O   GLY A 468      37.508 -12.822  10.498  1.00 17.39           O  
ANISOU 1832  O   GLY A 468     1785   1928   2892   -472   -309    318       O  
ATOM   1833  N   ASP A 469      37.910 -14.942  11.157  1.00 16.57           N  
ANISOU 1833  N   ASP A 469     1876   1866   2553   -517   -246    355       N  
ATOM   1834  CA  ASP A 469      38.617 -14.546  12.373  1.00 16.78           C  
ANISOU 1834  CA  ASP A 469     1895   1688   2791   -724   -133    307       C  
ATOM   1835  C   ASP A 469      39.906 -13.801  12.061  1.00 15.42           C  
ANISOU 1835  C   ASP A 469     1703   1843   2313   -583    -95    316       C  
ATOM   1836  O   ASP A 469      40.293 -12.873  12.780  1.00 15.97           O  
ANISOU 1836  O   ASP A 469     1994   1706   2368   -549   -196     81       O  
ATOM   1837  CB  ASP A 469      38.980 -15.770  13.218  1.00 16.63           C  
ANISOU 1837  CB  ASP A 469     1991   1653   2675   -759    148    706       C  
ATOM   1838  CG  ASP A 469      37.773 -16.470  13.804  1.00 19.44           C  
ANISOU 1838  CG  ASP A 469     2209   2048   3129   -525    122    647       C  
ATOM   1839  OD1 ASP A 469      36.687 -15.857  13.867  1.00 22.69           O  
ANISOU 1839  OD1 ASP A 469     2311   2832   3479   -322    535    465       O  
ATOM   1840  OD2 ASP A 469      37.931 -17.643  14.211  1.00 20.75           O  
ANISOU 1840  OD2 ASP A 469     2249   2079   3557   -547    157    571       O  
ATOM   1841  N   ALA A 470      40.593 -14.237  11.011  1.00 13.75           N  
ANISOU 1841  N   ALA A 470     1462   1533   2227   -705   -215    483       N  
ATOM   1842  CA  ALA A 470      41.881 -13.656  10.650  1.00 13.04           C  
ANISOU 1842  CA  ALA A 470     1650   1625   1680   -461   -302    228       C  
ATOM   1843  C   ALA A 470      42.103 -13.754   9.151  1.00 12.91           C  
ANISOU 1843  C   ALA A 470     1701   1343   1861   -593   -198    204       C  
ATOM   1844  O   ALA A 470      41.589 -14.669   8.495  1.00 13.90           O  
ANISOU 1844  O   ALA A 470     2011   1277   1992   -579   -408    -41       O  
ATOM   1845  CB  ALA A 470      43.007 -14.364  11.393  1.00 15.90           C  
ANISOU 1845  CB  ALA A 470     1930   2140   1971   -245   -569     63       C  
ATOM   1846  N   ALA A 471      42.862 -12.804   8.613  1.00 13.57           N  
ANISOU 1846  N   ALA A 471     1822   1564   1769   -537   -166     41       N  
ATOM   1847  CA  ALA A 471      43.280 -12.845   7.222  1.00 13.21           C  
ANISOU 1847  CA  ALA A 471     1795   1341   1882   -513   -271     24       C  
ATOM   1848  C   ALA A 471      44.676 -13.446   7.150  1.00 11.50           C  
ANISOU 1848  C   ALA A 471     1730   1147   1492   -439   -264   -139       C  
ATOM   1849  O   ALA A 471      45.627 -12.867   7.683  1.00 12.77           O  
ANISOU 1849  O   ALA A 471     1759   1170   1921   -406   -369   -388       O  
ATOM   1850  CB  ALA A 471      43.273 -11.436   6.616  1.00 13.77           C  
ANISOU 1850  CB  ALA A 471     1797   1223   2210   -419   -144     69       C  
ATOM   1851  N   LEU A 472      44.806 -14.597   6.496  1.00 12.10           N  
ANISOU 1851  N   LEU A 472     1695   1209   1692   -394   -246     88       N  
ATOM   1852  CA  LEU A 472      46.106 -15.230   6.308  1.00 12.01           C  
ANISOU 1852  CA  LEU A 472     1802    997   1764   -602   -205    -37       C  
ATOM   1853  C   LEU A 472      46.845 -14.503   5.197  1.00 11.14           C  
ANISOU 1853  C   LEU A 472     1756   1060   1415   -496   -374   -225       C  
ATOM   1854  O   LEU A 472      46.319 -14.361   4.081  1.00 11.88           O  
ANISOU 1854  O   LEU A 472     1791   1295   1426   -474   -475    120       O  
ATOM   1855  CB  LEU A 472      45.946 -16.710   5.924  1.00 12.45           C  
ANISOU 1855  CB  LEU A 472     1973    953   1803   -371   -372   -142       C  
ATOM   1856  CG  LEU A 472      47.240 -17.441   5.541  1.00 13.22           C  
ANISOU 1856  CG  LEU A 472     2033    963   2025   -359   -665   -186       C  
ATOM   1857  CD1 LEU A 472      48.183 -17.547   6.730  1.00 13.87           C  
ANISOU 1857  CD1 LEU A 472     2149   1083   2037   -285   -813   -142       C  
ATOM   1858  CD2 LEU A 472      46.938 -18.833   4.973  1.00 13.87           C  
ANISOU 1858  CD2 LEU A 472     2211    813   2244   -359   -380   -121       C  
ATOM   1859  N   LEU A 473      48.056 -14.037   5.511  1.00 10.38           N  
ANISOU 1859  N   LEU A 473     1524    800   1620   -524   -138     30       N  
ATOM   1860  CA  LEU A 473      48.935 -13.420   4.515  1.00 10.78           C  
ANISOU 1860  CA  LEU A 473     1619    874   1601   -449   -234     -2       C  
ATOM   1861  C   LEU A 473      50.173 -14.269   4.312  1.00 11.45           C  
ANISOU 1861  C   LEU A 473     1689   1002   1659   -346   -501    233       C  
ATOM   1862  O   LEU A 473      50.693 -14.859   5.268  1.00 11.81           O  
ANISOU 1862  O   LEU A 473     1841   1068   1579   -230   -360    168       O  
ATOM   1863  CB  LEU A 473      49.405 -12.032   4.955  1.00 11.19           C  
ANISOU 1863  CB  LEU A 473     1791    790   1670   -390   -319     20       C  
ATOM   1864  CG  LEU A 473      48.376 -11.034   5.453  1.00 10.84           C  
ANISOU 1864  CG  LEU A 473     1648    674   1796   -220   -453   -111       C  
ATOM   1865  CD1 LEU A 473      49.091  -9.714   5.729  1.00 12.03           C  
ANISOU 1865  CD1 LEU A 473     1762    811   1996   -415   -176   -315       C  
ATOM   1866  CD2 LEU A 473      47.275 -10.848   4.427  1.00 12.55           C  
ANISOU 1866  CD2 LEU A 473     1723   1166   1880   -383   -525      8       C  
ATOM   1867  N   HIS A 474      50.649 -14.322   3.070  1.00 11.40           N  
ANISOU 1867  N   HIS A 474     1805   1010   1515   -269   -266     73       N  
ATOM   1868  CA  HIS A 474      51.977 -14.836   2.797  1.00 10.85           C  
ANISOU 1868  CA  HIS A 474     1959    721   1440   -168      4   -148       C  
ATOM   1869  C   HIS A 474      52.863 -13.674   2.396  1.00 11.15           C  
ANISOU 1869  C   HIS A 474     1789    771   1675   -300   -161   -127       C  
ATOM   1870  O   HIS A 474      52.463 -12.819   1.608  1.00 13.04           O  
ANISOU 1870  O   HIS A 474     1926    990   2039   -210   -509    330       O  
ATOM   1871  CB  HIS A 474      51.947 -15.904   1.708  1.00 11.08           C  
ANISOU 1871  CB  HIS A 474     1853    693   1662   -392    -31   -206       C  
ATOM   1872  CG  HIS A 474      51.404 -17.205   2.187  1.00 11.36           C  
ANISOU 1872  CG  HIS A 474     1937    662   1717   -359   -127    105       C  
ATOM   1873  ND1 HIS A 474      51.288 -18.311   1.372  1.00 14.19           N  
ANISOU 1873  ND1 HIS A 474     2616    819   1954   -289   -352   -148       N  
ATOM   1874  CD2 HIS A 474      50.956 -17.586   3.408  1.00 13.15           C  
ANISOU 1874  CD2 HIS A 474     2268    808   1921   -262   -210    206       C  
ATOM   1875  CE1 HIS A 474      50.787 -19.312   2.069  1.00 14.45           C  
ANISOU 1875  CE1 HIS A 474     2718    845   1925   -291   -464    -78       C  
ATOM   1876  NE2 HIS A 474      50.584 -18.901   3.310  1.00 13.46           N  
ANISOU 1876  NE2 HIS A 474     2385    740   1988   -300   -244    -85       N  
ATOM   1877  N   TYR A 475      54.053 -13.630   2.979  1.00 10.49           N  
ANISOU 1877  N   TYR A 475     1635    650   1699   -158   -285   -122       N  
ATOM   1878  CA  TYR A 475      55.062 -12.640   2.639  1.00 10.38           C  
ANISOU 1878  CA  TYR A 475     1645    764   1534   -238   -239   -182       C  
ATOM   1879  C   TYR A 475      55.942 -13.314   1.607  1.00 11.23           C  
ANISOU 1879  C   TYR A 475     1848    861   1556    -26   -326    -55       C  
ATOM   1880  O   TYR A 475      56.675 -14.263   1.921  1.00 12.71           O  
ANISOU 1880  O   TYR A 475     1884    925   2019     86   -174   -143       O  
ATOM   1881  CB  TYR A 475      55.843 -12.274   3.897  1.00 10.78           C  
ANISOU 1881  CB  TYR A 475     1594    802   1698   -136   -189    -98       C  
ATOM   1882  CG  TYR A 475      56.923 -11.230   3.738  1.00 10.85           C  
ANISOU 1882  CG  TYR A 475     1683    699   1741   -112   -337   -136       C  
ATOM   1883  CD1 TYR A 475      56.608  -9.909   3.424  1.00 10.85           C  
ANISOU 1883  CD1 TYR A 475     1773    630   1717     34   -214   -206       C  
ATOM   1884  CD2 TYR A 475      58.262 -11.551   3.945  1.00 11.72           C  
ANISOU 1884  CD2 TYR A 475     1783    793   1878   -129   -196     58       C  
ATOM   1885  CE1 TYR A 475      57.595  -8.951   3.307  1.00 11.16           C  
ANISOU 1885  CE1 TYR A 475     1596    907   1735   -103   -252      7       C  
ATOM   1886  CE2 TYR A 475      59.262 -10.588   3.825  1.00 10.96           C  
ANISOU 1886  CE2 TYR A 475     1796    685   1681   -283   -322    238       C  
ATOM   1887  CZ  TYR A 475      58.918  -9.293   3.503  1.00 10.39           C  
ANISOU 1887  CZ  TYR A 475     1619    623   1705   -173   -136    232       C  
ATOM   1888  OH  TYR A 475      59.891  -8.321   3.391  1.00 11.26           O  
ANISOU 1888  OH  TYR A 475     1587    717   1974   -117   -175     13       O  
ATOM   1889  N   VAL A 476      55.834 -12.860   0.364  1.00 11.77           N  
ANISOU 1889  N   VAL A 476     1952    983   1535   -109    283   -371       N  
ATOM   1890  CA  VAL A 476      56.433 -13.585  -0.753  1.00 12.40           C  
ANISOU 1890  CA  VAL A 476     1905   1189   1618   -184    411   -199       C  
ATOM   1891  C   VAL A 476      57.595 -12.864  -1.430  1.00 12.37           C  
ANISOU 1891  C   VAL A 476     1962   1217   1520    -77    448   -511       C  
ATOM   1892  O   VAL A 476      57.683 -11.629  -1.415  1.00 14.15           O  
ANISOU 1892  O   VAL A 476     2334    917   2126   -219    249   -368       O  
ATOM   1893  CB  VAL A 476      55.375 -13.963  -1.810  1.00 13.61           C  
ANISOU 1893  CB  VAL A 476     2105   1402   1665   -181     89   -235       C  
ATOM   1894  CG1 VAL A 476      54.158 -14.600  -1.145  1.00 14.02           C  
ANISOU 1894  CG1 VAL A 476     1955   1306   2065   -510    280    -64       C  
ATOM   1895  CG2 VAL A 476      54.979 -12.748  -2.655  1.00 15.72           C  
ANISOU 1895  CG2 VAL A 476     2275   1597   2102     51   -286     39       C  
ATOM   1896  N   ASP A 477      58.481 -13.652  -2.026  1.00 13.94           N  
ANISOU 1896  N   ASP A 477     1990   1438   1869     85    171   -384       N  
ATOM   1897  CA  ASP A 477      59.572 -13.123  -2.832  1.00 16.31           C  
ANISOU 1897  CA  ASP A 477     2139   1686   2372    141    388   -295       C  
ATOM   1898  C   ASP A 477      58.967 -12.302  -3.964  1.00 16.49           C  
ANISOU 1898  C   ASP A 477     2402   1785   2076    -34    514   -275       C  
ATOM   1899  O   ASP A 477      58.056 -12.766  -4.636  1.00 16.43           O  
ANISOU 1899  O   ASP A 477     2433   1891   1919    -10    285     -3       O  
ATOM   1900  CB  ASP A 477      60.397 -14.277  -3.397  1.00 18.97           C  
ANISOU 1900  CB  ASP A 477     2139   2141   2927    346    592   -178       C  
ATOM   1901  CG  ASP A 477      61.597 -13.807  -4.187  1.00 22.15           C  
ANISOU 1901  CG  ASP A 477     2256   2540   3620    202    351   -110       C  
ATOM   1902  OD1 ASP A 477      62.722 -13.849  -3.643  1.00 27.66           O  
ANISOU 1902  OD1 ASP A 477     2476   3276   4757    189     55    165       O  
ATOM   1903  OD2 ASP A 477      61.422 -13.394  -5.352  1.00 22.11           O  
ANISOU 1903  OD2 ASP A 477     2211   2635   3555    439    629     46       O  
ATOM   1904  N   PRO A 478      59.467 -11.073  -4.173  1.00 17.62           N  
ANISOU 1904  N   PRO A 478     2659   1636   2398   -351    628   -196       N  
ATOM   1905  CA  PRO A 478      58.827 -10.160  -5.125  1.00 20.05           C  
ANISOU 1905  CA  PRO A 478     2951   1867   2801   -145    691    162       C  
ATOM   1906  C   PRO A 478      58.967 -10.612  -6.576  1.00 20.56           C  
ANISOU 1906  C   PRO A 478     3459   1882   2472    -80    607     26       C  
ATOM   1907  O   PRO A 478      58.224 -10.136  -7.432  1.00 24.33           O  
ANISOU 1907  O   PRO A 478     3791   2433   3019    176    337    121       O  
ATOM   1908  CB  PRO A 478      59.587  -8.848  -4.912  1.00 19.56           C  
ANISOU 1908  CB  PRO A 478     2759   1695   2976   -356    690    -32       C  
ATOM   1909  CG  PRO A 478      60.931  -9.274  -4.408  1.00 20.69           C  
ANISOU 1909  CG  PRO A 478     2908   1864   3089   -326    650    -86       C  
ATOM   1910  CD  PRO A 478      60.663 -10.475  -3.550  1.00 19.46           C  
ANISOU 1910  CD  PRO A 478     2875   1592   2928   -378    431   -254       C  
ATOM   1911  N   ASP A 479      59.901 -11.520  -6.843  1.00 20.21           N  
ANISOU 1911  N   ASP A 479     3652   1847   2180   -444    955   -299       N  
ATOM   1912  CA  ASP A 479      60.154 -11.973  -8.205  1.00 24.46           C  
ANISOU 1912  CA  ASP A 479     4225   2238   2829   -336   1038   -141       C  
ATOM   1913  C   ASP A 479      59.610 -13.367  -8.508  1.00 25.69           C  
ANISOU 1913  C   ASP A 479     4767   2332   2662   -274    923   -181       C  
ATOM   1914  O   ASP A 479      59.113 -13.615  -9.605  1.00 29.60           O  
ANISOU 1914  O   ASP A 479     5053   2879   3314   -272    173   -433       O  
ATOM   1915  CB  ASP A 479      61.649 -11.905  -8.510  1.00 26.39           C  
ANISOU 1915  CB  ASP A 479     4213   2529   3284   -219   1666   -214       C  
ATOM   1916  CG  ASP A 479      62.214 -10.516  -8.292  1.00 29.26           C  
ANISOU 1916  CG  ASP A 479     4303   2918   3895   -265   2014    100       C  
ATOM   1917  OD1 ASP A 479      61.936  -9.627  -9.122  1.00 32.23           O  
ANISOU 1917  OD1 ASP A 479     4578   2952   4715    -47   1510    134       O  
ATOM   1918  OD2 ASP A 479      62.925 -10.312  -7.287  1.00 33.32           O  
ANISOU 1918  OD2 ASP A 479     4298   3356   5005    -79   2041    128       O  
ATOM   1919  N   THR A 480      59.698 -14.273  -7.539  1.00 24.38           N  
ANISOU 1919  N   THR A 480     5001   2274   1989   -374    842   -142       N  
ATOM   1920  CA  THR A 480      59.248 -15.649  -7.746  1.00 25.41           C  
ANISOU 1920  CA  THR A 480     5258   2049   2347   -499    581   -508       C  
ATOM   1921  C   THR A 480      57.890 -15.929  -7.104  1.00 25.21           C  
ANISOU 1921  C   THR A 480     5329   2174   2075  -1004    145   -332       C  
ATOM   1922  O   THR A 480      57.237 -16.927  -7.420  1.00 27.31           O  
ANISOU 1922  O   THR A 480     5488   2484   2402  -1211    -23   -505       O  
ATOM   1923  CB  THR A 480      60.253 -16.651  -7.171  1.00 27.83           C  
ANISOU 1923  CB  THR A 480     5359   1994   3219   -224    994   -288       C  
ATOM   1924  OG1 THR A 480      60.256 -16.551  -5.740  1.00 29.00           O  
ANISOU 1924  OG1 THR A 480     5368   1656   3994   -140    989   -164       O  
ATOM   1925  CG2 THR A 480      61.653 -16.381  -7.717  1.00 29.69           C  
ANISOU 1925  CG2 THR A 480     5403   2111   3768   -245   1132   -253       C  
ATOM   1926  N   HIS A 481      57.484 -15.055  -6.189  1.00 24.88           N  
ANISOU 1926  N   HIS A 481     5207   2034   2211  -1077   -134   -115       N  
ATOM   1927  CA  HIS A 481      56.224 -15.197  -5.459  1.00 27.04           C  
ANISOU 1927  CA  HIS A 481     5211   2164   2898   -939   -487      9       C  
ATOM   1928  C   HIS A 481      56.208 -16.404  -4.523  1.00 25.55           C  
ANISOU 1928  C   HIS A 481     4759   2034   2913  -1063   -248   -415       C  
ATOM   1929  O   HIS A 481      55.151 -16.827  -4.044  1.00 26.73           O  
ANISOU 1929  O   HIS A 481     4592   2364   3200  -1392    408   -483       O  
ATOM   1930  CB  HIS A 481      55.036 -15.217  -6.423  1.00 33.18           C  
ANISOU 1930  CB  HIS A 481     5769   2942   3896   -430  -1430    456       C  
ATOM   1931  CG  HIS A 481      54.838 -13.924  -7.147  1.00 41.38           C  
ANISOU 1931  CG  HIS A 481     6408   3618   5696    174  -1989    508       C  
ATOM   1932  ND1 HIS A 481      55.202 -12.709  -6.607  1.00 44.01           N  
ANISOU 1932  ND1 HIS A 481     6649   3917   6154    397  -2338    630       N  
ATOM   1933  CD2 HIS A 481      54.328 -13.653  -8.373  1.00 44.52           C  
ANISOU 1933  CD2 HIS A 481     6713   3930   6270    480  -2239    678       C  
ATOM   1934  CE1 HIS A 481      54.918 -11.745  -7.465  1.00 46.10           C  
ANISOU 1934  CE1 HIS A 481     6814   4093   6610    485  -2477    673       C  
ATOM   1935  NE2 HIS A 481      54.388 -12.291  -8.545  1.00 46.16           N  
ANISOU 1935  NE2 HIS A 481     6872   4104   6563    577  -2391    739       N  
ATOM   1936  N   ARG A 482      57.391 -16.944  -4.254  1.00 20.62           N  
ANISOU 1936  N   ARG A 482     4342   1629   1864   -748    151   -463       N  
ATOM   1937  CA  ARG A 482      57.526 -18.015  -3.279  1.00 20.52           C  
ANISOU 1937  CA  ARG A 482     4077   1621   2097   -364    272   -215       C  
ATOM   1938  C   ARG A 482      57.260 -17.475  -1.880  1.00 17.00           C  
ANISOU 1938  C   ARG A 482     3334   1175   1951   -317    246    -47       C  
ATOM   1939  O   ARG A 482      57.740 -16.400  -1.522  1.00 16.12           O  
ANISOU 1939  O   ARG A 482     2852    941   2330   -302    137   -245       O  
ATOM   1940  CB  ARG A 482      58.933 -18.600  -3.344  1.00 25.31           C  
ANISOU 1940  CB  ARG A 482     4401   2456   2760    228    434     96       C  
ATOM   1941  CG  ARG A 482      59.110 -19.883  -2.565  1.00 33.00           C  
ANISOU 1941  CG  ARG A 482     4682   3529   4328    435    467    138       C  
ATOM   1942  CD  ARG A 482      60.504 -20.459  -2.781  1.00 39.83           C  
ANISOU 1942  CD  ARG A 482     5057   4279   5795    726    556      7       C  
ATOM   1943  NE  ARG A 482      61.539 -19.696  -2.078  1.00 45.44           N  
ANISOU 1943  NE  ARG A 482     5299   4964   7000    783    622   -231       N  
ATOM   1944  CZ  ARG A 482      62.229 -18.688  -2.603  1.00 50.68           C  
ANISOU 1944  CZ  ARG A 482     5523   5734   7999   1020    511   -670       C  
ATOM   1945  NH1 ARG A 482      62.003 -18.304  -3.849  1.00 51.84           N  
ANISOU 1945  NH1 ARG A 482     5569   5865   8263   1030    404   -743       N  
ATOM   1946  NH2 ARG A 482      63.145 -18.064  -1.877  1.00 52.02           N  
ANISOU 1946  NH2 ARG A 482     5628   5886   8251   1171    464   -905       N  
ATOM   1947  N   ASN A 483      56.500 -18.219  -1.090  1.00 17.19           N  
ANISOU 1947  N   ASN A 483     3197   1264   2070   -273    -97   -213       N  
ATOM   1948  CA  ASN A 483      56.217 -17.831   0.285  1.00 15.19           C  
ANISOU 1948  CA  ASN A 483     2819   1235   1717   -317   -136    108       C  
ATOM   1949  C   ASN A 483      57.458 -17.894   1.173  1.00 15.14           C  
ANISOU 1949  C   ASN A 483     2669   1064   2017     44   -350    252       C  
ATOM   1950  O   ASN A 483      58.139 -18.928   1.235  1.00 18.44           O  
ANISOU 1950  O   ASN A 483     3191    991   2823    305   -469     21       O  
ATOM   1951  CB  ASN A 483      55.120 -18.727   0.865  1.00 16.02           C  
ANISOU 1951  CB  ASN A 483     2698   1353   2034   -576   -206     73       C  
ATOM   1952  CG  ASN A 483      54.771 -18.366   2.290  1.00 18.65           C  
ANISOU 1952  CG  ASN A 483     2648   1920   2517   -361   -346    336       C  
ATOM   1953  OD1 ASN A 483      54.742 -17.187   2.657  1.00 19.16           O  
ANISOU 1953  OD1 ASN A 483     2527   2226   2525   -363   -272   -195       O  
ATOM   1954  ND2 ASN A 483      54.519 -19.381   3.110  1.00 21.89           N  
ANISOU 1954  ND2 ASN A 483     2857   2528   2932   -460    -96    657       N  
ATOM   1955  N   LEU A 484      57.737 -16.793   1.866  1.00 14.17           N  
ANISOU 1955  N   LEU A 484     2324   1067   1992   -130   -166   -421       N  
ATOM   1956  CA  LEU A 484      58.875 -16.700   2.776  1.00 13.63           C  
ANISOU 1956  CA  LEU A 484     1777   1207   2194   -354    -17   -137       C  
ATOM   1957  C   LEU A 484      58.464 -16.793   4.246  1.00 14.13           C  
ANISOU 1957  C   LEU A 484     1811   1281   2275    -26    254     74       C  
ATOM   1958  O   LEU A 484      59.304 -17.024   5.117  1.00 16.30           O  
ANISOU 1958  O   LEU A 484     2202   1919   2073    144   -463    -10       O  
ATOM   1959  CB  LEU A 484      59.616 -15.381   2.554  1.00 14.10           C  
ANISOU 1959  CB  LEU A 484     1806   1477   2073   -278    183   -194       C  
ATOM   1960  CG  LEU A 484      60.031 -15.092   1.112  1.00 15.29           C  
ANISOU 1960  CG  LEU A 484     1969   1569   2269    -28    287   -156       C  
ATOM   1961  CD1 LEU A 484      60.684 -13.724   1.019  1.00 17.33           C  
ANISOU 1961  CD1 LEU A 484     2279   1772   2531   -386    -58    -16       C  
ATOM   1962  CD2 LEU A 484      60.963 -16.173   0.601  1.00 17.92           C  
ANISOU 1962  CD2 LEU A 484     2080   1956   2771    341    458   -121       C  
ATOM   1963  N   GLY A 485      57.177 -16.601   4.519  1.00 12.94           N  
ANISOU 1963  N   GLY A 485     1876   1092   1946     65     13     16       N  
ATOM   1964  CA  GLY A 485      56.673 -16.613   5.881  1.00 13.25           C  
ANISOU 1964  CA  GLY A 485     1832   1503   1698     18    145     97       C  
ATOM   1965  C   GLY A 485      55.204 -16.252   5.953  1.00 11.68           C  
ANISOU 1965  C   GLY A 485     1770   1294   1372   -200   -196     71       C  
ATOM   1966  O   GLY A 485      54.723 -15.398   5.199  1.00 13.92           O  
ANISOU 1966  O   GLY A 485     1929   1443   1918    -67   -100    488       O  
ATOM   1967  N   GLU A 486      54.482 -16.909   6.857  1.00 12.24           N  
ANISOU 1967  N   GLU A 486     1824   1252   1573   -301     86    -38       N  
ATOM   1968  CA  GLU A 486      53.054 -16.655   7.028  1.00 11.79           C  
ANISOU 1968  CA  GLU A 486     1871    849   1758   -465   -277     68       C  
ATOM   1969  C   GLU A 486      52.775 -15.685   8.161  1.00 11.30           C  
ANISOU 1969  C   GLU A 486     1760    866   1666   -164   -423     56       C  
ATOM   1970  O   GLU A 486      53.499 -15.662   9.164  1.00 12.76           O  
ANISOU 1970  O   GLU A 486     1947   1178   1721     14   -577     69       O  
ATOM   1971  CB  GLU A 486      52.317 -17.948   7.354  1.00 12.35           C  
ANISOU 1971  CB  GLU A 486     2347    714   1631   -306   -207    -30       C  
ATOM   1972  CG  GLU A 486      52.408 -19.034   6.317  1.00 13.85           C  
ANISOU 1972  CG  GLU A 486     2523    778   1959   -258    -73   -202       C  
ATOM   1973  CD  GLU A 486      51.409 -20.123   6.619  1.00 13.62           C  
ANISOU 1973  CD  GLU A 486     2298    801   2074   -426   -271    119       C  
ATOM   1974  OE1 GLU A 486      51.551 -20.763   7.682  1.00 15.38           O  
ANISOU 1974  OE1 GLU A 486     2466   1081   2297   -312   -412    298       O  
ATOM   1975  OE2 GLU A 486      50.460 -20.296   5.825  1.00 14.30           O  
ANISOU 1975  OE2 GLU A 486     2170   1140   2121   -334   -396    -43       O  
ATOM   1976  N   PHE A 487      51.696 -14.919   8.012  1.00 10.83           N  
ANISOU 1976  N   PHE A 487     1589    899   1626   -222   -251    111       N  
ATOM   1977  CA  PHE A 487      51.258 -13.971   9.031  1.00  9.98           C  
ANISOU 1977  CA  PHE A 487     1452    775   1563   -415    -15    211       C  
ATOM   1978  C   PHE A 487      49.741 -14.023   9.127  1.00 11.27           C  
ANISOU 1978  C   PHE A 487     1580    928   1773   -323   -177    -17       C  
ATOM   1979  O   PHE A 487      49.065 -14.345   8.151  1.00 12.23           O  
ANISOU 1979  O   PHE A 487     1766   1319   1563   -306   -362     -8       O  
ATOM   1980  CB  PHE A 487      51.689 -12.546   8.648  1.00 11.30           C  
ANISOU 1980  CB  PHE A 487     1358    958   1978   -550   -112    196       C  
ATOM   1981  CG  PHE A 487      53.177 -12.359   8.582  1.00 10.53           C  
ANISOU 1981  CG  PHE A 487     1323    847   1832   -440   -167     42       C  
ATOM   1982  CD1 PHE A 487      53.865 -11.820   9.656  1.00 11.71           C  
ANISOU 1982  CD1 PHE A 487     1250   1272   1926   -277   -522   -130       C  
ATOM   1983  CD2 PHE A 487      53.892 -12.732   7.452  1.00 11.29           C  
ANISOU 1983  CD2 PHE A 487     1382   1034   1872   -344   -175    277       C  
ATOM   1984  CE1 PHE A 487      55.236 -11.637   9.602  1.00 12.42           C  
ANISOU 1984  CE1 PHE A 487     1212   1527   1981   -216   -277    -90       C  
ATOM   1985  CE2 PHE A 487      55.269 -12.566   7.398  1.00 11.35           C  
ANISOU 1985  CE2 PHE A 487     1527   1222   1564   -121   -361    -53       C  
ATOM   1986  CZ  PHE A 487      55.934 -12.015   8.474  1.00 11.65           C  
ANISOU 1986  CZ  PHE A 487     1247   1389   1788   -269   -184    -60       C  
ATOM   1987  N   LYS A 488      49.200 -13.714  10.299  1.00 11.18           N  
ANISOU 1987  N   LYS A 488     1555    928   1766   -193   -300    -96       N  
ATOM   1988  CA  LYS A 488      47.756 -13.592  10.448  1.00 11.13           C  
ANISOU 1988  CA  LYS A 488     1525    783   1919   -325   -304     94       C  
ATOM   1989  C   LYS A 488      47.402 -12.154  10.794  1.00 10.91           C  
ANISOU 1989  C   LYS A 488     1694    662   1790   -309   -315    -48       C  
ATOM   1990  O   LYS A 488      47.935 -11.605  11.763  1.00 13.40           O  
ANISOU 1990  O   LYS A 488     1864   1032   2196   -142   -765   -293       O  
ATOM   1991  CB  LYS A 488      47.242 -14.552  11.517  1.00 11.63           C  
ANISOU 1991  CB  LYS A 488     1669    788   1961   -407   -285   -177       C  
ATOM   1992  CG  LYS A 488      47.256 -16.009  11.028  1.00 12.54           C  
ANISOU 1992  CG  LYS A 488     1923    809   2033   -426   -362    -88       C  
ATOM   1993  CD  LYS A 488      47.177 -17.022  12.162  1.00 13.13           C  
ANISOU 1993  CD  LYS A 488     1761   1142   2084   -557   -246    195       C  
ATOM   1994  CE  LYS A 488      45.821 -17.016  12.848  1.00 14.08           C  
ANISOU 1994  CE  LYS A 488     1946   1247   2157   -525   -230    489       C  
ATOM   1995  NZ  LYS A 488      45.806 -17.982  13.980  1.00 14.10           N  
ANISOU 1995  NZ  LYS A 488     1906   1291   2160   -557   -135     95       N  
ATOM   1996  N   MET A 489      46.532 -11.538   9.985  1.00 10.87           N  
ANISOU 1996  N   MET A 489     1497    820   1811   -177   -388    238       N  
ATOM   1997  CA  MET A 489      46.038 -10.191  10.255  1.00 11.68           C  
ANISOU 1997  CA  MET A 489     1762    866   1811   -223   -319    -18       C  
ATOM   1998  C   MET A 489      44.691 -10.302  10.937  1.00 13.23           C  
ANISOU 1998  C   MET A 489     1575   1350   2102   -276   -172   -286       C  
ATOM   1999  O   MET A 489      43.801 -10.994  10.450  1.00 18.04           O  
ANISOU 1999  O   MET A 489     1699   2218   2937   -357   -267  -1142       O  
ATOM   2000  CB  MET A 489      45.828  -9.399   8.962  1.00 17.04           C  
ANISOU 2000  CB  MET A 489     2586   1770   2118    110   -305    516       C  
ATOM   2001  CG  MET A 489      47.046  -8.801   8.305  1.00 22.69           C  
ANISOU 2001  CG  MET A 489     2557   2853   3212    271    -39    288       C  
ATOM   2002  SD  MET A 489      46.580  -7.257   7.474  1.00 20.21           S  
ANISOU 2002  SD  MET A 489     1907   3061   2711   -258     -5   1545       S  
ATOM   2003  CE  MET A 489      46.619  -6.128   8.856  1.00 26.71           C  
ANISOU 2003  CE  MET A 489     2551   3226   4372     -9   -334   1003       C  
ATOM   2004  N   TYR A 490      44.519  -9.603  12.048  1.00 12.02           N  
ANISOU 2004  N   TYR A 490     1514   1247   1804   -293     35      9       N  
ATOM   2005  CA  TYR A 490      43.262  -9.660  12.774  1.00 11.68           C  
ANISOU 2005  CA  TYR A 490     1421   1231   1785   -363    105     15       C  
ATOM   2006  C   TYR A 490      42.413  -8.429  12.456  1.00 13.53           C  
ANISOU 2006  C   TYR A 490     1446   1525   2168   -300   -196    -29       C  
ATOM   2007  O   TYR A 490      42.948  -7.398  12.040  1.00 14.08           O  
ANISOU 2007  O   TYR A 490     1575   1513   2261   -116   -267     60       O  
ATOM   2008  CB  TYR A 490      43.527  -9.835  14.275  1.00 12.56           C  
ANISOU 2008  CB  TYR A 490     1667   1286   1817   -282     45    123       C  
ATOM   2009  CG  TYR A 490      44.068 -11.217  14.589  1.00 12.48           C  
ANISOU 2009  CG  TYR A 490     1668   1080   1994   -396   -298     46       C  
ATOM   2010  CD1 TYR A 490      43.210 -12.262  14.894  1.00 13.97           C  
ANISOU 2010  CD1 TYR A 490     1902   1002   2403   -521     10    -27       C  
ATOM   2011  CD2 TYR A 490      45.432 -11.484  14.535  1.00 12.68           C  
ANISOU 2011  CD2 TYR A 490     1636   1203   1979   -176   -386    183       C  
ATOM   2012  CE1 TYR A 490      43.695 -13.531  15.166  1.00 15.02           C  
ANISOU 2012  CE1 TYR A 490     1844   1409   2452   -267     46   -184       C  
ATOM   2013  CE2 TYR A 490      45.926 -12.747  14.800  1.00 12.94           C  
ANISOU 2013  CE2 TYR A 490     1710   1074   2130   -264   -410    195       C  
ATOM   2014  CZ  TYR A 490      45.053 -13.769  15.111  1.00 13.52           C  
ANISOU 2014  CZ  TYR A 490     1929   1082   2124   -356    -49    -50       C  
ATOM   2015  OH  TYR A 490      45.542 -15.034  15.377  1.00 15.26           O  
ANISOU 2015  OH  TYR A 490     2121   1089   2587   -523   -135    186       O  
ATOM   2016  N   PRO A 491      41.086  -8.542  12.624  1.00 13.91           N  
ANISOU 2016  N   PRO A 491     1301   1459   2524   -531   -329    183       N  
ATOM   2017  CA  PRO A 491      40.153  -7.482  12.219  1.00 14.55           C  
ANISOU 2017  CA  PRO A 491     1205   1526   2798   -338   -185    217       C  
ATOM   2018  C   PRO A 491      40.467  -6.119  12.830  1.00 14.68           C  
ANISOU 2018  C   PRO A 491     1316   1502   2760   -246    -56    130       C  
ATOM   2019  O   PRO A 491      40.160  -5.091  12.212  1.00 15.12           O  
ANISOU 2019  O   PRO A 491     1356   1550   2837   -170      2    340       O  
ATOM   2020  CB  PRO A 491      38.802  -7.994  12.724  1.00 15.97           C  
ANISOU 2020  CB  PRO A 491     1385   1445   3238   -404    -81    232       C  
ATOM   2021  CG  PRO A 491      38.951  -9.495  12.710  1.00 17.21           C  
ANISOU 2021  CG  PRO A 491     1340   1673   3526   -231   -187    591       C  
ATOM   2022  CD  PRO A 491      40.383  -9.731  13.144  1.00 14.62           C  
ANISOU 2022  CD  PRO A 491     1202   1518   2833   -569   -170    224       C  
ATOM   2023  N   GLU A 492      41.073  -6.113  14.014  1.00 14.34           N  
ANISOU 2023  N   GLU A 492     1469   1476   2504   -341    -35   -224       N  
ATOM   2024  CA  GLU A 492      41.445  -4.875  14.698  1.00 15.74           C  
ANISOU 2024  CA  GLU A 492     1885   1613   2481   -407    138    134       C  
ATOM   2025  C   GLU A 492      42.544  -4.085  13.976  1.00 14.17           C  
ANISOU 2025  C   GLU A 492     1859   1425   2101   -284    -75    261       C  
ATOM   2026  O   GLU A 492      42.810  -2.941  14.321  1.00 15.89           O  
ANISOU 2026  O   GLU A 492     2372   1358   2305   -453    331    -91       O  
ATOM   2027  CB  GLU A 492      41.870  -5.173  16.142  1.00 17.34           C  
ANISOU 2027  CB  GLU A 492     2210   2001   2377   -680    233    237       C  
ATOM   2028  CG  GLU A 492      40.743  -5.683  17.030  1.00 20.66           C  
ANISOU 2028  CG  GLU A 492     2576   2048   3227   -690    593    116       C  
ATOM   2029  CD  GLU A 492      40.482  -7.181  16.910  1.00 23.71           C  
ANISOU 2029  CD  GLU A 492     2981   2416   3610   -545    898    405       C  
ATOM   2030  OE1 GLU A 492      41.195  -7.885  16.163  1.00 20.77           O  
ANISOU 2030  OE1 GLU A 492     3029   2241   2620   -370    421    281       O  
ATOM   2031  OE2 GLU A 492      39.546  -7.654  17.584  1.00 28.73           O  
ANISOU 2031  OE2 GLU A 492     3366   2742   4808   -611   1260    425       O  
ATOM   2032  N   GLY A 493      43.189  -4.703  12.990  1.00 13.00           N  
ANISOU 2032  N   GLY A 493     1481   1343   2113   -315   -256    174       N  
ATOM   2033  CA  GLY A 493      44.166  -3.995  12.176  1.00 11.76           C  
ANISOU 2033  CA  GLY A 493     1131   1278   2058   -441   -171    265       C  
ATOM   2034  C   GLY A 493      45.598  -4.129  12.663  1.00 12.58           C  
ANISOU 2034  C   GLY A 493     1366   1227   2188   -238   -306    331       C  
ATOM   2035  O   GLY A 493      46.294  -3.134  12.850  1.00 17.01           O  
ANISOU 2035  O   GLY A 493     1630   1386   3445   -436   -697    483       O  
ATOM   2036  N   TYR A 494      46.038  -5.356  12.885  1.00 11.47           N  
ANISOU 2036  N   TYR A 494     1208   1092   2058   -254   -190    -23       N  
ATOM   2037  CA  TYR A 494      47.434  -5.635  13.208  1.00 11.14           C  
ANISOU 2037  CA  TYR A 494     1372   1099   1760   -225   -325   -416       C  
ATOM   2038  C   TYR A 494      47.725  -7.051  12.744  1.00 11.48           C  
ANISOU 2038  C   TYR A 494     1441    927   1995   -301   -232   -127       C  
ATOM   2039  O   TYR A 494      46.804  -7.805  12.397  1.00 13.19           O  
ANISOU 2039  O   TYR A 494     1383   1058   2571   -259   -323   -451       O  
ATOM   2040  CB  TYR A 494      47.697  -5.503  14.717  1.00 12.80           C  
ANISOU 2040  CB  TYR A 494     1687   1520   1656   -346   -241   -191       C  
ATOM   2041  CG  TYR A 494      47.015  -6.569  15.550  1.00 13.71           C  
ANISOU 2041  CG  TYR A 494     1890   1703   1617   -443   -258    -70       C  
ATOM   2042  CD1 TYR A 494      47.714  -7.686  15.989  1.00 15.44           C  
ANISOU 2042  CD1 TYR A 494     2449   1890   1527   -265     21    101       C  
ATOM   2043  CD2 TYR A 494      45.673  -6.460  15.898  1.00 15.65           C  
ANISOU 2043  CD2 TYR A 494     2072   1945   1929   -823   -533    241       C  
ATOM   2044  CE1 TYR A 494      47.097  -8.670  16.739  1.00 16.81           C  
ANISOU 2044  CE1 TYR A 494     2613   1978   1794   -526   -139   -133       C  
ATOM   2045  CE2 TYR A 494      45.047  -7.440  16.654  1.00 16.93           C  
ANISOU 2045  CE2 TYR A 494     2337   2088   2006   -883   -355    516       C  
ATOM   2046  CZ  TYR A 494      45.768  -8.539  17.072  1.00 16.70           C  
ANISOU 2046  CZ  TYR A 494     2708   1969   1668   -996   -255    434       C  
ATOM   2047  OH  TYR A 494      45.155  -9.522  17.822  1.00 21.38           O  
ANISOU 2047  OH  TYR A 494     3180   2394   2548   -852   -288    471       O  
ATOM   2048  N   MET A 495      48.993  -7.433  12.711  1.00 10.87           N  
ANISOU 2048  N   MET A 495     1374    971   1785     66   -268    -39       N  
ATOM   2049  CA  MET A 495      49.298  -8.804  12.331  1.00 12.21           C  
ANISOU 2049  CA  MET A 495     1602   1382   1653    133   -162     97       C  
ATOM   2050  C   MET A 495      50.225  -9.509  13.305  1.00 10.62           C  
ANISOU 2050  C   MET A 495     1438   1048   1548     58   -427    -23       C  
ATOM   2051  O   MET A 495      50.915  -8.875  14.105  1.00 11.16           O  
ANISOU 2051  O   MET A 495     1387   1062   1790    -93   -396   -170       O  
ATOM   2052  CB  MET A 495      49.774  -8.930  10.876  1.00 18.28           C  
ANISOU 2052  CB  MET A 495     2156   2438   2351    522    -92    384       C  
ATOM   2053  CG  MET A 495      51.179  -8.489  10.611  1.00 18.06           C  
ANISOU 2053  CG  MET A 495     1957   2264   2641   -117   -259    569       C  
ATOM   2054  SD  MET A 495      51.688  -8.685   8.869  1.00 12.99           S  
ANISOU 2054  SD  MET A 495     1814   1304   1816   -375   -220     84       S  
ATOM   2055  CE  MET A 495      50.779  -7.380   8.037  1.00 16.54           C  
ANISOU 2055  CE  MET A 495     2113   1616   2553   -233   -482    -61       C  
ATOM   2056  N   THR A 496      50.195 -10.833  13.259  1.00 11.24           N  
ANISOU 2056  N   THR A 496     1425    910   1934     47   -231     92       N  
ATOM   2057  CA  THR A 496      51.032 -11.646  14.118  1.00 10.86           C  
ANISOU 2057  CA  THR A 496     1501    907   1718    -99   -288   -106       C  
ATOM   2058  C   THR A 496      51.828 -12.641  13.298  1.00 10.92           C  
ANISOU 2058  C   THR A 496     1478    969   1702   -263   -419    -85       C  
ATOM   2059  O   THR A 496      51.541 -12.870  12.114  1.00 11.45           O  
ANISOU 2059  O   THR A 496     1495   1050   1804   -124   -470   -136       O  
ATOM   2060  CB  THR A 496      50.205 -12.444  15.122  1.00 12.62           C  
ANISOU 2060  CB  THR A 496     1629   1038   2126   -441   -104   -417       C  
ATOM   2061  OG1 THR A 496      49.403 -13.391  14.407  1.00 13.25           O  
ANISOU 2061  OG1 THR A 496     1756   1054   2222   -346   -250   -125       O  
ATOM   2062  CG2 THR A 496      49.312 -11.519  15.950  1.00 13.62           C  
ANISOU 2062  CG2 THR A 496     1766   1212   2197   -375    -61   -136       C  
ATOM   2063  N   CYS A 497      52.826 -13.228  13.945  1.00 11.95           N  
ANISOU 2063  N   CYS A 497     1452    881   2208   -108   -426    -26       N  
ATOM   2064  CA  CYS A 497      53.595 -14.322  13.382  1.00 11.40           C  
ANISOU 2064  CA  CYS A 497     1661    991   1680   -139   -287    -12       C  
ATOM   2065  C   CYS A 497      53.970 -15.242  14.529  1.00 11.74           C  
ANISOU 2065  C   CYS A 497     2011    842   1607   -413   -622    223       C  
ATOM   2066  O   CYS A 497      53.778 -14.905  15.695  1.00 13.34           O  
ANISOU 2066  O   CYS A 497     2218   1070   1781   -227   -544    155       O  
ATOM   2067  CB  CYS A 497      54.880 -13.796  12.742  1.00 13.49           C  
ANISOU 2067  CB  CYS A 497     1549   1220   2357   -578   -273    165       C  
ATOM   2068  SG  CYS A 497      56.101 -13.182  13.954  1.00 15.48           S  
ANISOU 2068  SG  CYS A 497     1854   1130   2898   -463   -755    402       S  
ATOM   2069  N   VAL A 498      54.511 -16.407  14.200  1.00 12.29           N  
ANISOU 2069  N   VAL A 498     1901    790   1978   -327   -638    152       N  
ATOM   2070  CA  VAL A 498      55.250 -17.176  15.185  1.00 14.05           C  
ANISOU 2070  CA  VAL A 498     2120    868   2348   -342   -659    120       C  
ATOM   2071  C   VAL A 498      56.719 -16.998  14.824  1.00 14.54           C  
ANISOU 2071  C   VAL A 498     2260    961   2302   -216   -944     78       C  
ATOM   2072  O   VAL A 498      57.178 -17.484  13.788  1.00 17.06           O  
ANISOU 2072  O   VAL A 498     2486   1585   2411    302   -695    -28       O  
ATOM   2073  CB  VAL A 498      54.855 -18.664  15.193  1.00 15.15           C  
ANISOU 2073  CB  VAL A 498     2602    978   2177   -284   -713    409       C  
ATOM   2074  CG1 VAL A 498      55.770 -19.437  16.130  1.00 18.47           C  
ANISOU 2074  CG1 VAL A 498     3092   1086   2838     38   -952    271       C  
ATOM   2075  CG2 VAL A 498      53.412 -18.814  15.628  1.00 16.05           C  
ANISOU 2075  CG2 VAL A 498     2714   1391   1993   -485   -248    220       C  
ATOM   2076  N   PRO A 499      57.453 -16.248  15.657  1.00 16.17           N  
ANISOU 2076  N   PRO A 499     2208   1183   2753   -120  -1000    236       N  
ATOM   2077  CA  PRO A 499      58.823 -15.882  15.302  1.00 18.02           C  
ANISOU 2077  CA  PRO A 499     2199   1243   3403    -86   -975     59       C  
ATOM   2078  C   PRO A 499      59.780 -17.029  15.534  1.00 18.92           C  
ANISOU 2078  C   PRO A 499     2232   1473   3482    -90  -1081    376       C  
ATOM   2079  O   PRO A 499      59.454 -17.982  16.246  1.00 19.18           O  
ANISOU 2079  O   PRO A 499     2274   1562   3452     51  -1093    194       O  
ATOM   2080  CB  PRO A 499      59.137 -14.744  16.278  1.00 19.01           C  
ANISOU 2080  CB  PRO A 499     2364   1363   3496   -196   -903   -131       C  
ATOM   2081  CG  PRO A 499      58.318 -15.056  17.474  1.00 19.33           C  
ANISOU 2081  CG  PRO A 499     2460   1614   3268   -153   -948   -129       C  
ATOM   2082  CD  PRO A 499      57.040 -15.670  16.949  1.00 16.68           C  
ANISOU 2082  CD  PRO A 499     2266   1555   2517   -372  -1170   -198       C  
ATOM   2083  N   ASN A 500      60.950 -16.932  14.919  1.00 19.10           N  
ANISOU 2083  N   ASN A 500     2237   1696   3322    -62   -983    513       N  
ATOM   2084  CA  ASN A 500      62.037 -17.844  15.218  1.00 20.49           C  
ANISOU 2084  CA  ASN A 500     2412   1828   3545     25  -1456    293       C  
ATOM   2085  C   ASN A 500      61.702 -19.289  14.881  1.00 24.50           C  
ANISOU 2085  C   ASN A 500     2911   2120   4277     72  -1550    112       C  
ATOM   2086  O   ASN A 500      62.069 -20.202  15.616  1.00 25.56           O  
ANISOU 2086  O   ASN A 500     3063   1791   4857     50  -1285    145       O  
ATOM   2087  CB  ASN A 500      62.423 -17.735  16.694  1.00 21.19           C  
ANISOU 2087  CB  ASN A 500     2280   2146   3623    138  -1185    671       C  
ATOM   2088  CG  ASN A 500      63.733 -18.406  16.990  1.00 21.28           C  
ANISOU 2088  CG  ASN A 500     2327   2107   3652    -78  -1041    447       C  
ATOM   2089  OD1 ASN A 500      64.615 -18.444  16.136  1.00 20.13           O  
ANISOU 2089  OD1 ASN A 500     2359   1936   3354   -363  -1186    266       O  
ATOM   2090  ND2 ASN A 500      63.872 -18.949  18.194  1.00 22.52           N  
ANISOU 2090  ND2 ASN A 500     2419   2476   3659     60  -1285    184       N  
ATOM   2091  N   ALA A 501      61.002 -19.491  13.770  1.00 27.86           N  
ANISOU 2091  N   ALA A 501     3333   2424   4826   -126  -1506   -680       N  
ATOM   2092  CA  ALA A 501      60.684 -20.834  13.309  1.00 34.88           C  
ANISOU 2092  CA  ALA A 501     3959   3614   5680    172  -1661  -1056       C  
ATOM   2093  C   ALA A 501      61.968 -21.585  12.974  1.00 40.48           C  
ANISOU 2093  C   ALA A 501     4581   4566   6234    391  -1215   -810       C  
ATOM   2094  O   ALA A 501      62.731 -21.171  12.097  1.00 40.73           O  
ANISOU 2094  O   ALA A 501     4622   4664   6190    368  -1221   -913       O  
ATOM   2095  CB  ALA A 501      59.773 -20.776  12.099  1.00 36.62           C  
ANISOU 2095  CB  ALA A 501     4003   3890   6020    212  -1945  -1342       C  
ATOM   2096  N   GLY A 502      62.207 -22.682  13.684  1.00 44.46           N  
ANISOU 2096  N   GLY A 502     5035   5075   6783    364   -880   -371       N  
ATOM   2097  CA  GLY A 502      63.384 -23.501  13.454  1.00 46.11           C  
ANISOU 2097  CA  GLY A 502     5435   5436   6647    222   -693   -347       C  
ATOM   2098  C   GLY A 502      64.623 -23.002  14.175  1.00 46.67           C  
ANISOU 2098  C   GLY A 502     5864   5683   6184     34   -441   -331       C  
ATOM   2099  O   GLY A 502      65.739 -23.137  13.666  1.00 46.95           O  
ANISOU 2099  O   GLY A 502     5891   5773   6173    -33   -165    -45       O  
ATOM   2100  N   GLY A 503      64.435 -22.428  15.362  1.00 47.06           N  
ANISOU 2100  N   GLY A 503     6235   5652   5993    -85   -582   -482       N  
ATOM   2101  CA  GLY A 503      65.558 -21.925  16.134  1.00 49.73           C  
ANISOU 2101  CA  GLY A 503     6619   5818   6457    -38   -265   -370       C  
ATOM   2102  C   GLY A 503      66.097 -20.635  15.552  1.00 52.00           C  
ANISOU 2102  C   GLY A 503     6956   5904   6898     -5    -39   -223       C  
ATOM   2103  O   GLY A 503      66.564 -19.762  16.286  1.00 53.52           O  
ANISOU 2103  O   GLY A 503     7107   6181   7048     -8     62   -369       O  
ATOM   2104  N   GLY A 504      66.055 -20.526  14.228  1.00 53.18           N  
ANISOU 2104  N   GLY A 504     7086   6060   7058    273     22    181       N  
ATOM   2105  CA  GLY A 504      66.280 -19.266  13.544  1.00 56.08           C  
ANISOU 2105  CA  GLY A 504     7321   6362   7623    692     75    519       C  
ATOM   2106  C   GLY A 504      67.688 -18.701  13.454  1.00 58.47           C  
ANISOU 2106  C   GLY A 504     7536   6748   7932   1257     52    658       C  
ATOM   2107  O   GLY A 504      68.032 -17.767  14.181  1.00 60.64           O  
ANISOU 2107  O   GLY A 504     7589   6962   8487   1350    129    545       O  
ATOM   2108  N   PRO A 505      68.522 -19.276  12.574  1.00 57.17           N  
ANISOU 2108  N   PRO A 505     7680   6786   7254   1695   -102    917       N  
ATOM   2109  CA  PRO A 505      69.673 -18.524  12.071  1.00 55.81           C  
ANISOU 2109  CA  PRO A 505     7718   6764   6721   1826   -220   1026       C  
ATOM   2110  C   PRO A 505      69.279 -17.916  10.727  1.00 55.34           C  
ANISOU 2110  C   PRO A 505     7670   6782   6573   1859   -342    983       C  
ATOM   2111  O   PRO A 505      70.130 -17.653   9.876  1.00 57.13           O  
ANISOU 2111  O   PRO A 505     7826   7076   6805   1809   -258    911       O  
ATOM   2112  CB  PRO A 505      70.748 -19.604  11.877  1.00 56.09           C  
ANISOU 2112  CB  PRO A 505     7795   6787   6730   1838   -146    999       C  
ATOM   2113  CG  PRO A 505      70.147 -20.895  12.410  1.00 56.38           C  
ANISOU 2113  CG  PRO A 505     7814   6841   6768   1854    -94   1077       C  
ATOM   2114  CD  PRO A 505      68.666 -20.714  12.314  1.00 56.56           C  
ANISOU 2114  CD  PRO A 505     7770   6760   6959   1833    -84    992       C  
ATOM   2115  N   GLN A 506      67.977 -17.706  10.552  1.00 52.22           N  
ANISOU 2115  N   GLN A 506     7379   6340   6121   2102   -729   1005       N  
ATOM   2116  CA  GLN A 506      67.424 -17.188   9.309  1.00 51.57           C  
ANISOU 2116  CA  GLN A 506     7097   6074   6421   2157   -930    837       C  
ATOM   2117  C   GLN A 506      67.025 -15.723   9.447  1.00 45.73           C  
ANISOU 2117  C   GLN A 506     6400   5442   5532   2101  -1223    951       C  
ATOM   2118  O   GLN A 506      66.702 -15.257  10.538  1.00 48.61           O  
ANISOU 2118  O   GLN A 506     6569   5549   6350   2096  -1378   1254       O  
ATOM   2119  CB  GLN A 506      66.214 -18.027   8.881  1.00 55.03           C  
ANISOU 2119  CB  GLN A 506     7442   6189   7279   2214   -798    674       C  
ATOM   2120  CG  GLN A 506      65.503 -18.736  10.036  1.00 58.45           C  
ANISOU 2120  CG  GLN A 506     7732   6395   8082   2221   -696    436       C  
ATOM   2121  CD  GLN A 506      64.167 -18.107  10.398  1.00 60.80           C  
ANISOU 2121  CD  GLN A 506     7992   6495   8613   2173   -732    285       C  
ATOM   2122  OE1 GLN A 506      63.607 -18.380  11.462  1.00 60.78           O  
ANISOU 2122  OE1 GLN A 506     8038   6378   8678   2046   -761    382       O  
ATOM   2123  NE2 GLN A 506      63.644 -17.268   9.509  1.00 62.00           N  
ANISOU 2123  NE2 GLN A 506     8130   6626   8800   2173   -682    148       N  
ATOM   2124  N   THR A 507      67.055 -14.999   8.334  1.00 37.51           N  
ANISOU 2124  N   THR A 507     5533   4755   3964   1919  -1242    783       N  
ATOM   2125  CA  THR A 507      66.591 -13.616   8.307  1.00 31.96           C  
ANISOU 2125  CA  THR A 507     4713   3984   3444   1482  -1339    317       C  
ATOM   2126  C   THR A 507      65.734 -13.402   7.066  1.00 25.48           C  
ANISOU 2126  C   THR A 507     4074   2860   2747   1245  -1053     54       C  
ATOM   2127  O   THR A 507      66.135 -13.770   5.967  1.00 27.17           O  
ANISOU 2127  O   THR A 507     4137   3244   2940   1512   -615    -32       O  
ATOM   2128  CB  THR A 507      67.775 -12.623   8.293  1.00 34.48           C  
ANISOU 2128  CB  THR A 507     4804   4287   4010   1152  -1540   -244       C  
ATOM   2129  OG1 THR A 507      68.473 -12.683   9.544  1.00 37.61           O  
ANISOU 2129  OG1 THR A 507     4923   4478   4889   1182  -1211    -16       O  
ATOM   2130  CG2 THR A 507      67.286 -11.204   8.066  1.00 36.24           C  
ANISOU 2130  CG2 THR A 507     4906   4293   4570    956  -1197   -407       C  
ATOM   2131  N   LEU A 508      64.549 -12.828   7.240  1.00 20.44           N  
ANISOU 2131  N   LEU A 508     3414   1479   2873    729   -655    104       N  
ATOM   2132  CA  LEU A 508      63.695 -12.520   6.097  1.00 16.81           C  
ANISOU 2132  CA  LEU A 508     2796   1288   2303    322   -702   -161       C  
ATOM   2133  C   LEU A 508      64.231 -11.279   5.400  1.00 15.77           C  
ANISOU 2133  C   LEU A 508     2351   1111   2530    430   -246      3       C  
ATOM   2134  O   LEU A 508      64.765 -10.386   6.052  1.00 15.41           O  
ANISOU 2134  O   LEU A 508     2110   1356   2389    245   -489     12       O  
ATOM   2135  CB  LEU A 508      62.260 -12.237   6.540  1.00 17.07           C  
ANISOU 2135  CB  LEU A 508     2787   1208   2489   -221     -2   -138       C  
ATOM   2136  CG  LEU A 508      61.427 -13.373   7.123  1.00 19.70           C  
ANISOU 2136  CG  LEU A 508     3263   1766   2457    -23   -101   -209       C  
ATOM   2137  CD1 LEU A 508      60.183 -12.814   7.787  1.00 19.60           C  
ANISOU 2137  CD1 LEU A 508     3204   1978   2266    326   -274   -174       C  
ATOM   2138  CD2 LEU A 508      61.065 -14.382   6.040  1.00 22.66           C  
ANISOU 2138  CD2 LEU A 508     3518   2076   3015    -84   -374  -1075       C  
ATOM   2139  N   PRO A 509      64.083 -11.220   4.071  1.00 15.72           N  
ANISOU 2139  N   PRO A 509     2441    944   2586    403   -198   -115       N  
ATOM   2140  CA  PRO A 509      64.436 -10.009   3.334  1.00 14.57           C  
ANISOU 2140  CA  PRO A 509     2390   1066   2078    476      4     38       C  
ATOM   2141  C   PRO A 509      63.392  -8.925   3.616  1.00 13.36           C  
ANISOU 2141  C   PRO A 509     2084   1065   1926    189   -358   -124       C  
ATOM   2142  O   PRO A 509      62.299  -9.237   4.101  1.00 13.81           O  
ANISOU 2142  O   PRO A 509     1925   1058   2262    111   -263     32       O  
ATOM   2143  CB  PRO A 509      64.369 -10.469   1.877  1.00 16.21           C  
ANISOU 2143  CB  PRO A 509     2713   1399   2045    394    117    -69       C  
ATOM   2144  CG  PRO A 509      63.309 -11.514   1.888  1.00 16.83           C  
ANISOU 2144  CG  PRO A 509     2872   1234   2288   -168   -169     48       C  
ATOM   2145  CD  PRO A 509      63.510 -12.254   3.191  1.00 16.51           C  
ANISOU 2145  CD  PRO A 509     2888   1208   2175     65   -348    -10       C  
ATOM   2146  N   ILE A 510      63.719  -7.673   3.315  1.00 12.37           N  
ANISOU 2146  N   ILE A 510     2046    732   1920    216   -284    -73       N  
ATOM   2147  CA  ILE A 510      62.809  -6.563   3.605  1.00 12.55           C  
ANISOU 2147  CA  ILE A 510     1928    821   2019     36   -369   -308       C  
ATOM   2148  C   ILE A 510      62.028  -6.107   2.374  1.00 12.25           C  
ANISOU 2148  C   ILE A 510     1830    989   1836    -46    -53    -86       C  
ATOM   2149  O   ILE A 510      61.231  -5.167   2.453  1.00 12.45           O  
ANISOU 2149  O   ILE A 510     1781    950   1998     55    121   -194       O  
ATOM   2150  CB  ILE A 510      63.544  -5.343   4.204  1.00 12.70           C  
ANISOU 2150  CB  ILE A 510     2024    966   1834   -288   -312    172       C  
ATOM   2151  CG1 ILE A 510      64.509  -4.743   3.183  1.00 15.03           C  
ANISOU 2151  CG1 ILE A 510     2131   1026   2554   -438   -270     43       C  
ATOM   2152  CG2 ILE A 510      64.251  -5.735   5.490  1.00 14.69           C  
ANISOU 2152  CG2 ILE A 510     2337   1246   1997      7   -590     14       C  
ATOM   2153  CD1 ILE A 510      65.070  -3.404   3.619  1.00 18.56           C  
ANISOU 2153  CD1 ILE A 510     2371   1771   2911   -515   -461    297       C  
ATOM   2154  N   ASN A 511      62.257  -6.770   1.240  1.00 11.74           N  
ANISOU 2154  N   ASN A 511     1700   1032   1729   -116   -299    153       N  
ATOM   2155  CA  ASN A 511      61.632  -6.368  -0.017  1.00 12.23           C  
ANISOU 2155  CA  ASN A 511     1858   1143   1645    -10   -137     68       C  
ATOM   2156  C   ASN A 511      60.558  -7.341  -0.509  1.00 11.22           C  
ANISOU 2156  C   ASN A 511     1715    814   1734   -132   -262     22       C  
ATOM   2157  O   ASN A 511      60.225  -7.363  -1.692  1.00 13.20           O  
ANISOU 2157  O   ASN A 511     2121   1143   1750    142   -156     41       O  
ATOM   2158  CB  ASN A 511      62.685  -6.137  -1.105  1.00 14.45           C  
ANISOU 2158  CB  ASN A 511     2068   1415   2008    180     -7    -65       C  
ATOM   2159  CG  ASN A 511      63.400  -7.412  -1.505  1.00 15.95           C  
ANISOU 2159  CG  ASN A 511     2294   1953   1813    435    358    284       C  
ATOM   2160  OD1 ASN A 511      63.348  -8.412  -0.791  1.00 15.33           O  
ANISOU 2160  OD1 ASN A 511     2387   1479   1959    531    213    100       O  
ATOM   2161  ND2 ASN A 511      64.065  -7.386  -2.655  1.00 21.29           N  
ANISOU 2161  ND2 ASN A 511     2754   2668   2667    795    637    299       N  
ATOM   2162  N   GLY A 512      60.014  -8.137   0.406  1.00 11.59           N  
ANISOU 2162  N   GLY A 512     1518    698   2186    -88    -63   -177       N  
ATOM   2163  CA  GLY A 512      58.928  -9.039   0.069  1.00 11.80           C  
ANISOU 2163  CA  GLY A 512     1615    824   2045    -65   -280   -119       C  
ATOM   2164  C   GLY A 512      57.605  -8.306  -0.071  1.00 11.90           C  
ANISOU 2164  C   GLY A 512     1712    936   1871    -29   -262    -78       C  
ATOM   2165  O   GLY A 512      57.479  -7.130   0.285  1.00 12.66           O  
ANISOU 2165  O   GLY A 512     1936    838   2034    -14   -206   -100       O  
ATOM   2166  N   VAL A 513      56.612  -9.027  -0.575  1.00 11.06           N  
ANISOU 2166  N   VAL A 513     1729    969   1503   -120    -18    -62       N  
ATOM   2167  CA  VAL A 513      55.282  -8.491  -0.821  1.00 11.58           C  
ANISOU 2167  CA  VAL A 513     1721   1065   1612   -152   -135    198       C  
ATOM   2168  C   VAL A 513      54.275  -9.314  -0.029  1.00 10.38           C  
ANISOU 2168  C   VAL A 513     1813    776   1355    -30    -41   -110       C  
ATOM   2169  O   VAL A 513      54.293 -10.539  -0.105  1.00 11.80           O  
ANISOU 2169  O   VAL A 513     2109    738   1636     38    -98   -172       O  
ATOM   2170  CB  VAL A 513      54.932  -8.559  -2.326  1.00 12.39           C  
ANISOU 2170  CB  VAL A 513     1894   1337   1476   -222   -126    474       C  
ATOM   2171  CG1 VAL A 513      53.497  -8.135  -2.557  1.00 15.57           C  
ANISOU 2171  CG1 VAL A 513     1863   2129   1924   -225   -440    408       C  
ATOM   2172  CG2 VAL A 513      55.891  -7.681  -3.138  1.00 13.69           C  
ANISOU 2172  CG2 VAL A 513     2338   1430   1431   -200     83    257       C  
ATOM   2173  N   PHE A 514      53.421  -8.656   0.750  1.00 10.17           N  
ANISOU 2173  N   PHE A 514     1458    816   1591   -116    -28      2       N  
ATOM   2174  CA  PHE A 514      52.353  -9.371   1.443  1.00 10.12           C  
ANISOU 2174  CA  PHE A 514     1434    849   1563   -329    -98     42       C  
ATOM   2175  C   PHE A 514      51.233  -9.676   0.462  1.00 10.41           C  
ANISOU 2175  C   PHE A 514     1703    764   1487   -149   -356    -49       C  
ATOM   2176  O   PHE A 514      50.822  -8.812  -0.315  1.00 11.49           O  
ANISOU 2176  O   PHE A 514     1578   1029   1757     -4   -266    112       O  
ATOM   2177  CB  PHE A 514      51.812  -8.588   2.646  1.00 10.85           C  
ANISOU 2177  CB  PHE A 514     1597    818   1706   -184     19   -384       C  
ATOM   2178  CG  PHE A 514      52.818  -8.388   3.740  1.00 10.38           C  
ANISOU 2178  CG  PHE A 514     1368    922   1652   -247   -338    -70       C  
ATOM   2179  CD1 PHE A 514      52.953  -9.333   4.747  1.00 10.71           C  
ANISOU 2179  CD1 PHE A 514     1510    913   1646   -110   -180     83       C  
ATOM   2180  CD2 PHE A 514      53.628  -7.258   3.765  1.00 11.85           C  
ANISOU 2180  CD2 PHE A 514     1313    870   2319   -108   -167   -329       C  
ATOM   2181  CE1 PHE A 514      53.881  -9.168   5.758  1.00 12.62           C  
ANISOU 2181  CE1 PHE A 514     1612   1410   1772    -27   -563   -380       C  
ATOM   2182  CE2 PHE A 514      54.564  -7.086   4.772  1.00 12.26           C  
ANISOU 2182  CE2 PHE A 514     1552   1022   2085     87   -353   -141       C  
ATOM   2183  CZ  PHE A 514      54.690  -8.046   5.771  1.00 11.83           C  
ANISOU 2183  CZ  PHE A 514     1599    996   1899    -63   -204   -372       C  
ATOM   2184  N   VAL A 515      50.751 -10.917   0.504  1.00 11.29           N  
ANISOU 2184  N   VAL A 515     1798    954   1537   -263   -336   -157       N  
ATOM   2185  CA  VAL A 515      49.641 -11.343  -0.331  1.00 12.15           C  
ANISOU 2185  CA  VAL A 515     2008   1028   1581   -364   -147    -33       C  
ATOM   2186  C   VAL A 515      48.565 -12.006   0.526  1.00 11.63           C  
ANISOU 2186  C   VAL A 515     1758    947   1712   -284   -428    117       C  
ATOM   2187  O   VAL A 515      48.839 -12.938   1.287  1.00 12.26           O  
ANISOU 2187  O   VAL A 515     1890    996   1770    -43   -364    138       O  
ATOM   2188  CB  VAL A 515      50.102 -12.345  -1.413  1.00 14.50           C  
ANISOU 2188  CB  VAL A 515     2234   1690   1585   -690   -259   -146       C  
ATOM   2189  CG1 VAL A 515      48.927 -12.774  -2.283  1.00 16.78           C  
ANISOU 2189  CG1 VAL A 515     2431   2112   1831   -544   -457   -175       C  
ATOM   2190  CG2 VAL A 515      51.207 -11.745  -2.267  1.00 15.79           C  
ANISOU 2190  CG2 VAL A 515     2332   2019   1649   -423    -70    -95       C  
ATOM   2191  N   PHE A 516      47.337 -11.517   0.408  1.00 11.36           N  
ANISOU 2191  N   PHE A 516     1702   1089   1525   -579   -278     71       N  
ATOM   2192  CA  PHE A 516      46.198 -12.149   1.054  1.00 12.16           C  
ANISOU 2192  CA  PHE A 516     1738   1018   1865   -526   -302    -13       C  
ATOM   2193  C   PHE A 516      45.878 -13.507   0.418  1.00 13.15           C  
ANISOU 2193  C   PHE A 516     2081   1078   1838   -441   -303    363       C  
ATOM   2194  O   PHE A 516      45.632 -13.603  -0.788  1.00 15.29           O  
ANISOU 2194  O   PHE A 516     2443   1576   1789   -706   -533    169       O  
ATOM   2195  CB  PHE A 516      44.983 -11.224   0.989  1.00 13.82           C  
ANISOU 2195  CB  PHE A 516     1610   1171   2470   -374   -210    400       C  
ATOM   2196  CG  PHE A 516      43.715 -11.848   1.496  1.00 13.14           C  
ANISOU 2196  CG  PHE A 516     1802   1223   1968   -267   -519     46       C  
ATOM   2197  CD1 PHE A 516      43.598 -12.236   2.822  1.00 14.01           C  
ANISOU 2197  CD1 PHE A 516     1798   1133   2390   -597   -213    183       C  
ATOM   2198  CD2 PHE A 516      42.631 -12.035   0.648  1.00 14.39           C  
ANISOU 2198  CD2 PHE A 516     1685   1449   2334   -628   -428    222       C  
ATOM   2199  CE1 PHE A 516      42.423 -12.802   3.298  1.00 13.52           C  
ANISOU 2199  CE1 PHE A 516     1960   1153   2022   -584   -595   -109       C  
ATOM   2200  CE2 PHE A 516      41.452 -12.602   1.112  1.00 15.13           C  
ANISOU 2200  CE2 PHE A 516     2018   1530   2200   -466   -619    242       C  
ATOM   2201  CZ  PHE A 516      41.349 -12.988   2.439  1.00 14.12           C  
ANISOU 2201  CZ  PHE A 516     2058   1314   1991   -535   -479     43       C  
ATOM   2202  N   ILE A 517      45.899 -14.548   1.245  1.00 11.75           N  
ANISOU 2202  N   ILE A 517     2114    916   1433   -553   -483     53       N  
ATOM   2203  CA  ILE A 517      45.601 -15.912   0.807  1.00 13.37           C  
ANISOU 2203  CA  ILE A 517     2282   1031   1768   -417   -645    -91       C  
ATOM   2204  C   ILE A 517      44.122 -16.230   1.007  1.00 14.19           C  
ANISOU 2204  C   ILE A 517     2336   1311   1744   -408   -573     91       C  
ATOM   2205  O   ILE A 517      43.418 -16.575   0.056  1.00 16.77           O  
ANISOU 2205  O   ILE A 517     2387   1832   2153   -587   -680   -179       O  
ATOM   2206  CB  ILE A 517      46.457 -16.945   1.579  1.00 14.53           C  
ANISOU 2206  CB  ILE A 517     2305    915   2299   -484   -411   -103       C  
ATOM   2207  CG1 ILE A 517      47.947 -16.625   1.426  1.00 14.57           C  
ANISOU 2207  CG1 ILE A 517     2526   1254   1756   -308    -68   -194       C  
ATOM   2208  CG2 ILE A 517      46.125 -18.372   1.133  1.00 16.00           C  
ANISOU 2208  CG2 ILE A 517     2613    905   2561   -208   -554   -226       C  
ATOM   2209  CD1 ILE A 517      48.417 -16.547  -0.015  1.00 15.63           C  
ANISOU 2209  CD1 ILE A 517     2505   1361   2073   -133   -190   -233       C  
ATOM   2210  N   SER A 518      43.656 -16.118   2.245  1.00 13.77           N  
ANISOU 2210  N   SER A 518     2031   1212   1989   -758   -489    293       N  
ATOM   2211  CA  SER A 518      42.256 -16.382   2.557  1.00 14.91           C  
ANISOU 2211  CA  SER A 518     2217   1168   2281   -800   -211    140       C  
ATOM   2212  C   SER A 518      41.940 -15.989   3.984  1.00 13.91           C  
ANISOU 2212  C   SER A 518     1973   1224   2087   -771   -334     41       C  
ATOM   2213  O   SER A 518      42.842 -15.780   4.795  1.00 13.80           O  
ANISOU 2213  O   SER A 518     1941   1258   2044   -578   -657    -35       O  
ATOM   2214  CB  SER A 518      41.936 -17.867   2.383  1.00 19.20           C  
ANISOU 2214  CB  SER A 518     2954   1551   2791   -385   -298    239       C  
ATOM   2215  OG  SER A 518      42.462 -18.601   3.470  1.00 19.28           O  
ANISOU 2215  OG  SER A 518     3490   1306   2527   -117   -155   -111       O  
ATOM   2216  N   TRP A 519      40.653 -15.895   4.288  1.00 14.01           N  
ANISOU 2216  N   TRP A 519     1972   1357   1993   -822   -489    203       N  
ATOM   2217  CA  TRP A 519      40.208 -15.817   5.667  1.00 13.56           C  
ANISOU 2217  CA  TRP A 519     1745   1486   1922   -836   -380    458       C  
ATOM   2218  C   TRP A 519      40.405 -17.197   6.294  1.00 15.06           C  
ANISOU 2218  C   TRP A 519     1959   1502   2259   -901   -464    211       C  
ATOM   2219  O   TRP A 519      40.169 -18.220   5.639  1.00 16.59           O  
ANISOU 2219  O   TRP A 519     2374   1362   2565   -407   -791    107       O  
ATOM   2220  CB  TRP A 519      38.735 -15.396   5.721  1.00 15.84           C  
ANISOU 2220  CB  TRP A 519     1709   1541   2769   -774   -507    184       C  
ATOM   2221  CG  TRP A 519      38.523 -13.997   5.203  1.00 15.32           C  
ANISOU 2221  CG  TRP A 519     1756   1418   2645   -551   -646    365       C  
ATOM   2222  CD1 TRP A 519      38.013 -13.632   3.989  1.00 16.35           C  
ANISOU 2222  CD1 TRP A 519     1892   1383   2937   -243   -616      0       C  
ATOM   2223  CD2 TRP A 519      38.839 -12.782   5.889  1.00 14.50           C  
ANISOU 2223  CD2 TRP A 519     1659   1364   2485   -668   -206    315       C  
ATOM   2224  NE1 TRP A 519      37.991 -12.260   3.879  1.00 16.37           N  
ANISOU 2224  NE1 TRP A 519     1835   1412   2974   -252   -492     53       N  
ATOM   2225  CE2 TRP A 519      38.485 -11.715   5.034  1.00 15.69           C  
ANISOU 2225  CE2 TRP A 519     1699   1496   2765   -633   -457    170       C  
ATOM   2226  CE3 TRP A 519      39.385 -12.493   7.144  1.00 15.02           C  
ANISOU 2226  CE3 TRP A 519     1629   1554   2524   -510   -250   -116       C  
ATOM   2227  CZ2 TRP A 519      38.664 -10.379   5.399  1.00 16.28           C  
ANISOU 2227  CZ2 TRP A 519     1712   1661   2812   -525   -465    110       C  
ATOM   2228  CZ3 TRP A 519      39.557 -11.171   7.504  1.00 15.39           C  
ANISOU 2228  CZ3 TRP A 519     1652   1499   2697   -448   -433    -16       C  
ATOM   2229  CH2 TRP A 519      39.199 -10.129   6.635  1.00 17.39           C  
ANISOU 2229  CH2 TRP A 519     1724   1808   3075   -285   -434    469       C  
ATOM   2230  N   VAL A 520      40.881 -17.222   7.537  1.00 14.68           N  
ANISOU 2230  N   VAL A 520     1876   1613   2088   -878   -480    426       N  
ATOM   2231  CA  VAL A 520      41.125 -18.472   8.244  1.00 15.42           C  
ANISOU 2231  CA  VAL A 520     1992   1736   2132   -736   -492    586       C  
ATOM   2232  C   VAL A 520      40.592 -18.350   9.660  1.00 16.02           C  
ANISOU 2232  C   VAL A 520     2044   1699   2345   -847   -667    639       C  
ATOM   2233  O   VAL A 520      40.348 -17.242  10.144  1.00 15.90           O  
ANISOU 2233  O   VAL A 520     2064   1554   2421   -731   -411    428       O  
ATOM   2234  CB  VAL A 520      42.625 -18.852   8.275  1.00 14.80           C  
ANISOU 2234  CB  VAL A 520     2035   1502   2085   -940   -415    202       C  
ATOM   2235  CG1 VAL A 520      43.151 -19.095   6.867  1.00 15.52           C  
ANISOU 2235  CG1 VAL A 520     2369   1423   2104   -595   -581    411       C  
ATOM   2236  CG2 VAL A 520      43.453 -17.780   9.000  1.00 16.12           C  
ANISOU 2236  CG2 VAL A 520     2058   1658   2409   -942   -247    298       C  
ATOM   2237  N   SER A 521      40.406 -19.480  10.334  1.00 16.37           N  
ANISOU 2237  N   SER A 521     2174   1767   2279   -955   -372    716       N  
ATOM   2238  CA  SER A 521      39.920 -19.420  11.701  1.00 18.25           C  
ANISOU 2238  CA  SER A 521     2370   2000   2563   -942   -366    608       C  
ATOM   2239  C   SER A 521      41.042 -18.991  12.641  1.00 16.48           C  
ANISOU 2239  C   SER A 521     2053   1878   2330   -722    142    857       C  
ATOM   2240  O   SER A 521      42.231 -19.040  12.284  1.00 14.85           O  
ANISOU 2240  O   SER A 521     2091   1388   2162   -595    -65    594       O  
ATOM   2241  CB  SER A 521      39.297 -20.750  12.126  1.00 24.50           C  
ANISOU 2241  CB  SER A 521     2888   2144   4275   -807   -832    587       C  
ATOM   2242  OG  SER A 521      40.167 -21.520  12.924  1.00 23.39           O  
ANISOU 2242  OG  SER A 521     2817   1838   4233   -802  -1200    136       O  
ATOM   2243  N   ARG A 522      40.670 -18.550  13.834  1.00 16.39           N  
ANISOU 2243  N   ARG A 522     2199   1614   2412   -789     31    454       N  
ATOM   2244  CA  ARG A 522      41.657 -18.131  14.823  1.00 15.81           C  
ANISOU 2244  CA  ARG A 522     2351   1433   2224   -770    169    298       C  
ATOM   2245  C   ARG A 522      42.601 -19.272  15.180  1.00 13.48           C  
ANISOU 2245  C   ARG A 522     2377   1143   1602   -573   -166     13       C  
ATOM   2246  O   ARG A 522      43.692 -19.032  15.684  1.00 14.50           O  
ANISOU 2246  O   ARG A 522     2338   1166   2006   -595   -220    -13       O  
ATOM   2247  CB  ARG A 522      40.963 -17.615  16.082  1.00 18.66           C  
ANISOU 2247  CB  ARG A 522     2637   1816   2636   -494    489    431       C  
ATOM   2248  CG  ARG A 522      40.036 -18.623  16.747  1.00 21.78           C  
ANISOU 2248  CG  ARG A 522     2976   2252   3047   -357   1322    564       C  
ATOM   2249  CD  ARG A 522      39.076 -17.906  17.691  1.00 26.69           C  
ANISOU 2249  CD  ARG A 522     3551   2726   3863    -78   1900    729       C  
ATOM   2250  NE  ARG A 522      38.100 -18.811  18.291  1.00 33.00           N  
ANISOU 2250  NE  ARG A 522     3932   3383   5222    216   1781    571       N  
ATOM   2251  CZ  ARG A 522      36.913 -19.094  17.760  1.00 35.73           C  
ANISOU 2251  CZ  ARG A 522     4132   3451   5991    259   2081    915       C  
ATOM   2252  NH1 ARG A 522      36.552 -18.545  16.608  1.00 36.31           N  
ANISOU 2252  NH1 ARG A 522     4236   3641   5918    570   1873    882       N  
ATOM   2253  NH2 ARG A 522      36.087 -19.931  18.380  1.00 36.48           N  
ANISOU 2253  NH2 ARG A 522     4154   3164   6542    113   2486    816       N  
ATOM   2254  N   TYR A 523      42.169 -20.510  14.922  1.00 14.26           N  
ANISOU 2254  N   TYR A 523     2304   1296   1818   -744   -273    135       N  
ATOM   2255  CA  TYR A 523      42.953 -21.695  15.264  1.00 14.26           C  
ANISOU 2255  CA  TYR A 523     2322   1158   1938   -778    -32    243       C  
ATOM   2256  C   TYR A 523      44.018 -22.055  14.234  1.00 13.36           C  
ANISOU 2256  C   TYR A 523     2290   1376   1408   -591     21    293       C  
ATOM   2257  O   TYR A 523      44.811 -22.967  14.457  1.00 14.62           O  
ANISOU 2257  O   TYR A 523     2342   1307   1906   -521    -54    305       O  
ATOM   2258  CB  TYR A 523      42.030 -22.891  15.536  1.00 14.72           C  
ANISOU 2258  CB  TYR A 523     2512   1192   1888   -819     52    186       C  
ATOM   2259  CG  TYR A 523      41.131 -22.651  16.725  1.00 15.87           C  
ANISOU 2259  CG  TYR A 523     2839   1424   1766   -745    277    194       C  
ATOM   2260  CD1 TYR A 523      41.622 -22.766  18.020  1.00 17.30           C  
ANISOU 2260  CD1 TYR A 523     3149   1746   1679   -537    330    291       C  
ATOM   2261  CD2 TYR A 523      39.810 -22.266  16.558  1.00 16.73           C  
ANISOU 2261  CD2 TYR A 523     2951   1379   2027   -841    235     72       C  
ATOM   2262  CE1 TYR A 523      40.816 -22.529  19.112  1.00 18.84           C  
ANISOU 2262  CE1 TYR A 523     3287   2196   1674   -587    652    113       C  
ATOM   2263  CE2 TYR A 523      38.993 -22.022  17.653  1.00 17.91           C  
ANISOU 2263  CE2 TYR A 523     3063   1415   2326   -771    750    118       C  
ATOM   2264  CZ  TYR A 523      39.507 -22.152  18.925  1.00 20.09           C  
ANISOU 2264  CZ  TYR A 523     3332   1893   2408   -891    967     72       C  
ATOM   2265  OH  TYR A 523      38.719 -21.911  20.025  1.00 23.87           O  
ANISOU 2265  OH  TYR A 523     3804   2315   2951   -799   1080   -196       O  
ATOM   2266  N   TYR A 524      44.044 -21.341  13.112  1.00 13.06           N  
ANISOU 2266  N   TYR A 524     2087   1353   1523   -894     77     37       N  
ATOM   2267  CA  TYR A 524      45.067 -21.585  12.098  1.00 12.67           C  
ANISOU 2267  CA  TYR A 524     2007   1425   1383   -583   -170    415       C  
ATOM   2268  C   TYR A 524      46.448 -21.489  12.748  1.00 13.21           C  
ANISOU 2268  C   TYR A 524     1936   1456   1627   -445   -236    255       C  
ATOM   2269  O   TYR A 524      46.796 -20.472  13.352  1.00 14.35           O  
ANISOU 2269  O   TYR A 524     1880   1279   2293   -579   -407   -211       O  
ATOM   2270  CB  TYR A 524      44.943 -20.578  10.952  1.00 13.21           C  
ANISOU 2270  CB  TYR A 524     2099   1287   1633   -374    -26    560       C  
ATOM   2271  CG  TYR A 524      45.851 -20.858   9.775  1.00 12.50           C  
ANISOU 2271  CG  TYR A 524     2012   1155   1581   -379    -59    399       C  
ATOM   2272  CD1 TYR A 524      45.354 -21.460   8.621  1.00 12.91           C  
ANISOU 2272  CD1 TYR A 524     2200   1004   1700   -253   -324    175       C  
ATOM   2273  CD2 TYR A 524      47.202 -20.513   9.808  1.00 13.49           C  
ANISOU 2273  CD2 TYR A 524     1989   1061   2076   -361     71    315       C  
ATOM   2274  CE1 TYR A 524      46.173 -21.718   7.539  1.00 13.59           C  
ANISOU 2274  CE1 TYR A 524     2100   1100   1961   -146   -184    202       C  
ATOM   2275  CE2 TYR A 524      48.031 -20.764   8.727  1.00 12.96           C  
ANISOU 2275  CE2 TYR A 524     2140   1053   1732   -240   -139    135       C  
ATOM   2276  CZ  TYR A 524      47.510 -21.370   7.593  1.00 13.06           C  
ANISOU 2276  CZ  TYR A 524     2220   1081   1661   -132    133    286       C  
ATOM   2277  OH  TYR A 524      48.317 -21.636   6.508  1.00 13.51           O  
ANISOU 2277  OH  TYR A 524     2244    896   1993   -239   -333     71       O  
ATOM   2278  N   GLN A 525      47.233 -22.552  12.629  1.00 12.41           N  
ANISOU 2278  N   GLN A 525     2128   1109   1477   -564   -410    271       N  
ATOM   2279  CA  GLN A 525      48.507 -22.638  13.333  1.00 12.49           C  
ANISOU 2279  CA  GLN A 525     2322   1007   1416   -332   -476     89       C  
ATOM   2280  C   GLN A 525      49.682 -22.219  12.452  1.00 12.26           C  
ANISOU 2280  C   GLN A 525     2290    978   1390   -521   -326    191       C  
ATOM   2281  O   GLN A 525      49.965 -22.855  11.433  1.00 13.25           O  
ANISOU 2281  O   GLN A 525     2205   1038   1792   -682   -315    -57       O  
ATOM   2282  CB  GLN A 525      48.730 -24.073  13.816  1.00 16.77           C  
ANISOU 2282  CB  GLN A 525     2645   1252   2473   -358   -646    290       C  
ATOM   2283  CG  GLN A 525      49.945 -24.218  14.694  1.00 23.68           C  
ANISOU 2283  CG  GLN A 525     3668   1994   3333    -39    -58    397       C  
ATOM   2284  CD  GLN A 525      49.833 -23.403  15.961  1.00 26.45           C  
ANISOU 2284  CD  GLN A 525     4389   2105   3555   -120   -298    199       C  
ATOM   2285  OE1 GLN A 525      49.072 -23.749  16.867  1.00 28.16           O  
ANISOU 2285  OE1 GLN A 525     4488   3099   3113    350   -447   -179       O  
ATOM   2286  NE2 GLN A 525      50.586 -22.310  16.032  1.00 28.04           N  
ANISOU 2286  NE2 GLN A 525     4942   1950   3760   -282     33    696       N  
ATOM   2287  N   LEU A 526      50.361 -21.139  12.831  1.00 13.06           N  
ANISOU 2287  N   LEU A 526     2165    954   1844   -625   -302    165       N  
ATOM   2288  CA  LEU A 526      51.528 -20.688  12.088  1.00 13.22           C  
ANISOU 2288  CA  LEU A 526     2096    933   1992   -571   -329     69       C  
ATOM   2289  C   LEU A 526      52.756 -21.492  12.489  1.00 14.36           C  
ANISOU 2289  C   LEU A 526     2313   1377   1766    -44   -118    207       C  
ATOM   2290  O   LEU A 526      52.839 -21.979  13.625  1.00 14.70           O  
ANISOU 2290  O   LEU A 526     2232   1287   2065   -409   -214    295       O  
ATOM   2291  CB  LEU A 526      51.771 -19.203  12.335  1.00 13.67           C  
ANISOU 2291  CB  LEU A 526     2191    910   2093   -543   -385     34       C  
ATOM   2292  CG  LEU A 526      50.634 -18.263  11.930  1.00 12.96           C  
ANISOU 2292  CG  LEU A 526     2117    916   1890   -301   -629   -113       C  
ATOM   2293  CD1 LEU A 526      50.929 -16.848  12.434  1.00 14.50           C  
ANISOU 2293  CD1 LEU A 526     2041    939   2528   -413   -443   -198       C  
ATOM   2294  CD2 LEU A 526      50.461 -18.266  10.427  1.00 15.57           C  
ANISOU 2294  CD2 LEU A 526     2457   1682   1775    -42   -378     -4       C  
ATOM   2295  OXT LEU A 526      53.676 -21.681  11.681  1.00 15.36           O  
ANISOU 2295  OXT LEU A 526     2492   1451   1891     24   -356     85       O  
TER    2296      LEU A 526                                                      
ATOM   2297  N   LYS B 230      42.856  -7.282 -14.969  1.00 43.62           N  
ANISOU 2297  N   LYS B 230     6505   3793   6276    -57    400   1370       N  
ATOM   2298  CA  LYS B 230      42.488  -6.416 -13.854  1.00 41.60           C  
ANISOU 2298  CA  LYS B 230     6496   3578   5733     37    162   1129       C  
ATOM   2299  C   LYS B 230      41.894  -5.102 -14.352  1.00 36.56           C  
ANISOU 2299  C   LYS B 230     6079   3041   4772   -257   -140    775       C  
ATOM   2300  O   LYS B 230      42.518  -4.397 -15.142  1.00 34.53           O  
ANISOU 2300  O   LYS B 230     6080   2926   4112   -362    157    595       O  
ATOM   2301  CB  LYS B 230      43.700  -6.152 -12.957  1.00 44.64           C  
ANISOU 2301  CB  LYS B 230     6803   3945   6213    248    264   1278       C  
ATOM   2302  CG  LYS B 230      43.469  -5.094 -11.885  1.00 46.92           C  
ANISOU 2302  CG  LYS B 230     7081   4199   6546    570    342   1223       C  
ATOM   2303  CD  LYS B 230      43.974  -5.558 -10.526  1.00 50.57           C  
ANISOU 2303  CD  LYS B 230     7322   4682   7209    683    368   1208       C  
ATOM   2304  CE  LYS B 230      45.388  -6.111 -10.614  1.00 53.46           C  
ANISOU 2304  CE  LYS B 230     7530   4947   7836    783    437   1505       C  
ATOM   2305  NZ  LYS B 230      45.980  -6.367  -9.269  1.00 55.67           N  
ANISOU 2305  NZ  LYS B 230     7643   5133   8376    848    434   1437       N  
ATOM   2306  N   PRO B 231      40.676  -4.779 -13.894  1.00 33.71           N  
ANISOU 2306  N   PRO B 231     5641   2676   4491   -451   -715    309       N  
ATOM   2307  CA  PRO B 231      39.963  -3.567 -14.314  1.00 30.57           C  
ANISOU 2307  CA  PRO B 231     5304   2531   3781   -565  -1061   -226       C  
ATOM   2308  C   PRO B 231      40.620  -2.299 -13.777  1.00 27.70           C  
ANISOU 2308  C   PRO B 231     4844   2336   3345   -417  -1037   -200       C  
ATOM   2309  O   PRO B 231      41.072  -2.255 -12.632  1.00 29.16           O  
ANISOU 2309  O   PRO B 231     5039   2468   3572   -228  -1068    -30       O  
ATOM   2310  CB  PRO B 231      38.571  -3.740 -13.692  1.00 33.12           C  
ANISOU 2310  CB  PRO B 231     5463   2589   4531   -621  -1128   -473       C  
ATOM   2311  CG  PRO B 231      38.457  -5.200 -13.383  1.00 35.88           C  
ANISOU 2311  CG  PRO B 231     5611   2904   5117   -329   -986     68       C  
ATOM   2312  CD  PRO B 231      39.846  -5.626 -13.023  1.00 36.07           C  
ANISOU 2312  CD  PRO B 231     5614   2964   5125   -427   -893    251       C  
ATOM   2313  N   PHE B 232      40.660  -1.267 -14.608  1.00 23.09           N  
ANISOU 2313  N   PHE B 232     4176   1972   2624   -561   -861   -130       N  
ATOM   2314  CA  PHE B 232      41.225   0.008 -14.198  1.00 21.82           C  
ANISOU 2314  CA  PHE B 232     3564   2187   2540   -369   -798   -151       C  
ATOM   2315  C   PHE B 232      40.334   0.695 -13.168  1.00 20.21           C  
ANISOU 2315  C   PHE B 232     3201   2288   2190   -455  -1000     48       C  
ATOM   2316  O   PHE B 232      39.118   0.525 -13.174  1.00 22.02           O  
ANISOU 2316  O   PHE B 232     3136   2330   2900   -798  -1311     44       O  
ATOM   2317  CB  PHE B 232      41.423   0.909 -15.417  1.00 20.51           C  
ANISOU 2317  CB  PHE B 232     3244   2224   2325   -101   -712    295       C  
ATOM   2318  CG  PHE B 232      42.031   2.240 -15.093  1.00 18.98           C  
ANISOU 2318  CG  PHE B 232     2814   2193   2202   -549   -600   -164       C  
ATOM   2319  CD1 PHE B 232      43.373   2.336 -14.752  1.00 18.70           C  
ANISOU 2319  CD1 PHE B 232     2659   2452   1993   -487   -302    241       C  
ATOM   2320  CD2 PHE B 232      41.269   3.394 -15.134  1.00 18.75           C  
ANISOU 2320  CD2 PHE B 232     2698   2266   2161   -396   -593     68       C  
ATOM   2321  CE1 PHE B 232      43.944   3.564 -14.451  1.00 19.31           C  
ANISOU 2321  CE1 PHE B 232     2671   2739   1927   -188   -289    230       C  
ATOM   2322  CE2 PHE B 232      41.832   4.626 -14.836  1.00 18.41           C  
ANISOU 2322  CE2 PHE B 232     2642   2111   2243   -626   -305    -20       C  
ATOM   2323  CZ  PHE B 232      43.171   4.712 -14.496  1.00 18.29           C  
ANISOU 2323  CZ  PHE B 232     2566   2491   1892   -566   -505    -26       C  
ATOM   2324  N   SER B 233      40.951   1.454 -12.269  1.00 17.85           N  
ANISOU 2324  N   SER B 233     2833   1943   2006   -388   -677    -15       N  
ATOM   2325  CA  SER B 233      40.214   2.268 -11.315  1.00 17.17           C  
ANISOU 2325  CA  SER B 233     2375   1870   2280   -660   -541    314       C  
ATOM   2326  C   SER B 233      41.106   3.389 -10.828  1.00 14.86           C  
ANISOU 2326  C   SER B 233     2010   1619   2018   -787   -475    213       C  
ATOM   2327  O   SER B 233      42.328   3.342 -11.007  1.00 15.90           O  
ANISOU 2327  O   SER B 233     1922   1969   2150   -309   -461     56       O  
ATOM   2328  CB  SER B 233      39.753   1.442 -10.114  1.00 18.64           C  
ANISOU 2328  CB  SER B 233     2184   1981   2915   -700   -887    452       C  
ATOM   2329  OG  SER B 233      40.847   0.926  -9.370  1.00 18.44           O  
ANISOU 2329  OG  SER B 233     2055   2164   2786   -902   -999    292       O  
ATOM   2330  N   VAL B 234      40.495   4.403 -10.226  1.00 15.27           N  
ANISOU 2330  N   VAL B 234     2050   1840   1911   -306   -614     -2       N  
ATOM   2331  CA  VAL B 234      41.250   5.428  -9.511  1.00 13.58           C  
ANISOU 2331  CA  VAL B 234     1783   1800   1575   -325   -288    -13       C  
ATOM   2332  C   VAL B 234      40.854   5.353  -8.035  1.00 13.93           C  
ANISOU 2332  C   VAL B 234     1573   1661   2058   -539   -336     66       C  
ATOM   2333  O   VAL B 234      39.841   4.737  -7.696  1.00 15.09           O  
ANISOU 2333  O   VAL B 234     1698   1882   2151   -416   -224    263       O  
ATOM   2334  CB  VAL B 234      41.010   6.843 -10.105  1.00 14.72           C  
ANISOU 2334  CB  VAL B 234     1610   1804   2180    -37     40    597       C  
ATOM   2335  CG1 VAL B 234      41.465   6.884 -11.566  1.00 14.39           C  
ANISOU 2335  CG1 VAL B 234     1402   2228   1836   -149    347    443       C  
ATOM   2336  CG2 VAL B 234      39.549   7.246  -9.967  1.00 15.21           C  
ANISOU 2336  CG2 VAL B 234     1306   1957   2516    -71    311    314       C  
ATOM   2337  N   PRO B 235      41.655   5.952  -7.145  1.00 13.82           N  
ANISOU 2337  N   PRO B 235     1586   1811   1852   -313   -229     56       N  
ATOM   2338  CA  PRO B 235      41.351   5.840  -5.714  1.00 15.42           C  
ANISOU 2338  CA  PRO B 235     1453   2141   2265   -251   -526    163       C  
ATOM   2339  C   PRO B 235      39.959   6.354  -5.356  1.00 15.49           C  
ANISOU 2339  C   PRO B 235     1872   2155   1859   -448   -561    592       C  
ATOM   2340  O   PRO B 235      39.491   7.370  -5.889  1.00 16.49           O  
ANISOU 2340  O   PRO B 235     1894   2318   2052    -85   -256    385       O  
ATOM   2341  CB  PRO B 235      42.423   6.716  -5.064  1.00 16.29           C  
ANISOU 2341  CB  PRO B 235     1619   1921   2647    -98   -499   -286       C  
ATOM   2342  CG  PRO B 235      43.568   6.673  -6.027  1.00 15.34           C  
ANISOU 2342  CG  PRO B 235     1519   1997   2311   -219   -126     55       C  
ATOM   2343  CD  PRO B 235      42.921   6.667  -7.386  1.00 14.54           C  
ANISOU 2343  CD  PRO B 235     1384   2080   2059   -445   -524   -251       C  
ATOM   2344  N   ASN B 236      39.310   5.614  -4.467  1.00 19.14           N  
ANISOU 2344  N   ASN B 236     2474   2493   2303   -751    -82    504       N  
ATOM   2345  CA  ASN B 236      38.040   5.976  -3.867  1.00 22.64           C  
ANISOU 2345  CA  ASN B 236     3199   3014   2390   -473    305    376       C  
ATOM   2346  C   ASN B 236      38.305   6.761  -2.580  1.00 22.12           C  
ANISOU 2346  C   ASN B 236     3138   3101   2163   -185    792    416       C  
ATOM   2347  O   ASN B 236      37.862   6.381  -1.493  1.00 26.74           O  
ANISOU 2347  O   ASN B 236     3483   3852   2825    -70    745    439       O  
ATOM   2348  CB  ASN B 236      37.265   4.692  -3.566  1.00 27.35           C  
ANISOU 2348  CB  ASN B 236     3589   3160   3642   -706    196    -51       C  
ATOM   2349  CG  ASN B 236      35.932   4.949  -2.923  1.00 32.94           C  
ANISOU 2349  CG  ASN B 236     4268   3571   4675   -385    362    516       C  
ATOM   2350  OD1 ASN B 236      35.260   5.932  -3.231  1.00 35.95           O  
ANISOU 2350  OD1 ASN B 236     4371   4069   5219   -206    134    679       O  
ATOM   2351  ND2 ASN B 236      35.538   4.061  -2.017  1.00 34.50           N  
ANISOU 2351  ND2 ASN B 236     4625   3635   4846   -329    109    702       N  
ATOM   2352  N   ILE B 237      39.068   7.842  -2.722  1.00 18.80           N  
ANISOU 2352  N   ILE B 237     2692   2372   2079     94    325    573       N  
ATOM   2353  CA  ILE B 237      39.464   8.711  -1.619  1.00 17.25           C  
ANISOU 2353  CA  ILE B 237     1993   2513   2047    124   -141    504       C  
ATOM   2354  C   ILE B 237      39.197  10.152  -2.030  1.00 16.05           C  
ANISOU 2354  C   ILE B 237     1701   2350   2045    171    -52    453       C  
ATOM   2355  O   ILE B 237      39.541  10.548  -3.144  1.00 15.29           O  
ANISOU 2355  O   ILE B 237     1562   2379   1868     20   -112    470       O  
ATOM   2356  CB  ILE B 237      40.978   8.582  -1.322  1.00 18.52           C  
ANISOU 2356  CB  ILE B 237     2219   2501   2317    101   -184    327       C  
ATOM   2357  CG1 ILE B 237      41.353   7.132  -1.013  1.00 20.68           C  
ANISOU 2357  CG1 ILE B 237     2616   2662   2578    247    260    497       C  
ATOM   2358  CG2 ILE B 237      41.401   9.519  -0.183  1.00 17.61           C  
ANISOU 2358  CG2 ILE B 237     2041   2364   2284      9   -278     95       C  
ATOM   2359  CD1 ILE B 237      40.709   6.599   0.244  1.00 25.47           C  
ANISOU 2359  CD1 ILE B 237     3045   2796   3834    471     -2    422       C  
ATOM   2360  N   PRO B 238      38.566  10.938  -1.148  1.00 15.31           N  
ANISOU 2360  N   PRO B 238     1546   2429   1842    166     58    503       N  
ATOM   2361  CA  PRO B 238      38.330  12.349  -1.472  1.00 14.55           C  
ANISOU 2361  CA  PRO B 238     1365   2181   1980     61    194    354       C  
ATOM   2362  C   PRO B 238      39.637  13.076  -1.787  1.00 13.98           C  
ANISOU 2362  C   PRO B 238     1473   2026   1813    270    110    460       C  
ATOM   2363  O   PRO B 238      40.675  12.825  -1.159  1.00 14.79           O  
ANISOU 2363  O   PRO B 238     1348   2140   2132    125   -331    343       O  
ATOM   2364  CB  PRO B 238      37.683  12.902  -0.197  1.00 17.39           C  
ANISOU 2364  CB  PRO B 238     1599   2653   2356    340    -43    381       C  
ATOM   2365  CG  PRO B 238      37.081  11.702   0.479  1.00 17.45           C  
ANISOU 2365  CG  PRO B 238     1718   2560   2353    216    329    753       C  
ATOM   2366  CD  PRO B 238      38.026  10.571   0.172  1.00 17.35           C  
ANISOU 2366  CD  PRO B 238     1694   2658   2240    434    204    545       C  
ATOM   2367  N   MET B 239      39.583  13.969  -2.770  1.00 12.78           N  
ANISOU 2367  N   MET B 239     1214   1876   1766    -45    275    442       N  
ATOM   2368  CA  MET B 239      40.775  14.671  -3.230  1.00 12.49           C  
ANISOU 2368  CA  MET B 239     1204   1987   1555    145     -3    527       C  
ATOM   2369  C   MET B 239      41.515  15.367  -2.094  1.00 11.94           C  
ANISOU 2369  C   MET B 239     1060   1883   1593    198    -19    310       C  
ATOM   2370  O   MET B 239      42.748  15.358  -2.053  1.00 12.76           O  
ANISOU 2370  O   MET B 239     1145   2033   1669    378      8    358       O  
ATOM   2371  CB  MET B 239      40.424  15.685  -4.320  1.00 13.85           C  
ANISOU 2371  CB  MET B 239     1352   2076   1833     52     80    648       C  
ATOM   2372  CG  MET B 239      41.645  16.346  -4.942  1.00 14.57           C  
ANISOU 2372  CG  MET B 239     1367   2271   1896    181      3    650       C  
ATOM   2373  SD  MET B 239      41.231  17.554  -6.211  1.00 15.07           S  
ANISOU 2373  SD  MET B 239     1466   2462   1797    223    -32    336       S  
ATOM   2374  CE  MET B 239      40.527  18.864  -5.213  1.00 17.18           C  
ANISOU 2374  CE  MET B 239     1718   2594   2216    508    263     93       C  
ATOM   2375  N   ASN B 240      40.770  15.972  -1.174  1.00 12.93           N  
ANISOU 2375  N   ASN B 240     1490   1906   1516    532     77    137       N  
ATOM   2376  CA  ASN B 240      41.400  16.737  -0.098  1.00 13.63           C  
ANISOU 2376  CA  ASN B 240     1414   2008   1757    691   -192    122       C  
ATOM   2377  C   ASN B 240      41.998  15.899   1.032  1.00 12.72           C  
ANISOU 2377  C   ASN B 240     1264   1856   1714    344     17    369       C  
ATOM   2378  O   ASN B 240      42.479  16.450   2.020  1.00 13.94           O  
ANISOU 2378  O   ASN B 240     1420   2008   1867    493   -101    276       O  
ATOM   2379  CB  ASN B 240      40.454  17.810   0.455  1.00 15.90           C  
ANISOU 2379  CB  ASN B 240     1470   2447   2123   1002    -89    223       C  
ATOM   2380  CG  ASN B 240      39.259  17.227   1.173  1.00 17.22           C  
ANISOU 2380  CG  ASN B 240     1672   2765   2104    829      9     91       C  
ATOM   2381  OD1 ASN B 240      38.813  16.121   0.873  1.00 16.86           O  
ANISOU 2381  OD1 ASN B 240     1476   2789   2140    658     48    142       O  
ATOM   2382  ND2 ASN B 240      38.728  17.979   2.131  1.00 19.34           N  
ANISOU 2382  ND2 ASN B 240     1889   3044   2416    620     74   -257       N  
ATOM   2383  N   LEU B 241      41.963  14.575   0.886  1.00 12.28           N  
ANISOU 2383  N   LEU B 241     1151   1672   1842    371    240    277       N  
ATOM   2384  CA  LEU B 241      42.660  13.674   1.810  1.00 12.00           C  
ANISOU 2384  CA  LEU B 241     1292   1729   1536    150    348    364       C  
ATOM   2385  C   LEU B 241      43.939  13.117   1.189  1.00 11.02           C  
ANISOU 2385  C   LEU B 241     1266   1522   1398    216    190     28       C  
ATOM   2386  O   LEU B 241      44.684  12.388   1.842  1.00 12.23           O  
ANISOU 2386  O   LEU B 241     1465   1498   1683    414    -33    139       O  
ATOM   2387  CB  LEU B 241      41.768  12.502   2.214  1.00 15.06           C  
ANISOU 2387  CB  LEU B 241     1712   2262   1748   -183    435    306       C  
ATOM   2388  CG  LEU B 241      40.503  12.847   2.982  1.00 21.15           C  
ANISOU 2388  CG  LEU B 241     2305   2650   3080   -278   1076    517       C  
ATOM   2389  CD1 LEU B 241      39.868  11.586   3.566  1.00 21.53           C  
ANISOU 2389  CD1 LEU B 241     2436   2803   2942    -75   1099    716       C  
ATOM   2390  CD2 LEU B 241      40.820  13.841   4.060  1.00 26.19           C  
ANISOU 2390  CD2 LEU B 241     3036   3262   3654    211   1226    -18       C  
ATOM   2391  N   MET B 242      44.186  13.451  -0.074  1.00 10.03           N  
ANISOU 2391  N   MET B 242     1064   1329   1419     29    169     30       N  
ATOM   2392  CA  MET B 242      45.365  12.977  -0.778  1.00  9.58           C  
ANISOU 2392  CA  MET B 242     1130   1359   1149     41   -118   -120       C  
ATOM   2393  C   MET B 242      46.466  14.016  -0.783  1.00  9.84           C  
ANISOU 2393  C   MET B 242      992   1167   1579    226    133   -145       C  
ATOM   2394  O   MET B 242      46.211  15.209  -0.597  1.00 11.34           O  
ANISOU 2394  O   MET B 242     1195   1245   1869    208    -17    -16       O  
ATOM   2395  CB  MET B 242      45.013  12.590  -2.210  1.00 12.87           C  
ANISOU 2395  CB  MET B 242     1180   2040   1670     76   -297   -306       C  
ATOM   2396  CG  MET B 242      44.089  11.391  -2.267  1.00 15.49           C  
ANISOU 2396  CG  MET B 242     1297   2793   1794   -342   -229   -938       C  
ATOM   2397  SD  MET B 242      43.793  10.769  -3.923  1.00 21.58           S  
ANISOU 2397  SD  MET B 242     1409   4429   2359     83   -169  -1224       S  
ATOM   2398  CE  MET B 242      42.570  11.927  -4.514  1.00 23.40           C  
ANISOU 2398  CE  MET B 242     1707   4637   2545    473   -330  -1090       C  
ATOM   2399  N   SER B 243      47.692  13.545  -0.981  1.00 10.04           N  
ANISOU 2399  N   SER B 243      966   1202   1647     19     -8    103       N  
ATOM   2400  CA  SER B 243      48.864  14.416  -0.978  1.00  9.36           C  
ANISOU 2400  CA  SER B 243      954   1161   1440    131     30    142       C  
ATOM   2401  C   SER B 243      49.210  14.925  -2.375  1.00  8.36           C  
ANISOU 2401  C   SER B 243      913   1024   1237    133   -101   -285       C  
ATOM   2402  O   SER B 243      48.995  14.239  -3.379  1.00  9.66           O  
ANISOU 2402  O   SER B 243     1112   1030   1527    233   -120    -79       O  
ATOM   2403  CB  SER B 243      50.067  13.653  -0.408  1.00 10.49           C  
ANISOU 2403  CB  SER B 243      846   1209   1929   -216   -143     72       C  
ATOM   2404  OG  SER B 243      51.227  14.472  -0.350  1.00 10.50           O  
ANISOU 2404  OG  SER B 243     1185   1182   1621    296    -17   -153       O  
ATOM   2405  N   ASN B 244      49.751  16.135  -2.427  1.00  8.91           N  
ANISOU 2405  N   ASN B 244      927    800   1658    120    210     65       N  
ATOM   2406  CA  ASN B 244      50.504  16.601  -3.582  1.00  9.05           C  
ANISOU 2406  CA  ASN B 244     1040    744   1652    219    230    -55       C  
ATOM   2407  C   ASN B 244      51.609  15.572  -3.886  1.00  7.73           C  
ANISOU 2407  C   ASN B 244     1069    665   1202     60    214     -9       C  
ATOM   2408  O   ASN B 244      52.090  14.878  -2.970  1.00  9.45           O  
ANISOU 2408  O   ASN B 244     1197   1017   1376    169     41    121       O  
ATOM   2409  CB  ASN B 244      51.125  17.960  -3.238  1.00  8.87           C  
ANISOU 2409  CB  ASN B 244     1369    611   1391     71    -40    199       C  
ATOM   2410  CG  ASN B 244      51.442  18.807  -4.461  1.00  8.68           C  
ANISOU 2410  CG  ASN B 244     1140    843   1313    229    -49     55       C  
ATOM   2411  OD1 ASN B 244      52.423  18.561  -5.160  1.00  9.66           O  
ANISOU 2411  OD1 ASN B 244     1077    977   1615    269    124    -27       O  
ATOM   2412  ND2 ASN B 244      50.633  19.845  -4.695  1.00 10.17           N  
ANISOU 2412  ND2 ASN B 244     1330    812   1723    301    -91     13       N  
ATOM   2413  N   SER B 245      52.010  15.456  -5.149  1.00  7.74           N  
ANISOU 2413  N   SER B 245      987    665   1290    153    264   -108       N  
ATOM   2414  CA  SER B 245      53.113  14.560  -5.480  1.00  8.65           C  
ANISOU 2414  CA  SER B 245     1117    891   1276     94    -61   -196       C  
ATOM   2415  C   SER B 245      54.482  15.245  -5.536  1.00  8.67           C  
ANISOU 2415  C   SER B 245      923    857   1515     66   -177   -201       C  
ATOM   2416  O   SER B 245      55.504  14.566  -5.700  1.00 10.32           O  
ANISOU 2416  O   SER B 245     1236    974   1711    242    142    -47       O  
ATOM   2417  CB  SER B 245      52.838  13.812  -6.784  1.00  9.57           C  
ANISOU 2417  CB  SER B 245     1279   1004   1352    174     27     -9       C  
ATOM   2418  OG  SER B 245      52.473  14.710  -7.819  1.00  9.79           O  
ANISOU 2418  OG  SER B 245     1553    963   1204    290     30    140       O  
ATOM   2419  N   ARG B 246      54.516  16.572  -5.389  1.00  8.53           N  
ANISOU 2419  N   ARG B 246     1165    614   1463    -97    138    -65       N  
ATOM   2420  CA  ARG B 246      55.781  17.305  -5.429  1.00  9.22           C  
ANISOU 2420  CA  ARG B 246     1335    780   1388    142     71    369       C  
ATOM   2421  C   ARG B 246      56.234  17.826  -4.060  1.00  8.21           C  
ANISOU 2421  C   ARG B 246     1192    620   1307    100   -122   -161       C  
ATOM   2422  O   ARG B 246      57.414  18.128  -3.864  1.00  9.45           O  
ANISOU 2422  O   ARG B 246      993    876   1719   -111    -13     66       O  
ATOM   2423  CB  ARG B 246      55.704  18.463  -6.430  1.00  9.00           C  
ANISOU 2423  CB  ARG B 246     1175    878   1364    138     62    241       C  
ATOM   2424  CG  ARG B 246      55.534  18.031  -7.880  1.00  9.15           C  
ANISOU 2424  CG  ARG B 246     1436   1066    975    126    192    200       C  
ATOM   2425  CD  ARG B 246      55.391  19.241  -8.772  1.00  9.69           C  
ANISOU 2425  CD  ARG B 246     1346   1019   1316    -18    171    462       C  
ATOM   2426  NE  ARG B 246      56.671  19.901  -9.002  1.00 10.37           N  
ANISOU 2426  NE  ARG B 246     1271    917   1751    -85    279    176       N  
ATOM   2427  CZ  ARG B 246      56.814  21.161  -9.401  1.00 10.07           C  
ANISOU 2427  CZ  ARG B 246     1141    977   1708     68      1   -126       C  
ATOM   2428  NH1 ARG B 246      55.750  21.936  -9.564  1.00 11.04           N  
ANISOU 2428  NH1 ARG B 246     1299   1073   1823    319    455     26       N  
ATOM   2429  NH2 ARG B 246      58.029  21.651  -9.625  1.00 11.50           N  
ANISOU 2429  NH2 ARG B 246     1206   1376   1785    118     73     42       N  
ATOM   2430  N   VAL B 247      55.291  17.953  -3.130  1.00  9.09           N  
ANISOU 2430  N   VAL B 247     1246    879   1328    164    -17    -14       N  
ATOM   2431  CA  VAL B 247      55.585  18.228  -1.723  1.00  9.34           C  
ANISOU 2431  CA  VAL B 247     1245    692   1612    134     97     40       C  
ATOM   2432  C   VAL B 247      54.625  17.381  -0.913  1.00  9.11           C  
ANISOU 2432  C   VAL B 247     1147    884   1429    385    -63    132       C  
ATOM   2433  O   VAL B 247      53.526  17.086  -1.377  1.00  9.52           O  
ANISOU 2433  O   VAL B 247     1080   1035   1503    209   -123     48       O  
ATOM   2434  CB  VAL B 247      55.390  19.733  -1.331  1.00  9.84           C  
ANISOU 2434  CB  VAL B 247      934    960   1843     99     25    -74       C  
ATOM   2435  CG1 VAL B 247      56.467  20.608  -1.972  1.00 11.24           C  
ANISOU 2435  CG1 VAL B 247     1119    984   2167   -174    303     56       C  
ATOM   2436  CG2 VAL B 247      53.994  20.225  -1.713  1.00 11.22           C  
ANISOU 2436  CG2 VAL B 247     1466    866   1931    172    107     19       C  
ATOM   2437  N   PRO B 248      55.038  16.962   0.294  1.00 10.16           N  
ANISOU 2437  N   PRO B 248      992   1034   1832    272    -28    219       N  
ATOM   2438  CA  PRO B 248      54.148  16.167   1.150  1.00 10.12           C  
ANISOU 2438  CA  PRO B 248     1024   1225   1594    412    152    476       C  
ATOM   2439  C   PRO B 248      53.179  17.091   1.884  1.00 10.19           C  
ANISOU 2439  C   PRO B 248     1222   1207   1441    283   -122    102       C  
ATOM   2440  O   PRO B 248      53.406  17.512   3.024  1.00 14.70           O  
ANISOU 2440  O   PRO B 248     1900   1796   1887    762   -423   -416       O  
ATOM   2441  CB  PRO B 248      55.123  15.483   2.113  1.00 11.53           C  
ANISOU 2441  CB  PRO B 248     1144   1271   1964    263   -116    242       C  
ATOM   2442  CG  PRO B 248      56.255  16.468   2.229  1.00 10.95           C  
ANISOU 2442  CG  PRO B 248     1075   1180   1904   -102   -314    101       C  
ATOM   2443  CD  PRO B 248      56.398  17.074   0.853  1.00 11.42           C  
ANISOU 2443  CD  PRO B 248     1190   1559   1588    237   -298    321       C  
ATOM   2444  N   MET B 249      52.098  17.417   1.190  1.00 11.05           N  
ANISOU 2444  N   MET B 249     1146   1390   1661    400   -111    134       N  
ATOM   2445  CA  MET B 249      51.111  18.371   1.662  1.00 10.60           C  
ANISOU 2445  CA  MET B 249     1445   1046   1537    162   -107     28       C  
ATOM   2446  C   MET B 249      49.774  17.962   1.075  1.00 10.00           C  
ANISOU 2446  C   MET B 249     1255   1080   1464    278    230     65       C  
ATOM   2447  O   MET B 249      49.705  17.594  -0.099  1.00 10.85           O  
ANISOU 2447  O   MET B 249     1477   1203   1443    423    151     33       O  
ATOM   2448  CB  MET B 249      51.454  19.762   1.136  1.00 15.22           C  
ANISOU 2448  CB  MET B 249     2545   1292   1944    259    -80    399       C  
ATOM   2449  CG  MET B 249      51.209  20.868   2.106  1.00 22.05           C  
ANISOU 2449  CG  MET B 249     3485   2216   2676   -233   -387     -6       C  
ATOM   2450  SD  MET B 249      52.358  20.766   3.486  1.00 21.73           S  
ANISOU 2450  SD  MET B 249     3789   2342   2126   -944   -657     33       S  
ATOM   2451  CE  MET B 249      52.265  22.449   4.049  1.00 24.47           C  
ANISOU 2451  CE  MET B 249     3737   2183   3377   -710   -451    389       C  
ATOM   2452  N   LEU B 250      48.707  18.038   1.866  1.00  9.81           N  
ANISOU 2452  N   LEU B 250     1023   1243   1462    251     80    -59       N  
ATOM   2453  CA  LEU B 250      47.384  17.731   1.341  1.00 10.56           C  
ANISOU 2453  CA  LEU B 250     1109   1695   1209    267    130    275       C  
ATOM   2454  C   LEU B 250      47.049  18.631   0.159  1.00 10.07           C  
ANISOU 2454  C   LEU B 250     1236   1375   1216    437     47   -156       C  
ATOM   2455  O   LEU B 250      47.437  19.819   0.112  1.00 11.45           O  
ANISOU 2455  O   LEU B 250     1403   1099   1849    275   -174    -78       O  
ATOM   2456  CB  LEU B 250      46.317  17.888   2.422  1.00 11.58           C  
ANISOU 2456  CB  LEU B 250     1329   1654   1416    335      4    579       C  
ATOM   2457  CG  LEU B 250      46.346  16.867   3.558  1.00 12.58           C  
ANISOU 2457  CG  LEU B 250     1632   1738   1409    406     87    186       C  
ATOM   2458  CD1 LEU B 250      45.394  17.284   4.690  1.00 15.66           C  
ANISOU 2458  CD1 LEU B 250     1789   2440   1720    692    666    116       C  
ATOM   2459  CD2 LEU B 250      46.033  15.466   3.054  1.00 14.79           C  
ANISOU 2459  CD2 LEU B 250     1928   1669   2022     86   -530    123       C  
ATOM   2460  N   ILE B 251      46.317  18.065  -0.794  1.00 10.20           N  
ANISOU 2460  N   ILE B 251     1386   1427   1062    629   -115     89       N  
ATOM   2461  CA  ILE B 251      45.760  18.841  -1.894  1.00  9.87           C  
ANISOU 2461  CA  ILE B 251     1265   1247   1237    514   -232    -57       C  
ATOM   2462  C   ILE B 251      44.634  19.742  -1.387  1.00 11.07           C  
ANISOU 2462  C   ILE B 251     1349   1266   1591    529     27    207       C  
ATOM   2463  O   ILE B 251      43.735  19.286  -0.678  1.00 12.48           O  
ANISOU 2463  O   ILE B 251     1390   1611   1742    518    107    144       O  
ATOM   2464  CB  ILE B 251      45.232  17.915  -3.015  1.00 10.12           C  
ANISOU 2464  CB  ILE B 251     1316   1435   1093    351   -256     38       C  
ATOM   2465  CG1 ILE B 251      46.396  17.137  -3.643  1.00 12.70           C  
ANISOU 2465  CG1 ILE B 251     1650   1677   1496    675     -3   -362       C  
ATOM   2466  CG2 ILE B 251      44.481  18.714  -4.083  1.00 11.69           C  
ANISOU 2466  CG2 ILE B 251     1288   1684   1469    113   -171    135       C  
ATOM   2467  CD1 ILE B 251      45.957  16.013  -4.528  1.00 15.70           C  
ANISOU 2467  CD1 ILE B 251     1920   1762   2281    384     24   -294       C  
ATOM   2468  N   ASP B 252      44.683  21.022  -1.747  1.00 11.14           N  
ANISOU 2468  N   ASP B 252     1285   1259   1687    665     87     64       N  
ATOM   2469  CA  ASP B 252      43.629  21.948  -1.336  1.00 11.91           C  
ANISOU 2469  CA  ASP B 252     1485   1377   1663    600    215      3       C  
ATOM   2470  C   ASP B 252      43.009  22.697  -2.511  1.00 13.88           C  
ANISOU 2470  C   ASP B 252     1870   1567   1835    713    371    132       C  
ATOM   2471  O   ASP B 252      42.312  23.696  -2.327  1.00 15.19           O  
ANISOU 2471  O   ASP B 252     2012   1732   2028    767    296    142       O  
ATOM   2472  CB  ASP B 252      44.128  22.915  -0.257  1.00 14.31           C  
ANISOU 2472  CB  ASP B 252     1554   1410   2473    307    -69   -261       C  
ATOM   2473  CG  ASP B 252      45.151  23.899  -0.769  1.00 20.01           C  
ANISOU 2473  CG  ASP B 252     2193   1560   3851    387    387   -822       C  
ATOM   2474  OD1 ASP B 252      45.592  23.771  -1.924  1.00 23.55           O  
ANISOU 2474  OD1 ASP B 252     2301   1721   4924    283   1259   -246       O  
ATOM   2475  OD2 ASP B 252      45.498  24.830  -0.009  1.00 26.17           O  
ANISOU 2475  OD2 ASP B 252     2310   2241   5391    113   -153   -907       O  
ATOM   2476  N   GLY B 253      43.248  22.212  -3.722  1.00 14.13           N  
ANISOU 2476  N   GLY B 253     1942   1852   1574    998    269    451       N  
ATOM   2477  CA  GLY B 253      42.620  22.808  -4.886  1.00 15.41           C  
ANISOU 2477  CA  GLY B 253     2072   2130   1654   1152    312    429       C  
ATOM   2478  C   GLY B 253      42.996  22.150  -6.196  1.00 13.70           C  
ANISOU 2478  C   GLY B 253     1823   2124   1259    969    305    284       C  
ATOM   2479  O   GLY B 253      43.857  21.261  -6.243  1.00 12.94           O  
ANISOU 2479  O   GLY B 253     1395   1672   1850    503     85    132       O  
ATOM   2480  N   MET B 254      42.324  22.592  -7.257  1.00 16.43           N  
ANISOU 2480  N   MET B 254     2048   2508   1685   1136    202    695       N  
ATOM   2481  CA  MET B 254      42.665  22.272  -8.638  1.00 16.07           C  
ANISOU 2481  CA  MET B 254     2324   2382   1398    944    271    483       C  
ATOM   2482  C   MET B 254      42.772  23.587  -9.383  1.00 17.68           C  
ANISOU 2482  C   MET B 254     2757   2305   1656   1357    473    588       C  
ATOM   2483  O   MET B 254      42.118  24.562  -9.013  1.00 22.23           O  
ANISOU 2483  O   MET B 254     3468   2830   2147   1776    654    591       O  
ATOM   2484  CB  MET B 254      41.571  21.429  -9.286  1.00 18.86           C  
ANISOU 2484  CB  MET B 254     2405   2508   2252    919    -54    613       C  
ATOM   2485  CG  MET B 254      41.624  19.956  -8.936  1.00 19.03           C  
ANISOU 2485  CG  MET B 254     2268   2674   2287   1037    -11    877       C  
ATOM   2486  SD  MET B 254      40.347  19.033  -9.816  1.00 19.82           S  
ANISOU 2486  SD  MET B 254     2185   2836   2509    635    122    773       S  
ATOM   2487  CE  MET B 254      38.928  19.302  -8.762  1.00 20.60           C  
ANISOU 2487  CE  MET B 254     2053   3281   2493    620    -89    630       C  
ATOM   2488  N   MET B 255      43.589  23.620 -10.427  1.00 15.15           N  
ANISOU 2488  N   MET B 255     2424   2061   1269   1011    311    590       N  
ATOM   2489  CA  MET B 255      43.712  24.805 -11.273  1.00 15.82           C  
ANISOU 2489  CA  MET B 255     2528   1983   1501    546    349    562       C  
ATOM   2490  C   MET B 255      44.071  24.402 -12.687  1.00 15.01           C  
ANISOU 2490  C   MET B 255     2450   1889   1362    693    403    404       C  
ATOM   2491  O   MET B 255      44.531  23.288 -12.930  1.00 15.22           O  
ANISOU 2491  O   MET B 255     2549   1549   1686    898    375    302       O  
ATOM   2492  CB  MET B 255      44.796  25.755 -10.745  1.00 18.50           C  
ANISOU 2492  CB  MET B 255     2992   2032   2003    504    265   -339       C  
ATOM   2493  CG  MET B 255      46.219  25.192 -10.865  1.00 22.47           C  
ANISOU 2493  CG  MET B 255     3518   2195   2822     46    216   -360       C  
ATOM   2494  SD  MET B 255      47.557  26.316 -10.367  1.00 26.18           S  
ANISOU 2494  SD  MET B 255     4085   2958   2904   -150    215    137       S  
ATOM   2495  CE  MET B 255      47.692  27.380 -11.803  1.00 28.73           C  
ANISOU 2495  CE  MET B 255     4101   3430   3384    -45   -113    550       C  
ATOM   2496  N   VAL B 256      43.852  25.322 -13.618  1.00 16.93           N  
ANISOU 2496  N   VAL B 256     2796   1982   1653   1008    154    393       N  
ATOM   2497  CA  VAL B 256      44.455  25.239 -14.930  1.00 16.69           C  
ANISOU 2497  CA  VAL B 256     2794   1982   1565    789     89    267       C  
ATOM   2498  C   VAL B 256      45.475  26.364 -15.002  1.00 17.74           C  
ANISOU 2498  C   VAL B 256     2947   1791   2001    699    267    571       C  
ATOM   2499  O   VAL B 256      45.341  27.371 -14.301  1.00 21.11           O  
ANISOU 2499  O   VAL B 256     3406   2123   2491    521    178    124       O  
ATOM   2500  CB  VAL B 256      43.408  25.381 -16.050  1.00 18.72           C  
ANISOU 2500  CB  VAL B 256     2806   2190   2117   1091    -86    206       C  
ATOM   2501  CG1 VAL B 256      42.455  24.198 -16.026  1.00 19.58           C  
ANISOU 2501  CG1 VAL B 256     2838   2550   2050    915   -388   -229       C  
ATOM   2502  CG2 VAL B 256      42.646  26.707 -15.929  1.00 20.08           C  
ANISOU 2502  CG2 VAL B 256     2765   2354   2511   1331     -7    129       C  
ATOM   2503  N   SER B 257      46.507  26.201 -15.823  1.00 15.89           N  
ANISOU 2503  N   SER B 257     2620   1384   2034    279     30    355       N  
ATOM   2504  CA  SER B 257      47.553  27.218 -15.896  1.00 18.14           C  
ANISOU 2504  CA  SER B 257     2857   1631   2404    309     28    343       C  
ATOM   2505  C   SER B 257      47.073  28.493 -16.587  1.00 20.04           C  
ANISOU 2505  C   SER B 257     3373   1711   2528    491     98    299       C  
ATOM   2506  O   SER B 257      46.228  28.444 -17.480  1.00 20.68           O  
ANISOU 2506  O   SER B 257     3251   1670   2934    617     46    603       O  
ATOM   2507  CB  SER B 257      48.809  26.670 -16.579  1.00 18.00           C  
ANISOU 2507  CB  SER B 257     2677   1840   2322    242   -362   -188       C  
ATOM   2508  OG  SER B 257      48.506  26.155 -17.861  1.00 17.48           O  
ANISOU 2508  OG  SER B 257     2412   1560   2668    237    -39     32       O  
ATOM   2509  N   ASN B 258      47.614  29.626 -16.147  1.00 22.47           N  
ANISOU 2509  N   ASN B 258     4054   1653   2831    708    139    245       N  
ATOM   2510  CA  ASN B 258      47.303  30.929 -16.723  1.00 24.24           C  
ANISOU 2510  CA  ASN B 258     4398   1649   3163    784    110    501       C  
ATOM   2511  C   ASN B 258      47.475  30.891 -18.234  1.00 24.31           C  
ANISOU 2511  C   ASN B 258     4233   1609   3394    540   -264    115       C  
ATOM   2512  O   ASN B 258      46.575  31.263 -18.991  1.00 26.49           O  
ANISOU 2512  O   ASN B 258     4212   2297   3556    609   -351    692       O  
ATOM   2513  CB  ASN B 258      48.216  31.990 -16.094  1.00 28.67           C  
ANISOU 2513  CB  ASN B 258     4918   1630   4346    875    190    160       C  
ATOM   2514  CG  ASN B 258      47.815  33.412 -16.452  1.00 33.64           C  
ANISOU 2514  CG  ASN B 258     5370   2201   5211   1129    100     61       C  
ATOM   2515  OD1 ASN B 258      46.677  33.677 -16.840  1.00 36.81           O  
ANISOU 2515  OD1 ASN B 258     5575   2349   6060   1411     74    -90       O  
ATOM   2516  ND2 ASN B 258      48.759  34.339 -16.312  1.00 34.42           N  
ANISOU 2516  ND2 ASN B 258     5621   2346   5111   1174    295    230       N  
ATOM   2517  N   ASP B 259      48.649  30.440 -18.662  1.00 22.93           N  
ANISOU 2517  N   ASP B 259     4132   1408   3173    466    -36    294       N  
ATOM   2518  CA  ASP B 259      48.907  30.147 -20.062  1.00 24.47           C  
ANISOU 2518  CA  ASP B 259     4040   1811   3444    654    175    485       C  
ATOM   2519  C   ASP B 259      48.555  28.685 -20.308  1.00 23.62           C  
ANISOU 2519  C   ASP B 259     3688   1838   3447    766   -309   -132       C  
ATOM   2520  O   ASP B 259      49.250  27.791 -19.832  1.00 21.52           O  
ANISOU 2520  O   ASP B 259     3278   1806   3091    963   -115    543       O  
ATOM   2521  CB  ASP B 259      50.385  30.379 -20.372  1.00 27.94           C  
ANISOU 2521  CB  ASP B 259     4238   2376   4003    495    849    842       C  
ATOM   2522  CG  ASP B 259      50.714  30.180 -21.837  1.00 33.83           C  
ANISOU 2522  CG  ASP B 259     4532   3418   4902    607   1139    852       C  
ATOM   2523  OD1 ASP B 259      49.870  29.633 -22.579  1.00 34.35           O  
ANISOU 2523  OD1 ASP B 259     4553   3717   4781    701   1287    927       O  
ATOM   2524  OD2 ASP B 259      51.825  30.567 -22.244  1.00 38.65           O  
ANISOU 2524  OD2 ASP B 259     4691   3966   6026    549   1105    542       O  
ATOM   2525  N   GLN B 260      47.482  28.434 -21.050  1.00 26.32           N  
ANISOU 2525  N   GLN B 260     3813   2391   3797    953   -906   -451       N  
ATOM   2526  CA  GLN B 260      47.024  27.062 -21.253  1.00 28.78           C  
ANISOU 2526  CA  GLN B 260     3975   2575   4386   1124  -1214   -953       C  
ATOM   2527  C   GLN B 260      47.962  26.259 -22.154  1.00 29.95           C  
ANISOU 2527  C   GLN B 260     4226   3125   4028   1516  -1142   -719       C  
ATOM   2528  O   GLN B 260      47.782  25.050 -22.334  1.00 29.87           O  
ANISOU 2528  O   GLN B 260     4226   2988   4133   1425  -1347  -1046       O  
ATOM   2529  CB  GLN B 260      45.581  27.038 -21.770  1.00 32.77           C  
ANISOU 2529  CB  GLN B 260     4220   2715   5517    940  -1141  -1211       C  
ATOM   2530  CG  GLN B 260      44.636  27.864 -20.903  1.00 36.21           C  
ANISOU 2530  CG  GLN B 260     4454   3135   6168    701   -727   -772       C  
ATOM   2531  CD  GLN B 260      43.207  27.349 -20.892  1.00 36.57           C  
ANISOU 2531  CD  GLN B 260     4690   3159   6045    574   -214      3       C  
ATOM   2532  OE1 GLN B 260      42.765  26.662 -21.814  1.00 37.21           O  
ANISOU 2532  OE1 GLN B 260     4862   2931   6343    570   -108    358       O  
ATOM   2533  NE2 GLN B 260      42.474  27.686 -19.838  1.00 34.86           N  
ANISOU 2533  NE2 GLN B 260     4684   3308   5251    358    -95    333       N  
ATOM   2534  N   ASN B 261      48.974  26.929 -22.701  1.00 27.36           N  
ANISOU 2534  N   ASN B 261     4447   3310   2639   1869   -824    198       N  
ATOM   2535  CA  ASN B 261      50.004  26.257 -23.494  1.00 30.18           C  
ANISOU 2535  CA  ASN B 261     4848   3700   2918   1973   -563    205       C  
ATOM   2536  C   ASN B 261      51.249  25.860 -22.690  1.00 25.34           C  
ANISOU 2536  C   ASN B 261     4324   3002   2303   1484   -332    236       C  
ATOM   2537  O   ASN B 261      52.178  25.253 -23.231  1.00 25.98           O  
ANISOU 2537  O   ASN B 261     4211   3307   2352   1627     22    400       O  
ATOM   2538  CB  ASN B 261      50.409  27.116 -24.693  1.00 34.92           C  
ANISOU 2538  CB  ASN B 261     5545   4444   3279   2495   -648    346       C  
ATOM   2539  CG  ASN B 261      49.287  27.284 -25.697  1.00 42.20           C  
ANISOU 2539  CG  ASN B 261     6210   5148   4676   2772   -824     51       C  
ATOM   2540  OD1 ASN B 261      48.555  26.338 -25.992  1.00 45.65           O  
ANISOU 2540  OD1 ASN B 261     6500   5535   5309   2694   -779   -251       O  
ATOM   2541  ND2 ASN B 261      49.142  28.494 -26.225  1.00 44.84           N  
ANISOU 2541  ND2 ASN B 261     6404   5353   5281   2827   -856    245       N  
ATOM   2542  N   GLN B 262      51.271  26.207 -21.405  1.00 20.05           N  
ANISOU 2542  N   GLN B 262     3572   2223   1822    614   -139    417       N  
ATOM   2543  CA  GLN B 262      52.388  25.844 -20.531  1.00 17.97           C  
ANISOU 2543  CA  GLN B 262     3017   1889   1920    253   -119    321       C  
ATOM   2544  C   GLN B 262      52.608  24.333 -20.496  1.00 16.77           C  
ANISOU 2544  C   GLN B 262     2486   1779   2105    211     59    378       C  
ATOM   2545  O   GLN B 262      51.677  23.564 -20.271  1.00 17.63           O  
ANISOU 2545  O   GLN B 262     2118   1835   2743    379   -153    141       O  
ATOM   2546  CB  GLN B 262      52.161  26.381 -19.112  1.00 19.38           C  
ANISOU 2546  CB  GLN B 262     3232   2244   1885    402   -435    323       C  
ATOM   2547  CG  GLN B 262      53.139  25.857 -18.070  1.00 23.07           C  
ANISOU 2547  CG  GLN B 262     3491   2504   2768    200   -447    162       C  
ATOM   2548  CD  GLN B 262      54.529  26.442 -18.216  1.00 26.82           C  
ANISOU 2548  CD  GLN B 262     4021   2277   3893    320   -510     56       C  
ATOM   2549  OE1 GLN B 262      54.721  27.652 -18.091  1.00 30.94           O  
ANISOU 2549  OE1 GLN B 262     4381   2033   5340    356   -613    125       O  
ATOM   2550  NE2 GLN B 262      55.513  25.582 -18.468  1.00 27.47           N  
ANISOU 2550  NE2 GLN B 262     4071   2439   3928    292  -1068     89       N  
ATOM   2551  N   VAL B 263      53.853  23.925 -20.720  1.00 15.78           N  
ANISOU 2551  N   VAL B 263     2225   1496   2273    349    235    201       N  
ATOM   2552  CA  VAL B 263      54.233  22.521 -20.724  1.00 16.11           C  
ANISOU 2552  CA  VAL B 263     2134   1790   2195    356    384    656       C  
ATOM   2553  C   VAL B 263      54.841  22.127 -19.374  1.00 15.17           C  
ANISOU 2553  C   VAL B 263     1851   1771   2141    227    276    731       C  
ATOM   2554  O   VAL B 263      55.926  22.592 -19.012  1.00 18.83           O  
ANISOU 2554  O   VAL B 263     2248   1988   2917    111    -55    630       O  
ATOM   2555  CB  VAL B 263      55.248  22.235 -21.855  1.00 16.03           C  
ANISOU 2555  CB  VAL B 263     1908   2051   2131    367    269    850       C  
ATOM   2556  CG1 VAL B 263      55.683  20.774 -21.847  1.00 16.58           C  
ANISOU 2556  CG1 VAL B 263     1874   1932   2494    420    202    544       C  
ATOM   2557  CG2 VAL B 263      54.656  22.618 -23.203  1.00 17.27           C  
ANISOU 2557  CG2 VAL B 263     2141   2189   2232    259    125    735       C  
ATOM   2558  N   PRO B 264      54.139  21.272 -18.613  1.00 13.63           N  
ANISOU 2558  N   PRO B 264     1673   1643   1863    288     27    376       N  
ATOM   2559  CA  PRO B 264      54.727  20.741 -17.381  1.00 13.34           C  
ANISOU 2559  CA  PRO B 264     1886   1453   1730    537    266    290       C  
ATOM   2560  C   PRO B 264      55.673  19.582 -17.680  1.00 12.34           C  
ANISOU 2560  C   PRO B 264     1840   1307   1542    397    -33     -8       C  
ATOM   2561  O   PRO B 264      55.435  18.805 -18.611  1.00 13.12           O  
ANISOU 2561  O   PRO B 264     1955   1404   1625    211     80      0       O  
ATOM   2562  CB  PRO B 264      53.507  20.236 -16.607  1.00 14.23           C  
ANISOU 2562  CB  PRO B 264     1913   1552   1942    428    287    394       C  
ATOM   2563  CG  PRO B 264      52.536  19.834 -17.673  1.00 14.32           C  
ANISOU 2563  CG  PRO B 264     1738   1649   2052    294    -49    189       C  
ATOM   2564  CD  PRO B 264      52.765  20.781 -18.833  1.00 13.92           C  
ANISOU 2564  CD  PRO B 264     1678   1785   1826    222    192    613       C  
ATOM   2565  N   GLN B 265      56.745  19.480 -16.908  1.00 11.92           N  
ANISOU 2565  N   GLN B 265     1603   1236   1689    449     56    389       N  
ATOM   2566  CA  GLN B 265      57.628  18.326 -17.003  1.00 12.04           C  
ANISOU 2566  CA  GLN B 265     1572   1452   1549    326    337    337       C  
ATOM   2567  C   GLN B 265      58.113  17.984 -15.602  1.00 10.80           C  
ANISOU 2567  C   GLN B 265     1429   1163   1512    212    242    195       C  
ATOM   2568  O   GLN B 265      59.311  17.858 -15.341  1.00 11.62           O  
ANISOU 2568  O   GLN B 265     1357   1131   1928     57    332    -10       O  
ATOM   2569  CB  GLN B 265      58.795  18.570 -17.972  1.00 14.12           C  
ANISOU 2569  CB  GLN B 265     1827   1557   1979    217    399    296       C  
ATOM   2570  CG  GLN B 265      59.620  17.309 -18.243  1.00 14.21           C  
ANISOU 2570  CG  GLN B 265     1730   1682   1985    221    755    -29       C  
ATOM   2571  CD  GLN B 265      60.684  17.486 -19.311  1.00 15.02           C  
ANISOU 2571  CD  GLN B 265     2054   1446   2205    309    560     85       C  
ATOM   2572  OE1 GLN B 265      60.906  18.586 -19.817  1.00 19.61           O  
ANISOU 2572  OE1 GLN B 265     2866   1599   2984    393   1196    114       O  
ATOM   2573  NE2 GLN B 265      61.349  16.389 -19.664  1.00 14.42           N  
ANISOU 2573  NE2 GLN B 265     1637   1549   2293    269    568     90       N  
ATOM   2574  N   PHE B 266      57.162  17.854 -14.688  1.00 10.34           N  
ANISOU 2574  N   PHE B 266     1485   1061   1382    374    316    150       N  
ATOM   2575  CA  PHE B 266      57.492  17.468 -13.327  1.00  9.72           C  
ANISOU 2575  CA  PHE B 266     1258   1025   1411    373    265    205       C  
ATOM   2576  C   PHE B 266      58.165  16.097 -13.329  1.00 10.25           C  
ANISOU 2576  C   PHE B 266     1317    903   1674    362    115    247       C  
ATOM   2577  O   PHE B 266      57.933  15.271 -14.223  1.00 10.81           O  
ANISOU 2577  O   PHE B 266     1346   1160   1602    112     -4     19       O  
ATOM   2578  CB  PHE B 266      56.238  17.465 -12.451  1.00 10.16           C  
ANISOU 2578  CB  PHE B 266     1169    984   1706    262    478     42       C  
ATOM   2579  CG  PHE B 266      55.451  18.751 -12.511  1.00 10.23           C  
ANISOU 2579  CG  PHE B 266     1364    858   1665    232    138    -51       C  
ATOM   2580  CD1 PHE B 266      56.093  19.977 -12.577  1.00 11.59           C  
ANISOU 2580  CD1 PHE B 266     1670    810   1922    353    255     19       C  
ATOM   2581  CD2 PHE B 266      54.069  18.726 -12.515  1.00 11.02           C  
ANISOU 2581  CD2 PHE B 266     1328   1218   1639    371    -83     19       C  
ATOM   2582  CE1 PHE B 266      55.360  21.167 -12.639  1.00 11.65           C  
ANISOU 2582  CE1 PHE B 266     1527   1110   1787    412    444    -78       C  
ATOM   2583  CE2 PHE B 266      53.334  19.900 -12.579  1.00 11.63           C  
ANISOU 2583  CE2 PHE B 266     1528   1430   1460    539    135     30       C  
ATOM   2584  CZ  PHE B 266      53.983  21.120 -12.646  1.00 11.54           C  
ANISOU 2584  CZ  PHE B 266     1624   1375   1386    370    127     63       C  
ATOM   2585  N   GLN B 267      59.017  15.869 -12.340  1.00  9.86           N  
ANISOU 2585  N   GLN B 267     1102    857   1786    241     75     99       N  
ATOM   2586  CA  GLN B 267      59.735  14.599 -12.234  1.00  9.35           C  
ANISOU 2586  CA  GLN B 267      891   1010   1651    167     97    175       C  
ATOM   2587  C   GLN B 267      59.170  13.713 -11.130  1.00  9.46           C  
ANISOU 2587  C   GLN B 267     1010    918   1667    -70    115    -29       C  
ATOM   2588  O   GLN B 267      59.375  12.500 -11.138  1.00 10.13           O  
ANISOU 2588  O   GLN B 267     1178    857   1812     34    151     15       O  
ATOM   2589  CB  GLN B 267      61.234  14.842 -12.037  1.00  9.83           C  
ANISOU 2589  CB  GLN B 267      862   1229   1644     -1    173    219       C  
ATOM   2590  CG  GLN B 267      61.874  15.515 -13.232  1.00 10.87           C  
ANISOU 2590  CG  GLN B 267     1293   1245   1590    121     78     25       C  
ATOM   2591  CD  GLN B 267      61.658  14.720 -14.507  1.00 10.84           C  
ANISOU 2591  CD  GLN B 267     1197   1246   1674     34    139    186       C  
ATOM   2592  OE1 GLN B 267      62.030  13.548 -14.583  1.00 11.92           O  
ANISOU 2592  OE1 GLN B 267     1535    987   2007    235    327    -68       O  
ATOM   2593  NE2 GLN B 267      61.048  15.347 -15.510  1.00 11.79           N  
ANISOU 2593  NE2 GLN B 267     1231   1336   1913     22    307    -82       N  
ATOM   2594  N   ASN B 268      58.462  14.326 -10.186  1.00  9.55           N  
ANISOU 2594  N   ASN B 268     1113   1096   1417    119    185     54       N  
ATOM   2595  CA  ASN B 268      57.687  13.588  -9.197  1.00  9.68           C  
ANISOU 2595  CA  ASN B 268     1065   1266   1345     28      2   -257       C  
ATOM   2596  C   ASN B 268      56.212  13.544  -9.594  1.00 10.34           C  
ANISOU 2596  C   ASN B 268     1032   1072   1823     31    143   -323       C  
ATOM   2597  O   ASN B 268      55.748  14.367 -10.397  1.00 11.78           O  
ANISOU 2597  O   ASN B 268     1312   1241   1923    106    -19     27       O  
ATOM   2598  CB  ASN B 268      57.893  14.178  -7.802  1.00 10.20           C  
ANISOU 2598  CB  ASN B 268     1027   1147   1702    127   -204   -294       C  
ATOM   2599  CG  ASN B 268      59.286  13.902  -7.280  1.00  9.02           C  
ANISOU 2599  CG  ASN B 268      810   1123   1494     41   -170   -231       C  
ATOM   2600  OD1 ASN B 268      59.797  12.798  -7.460  1.00 10.76           O  
ANISOU 2600  OD1 ASN B 268     1261    860   1965    263     81    -74       O  
ATOM   2601  ND2 ASN B 268      59.920  14.901  -6.659  1.00 10.72           N  
ANISOU 2601  ND2 ASN B 268      985   1317   1770    -65     19   -226       N  
ATOM   2602  N   GLY B 269      55.494  12.557  -9.067  1.00  9.42           N  
ANISOU 2602  N   GLY B 269      905    953   1720   -136     37   -258       N  
ATOM   2603  CA  GLY B 269      54.109  12.335  -9.437  1.00  9.72           C  
ANISOU 2603  CA  GLY B 269     1016   1117   1559     -8   -151   -339       C  
ATOM   2604  C   GLY B 269      53.916  11.819 -10.854  1.00  9.90           C  
ANISOU 2604  C   GLY B 269     1088   1055   1619    219   -148    -85       C  
ATOM   2605  O   GLY B 269      52.838  11.990 -11.431  1.00 11.37           O  
ANISOU 2605  O   GLY B 269     1107   1570   1643    215   -162   -254       O  
ATOM   2606  N   ARG B 270      54.949  11.192 -11.416  1.00  9.59           N  
ANISOU 2606  N   ARG B 270     1323    873   1448    252    -15   -167       N  
ATOM   2607  CA  ARG B 270      54.911  10.733 -12.804  1.00  9.58           C  
ANISOU 2607  CA  ARG B 270     1248    776   1616     -6    271   -203       C  
ATOM   2608  C   ARG B 270      54.801   9.217 -12.865  1.00  9.46           C  
ANISOU 2608  C   ARG B 270     1134    933   1525     44    126   -279       C  
ATOM   2609  O   ARG B 270      55.677   8.495 -12.379  1.00 10.73           O  
ANISOU 2609  O   ARG B 270     1293   1021   1764    317    -79    -74       O  
ATOM   2610  CB  ARG B 270      56.152  11.198 -13.578  1.00 10.48           C  
ANISOU 2610  CB  ARG B 270     1451    857   1674    202    377     50       C  
ATOM   2611  CG  ARG B 270      56.382  12.711 -13.570  1.00  9.75           C  
ANISOU 2611  CG  ARG B 270     1272    711   1722    154    -92     61       C  
ATOM   2612  CD  ARG B 270      55.222  13.463 -14.230  1.00 10.68           C  
ANISOU 2612  CD  ARG B 270     1395   1027   1636     95     26     52       C  
ATOM   2613  NE  ARG B 270      54.993  13.024 -15.606  1.00 11.12           N  
ANISOU 2613  NE  ARG B 270     1519   1286   1421    125   -115     14       N  
ATOM   2614  CZ  ARG B 270      55.587  13.542 -16.677  1.00 10.07           C  
ANISOU 2614  CZ  ARG B 270     1481    953   1392     16   -232    -64       C  
ATOM   2615  NH1 ARG B 270      56.444  14.556 -16.552  1.00 11.22           N  
ANISOU 2615  NH1 ARG B 270     1462    976   1823    139    166    -91       N  
ATOM   2616  NH2 ARG B 270      55.319  13.051 -17.884  1.00 11.95           N  
ANISOU 2616  NH2 ARG B 270     1589   1233   1717    119   -111   -193       N  
ATOM   2617  N   VAL B 271      53.709   8.754 -13.458  1.00 10.20           N  
ANISOU 2617  N   VAL B 271     1301    842   1731   -185    -30   -364       N  
ATOM   2618  CA  VAL B 271      53.432   7.331 -13.584  1.00 11.10           C  
ANISOU 2618  CA  VAL B 271     1562   1103   1553   -214   -259   -363       C  
ATOM   2619  C   VAL B 271      52.443   7.146 -14.729  1.00 10.25           C  
ANISOU 2619  C   VAL B 271     1485    960   1448   -283   -240   -368       C  
ATOM   2620  O   VAL B 271      51.605   8.016 -14.981  1.00 12.95           O  
ANISOU 2620  O   VAL B 271     1600   1416   1902    124   -441    -93       O  
ATOM   2621  CB  VAL B 271      52.838   6.784 -12.270  1.00 12.12           C  
ANISOU 2621  CB  VAL B 271     1649   1032   1923    -90    -63    -24       C  
ATOM   2622  CG1 VAL B 271      51.430   7.332 -12.048  1.00 14.32           C  
ANISOU 2622  CG1 VAL B 271     1762   1461   2218     80   -230   -202       C  
ATOM   2623  CG2 VAL B 271      52.833   5.254 -12.263  1.00 13.16           C  
ANISOU 2623  CG2 VAL B 271     2101    818   2080     54   -244    -35       C  
ATOM   2624  N   THR B 272      52.545   6.025 -15.437  1.00 11.37           N  
ANISOU 2624  N   THR B 272     1647   1220   1452   -121   -158   -312       N  
ATOM   2625  CA  THR B 272      51.556   5.709 -16.454  1.00 12.27           C  
ANISOU 2625  CA  THR B 272     1640   1526   1494   -136   -227   -494       C  
ATOM   2626  C   THR B 272      50.317   5.124 -15.785  1.00 12.36           C  
ANISOU 2626  C   THR B 272     1666   1397   1634   -108   -354   -491       C  
ATOM   2627  O   THR B 272      50.367   4.696 -14.624  1.00 12.53           O  
ANISOU 2627  O   THR B 272     1827   1227   1705    111   -315   -246       O  
ATOM   2628  CB  THR B 272      52.095   4.691 -17.458  1.00 14.28           C  
ANISOU 2628  CB  THR B 272     1882   1609   1934    133     98   -391       C  
ATOM   2629  OG1 THR B 272      52.428   3.485 -16.763  1.00 14.92           O  
ANISOU 2629  OG1 THR B 272     1986   1522   2159    193   -155   -370       O  
ATOM   2630  CG2 THR B 272      53.339   5.228 -18.151  1.00 14.58           C  
ANISOU 2630  CG2 THR B 272     1917   1738   1884    -58    248   -384       C  
ATOM   2631  N   LEU B 273      49.210   5.081 -16.522  1.00 13.18           N  
ANISOU 2631  N   LEU B 273     1833   1439   1734   -203   -299   -320       N  
ATOM   2632  CA  LEU B 273      47.984   4.518 -15.978  1.00 13.95           C  
ANISOU 2632  CA  LEU B 273     1592   1416   2292   -226   -224     10       C  
ATOM   2633  C   LEU B 273      48.123   3.027 -15.663  1.00 13.57           C  
ANISOU 2633  C   LEU B 273     1898   1236   2021   -180   -479   -258       C  
ATOM   2634  O   LEU B 273      47.404   2.512 -14.803  1.00 15.21           O  
ANISOU 2634  O   LEU B 273     1897   1384   2497   -119   -317   -230       O  
ATOM   2635  CB  LEU B 273      46.798   4.766 -16.911  1.00 13.83           C  
ANISOU 2635  CB  LEU B 273     1529   1566   2160      7   -327   -234       C  
ATOM   2636  CG  LEU B 273      46.431   6.233 -17.149  1.00 14.37           C  
ANISOU 2636  CG  LEU B 273     1749   1727   1983    103   -223   -294       C  
ATOM   2637  CD1 LEU B 273      45.123   6.344 -17.931  1.00 16.69           C  
ANISOU 2637  CD1 LEU B 273     1750   1961   2628     24   -509   -284       C  
ATOM   2638  CD2 LEU B 273      46.342   7.000 -15.823  1.00 15.79           C  
ANISOU 2638  CD2 LEU B 273     2051   1687   2260    237    140   -240       C  
ATOM   2639  N   ASP B 274      49.044   2.337 -16.341  1.00 14.14           N  
ANISOU 2639  N   ASP B 274     1955   1129   2286   -145   -545   -457       N  
ATOM   2640  CA  ASP B 274      49.282   0.927 -16.025  1.00 16.01           C  
ANISOU 2640  CA  ASP B 274     2192   1431   2460    -57   -674   -434       C  
ATOM   2641  C   ASP B 274      50.399   0.707 -15.001  1.00 14.57           C  
ANISOU 2641  C   ASP B 274     1930   1310   2297    -91   -451   -431       C  
ATOM   2642  O   ASP B 274      50.866  -0.422 -14.806  1.00 16.41           O  
ANISOU 2642  O   ASP B 274     2229   1180   2827     39   -406   -160       O  
ATOM   2643  CB  ASP B 274      49.452   0.046 -17.277  1.00 17.77           C  
ANISOU 2643  CB  ASP B 274     2499   1787   2465    176   -347   -809       C  
ATOM   2644  CG  ASP B 274      50.699   0.369 -18.088  1.00 18.37           C  
ANISOU 2644  CG  ASP B 274     2751   2073   2155    162   -283  -1016       C  
ATOM   2645  OD1 ASP B 274      50.801  -0.154 -19.223  1.00 20.82           O  
ANISOU 2645  OD1 ASP B 274     3009   2417   2483    -73    -58  -1028       O  
ATOM   2646  OD2 ASP B 274      51.578   1.114 -17.616  1.00 19.17           O  
ANISOU 2646  OD2 ASP B 274     2501   1941   2841      6   -231   -764       O  
ATOM   2647  N   GLY B 275      50.797   1.790 -14.331  1.00 13.15           N  
ANISOU 2647  N   GLY B 275     1573   1298   2126   -215   -397   -365       N  
ATOM   2648  CA  GLY B 275      51.625   1.695 -13.141  1.00 13.38           C  
ANISOU 2648  CA  GLY B 275     1379   1379   2324    -71   -407   -249       C  
ATOM   2649  C   GLY B 275      53.134   1.670 -13.319  1.00 13.82           C  
ANISOU 2649  C   GLY B 275     1590   1304   2358    133   -194   -142       C  
ATOM   2650  O   GLY B 275      53.847   1.127 -12.469  1.00 16.09           O  
ANISOU 2650  O   GLY B 275     1948   1726   2438    432   -496    -11       O  
ATOM   2651  N   GLN B 276      53.629   2.263 -14.402  1.00 13.25           N  
ANISOU 2651  N   GLN B 276     1614   1104   2315   -186   -164   -473       N  
ATOM   2652  CA  GLN B 276      55.070   2.381 -14.612  1.00 13.33           C  
ANISOU 2652  CA  GLN B 276     1700   1189   2175    -70   -258   -648       C  
ATOM   2653  C   GLN B 276      55.563   3.738 -14.132  1.00 12.99           C  
ANISOU 2653  C   GLN B 276     1648   1186   2099    194    -56   -347       C  
ATOM   2654  O   GLN B 276      55.185   4.778 -14.681  1.00 14.07           O  
ANISOU 2654  O   GLN B 276     1763   1211   2371    326   -407   -274       O  
ATOM   2655  CB  GLN B 276      55.417   2.227 -16.092  1.00 15.54           C  
ANISOU 2655  CB  GLN B 276     2031   1584   2288      2    -44   -882       C  
ATOM   2656  CG  GLN B 276      55.011   0.899 -16.701  1.00 19.87           C  
ANISOU 2656  CG  GLN B 276     2464   2490   2594    309    249  -1112       C  
ATOM   2657  CD  GLN B 276      55.192   0.886 -18.208  1.00 26.39           C  
ANISOU 2657  CD  GLN B 276     2931   3567   3529    188     -3  -1451       C  
ATOM   2658  OE1 GLN B 276      54.220   0.835 -18.963  1.00 30.24           O  
ANISOU 2658  OE1 GLN B 276     3452   3903   4135    161    -97  -1471       O  
ATOM   2659  NE2 GLN B 276      56.442   0.941 -18.652  1.00 28.85           N  
ANISOU 2659  NE2 GLN B 276     3012   3982   3967    186    204  -1115       N  
ATOM   2660  N   LEU B 277      56.411   3.721 -13.109  1.00 12.64           N  
ANISOU 2660  N   LEU B 277     1629   1100   2072    -24   -170   -463       N  
ATOM   2661  CA  LEU B 277      56.956   4.949 -12.551  1.00 11.09           C  
ANISOU 2661  CA  LEU B 277     1574   1012   1628    -52   -140   -172       C  
ATOM   2662  C   LEU B 277      57.942   5.615 -13.505  1.00 11.32           C  
ANISOU 2662  C   LEU B 277     1604    844   1854    -18    -35     21       C  
ATOM   2663  O   LEU B 277      58.648   4.936 -14.246  1.00 14.52           O  
ANISOU 2663  O   LEU B 277     1793   1299   2425    -26     24   -339       O  
ATOM   2664  CB  LEU B 277      57.650   4.648 -11.224  1.00 12.15           C  
ANISOU 2664  CB  LEU B 277     1696   1256   1665    193   -244   -230       C  
ATOM   2665  CG  LEU B 277      56.749   4.145 -10.100  1.00 13.62           C  
ANISOU 2665  CG  LEU B 277     1856   1526   1791    257    475    -52       C  
ATOM   2666  CD1 LEU B 277      57.583   3.574  -8.986  1.00 16.10           C  
ANISOU 2666  CD1 LEU B 277     2207   1752   2158    574    106    438       C  
ATOM   2667  CD2 LEU B 277      55.887   5.285  -9.589  1.00 15.22           C  
ANISOU 2667  CD2 LEU B 277     2021   1613   2147    511    304   -166       C  
ATOM   2668  N   GLN B 278      57.985   6.946 -13.472  1.00 10.78           N  
ANISOU 2668  N   GLN B 278     1434    748   1915    -60    -84    -16       N  
ATOM   2669  CA  GLN B 278      58.910   7.729 -14.284  1.00 10.80           C  
ANISOU 2669  CA  GLN B 278     1441   1035   1628     70   -149    -92       C  
ATOM   2670  C   GLN B 278      59.585   8.825 -13.457  1.00 10.97           C  
ANISOU 2670  C   GLN B 278     1231   1151   1784     86     48   -107       C  
ATOM   2671  O   GLN B 278      59.126   9.169 -12.362  1.00 10.84           O  
ANISOU 2671  O   GLN B 278     1400   1103   1614     79      2   -174       O  
ATOM   2672  CB  GLN B 278      58.166   8.378 -15.454  1.00 12.36           C  
ANISOU 2672  CB  GLN B 278     1549   1316   1831    117    119   -224       C  
ATOM   2673  CG  GLN B 278      57.436   7.387 -16.367  1.00 12.98           C  
ANISOU 2673  CG  GLN B 278     1924   1302   1704    -91   -261   -437       C  
ATOM   2674  CD  GLN B 278      56.612   8.092 -17.422  1.00 16.04           C  
ANISOU 2674  CD  GLN B 278     2566   1629   1897    138   -202   -205       C  
ATOM   2675  OE1 GLN B 278      56.219   9.247 -17.247  1.00 18.19           O  
ANISOU 2675  OE1 GLN B 278     2774   1733   2402    183   -482   -135       O  
ATOM   2676  NE2 GLN B 278      56.352   7.409 -18.528  1.00 18.97           N  
ANISOU 2676  NE2 GLN B 278     3007   2118   2081    408   -220   -532       N  
ATOM   2677  N   GLY B 279      60.665   9.390 -13.993  1.00 11.36           N  
ANISOU 2677  N   GLY B 279     1096   1311   1909    172     56   -158       N  
ATOM   2678  CA  GLY B 279      61.364  10.466 -13.315  1.00 10.85           C  
ANISOU 2678  CA  GLY B 279     1251   1174   1696    114    -94   -299       C  
ATOM   2679  C   GLY B 279      61.944  10.016 -11.986  1.00 10.42           C  
ANISOU 2679  C   GLY B 279     1157   1215   1585     51   -162   -119       C  
ATOM   2680  O   GLY B 279      62.578   8.964 -11.898  1.00 12.49           O  
ANISOU 2680  O   GLY B 279     1529   1152   2063    352    -82    -48       O  
ATOM   2681  N   THR B 280      61.727  10.824 -10.952  1.00 10.10           N  
ANISOU 2681  N   THR B 280     1153   1191   1492    -25     10   -128       N  
ATOM   2682  CA  THR B 280      62.165  10.493  -9.601  1.00  9.93           C  
ANISOU 2682  CA  THR B 280     1164   1007   1601    -48     32   -105       C  
ATOM   2683  C   THR B 280      60.996  10.003  -8.740  1.00  9.53           C  
ANISOU 2683  C   THR B 280      980   1009   1631    263    -56    -18       C  
ATOM   2684  O   THR B 280      61.089   9.917  -7.515  1.00  9.98           O  
ANISOU 2684  O   THR B 280     1095    923   1775     38     -9     41       O  
ATOM   2685  CB  THR B 280      62.818  11.711  -8.933  1.00  9.37           C  
ANISOU 2685  CB  THR B 280      807    884   1870     44    378   -117       C  
ATOM   2686  OG1 THR B 280      61.941  12.840  -9.045  1.00 10.27           O  
ANISOU 2686  OG1 THR B 280     1007    954   1941    273     67    -83       O  
ATOM   2687  CG2 THR B 280      64.129  12.044  -9.628  1.00 11.11           C  
ANISOU 2687  CG2 THR B 280      924   1005   2292    239    351    -80       C  
ATOM   2688  N   THR B 281      59.892   9.661  -9.385  1.00 10.33           N  
ANISOU 2688  N   THR B 281      982    923   2018    260    212     32       N  
ATOM   2689  CA  THR B 281      58.678   9.303  -8.658  1.00 10.07           C  
ANISOU 2689  CA  THR B 281     1109    864   1854    198   -161    164       C  
ATOM   2690  C   THR B 281      58.835   8.027  -7.828  1.00 11.44           C  
ANISOU 2690  C   THR B 281     1074    856   2417    164    -84      0       C  
ATOM   2691  O   THR B 281      59.425   7.050  -8.290  1.00 15.47           O  
ANISOU 2691  O   THR B 281     1453   1076   3350    246    629    422       O  
ATOM   2692  CB  THR B 281      57.492   9.205  -9.637  1.00  9.94           C  
ANISOU 2692  CB  THR B 281     1048   1082   1645    123    -69    -54       C  
ATOM   2693  OG1 THR B 281      57.390  10.448 -10.333  1.00 10.87           O  
ANISOU 2693  OG1 THR B 281     1152   1261   1717    148    -48    153       O  
ATOM   2694  CG2 THR B 281      56.171   8.901  -8.914  1.00 11.44           C  
ANISOU 2694  CG2 THR B 281      769   1572   2006    175    257     91       C  
ATOM   2695  N   THR B 282      58.320   8.079  -6.602  1.00 12.14           N  
ANISOU 2695  N   THR B 282     1405   1065   2141    -56     -1    337       N  
ATOM   2696  CA  THR B 282      58.298   6.966  -5.663  1.00 15.27           C  
ANISOU 2696  CA  THR B 282     1815   1429   2556   -195     46    404       C  
ATOM   2697  C   THR B 282      56.874   6.501  -5.429  1.00 11.04           C  
ANISOU 2697  C   THR B 282     1670    924   1599    -69    -96    125       C  
ATOM   2698  O   THR B 282      55.909   7.192  -5.765  1.00 11.37           O  
ANISOU 2698  O   THR B 282     1480    961   1877     53   -155    182       O  
ATOM   2699  CB  THR B 282      58.846   7.382  -4.255  1.00 15.77           C  
ANISOU 2699  CB  THR B 282     2241   1648   2103    278    144   -865       C  
ATOM   2700  OG1 THR B 282      58.110   8.517  -3.760  1.00 17.99           O  
ANISOU 2700  OG1 THR B 282     2222   2130   2484   -130     46   -256       O  
ATOM   2701  CG2 THR B 282      60.298   7.745  -4.329  1.00 18.56           C  
ANISOU 2701  CG2 THR B 282     2154   2238   2658    603   -244   -225       C  
ATOM   2702  N   VAL B 283      56.748   5.353  -4.782  1.00 10.47           N  
ANISOU 2702  N   VAL B 283     1432    722   1825   -219    114     61       N  
ATOM   2703  CA  VAL B 283      55.439   4.861  -4.387  1.00 10.31           C  
ANISOU 2703  CA  VAL B 283     1451    662   1805   -379     15    131       C  
ATOM   2704  C   VAL B 283      54.885   5.692  -3.222  1.00 10.09           C  
ANISOU 2704  C   VAL B 283     1356    970   1508   -194   -152     54       C  
ATOM   2705  O   VAL B 283      53.741   6.136  -3.260  1.00 11.53           O  
ANISOU 2705  O   VAL B 283     1369   1104   1906    133    -14     97       O  
ATOM   2706  CB  VAL B 283      55.501   3.382  -3.988  1.00 10.86           C  
ANISOU 2706  CB  VAL B 283     1536    701   1888   -380     67    201       C  
ATOM   2707  CG1 VAL B 283      54.155   2.925  -3.446  1.00 15.06           C  
ANISOU 2707  CG1 VAL B 283     1683   1025   3015   -239     70    517       C  
ATOM   2708  CG2 VAL B 283      55.901   2.532  -5.193  1.00 14.17           C  
ANISOU 2708  CG2 VAL B 283     2042   1133   2208    152   -135   -438       C  
ATOM   2709  N   SER B 284      55.706   5.923  -2.201  1.00 10.00           N  
ANISOU 2709  N   SER B 284     1317   1021   1462      2     86      9       N  
ATOM   2710  CA  SER B 284      55.226   6.525  -0.962  1.00  9.86           C  
ANISOU 2710  CA  SER B 284     1442    837   1466    244   -120     60       C  
ATOM   2711  C   SER B 284      55.380   8.046  -0.880  1.00  9.07           C  
ANISOU 2711  C   SER B 284     1270    645   1532     49     50     44       C  
ATOM   2712  O   SER B 284      56.409   8.604  -1.266  1.00 10.99           O  
ANISOU 2712  O   SER B 284     1111   1133   1930     -6    274    100       O  
ATOM   2713  CB  SER B 284      55.943   5.893   0.226  1.00 10.96           C  
ANISOU 2713  CB  SER B 284     1537   1303   1325    183    167    -33       C  
ATOM   2714  OG  SER B 284      55.432   6.405   1.446  1.00 10.71           O  
ANISOU 2714  OG  SER B 284     1389   1037   1643      0    -48     88       O  
ATOM   2715  N   ALA B 285      54.364   8.703  -0.324  1.00  9.85           N  
ANISOU 2715  N   ALA B 285     1306    892   1544    276     48   -198       N  
ATOM   2716  CA  ALA B 285      54.438  10.139  -0.055  1.00 10.70           C  
ANISOU 2716  CA  ALA B 285     1150   1021   1893    342     70   -270       C  
ATOM   2717  C   ALA B 285      55.551  10.458   0.948  1.00 10.27           C  
ANISOU 2717  C   ALA B 285     1243   1055   1602    418     45    329       C  
ATOM   2718  O   ALA B 285      56.011  11.599   1.033  1.00 12.19           O  
ANISOU 2718  O   ALA B 285     1521    967   2142    143    -62    124       O  
ATOM   2719  CB  ALA B 285      53.101  10.664   0.445  1.00 11.60           C  
ANISOU 2719  CB  ALA B 285     1222   1262   1921    501    224   -132       C  
ATOM   2720  N   ALA B 286      55.979   9.454   1.712  1.00 10.17           N  
ANISOU 2720  N   ALA B 286     1234   1103   1526    -42   -215    -91       N  
ATOM   2721  CA  ALA B 286      57.054   9.645   2.685  1.00 10.20           C  
ANISOU 2721  CA  ALA B 286     1386    957   1533     14     94    302       C  
ATOM   2722  C   ALA B 286      58.399   9.995   2.039  1.00 10.66           C  
ANISOU 2722  C   ALA B 286     1466    909   1676    -52    330    302       C  
ATOM   2723  O   ALA B 286      59.318  10.454   2.724  1.00 13.17           O  
ANISOU 2723  O   ALA B 286     1498   1493   2012   -212   -159    -38       O  
ATOM   2724  CB  ALA B 286      57.199   8.411   3.589  1.00 12.14           C  
ANISOU 2724  CB  ALA B 286     1722   1160   1731   -141   -177    371       C  
ATOM   2725  N   CYS B 287      58.515   9.785   0.732  1.00  9.29           N  
ANISOU 2725  N   CYS B 287     1239    937   1352    189    234     86       N  
ATOM   2726  CA  CYS B 287      59.776  10.060   0.028  1.00  9.82           C  
ANISOU 2726  CA  CYS B 287     1379    774   1577    152    122     57       C  
ATOM   2727  C   CYS B 287      59.811  11.411  -0.679  1.00  9.26           C  
ANISOU 2727  C   CYS B 287     1181    697   1639    105    -37    154       C  
ATOM   2728  O   CYS B 287      60.861  11.837  -1.157  1.00 10.68           O  
ANISOU 2728  O   CYS B 287     1139    941   1977    125     83     10       O  
ATOM   2729  CB  CYS B 287      60.050   8.984  -1.013  1.00 10.35           C  
ANISOU 2729  CB  CYS B 287     1588    630   1715    271    -33    -86       C  
ATOM   2730  SG  CYS B 287      60.199   7.333  -0.332  1.00 13.69           S  
ANISOU 2730  SG  CYS B 287     1777    947   2475    240     37     53       S  
ATOM   2731  N   ILE B 288      58.662  12.073  -0.775  1.00  8.64           N  
ANISOU 2731  N   ILE B 288     1032    582   1668    155   -161     70       N  
ATOM   2732  CA  ILE B 288      58.554  13.267  -1.608  1.00  8.01           C  
ANISOU 2732  CA  ILE B 288      856    496   1692     59   -249     33       C  
ATOM   2733  C   ILE B 288      59.426  14.426  -1.116  1.00  8.28           C  
ANISOU 2733  C   ILE B 288     1055    541   1551     26   -305   -131       C  
ATOM   2734  O   ILE B 288      59.340  14.838   0.046  1.00  9.73           O  
ANISOU 2734  O   ILE B 288     1123    941   1632     70   -180   -138       O  
ATOM   2735  CB  ILE B 288      57.101  13.749  -1.719  1.00  8.97           C  
ANISOU 2735  CB  ILE B 288      767    627   2013    111   -157     86       C  
ATOM   2736  CG1 ILE B 288      56.204  12.688  -2.372  1.00  9.92           C  
ANISOU 2736  CG1 ILE B 288      847    969   1953     95     10    -54       C  
ATOM   2737  CG2 ILE B 288      57.043  15.040  -2.524  1.00 11.29           C  
ANISOU 2737  CG2 ILE B 288     1261    792   2237    207    -31    390       C  
ATOM   2738  CD1 ILE B 288      54.724  12.995  -2.234  1.00 10.82           C  
ANISOU 2738  CD1 ILE B 288      957    988   2167     98    -96    159       C  
ATOM   2739  N   ALA B 289      60.263  14.932  -2.020  1.00  8.97           N  
ANISOU 2739  N   ALA B 289     1020    545   1842    -69    -67    172       N  
ATOM   2740  CA  ALA B 289      61.088  16.123  -1.794  1.00  9.71           C  
ANISOU 2740  CA  ALA B 289     1040    788   1860     85   -149    -91       C  
ATOM   2741  C   ALA B 289      62.108  15.925  -0.679  1.00  9.63           C  
ANISOU 2741  C   ALA B 289     1247    727   1683    -12   -232   -328       C  
ATOM   2742  O   ALA B 289      62.394  16.834   0.092  1.00 13.19           O  
ANISOU 2742  O   ALA B 289     1908    846   2256    319   -593   -309       O  
ATOM   2743  CB  ALA B 289      60.221  17.373  -1.543  1.00 11.54           C  
ANISOU 2743  CB  ALA B 289     1281    805   2299    230   -260   -347       C  
ATOM   2744  N   ARG B 290      62.670  14.724  -0.622  1.00  9.25           N  
ANISOU 2744  N   ARG B 290      929    792   1794    176    -87    -95       N  
ATOM   2745  CA  ARG B 290      63.703  14.394   0.346  1.00  8.77           C  
ANISOU 2745  CA  ARG B 290      938    891   1503     13      3   -109       C  
ATOM   2746  C   ARG B 290      64.992  14.003  -0.353  1.00  9.06           C  
ANISOU 2746  C   ARG B 290     1021    798   1624    242     42    -59       C  
ATOM   2747  O   ARG B 290      64.992  13.690  -1.548  1.00 10.40           O  
ANISOU 2747  O   ARG B 290     1103   1177   1671    214   -114   -161       O  
ATOM   2748  CB  ARG B 290      63.220  13.281   1.281  1.00  9.60           C  
ANISOU 2748  CB  ARG B 290     1075   1016   1554     33    203    169       C  
ATOM   2749  CG  ARG B 290      62.063  13.740   2.150  1.00 11.61           C  
ANISOU 2749  CG  ARG B 290     1314   1257   1841   -144    555     30       C  
ATOM   2750  CD  ARG B 290      61.625  12.659   3.119  1.00 15.39           C  
ANISOU 2750  CD  ARG B 290     1869   1420   2558   -221    767    443       C  
ATOM   2751  NE  ARG B 290      60.461  13.064   3.893  1.00 16.08           N  
ANISOU 2751  NE  ARG B 290     2238   1936   1934   -324    521     92       N  
ATOM   2752  CZ  ARG B 290      60.490  13.404   5.180  1.00 19.61           C  
ANISOU 2752  CZ  ARG B 290     2401   2340   2708   -169    135   -101       C  
ATOM   2753  NH1 ARG B 290      61.636  13.395   5.848  1.00 22.99           N  
ANISOU 2753  NH1 ARG B 290     2900   2439   3397   -109   -977   -170       N  
ATOM   2754  NH2 ARG B 290      59.367  13.749   5.804  1.00 21.75           N  
ANISOU 2754  NH2 ARG B 290     2682   2521   3061    -19    360     99       N  
ATOM   2755  N   MET B 291      66.089  14.049   0.398  1.00 10.05           N  
ANISOU 2755  N   MET B 291      920    865   2032    223    -55      0       N  
ATOM   2756  CA  MET B 291      67.398  13.638  -0.090  1.00 10.65           C  
ANISOU 2756  CA  MET B 291      970   1053   2021    227     31     71       C  
ATOM   2757  C   MET B 291      68.094  12.840   0.991  1.00  9.72           C  
ANISOU 2757  C   MET B 291      900    936   1858     90    141     23       C  
ATOM   2758  O   MET B 291      67.746  12.939   2.166  1.00  9.49           O  
ANISOU 2758  O   MET B 291      987   1012   1605     60    -28   -152       O  
ATOM   2759  CB  MET B 291      68.283  14.850  -0.403  1.00 10.58           C  
ANISOU 2759  CB  MET B 291     1037    811   2173    -65    -53    160       C  
ATOM   2760  CG  MET B 291      67.678  15.903  -1.307  1.00 11.37           C  
ANISOU 2760  CG  MET B 291     1160    879   2279   -236     64     76       C  
ATOM   2761  SD  MET B 291      68.828  17.285  -1.412  1.00 11.94           S  
ANISOU 2761  SD  MET B 291     1222   1101   2213    -67    -73    -85       S  
ATOM   2762  CE  MET B 291      67.844  18.478  -2.330  1.00 12.06           C  
ANISOU 2762  CE  MET B 291     1254   1062   2267    165   -303     85       C  
ATOM   2763  N   ARG B 292      69.107  12.076   0.594  1.00 10.37           N  
ANISOU 2763  N   ARG B 292      742   1135   2062    193    -94    -34       N  
ATOM   2764  CA  ARG B 292      69.951  11.382   1.559  1.00 10.20           C  
ANISOU 2764  CA  ARG B 292      635   1013   2225    -80   -164    -20       C  
ATOM   2765  C   ARG B 292      71.374  11.350   1.045  1.00  9.86           C  
ANISOU 2765  C   ARG B 292      658   1071   2017   -125   -159     33       C  
ATOM   2766  O   ARG B 292      71.602  11.254  -0.163  1.00 11.04           O  
ANISOU 2766  O   ARG B 292     1013   1265   1916     93    108    -52       O  
ATOM   2767  CB  ARG B 292      69.458   9.954   1.791  1.00  9.88           C  
ANISOU 2767  CB  ARG B 292      992    771   1989     64   -231    149       C  
ATOM   2768  CG  ARG B 292      70.324   9.158   2.766  1.00 10.42           C  
ANISOU 2768  CG  ARG B 292      958    792   2210     61   -138    101       C  
ATOM   2769  CD  ARG B 292      69.637   7.860   3.169  1.00 10.35           C  
ANISOU 2769  CD  ARG B 292     1014    833   2083    -19   -252    169       C  
ATOM   2770  NE  ARG B 292      70.456   7.074   4.088  1.00 12.00           N  
ANISOU 2770  NE  ARG B 292     1413   1094   2053    354   -391     -7       N  
ATOM   2771  CZ  ARG B 292      69.968   6.171   4.928  1.00 13.36           C  
ANISOU 2771  CZ  ARG B 292     1619   1238   2220    279   -470     96       C  
ATOM   2772  NH1 ARG B 292      68.662   5.940   4.966  1.00 12.93           N  
ANISOU 2772  NH1 ARG B 292     1778   1196   1939     10   -198     77       N  
ATOM   2773  NH2 ARG B 292      70.782   5.492   5.722  1.00 14.49           N  
ANISOU 2773  NH2 ARG B 292     1689   1280   2536    275   -494     30       N  
ATOM   2774  N   GLY B 293      72.328  11.440   1.960  1.00 10.62           N  
ANISOU 2774  N   GLY B 293      627   1182   2226     72   -125   -218       N  
ATOM   2775  CA  GLY B 293      73.711  11.239   1.570  1.00 12.00           C  
ANISOU 2775  CA  GLY B 293      691   1433   2435     -4   -222   -161       C  
ATOM   2776  C   GLY B 293      74.676  11.644   2.651  1.00 11.80           C  
ANISOU 2776  C   GLY B 293      738   1531   2215     81    112   -103       C  
ATOM   2777  O   GLY B 293      74.287  11.947   3.780  1.00 14.57           O  
ANISOU 2777  O   GLY B 293      946   2254   2336    101    -95   -108       O  
ATOM   2778  N   ARG B 294      75.953  11.642   2.290  1.00 12.13           N  
ANISOU 2778  N   ARG B 294      714   1474   2420      9   -231   -140       N  
ATOM   2779  CA  ARG B 294      77.018  11.961   3.226  1.00 13.14           C  
ANISOU 2779  CA  ARG B 294      849   1544   2599    -34   -177   -247       C  
ATOM   2780  C   ARG B 294      77.581  13.342   2.916  1.00 14.29           C  
ANISOU 2780  C   ARG B 294     1097   1711   2620     38    -15   -365       C  
ATOM   2781  O   ARG B 294      77.927  13.654   1.775  1.00 15.09           O  
ANISOU 2781  O   ARG B 294     1173   1931   2629   -284     74   -275       O  
ATOM   2782  CB  ARG B 294      78.113  10.889   3.177  1.00 16.22           C  
ANISOU 2782  CB  ARG B 294     1143   2300   2719    341   -217   -390       C  
ATOM   2783  CG  ARG B 294      79.068  10.909   4.371  1.00 19.23           C  
ANISOU 2783  CG  ARG B 294     1592   2450   3264    379   -381   -377       C  
ATOM   2784  CD  ARG B 294      80.021   9.707   4.371  1.00 20.87           C  
ANISOU 2784  CD  ARG B 294     1644   2564   3720    379   -177     52       C  
ATOM   2785  NE  ARG B 294      79.296   8.441   4.406  1.00 21.79           N  
ANISOU 2785  NE  ARG B 294     2029   2476   3775    536   -168   -130       N  
ATOM   2786  CZ  ARG B 294      78.879   7.841   5.519  1.00 24.13           C  
ANISOU 2786  CZ  ARG B 294     2335   2479   4352    609   -309    165       C  
ATOM   2787  NH1 ARG B 294      79.113   8.385   6.706  1.00 21.30           N  
ANISOU 2787  NH1 ARG B 294     2060   2192   3842    400   -469   -183       N  
ATOM   2788  NH2 ARG B 294      78.218   6.696   5.445  1.00 26.81           N  
ANISOU 2788  NH2 ARG B 294     2694   2594   4896    610   -318   -187       N  
ATOM   2789  N   ILE B 295      77.654  14.179   3.940  1.00 13.72           N  
ANISOU 2789  N   ILE B 295     1012   1530   2669   -110   -301   -284       N  
ATOM   2790  CA  ILE B 295      78.151  15.538   3.769  1.00 14.53           C  
ANISOU 2790  CA  ILE B 295     1035   1741   2745   -357     -4   -338       C  
ATOM   2791  C   ILE B 295      79.675  15.534   3.672  1.00 14.76           C  
ANISOU 2791  C   ILE B 295     1148   1856   2605   -471    -46   -100       C  
ATOM   2792  O   ILE B 295      80.353  14.814   4.410  1.00 16.71           O  
ANISOU 2792  O   ILE B 295     1268   1891   3189    -86   -399     58       O  
ATOM   2793  CB  ILE B 295      77.660  16.444   4.913  1.00 14.31           C  
ANISOU 2793  CB  ILE B 295     1023   1669   2745   -484   -204   -136       C  
ATOM   2794  CG1 ILE B 295      76.151  16.676   4.771  1.00 15.16           C  
ANISOU 2794  CG1 ILE B 295      992   1902   2864   -387   -226   -379       C  
ATOM   2795  CG2 ILE B 295      78.400  17.775   4.922  1.00 16.33           C  
ANISOU 2795  CG2 ILE B 295     1234   1707   3262   -552   -130    -92       C  
ATOM   2796  CD1 ILE B 295      75.516  17.390   5.949  1.00 15.60           C  
ANISOU 2796  CD1 ILE B 295     1397   1800   2729   -202    -95   -538       C  
ATOM   2797  N   PHE B 296      80.203  16.315   2.735  1.00 15.60           N  
ANISOU 2797  N   PHE B 296     1089   2114   2724   -512    128    -73       N  
ATOM   2798  CA  PHE B 296      81.648  16.438   2.571  1.00 17.23           C  
ANISOU 2798  CA  PHE B 296     1126   2391   3029   -641    243   -273       C  
ATOM   2799  C   PHE B 296      82.085  17.891   2.534  1.00 18.44           C  
ANISOU 2799  C   PHE B 296     1217   2473   3316   -553   -222   -323       C  
ATOM   2800  O   PHE B 296      81.273  18.797   2.335  1.00 17.59           O  
ANISOU 2800  O   PHE B 296     1297   2316   3070   -474   -166   -111       O  
ATOM   2801  CB  PHE B 296      82.126  15.722   1.302  1.00 20.23           C  
ANISOU 2801  CB  PHE B 296     1318   2700   3668   -451    327   -650       C  
ATOM   2802  CG  PHE B 296      81.604  16.323   0.025  1.00 21.15           C  
ANISOU 2802  CG  PHE B 296     1421   2880   3735   -676    345   -913       C  
ATOM   2803  CD1 PHE B 296      82.219  17.433  -0.537  1.00 23.53           C  
ANISOU 2803  CD1 PHE B 296     1624   3279   4036   -445    225   -619       C  
ATOM   2804  CD2 PHE B 296      80.506  15.771  -0.620  1.00 21.64           C  
ANISOU 2804  CD2 PHE B 296     1381   3255   3587   -625    457   -927       C  
ATOM   2805  CE1 PHE B 296      81.747  17.989  -1.714  1.00 23.39           C  
ANISOU 2805  CE1 PHE B 296     1552   3215   4119   -600      4   -818       C  
ATOM   2806  CE2 PHE B 296      80.033  16.316  -1.798  1.00 22.95           C  
ANISOU 2806  CE2 PHE B 296     1395   3348   3975   -660    461   -573       C  
ATOM   2807  CZ  PHE B 296      80.650  17.431  -2.346  1.00 23.46           C  
ANISOU 2807  CZ  PHE B 296     1491   3451   3972   -650    313   -782       C  
ATOM   2808  N   ASN B 297      83.380  18.106   2.739  1.00 19.78           N  
ANISOU 2808  N   ASN B 297     1392   2602   3519   -861   -140   -173       N  
ATOM   2809  CA  ASN B 297      83.972  19.429   2.635  1.00 19.99           C  
ANISOU 2809  CA  ASN B 297     1570   2709   3315   -964    -16   -262       C  
ATOM   2810  C   ASN B 297      85.257  19.326   1.834  1.00 21.25           C  
ANISOU 2810  C   ASN B 297     1577   3084   3412  -1132     56    -73       C  
ATOM   2811  O   ASN B 297      86.250  18.777   2.307  1.00 25.42           O  
ANISOU 2811  O   ASN B 297     1631   3856   4169   -513   -194    -83       O  
ATOM   2812  CB  ASN B 297      84.262  19.998   4.024  1.00 21.64           C  
ANISOU 2812  CB  ASN B 297     1900   2691   3631  -1217   -204   -277       C  
ATOM   2813  CG  ASN B 297      85.075  21.285   3.975  1.00 23.71           C  
ANISOU 2813  CG  ASN B 297     2470   2940   3599   -812   -232   -437       C  
ATOM   2814  OD1 ASN B 297      85.211  21.916   2.925  1.00 24.19           O  
ANISOU 2814  OD1 ASN B 297     2706   2770   3714   -814    -61   -288       O  
ATOM   2815  ND2 ASN B 297      85.610  21.681   5.118  1.00 26.11           N  
ANISOU 2815  ND2 ASN B 297     2701   3209   4008   -929   -431   -460       N  
ATOM   2816  N   ASN B 298      85.217  19.825   0.604  1.00 21.30           N  
ANISOU 2816  N   ASN B 298     1718   3211   3162  -1203    124   -338       N  
ATOM   2817  CA  ASN B 298      86.406  19.880  -0.236  1.00 24.22           C  
ANISOU 2817  CA  ASN B 298     2248   3247   3705  -1320    -71   -713       C  
ATOM   2818  C   ASN B 298      86.921  21.308  -0.340  1.00 26.04           C  
ANISOU 2818  C   ASN B 298     2393   3351   4149  -1327    466   -449       C  
ATOM   2819  O   ASN B 298      86.360  22.122  -1.073  1.00 25.92           O  
ANISOU 2819  O   ASN B 298     2505   3521   3820  -1149    480   -617       O  
ATOM   2820  CB  ASN B 298      86.107  19.341  -1.636  1.00 30.33           C  
ANISOU 2820  CB  ASN B 298     2994   3664   4864   -668   -251  -1050       C  
ATOM   2821  CG  ASN B 298      85.863  17.846  -1.646  1.00 37.00           C  
ANISOU 2821  CG  ASN B 298     3533   4372   6154   -142   -691  -1374       C  
ATOM   2822  OD1 ASN B 298      86.508  17.096  -0.915  1.00 40.24           O  
ANISOU 2822  OD1 ASN B 298     3860   4544   6885    171   -702  -1453       O  
ATOM   2823  ND2 ASN B 298      84.927  17.403  -2.478  1.00 39.64           N  
ANISOU 2823  ND2 ASN B 298     3705   4799   6557     96   -752  -1570       N  
ATOM   2824  N   ASN B 299      87.978  21.611   0.404  1.00 27.79           N  
ANISOU 2824  N   ASN B 299     2627   3401   4531  -1077    266   -866       N  
ATOM   2825  CA  ASN B 299      88.628  22.915   0.311  1.00 29.10           C  
ANISOU 2825  CA  ASN B 299     2837   3255   4965  -1137    466   -674       C  
ATOM   2826  C   ASN B 299      87.667  24.085   0.543  1.00 25.47           C  
ANISOU 2826  C   ASN B 299     2511   3131   4035  -1252    431   -587       C  
ATOM   2827  O   ASN B 299      87.781  25.123  -0.099  1.00 24.50           O  
ANISOU 2827  O   ASN B 299     2536   3021   3753  -1141    358   -955       O  
ATOM   2828  CB  ASN B 299      89.307  23.060  -1.057  1.00 34.28           C  
ANISOU 2828  CB  ASN B 299     3263   3613   6149   -941    885     15       C  
ATOM   2829  CG  ASN B 299      90.273  24.233  -1.117  1.00 40.22           C  
ANISOU 2829  CG  ASN B 299     3789   4305   7187   -551    809    328       C  
ATOM   2830  OD1 ASN B 299      91.035  24.475  -0.181  1.00 40.65           O  
ANISOU 2830  OD1 ASN B 299     3810   4307   7329   -719    732     22       O  
ATOM   2831  ND2 ASN B 299      90.243  24.968  -2.225  1.00 42.68           N  
ANISOU 2831  ND2 ASN B 299     4076   4390   7748   -395    765    611       N  
ATOM   2832  N   GLY B 300      86.720  23.915   1.459  1.00 23.63           N  
ANISOU 2832  N   GLY B 300     2459   3049   3468  -1097    101   -824       N  
ATOM   2833  CA  GLY B 300      85.787  24.983   1.769  1.00 25.54           C  
ANISOU 2833  CA  GLY B 300     2669   3280   3756   -744    140   -467       C  
ATOM   2834  C   GLY B 300      84.540  24.927   0.914  1.00 25.32           C  
ANISOU 2834  C   GLY B 300     2560   3239   3819   -854    336   -230       C  
ATOM   2835  O   GLY B 300      83.633  25.747   1.065  1.00 28.64           O  
ANISOU 2835  O   GLY B 300     3005   3723   4152   -284    445     94       O  
ATOM   2836  N   ASN B 301      84.499  23.962   0.001  1.00 23.06           N  
ANISOU 2836  N   ASN B 301     2177   3012   3573  -1439    222   -132       N  
ATOM   2837  CA  ASN B 301      83.293  23.690  -0.770  1.00 24.43           C  
ANISOU 2837  CA  ASN B 301     2382   3033   3867  -1284    382     55       C  
ATOM   2838  C   ASN B 301      82.538  22.515  -0.157  1.00 23.09           C  
ANISOU 2838  C   ASN B 301     1988   2722   4064  -1113     33   -121       C  
ATOM   2839  O   ASN B 301      83.019  21.385  -0.181  1.00 22.22           O  
ANISOU 2839  O   ASN B 301     1892   2810   3738   -860    353     58       O  
ATOM   2840  CB  ASN B 301      83.647  23.376  -2.223  1.00 27.33           C  
ANISOU 2840  CB  ASN B 301     2932   3323   4129  -1239    -39    392       C  
ATOM   2841  CG  ASN B 301      84.525  24.442  -2.853  1.00 32.20           C  
ANISOU 2841  CG  ASN B 301     3350   3885   5000   -925    -86    632       C  
ATOM   2842  OD1 ASN B 301      84.043  25.503  -3.249  1.00 32.21           O  
ANISOU 2842  OD1 ASN B 301     3605   3928   4704   -694   -471    767       O  
ATOM   2843  ND2 ASN B 301      85.820  24.159  -2.958  1.00 35.42           N  
ANISOU 2843  ND2 ASN B 301     3555   4279   5625   -639    184    584       N  
ATOM   2844  N   TYR B 302      81.360  22.785   0.395  1.00 20.38           N  
ANISOU 2844  N   TYR B 302     1712   2384   3645  -1033   -129    -46       N  
ATOM   2845  CA  TYR B 302      80.573  21.749   1.059  1.00 17.56           C  
ANISOU 2845  CA  TYR B 302     1562   2150   2960  -1001   -177   -147       C  
ATOM   2846  C   TYR B 302      79.565  21.139   0.100  1.00 15.66           C  
ANISOU 2846  C   TYR B 302     1325   1890   2733   -835     21    -37       C  
ATOM   2847  O   TYR B 302      79.106  21.790  -0.836  1.00 17.18           O  
ANISOU 2847  O   TYR B 302     1346   1942   3239   -462    257    -96       O  
ATOM   2848  CB  TYR B 302      79.840  22.315   2.278  1.00 17.86           C  
ANISOU 2848  CB  TYR B 302     1706   2421   2659   -818   -332   -162       C  
ATOM   2849  CG  TYR B 302      80.768  22.811   3.360  1.00 18.75           C  
ANISOU 2849  CG  TYR B 302     1878   2428   2818   -723   -496   -434       C  
ATOM   2850  CD1 TYR B 302      81.084  22.010   4.450  1.00 21.05           C  
ANISOU 2850  CD1 TYR B 302     2123   2843   3032   -645   -420   -183       C  
ATOM   2851  CD2 TYR B 302      81.343  24.071   3.279  1.00 21.33           C  
ANISOU 2851  CD2 TYR B 302     2280   2384   3441   -602   -641   -580       C  
ATOM   2852  CE1 TYR B 302      81.943  22.452   5.434  1.00 21.83           C  
ANISOU 2852  CE1 TYR B 302     2290   2719   3285   -697   -785   -394       C  
ATOM   2853  CE2 TYR B 302      82.199  24.521   4.257  1.00 23.33           C  
ANISOU 2853  CE2 TYR B 302     2467   2793   3603   -465   -940   -280       C  
ATOM   2854  CZ  TYR B 302      82.493  23.713   5.330  1.00 22.82           C  
ANISOU 2854  CZ  TYR B 302     2470   2793   3406   -772   -999   -187       C  
ATOM   2855  OH  TYR B 302      83.349  24.167   6.301  1.00 25.01           O  
ANISOU 2855  OH  TYR B 302     2589   3146   3767   -884  -1067   -192       O  
ATOM   2856  N   GLY B 303      79.216  19.887   0.346  1.00 15.87           N  
ANISOU 2856  N   GLY B 303     1334   1742   2953   -690    -33   -296       N  
ATOM   2857  CA  GLY B 303      78.286  19.202  -0.528  1.00 15.86           C  
ANISOU 2857  CA  GLY B 303     1408   1686   2931   -636   -178   -214       C  
ATOM   2858  C   GLY B 303      77.758  17.930   0.087  1.00 13.91           C  
ANISOU 2858  C   GLY B 303     1258   1566   2462   -492   -113     79       C  
ATOM   2859  O   GLY B 303      78.127  17.577   1.211  1.00 14.71           O  
ANISOU 2859  O   GLY B 303     1301   1765   2523   -392   -115      1       O  
ATOM   2860  N   VAL B 304      76.884  17.252  -0.650  1.00 13.86           N  
ANISOU 2860  N   VAL B 304     1276   1573   2417   -338     77     77       N  
ATOM   2861  CA  VAL B 304      76.410  15.940  -0.252  1.00 13.10           C  
ANISOU 2861  CA  VAL B 304     1122   1465   2391   -447    359   -109       C  
ATOM   2862  C   VAL B 304      76.677  14.951  -1.378  1.00 14.88           C  
ANISOU 2862  C   VAL B 304     1191   2006   2456   -139      3   -118       C  
ATOM   2863  O   VAL B 304      76.388  15.235  -2.545  1.00 15.25           O  
ANISOU 2863  O   VAL B 304     1216   1898   2678   -144     27   -114       O  
ATOM   2864  CB  VAL B 304      74.895  15.945   0.069  1.00 15.29           C  
ANISOU 2864  CB  VAL B 304     1182   1546   3080   -331    441   -240       C  
ATOM   2865  CG1 VAL B 304      74.402  14.524   0.343  1.00 15.32           C  
ANISOU 2865  CG1 VAL B 304     1263   1231   3325   -240    378    -46       C  
ATOM   2866  CG2 VAL B 304      74.611  16.815   1.277  1.00 17.87           C  
ANISOU 2866  CG2 VAL B 304     1647   1775   3366   -218    185   -614       C  
ATOM   2867  N   ASN B 305      77.265  13.809  -1.026  1.00 14.15           N  
ANISOU 2867  N   ASN B 305     1043   1897   2436   -139    167   -495       N  
ATOM   2868  CA  ASN B 305      77.344  12.676  -1.931  1.00 15.12           C  
ANISOU 2868  CA  ASN B 305      888   2053   2802    -29     26   -216       C  
ATOM   2869  C   ASN B 305      76.076  11.861  -1.737  1.00 13.46           C  
ANISOU 2869  C   ASN B 305      967   1803   2342     24    186   -177       C  
ATOM   2870  O   ASN B 305      75.872  11.256  -0.685  1.00 13.62           O  
ANISOU 2870  O   ASN B 305     1050   1702   2421     82    -43    -91       O  
ATOM   2871  CB  ASN B 305      78.594  11.833  -1.655  1.00 17.90           C  
ANISOU 2871  CB  ASN B 305     1004   2499   3296   -242    379   -374       C  
ATOM   2872  CG  ASN B 305      79.870  12.524  -2.097  1.00 21.10           C  
ANISOU 2872  CG  ASN B 305     1568   3201   3246   -197    214   -586       C  
ATOM   2873  OD1 ASN B 305      79.922  13.126  -3.171  1.00 24.05           O  
ANISOU 2873  OD1 ASN B 305     1802   3475   3860   -278    261   -774       O  
ATOM   2874  ND2 ASN B 305      80.905  12.448  -1.268  1.00 23.83           N  
ANISOU 2874  ND2 ASN B 305     1797   3581   3677     43   -186   -901       N  
ATOM   2875  N   LEU B 306      75.218  11.881  -2.752  1.00 12.83           N  
ANISOU 2875  N   LEU B 306      883   1798   2192    -62    215   -214       N  
ATOM   2876  CA  LEU B 306      73.857  11.379  -2.636  1.00 11.80           C  
ANISOU 2876  CA  LEU B 306      982   1328   2171   -147      8   -103       C  
ATOM   2877  C   LEU B 306      73.748   9.859  -2.663  1.00 12.46           C  
ANISOU 2877  C   LEU B 306     1064   1226   2443    201   -125    -83       C  
ATOM   2878  O   LEU B 306      74.573   9.168  -3.264  1.00 14.17           O  
ANISOU 2878  O   LEU B 306     1212   1388   2784    323    225   -184       O  
ATOM   2879  CB  LEU B 306      72.987  11.971  -3.747  1.00 12.93           C  
ANISOU 2879  CB  LEU B 306     1165   1388   2359   -212   -199    168       C  
ATOM   2880  CG  LEU B 306      72.809  13.489  -3.732  1.00 12.18           C  
ANISOU 2880  CG  LEU B 306     1330   1297   1999     43    114     19       C  
ATOM   2881  CD1 LEU B 306      72.231  13.963  -5.059  1.00 12.95           C  
ANISOU 2881  CD1 LEU B 306     1420   1773   1727     87   -147    105       C  
ATOM   2882  CD2 LEU B 306      71.914  13.898  -2.565  1.00 13.42           C  
ANISOU 2882  CD2 LEU B 306     1429   1586   2083     33    125    -44       C  
ATOM   2883  N   ALA B 307      72.699   9.366  -2.015  1.00 11.76           N  
ANISOU 2883  N   ALA B 307     1093   1176   2200    -40    102   -202       N  
ATOM   2884  CA  ALA B 307      72.302   7.969  -2.058  1.00 11.20           C  
ANISOU 2884  CA  ALA B 307      894   1148   2213   -121     47     26       C  
ATOM   2885  C   ALA B 307      70.787   7.937  -2.213  1.00 10.33           C  
ANISOU 2885  C   ALA B 307      969   1049   1906   -172     38    -29       C  
ATOM   2886  O   ALA B 307      70.126   8.982  -2.127  1.00 11.76           O  
ANISOU 2886  O   ALA B 307     1179    838   2451    122     20   -105       O  
ATOM   2887  CB  ALA B 307      72.713   7.266  -0.771  1.00 13.14           C  
ANISOU 2887  CB  ALA B 307     1162   1501   2327    356   -119    106       C  
ATOM   2888  N   GLU B 308      70.228   6.751  -2.437  1.00 10.52           N  
ANISOU 2888  N   GLU B 308      955   1013   2027   -227     19    -34       N  
ATOM   2889  CA  GLU B 308      68.776   6.600  -2.355  1.00  9.96           C  
ANISOU 2889  CA  GLU B 308      964    887   1931   -219    145   -387       C  
ATOM   2890  C   GLU B 308      68.339   6.789  -0.903  1.00 10.36           C  
ANISOU 2890  C   GLU B 308      981    905   2051    174     33   -266       C  
ATOM   2891  O   GLU B 308      69.158   6.688   0.023  1.00 10.63           O  
ANISOU 2891  O   GLU B 308      962   1019   2057    112    -54   -129       O  
ATOM   2892  CB  GLU B 308      68.331   5.227  -2.873  1.00 11.18           C  
ANISOU 2892  CB  GLU B 308     1331    792   2125     53     63   -301       C  
ATOM   2893  CG  GLU B 308      68.754   4.938  -4.318  1.00 11.74           C  
ANISOU 2893  CG  GLU B 308     1525    996   1940    187   -128   -196       C  
ATOM   2894  CD  GLU B 308      67.932   5.685  -5.376  1.00 12.89           C  
ANISOU 2894  CD  GLU B 308     1501   1222   2172     74    115   -441       C  
ATOM   2895  OE1 GLU B 308      66.959   6.393  -5.039  1.00 13.84           O  
ANISOU 2895  OE1 GLU B 308     1761   1561   1935    394      7   -309       O  
ATOM   2896  OE2 GLU B 308      68.257   5.550  -6.569  1.00 15.59           O  
ANISOU 2896  OE2 GLU B 308     1688   2092   2142    280    202    -91       O  
ATOM   2897  N   LEU B 309      67.052   7.063  -0.695  1.00 10.86           N  
ANISOU 2897  N   LEU B 309     1018    962   2145    210    109     -5       N  
ATOM   2898  CA  LEU B 309      66.548   7.381   0.647  1.00 10.73           C  
ANISOU 2898  CA  LEU B 309      913    984   2181    204    -73    -70       C  
ATOM   2899  C   LEU B 309      66.677   6.244   1.658  1.00 11.13           C  
ANISOU 2899  C   LEU B 309     1204    799   2227    114   -225   -226       C  
ATOM   2900  O   LEU B 309      66.703   6.485   2.863  1.00 11.78           O  
ANISOU 2900  O   LEU B 309     1263    986   2226    166   -146   -225       O  
ATOM   2901  CB  LEU B 309      65.096   7.872   0.583  1.00 11.56           C  
ANISOU 2901  CB  LEU B 309      949    947   2494    239   -276     66       C  
ATOM   2902  CG  LEU B 309      64.931   9.222  -0.114  1.00 11.98           C  
ANISOU 2902  CG  LEU B 309     1105    811   2636     99   -295     74       C  
ATOM   2903  CD1 LEU B 309      63.450   9.568  -0.249  1.00 15.03           C  
ANISOU 2903  CD1 LEU B 309     1101   1286   3322    217   -522   -233       C  
ATOM   2904  CD2 LEU B 309      65.662  10.334   0.640  1.00 13.55           C  
ANISOU 2904  CD2 LEU B 309     1397    937   2814    114   -443   -327       C  
ATOM   2905  N   ASP B 310      66.767   5.006   1.174  1.00 10.88           N  
ANISOU 2905  N   ASP B 310     1141    680   2311    104    -40     18       N  
ATOM   2906  CA  ASP B 310      66.991   3.867   2.067  1.00 12.48           C  
ANISOU 2906  CA  ASP B 310     1444    885   2413     78     12     41       C  
ATOM   2907  C   ASP B 310      68.473   3.643   2.384  1.00 12.51           C  
ANISOU 2907  C   ASP B 310     1372   1170   2209    299    102     82       C  
ATOM   2908  O   ASP B 310      68.821   2.746   3.148  1.00 15.31           O  
ANISOU 2908  O   ASP B 310     1873   1411   2533    625     78    311       O  
ATOM   2909  CB  ASP B 310      66.333   2.590   1.529  1.00 14.20           C  
ANISOU 2909  CB  ASP B 310     1913    931   2550    -10    135   -304       C  
ATOM   2910  CG  ASP B 310      66.981   2.072   0.258  1.00 14.88           C  
ANISOU 2910  CG  ASP B 310     2222    743   2688    -68    226     67       C  
ATOM   2911  OD1 ASP B 310      67.890   2.732  -0.284  1.00 14.00           O  
ANISOU 2911  OD1 ASP B 310     1753   1087   2478    135    153    -33       O  
ATOM   2912  OD2 ASP B 310      66.570   0.978  -0.202  1.00 19.44           O  
ANISOU 2912  OD2 ASP B 310     2888   1019   3477    -58    523   -151       O  
ATOM   2913  N   GLY B 311      69.340   4.465   1.802  1.00 12.00           N  
ANISOU 2913  N   GLY B 311     1105   1214   2241    282     58   -202       N  
ATOM   2914  CA  GLY B 311      70.759   4.398   2.102  1.00 13.81           C  
ANISOU 2914  CA  GLY B 311     1405   1311   2531    517    203     86       C  
ATOM   2915  C   GLY B 311      71.578   3.586   1.119  1.00 14.85           C  
ANISOU 2915  C   GLY B 311     1697   1247   2696    367    -86     24       C  
ATOM   2916  O   GLY B 311      72.813   3.593   1.176  1.00 17.81           O  
ANISOU 2916  O   GLY B 311     1525   1782   3461    600    189    -28       O  
ATOM   2917  N   ASN B 312      70.898   2.878   0.224  1.00 13.71           N  
ANISOU 2917  N   ASN B 312     1673   1192   2342    395    500    129       N  
ATOM   2918  CA  ASN B 312      71.584   2.138  -0.829  1.00 16.07           C  
ANISOU 2918  CA  ASN B 312     1857   1392   2855    391    493   -300       C  
ATOM   2919  C   ASN B 312      72.067   3.089  -1.918  1.00 14.70           C  
ANISOU 2919  C   ASN B 312     1610   1316   2658    402    200     17       C  
ATOM   2920  O   ASN B 312      71.551   4.194  -2.042  1.00 14.40           O  
ANISOU 2920  O   ASN B 312     1606   1097   2769    494     65     55       O  
ATOM   2921  CB  ASN B 312      70.673   1.052  -1.396  1.00 19.91           C  
ANISOU 2921  CB  ASN B 312     2411   1629   3523    494   1029   -283       C  
ATOM   2922  CG  ASN B 312      70.476  -0.092  -0.429  1.00 24.46           C  
ANISOU 2922  CG  ASN B 312     2740   1703   4849    520   1297     78       C  
ATOM   2923  OD1 ASN B 312      71.442  -0.698   0.040  1.00 28.37           O  
ANISOU 2923  OD1 ASN B 312     3086   2186   5508    838   1566    762       O  
ATOM   2924  ND2 ASN B 312      69.223  -0.389  -0.113  1.00 25.99           N  
ANISOU 2924  ND2 ASN B 312     2850   1799   5226    530   1328     56       N  
ATOM   2925  N   PRO B 313      73.070   2.676  -2.699  1.00 15.00           N  
ANISOU 2925  N   PRO B 313     1754   1315   2630    690    365    403       N  
ATOM   2926  CA  PRO B 313      73.683   3.621  -3.638  1.00 16.19           C  
ANISOU 2926  CA  PRO B 313     1762   1582   2808    668    526    836       C  
ATOM   2927  C   PRO B 313      72.730   4.073  -4.733  1.00 16.28           C  
ANISOU 2927  C   PRO B 313     1933   1439   2812    506    264    366       C  
ATOM   2928  O   PRO B 313      71.858   3.308  -5.151  1.00 16.75           O  
ANISOU 2928  O   PRO B 313     1980   1783   2599    361    200    168       O  
ATOM   2929  CB  PRO B 313      74.836   2.819  -4.258  1.00 17.98           C  
ANISOU 2929  CB  PRO B 313     1822   1754   3253    759    754    610       C  
ATOM   2930  CG  PRO B 313      75.075   1.690  -3.318  1.00 21.15           C  
ANISOU 2930  CG  PRO B 313     2220   2033   3783    910    935    762       C  
ATOM   2931  CD  PRO B 313      73.762   1.376  -2.677  1.00 17.50           C  
ANISOU 2931  CD  PRO B 313     1885   1737   3025    826    728    447       C  
ATOM   2932  N   TYR B 314      72.894   5.314  -5.178  1.00 15.72           N  
ANISOU 2932  N   TYR B 314     2049   1499   2424    618    274    337       N  
ATOM   2933  CA  TYR B 314      72.185   5.800  -6.347  1.00 17.37           C  
ANISOU 2933  CA  TYR B 314     2384   1671   2544    898    630    107       C  
ATOM   2934  C   TYR B 314      73.021   5.463  -7.573  1.00 21.62           C  
ANISOU 2934  C   TYR B 314     2803   2405   3005    975    879    402       C  
ATOM   2935  O   TYR B 314      74.141   5.955  -7.726  1.00 21.83           O  
ANISOU 2935  O   TYR B 314     2839   2616   2839    769    927    553       O  
ATOM   2936  CB  TYR B 314      71.939   7.311  -6.244  1.00 15.80           C  
ANISOU 2936  CB  TYR B 314     2289   1202   2511    497    520    350       C  
ATOM   2937  CG  TYR B 314      71.490   7.953  -7.537  1.00 15.38           C  
ANISOU 2937  CG  TYR B 314     2136   1491   2216    566    396    293       C  
ATOM   2938  CD1 TYR B 314      70.329   7.540  -8.181  1.00 15.48           C  
ANISOU 2938  CD1 TYR B 314     1773   1620   2487    450    660    314       C  
ATOM   2939  CD2 TYR B 314      72.227   8.980  -8.107  1.00 17.21           C  
ANISOU 2939  CD2 TYR B 314     2272   1540   2726    292    474    543       C  
ATOM   2940  CE1 TYR B 314      69.923   8.129  -9.364  1.00 15.25           C  
ANISOU 2940  CE1 TYR B 314     1929   1726   2138    673    696    457       C  
ATOM   2941  CE2 TYR B 314      71.831   9.572  -9.289  1.00 16.26           C  
ANISOU 2941  CE2 TYR B 314     2181   1567   2429    319     83    507       C  
ATOM   2942  CZ  TYR B 314      70.680   9.145  -9.911  1.00 14.59           C  
ANISOU 2942  CZ  TYR B 314     2053   1433   2058    482    454    513       C  
ATOM   2943  OH  TYR B 314      70.292   9.747 -11.084  1.00 16.79           O  
ANISOU 2943  OH  TYR B 314     2143   1717   2519    538    328    532       O  
ATOM   2944  N   HIS B 315      72.477   4.608  -8.433  1.00 23.52           N  
ANISOU 2944  N   HIS B 315     3221   2724   2989   1490    978     88       N  
ATOM   2945  CA  HIS B 315      73.212   4.102  -9.587  1.00 28.51           C  
ANISOU 2945  CA  HIS B 315     4054   3147   3631   1886   1037    189       C  
ATOM   2946  C   HIS B 315      72.879   4.826 -10.890  1.00 28.70           C  
ANISOU 2946  C   HIS B 315     4022   3456   3427   1856   1049     96       C  
ATOM   2947  O   HIS B 315      73.551   4.627 -11.901  1.00 30.17           O  
ANISOU 2947  O   HIS B 315     4015   3532   3914   1741    994    -38       O  
ATOM   2948  CB  HIS B 315      72.985   2.594  -9.744  1.00 31.80           C  
ANISOU 2948  CB  HIS B 315     4651   3350   4081   2126   1047    250       C  
ATOM   2949  CG  HIS B 315      73.684   1.767  -8.710  1.00 37.26           C  
ANISOU 2949  CG  HIS B 315     5394   3757   5006   2416   1046    467       C  
ATOM   2950  ND1 HIS B 315      73.007   0.990  -7.793  1.00 40.48           N  
ANISOU 2950  ND1 HIS B 315     5731   3826   5822   2363    708    560       N  
ATOM   2951  CD2 HIS B 315      75.002   1.597  -8.445  1.00 38.25           C  
ANISOU 2951  CD2 HIS B 315     5502   3847   5185   2531   1019    646       C  
ATOM   2952  CE1 HIS B 315      73.877   0.373  -7.014  1.00 40.41           C  
ANISOU 2952  CE1 HIS B 315     5678   3887   5788   2512    803    823       C  
ATOM   2953  NE2 HIS B 315      75.095   0.725  -7.386  1.00 40.44           N  
ANISOU 2953  NE2 HIS B 315     5711   4007   5645   2644    920    554       N  
ATOM   2954  N   ALA B 316      71.846   5.663 -10.858  1.00 26.82           N  
ANISOU 2954  N   ALA B 316     3805   3508   2878   1805    872   -227       N  
ATOM   2955  CA  ALA B 316      71.434   6.449 -12.022  1.00 27.21           C  
ANISOU 2955  CA  ALA B 316     4175   3281   2883   1694   1308    289       C  
ATOM   2956  C   ALA B 316      71.003   5.604 -13.228  1.00 30.05           C  
ANISOU 2956  C   ALA B 316     4502   3463   3453   1712    988    157       C  
ATOM   2957  O   ALA B 316      71.104   6.048 -14.372  1.00 32.78           O  
ANISOU 2957  O   ALA B 316     5002   3895   3556   1679    157     72       O  
ATOM   2958  CB  ALA B 316      72.532   7.431 -12.423  1.00 28.51           C  
ANISOU 2958  CB  ALA B 316     4185   3132   3515   1611   1095    627       C  
ATOM   2959  N   PHE B 317      70.511   4.396 -12.972  1.00 29.51           N  
ANISOU 2959  N   PHE B 317     4293   3407   3510   1940    735   -481       N  
ATOM   2960  CA  PHE B 317      70.035   3.531 -14.046  1.00 31.03           C  
ANISOU 2960  CA  PHE B 317     4582   3422   3786   2074    381   -548       C  
ATOM   2961  C   PHE B 317      68.629   3.916 -14.489  1.00 30.10           C  
ANISOU 2961  C   PHE B 317     4663   3084   3690   1456     85   -690       C  
ATOM   2962  O   PHE B 317      68.267   3.749 -15.655  1.00 32.05           O  
ANISOU 2962  O   PHE B 317     4949   3415   3811   1376   -301   -908       O  
ATOM   2963  CB  PHE B 317      70.020   2.068 -13.594  1.00 36.80           C  
ANISOU 2963  CB  PHE B 317     4898   4112   4970   2562    274   -490       C  
ATOM   2964  CG  PHE B 317      71.382   1.487 -13.346  1.00 42.78           C  
ANISOU 2964  CG  PHE B 317     5167   4864   6223   2795    330   -383       C  
ATOM   2965  CD1 PHE B 317      72.513   2.043 -13.928  1.00 43.94           C  
ANISOU 2965  CD1 PHE B 317     5150   5162   6384   2961    419   -400       C  
ATOM   2966  CD2 PHE B 317      71.531   0.377 -12.531  1.00 45.27           C  
ANISOU 2966  CD2 PHE B 317     5270   5128   6803   2775    279   -256       C  
ATOM   2967  CE1 PHE B 317      73.764   1.506 -13.695  1.00 45.92           C  
ANISOU 2967  CE1 PHE B 317     5266   5460   6722   3021    405   -204       C  
ATOM   2968  CE2 PHE B 317      72.779  -0.169 -12.296  1.00 46.93           C  
ANISOU 2968  CE2 PHE B 317     5285   5421   7126   2853    432   -179       C  
ATOM   2969  CZ  PHE B 317      73.898   0.395 -12.879  1.00 47.33           C  
ANISOU 2969  CZ  PHE B 317     5326   5471   7184   2922    326   -112       C  
ATOM   2970  N   ASP B 318      67.846   4.433 -13.549  1.00 27.30           N  
ANISOU 2970  N   ASP B 318     4226   2210   3937   1317    516   -611       N  
ATOM   2971  CA  ASP B 318      66.404   4.545 -13.728  1.00 27.96           C  
ANISOU 2971  CA  ASP B 318     4253   2058   4311    875    451   -116       C  
ATOM   2972  C   ASP B 318      65.883   5.973 -13.645  1.00 23.47           C  
ANISOU 2972  C   ASP B 318     3535   1774   3607    601     -2   -237       C  
ATOM   2973  O   ASP B 318      64.812   6.273 -14.164  1.00 24.85           O  
ANISOU 2973  O   ASP B 318     3492   1741   4208    318      1   -421       O  
ATOM   2974  CB  ASP B 318      65.688   3.701 -12.667  1.00 32.78           C  
ANISOU 2974  CB  ASP B 318     5014   2000   5441    739    735     71       C  
ATOM   2975  CG  ASP B 318      66.218   2.289 -12.594  1.00 40.28           C  
ANISOU 2975  CG  ASP B 318     5721   2651   6932    840    721   -404       C  
ATOM   2976  OD1 ASP B 318      66.496   1.710 -13.662  1.00 41.27           O  
ANISOU 2976  OD1 ASP B 318     5980   2799   6901    845    818  -1161       O  
ATOM   2977  OD2 ASP B 318      66.362   1.762 -11.470  1.00 43.62           O  
ANISOU 2977  OD2 ASP B 318     6099   2778   7697    801    672   -426       O  
ATOM   2978  N   SER B 319      66.625   6.855 -12.986  1.00 18.19           N  
ANISOU 2978  N   SER B 319     2840   1300   2770    321    -51   -144       N  
ATOM   2979  CA  SER B 319      66.084   8.172 -12.662  1.00 15.03           C  
ANISOU 2979  CA  SER B 319     2379   1415   1915    259    225    -61       C  
ATOM   2980  C   SER B 319      67.144   9.262 -12.762  1.00 15.47           C  
ANISOU 2980  C   SER B 319     2000   1507   2372    314    184    271       C  
ATOM   2981  O   SER B 319      68.342   8.976 -12.644  1.00 16.24           O  
ANISOU 2981  O   SER B 319     1766   1812   2591    400    420     36       O  
ATOM   2982  CB  SER B 319      65.468   8.150 -11.264  1.00 15.19           C  
ANISOU 2982  CB  SER B 319     2192   1998   1582    206   -422    208       C  
ATOM   2983  OG  SER B 319      66.432   7.743 -10.311  1.00 16.65           O  
ANISOU 2983  OG  SER B 319     2345   1919   2062    354    -72    169       O  
ATOM   2984  N   PRO B 320      66.703  10.513 -12.995  1.00 14.16           N  
ANISOU 2984  N   PRO B 320     1732   1555   2091    451     92   -125       N  
ATOM   2985  CA  PRO B 320      67.597  11.660 -13.197  1.00 14.41           C  
ANISOU 2985  CA  PRO B 320     1802   1577   2097    259    249    186       C  
ATOM   2986  C   PRO B 320      68.251  12.124 -11.901  1.00 12.49           C  
ANISOU 2986  C   PRO B 320     1362   1258   2124     10    359    176       C  
ATOM   2987  O   PRO B 320      69.171  12.940 -11.929  1.00 13.94           O  
ANISOU 2987  O   PRO B 320     1263   1442   2591     65    493     96       O  
ATOM   2988  CB  PRO B 320      66.659  12.739 -13.728  1.00 15.20           C  
ANISOU 2988  CB  PRO B 320     1976   1559   2240    420    -24    230       C  
ATOM   2989  CG  PRO B 320      65.341  12.404 -13.151  1.00 16.01           C  
ANISOU 2989  CG  PRO B 320     1765   1460   2857    350     94    290       C  
ATOM   2990  CD  PRO B 320      65.285  10.899 -13.129  1.00 13.38           C  
ANISOU 2990  CD  PRO B 320     1779   1206   2098    387   -243    -79       C  
ATOM   2991  N   ALA B 321      67.762  11.605 -10.781  1.00 12.51           N  
ANISOU 2991  N   ALA B 321     1427   1536   1789    101    205    119       N  
ATOM   2992  CA  ALA B 321      68.318  11.857  -9.465  1.00 11.30           C  
ANISOU 2992  CA  ALA B 321     1326   1001   1967     12    271    -48       C  
ATOM   2993  C   ALA B 321      67.789  10.725  -8.590  1.00 11.52           C  
ANISOU 2993  C   ALA B 321     1029   1313   2036    125    176   -126       C  
ATOM   2994  O   ALA B 321      66.957   9.940  -9.034  1.00 11.48           O  
ANISOU 2994  O   ALA B 321     1198   1276   1887    128    247    -24       O  
ATOM   2995  CB  ALA B 321      67.846  13.215  -8.932  1.00 12.82           C  
ANISOU 2995  CB  ALA B 321     1303    913   2654     11    254    207       C  
ATOM   2996  N   PRO B 322      68.254  10.630  -7.340  1.00 11.43           N  
ANISOU 2996  N   PRO B 322      966   1183   2192   -136    182   -339       N  
ATOM   2997  CA  PRO B 322      67.670   9.600  -6.469  1.00 10.82           C  
ANISOU 2997  CA  PRO B 322      865   1302   1943   -134      6   -176       C  
ATOM   2998  C   PRO B 322      66.153   9.752  -6.348  1.00 10.05           C  
ANISOU 2998  C   PRO B 322     1003    919   1895    -38    141   -147       C  
ATOM   2999  O   PRO B 322      65.617  10.864  -6.455  1.00 10.86           O  
ANISOU 2999  O   PRO B 322     1119    921   2085     31    385    -44       O  
ATOM   3000  CB  PRO B 322      68.350   9.856  -5.125  1.00 12.10           C  
ANISOU 3000  CB  PRO B 322      947   1465   2186   -171    -40   -119       C  
ATOM   3001  CG  PRO B 322      69.657  10.500  -5.490  1.00 12.04           C  
ANISOU 3001  CG  PRO B 322     1080   1473   2021     52   -117     20       C  
ATOM   3002  CD  PRO B 322      69.359  11.353  -6.690  1.00 11.78           C  
ANISOU 3002  CD  PRO B 322     1227   1298   1951    -26   -169   -219       C  
ATOM   3003  N   LEU B 323      65.454   8.644  -6.136  1.00 10.16           N  
ANISOU 3003  N   LEU B 323      962   1016   1880    -98     20   -136       N  
ATOM   3004  CA  LEU B 323      63.998   8.722  -6.037  1.00  9.64           C  
ANISOU 3004  CA  LEU B 323      971    763   1928   -129    175   -103       C  
ATOM   3005  C   LEU B 323      63.579   9.682  -4.918  1.00  8.75           C  
ANISOU 3005  C   LEU B 323     1044    733   1547    -89    -89   -132       C  
ATOM   3006  O   LEU B 323      64.215   9.727  -3.856  1.00 10.09           O  
ANISOU 3006  O   LEU B 323     1133    915   1786    -42      2   -156       O  
ATOM   3007  CB  LEU B 323      63.385   7.334  -5.822  1.00 10.97           C  
ANISOU 3007  CB  LEU B 323     1275    756   2135    -44    179   -322       C  
ATOM   3008  CG  LEU B 323      63.715   6.303  -6.903  1.00 10.86           C  
ANISOU 3008  CG  LEU B 323     1423    910   1793    189     70   -510       C  
ATOM   3009  CD1 LEU B 323      62.930   5.027  -6.634  1.00 14.12           C  
ANISOU 3009  CD1 LEU B 323     1579    985   2801   -190    207   -580       C  
ATOM   3010  CD2 LEU B 323      63.409   6.849  -8.303  1.00 12.60           C  
ANISOU 3010  CD2 LEU B 323     1583   1271   1932    236     22   -550       C  
ATOM   3011  N   GLY B 324      62.531  10.469  -5.182  1.00  9.03           N  
ANISOU 3011  N   GLY B 324      935    687   1809    229     82    -36       N  
ATOM   3012  CA  GLY B 324      61.996  11.412  -4.212  1.00  9.53           C  
ANISOU 3012  CA  GLY B 324      900    990   1732     50    417   -243       C  
ATOM   3013  C   GLY B 324      62.628  12.797  -4.271  1.00  8.71           C  
ANISOU 3013  C   GLY B 324      721    930   1656   -262    247    152       C  
ATOM   3014  O   GLY B 324      62.103  13.746  -3.687  1.00 10.55           O  
ANISOU 3014  O   GLY B 324     1144    877   1986    118    253    -24       O  
ATOM   3015  N   PHE B 325      63.746  12.925  -4.975  1.00  8.65           N  
ANISOU 3015  N   PHE B 325      790    757   1739   -257     21     94       N  
ATOM   3016  CA  PHE B 325      64.497  14.176  -5.006  1.00  9.63           C  
ANISOU 3016  CA  PHE B 325      738    887   2032   -102    253     -8       C  
ATOM   3017  C   PHE B 325      63.582  15.339  -5.407  1.00  9.53           C  
ANISOU 3017  C   PHE B 325      852    895   1874    167    -77     95       C  
ATOM   3018  O   PHE B 325      62.768  15.198  -6.314  1.00 10.14           O  
ANISOU 3018  O   PHE B 325     1060   1055   1738      3     -9     41       O  
ATOM   3019  CB  PHE B 325      65.650  14.053  -6.008  1.00 10.91           C  
ANISOU 3019  CB  PHE B 325      764   1160   2219    -13    280    -70       C  
ATOM   3020  CG  PHE B 325      66.769  15.034  -5.782  1.00 11.19           C  
ANISOU 3020  CG  PHE B 325     1004   1171   2077    -23    210    -34       C  
ATOM   3021  CD1 PHE B 325      67.815  14.730  -4.920  1.00 13.82           C  
ANISOU 3021  CD1 PHE B 325     1116   1657   2477     34    301   -642       C  
ATOM   3022  CD2 PHE B 325      66.783  16.252  -6.444  1.00 12.45           C  
ANISOU 3022  CD2 PHE B 325     1304   1150   2275   -139    740   -304       C  
ATOM   3023  CE1 PHE B 325      68.849  15.633  -4.719  1.00 14.52           C  
ANISOU 3023  CE1 PHE B 325     1261   1807   2450    -53    387   -910       C  
ATOM   3024  CE2 PHE B 325      67.808  17.156  -6.242  1.00 15.43           C  
ANISOU 3024  CE2 PHE B 325     1446   1564   2852   -187    719   -135       C  
ATOM   3025  CZ  PHE B 325      68.842  16.844  -5.382  1.00 15.96           C  
ANISOU 3025  CZ  PHE B 325     1398   1843   2823    -95    570   -623       C  
ATOM   3026  N   PRO B 326      63.711  16.496  -4.735  1.00  9.92           N  
ANISOU 3026  N   PRO B 326      985    756   2029     -9   -102     43       N  
ATOM   3027  CA  PRO B 326      62.859  17.632  -5.134  1.00  9.99           C  
ANISOU 3027  CA  PRO B 326     1162    928   1706    -84   -308    -75       C  
ATOM   3028  C   PRO B 326      62.991  17.972  -6.625  1.00 10.19           C  
ANISOU 3028  C   PRO B 326     1010   1046   1816   -117   -247    -50       C  
ATOM   3029  O   PRO B 326      64.094  17.913  -7.169  1.00 11.66           O  
ANISOU 3029  O   PRO B 326     1282   1273   1874     -8     14    193       O  
ATOM   3030  CB  PRO B 326      63.388  18.797  -4.280  1.00 11.87           C  
ANISOU 3030  CB  PRO B 326     1486   1027   1995    222   -169   -278       C  
ATOM   3031  CG  PRO B 326      64.073  18.160  -3.120  1.00 14.23           C  
ANISOU 3031  CG  PRO B 326     1406   1171   2829    382   -687   -462       C  
ATOM   3032  CD  PRO B 326      64.591  16.816  -3.599  1.00 10.49           C  
ANISOU 3032  CD  PRO B 326     1260    699   2025    136   -443   -332       C  
ATOM   3033  N   ASP B 327      61.885  18.343  -7.269  1.00  9.40           N  
ANISOU 3033  N   ASP B 327     1125    737   1707    -33   -115    164       N  
ATOM   3034  CA  ASP B 327      61.912  18.723  -8.685  1.00 10.23           C  
ANISOU 3034  CA  ASP B 327     1220    752   1914    119    -28     68       C  
ATOM   3035  C   ASP B 327      61.621  20.212  -8.919  1.00 10.18           C  
ANISOU 3035  C   ASP B 327     1165    732   1972    -38     33     44       C  
ATOM   3036  O   ASP B 327      61.055  20.606  -9.952  1.00 11.40           O  
ANISOU 3036  O   ASP B 327     1396   1067   1869      5    -75    165       O  
ATOM   3037  CB  ASP B 327      61.007  17.820  -9.539  1.00 11.62           C  
ANISOU 3037  CB  ASP B 327     1137    958   2320     10    176   -104       C  
ATOM   3038  CG  ASP B 327      59.524  18.037  -9.287  1.00 10.70           C  
ANISOU 3038  CG  ASP B 327     1316    855   1894    183    -31   -327       C  
ATOM   3039  OD1 ASP B 327      59.153  18.801  -8.372  1.00 10.65           O  
ANISOU 3039  OD1 ASP B 327     1185    895   1965    166     91   -104       O  
ATOM   3040  OD2 ASP B 327      58.723  17.415 -10.019  1.00 11.49           O  
ANISOU 3040  OD2 ASP B 327     1361   1048   1955    161    -23   -208       O  
ATOM   3041  N   PHE B 328      62.054  21.038  -7.968  1.00  9.75           N  
ANISOU 3041  N   PHE B 328     1248    578   1876    -56    209   -117       N  
ATOM   3042  CA  PHE B 328      61.966  22.489  -8.106  1.00 10.22           C  
ANISOU 3042  CA  PHE B 328     1371    809   1701    -19    378     77       C  
ATOM   3043  C   PHE B 328      63.291  23.005  -8.633  1.00 10.82           C  
ANISOU 3043  C   PHE B 328     1462    947   1702   -118     61     29       C  
ATOM   3044  O   PHE B 328      64.325  22.820  -7.996  1.00 12.52           O  
ANISOU 3044  O   PHE B 328     1448   1241   2069    -88     25    -83       O  
ATOM   3045  CB  PHE B 328      61.618  23.117  -6.759  1.00 10.52           C  
ANISOU 3045  CB  PHE B 328     1336    817   1844    -76    181    -86       C  
ATOM   3046  CG  PHE B 328      60.285  22.669  -6.233  1.00 10.68           C  
ANISOU 3046  CG  PHE B 328     1309    903   1845   -158    196    -69       C  
ATOM   3047  CD1 PHE B 328      59.114  23.165  -6.788  1.00 12.36           C  
ANISOU 3047  CD1 PHE B 328     1388   1385   1923    165    116     18       C  
ATOM   3048  CD2 PHE B 328      60.201  21.710  -5.232  1.00 11.93           C  
ANISOU 3048  CD2 PHE B 328     1406   1403   1723     48    225     69       C  
ATOM   3049  CE1 PHE B 328      57.877  22.735  -6.333  1.00 12.32           C  
ANISOU 3049  CE1 PHE B 328     1506   1411   1763      3    214    108       C  
ATOM   3050  CE2 PHE B 328      58.966  21.278  -4.769  1.00 12.38           C  
ANISOU 3050  CE2 PHE B 328     1598   1358   1749     48    311    171       C  
ATOM   3051  CZ  PHE B 328      57.805  21.794  -5.323  1.00 12.07           C  
ANISOU 3051  CZ  PHE B 328     1577   1249   1759    159    -79     29       C  
ATOM   3052  N   GLY B 329      63.262  23.629  -9.810  1.00 11.07           N  
ANISOU 3052  N   GLY B 329     1445   1016   1744   -217    321    116       N  
ATOM   3053  CA  GLY B 329      64.485  24.059 -10.468  1.00 12.10           C  
ANISOU 3053  CA  GLY B 329     1579   1107   1912   -252    310    114       C  
ATOM   3054  C   GLY B 329      64.755  25.547 -10.374  1.00 11.46           C  
ANISOU 3054  C   GLY B 329     1456   1035   1861   -305    474     38       C  
ATOM   3055  O   GLY B 329      63.836  26.362 -10.228  1.00 12.96           O  
ANISOU 3055  O   GLY B 329     1427   1332   2164   -296    312     -7       O  
ATOM   3056  N   ASN B 330      66.034  25.896 -10.457  1.00 11.78           N  
ANISOU 3056  N   ASN B 330     1553    937   1985   -324    253     78       N  
ATOM   3057  CA  ASN B 330      66.469  27.298 -10.488  1.00 13.31           C  
ANISOU 3057  CA  ASN B 330     1762   1168   2126   -321    235    254       C  
ATOM   3058  C   ASN B 330      66.020  28.117  -9.281  1.00 13.24           C  
ANISOU 3058  C   ASN B 330     1859   1231   1938   -177    227    103       C  
ATOM   3059  O   ASN B 330      65.624  29.278  -9.422  1.00 14.75           O  
ANISOU 3059  O   ASN B 330     2172   1292   2140   -154    352    360       O  
ATOM   3060  CB  ASN B 330      66.027  28.008 -11.774  1.00 14.68           C  
ANISOU 3060  CB  ASN B 330     1838   1469   2269   -311    370    417       C  
ATOM   3061  CG  ASN B 330      66.910  29.189 -12.096  1.00 14.76           C  
ANISOU 3061  CG  ASN B 330     2030   1523   2054   -252    576    367       C  
ATOM   3062  OD1 ASN B 330      68.138  29.082 -12.036  1.00 17.80           O  
ANISOU 3062  OD1 ASN B 330     1977   1822   2962   -334    484    502       O  
ATOM   3063  ND2 ASN B 330      66.300  30.328 -12.421  1.00 16.17           N  
ANISOU 3063  ND2 ASN B 330     2269   1528   2347    -86    354    374       N  
ATOM   3064  N   CYS B 331      66.086  27.518  -8.099  1.00 12.25           N  
ANISOU 3064  N   CYS B 331     1576   1046   2033   -170    187      4       N  
ATOM   3065  CA  CYS B 331      65.647  28.190  -6.889  1.00 11.61           C  
ANISOU 3065  CA  CYS B 331     1539   1268   1604   -222    152    -27       C  
ATOM   3066  C   CYS B 331      66.451  27.725  -5.684  1.00 11.91           C  
ANISOU 3066  C   CYS B 331     1557    930   2037   -181     46     20       C  
ATOM   3067  O   CYS B 331      67.320  26.865  -5.801  1.00 12.47           O  
ANISOU 3067  O   CYS B 331     1553    867   2319   -151    185    -36       O  
ATOM   3068  CB  CYS B 331      64.151  27.953  -6.658  1.00 12.51           C  
ANISOU 3068  CB  CYS B 331     1350   1144   2258   -312    129   -112       C  
ATOM   3069  SG  CYS B 331      63.673  26.212  -6.581  1.00 13.04           S  
ANISOU 3069  SG  CYS B 331     1678   1115   2161   -185    287     24       S  
ATOM   3070  N   ASP B 332      66.165  28.310  -4.528  1.00 12.03           N  
ANISOU 3070  N   ASP B 332     1516   1168   1887   -290    -29   -178       N  
ATOM   3071  CA  ASP B 332      66.898  28.000  -3.312  1.00 11.67           C  
ANISOU 3071  CA  ASP B 332     1533   1018   1882   -343   -104   -142       C  
ATOM   3072  C   ASP B 332      66.078  27.065  -2.439  1.00 11.18           C  
ANISOU 3072  C   ASP B 332     1497    906   1843    -98    141   -100       C  
ATOM   3073  O   ASP B 332      65.014  27.443  -1.936  1.00 12.19           O  
ANISOU 3073  O   ASP B 332     1444   1037   2150    187    242    -15       O  
ATOM   3074  CB  ASP B 332      67.219  29.291  -2.549  1.00 13.25           C  
ANISOU 3074  CB  ASP B 332     1635   1027   2370   -423    198    -22       C  
ATOM   3075  CG  ASP B 332      68.267  30.144  -3.245  1.00 14.38           C  
ANISOU 3075  CG  ASP B 332     1920   1163   2379   -192     44   -446       C  
ATOM   3076  OD1 ASP B 332      68.693  29.794  -4.371  1.00 14.79           O  
ANISOU 3076  OD1 ASP B 332     1883   1113   2621   -255    297     17       O  
ATOM   3077  OD2 ASP B 332      68.659  31.180  -2.661  1.00 16.79           O  
ANISOU 3077  OD2 ASP B 332     2012   1127   3239   -377   -130   -477       O  
ATOM   3078  N   LEU B 333      66.589  25.848  -2.264  1.00 11.05           N  
ANISOU 3078  N   LEU B 333     1577    683   1937   -375   -146     64       N  
ATOM   3079  CA  LEU B 333      65.921  24.837  -1.452  1.00 10.88           C  
ANISOU 3079  CA  LEU B 333     1445    705   1983   -252    -69   -294       C  
ATOM   3080  C   LEU B 333      66.411  24.964  -0.013  1.00  9.92           C  
ANISOU 3080  C   LEU B 333     1323    972   1472   -203    -35   -244       C  
ATOM   3081  O   LEU B 333      67.600  24.806   0.268  1.00 12.73           O  
ANISOU 3081  O   LEU B 333     1084   1619   2134   -147    -96   -221       O  
ATOM   3082  CB  LEU B 333      66.237  23.437  -1.984  1.00  9.71           C  
ANISOU 3082  CB  LEU B 333     1421    707   1560    -26    116   -289       C  
ATOM   3083  CG  LEU B 333      66.009  23.206  -3.480  1.00 10.17           C  
ANISOU 3083  CG  LEU B 333     1199    842   1823    -34   -139    -73       C  
ATOM   3084  CD1 LEU B 333      66.510  21.817  -3.846  1.00 11.54           C  
ANISOU 3084  CD1 LEU B 333     1392    775   2218   -150    134      4       C  
ATOM   3085  CD2 LEU B 333      64.542  23.376  -3.818  1.00 12.14           C  
ANISOU 3085  CD2 LEU B 333     1212   1395   2006   -136      8      2       C  
ATOM   3086  N   HIS B 334      65.489  25.253   0.898  1.00  9.55           N  
ANISOU 3086  N   HIS B 334     1313    852   1463   -207    125   -139       N  
ATOM   3087  CA  HIS B 334      65.838  25.353   2.303  1.00  9.50           C  
ANISOU 3087  CA  HIS B 334     1226    675   1708    -68    197   -225       C  
ATOM   3088  C   HIS B 334      65.506  24.028   2.967  1.00  9.81           C  
ANISOU 3088  C   HIS B 334     1151    689   1885   -295    270    -89       C  
ATOM   3089  O   HIS B 334      64.333  23.708   3.193  1.00 10.06           O  
ANISOU 3089  O   HIS B 334     1100    767   1956    -61    128    -18       O  
ATOM   3090  CB  HIS B 334      65.101  26.518   2.958  1.00 11.31           C  
ANISOU 3090  CB  HIS B 334     1349    882   2067    -68     84    -85       C  
ATOM   3091  CG  HIS B 334      65.432  27.842   2.346  1.00 11.13           C  
ANISOU 3091  CG  HIS B 334     1271    749   2210   -298    197   -136       C  
ATOM   3092  ND1 HIS B 334      66.374  28.696   2.879  1.00 13.30           N  
ANISOU 3092  ND1 HIS B 334     1580    978   2493   -142    -40     30       N  
ATOM   3093  CD2 HIS B 334      64.962  28.446   1.230  1.00 13.49           C  
ANISOU 3093  CD2 HIS B 334     1728    941   2454     30    110    116       C  
ATOM   3094  CE1 HIS B 334      66.469  29.770   2.116  1.00 14.75           C  
ANISOU 3094  CE1 HIS B 334     1539   1050   3013   -248    -69     45       C  
ATOM   3095  NE2 HIS B 334      65.616  29.650   1.114  1.00 14.22           N  
ANISOU 3095  NE2 HIS B 334     1787   1033   2583     83    101     84       N  
ATOM   3096  N   MET B 335      66.553  23.260   3.252  1.00 10.21           N  
ANISOU 3096  N   MET B 335     1354    786   1739    178    -14    -17       N  
ATOM   3097  CA  MET B 335      66.404  21.916   3.790  1.00 10.64           C  
ANISOU 3097  CA  MET B 335     1283    787   1972    102   -128    170       C  
ATOM   3098  C   MET B 335      66.593  21.866   5.299  1.00 10.75           C  
ANISOU 3098  C   MET B 335     1235    784   2064   -150   -285    -74       C  
ATOM   3099  O   MET B 335      67.398  22.607   5.869  1.00 13.35           O  
ANISOU 3099  O   MET B 335     1402   1269   2399   -416   -337    -23       O  
ATOM   3100  CB  MET B 335      67.421  20.965   3.149  1.00 11.97           C  
ANISOU 3100  CB  MET B 335     1335   1107   2107    254   -151     92       C  
ATOM   3101  CG  MET B 335      67.538  21.062   1.628  1.00 11.87           C  
ANISOU 3101  CG  MET B 335     1436   1155   1918    175    -39   -118       C  
ATOM   3102  SD  MET B 335      66.049  20.591   0.732  1.00 12.17           S  
ANISOU 3102  SD  MET B 335     1389   1230   2003    238    -70    -18       S  
ATOM   3103  CE  MET B 335      65.999  18.814   1.038  1.00 11.87           C  
ANISOU 3103  CE  MET B 335     1523    859   2127    214    -90      2       C  
ATOM   3104  N   THR B 336      65.852  20.968   5.939  1.00 10.40           N  
ANISOU 3104  N   THR B 336     1213    695   2041   -137   -216   -100       N  
ATOM   3105  CA  THR B 336      66.126  20.559   7.301  1.00  9.76           C  
ANISOU 3105  CA  THR B 336     1209    806   1692    151   -137    -27       C  
ATOM   3106  C   THR B 336      66.681  19.151   7.220  1.00 10.11           C  
ANISOU 3106  C   THR B 336     1189    866   1784     42   -571    -36       C  
ATOM   3107  O   THR B 336      66.260  18.368   6.373  1.00 11.89           O  
ANISOU 3107  O   THR B 336     1548    855   2114    107   -585   -116       O  
ATOM   3108  CB  THR B 336      64.847  20.588   8.143  1.00 10.61           C  
ANISOU 3108  CB  THR B 336     1314    999   1719    245    212    123       C  
ATOM   3109  OG1 THR B 336      64.436  21.955   8.300  1.00 12.01           O  
ANISOU 3109  OG1 THR B 336     1375   1062   2127    467    -85   -169       O  
ATOM   3110  CG2 THR B 336      65.061  19.967   9.522  1.00 13.65           C  
ANISOU 3110  CG2 THR B 336     1678   1433   2076    308     77    238       C  
ATOM   3111  N   PHE B 337      67.650  18.825   8.069  1.00  9.17           N  
ANISOU 3111  N   PHE B 337     1011    654   1819    245   -235     46       N  
ATOM   3112  CA  PHE B 337      68.230  17.487   8.000  1.00 10.21           C  
ANISOU 3112  CA  PHE B 337      949    970   1959    279   -313    180       C  
ATOM   3113  C   PHE B 337      68.545  16.911   9.370  1.00 10.25           C  
ANISOU 3113  C   PHE B 337     1032    943   1920    168   -420     78       C  
ATOM   3114  O   PHE B 337      68.649  17.638  10.359  1.00 10.65           O  
ANISOU 3114  O   PHE B 337     1146    919   1979     64   -286   -253       O  
ATOM   3115  CB  PHE B 337      69.452  17.456   7.067  1.00 11.98           C  
ANISOU 3115  CB  PHE B 337     1048   1167   2335    -52    -23   -207       C  
ATOM   3116  CG  PHE B 337      70.634  18.251   7.566  1.00 11.51           C  
ANISOU 3116  CG  PHE B 337     1158    998   2217    182    -68   -323       C  
ATOM   3117  CD1 PHE B 337      71.510  17.709   8.503  1.00 12.42           C  
ANISOU 3117  CD1 PHE B 337      970   1183   2565   -104      8   -476       C  
ATOM   3118  CD2 PHE B 337      70.886  19.532   7.079  1.00 12.82           C  
ANISOU 3118  CD2 PHE B 337     1382   1103   2384    -38     28   -427       C  
ATOM   3119  CE1 PHE B 337      72.618  18.438   8.949  1.00 12.89           C  
ANISOU 3119  CE1 PHE B 337     1102    928   2867    -75    -61   -161       C  
ATOM   3120  CE2 PHE B 337      71.987  20.261   7.521  1.00 14.11           C  
ANISOU 3120  CE2 PHE B 337     1361   1387   2612     67   -104   -213       C  
ATOM   3121  CZ  PHE B 337      72.849  19.713   8.461  1.00 14.37           C  
ANISOU 3121  CZ  PHE B 337     1253   1080   3128    -83      4    -95       C  
ATOM   3122  N   VAL B 338      68.665  15.588   9.415  1.00 10.11           N  
ANISOU 3122  N   VAL B 338     1076    777   1988    199   -271    -36       N  
ATOM   3123  CA  VAL B 338      69.073  14.876  10.609  1.00 10.43           C  
ANISOU 3123  CA  VAL B 338      962    985   2016    378   -236     83       C  
ATOM   3124  C   VAL B 338      70.082  13.806  10.236  1.00  9.49           C  
ANISOU 3124  C   VAL B 338      963    940   1701    251   -383    -67       C  
ATOM   3125  O   VAL B 338      70.002  13.212   9.154  1.00 10.76           O  
ANISOU 3125  O   VAL B 338     1145   1043   1900    189   -319   -216       O  
ATOM   3126  CB  VAL B 338      67.876  14.205  11.320  1.00 10.36           C  
ANISOU 3126  CB  VAL B 338      954    993   1990    -85    -42   -495       C  
ATOM   3127  CG1 VAL B 338      66.929  15.263  11.883  1.00 11.73           C  
ANISOU 3127  CG1 VAL B 338     1268   1172   2017    332    -26   -469       C  
ATOM   3128  CG2 VAL B 338      67.133  13.265  10.383  1.00 11.64           C  
ANISOU 3128  CG2 VAL B 338     1209   1088   2126   -197    140   -245       C  
ATOM   3129  N   LYS B 339      71.038  13.578  11.128  1.00 10.61           N  
ANISOU 3129  N   LYS B 339     1041    931   2059    302   -344     86       N  
ATOM   3130  CA  LYS B 339      71.894  12.401  11.022  1.00 10.72           C  
ANISOU 3130  CA  LYS B 339      990    815   2269    162   -417    -88       C  
ATOM   3131  C   LYS B 339      71.004  11.167  11.073  1.00 10.99           C  
ANISOU 3131  C   LYS B 339     1039    921   2214    110   -249   -258       C  
ATOM   3132  O   LYS B 339      69.989  11.148  11.783  1.00 12.41           O  
ANISOU 3132  O   LYS B 339     1240   1218   2255    315    -64    -39       O  
ATOM   3133  CB  LYS B 339      72.927  12.391  12.154  1.00 12.65           C  
ANISOU 3133  CB  LYS B 339     1163   1214   2427    221   -787   -248       C  
ATOM   3134  CG  LYS B 339      73.936  13.545  12.056  1.00 12.83           C  
ANISOU 3134  CG  LYS B 339     1118   1298   2458   -230   -664    -29       C  
ATOM   3135  CD  LYS B 339      75.105  13.372  13.019  1.00 15.31           C  
ANISOU 3135  CD  LYS B 339     1306   1940   2570    157   -681   -460       C  
ATOM   3136  CE  LYS B 339      74.655  13.479  14.473  1.00 16.96           C  
ANISOU 3136  CE  LYS B 339     1376   2326   2741    441   -699   -355       C  
ATOM   3137  NZ  LYS B 339      75.835  13.458  15.410  1.00 18.21           N  
ANISOU 3137  NZ  LYS B 339     1424   2640   2853    486   -836   -447       N  
ATOM   3138  N   ILE B 340      71.368  10.142  10.311  1.00 11.15           N  
ANISOU 3138  N   ILE B 340     1113   1037   2085    221   -434   -342       N  
ATOM   3139  CA  ILE B 340      70.498   8.979  10.161  1.00 12.06           C  
ANISOU 3139  CA  ILE B 340     1151   1044   2385    385   -315   -159       C  
ATOM   3140  C   ILE B 340      71.166   7.641  10.523  1.00 12.10           C  
ANISOU 3140  C   ILE B 340      930   1179   2489    183   -282   -160       C  
ATOM   3141  O   ILE B 340      70.494   6.611  10.595  1.00 13.37           O  
ANISOU 3141  O   ILE B 340     1379   1044   2657     43   -406    -69       O  
ATOM   3142  CB  ILE B 340      69.879   8.936   8.737  1.00 11.04           C  
ANISOU 3142  CB  ILE B 340     1066   1102   2027     67   -170   -149       C  
ATOM   3143  CG1 ILE B 340      68.649   8.023   8.697  1.00 12.21           C  
ANISOU 3143  CG1 ILE B 340     1179   1213   2247    -10      0   -186       C  
ATOM   3144  CG2 ILE B 340      70.912   8.539   7.700  1.00 12.51           C  
ANISOU 3144  CG2 ILE B 340     1134   1237   2381     42    176   -294       C  
ATOM   3145  CD1 ILE B 340      67.501   8.484   9.609  1.00 14.34           C  
ANISOU 3145  CD1 ILE B 340     1217   1570   2662    -65   -337   -165       C  
ATOM   3146  N   ASN B 341      72.473   7.655  10.772  1.00 12.76           N  
ANISOU 3146  N   ASN B 341     1102   1252   2495    460   -275      4       N  
ATOM   3147  CA  ASN B 341      73.137   6.443  11.241  1.00 13.73           C  
ANISOU 3147  CA  ASN B 341     1210   1380   2627    501   -188    208       C  
ATOM   3148  C   ASN B 341      72.762   6.213  12.702  1.00 14.04           C  
ANISOU 3148  C   ASN B 341     1298   1270   2766    507   -238    136       C  
ATOM   3149  O   ASN B 341      72.921   7.111  13.524  1.00 13.96           O  
ANISOU 3149  O   ASN B 341     1349   1271   2683    407   -442    -66       O  
ATOM   3150  CB  ASN B 341      74.655   6.595  11.101  1.00 15.46           C  
ANISOU 3150  CB  ASN B 341     1286   1719   2869    661   -202    202       C  
ATOM   3151  CG  ASN B 341      75.418   5.323  11.429  1.00 18.50           C  
ANISOU 3151  CG  ASN B 341     1586   2184   3258    827    101    463       C  
ATOM   3152  OD1 ASN B 341      74.994   4.506  12.241  1.00 18.14           O  
ANISOU 3152  OD1 ASN B 341     1579   1948   3366    823    150    253       O  
ATOM   3153  ND2 ASN B 341      76.572   5.168  10.798  1.00 26.68           N  
ANISOU 3153  ND2 ASN B 341     2428   3280   4430   1350    835    861       N  
ATOM   3154  N   PRO B 342      72.251   5.017  13.035  1.00 13.82           N  
ANISOU 3154  N   PRO B 342     1413   1210   2627    223    -95    -72       N  
ATOM   3155  CA  PRO B 342      71.863   4.798  14.434  1.00 15.55           C  
ANISOU 3155  CA  PRO B 342     1660   1218   3030    307      0    129       C  
ATOM   3156  C   PRO B 342      72.975   5.106  15.436  1.00 15.65           C  
ANISOU 3156  C   PRO B 342     1593   1531   2822    462    -58    333       C  
ATOM   3157  O   PRO B 342      72.673   5.515  16.557  1.00 16.67           O  
ANISOU 3157  O   PRO B 342     1975   1493   2866    702    -41    244       O  
ATOM   3158  CB  PRO B 342      71.488   3.313  14.466  1.00 17.50           C  
ANISOU 3158  CB  PRO B 342     2067   1457   3125    232    233    262       C  
ATOM   3159  CG  PRO B 342      71.036   3.023  13.074  1.00 20.37           C  
ANISOU 3159  CG  PRO B 342     2263   1723   3752    117   -368   -116       C  
ATOM   3160  CD  PRO B 342      71.907   3.869  12.177  1.00 16.06           C  
ANISOU 3160  CD  PRO B 342     1871   1187   3045   -111   -309   -119       C  
ATOM   3161  N   THR B 343      74.237   4.913  15.056  1.00 15.64           N  
ANISOU 3161  N   THR B 343     1530   1582   2830    389   -566    291       N  
ATOM   3162  CA  THR B 343      75.331   5.182  15.990  1.00 17.26           C  
ANISOU 3162  CA  THR B 343     1607   2140   2811    485   -440    156       C  
ATOM   3163  C   THR B 343      75.474   6.670  16.308  1.00 17.55           C  
ANISOU 3163  C   THR B 343     1780   2137   2749    553   -536    -65       C  
ATOM   3164  O   THR B 343      76.082   7.042  17.315  1.00 20.73           O  
ANISOU 3164  O   THR B 343     2227   2461   3186    724   -749     37       O  
ATOM   3165  CB  THR B 343      76.676   4.628  15.482  1.00 21.20           C  
ANISOU 3165  CB  THR B 343     1802   2748   3504    729   -581   -159       C  
ATOM   3166  OG1 THR B 343      77.077   5.335  14.306  1.00 23.99           O  
ANISOU 3166  OG1 THR B 343     1924   3346   3845    765   -204   -361       O  
ATOM   3167  CG2 THR B 343      76.564   3.139  15.173  1.00 23.33           C  
ANISOU 3167  CG2 THR B 343     2170   2763   3929   1172   -478    -67       C  
ATOM   3168  N   GLU B 344      74.897   7.513  15.456  1.00 15.65           N  
ANISOU 3168  N   GLU B 344     1518   1653   2775    487   -465    301       N  
ATOM   3169  CA  GLU B 344      74.924   8.958  15.656  1.00 15.23           C  
ANISOU 3169  CA  GLU B 344     1443   1417   2927    254   -312    173       C  
ATOM   3170  C   GLU B 344      73.646   9.438  16.332  1.00 14.56           C  
ANISOU 3170  C   GLU B 344     1478   1295   2759    354   -512   -316       C  
ATOM   3171  O   GLU B 344      73.430  10.644  16.469  1.00 16.18           O  
ANISOU 3171  O   GLU B 344     1666   1427   3053    321   -414   -435       O  
ATOM   3172  CB  GLU B 344      75.075   9.680  14.312  1.00 15.76           C  
ANISOU 3172  CB  GLU B 344     1319   1796   2871    325   -427     93       C  
ATOM   3173  CG  GLU B 344      76.406   9.435  13.614  1.00 17.17           C  
ANISOU 3173  CG  GLU B 344     1118   2141   3265    223   -386    -68       C  
ATOM   3174  CD  GLU B 344      77.570  10.129  14.299  1.00 19.09           C  
ANISOU 3174  CD  GLU B 344     1543   2328   3383    417   -774   -158       C  
ATOM   3175  OE1 GLU B 344      77.346  11.142  15.000  1.00 19.19           O  
ANISOU 3175  OE1 GLU B 344     1618   2138   3534    341   -560    106       O  
ATOM   3176  OE2 GLU B 344      78.713   9.661  14.132  1.00 22.63           O  
ANISOU 3176  OE2 GLU B 344     1649   2755   4193    435   -555   -418       O  
ATOM   3177  N   LEU B 345      72.803   8.493  16.749  1.00 13.85           N  
ANISOU 3177  N   LEU B 345     1254   1673   2335    284   -446    116       N  
ATOM   3178  CA  LEU B 345      71.494   8.831  17.299  1.00 13.69           C  
ANISOU 3178  CA  LEU B 345     1486   1653   2060    245   -566    -21       C  
ATOM   3179  C   LEU B 345      71.285   8.290  18.709  1.00 15.45           C  
ANISOU 3179  C   LEU B 345     1737   1539   2592    236   -810   -206       C  
ATOM   3180  O   LEU B 345      70.159   7.971  19.101  1.00 15.35           O  
ANISOU 3180  O   LEU B 345     1677   1733   2421    520   -725   -193       O  
ATOM   3181  CB  LEU B 345      70.383   8.327  16.370  1.00 13.58           C  
ANISOU 3181  CB  LEU B 345     1498   1401   2261    315   -472     98       C  
ATOM   3182  CG  LEU B 345      70.329   9.003  14.996  1.00 13.39           C  
ANISOU 3182  CG  LEU B 345     1432   1295   2358    331   -713   -200       C  
ATOM   3183  CD1 LEU B 345      69.364   8.281  14.052  1.00 12.70           C  
ANISOU 3183  CD1 LEU B 345     1212   1270   2343     66   -387   -263       C  
ATOM   3184  CD2 LEU B 345      69.989  10.483  15.131  1.00 14.42           C  
ANISOU 3184  CD2 LEU B 345     1520   1031   2926    326   -476    -56       C  
ATOM   3185  N   SER B 346      72.364   8.194  19.479  1.00 16.75           N  
ANISOU 3185  N   SER B 346     2090   1788   2486    523  -1024   -205       N  
ATOM   3186  CA  SER B 346      72.250   7.714  20.852  1.00 17.43           C  
ANISOU 3186  CA  SER B 346     2122   2053   2447    697  -1070    -41       C  
ATOM   3187  C   SER B 346      72.030   8.861  21.839  1.00 17.53           C  
ANISOU 3187  C   SER B 346     2263   1971   2426    427   -994    298       C  
ATOM   3188  O   SER B 346      71.365   8.697  22.861  1.00 18.54           O  
ANISOU 3188  O   SER B 346     2544   2146   2353    299   -822     57       O  
ATOM   3189  CB  SER B 346      73.482   6.894  21.249  1.00 22.49           C  
ANISOU 3189  CB  SER B 346     2202   2631   3711    581  -1020     61       C  
ATOM   3190  OG  SER B 346      74.640   7.704  21.293  1.00 28.90           O  
ANISOU 3190  OG  SER B 346     3001   3339   4639   1064   -999   -478       O  
ATOM   3191  N   THR B 347      72.590  10.024  21.518  1.00 17.46           N  
ANISOU 3191  N   THR B 347     2179   1605   2848    435   -831   -102       N  
ATOM   3192  CA  THR B 347      72.538  11.179  22.397  1.00 17.44           C  
ANISOU 3192  CA  THR B 347     1977   2015   2635    109   -857    185       C  
ATOM   3193  C   THR B 347      72.702  12.445  21.559  1.00 17.08           C  
ANISOU 3193  C   THR B 347     1856   1919   2715     73   -806   -262       C  
ATOM   3194  O   THR B 347      73.201  12.387  20.434  1.00 18.49           O  
ANISOU 3194  O   THR B 347     2039   2283   2701    283   -992   -162       O  
ATOM   3195  CB  THR B 347      73.671  11.123  23.444  1.00 22.69           C  
ANISOU 3195  CB  THR B 347     2332   2766   3521    597  -1134   -399       C  
ATOM   3196  OG1 THR B 347      73.505  12.171  24.401  1.00 27.36           O  
ANISOU 3196  OG1 THR B 347     2868   3408   4117   1247  -1219   -241       O  
ATOM   3197  CG2 THR B 347      75.029  11.271  22.772  1.00 22.39           C  
ANISOU 3197  CG2 THR B 347     1973   2931   3603    138  -1415    -17       C  
ATOM   3198  N   GLY B 348      72.276  13.583  22.104  1.00 16.65           N  
ANISOU 3198  N   GLY B 348     1848   1836   2641    164  -1059   -178       N  
ATOM   3199  CA  GLY B 348      72.515  14.868  21.469  1.00 16.57           C  
ANISOU 3199  CA  GLY B 348     1829   1857   2609    221  -1019   -152       C  
ATOM   3200  C   GLY B 348      71.525  15.242  20.377  1.00 15.25           C  
ANISOU 3200  C   GLY B 348     1610   1855   2330     15   -895   -329       C  
ATOM   3201  O   GLY B 348      70.610  14.483  20.057  1.00 16.90           O  
ANISOU 3201  O   GLY B 348     1647   1798   2974    183   -938   -178       O  
ATOM   3202  N   ASP B 349      71.725  16.421  19.800  1.00 14.82           N  
ANISOU 3202  N   ASP B 349     1575   1803   2252    151   -609   -105       N  
ATOM   3203  CA  ASP B 349      70.853  16.965  18.761  1.00 14.08           C  
ANISOU 3203  CA  ASP B 349     1571   1531   2247    312   -616   -372       C  
ATOM   3204  C   ASP B 349      71.412  16.577  17.392  1.00 12.66           C  
ANISOU 3204  C   ASP B 349     1328   1308   2173     80   -606   -276       C  
ATOM   3205  O   ASP B 349      72.493  17.013  17.013  1.00 14.74           O  
ANISOU 3205  O   ASP B 349     1406   1659   2533    -33   -392   -429       O  
ATOM   3206  CB  ASP B 349      70.799  18.490  18.911  1.00 14.72           C  
ANISOU 3206  CB  ASP B 349     1637   1353   2603    389   -681   -704       C  
ATOM   3207  CG  ASP B 349      69.830  19.155  17.950  1.00 13.36           C  
ANISOU 3207  CG  ASP B 349     1582   1251   2244      6   -548   -492       C  
ATOM   3208  OD1 ASP B 349      69.443  18.526  16.944  1.00 13.23           O  
ANISOU 3208  OD1 ASP B 349     1496   1337   2194    132   -550   -393       O  
ATOM   3209  OD2 ASP B 349      69.467  20.327  18.201  1.00 16.60           O  
ANISOU 3209  OD2 ASP B 349     1832   1650   2826     80   -746   -404       O  
ATOM   3210  N   PRO B 350      70.673  15.743  16.639  1.00 11.60           N  
ANISOU 3210  N   PRO B 350     1158   1112   2136    -16   -371    -40       N  
ATOM   3211  CA  PRO B 350      71.187  15.264  15.353  1.00 11.60           C  
ANISOU 3211  CA  PRO B 350     1368   1079   1961    121   -426    -86       C  
ATOM   3212  C   PRO B 350      70.825  16.182  14.194  1.00 10.47           C  
ANISOU 3212  C   PRO B 350     1145   1210   1622    -59   -561   -337       C  
ATOM   3213  O   PRO B 350      71.108  15.833  13.048  1.00 12.07           O  
ANISOU 3213  O   PRO B 350     1449   1179   1956    125   -440   -333       O  
ATOM   3214  CB  PRO B 350      70.441  13.941  15.178  1.00 13.06           C  
ANISOU 3214  CB  PRO B 350     1260   1450   2250    134   -262   -163       C  
ATOM   3215  CG  PRO B 350      69.097  14.230  15.773  1.00 13.44           C  
ANISOU 3215  CG  PRO B 350     1584   1422   2100    -16   -423   -446       C  
ATOM   3216  CD  PRO B 350      69.376  15.125  16.975  1.00 13.48           C  
ANISOU 3216  CD  PRO B 350     1486   1329   2306    -85   -611   -364       C  
ATOM   3217  N   SER B 351      70.194  17.322  14.473  1.00 11.71           N  
ANISOU 3217  N   SER B 351     1001   1138   2308     44   -485   -148       N  
ATOM   3218  CA  SER B 351      69.560  18.097  13.407  1.00 11.22           C  
ANISOU 3218  CA  SER B 351     1114   1145   2004    103   -328    -61       C  
ATOM   3219  C   SER B 351      70.338  19.327  12.942  1.00 11.38           C  
ANISOU 3219  C   SER B 351     1272   1250   1801     64   -385   -224       C  
ATOM   3220  O   SER B 351      71.146  19.905  13.678  1.00 13.66           O  
ANISOU 3220  O   SER B 351     1555   1434   2202      7   -609   -242       O  
ATOM   3221  CB  SER B 351      68.152  18.526  13.825  1.00 12.76           C  
ANISOU 3221  CB  SER B 351     1184   1368   2295    269   -267   -392       C  
ATOM   3222  OG  SER B 351      68.200  19.565  14.789  1.00 13.37           O  
ANISOU 3222  OG  SER B 351     1492   1262   2327    354   -258   -311       O  
ATOM   3223  N   GLY B 352      70.063  19.731  11.709  1.00 11.45           N  
ANISOU 3223  N   GLY B 352     1383   1080   1887    111   -125    -92       N  
ATOM   3224  CA  GLY B 352      70.609  20.959  11.165  1.00 12.15           C  
ANISOU 3224  CA  GLY B 352     1552   1001   2062     13   -420    131       C  
ATOM   3225  C   GLY B 352      69.736  21.469  10.039  1.00 11.42           C  
ANISOU 3225  C   GLY B 352     1492    832   2016    -73   -230     -5       C  
ATOM   3226  O   GLY B 352      68.637  20.954   9.807  1.00 11.93           O  
ANISOU 3226  O   GLY B 352     1234   1078   2222   -204   -230   -380       O  
ATOM   3227  N   LYS B 353      70.225  22.483   9.336  1.00 13.07           N  
ANISOU 3227  N   LYS B 353     1729   1102   2133    -24   -311    -40       N  
ATOM   3228  CA  LYS B 353      69.514  23.041   8.199  1.00 13.22           C  
ANISOU 3228  CA  LYS B 353     1584   1317   2121    -21   -387    109       C  
ATOM   3229  C   LYS B 353      70.544  23.566   7.222  1.00 12.12           C  
ANISOU 3229  C   LYS B 353     1622   1205   1778   -345   -446   -256       C  
ATOM   3230  O   LYS B 353      71.674  23.871   7.611  1.00 14.77           O  
ANISOU 3230  O   LYS B 353     1710   1467   2435   -421   -456   -124       O  
ATOM   3231  CB  LYS B 353      68.574  24.164   8.644  1.00 15.96           C  
ANISOU 3231  CB  LYS B 353     2023   1449   2593     42   -529     46       C  
ATOM   3232  CG  LYS B 353      69.266  25.291   9.377  1.00 17.31           C  
ANISOU 3232  CG  LYS B 353     2355   1220   3003    146   -425   -251       C  
ATOM   3233  CD  LYS B 353      68.275  26.290   9.975  1.00 21.44           C  
ANISOU 3233  CD  LYS B 353     2815   1572   3759    427   -206   -408       C  
ATOM   3234  CE  LYS B 353      67.413  26.959   8.909  1.00 20.73           C  
ANISOU 3234  CE  LYS B 353     2739   1701   3434    504   -567   -257       C  
ATOM   3235  NZ  LYS B 353      66.614  28.090   9.486  1.00 21.20           N  
ANISOU 3235  NZ  LYS B 353     2779   1841   3435    603   -630   -404       N  
ATOM   3236  N   VAL B 354      70.157  23.678   5.957  1.00 11.69           N  
ANISOU 3236  N   VAL B 354     1316   1258   1866   -151   -157   -127       N  
ATOM   3237  CA  VAL B 354      71.087  24.124   4.929  1.00 11.58           C  
ANISOU 3237  CA  VAL B 354     1229   1221   1950   -144      9    -24       C  
ATOM   3238  C   VAL B 354      70.334  24.541   3.669  1.00 12.15           C  
ANISOU 3238  C   VAL B 354     1343   1251   2021    -61   -328   -103       C  
ATOM   3239  O   VAL B 354      69.232  24.057   3.398  1.00 12.71           O  
ANISOU 3239  O   VAL B 354     1345   1302   2182   -197    -37      7       O  
ATOM   3240  CB  VAL B 354      72.126  23.011   4.602  1.00 13.06           C  
ANISOU 3240  CB  VAL B 354     1318   1112   2532   -180     89   -223       C  
ATOM   3241  CG1 VAL B 354      71.457  21.828   3.894  1.00 13.50           C  
ANISOU 3241  CG1 VAL B 354     1470   1129   2529   -174    -78   -452       C  
ATOM   3242  CG2 VAL B 354      73.276  23.550   3.777  1.00 14.92           C  
ANISOU 3242  CG2 VAL B 354     1374   1371   2925     81    347    130       C  
ATOM   3243  N   VAL B 355      70.933  25.441   2.899  1.00 12.59           N  
ANISOU 3243  N   VAL B 355     1475   1144   2164      2   -172     16       N  
ATOM   3244  CA  VAL B 355      70.369  25.833   1.619  1.00 12.34           C  
ANISOU 3244  CA  VAL B 355     1535    919   2233    -54   -147    -79       C  
ATOM   3245  C   VAL B 355      71.087  25.098   0.499  1.00 12.23           C  
ANISOU 3245  C   VAL B 355     1275   1159   2211   -214    -54    -49       C  
ATOM   3246  O   VAL B 355      72.321  24.978   0.501  1.00 13.19           O  
ANISOU 3246  O   VAL B 355     1134   1518   2357   -290     70   -284       O  
ATOM   3247  CB  VAL B 355      70.489  27.356   1.397  1.00 12.65           C  
ANISOU 3247  CB  VAL B 355     1658    904   2245   -118    -57    -52       C  
ATOM   3248  CG1 VAL B 355      69.968  27.762   0.015  1.00 14.85           C  
ANISOU 3248  CG1 VAL B 355     2020   1072   2551      5   -359    171       C  
ATOM   3249  CG2 VAL B 355      69.758  28.100   2.496  1.00 14.86           C  
ANISOU 3249  CG2 VAL B 355     1845   1028   2772   -210    177   -505       C  
ATOM   3250  N   ILE B 356      70.307  24.600  -0.453  1.00 11.12           N  
ANISOU 3250  N   ILE B 356     1450    900   1875   -218    -62   -236       N  
ATOM   3251  CA  ILE B 356      70.853  23.963  -1.645  1.00 11.29           C  
ANISOU 3251  CA  ILE B 356     1422    786   2082    -85    -31    -42       C  
ATOM   3252  C   ILE B 356      70.285  24.664  -2.878  1.00 11.21           C  
ANISOU 3252  C   ILE B 356     1311   1082   1866   -197    123     82       C  
ATOM   3253  O   ILE B 356      69.069  24.748  -3.048  1.00 12.39           O  
ANISOU 3253  O   ILE B 356     1034   1355   2319    -86    -68    -50       O  
ATOM   3254  CB  ILE B 356      70.509  22.452  -1.697  1.00 11.03           C  
ANISOU 3254  CB  ILE B 356     1172    938   2079   -114     68    -61       C  
ATOM   3255  CG1 ILE B 356      71.089  21.727  -0.473  1.00 12.51           C  
ANISOU 3255  CG1 ILE B 356     1387    985   2379      3   -136    344       C  
ATOM   3256  CG2 ILE B 356      71.014  21.835  -3.004  1.00 12.40           C  
ANISOU 3256  CG2 ILE B 356     1452   1182   2075    -77    337   -205       C  
ATOM   3257  CD1 ILE B 356      70.725  20.256  -0.399  1.00 12.55           C  
ANISOU 3257  CD1 ILE B 356     1465    951   2351    -84    269     72       C  
ATOM   3258  N   HIS B 357      71.167  25.185  -3.722  1.00 12.13           N  
ANISOU 3258  N   HIS B 357     1446   1147   2015   -218    126    148       N  
ATOM   3259  CA  HIS B 357      70.759  25.799  -4.982  1.00 12.33           C  
ANISOU 3259  CA  HIS B 357     1531   1134   2018   -415    130    126       C  
ATOM   3260  C   HIS B 357      70.460  24.726  -6.014  1.00 12.20           C  
ANISOU 3260  C   HIS B 357     1399   1142   2094   -582    355   -298       C  
ATOM   3261  O   HIS B 357      71.323  23.894  -6.298  1.00 13.67           O  
ANISOU 3261  O   HIS B 357     1392   1393   2407   -187    323   -108       O  
ATOM   3262  CB  HIS B 357      71.898  26.654  -5.542  1.00 13.80           C  
ANISOU 3262  CB  HIS B 357     1543   1157   2542   -582    103     65       C  
ATOM   3263  CG  HIS B 357      72.222  27.859  -4.717  1.00 14.07           C  
ANISOU 3263  CG  HIS B 357     1538   1103   2704   -462   -288    112       C  
ATOM   3264  ND1 HIS B 357      73.319  28.654  -4.970  1.00 15.59           N  
ANISOU 3264  ND1 HIS B 357     1772   1233   2916   -646   -200    240       N  
ATOM   3265  CD2 HIS B 357      71.592  28.411  -3.654  1.00 14.72           C  
ANISOU 3265  CD2 HIS B 357     1724   1110   2757   -159   -286   -272       C  
ATOM   3266  CE1 HIS B 357      73.350  29.645  -4.095  1.00 16.23           C  
ANISOU 3266  CE1 HIS B 357     1751   1378   3036   -557   -352     63       C  
ATOM   3267  NE2 HIS B 357      72.315  29.521  -3.284  1.00 16.20           N  
ANISOU 3267  NE2 HIS B 357     1719   1519   2915   -418    -65    158       N  
ATOM   3268  N   SER B 358      69.266  24.752  -6.601  1.00 11.75           N  
ANISOU 3268  N   SER B 358     1312   1251   1899   -545    140   -111       N  
ATOM   3269  CA  SER B 358      68.968  23.830  -7.693  1.00 11.60           C  
ANISOU 3269  CA  SER B 358     1300   1012   2096   -520     25     90       C  
ATOM   3270  C   SER B 358      69.372  24.440  -9.039  1.00 12.54           C  
ANISOU 3270  C   SER B 358     1228   1227   2308   -375    200    162       C  
ATOM   3271  O   SER B 358      68.572  24.527  -9.982  1.00 12.51           O  
ANISOU 3271  O   SER B 358     1395   1263   2093   -121    306    -34       O  
ATOM   3272  CB  SER B 358      67.497  23.402  -7.679  1.00 11.62           C  
ANISOU 3272  CB  SER B 358     1242   1041   2131   -532     27    189       C  
ATOM   3273  OG  SER B 358      66.624  24.515  -7.715  1.00 12.32           O  
ANISOU 3273  OG  SER B 358     1547   1072   2060    130     84    140       O  
ATOM   3274  N   TYR B 359      70.629  24.863  -9.105  1.00 13.17           N  
ANISOU 3274  N   TYR B 359     1456   1282   2265   -412    628    215       N  
ATOM   3275  CA  TYR B 359      71.193  25.499 -10.293  1.00 13.92           C  
ANISOU 3275  CA  TYR B 359     1441   1478   2369   -314    516    257       C  
ATOM   3276  C   TYR B 359      72.707  25.556 -10.162  1.00 15.15           C  
ANISOU 3276  C   TYR B 359     1502   1687   2565   -411    413      9       C  
ATOM   3277  O   TYR B 359      73.255  25.289  -9.081  1.00 14.90           O  
ANISOU 3277  O   TYR B 359     1646   1671   2345   -457    345    157       O  
ATOM   3278  CB  TYR B 359      70.606  26.895 -10.514  1.00 14.34           C  
ANISOU 3278  CB  TYR B 359     1918   1115   2413   -119    407    224       C  
ATOM   3279  CG  TYR B 359      70.654  27.819  -9.318  1.00 14.83           C  
ANISOU 3279  CG  TYR B 359     1776   1220   2637   -417    231    181       C  
ATOM   3280  CD1 TYR B 359      71.721  28.692  -9.126  1.00 15.61           C  
ANISOU 3280  CD1 TYR B 359     1982   1496   2454    -21     81    -15       C  
ATOM   3281  CD2 TYR B 359      69.616  27.845  -8.394  1.00 14.94           C  
ANISOU 3281  CD2 TYR B 359     1986   1466   2222     88    323    157       C  
ATOM   3282  CE1 TYR B 359      71.759  29.557  -8.032  1.00 16.50           C  
ANISOU 3282  CE1 TYR B 359     1854   1564   2849   -227    260    526       C  
ATOM   3283  CE2 TYR B 359      69.641  28.706  -7.304  1.00 15.27           C  
ANISOU 3283  CE2 TYR B 359     1827   1213   2761   -277    152    204       C  
ATOM   3284  CZ  TYR B 359      70.716  29.557  -7.125  1.00 15.12           C  
ANISOU 3284  CZ  TYR B 359     2004   1232   2510   -255    169   -176       C  
ATOM   3285  OH  TYR B 359      70.731  30.411  -6.043  1.00 15.86           O  
ANISOU 3285  OH  TYR B 359     1927   1233   2865   -372    195     75       O  
ATOM   3286  N   ASP B 360      73.362  25.909 -11.272  1.00 17.09           N  
ANISOU 3286  N   ASP B 360     1600   1895   2999   -373    897    309       N  
ATOM   3287  CA  ASP B 360      74.821  25.843 -11.447  1.00 17.86           C  
ANISOU 3287  CA  ASP B 360     1688   2057   3039   -289    756    154       C  
ATOM   3288  C   ASP B 360      75.311  24.404 -11.640  1.00 17.13           C  
ANISOU 3288  C   ASP B 360     1713   1979   2817   -296    874    495       C  
ATOM   3289  O   ASP B 360      74.623  23.445 -11.278  1.00 17.25           O  
ANISOU 3289  O   ASP B 360     1877   2067   2609   -284    399    323       O  
ATOM   3290  CB  ASP B 360      75.566  26.518 -10.299  1.00 19.14           C  
ANISOU 3290  CB  ASP B 360     1873   2083   3316   -559    793     93       C  
ATOM   3291  CG  ASP B 360      75.328  28.013 -10.251  1.00 21.02           C  
ANISOU 3291  CG  ASP B 360     2331   2406   3250   -655    559    416       C  
ATOM   3292  OD1 ASP B 360      74.998  28.607 -11.300  1.00 22.85           O  
ANISOU 3292  OD1 ASP B 360     2556   2508   3617   -670    284    300       O  
ATOM   3293  OD2 ASP B 360      75.466  28.595  -9.158  1.00 22.54           O  
ANISOU 3293  OD2 ASP B 360     2486   2562   3514   -618    709    291       O  
ATOM   3294  N   ALA B 361      76.501  24.261 -12.216  1.00 18.92           N  
ANISOU 3294  N   ALA B 361     1766   2512   2911    120    871    457       N  
ATOM   3295  CA  ALA B 361      77.049  22.941 -12.496  1.00 20.60           C  
ANISOU 3295  CA  ALA B 361     1985   2775   3065    168   1115    593       C  
ATOM   3296  C   ALA B 361      77.312  22.152 -11.219  1.00 19.77           C  
ANISOU 3296  C   ALA B 361     1921   2553   3037    110    951    628       C  
ATOM   3297  O   ALA B 361      77.393  20.922 -11.249  1.00 22.22           O  
ANISOU 3297  O   ALA B 361     2338   2798   3305    281    813    -31       O  
ATOM   3298  CB  ALA B 361      78.323  23.055 -13.325  1.00 24.09           C  
ANISOU 3298  CB  ALA B 361     2212   3253   3688    547   1429    935       C  
ATOM   3299  N   THR B 362      77.443  22.862 -10.101  1.00 18.74           N  
ANISOU 3299  N   THR B 362     1490   2448   3183   -215    611     81       N  
ATOM   3300  CA  THR B 362      77.664  22.216  -8.809  1.00 18.69           C  
ANISOU 3300  CA  THR B 362     1540   2242   3320   -379    670     91       C  
ATOM   3301  C   THR B 362      76.395  21.545  -8.266  1.00 16.61           C  
ANISOU 3301  C   THR B 362     1420   2024   2866   -333    478   -145       C  
ATOM   3302  O   THR B 362      76.446  20.806  -7.282  1.00 17.06           O  
ANISOU 3302  O   THR B 362     1672   1882   2929    -40    610     76       O  
ATOM   3303  CB  THR B 362      78.223  23.198  -7.767  1.00 19.97           C  
ANISOU 3303  CB  THR B 362     1494   2537   3555   -536    751    174       C  
ATOM   3304  OG1 THR B 362      77.525  24.447  -7.859  1.00 20.63           O  
ANISOU 3304  OG1 THR B 362     1684   2241   3914   -301    642    168       O  
ATOM   3305  CG2 THR B 362      79.701  23.436  -8.015  1.00 22.45           C  
ANISOU 3305  CG2 THR B 362     1509   3055   3966   -454    472    335       C  
ATOM   3306  N   PHE B 363      75.257  21.822  -8.896  1.00 14.71           N  
ANISOU 3306  N   PHE B 363     1176   1823   2588   -364    354   -122       N  
ATOM   3307  CA  PHE B 363      74.034  21.074  -8.618  1.00 14.67           C  
ANISOU 3307  CA  PHE B 363     1167   1712   2693   -103    160   -552       C  
ATOM   3308  C   PHE B 363      73.968  19.987  -9.679  1.00 14.66           C  
ANISOU 3308  C   PHE B 363     1345   1745   2478   -153     30   -391       C  
ATOM   3309  O   PHE B 363      73.499  20.223 -10.794  1.00 16.27           O  
ANISOU 3309  O   PHE B 363     1711   1940   2529     21    307   -254       O  
ATOM   3310  CB  PHE B 363      72.809  21.988  -8.699  1.00 14.00           C  
ANISOU 3310  CB  PHE B 363     1011   1553   2756   -224    486   -238       C  
ATOM   3311  CG  PHE B 363      71.488  21.283  -8.500  1.00 13.20           C  
ANISOU 3311  CG  PHE B 363     1196   1485   2334    -96    276   -349       C  
ATOM   3312  CD1 PHE B 363      71.058  20.939  -7.229  1.00 14.01           C  
ANISOU 3312  CD1 PHE B 363     1308   1113   2902   -150    431   -128       C  
ATOM   3313  CD2 PHE B 363      70.663  21.005  -9.584  1.00 15.40           C  
ANISOU 3313  CD2 PHE B 363     1446   1641   2765    159    -84   -396       C  
ATOM   3314  CE1 PHE B 363      69.832  20.306  -7.036  1.00 15.55           C  
ANISOU 3314  CE1 PHE B 363     1420   1344   3143    135     30   -376       C  
ATOM   3315  CE2 PHE B 363      69.444  20.379  -9.405  1.00 15.61           C  
ANISOU 3315  CE2 PHE B 363     1265   1617   3050     89   -141   -198       C  
ATOM   3316  CZ  PHE B 363      69.025  20.023  -8.131  1.00 16.65           C  
ANISOU 3316  CZ  PHE B 363     1327   1421   3577   -119    176   -185       C  
ATOM   3317  N   ALA B 364      74.469  18.805  -9.333  1.00 13.84           N  
ANISOU 3317  N   ALA B 364     1537   1379   2340   -113    511   -446       N  
ATOM   3318  CA  ALA B 364      74.587  17.709 -10.291  1.00 14.22           C  
ANISOU 3318  CA  ALA B 364     1511   1465   2425   -282    953   -255       C  
ATOM   3319  C   ALA B 364      74.094  16.390  -9.699  1.00 12.74           C  
ANISOU 3319  C   ALA B 364     1327   1510   2004   -173    478   -343       C  
ATOM   3320  O   ALA B 364      74.837  15.407  -9.671  1.00 14.27           O  
ANISOU 3320  O   ALA B 364     1406   1647   2368     78    274   -209       O  
ATOM   3321  CB  ALA B 364      76.032  17.578 -10.764  1.00 17.01           C  
ANISOU 3321  CB  ALA B 364     1591   1910   2962   -249    948   -179       C  
ATOM   3322  N   PRO B 365      72.830  16.356  -9.242  1.00 12.99           N  
ANISOU 3322  N   PRO B 365     1248   1530   2158     83    434   -280       N  
ATOM   3323  CA  PRO B 365      72.320  15.151  -8.572  1.00 13.44           C  
ANISOU 3323  CA  PRO B 365     1513   1599   1992      0    669   -257       C  
ATOM   3324  C   PRO B 365      72.342  13.900  -9.461  1.00 12.72           C  
ANISOU 3324  C   PRO B 365     1447   1656   1729    -68    610   -175       C  
ATOM   3325  O   PRO B 365      72.464  12.791  -8.935  1.00 13.89           O  
ANISOU 3325  O   PRO B 365     1665   1428   2185    -89    421      9       O  
ATOM   3326  CB  PRO B 365      70.883  15.543  -8.190  1.00 14.25           C  
ANISOU 3326  CB  PRO B 365     1445   1543   2424     73    644   -355       C  
ATOM   3327  CG  PRO B 365      70.520  16.625  -9.133  1.00 14.98           C  
ANISOU 3327  CG  PRO B 365     1347   1576   2767    -95    497   -255       C  
ATOM   3328  CD  PRO B 365      71.792  17.396  -9.353  1.00 13.97           C  
ANISOU 3328  CD  PRO B 365     1130   1562   2617    -17    603   -273       C  
ATOM   3329  N   HIS B 366      72.258  14.068 -10.778  1.00 12.84           N  
ANISOU 3329  N   HIS B 366     1287   1464   2127    -80    554   -457       N  
ATOM   3330  CA  HIS B 366      72.352  12.931 -11.693  1.00 12.15           C  
ANISOU 3330  CA  HIS B 366     1444   1409   1761     66    285   -599       C  
ATOM   3331  C   HIS B 366      73.728  12.272 -11.585  1.00 12.99           C  
ANISOU 3331  C   HIS B 366     1360   1512   2061     50    660    194       C  
ATOM   3332  O   HIS B 366      73.856  11.062 -11.769  1.00 14.24           O  
ANISOU 3332  O   HIS B 366     1476   1497   2436     32    406     72       O  
ATOM   3333  CB  HIS B 366      72.076  13.391 -13.130  1.00 13.53           C  
ANISOU 3333  CB  HIS B 366     1803   1687   1650    116    382   -377       C  
ATOM   3334  CG  HIS B 366      71.965  12.280 -14.132  1.00 15.67           C  
ANISOU 3334  CG  HIS B 366     2244   1420   2291     80    153   -349       C  
ATOM   3335  ND1 HIS B 366      71.397  11.060 -13.847  1.00 19.17           N  
ANISOU 3335  ND1 HIS B 366     2607   2122   2554     90    157   -706       N  
ATOM   3336  CD2 HIS B 366      72.316  12.236 -15.440  1.00 17.95           C  
ANISOU 3336  CD2 HIS B 366     2901   1788   2132    214    286   -748       C  
ATOM   3337  CE1 HIS B 366      71.421  10.300 -14.930  1.00 17.81           C  
ANISOU 3337  CE1 HIS B 366     2545   1687   2534    -56    164     51       C  
ATOM   3338  NE2 HIS B 366      71.979  10.987 -15.908  1.00 20.32           N  
ANISOU 3338  NE2 HIS B 366     2989   1995   2736    450    195  -1156       N  
ATOM   3339  N   LEU B 367      74.744  13.074 -11.277  1.00 13.06           N  
ANISOU 3339  N   LEU B 367     1260   1577   2123    -40    351     12       N  
ATOM   3340  CA  LEU B 367      76.105  12.580 -11.072  1.00 13.88           C  
ANISOU 3340  CA  LEU B 367     1246   1585   2441    -84    407    148       C  
ATOM   3341  C   LEU B 367      76.390  12.296  -9.595  1.00 14.65           C  
ANISOU 3341  C   LEU B 367     1551   1552   2461    168    287    169       C  
ATOM   3342  O   LEU B 367      77.530  12.009  -9.210  1.00 16.62           O  
ANISOU 3342  O   LEU B 367     1929   1734   2652    435     -9    124       O  
ATOM   3343  CB  LEU B 367      77.129  13.578 -11.613  1.00 15.47           C  
ANISOU 3343  CB  LEU B 367     1327   1876   2674     -6    614    261       C  
ATOM   3344  CG  LEU B 367      77.093  13.822 -13.120  1.00 18.90           C  
ANISOU 3344  CG  LEU B 367     1927   2262   2990     24    981    718       C  
ATOM   3345  CD1 LEU B 367      78.166  14.816 -13.522  1.00 22.89           C  
ANISOU 3345  CD1 LEU B 367     1951   2901   3845   -248    785    857       C  
ATOM   3346  CD2 LEU B 367      77.293  12.523 -13.851  1.00 24.14           C  
ANISOU 3346  CD2 LEU B 367     2543   2764   3864    676    336    -28       C  
ATOM   3347  N   GLY B 368      75.358  12.409  -8.764  1.00 14.19           N  
ANISOU 3347  N   GLY B 368     1733   1675   1983     40    187     23       N  
ATOM   3348  CA  GLY B 368      75.452  12.009  -7.372  1.00 15.45           C  
ANISOU 3348  CA  GLY B 368     1788   1712   2371   -176     94   -124       C  
ATOM   3349  C   GLY B 368      75.903  13.062  -6.377  1.00 14.90           C  
ANISOU 3349  C   GLY B 368     1407   1623   2629   -327    312     82       C  
ATOM   3350  O   GLY B 368      76.146  12.744  -5.213  1.00 15.79           O  
ANISOU 3350  O   GLY B 368     1544   2178   2276   -170    302    -43       O  
ATOM   3351  N   THR B 369      76.014  14.315  -6.805  1.00 13.48           N  
ANISOU 3351  N   THR B 369     1196   1611   2315    -36    306   -250       N  
ATOM   3352  CA  THR B 369      76.495  15.355  -5.896  1.00 15.34           C  
ANISOU 3352  CA  THR B 369     1138   1765   2926     68    374    -71       C  
ATOM   3353  C   THR B 369      75.762  16.675  -6.041  1.00 13.66           C  
ANISOU 3353  C   THR B 369     1346   1539   2306     25     33   -138       C  
ATOM   3354  O   THR B 369      75.389  17.078  -7.148  1.00 15.61           O  
ANISOU 3354  O   THR B 369     1641   1859   2430    238     85   -150       O  
ATOM   3355  CB  THR B 369      77.999  15.629  -6.102  1.00 21.70           C  
ANISOU 3355  CB  THR B 369     1589   2827   3827    437    747    713       C  
ATOM   3356  OG1 THR B 369      78.210  16.161  -7.416  1.00 25.68           O  
ANISOU 3356  OG1 THR B 369     1848   2931   4978    159    547     82       O  
ATOM   3357  CG2 THR B 369      78.803  14.351  -5.940  1.00 24.40           C  
ANISOU 3357  CG2 THR B 369     1763   2849   4658    473    325    209       C  
ATOM   3358  N   VAL B 370      75.558  17.345  -4.910  1.00 13.22           N  
ANISOU 3358  N   VAL B 370     1237   1478   2307   -164    172   -298       N  
ATOM   3359  CA  VAL B 370      75.032  18.704  -4.905  1.00 13.78           C  
ANISOU 3359  CA  VAL B 370     1116   1412   2707   -207    181   -120       C  
ATOM   3360  C   VAL B 370      75.830  19.561  -3.932  1.00 14.62           C  
ANISOU 3360  C   VAL B 370     1355   1761   2437   -136    -17    -22       C  
ATOM   3361  O   VAL B 370      76.278  19.077  -2.896  1.00 14.26           O  
ANISOU 3361  O   VAL B 370     1380   1609   2428   -358    -78   -127       O  
ATOM   3362  CB  VAL B 370      73.528  18.750  -4.517  1.00 14.35           C  
ANISOU 3362  CB  VAL B 370     1214   1560   2677   -217    269     83       C  
ATOM   3363  CG1 VAL B 370      72.683  18.063  -5.579  1.00 14.63           C  
ANISOU 3363  CG1 VAL B 370     1277   1707   2573   -239   -270   -526       C  
ATOM   3364  CG2 VAL B 370      73.299  18.135  -3.138  1.00 15.76           C  
ANISOU 3364  CG2 VAL B 370     1248   1891   2850    -98    499    -13       C  
ATOM   3365  N   LYS B 371      76.016  20.831  -4.277  1.00 15.29           N  
ANISOU 3365  N   LYS B 371     1522   1691   2594   -451    372   -334       N  
ATOM   3366  CA  LYS B 371      76.693  21.767  -3.388  1.00 14.66           C  
ANISOU 3366  CA  LYS B 371     1615   1520   2434   -565    379   -205       C  
ATOM   3367  C   LYS B 371      75.751  22.253  -2.288  1.00 14.12           C  
ANISOU 3367  C   LYS B 371     1388   1395   2580   -503     78    -94       C  
ATOM   3368  O   LYS B 371      74.572  22.527  -2.544  1.00 14.60           O  
ANISOU 3368  O   LYS B 371     1417   1343   2785   -381   -252    -25       O  
ATOM   3369  CB  LYS B 371      77.220  22.966  -4.180  1.00 16.80           C  
ANISOU 3369  CB  LYS B 371     1792   1597   2992   -719    299      7       C  
ATOM   3370  CG  LYS B 371      77.766  24.094  -3.303  1.00 17.97           C  
ANISOU 3370  CG  LYS B 371     1836   1931   3061  -1068     87     13       C  
ATOM   3371  CD  LYS B 371      78.267  25.276  -4.120  1.00 19.44           C  
ANISOU 3371  CD  LYS B 371     1967   2008   3411  -1065    195   -125       C  
ATOM   3372  CE  LYS B 371      78.914  26.313  -3.212  1.00 21.01           C  
ANISOU 3372  CE  LYS B 371     2309   2074   3598  -1020    191   -145       C  
ATOM   3373  NZ  LYS B 371      79.474  27.474  -3.954  1.00 23.97           N  
ANISOU 3373  NZ  LYS B 371     2425   2400   4283   -863    316    432       N  
ATOM   3374  N   LEU B 372      76.275  22.346  -1.068  1.00 14.12           N  
ANISOU 3374  N   LEU B 372     1490   1643   2231   -438    162   -152       N  
ATOM   3375  CA  LEU B 372      75.561  22.967   0.044  1.00 14.73           C  
ANISOU 3375  CA  LEU B 372     1520   1549   2528   -436     85   -106       C  
ATOM   3376  C   LEU B 372      76.111  24.363   0.249  1.00 14.74           C  
ANISOU 3376  C   LEU B 372     1239   1478   2883   -458    -12   -127       C  
ATOM   3377  O   LEU B 372      77.333  24.560   0.213  1.00 16.63           O  
ANISOU 3377  O   LEU B 372     1161   1876   3282   -465   -126   -429       O  
ATOM   3378  CB  LEU B 372      75.771  22.184   1.345  1.00 16.91           C  
ANISOU 3378  CB  LEU B 372     1752   1509   3164   -569      3    389       C  
ATOM   3379  CG  LEU B 372      75.455  20.692   1.392  1.00 21.16           C  
ANISOU 3379  CG  LEU B 372     2471   1971   3596   -468   -312    604       C  
ATOM   3380  CD1 LEU B 372      75.421  20.196   2.824  1.00 21.99           C  
ANISOU 3380  CD1 LEU B 372     2944   1983   3426    -73   -110    803       C  
ATOM   3381  CD2 LEU B 372      74.146  20.429   0.712  1.00 23.97           C  
ANISOU 3381  CD2 LEU B 372     2019   2284   4802   -610   -723   1241       C  
ATOM   3382  N   GLU B 373      75.228  25.335   0.467  1.00 14.67           N  
ANISOU 3382  N   GLU B 373     1482   1365   2727   -460   -121    -15       N  
ATOM   3383  CA  GLU B 373      75.691  26.672   0.835  1.00 15.87           C  
ANISOU 3383  CA  GLU B 373     1485   1611   2935   -559   -377   -293       C  
ATOM   3384  C   GLU B 373      76.266  26.648   2.251  1.00 15.84           C  
ANISOU 3384  C   GLU B 373     1383   1714   2922   -670   -230   -173       C  
ATOM   3385  O   GLU B 373      75.648  26.123   3.175  1.00 16.07           O  
ANISOU 3385  O   GLU B 373     1480   1629   2997   -532    -42    -87       O  
ATOM   3386  CB  GLU B 373      74.558  27.695   0.729  1.00 16.88           C  
ANISOU 3386  CB  GLU B 373     1607   1653   3154   -409   -144   -177       C  
ATOM   3387  CG  GLU B 373      74.012  27.863  -0.687  1.00 15.98           C  
ANISOU 3387  CG  GLU B 373     1710   1767   2595   -511    -44    119       C  
ATOM   3388  CD  GLU B 373      75.096  28.242  -1.679  1.00 16.88           C  
ANISOU 3388  CD  GLU B 373     1942   1588   2882   -681   -137   -145       C  
ATOM   3389  OE1 GLU B 373      75.690  29.332  -1.521  1.00 19.14           O  
ANISOU 3389  OE1 GLU B 373     2345   1657   3271   -778    106   -121       O  
ATOM   3390  OE2 GLU B 373      75.366  27.454  -2.608  1.00 17.17           O  
ANISOU 3390  OE2 GLU B 373     2081   1558   2885   -633     44     25       O  
ATOM   3391  N   ASP B 374      77.452  27.214   2.427  1.00 16.99           N  
ANISOU 3391  N   ASP B 374     1444   1990   3020   -751   -463    -15       N  
ATOM   3392  CA  ASP B 374      78.073  27.203   3.738  1.00 18.46           C  
ANISOU 3392  CA  ASP B 374     1827   2137   3050   -875   -688   -200       C  
ATOM   3393  C   ASP B 374      77.373  28.193   4.668  1.00 19.47           C  
ANISOU 3393  C   ASP B 374     2424   2072   2901   -533   -637   -247       C  
ATOM   3394  O   ASP B 374      77.404  29.400   4.435  1.00 23.54           O  
ANISOU 3394  O   ASP B 374     3100   2204   3638     23    -76    148       O  
ATOM   3395  CB  ASP B 374      79.563  27.541   3.607  1.00 19.59           C  
ANISOU 3395  CB  ASP B 374     1746   2541   3154   -898   -769    -75       C  
ATOM   3396  CG  ASP B 374      80.314  27.413   4.917  1.00 21.66           C  
ANISOU 3396  CG  ASP B 374     1929   2667   3632  -1079   -678    100       C  
ATOM   3397  OD1 ASP B 374      79.707  26.999   5.932  1.00 22.90           O  
ANISOU 3397  OD1 ASP B 374     1984   3022   3695   -936   -796    -29       O  
ATOM   3398  OD2 ASP B 374      81.528  27.719   4.923  1.00 23.93           O  
ANISOU 3398  OD2 ASP B 374     1995   3294   3802  -1040   -830    207       O  
ATOM   3399  N   ASN B 375      76.742  27.676   5.719  1.00 18.79           N  
ANISOU 3399  N   ASN B 375     2485   2087   2568   -739   -423   -502       N  
ATOM   3400  CA  ASN B 375      76.076  28.523   6.706  1.00 19.22           C  
ANISOU 3400  CA  ASN B 375     2588   1794   2921   -985   -385   -166       C  
ATOM   3401  C   ASN B 375      76.807  28.523   8.041  1.00 21.10           C  
ANISOU 3401  C   ASN B 375     2910   2084   3022   -780   -724     78       C  
ATOM   3402  O   ASN B 375      76.236  28.885   9.071  1.00 20.41           O  
ANISOU 3402  O   ASN B 375     2783   2064   2908   -796   -560   -114       O  
ATOM   3403  CB  ASN B 375      74.615  28.105   6.900  1.00 20.26           C  
ANISOU 3403  CB  ASN B 375     2625   1802   3270  -1021   -367   -263       C  
ATOM   3404  CG  ASN B 375      74.475  26.681   7.394  1.00 21.08           C  
ANISOU 3404  CG  ASN B 375     2733   1918   3359  -1091   -310   -647       C  
ATOM   3405  OD1 ASN B 375      75.460  26.029   7.747  1.00 21.25           O  
ANISOU 3405  OD1 ASN B 375     2793   1913   3369   -882   -213   -544       O  
ATOM   3406  ND2 ASN B 375      73.241  26.193   7.433  1.00 22.44           N  
ANISOU 3406  ND2 ASN B 375     2758   2166   3603  -1219   -209   -670       N  
ATOM   3407  N   ASN B 376      78.067  28.099   8.010  1.00 22.34           N  
ANISOU 3407  N   ASN B 376     3127   2152   3209   -762  -1182   -278       N  
ATOM   3408  CA  ASN B 376      78.928  28.107   9.192  1.00 23.52           C  
ANISOU 3408  CA  ASN B 376     3467   2163   3304   -425  -1451   -676       C  
ATOM   3409  C   ASN B 376      78.514  27.068  10.232  1.00 24.38           C  
ANISOU 3409  C   ASN B 376     3734   1963   3564   -559  -1492   -355       C  
ATOM   3410  O   ASN B 376      79.044  27.045  11.342  1.00 27.72           O  
ANISOU 3410  O   ASN B 376     4172   2272   4089   -440  -1444   -508       O  
ATOM   3411  CB  ASN B 376      78.990  29.511   9.818  1.00 26.31           C  
ANISOU 3411  CB  ASN B 376     3517   2463   4015   -348  -1662   -849       C  
ATOM   3412  CG  ASN B 376      80.262  29.744  10.617  1.00 29.52           C  
ANISOU 3412  CG  ASN B 376     3789   2421   5006   -188  -1862   -781       C  
ATOM   3413  OD1 ASN B 376      80.212  30.140  11.783  1.00 33.31           O  
ANISOU 3413  OD1 ASN B 376     4125   2646   5883    -83  -1434   -894       O  
ATOM   3414  ND2 ASN B 376      81.409  29.491   9.993  1.00 31.67           N  
ANISOU 3414  ND2 ASN B 376     3677   2856   5498   -420  -1819   -962       N  
ATOM   3415  N   GLU B 377      77.586  26.191   9.861  1.00 22.67           N  
ANISOU 3415  N   GLU B 377     3812   1762   3038   -520  -1252   -453       N  
ATOM   3416  CA  GLU B 377      77.100  25.172  10.786  1.00 25.78           C  
ANISOU 3416  CA  GLU B 377     4207   2028   3558   -313   -687   -418       C  
ATOM   3417  C   GLU B 377      77.105  23.772  10.182  1.00 23.20           C  
ANISOU 3417  C   GLU B 377     3913   1811   3092   -745   -532   -526       C  
ATOM   3418  O   GLU B 377      76.300  22.922  10.572  1.00 26.76           O  
ANISOU 3418  O   GLU B 377     4275   2058   3834   -606   -101     15       O  
ATOM   3419  CB  GLU B 377      75.692  25.525  11.265  1.00 30.96           C  
ANISOU 3419  CB  GLU B 377     4827   2508   4429    157   -196   -726       C  
ATOM   3420  CG  GLU B 377      75.606  26.882  11.951  1.00 38.88           C  
ANISOU 3420  CG  GLU B 377     5284   3320   6168    638    327   -592       C  
ATOM   3421  CD  GLU B 377      74.185  27.258  12.317  1.00 47.26           C  
ANISOU 3421  CD  GLU B 377     5796   4147   8013   1070    622   -424       C  
ATOM   3422  OE1 GLU B 377      73.953  28.431  12.678  1.00 50.34           O  
ANISOU 3422  OE1 GLU B 377     5913   4656   8558   1277    759   -319       O  
ATOM   3423  OE2 GLU B 377      73.297  26.381  12.241  1.00 51.14           O  
ANISOU 3423  OE2 GLU B 377     6061   4530   8841   1142    807   -274       O  
ATOM   3424  N   LEU B 378      78.014  23.525   9.244  1.00 21.10           N  
ANISOU 3424  N   LEU B 378     3302   1838   2875   -750   -579    -82       N  
ATOM   3425  CA  LEU B 378      78.068  22.234   8.563  1.00 20.69           C  
ANISOU 3425  CA  LEU B 378     2876   2002   2981   -599   -790   -109       C  
ATOM   3426  C   LEU B 378      79.201  21.342   9.056  1.00 21.14           C  
ANISOU 3426  C   LEU B 378     2652   2273   3107   -716  -1005   -205       C  
ATOM   3427  O   LEU B 378      79.177  20.130   8.861  1.00 20.42           O  
ANISOU 3427  O   LEU B 378     2500   2139   3119   -873   -800     30       O  
ATOM   3428  CB  LEU B 378      78.208  22.437   7.055  1.00 19.16           C  
ANISOU 3428  CB  LEU B 378     2603   2170   2508   -550   -810    142       C  
ATOM   3429  CG  LEU B 378      77.027  23.131   6.379  1.00 18.99           C  
ANISOU 3429  CG  LEU B 378     2047   2403   2765   -842   -762     67       C  
ATOM   3430  CD1 LEU B 378      77.287  23.319   4.886  1.00 19.05           C  
ANISOU 3430  CD1 LEU B 378     2143   2516   2579   -468   -293    -55       C  
ATOM   3431  CD2 LEU B 378      75.753  22.332   6.620  1.00 22.21           C  
ANISOU 3431  CD2 LEU B 378     2262   2829   3347   -837   -716    425       C  
ATOM   3432  N   ASP B 379      80.198  21.933   9.699  1.00 22.75           N  
ANISOU 3432  N   ASP B 379     2788   2392   3463   -473   -852     17       N  
ATOM   3433  CA  ASP B 379      81.402  21.175  10.004  1.00 22.90           C  
ANISOU 3433  CA  ASP B 379     2682   2462   3556   -779  -1197    -15       C  
ATOM   3434  C   ASP B 379      81.184  19.955  10.896  1.00 21.92           C  
ANISOU 3434  C   ASP B 379     2412   2600   3314   -577  -1098    217       C  
ATOM   3435  O   ASP B 379      81.832  18.927  10.700  1.00 22.45           O  
ANISOU 3435  O   ASP B 379     2240   2852   3438   -645   -865    208       O  
ATOM   3436  CB  ASP B 379      82.495  22.088  10.558  1.00 26.15           C  
ANISOU 3436  CB  ASP B 379     3185   2718   4032   -663  -1552   -218       C  
ATOM   3437  CG  ASP B 379      82.988  23.072   9.525  1.00 31.61           C  
ANISOU 3437  CG  ASP B 379     3846   3033   5132   -413  -1271   -226       C  
ATOM   3438  OD1 ASP B 379      83.546  22.622   8.500  1.00 31.03           O  
ANISOU 3438  OD1 ASP B 379     3835   3136   4817   -636  -1444   -306       O  
ATOM   3439  OD2 ASP B 379      82.810  24.290   9.726  1.00 36.08           O  
ANISOU 3439  OD2 ASP B 379     4381   3333   5995    -56  -1000      6       O  
ATOM   3440  N   GLN B 380      80.266  20.053  11.856  1.00 20.94           N  
ANISOU 3440  N   GLN B 380     2403   2714   2838   -180   -895     76       N  
ATOM   3441  CA  GLN B 380      80.007  18.925  12.745  1.00 22.11           C  
ANISOU 3441  CA  GLN B 380     2355   2863   3182     67  -1072   -197       C  
ATOM   3442  C   GLN B 380      79.438  17.740  11.968  1.00 19.79           C  
ANISOU 3442  C   GLN B 380     2035   2684   2801     43   -699    -49       C  
ATOM   3443  O   GLN B 380      79.447  16.609  12.454  1.00 20.62           O  
ANISOU 3443  O   GLN B 380     2192   2560   3081     88   -651    208       O  
ATOM   3444  CB  GLN B 380      79.077  19.313  13.903  1.00 24.03           C  
ANISOU 3444  CB  GLN B 380     2823   3177   3131    569   -850   -181       C  
ATOM   3445  CG  GLN B 380      77.639  19.594  13.498  1.00 26.18           C  
ANISOU 3445  CG  GLN B 380     3138   3518   3289    899  -1160   -436       C  
ATOM   3446  CD  GLN B 380      76.656  19.434  14.654  1.00 29.71           C  
ANISOU 3446  CD  GLN B 380     3715   3717   3854   1336   -930    -34       C  
ATOM   3447  OE1 GLN B 380      75.915  20.358  14.986  1.00 33.35           O  
ANISOU 3447  OE1 GLN B 380     4378   3788   4506   1460   -148    -94       O  
ATOM   3448  NE2 GLN B 380      76.636  18.250  15.259  1.00 30.13           N  
ANISOU 3448  NE2 GLN B 380     3656   3645   4146   1147  -1100   -443       N  
ATOM   3449  N   PHE B 381      78.961  17.999  10.754  1.00 17.69           N  
ANISOU 3449  N   PHE B 381     1630   2384   2706   -145   -393   -222       N  
ATOM   3450  CA  PHE B 381      78.295  16.963   9.971  1.00 17.04           C  
ANISOU 3450  CA  PHE B 381     1314   2294   2867   -164   -385    134       C  
ATOM   3451  C   PHE B 381      79.163  16.394   8.858  1.00 15.74           C  
ANISOU 3451  C   PHE B 381     1275   2063   2640   -265   -338    -15       C  
ATOM   3452  O   PHE B 381      78.758  15.460   8.176  1.00 16.42           O  
ANISOU 3452  O   PHE B 381     1211   1888   3138   -254   -279    116       O  
ATOM   3453  CB  PHE B 381      76.971  17.478   9.390  1.00 17.05           C  
ANISOU 3453  CB  PHE B 381     1227   2038   3213    -91   -434    291       C  
ATOM   3454  CG  PHE B 381      75.984  17.918  10.429  1.00 16.43           C  
ANISOU 3454  CG  PHE B 381     1197   1805   3240    -21      3    137       C  
ATOM   3455  CD1 PHE B 381      75.325  16.982  11.214  1.00 16.63           C  
ANISOU 3455  CD1 PHE B 381     1150   1836   3332    101    -39    -63       C  
ATOM   3456  CD2 PHE B 381      75.710  19.263  10.620  1.00 17.33           C  
ANISOU 3456  CD2 PHE B 381     1351   1769   3464     85   -348   -121       C  
ATOM   3457  CE1 PHE B 381      74.412  17.383  12.175  1.00 16.17           C  
ANISOU 3457  CE1 PHE B 381     1305   1728   3109    182     39   -297       C  
ATOM   3458  CE2 PHE B 381      74.802  19.668  11.572  1.00 17.13           C  
ANISOU 3458  CE2 PHE B 381     1376   1713   3418    103   -447    -55       C  
ATOM   3459  CZ  PHE B 381      74.153  18.729  12.356  1.00 17.57           C  
ANISOU 3459  CZ  PHE B 381     1471   1687   3517    190    -54    227       C  
ATOM   3460  N   VAL B 382      80.353  16.952   8.668  1.00 16.09           N  
ANISOU 3460  N   VAL B 382     1177   2061   2873   -235   -417     86       N  
ATOM   3461  CA  VAL B 382      81.227  16.458   7.615  1.00 16.70           C  
ANISOU 3461  CA  VAL B 382     1165   2039   3142   -389   -166    -84       C  
ATOM   3462  C   VAL B 382      81.591  15.001   7.891  1.00 16.88           C  
ANISOU 3462  C   VAL B 382     1125   2103   3185   -379   -526   -125       C  
ATOM   3463  O   VAL B 382      82.006  14.648   8.995  1.00 19.70           O  
ANISOU 3463  O   VAL B 382     1379   2522   3584    -39   -441    -62       O  
ATOM   3464  CB  VAL B 382      82.486  17.338   7.454  1.00 18.12           C  
ANISOU 3464  CB  VAL B 382     1237   2122   3526   -472    126   -134       C  
ATOM   3465  CG1 VAL B 382      83.487  16.693   6.500  1.00 21.11           C  
ANISOU 3465  CG1 VAL B 382     1396   2461   4162   -495    118    105       C  
ATOM   3466  CG2 VAL B 382      82.088  18.726   6.964  1.00 20.25           C  
ANISOU 3466  CG2 VAL B 382     1498   2109   4085   -324    168   -116       C  
ATOM   3467  N   GLY B 383      81.399  14.149   6.890  1.00 17.03           N  
ANISOU 3467  N   GLY B 383     1038   1843   3588   -215   -203    -50       N  
ATOM   3468  CA  GLY B 383      81.627  12.728   7.047  1.00 17.68           C  
ANISOU 3468  CA  GLY B 383     1152   1834   3730    -55   -146    258       C  
ATOM   3469  C   GLY B 383      80.430  11.948   7.568  1.00 17.70           C  
ANISOU 3469  C   GLY B 383     1210   1935   3581    -38   -301    159       C  
ATOM   3470  O   GLY B 383      80.484  10.723   7.645  1.00 19.90           O  
ANISOU 3470  O   GLY B 383     1651   2023   3886    155   -283    135       O  
ATOM   3471  N   LYS B 384      79.348  12.648   7.919  1.00 16.26           N  
ANISOU 3471  N   LYS B 384     1059   1997   3121    -67   -519    248       N  
ATOM   3472  CA  LYS B 384      78.158  12.007   8.484  1.00 15.27           C  
ANISOU 3472  CA  LYS B 384     1083   2009   2709   -206   -349    244       C  
ATOM   3473  C   LYS B 384      77.066  11.823   7.439  1.00 13.33           C  
ANISOU 3473  C   LYS B 384      986   1570   2507    113   -333    198       C  
ATOM   3474  O   LYS B 384      76.869  12.687   6.569  1.00 14.31           O  
ANISOU 3474  O   LYS B 384     1127   1670   2639    -87   -347     88       O  
ATOM   3475  CB  LYS B 384      77.578  12.842   9.633  1.00 17.24           C  
ANISOU 3475  CB  LYS B 384     1474   2489   2588   -271   -646    -44       C  
ATOM   3476  CG  LYS B 384      78.577  13.294  10.681  1.00 22.74           C  
ANISOU 3476  CG  LYS B 384     1947   3259   3432   -300   -868    214       C  
ATOM   3477  CD  LYS B 384      78.939  12.175  11.609  1.00 24.89           C  
ANISOU 3477  CD  LYS B 384     1977   3740   3741   -434  -1344    415       C  
ATOM   3478  CE  LYS B 384      79.887  12.655  12.712  1.00 23.81           C  
ANISOU 3478  CE  LYS B 384     2009   3796   3241   -474  -1262    636       C  
ATOM   3479  NZ  LYS B 384      80.560  11.497  13.356  1.00 26.97           N  
ANISOU 3479  NZ  LYS B 384     2353   4301   3592   -276   -939    732       N  
ATOM   3480  N   GLU B 385      76.329  10.719   7.542  1.00 13.11           N  
ANISOU 3480  N   GLU B 385      799   1473   2709     45     53   -293       N  
ATOM   3481  CA  GLU B 385      75.180  10.498   6.668  1.00 12.64           C  
ANISOU 3481  CA  GLU B 385      777   1463   2561    -53   -136   -408       C  
ATOM   3482  C   GLU B 385      73.937  11.177   7.232  1.00 11.22           C  
ANISOU 3482  C   GLU B 385      818   1255   2191     79     39   -225       C  
ATOM   3483  O   GLU B 385      73.625  11.057   8.421  1.00 12.23           O  
ANISOU 3483  O   GLU B 385     1108   1284   2254    298    -34    -40       O  
ATOM   3484  CB  GLU B 385      74.896   9.005   6.460  1.00 14.91           C  
ANISOU 3484  CB  GLU B 385     1130   1647   2886    148   -116   -505       C  
ATOM   3485  CG  GLU B 385      74.013   8.761   5.239  1.00 17.60           C  
ANISOU 3485  CG  GLU B 385     1397   1905   3383    -20   -564  -1067       C  
ATOM   3486  CD  GLU B 385      73.612   7.318   5.029  1.00 23.25           C  
ANISOU 3486  CD  GLU B 385     1821   2284   4728    276   -247  -1096       C  
ATOM   3487  OE1 GLU B 385      73.616   6.544   6.007  1.00 23.44           O  
ANISOU 3487  OE1 GLU B 385     2414   1984   4508    182    985    -75       O  
ATOM   3488  OE2 GLU B 385      73.278   6.964   3.872  1.00 26.68           O  
ANISOU 3488  OE2 GLU B 385     1825   2857   5456    380   -829  -1610       O  
ATOM   3489  N   VAL B 386      73.223  11.889   6.372  1.00 10.87           N  
ANISOU 3489  N   VAL B 386      748    944   2437     81   -111   -263       N  
ATOM   3490  CA  VAL B 386      72.027  12.598   6.800  1.00 10.66           C  
ANISOU 3490  CA  VAL B 386      903    886   2261     -3   -138   -426       C  
ATOM   3491  C   VAL B 386      70.866  12.329   5.853  1.00 10.01           C  
ANISOU 3491  C   VAL B 386      982   1031   1791     67   -129   -363       C  
ATOM   3492  O   VAL B 386      71.061  11.959   4.686  1.00 10.88           O  
ANISOU 3492  O   VAL B 386      947   1158   2030     57    -96   -345       O  
ATOM   3493  CB  VAL B 386      72.270  14.128   6.886  1.00 11.49           C  
ANISOU 3493  CB  VAL B 386     1145   1183   2038   -108   -293   -176       C  
ATOM   3494  CG1 VAL B 386      73.374  14.439   7.897  1.00 12.52           C  
ANISOU 3494  CG1 VAL B 386     1001   1466   2289    -95   -520   -323       C  
ATOM   3495  CG2 VAL B 386      72.603  14.720   5.512  1.00 13.25           C  
ANISOU 3495  CG2 VAL B 386     1498   1305   2230     25   -189     -6       C  
ATOM   3496  N   VAL B 387      69.650  12.522   6.356  1.00  9.71           N  
ANISOU 3496  N   VAL B 387      626   1218   1844     64   -212    -24       N  
ATOM   3497  CA  VAL B 387      68.499  12.623   5.479  1.00 11.24           C  
ANISOU 3497  CA  VAL B 387     1014    964   2292     86   -227   -200       C  
ATOM   3498  C   VAL B 387      67.998  14.058   5.535  1.00 10.63           C  
ANISOU 3498  C   VAL B 387     1125    978   1934    180    240   -291       C  
ATOM   3499  O   VAL B 387      67.936  14.661   6.610  1.00 10.87           O  
ANISOU 3499  O   VAL B 387     1309    914   1908    107    -23   -257       O  
ATOM   3500  CB  VAL B 387      67.383  11.623   5.847  1.00 10.46           C  
ANISOU 3500  CB  VAL B 387      811    929   2235   -158    -62    -99       C  
ATOM   3501  CG1 VAL B 387      67.769  10.202   5.432  1.00 12.72           C  
ANISOU 3501  CG1 VAL B 387     1261    800   2772    162   -173   -163       C  
ATOM   3502  CG2 VAL B 387      67.046  11.674   7.323  1.00 13.26           C  
ANISOU 3502  CG2 VAL B 387     1181   1663   2192    236    303   -187       C  
ATOM   3503  N   LEU B 388      67.685  14.605   4.365  1.00 10.30           N  
ANISOU 3503  N   LEU B 388      961    796   2157    161   -208     61       N  
ATOM   3504  CA  LEU B 388      67.244  15.991   4.240  1.00  9.29           C  
ANISOU 3504  CA  LEU B 388      829    838   1863      2   -206      9       C  
ATOM   3505  C   LEU B 388      65.806  16.045   3.736  1.00  9.21           C  
ANISOU 3505  C   LEU B 388      889    988   1621    109   -147   -130       C  
ATOM   3506  O   LEU B 388      65.391  15.220   2.916  1.00 11.50           O  
ANISOU 3506  O   LEU B 388     1183   1176   2011    162   -331   -443       O  
ATOM   3507  CB  LEU B 388      68.144  16.753   3.267  1.00 10.48           C  
ANISOU 3507  CB  LEU B 388      831   1040   2112    -46   -260    -39       C  
ATOM   3508  CG  LEU B 388      69.653  16.730   3.533  1.00 10.43           C  
ANISOU 3508  CG  LEU B 388      892    987   2083   -149   -105   -463       C  
ATOM   3509  CD1 LEU B 388      70.336  15.678   2.650  1.00 12.98           C  
ANISOU 3509  CD1 LEU B 388     1318   1618   1995    163    -55   -207       C  
ATOM   3510  CD2 LEU B 388      70.261  18.109   3.303  1.00 13.57           C  
ANISOU 3510  CD2 LEU B 388     1257   1157   2741   -245   -153    -59       C  
ATOM   3511  N   GLU B 389      65.059  17.034   4.206  1.00 10.35           N  
ANISOU 3511  N   GLU B 389     1002   1024   1905    265   -189   -275       N  
ATOM   3512  CA  GLU B 389      63.695  17.257   3.740  1.00 10.68           C  
ANISOU 3512  CA  GLU B 389     1110    899   2050     45   -223     99       C  
ATOM   3513  C   GLU B 389      63.516  18.726   3.377  1.00  9.53           C  
ANISOU 3513  C   GLU B 389      924    719   1979     68   -243     59       C  
ATOM   3514  O   GLU B 389      64.141  19.615   3.965  1.00 10.03           O  
ANISOU 3514  O   GLU B 389     1028    929   1853    -13   -235    -94       O  
ATOM   3515  CB  GLU B 389      62.678  16.823   4.797  1.00 13.30           C  
ANISOU 3515  CB  GLU B 389     1565   1417   2072     45     47    100       C  
ATOM   3516  CG  GLU B 389      62.835  17.527   6.130  1.00 18.53           C  
ANISOU 3516  CG  GLU B 389     2116   2344   2578    194    130    -55       C  
ATOM   3517  CD  GLU B 389      61.730  17.206   7.120  1.00 24.52           C  
ANISOU 3517  CD  GLU B 389     2340   3367   3608    163    287    236       C  
ATOM   3518  OE1 GLU B 389      60.655  16.744   6.687  1.00 22.11           O  
ANISOU 3518  OE1 GLU B 389     2286   3102   3012   -505    117    -73       O  
ATOM   3519  OE2 GLU B 389      61.943  17.418   8.336  1.00 30.71           O  
ANISOU 3519  OE2 GLU B 389     2630   4280   4758    522   -161    429       O  
ATOM   3520  N   LEU B 390      62.648  18.978   2.409  1.00 10.36           N  
ANISOU 3520  N   LEU B 390     1217    879   1839    398   -372    104       N  
ATOM   3521  CA  LEU B 390      62.402  20.336   1.941  1.00  9.79           C  
ANISOU 3521  CA  LEU B 390     1287    835   1596    472   -213    194       C  
ATOM   3522  C   LEU B 390      61.463  21.081   2.884  1.00 10.61           C  
ANISOU 3522  C   LEU B 390     1184    931   1915     19    -74   -198       C  
ATOM   3523  O   LEU B 390      60.274  20.788   2.957  1.00 15.72           O  
ANISOU 3523  O   LEU B 390     1265   1708   2999   -434    105   -630       O  
ATOM   3524  CB  LEU B 390      61.809  20.294   0.533  1.00 10.85           C  
ANISOU 3524  CB  LEU B 390     1373   1025   1723    300   -454    283       C  
ATOM   3525  CG  LEU B 390      61.584  21.645  -0.146  1.00 10.45           C  
ANISOU 3525  CG  LEU B 390     1295    847   1827     77    -78    321       C  
ATOM   3526  CD1 LEU B 390      62.911  22.377  -0.335  1.00 12.82           C  
ANISOU 3526  CD1 LEU B 390     1172   1148   2549   -129    101    169       C  
ATOM   3527  CD2 LEU B 390      60.869  21.451  -1.479  1.00 11.88           C  
ANISOU 3527  CD2 LEU B 390     1772   1223   1518    412   -503    -15       C  
ATOM   3528  N   THR B 391      62.004  22.065   3.595  1.00  9.98           N  
ANISOU 3528  N   THR B 391     1168    811   1812     13     23   -188       N  
ATOM   3529  CA  THR B 391      61.200  22.838   4.531  1.00  9.80           C  
ANISOU 3529  CA  THR B 391     1243   1040   1439    338   -154    -62       C  
ATOM   3530  C   THR B 391      60.508  24.002   3.843  1.00  9.60           C  
ANISOU 3530  C   THR B 391     1120    895   1633     30    101    159       C  
ATOM   3531  O   THR B 391      59.314  24.231   4.039  1.00 10.76           O  
ANISOU 3531  O   THR B 391     1034   1074   1979    168     86    -22       O  
ATOM   3532  CB  THR B 391      62.061  23.335   5.689  1.00 10.20           C  
ANISOU 3532  CB  THR B 391     1466    973   1437    415   -151   -164       C  
ATOM   3533  OG1 THR B 391      62.633  22.195   6.334  1.00 12.67           O  
ANISOU 3533  OG1 THR B 391     1627   1292   1893    512   -390     29       O  
ATOM   3534  CG2 THR B 391      61.227  24.115   6.695  1.00 11.38           C  
ANISOU 3534  CG2 THR B 391     1624   1086   1614    184    -19   -128       C  
ATOM   3535  N   TRP B 392      61.259  24.745   3.042  1.00  9.86           N  
ANISOU 3535  N   TRP B 392     1362    595   1787    116   -186     89       N  
ATOM   3536  CA  TRP B 392      60.671  25.835   2.281  1.00  9.70           C  
ANISOU 3536  CA  TRP B 392     1504    524   1656    230     31   -121       C  
ATOM   3537  C   TRP B 392      61.557  26.185   1.096  1.00 10.32           C  
ANISOU 3537  C   TRP B 392     1500    962   1457     11     85    245       C  
ATOM   3538  O   TRP B 392      62.676  25.670   0.977  1.00 10.89           O  
ANISOU 3538  O   TRP B 392     1342    949   1846    -31    -73   -159       O  
ATOM   3539  CB  TRP B 392      60.362  27.054   3.174  1.00 10.49           C  
ANISOU 3539  CB  TRP B 392     1542    623   1820     90    -55   -349       C  
ATOM   3540  CG  TRP B 392      61.552  27.755   3.773  1.00 10.46           C  
ANISOU 3540  CG  TRP B 392     1546    768   1658     97    -24   -205       C  
ATOM   3541  CD1 TRP B 392      62.339  27.331   4.818  1.00 11.20           C  
ANISOU 3541  CD1 TRP B 392     1414    841   2001   -148   -155   -491       C  
ATOM   3542  CD2 TRP B 392      62.045  29.048   3.401  1.00 11.29           C  
ANISOU 3542  CD2 TRP B 392     1621    683   1984     17     12   -210       C  
ATOM   3543  NE1 TRP B 392      63.304  28.278   5.096  1.00 12.20           N  
ANISOU 3543  NE1 TRP B 392     1547    901   2185    123    -37     39       N  
ATOM   3544  CE2 TRP B 392      63.141  29.339   4.243  1.00 11.88           C  
ANISOU 3544  CE2 TRP B 392     1687    791   2036   -167    117   -161       C  
ATOM   3545  CE3 TRP B 392      61.671  29.984   2.428  1.00 12.26           C  
ANISOU 3545  CE3 TRP B 392     1787    892   1977    -65    105     65       C  
ATOM   3546  CZ2 TRP B 392      63.865  30.532   4.143  1.00 13.30           C  
ANISOU 3546  CZ2 TRP B 392     1880   1019   2152      6    149     35       C  
ATOM   3547  CZ3 TRP B 392      62.386  31.175   2.342  1.00 13.51           C  
ANISOU 3547  CZ3 TRP B 392     1913    889   2332   -198     76   -147       C  
ATOM   3548  CH2 TRP B 392      63.475  31.428   3.185  1.00 14.05           C  
ANISOU 3548  CH2 TRP B 392     1874   1015   2448   -215     81   -259       C  
ATOM   3549  N   VAL B 393      61.044  27.036   0.212  1.00 10.51           N  
ANISOU 3549  N   VAL B 393     1515    801   1678   -146    -35    161       N  
ATOM   3550  CA  VAL B 393      61.731  27.382  -1.024  1.00 10.58           C  
ANISOU 3550  CA  VAL B 393     1561    790   1667    -62      0     78       C  
ATOM   3551  C   VAL B 393      61.675  28.890  -1.219  1.00 11.30           C  
ANISOU 3551  C   VAL B 393     1559    704   2031    -33     31    142       C  
ATOM   3552  O   VAL B 393      60.651  29.523  -0.937  1.00 11.97           O  
ANISOU 3552  O   VAL B 393     1548    913   2088    134     94     17       O  
ATOM   3553  CB  VAL B 393      61.063  26.701  -2.240  1.00 11.41           C  
ANISOU 3553  CB  VAL B 393     1585   1056   1693    131    200    145       C  
ATOM   3554  CG1 VAL B 393      61.758  27.107  -3.539  1.00 12.39           C  
ANISOU 3554  CG1 VAL B 393     1797   1268   1643    118     44    192       C  
ATOM   3555  CG2 VAL B 393      61.046  25.176  -2.064  1.00 12.52           C  
ANISOU 3555  CG2 VAL B 393     1738    758   2259     75     81     32       C  
ATOM   3556  N   SER B 394      62.775  29.470  -1.692  1.00 11.71           N  
ANISOU 3556  N   SER B 394     1623    627   2198   -125    104    137       N  
ATOM   3557  CA  SER B 394      62.768  30.882  -2.081  1.00 12.61           C  
ANISOU 3557  CA  SER B 394     1698    798   2294   -198    274    359       C  
ATOM   3558  C   SER B 394      63.328  31.057  -3.488  1.00 12.16           C  
ANISOU 3558  C   SER B 394     1724    870   2026      1    269    115       C  
ATOM   3559  O   SER B 394      63.951  30.146  -4.045  1.00 13.37           O  
ANISOU 3559  O   SER B 394     1903    995   2183    115     60     87       O  
ATOM   3560  CB  SER B 394      63.561  31.724  -1.078  1.00 14.10           C  
ANISOU 3560  CB  SER B 394     1843   1139   2376   -165    -91    -41       C  
ATOM   3561  OG  SER B 394      64.923  31.324  -1.023  1.00 14.03           O  
ANISOU 3561  OG  SER B 394     1929   1018   2384   -117    106    152       O  
ATOM   3562  N   ASN B 395      63.099  32.231  -4.065  1.00 12.85           N  
ANISOU 3562  N   ASN B 395     1816    878   2189    -61      7    531       N  
ATOM   3563  CA  ASN B 395      63.613  32.504  -5.397  1.00 13.49           C  
ANISOU 3563  CA  ASN B 395     1910   1014   2202   -118    252    449       C  
ATOM   3564  C   ASN B 395      65.120  32.692  -5.379  1.00 14.31           C  
ANISOU 3564  C   ASN B 395     1998   1276   2162   -121    293    283       C  
ATOM   3565  O   ASN B 395      65.696  33.164  -4.393  1.00 16.31           O  
ANISOU 3565  O   ASN B 395     2263   1387   2546   -179     77    124       O  
ATOM   3566  CB  ASN B 395      62.936  33.737  -6.015  1.00 14.87           C  
ANISOU 3566  CB  ASN B 395     2389    834   2427    113     19    304       C  
ATOM   3567  CG  ASN B 395      63.320  35.035  -5.317  1.00 16.18           C  
ANISOU 3567  CG  ASN B 395     2581    963   2603     37    120    113       C  
ATOM   3568  OD1 ASN B 395      62.938  35.269  -4.170  1.00 17.21           O  
ANISOU 3568  OD1 ASN B 395     2880   1003   2654   -129    228    186       O  
ATOM   3569  ND2 ASN B 395      64.067  35.890  -6.012  1.00 18.68           N  
ANISOU 3569  ND2 ASN B 395     2554   1311   3233   -165    209    610       N  
ATOM   3570  N   ARG B 396      65.751  32.291  -6.474  1.00 14.64           N  
ANISOU 3570  N   ARG B 396     2008   1129   2423   -327    310    387       N  
ATOM   3571  CA  ARG B 396      67.147  32.610  -6.721  1.00 15.66           C  
ANISOU 3571  CA  ARG B 396     2100   1142   2707   -685    317     89       C  
ATOM   3572  C   ARG B 396      67.242  34.112  -6.957  1.00 17.41           C  
ANISOU 3572  C   ARG B 396     2292   1432   2890   -629     41   -124       C  
ATOM   3573  O   ARG B 396      66.385  34.685  -7.626  1.00 17.74           O  
ANISOU 3573  O   ARG B 396     2198   1585   2958   -544    135    442       O  
ATOM   3574  CB  ARG B 396      67.614  31.852  -7.965  1.00 19.60           C  
ANISOU 3574  CB  ARG B 396     2412   1260   3775   -457    791    -46       C  
ATOM   3575  CG  ARG B 396      68.968  32.245  -8.491  1.00 21.35           C  
ANISOU 3575  CG  ARG B 396     2918   1416   3777   -215    501     10       C  
ATOM   3576  CD  ARG B 396      69.277  31.535  -9.796  1.00 18.95           C  
ANISOU 3576  CD  ARG B 396     3015   1371   2813   -307    488    407       C  
ATOM   3577  NE  ARG B 396      70.637  31.832 -10.228  1.00 21.84           N  
ANISOU 3577  NE  ARG B 396     3089   1836   3374   -434    118    434       N  
ATOM   3578  CZ  ARG B 396      71.244  31.273 -11.265  1.00 23.03           C  
ANISOU 3578  CZ  ARG B 396     2912   2172   3664   -583    415    966       C  
ATOM   3579  NH1 ARG B 396      70.608  30.380 -12.007  1.00 22.35           N  
ANISOU 3579  NH1 ARG B 396     2866   2023   3601   -787    359    681       N  
ATOM   3580  NH2 ARG B 396      72.491  31.617 -11.562  1.00 26.41           N  
ANISOU 3580  NH2 ARG B 396     2802   2649   4581   -809    161    846       N  
ATOM   3581  N   THR B 397      68.263  34.752  -6.395  1.00 17.95           N  
ANISOU 3581  N   THR B 397     2717   1186   2915   -571    332    199       N  
ATOM   3582  CA  THR B 397      68.489  36.174  -6.637  1.00 20.09           C  
ANISOU 3582  CA  THR B 397     2994   1492   3145   -979    196    388       C  
ATOM   3583  C   THR B 397      68.469  36.450  -8.138  1.00 21.61           C  
ANISOU 3583  C   THR B 397     3181   1568   3461   -713    197    655       C  
ATOM   3584  O   THR B 397      69.142  35.766  -8.910  1.00 21.48           O  
ANISOU 3584  O   THR B 397     3264   1793   3103   -827    344    548       O  
ATOM   3585  CB  THR B 397      69.839  36.626  -6.058  1.00 24.22           C  
ANISOU 3585  CB  THR B 397     3614   1796   3792  -1231   -134    406       C  
ATOM   3586  OG1 THR B 397      69.841  36.433  -4.639  1.00 28.18           O  
ANISOU 3586  OG1 THR B 397     4106   2362   4240  -1070   -305     41       O  
ATOM   3587  CG2 THR B 397      70.082  38.102  -6.358  1.00 26.12           C  
ANISOU 3587  CG2 THR B 397     3999   1586   4339   -862   -332    425       C  
ATOM   3588  N   GLY B 398      67.678  37.435  -8.549  1.00 21.26           N  
ANISOU 3588  N   GLY B 398     3234   1630   3215   -740     57    916       N  
ATOM   3589  CA  GLY B 398      67.621  37.824  -9.945  1.00 22.89           C  
ANISOU 3589  CA  GLY B 398     3304   1809   3582   -624    -13    730       C  
ATOM   3590  C   GLY B 398      66.580  37.089 -10.765  1.00 23.46           C  
ANISOU 3590  C   GLY B 398     3481   2184   3247   -435     -4    975       C  
ATOM   3591  O   GLY B 398      66.409  37.373 -11.955  1.00 27.52           O  
ANISOU 3591  O   GLY B 398     3854   2771   3829   -454    106   1299       O  
ATOM   3592  N   ALA B 399      65.872  36.154 -10.132  1.00 21.46           N  
ANISOU 3592  N   ALA B 399     3263   1753   3138   -520    137    600       N  
ATOM   3593  CA  ALA B 399      64.870  35.355 -10.827  1.00 20.63           C  
ANISOU 3593  CA  ALA B 399     3142   1630   3065   -175    100    324       C  
ATOM   3594  C   ALA B 399      63.579  35.291 -10.028  1.00 19.73           C  
ANISOU 3594  C   ALA B 399     3031   1482   2981   -201     36    375       C  
ATOM   3595  O   ALA B 399      63.582  35.477  -8.811  1.00 20.66           O  
ANISOU 3595  O   ALA B 399     3164   1918   2769     -6    107    406       O  
ATOM   3596  CB  ALA B 399      65.393  33.948 -11.079  1.00 21.80           C  
ANISOU 3596  CB  ALA B 399     3188   1808   3288    142     60    341       C  
ATOM   3597  N   THR B 400      62.473  35.022 -10.716  1.00 18.24           N  
ANISOU 3597  N   THR B 400     2963   1526   2441     13    282    509       N  
ATOM   3598  CA  THR B 400      61.223  34.728 -10.032  1.00 18.60           C  
ANISOU 3598  CA  THR B 400     2876   1464   2726      6     12    587       C  
ATOM   3599  C   THR B 400      61.226  33.258  -9.639  1.00 18.33           C  
ANISOU 3599  C   THR B 400     2584   1313   3065     93    140    347       C  
ATOM   3600  O   THR B 400      62.019  32.469 -10.166  1.00 17.30           O  
ANISOU 3600  O   THR B 400     2330   1264   2978   -152     53    411       O  
ATOM   3601  CB  THR B 400      60.000  34.986 -10.923  1.00 21.39           C  
ANISOU 3601  CB  THR B 400     3343   2073   2711    356    190    702       C  
ATOM   3602  OG1 THR B 400      60.064  34.152 -12.086  1.00 24.75           O  
ANISOU 3602  OG1 THR B 400     3506   2854   3044    456   -246    428       O  
ATOM   3603  CG2 THR B 400      59.960  36.441 -11.360  1.00 24.92           C  
ANISOU 3603  CG2 THR B 400     3706   2153   3608    497    410   1440       C  
ATOM   3604  N   LEU B 401      60.353  32.892  -8.707  1.00 15.18           N  
ANISOU 3604  N   LEU B 401     2378   1059   2331   -305     83    384       N  
ATOM   3605  CA  LEU B 401      60.197  31.494  -8.339  1.00 15.31           C  
ANISOU 3605  CA  LEU B 401     2257   1238   2323   -168     -5    496       C  
ATOM   3606  C   LEU B 401      59.229  30.812  -9.306  1.00 15.96           C  
ANISOU 3606  C   LEU B 401     2225   1456   2382   -260     36     20       C  
ATOM   3607  O   LEU B 401      58.012  30.971  -9.201  1.00 20.03           O  
ANISOU 3607  O   LEU B 401     2308   2161   3142    179   -149   -523       O  
ATOM   3608  CB  LEU B 401      59.720  31.369  -6.892  1.00 15.15           C  
ANISOU 3608  CB  LEU B 401     2233   1087   2437    130     18    526       C  
ATOM   3609  CG  LEU B 401      59.558  29.937  -6.377  1.00 13.42           C  
ANISOU 3609  CG  LEU B 401     2067    917   2113    221    225    370       C  
ATOM   3610  CD1 LEU B 401      60.804  29.091  -6.642  1.00 14.71           C  
ANISOU 3610  CD1 LEU B 401     2095   1099   2393    336     65    169       C  
ATOM   3611  CD2 LEU B 401      59.217  29.952  -4.895  1.00 15.62           C  
ANISOU 3611  CD2 LEU B 401     2076   1456   2403    330    212    259       C  
ATOM   3612  N   ASN B 402      59.789  30.076 -10.262  1.00 14.40           N  
ANISOU 3612  N   ASN B 402     2367   1426   1678   -319    208     51       N  
ATOM   3613  CA  ASN B 402      59.023  29.443 -11.333  1.00 14.23           C  
ANISOU 3613  CA  ASN B 402     2408   1247   1752   -273    311    405       C  
ATOM   3614  C   ASN B 402      58.841  27.957 -11.031  1.00 13.36           C  
ANISOU 3614  C   ASN B 402     2283   1051   1743   -227    503    351       C  
ATOM   3615  O   ASN B 402      59.783  27.170 -11.138  1.00 14.57           O  
ANISOU 3615  O   ASN B 402     2086   1406   2045   -163    238    317       O  
ATOM   3616  CB  ASN B 402      59.756  29.653 -12.666  1.00 16.26           C  
ANISOU 3616  CB  ASN B 402     2672   1710   1797   -421    474    379       C  
ATOM   3617  CG  ASN B 402      59.104  28.929 -13.836  1.00 18.17           C  
ANISOU 3617  CG  ASN B 402     2967   2141   1794   -467    380    636       C  
ATOM   3618  OD1 ASN B 402      58.059  28.297 -13.708  1.00 17.91           O  
ANISOU 3618  OD1 ASN B 402     2987   1812   2005   -440    186    391       O  
ATOM   3619  ND2 ASN B 402      59.741  29.025 -15.001  1.00 23.91           N  
ANISOU 3619  ND2 ASN B 402     3292   3029   2763   -738    789    590       N  
ATOM   3620  N   LEU B 403      57.632  27.579 -10.628  1.00 12.86           N  
ANISOU 3620  N   LEU B 403     2082   1138   1666   -396    544    133       N  
ATOM   3621  CA  LEU B 403      57.375  26.205 -10.198  1.00 12.13           C  
ANISOU 3621  CA  LEU B 403     1940    991   1676   -377    370    151       C  
ATOM   3622  C   LEU B 403      57.195  25.229 -11.366  1.00 12.91           C  
ANISOU 3622  C   LEU B 403     2045   1195   1663    -63     11    244       C  
ATOM   3623  O   LEU B 403      56.974  24.033 -11.153  1.00 12.78           O  
ANISOU 3623  O   LEU B 403     2052   1014   1789   -175    221    168       O  
ATOM   3624  CB  LEU B 403      56.181  26.161  -9.242  1.00 13.94           C  
ANISOU 3624  CB  LEU B 403     1905   1294   2095   -261    663     -5       C  
ATOM   3625  CG  LEU B 403      56.378  27.029  -7.991  1.00 13.34           C  
ANISOU 3625  CG  LEU B 403     1857   1437   1773     17    467     66       C  
ATOM   3626  CD1 LEU B 403      55.193  26.906  -7.036  1.00 15.14           C  
ANISOU 3626  CD1 LEU B 403     1910   1835   2006    -48    710    -58       C  
ATOM   3627  CD2 LEU B 403      57.690  26.688  -7.272  1.00 13.69           C  
ANISOU 3627  CD2 LEU B 403     1841   1531   1829    223     34   -137       C  
ATOM   3628  N   TRP B 404      57.290  25.743 -12.591  1.00 12.64           N  
ANISOU 3628  N   TRP B 404     1969   1231   1603     23   -325     22       N  
ATOM   3629  CA  TRP B 404      57.270  24.914 -13.792  1.00 13.96           C  
ANISOU 3629  CA  TRP B 404     2081   1706   1517    -86   -414     60       C  
ATOM   3630  C   TRP B 404      58.680  24.613 -14.307  1.00 14.37           C  
ANISOU 3630  C   TRP B 404     2022   1392   2044   -183    -83     43       C  
ATOM   3631  O   TRP B 404      58.854  23.797 -15.221  1.00 15.87           O  
ANISOU 3631  O   TRP B 404     2045   1592   2393    107     56   -146       O  
ATOM   3632  CB  TRP B 404      56.421  25.571 -14.891  1.00 17.33           C  
ANISOU 3632  CB  TRP B 404     2645   2320   1620   -164   -550   -187       C  
ATOM   3633  CG  TRP B 404      54.978  25.126 -14.861  1.00 21.72           C  
ANISOU 3633  CG  TRP B 404     3148   2713   2391    336   -743   -256       C  
ATOM   3634  CD1 TRP B 404      54.425  24.105 -15.580  1.00 23.79           C  
ANISOU 3634  CD1 TRP B 404     3064   2454   3522    458   -853   -145       C  
ATOM   3635  CD2 TRP B 404      53.915  25.677 -14.071  1.00 23.62           C  
ANISOU 3635  CD2 TRP B 404     3250   2265   3459    471   -469   -393       C  
ATOM   3636  NE1 TRP B 404      53.090  23.985 -15.287  1.00 24.95           N  
ANISOU 3636  NE1 TRP B 404     3405   2418   3656   1252   -333    159       N  
ATOM   3637  CE2 TRP B 404      52.751  24.936 -14.362  1.00 26.53           C  
ANISOU 3637  CE2 TRP B 404     3496   2993   3591   1067   -347    258       C  
ATOM   3638  CE3 TRP B 404      53.835  26.718 -13.140  1.00 28.18           C  
ANISOU 3638  CE3 TRP B 404     3171   2983   4553    550    573   -577       C  
ATOM   3639  CZ2 TRP B 404      51.524  25.208 -13.773  1.00 24.44           C  
ANISOU 3639  CZ2 TRP B 404     2912   3084   3291   1007   -364     72       C  
ATOM   3640  CZ3 TRP B 404      52.613  26.984 -12.546  1.00 29.36           C  
ANISOU 3640  CZ3 TRP B 404     3095   2955   5104    546    333   -227       C  
ATOM   3641  CH2 TRP B 404      51.474  26.232 -12.866  1.00 28.83           C  
ANISOU 3641  CH2 TRP B 404     3100   2928   4925    715   -133   -219       C  
ATOM   3642  N   ALA B 405      59.687  25.267 -13.729  1.00 13.86           N  
ANISOU 3642  N   ALA B 405     1917   1375   1974     66    427    271       N  
ATOM   3643  CA  ALA B 405      61.073  25.028 -14.132  1.00 15.30           C  
ANISOU 3643  CA  ALA B 405     1956   1343   2513    -50    265    295       C  
ATOM   3644  C   ALA B 405      61.504  23.586 -13.859  1.00 14.61           C  
ANISOU 3644  C   ALA B 405     2035   1220   2295    -10    279    168       C  
ATOM   3645  O   ALA B 405      61.248  23.042 -12.787  1.00 16.86           O  
ANISOU 3645  O   ALA B 405     2283   1623   2499    102    401    535       O  
ATOM   3646  CB  ALA B 405      62.011  25.992 -13.420  1.00 15.26           C  
ANISOU 3646  CB  ALA B 405     1797   1545   2455   -405    130    314       C  
ATOM   3647  N   VAL B 406      62.170  22.972 -14.831  1.00 14.16           N  
ANISOU 3647  N   VAL B 406     1841   1552   1985    236    272     69       N  
ATOM   3648  CA  VAL B 406      62.739  21.646 -14.639  1.00 15.19           C  
ANISOU 3648  CA  VAL B 406     1802   1663   2304    261     86      0       C  
ATOM   3649  C   VAL B 406      64.183  21.821 -14.187  1.00 14.52           C  
ANISOU 3649  C   VAL B 406     1682   1657   2179    290    227    113       C  
ATOM   3650  O   VAL B 406      64.944  22.537 -14.827  1.00 14.37           O  
ANISOU 3650  O   VAL B 406     1753   1633   2074   -116    252    189       O  
ATOM   3651  CB  VAL B 406      62.721  20.823 -15.945  1.00 17.38           C  
ANISOU 3651  CB  VAL B 406     1845   2024   2733    455   -258    -79       C  
ATOM   3652  CG1 VAL B 406      63.219  19.404 -15.690  1.00 17.98           C  
ANISOU 3652  CG1 VAL B 406     2238   1909   2683    567     58   -233       C  
ATOM   3653  CG2 VAL B 406      61.325  20.795 -16.540  1.00 19.05           C  
ANISOU 3653  CG2 VAL B 406     1870   2370   2998     90     40    275       C  
ATOM   3654  N   PRO B 407      64.565  21.184 -13.070  1.00 12.35           N  
ANISOU 3654  N   PRO B 407     1280   1030   2381   -207    260     87       N  
ATOM   3655  CA  PRO B 407      65.968  21.270 -12.647  1.00 12.00           C  
ANISOU 3655  CA  PRO B 407     1362   1306   1890     12    344    -51       C  
ATOM   3656  C   PRO B 407      66.906  20.747 -13.730  1.00 12.92           C  
ANISOU 3656  C   PRO B 407     1502   1163   2245   -122    621     33       C  
ATOM   3657  O   PRO B 407      66.565  19.816 -14.466  1.00 14.74           O  
ANISOU 3657  O   PRO B 407     1689   1394   2517   -193    665   -280       O  
ATOM   3658  CB  PRO B 407      66.019  20.347 -11.421  1.00 13.40           C  
ANISOU 3658  CB  PRO B 407     1764   1285   2042    275    195     65       C  
ATOM   3659  CG  PRO B 407      64.588  20.321 -10.908  1.00 12.68           C  
ANISOU 3659  CG  PRO B 407     1417   1197   2205    -68    345    -33       C  
ATOM   3660  CD  PRO B 407      63.756  20.348 -12.167  1.00 13.11           C  
ANISOU 3660  CD  PRO B 407     1507   1407   2067     -3     87    125       C  
ATOM   3661  N   ASN B 408      68.082  21.351 -13.828  1.00 13.26           N  
ANISOU 3661  N   ASN B 408     1361   1295   2381    -14    764    195       N  
ATOM   3662  CA  ASN B 408      69.150  20.757 -14.610  1.00 13.77           C  
ANISOU 3662  CA  ASN B 408     1620   1258   2352   -233    799    185       C  
ATOM   3663  C   ASN B 408      69.889  19.764 -13.725  1.00 13.59           C  
ANISOU 3663  C   ASN B 408     1535   1187   2441      7    504     64       C  
ATOM   3664  O   ASN B 408      70.779  20.136 -12.965  1.00 14.63           O  
ANISOU 3664  O   ASN B 408     1721   1235   2601    158    134   -148       O  
ATOM   3665  CB  ASN B 408      70.106  21.819 -15.155  1.00 16.91           C  
ANISOU 3665  CB  ASN B 408     2006   1847   2570    -83    823    239       C  
ATOM   3666  CG  ASN B 408      71.155  21.226 -16.078  1.00 24.51           C  
ANISOU 3666  CG  ASN B 408     2739   2748   3825    485   1108   1186       C  
ATOM   3667  OD1 ASN B 408      71.451  20.026 -16.008  1.00 28.57           O  
ANISOU 3667  OD1 ASN B 408     3024   3535   4297    778   1137   1424       O  
ATOM   3668  ND2 ASN B 408      71.722  22.052 -16.948  1.00 28.04           N  
ANISOU 3668  ND2 ASN B 408     3202   3236   4217    364   1432    934       N  
ATOM   3669  N   TYR B 409      69.500  18.495 -13.816  1.00 13.63           N  
ANISOU 3669  N   TYR B 409     1422   1208   2549     80    673     51       N  
ATOM   3670  CA  TYR B 409      70.015  17.468 -12.921  1.00 13.05           C  
ANISOU 3670  CA  TYR B 409     1296   1068   2593     53    691    261       C  
ATOM   3671  C   TYR B 409      71.453  17.079 -13.234  1.00 13.15           C  
ANISOU 3671  C   TYR B 409     1532   1218   2246    -51    727    -82       C  
ATOM   3672  O   TYR B 409      72.138  16.483 -12.391  1.00 14.47           O  
ANISOU 3672  O   TYR B 409     1711   1404   2383      6    504   -169       O  
ATOM   3673  CB  TYR B 409      69.140  16.216 -12.997  1.00 13.52           C  
ANISOU 3673  CB  TYR B 409     1257   1341   2539   -243    734    111       C  
ATOM   3674  CG  TYR B 409      67.726  16.404 -12.490  1.00 11.25           C  
ANISOU 3674  CG  TYR B 409     1068   1121   2086    -98    578     34       C  
ATOM   3675  CD1 TYR B 409      66.703  16.765 -13.353  1.00 12.42           C  
ANISOU 3675  CD1 TYR B 409     1225   1244   2249     58    216   -232       C  
ATOM   3676  CD2 TYR B 409      67.418  16.218 -11.145  1.00 12.50           C  
ANISOU 3676  CD2 TYR B 409     1062   1466   2222     29    613    288       C  
ATOM   3677  CE1 TYR B 409      65.410  16.930 -12.897  1.00 11.48           C  
ANISOU 3677  CE1 TYR B 409     1335   1088   1939     52    588   -143       C  
ATOM   3678  CE2 TYR B 409      66.119  16.375 -10.673  1.00 12.62           C  
ANISOU 3678  CE2 TYR B 409     1226   1395   2174     68    271     75       C  
ATOM   3679  CZ  TYR B 409      65.126  16.729 -11.557  1.00 10.21           C  
ANISOU 3679  CZ  TYR B 409     1061    932   1885    -37    351    -13       C  
ATOM   3680  OH  TYR B 409      63.840  16.892 -11.104  1.00 10.79           O  
ANISOU 3680  OH  TYR B 409     1049   1031   2020     30    299     -9       O  
ATOM   3681  N   GLY B 410      71.898  17.402 -14.446  1.00 13.62           N  
ANISOU 3681  N   GLY B 410     1496   1235   2443   -123    974   -448       N  
ATOM   3682  CA  GLY B 410      73.237  17.055 -14.887  1.00 14.43           C  
ANISOU 3682  CA  GLY B 410     1822   1396   2264     61   1033   -255       C  
ATOM   3683  C   GLY B 410      73.245  15.970 -15.948  1.00 15.49           C  
ANISOU 3683  C   GLY B 410     2146   1389   2350    253   1006   -253       C  
ATOM   3684  O   GLY B 410      72.369  15.113 -15.982  1.00 19.43           O  
ANISOU 3684  O   GLY B 410     2671   1587   3123   -101   1184   -484       O  
ATOM   3685  N   SER B 411      74.234  16.028 -16.830  1.00 14.50           N  
ANISOU 3685  N   SER B 411     2071   1305   2133    622    896    120       N  
ATOM   3686  CA  SER B 411      74.384  15.037 -17.885  1.00 14.75           C  
ANISOU 3686  CA  SER B 411     2121   1575   1909    745    699   -170       C  
ATOM   3687  C   SER B 411      75.651  14.246 -17.617  1.00 15.58           C  
ANISOU 3687  C   SER B 411     1888   1481   2549    637    566   -418       C  
ATOM   3688  O   SER B 411      76.602  14.748 -17.027  1.00 20.99           O  
ANISOU 3688  O   SER B 411     2228   1662   4084    641    215   -635       O  
ATOM   3689  CB  SER B 411      74.487  15.719 -19.242  1.00 20.99           C  
ANISOU 3689  CB  SER B 411     2730   2599   2646    777    796    587       C  
ATOM   3690  OG  SER B 411      75.752  16.338 -19.387  1.00 28.20           O  
ANISOU 3690  OG  SER B 411     3474   3085   4154    827    751    542       O  
ATOM   3691  N   ASN B 412      75.649  12.990 -18.039  1.00 13.61           N  
ANISOU 3691  N   ASN B 412     1770   1452   1950    817    364   -190       N  
ATOM   3692  CA  ASN B 412      76.806  12.127 -17.836  1.00 13.41           C  
ANISOU 3692  CA  ASN B 412     1792   1372   1930    775    496     -6       C  
ATOM   3693  C   ASN B 412      77.204  11.478 -19.149  1.00 12.55           C  
ANISOU 3693  C   ASN B 412     1694   1130   1943    493    459     56       C  
ATOM   3694  O   ASN B 412      76.777  10.368 -19.448  1.00 12.35           O  
ANISOU 3694  O   ASN B 412     1717   1087   1887    383    384    -46       O  
ATOM   3695  CB  ASN B 412      76.502  11.065 -16.777  1.00 13.99           C  
ANISOU 3695  CB  ASN B 412     1591   1696   2026    893    175    144       C  
ATOM   3696  CG  ASN B 412      77.745  10.288 -16.356  1.00 12.72           C  
ANISOU 3696  CG  ASN B 412     1629   1501   1702    528    470     80       C  
ATOM   3697  OD1 ASN B 412      78.785  10.360 -17.014  1.00 13.73           O  
ANISOU 3697  OD1 ASN B 412     1620   1549   2048    470    470   -149       O  
ATOM   3698  ND2 ASN B 412      77.641   9.538 -15.258  1.00 12.90           N  
ANISOU 3698  ND2 ASN B 412     1680   1463   1758    464    271   -139       N  
ATOM   3699  N   LEU B 413      78.032  12.176 -19.924  1.00 11.88           N  
ANISOU 3699  N   LEU B 413     1732    959   1822    261    254   -249       N  
ATOM   3700  CA  LEU B 413      78.483  11.694 -21.233  1.00 11.65           C  
ANISOU 3700  CA  LEU B 413     1632    783   2009    399    329    -87       C  
ATOM   3701  C   LEU B 413      77.326  11.139 -22.075  1.00 10.07           C  
ANISOU 3701  C   LEU B 413     1496    672   1656     71    454   -278       C  
ATOM   3702  O   LEU B 413      76.429  11.893 -22.447  1.00 12.32           O  
ANISOU 3702  O   LEU B 413     1762    768   2149    446     91   -119       O  
ATOM   3703  CB  LEU B 413      79.661  10.710 -21.094  1.00 12.06           C  
ANISOU 3703  CB  LEU B 413     1396    839   2348   -164    386    -68       C  
ATOM   3704  CG  LEU B 413      80.881  11.346 -20.414  1.00 12.38           C  
ANISOU 3704  CG  LEU B 413     1538    704   2460    -92    374     44       C  
ATOM   3705  CD1 LEU B 413      82.008  10.329 -20.228  1.00 12.81           C  
ANISOU 3705  CD1 LEU B 413     1415   1014   2438    273    366    -56       C  
ATOM   3706  CD2 LEU B 413      81.378  12.579 -21.193  1.00 16.07           C  
ANISOU 3706  CD2 LEU B 413     1896    932   3279     48    300    325       C  
ATOM   3707  N   THR B 414      77.339   9.841 -22.404  1.00 10.70           N  
ANISOU 3707  N   THR B 414     1540    802   1723    -16    242   -245       N  
ATOM   3708  CA  THR B 414      76.304   9.296 -23.289  1.00 10.23           C  
ANISOU 3708  CA  THR B 414     1475    759   1654    233    465   -243       C  
ATOM   3709  C   THR B 414      75.081   8.766 -22.544  1.00 12.23           C  
ANISOU 3709  C   THR B 414     1529    996   2123    431    705    287       C  
ATOM   3710  O   THR B 414      74.120   8.327 -23.175  1.00 13.04           O  
ANISOU 3710  O   THR B 414     1432   1138   2384    305    429     72       O  
ATOM   3711  CB  THR B 414      76.821   8.146 -24.185  1.00 10.62           C  
ANISOU 3711  CB  THR B 414     1468    690   1877    291    440     70       C  
ATOM   3712  OG1 THR B 414      77.045   6.988 -23.375  1.00 10.77           O  
ANISOU 3712  OG1 THR B 414     1393    802   1895    299    378    152       O  
ATOM   3713  CG2 THR B 414      78.113   8.539 -24.912  1.00 12.40           C  
ANISOU 3713  CG2 THR B 414     1452    960   2300    -13    617    -85       C  
ATOM   3714  N   GLN B 415      75.112   8.786 -21.216  1.00 12.15           N  
ANISOU 3714  N   GLN B 415     1277   1223   2116    324    689    238       N  
ATOM   3715  CA  GLN B 415      74.028   8.167 -20.456  1.00 13.48           C  
ANISOU 3715  CA  GLN B 415     1226   1904   1991    -15    551    353       C  
ATOM   3716  C   GLN B 415      72.716   8.929 -20.625  1.00 15.06           C  
ANISOU 3716  C   GLN B 415     1239   2237   2247    184    629   -192       C  
ATOM   3717  O   GLN B 415      72.702  10.159 -20.697  1.00 16.80           O  
ANISOU 3717  O   GLN B 415     1568   2119   2695    386    428   -376       O  
ATOM   3718  CB  GLN B 415      74.387   8.038 -18.971  1.00 17.12           C  
ANISOU 3718  CB  GLN B 415     1582   2682   2239    203    794    535       C  
ATOM   3719  CG  GLN B 415      75.695   7.279 -18.698  1.00 16.91           C  
ANISOU 3719  CG  GLN B 415     1435   2789   2201   -151    441    348       C  
ATOM   3720  CD  GLN B 415      75.716   5.882 -19.305  1.00 17.90           C  
ANISOU 3720  CD  GLN B 415     1878   2622   2299   -248    212    359       C  
ATOM   3721  OE1 GLN B 415      76.482   5.604 -20.228  1.00 20.75           O  
ANISOU 3721  OE1 GLN B 415     2293   2531   3059   -197    442     60       O  
ATOM   3722  NE2 GLN B 415      74.884   4.992 -18.774  1.00 19.28           N  
ANISOU 3722  NE2 GLN B 415     1987   2473   2863   -464    376    429       N  
ATOM   3723  N   ALA B 416      71.613   8.189 -20.666  1.00 17.05           N  
ANISOU 3723  N   ALA B 416     1214   2385   2880    114    172   -507       N  
ATOM   3724  CA  ALA B 416      70.290   8.796 -20.810  1.00 19.19           C  
ANISOU 3724  CA  ALA B 416     1270   2777   3242     20    186  -1002       C  
ATOM   3725  C   ALA B 416      69.956   9.725 -19.642  1.00 21.38           C  
ANISOU 3725  C   ALA B 416     1681   3170   3272     65    493   -612       C  
ATOM   3726  O   ALA B 416      70.393   9.501 -18.515  1.00 22.60           O  
ANISOU 3726  O   ALA B 416     1884   3456   3245    383    884   -413       O  
ATOM   3727  CB  ALA B 416      69.231   7.713 -20.955  1.00 21.88           C  
ANISOU 3727  CB  ALA B 416     1599   2854   3858    129    101  -1431       C  
ATOM   3728  N   SER B 417      69.187  10.776 -19.920  1.00 21.08           N  
ANISOU 3728  N   SER B 417     2040   2910   3057    254    599   -484       N  
ATOM   3729  CA  SER B 417      68.782  11.726 -18.882  1.00 20.24           C  
ANISOU 3729  CA  SER B 417     2128   2671   2890    305    659    -60       C  
ATOM   3730  C   SER B 417      67.892  11.065 -17.831  1.00 19.76           C  
ANISOU 3730  C   SER B 417     2281   2787   2439    550    726   -398       C  
ATOM   3731  O   SER B 417      67.951  11.420 -16.650  1.00 22.29           O  
ANISOU 3731  O   SER B 417     2652   3214   2601    863    454   -708       O  
ATOM   3732  CB  SER B 417      68.054  12.930 -19.489  1.00 22.48           C  
ANISOU 3732  CB  SER B 417     2151   2650   3741    387    712    -26       C  
ATOM   3733  OG  SER B 417      66.726  12.593 -19.870  1.00 18.31           O  
ANISOU 3733  OG  SER B 417     1890   2359   2708    197    638    -64       O  
ATOM   3734  N   GLN B 418      67.070  10.114 -18.276  1.00 15.77           N  
ANISOU 3734  N   GLN B 418     1641   1895   2456    441    430   -282       N  
ATOM   3735  CA  GLN B 418      66.083   9.442 -17.428  1.00 16.97           C  
ANISOU 3735  CA  GLN B 418     1890   1977   2580    604    671    351       C  
ATOM   3736  C   GLN B 418      64.913  10.351 -17.039  1.00 15.48           C  
ANISOU 3736  C   GLN B 418     1772   1580   2530    417    428     59       C  
ATOM   3737  O   GLN B 418      64.107   9.998 -16.178  1.00 16.02           O  
ANISOU 3737  O   GLN B 418     2022   1661   2404    430    625    126       O  
ATOM   3738  CB  GLN B 418      66.726   8.858 -16.164  1.00 20.31           C  
ANISOU 3738  CB  GLN B 418     2273   2738   2704   1056    740    363       C  
ATOM   3739  CG  GLN B 418      68.027   8.088 -16.390  1.00 23.93           C  
ANISOU 3739  CG  GLN B 418     2703   2902   3488   1385    938    327       C  
ATOM   3740  CD  GLN B 418      67.855   6.821 -17.213  1.00 29.05           C  
ANISOU 3740  CD  GLN B 418     3313   3123   4601   1625   1152    557       C  
ATOM   3741  OE1 GLN B 418      68.839   6.181 -17.596  1.00 35.86           O  
ANISOU 3741  OE1 GLN B 418     3760   3669   6197   1797   1074    -79       O  
ATOM   3742  NE2 GLN B 418      66.616   6.449 -17.487  1.00 27.66           N  
ANISOU 3742  NE2 GLN B 418     3341   3028   4138   1621   1215    752       N  
ATOM   3743  N   LEU B 419      64.818  11.524 -17.659  1.00 13.08           N  
ANISOU 3743  N   LEU B 419     1490   1468   2012    309    507    -74       N  
ATOM   3744  CA  LEU B 419      63.733  12.448 -17.329  1.00 13.42           C  
ANISOU 3744  CA  LEU B 419     1488   1362   2248    100    497      9       C  
ATOM   3745  C   LEU B 419      62.365  11.913 -17.730  1.00 12.59           C  
ANISOU 3745  C   LEU B 419     1401   1365   2016     11    281   -125       C  
ATOM   3746  O   LEU B 419      62.203  11.351 -18.815  1.00 15.59           O  
ANISOU 3746  O   LEU B 419     1630   2077   2216     71    199   -542       O  
ATOM   3747  CB  LEU B 419      63.941  13.800 -18.011  1.00 13.94           C  
ANISOU 3747  CB  LEU B 419     1670   1382   2243     -1    374    -75       C  
ATOM   3748  CG  LEU B 419      65.122  14.643 -17.537  1.00 15.01           C  
ANISOU 3748  CG  LEU B 419     1974   1529   2198   -190     66    162       C  
ATOM   3749  CD1 LEU B 419      65.393  15.772 -18.523  1.00 17.51           C  
ANISOU 3749  CD1 LEU B 419     2452   1889   2311   -249    225    308       C  
ATOM   3750  CD2 LEU B 419      64.861  15.186 -16.149  1.00 14.53           C  
ANISOU 3750  CD2 LEU B 419     2012   1614   1895    -47    378    -50       C  
ATOM   3751  N   ALA B 420      61.376  12.092 -16.857  1.00 11.61           N  
ANISOU 3751  N   ALA B 420     1230   1100   2079    -14    256    -45       N  
ATOM   3752  CA  ALA B 420      60.000  11.892 -17.274  1.00 11.67           C  
ANISOU 3752  CA  ALA B 420     1347   1179   1907     12    161    -95       C  
ATOM   3753  C   ALA B 420      59.728  12.915 -18.372  1.00 12.78           C  
ANISOU 3753  C   ALA B 420     1656   1297   1904    181    212   -118       C  
ATOM   3754  O   ALA B 420      60.207  14.043 -18.302  1.00 12.57           O  
ANISOU 3754  O   ALA B 420     1632   1343   1802    173     92    -17       O  
ATOM   3755  CB  ALA B 420      59.047  12.070 -16.102  1.00 12.24           C  
ANISOU 3755  CB  ALA B 420     1599   1403   1647    116    429     27       C  
ATOM   3756  N   PRO B 421      58.970  12.524 -19.404  1.00 14.43           N  
ANISOU 3756  N   PRO B 421     1753   1573   2157     60    198     20       N  
ATOM   3757  CA  PRO B 421      58.825  13.406 -20.569  1.00 14.24           C  
ANISOU 3757  CA  PRO B 421     1859   1761   1789    182     53   -279       C  
ATOM   3758  C   PRO B 421      57.941  14.638 -20.323  1.00 13.34           C  
ANISOU 3758  C   PRO B 421     1779   1621   1667    -36    356    106       C  
ATOM   3759  O   PRO B 421      57.128  14.655 -19.390  1.00 13.46           O  
ANISOU 3759  O   PRO B 421     1725   1579   1809    103    198     12       O  
ATOM   3760  CB  PRO B 421      58.174  12.493 -21.613  1.00 15.60           C  
ANISOU 3760  CB  PRO B 421     2170   1847   1909   -119    289   -467       C  
ATOM   3761  CG  PRO B 421      57.450  11.461 -20.808  1.00 19.20           C  
ANISOU 3761  CG  PRO B 421     2362   2085   2846    103   -116   -409       C  
ATOM   3762  CD  PRO B 421      58.310  11.224 -19.602  1.00 15.46           C  
ANISOU 3762  CD  PRO B 421     1975   1657   2240     66   -260   -483       C  
ATOM   3763  N   PRO B 422      58.087  15.666 -21.172  1.00 14.01           N  
ANISOU 3763  N   PRO B 422     1854   1777   1691    305    533    164       N  
ATOM   3764  CA  PRO B 422      57.145  16.785 -21.087  1.00 14.07           C  
ANISOU 3764  CA  PRO B 422     1917   1797   1630    238    227    110       C  
ATOM   3765  C   PRO B 422      55.733  16.335 -21.451  1.00 14.78           C  
ANISOU 3765  C   PRO B 422     1958   1872   1785    255    290    166       C  
ATOM   3766  O   PRO B 422      55.549  15.358 -22.189  1.00 16.04           O  
ANISOU 3766  O   PRO B 422     1975   2181   1938    173     25    -43       O  
ATOM   3767  CB  PRO B 422      57.672  17.774 -22.133  1.00 16.55           C  
ANISOU 3767  CB  PRO B 422     2111   2027   2150    374    657    566       C  
ATOM   3768  CG  PRO B 422      58.467  16.942 -23.079  1.00 21.33           C  
ANISOU 3768  CG  PRO B 422     2586   2460   3056    832    972    876       C  
ATOM   3769  CD  PRO B 422      59.035  15.807 -22.291  1.00 16.37           C  
ANISOU 3769  CD  PRO B 422     2249   2291   1680    602    554    330       C  
ATOM   3770  N   ILE B 423      54.742  17.031 -20.913  1.00 14.09           N  
ANISOU 3770  N   ILE B 423     1676   1853   1825    -38    270     60       N  
ATOM   3771  CA  ILE B 423      53.355  16.792 -21.278  1.00 14.09           C  
ANISOU 3771  CA  ILE B 423     1750   1852   1751    -43    146    242       C  
ATOM   3772  C   ILE B 423      52.878  17.996 -22.071  1.00 15.08           C  
ANISOU 3772  C   ILE B 423     1955   2068   1705    -20   -315     16       C  
ATOM   3773  O   ILE B 423      52.853  19.118 -21.566  1.00 15.73           O  
ANISOU 3773  O   ILE B 423     2061   1876   2038      5    -59    -22       O  
ATOM   3774  CB  ILE B 423      52.448  16.604 -20.049  1.00 13.96           C  
ANISOU 3774  CB  ILE B 423     1679   1708   1916      1   -126    289       C  
ATOM   3775  CG1 ILE B 423      52.959  15.464 -19.159  1.00 16.50           C  
ANISOU 3775  CG1 ILE B 423     2022   1935   2311    123    134    511       C  
ATOM   3776  CG2 ILE B 423      51.006  16.351 -20.484  1.00 15.63           C  
ANISOU 3776  CG2 ILE B 423     1645   1739   2553   -141   -304     48       C  
ATOM   3777  CD1 ILE B 423      52.232  15.355 -17.825  1.00 17.04           C  
ANISOU 3777  CD1 ILE B 423     2182   2253   2037     95    475    346       C  
ATOM   3778  N   TYR B 424      52.526  17.769 -23.328  1.00 16.89           N  
ANISOU 3778  N   TYR B 424     2019   2601   1796    149   -337    237       N  
ATOM   3779  CA  TYR B 424      52.063  18.863 -24.163  1.00 18.75           C  
ANISOU 3779  CA  TYR B 424     2272   3186   1664    391    -71    556       C  
ATOM   3780  C   TYR B 424      50.555  19.023 -24.037  1.00 21.22           C  
ANISOU 3780  C   TYR B 424     2361   3441   2260    393   -447    365       C  
ATOM   3781  O   TYR B 424      49.806  18.050 -24.121  1.00 22.54           O  
ANISOU 3781  O   TYR B 424     2533   3634   2395    298   -370    412       O  
ATOM   3782  CB  TYR B 424      52.510  18.660 -25.611  1.00 22.33           C  
ANISOU 3782  CB  TYR B 424     2635   3870   1979    765    127    445       C  
ATOM   3783  CG  TYR B 424      54.016  18.689 -25.739  1.00 25.70           C  
ANISOU 3783  CG  TYR B 424     3008   4484   2272    851    411    681       C  
ATOM   3784  CD1 TYR B 424      54.700  19.897 -25.829  1.00 27.41           C  
ANISOU 3784  CD1 TYR B 424     3138   4766   2509    773    579    638       C  
ATOM   3785  CD2 TYR B 424      54.761  17.516 -25.733  1.00 27.98           C  
ANISOU 3785  CD2 TYR B 424     3186   4844   2600   1039    668    768       C  
ATOM   3786  CE1 TYR B 424      56.078  19.935 -25.925  1.00 29.10           C  
ANISOU 3786  CE1 TYR B 424     3230   5023   2802    859    680    683       C  
ATOM   3787  CE2 TYR B 424      56.143  17.546 -25.834  1.00 29.60           C  
ANISOU 3787  CE2 TYR B 424     3323   5067   2855   1072    754   1029       C  
ATOM   3788  CZ  TYR B 424      56.794  18.758 -25.927  1.00 29.07           C  
ANISOU 3788  CZ  TYR B 424     3257   5109   2678    895    915   1045       C  
ATOM   3789  OH  TYR B 424      58.168  18.801 -26.022  1.00 31.69           O  
ANISOU 3789  OH  TYR B 424     3282   5454   3303    885    600    867       O  
ATOM   3790  N   PRO B 425      50.108  20.256 -23.782  1.00 23.10           N  
ANISOU 3790  N   PRO B 425     2055   3674   3048    568   -818   -376       N  
ATOM   3791  CA  PRO B 425      48.675  20.542 -23.688  1.00 24.02           C  
ANISOU 3791  CA  PRO B 425     2026   3964   3135    734   -612   -377       C  
ATOM   3792  C   PRO B 425      47.916  20.040 -24.914  1.00 20.81           C  
ANISOU 3792  C   PRO B 425     2095   3949   1864    602   -199      9       C  
ATOM   3793  O   PRO B 425      48.380  20.187 -26.042  1.00 23.20           O  
ANISOU 3793  O   PRO B 425     2094   4015   2706    521   -128    170       O  
ATOM   3794  CB  PRO B 425      48.634  22.069 -23.612  1.00 28.89           C  
ANISOU 3794  CB  PRO B 425     2256   3997   4724    920   -701   -605       C  
ATOM   3795  CG  PRO B 425      49.917  22.427 -22.942  1.00 30.86           C  
ANISOU 3795  CG  PRO B 425     2363   4068   5293    998   -864   -493       C  
ATOM   3796  CD  PRO B 425      50.931  21.436 -23.458  1.00 27.05           C  
ANISOU 3796  CD  PRO B 425     2038   3733   4505    687   -870   -391       C  
ATOM   3797  N   PRO B 426      46.745  19.439 -24.681  1.00 22.49           N  
ANISOU 3797  N   PRO B 426     2271   4149   2124    348   -223    323       N  
ATOM   3798  CA  PRO B 426      45.918  18.823 -25.720  1.00 23.68           C  
ANISOU 3798  CA  PRO B 426     2650   4000   2347    485   -318    949       C  
ATOM   3799  C   PRO B 426      45.293  19.845 -26.667  1.00 21.28           C  
ANISOU 3799  C   PRO B 426     2583   3285   2215    571   -705    207       C  
ATOM   3800  O   PRO B 426      45.063  19.525 -27.822  1.00 21.24           O  
ANISOU 3800  O   PRO B 426     2806   3096   2166    844   -685    -76       O  
ATOM   3801  CB  PRO B 426      44.825  18.117 -24.916  1.00 29.47           C  
ANISOU 3801  CB  PRO B 426     3030   4448   3720    452     69    926       C  
ATOM   3802  CG  PRO B 426      44.735  18.894 -23.650  1.00 30.60           C  
ANISOU 3802  CG  PRO B 426     2869   4733   4024    353   -140   1173       C  
ATOM   3803  CD  PRO B 426      46.141  19.310 -23.343  1.00 26.94           C  
ANISOU 3803  CD  PRO B 426     2550   4637   3048    233   -241   1057       C  
ATOM   3804  N   GLY B 427      45.021  21.052 -26.183  1.00 20.36           N  
ANISOU 3804  N   GLY B 427     2604   2842   2290    377   -759    -65       N  
ATOM   3805  CA  GLY B 427      44.358  22.054 -26.999  1.00 20.00           C  
ANISOU 3805  CA  GLY B 427     2503   2611   2486    430   -869     32       C  
ATOM   3806  C   GLY B 427      42.917  21.668 -27.273  1.00 18.56           C  
ANISOU 3806  C   GLY B 427     2567   2292   2193    607   -653    126       C  
ATOM   3807  O   GLY B 427      42.371  20.783 -26.608  1.00 17.12           O  
ANISOU 3807  O   GLY B 427     2446   2181   1879    554   -314     -9       O  
ATOM   3808  N   PHE B 428      42.306  22.338 -28.246  1.00 17.75           N  
ANISOU 3808  N   PHE B 428     2593   2347   1802    850   -346   -222       N  
ATOM   3809  CA  PHE B 428      40.918  22.090 -28.628  1.00 16.57           C  
ANISOU 3809  CA  PHE B 428     2455   2276   1565    645    -86   -286       C  
ATOM   3810  C   PHE B 428      39.963  22.148 -27.440  1.00 18.71           C  
ANISOU 3810  C   PHE B 428     2762   2520   1828    934    -78    -44       C  
ATOM   3811  O   PHE B 428      39.067  21.314 -27.297  1.00 20.83           O  
ANISOU 3811  O   PHE B 428     2839   2965   2111    797     52    -20       O  
ATOM   3812  CB  PHE B 428      40.791  20.775 -29.399  1.00 16.87           C  
ANISOU 3812  CB  PHE B 428     2573   2240   1595    565     19    143       C  
ATOM   3813  CG  PHE B 428      41.568  20.766 -30.678  1.00 16.34           C  
ANISOU 3813  CG  PHE B 428     2601   2148   1458    539     68    185       C  
ATOM   3814  CD1 PHE B 428      41.029  21.309 -31.833  1.00 16.58           C  
ANISOU 3814  CD1 PHE B 428     2644   2229   1425    585   -247    -49       C  
ATOM   3815  CD2 PHE B 428      42.853  20.252 -30.718  1.00 17.91           C  
ANISOU 3815  CD2 PHE B 428     2613   2393   1797    558     -6    -16       C  
ATOM   3816  CE1 PHE B 428      41.749  21.321 -33.005  1.00 18.81           C  
ANISOU 3816  CE1 PHE B 428     2763   2312   2071    664    -19   -157       C  
ATOM   3817  CE2 PHE B 428      43.577  20.252 -31.900  1.00 17.96           C  
ANISOU 3817  CE2 PHE B 428     2655   2544   1624    695    323   -129       C  
ATOM   3818  CZ  PHE B 428      43.018  20.793 -33.042  1.00 17.45           C  
ANISOU 3818  CZ  PHE B 428     2868   2442   1319    755    -11    270       C  
ATOM   3819  N   GLY B 429      40.170  23.148 -26.591  1.00 19.74           N  
ANISOU 3819  N   GLY B 429     3075   2548   1877   1246    -64    124       N  
ATOM   3820  CA  GLY B 429      39.289  23.389 -25.463  1.00 19.78           C  
ANISOU 3820  CA  GLY B 429     3259   2756   1498   1327    248    255       C  
ATOM   3821  C   GLY B 429      39.700  22.677 -24.190  1.00 20.46           C  
ANISOU 3821  C   GLY B 429     3290   2720   1765   1138    124    449       C  
ATOM   3822  O   GLY B 429      39.252  23.043 -23.107  1.00 21.59           O  
ANISOU 3822  O   GLY B 429     3582   3029   1590   1177    122     95       O  
ATOM   3823  N   GLU B 430      40.543  21.654 -24.302  1.00 18.35           N  
ANISOU 3823  N   GLU B 430     2916   2555   1502    890   -210    290       N  
ATOM   3824  CA  GLU B 430      41.004  20.951 -23.109  1.00 18.14           C  
ANISOU 3824  CA  GLU B 430     2729   2349   1812    452   -272   -228       C  
ATOM   3825  C   GLU B 430      42.168  21.683 -22.459  1.00 17.75           C  
ANISOU 3825  C   GLU B 430     2685   2544   1515    427   -189    178       C  
ATOM   3826  O   GLU B 430      42.936  22.376 -23.131  1.00 20.17           O  
ANISOU 3826  O   GLU B 430     2927   2908   1829    344    181    258       O  
ATOM   3827  CB  GLU B 430      41.391  19.502 -23.424  1.00 18.93           C  
ANISOU 3827  CB  GLU B 430     2739   2205   2249    472   -539   -357       C  
ATOM   3828  CG  GLU B 430      40.203  18.580 -23.679  1.00 19.28           C  
ANISOU 3828  CG  GLU B 430     2821   2078   2425    387   -627   -201       C  
ATOM   3829  CD  GLU B 430      40.620  17.140 -23.938  1.00 20.42           C  
ANISOU 3829  CD  GLU B 430     3060   2361   2338    408   -969   -174       C  
ATOM   3830  OE1 GLU B 430      41.575  16.665 -23.291  1.00 18.41           O  
ANISOU 3830  OE1 GLU B 430     2923   2547   1526    269   -587      2       O  
ATOM   3831  OE2 GLU B 430      40.002  16.485 -24.800  1.00 24.71           O  
ANISOU 3831  OE2 GLU B 430     3413   2700   3275    577  -1428   -285       O  
ATOM   3832  N   ALA B 431      42.295  21.515 -21.147  1.00 16.90           N  
ANISOU 3832  N   ALA B 431     2463   2350   1607    504   -365     59       N  
ATOM   3833  CA  ALA B 431      43.404  22.085 -20.395  1.00 16.37           C  
ANISOU 3833  CA  ALA B 431     2423   2007   1790    643   -545    221       C  
ATOM   3834  C   ALA B 431      43.871  21.066 -19.368  1.00 15.20           C  
ANISOU 3834  C   ALA B 431     1994   1961   1818    468   -322    319       C  
ATOM   3835  O   ALA B 431      43.058  20.351 -18.781  1.00 14.89           O  
ANISOU 3835  O   ALA B 431     1941   2051   1664    134   -141    225       O  
ATOM   3836  CB  ALA B 431      42.974  23.369 -19.704  1.00 18.29           C  
ANISOU 3836  CB  ALA B 431     2591   2045   2312    543   -478    -67       C  
ATOM   3837  N   ILE B 432      45.181  20.992 -19.157  1.00 14.09           N  
ANISOU 3837  N   ILE B 432     1830   2001   1521    379   -326    278       N  
ATOM   3838  CA  ILE B 432      45.734  20.120 -18.129  1.00 12.43           C  
ANISOU 3838  CA  ILE B 432     1649   1858   1215    378     31    231       C  
ATOM   3839  C   ILE B 432      45.239  20.564 -16.753  1.00 12.89           C  
ANISOU 3839  C   ILE B 432     1791   1613   1493    525    -71    421       C  
ATOM   3840  O   ILE B 432      45.200  21.767 -16.452  1.00 14.36           O  
ANISOU 3840  O   ILE B 432     1969   1626   1860    485   -145    341       O  
ATOM   3841  CB  ILE B 432      47.272  20.127 -18.162  1.00 13.25           C  
ANISOU 3841  CB  ILE B 432     1675   1835   1524    326    -90    141       C  
ATOM   3842  CG1 ILE B 432      47.780  19.571 -19.501  1.00 15.53           C  
ANISOU 3842  CG1 ILE B 432     2107   2074   1719    452    275   -375       C  
ATOM   3843  CG2 ILE B 432      47.838  19.342 -16.983  1.00 14.62           C  
ANISOU 3843  CG2 ILE B 432     1654   1841   2060    150   -405    174       C  
ATOM   3844  CD1 ILE B 432      49.273  19.732 -19.715  1.00 17.73           C  
ANISOU 3844  CD1 ILE B 432     2033   2279   2425    416    493   -239       C  
ATOM   3845  N   VAL B 433      44.838  19.600 -15.932  1.00 12.24           N  
ANISOU 3845  N   VAL B 433     1700   1785   1166    159     61    196       N  
ATOM   3846  CA  VAL B 433      44.430  19.889 -14.564  1.00 14.01           C  
ANISOU 3846  CA  VAL B 433     1671   1997   1653   -215   -109    -48       C  
ATOM   3847  C   VAL B 433      45.619  19.741 -13.623  1.00 11.77           C  
ANISOU 3847  C   VAL B 433     1643   1711   1117    227     29   -199       C  
ATOM   3848  O   VAL B 433      46.323  18.734 -13.652  1.00 14.02           O  
ANISOU 3848  O   VAL B 433     1974   1611   1743    553   -169    -29       O  
ATOM   3849  CB  VAL B 433      43.311  18.940 -14.084  1.00 16.04           C  
ANISOU 3849  CB  VAL B 433     1843   2608   1643   -346    117     80       C  
ATOM   3850  CG1 VAL B 433      42.982  19.203 -12.612  1.00 17.86           C  
ANISOU 3850  CG1 VAL B 433     1960   2950   1877   -342     87    -51       C  
ATOM   3851  CG2 VAL B 433      42.073  19.077 -14.963  1.00 17.79           C  
ANISOU 3851  CG2 VAL B 433     1735   3080   1945   -391   -185     25       C  
ATOM   3852  N   TYR B 434      45.843  20.755 -12.798  1.00 10.95           N  
ANISOU 3852  N   TYR B 434     1571   1433   1154    329   -182     34       N  
ATOM   3853  CA  TYR B 434      46.867  20.696 -11.769  1.00 11.20           C  
ANISOU 3853  CA  TYR B 434     1590   1117   1549    296    -22    168       C  
ATOM   3854  C   TYR B 434      46.222  20.613 -10.399  1.00 10.50           C  
ANISOU 3854  C   TYR B 434     1462   1222   1304    437     44    165       C  
ATOM   3855  O   TYR B 434      45.278  21.335 -10.100  1.00 12.91           O  
ANISOU 3855  O   TYR B 434     1612   1637   1655    928     -8    115       O  
ATOM   3856  CB  TYR B 434      47.785  21.924 -11.840  1.00 11.92           C  
ANISOU 3856  CB  TYR B 434     1650   1155   1725    221    183    175       C  
ATOM   3857  CG  TYR B 434      48.503  22.024 -13.159  1.00 10.58           C  
ANISOU 3857  CG  TYR B 434     1627   1136   1255    326     87     77       C  
ATOM   3858  CD1 TYR B 434      49.679  21.317 -13.383  1.00 14.16           C  
ANISOU 3858  CD1 TYR B 434     1777   1566   2037    539    383    -10       C  
ATOM   3859  CD2 TYR B 434      48.000  22.812 -14.194  1.00 12.18           C  
ANISOU 3859  CD2 TYR B 434     1925   1141   1561    428   -144     99       C  
ATOM   3860  CE1 TYR B 434      50.334  21.383 -14.590  1.00 15.19           C  
ANISOU 3860  CE1 TYR B 434     2079   1869   1823    576    457    428       C  
ATOM   3861  CE2 TYR B 434      48.652  22.879 -15.417  1.00 12.70           C  
ANISOU 3861  CE2 TYR B 434     1939   1277   1608    438    156     75       C  
ATOM   3862  CZ  TYR B 434      49.819  22.165 -15.603  1.00 14.44           C  
ANISOU 3862  CZ  TYR B 434     2104   1749   1631    749    432    558       C  
ATOM   3863  OH  TYR B 434      50.478  22.222 -16.804  1.00 17.84           O  
ANISOU 3863  OH  TYR B 434     2432   2173   2173    947    661    982       O  
ATOM   3864  N   PHE B 435      46.750  19.726  -9.570  1.00  9.91           N  
ANISOU 3864  N   PHE B 435     1417   1119   1227    294   -196    181       N  
ATOM   3865  CA  PHE B 435      46.363  19.618  -8.183  1.00  9.66           C  
ANISOU 3865  CA  PHE B 435     1465   1057   1147    445   -109    130       C  
ATOM   3866  C   PHE B 435      47.314  20.479  -7.367  1.00  9.84           C  
ANISOU 3866  C   PHE B 435     1507    980   1252    361   -115   -275       C  
ATOM   3867  O   PHE B 435      48.535  20.395  -7.524  1.00 11.15           O  
ANISOU 3867  O   PHE B 435     1396   1222   1618    426    262    -51       O  
ATOM   3868  CB  PHE B 435      46.408  18.144  -7.778  1.00 10.69           C  
ANISOU 3868  CB  PHE B 435     1307   1096   1657    300    -41     22       C  
ATOM   3869  CG  PHE B 435      45.566  17.282  -8.670  1.00  9.99           C  
ANISOU 3869  CG  PHE B 435     1159   1114   1523    232   -177   -224       C  
ATOM   3870  CD1 PHE B 435      44.214  17.131  -8.423  1.00 12.55           C  
ANISOU 3870  CD1 PHE B 435     1164   1592   2010      7   -237     91       C  
ATOM   3871  CD2 PHE B 435      46.117  16.677  -9.799  1.00 11.71           C  
ANISOU 3871  CD2 PHE B 435     1672    864   1912    284   -225   -229       C  
ATOM   3872  CE1 PHE B 435      43.426  16.374  -9.266  1.00 13.54           C  
ANISOU 3872  CE1 PHE B 435     1444   1587   2112    -32   -537   -118       C  
ATOM   3873  CE2 PHE B 435      45.336  15.914 -10.645  1.00 13.39           C  
ANISOU 3873  CE2 PHE B 435     1576   1297   2215    147   -287   -115       C  
ATOM   3874  CZ  PHE B 435      43.987  15.764 -10.380  1.00 14.81           C  
ANISOU 3874  CZ  PHE B 435     1808   1802   2017    388   -343   -244       C  
ATOM   3875  N   THR B 436      46.758  21.333  -6.517  1.00 10.04           N  
ANISOU 3875  N   THR B 436     1561   1029   1223    149   -148    -79       N  
ATOM   3876  CA  THR B 436      47.565  22.334  -5.829  1.00 11.10           C  
ANISOU 3876  CA  THR B 436     1726   1036   1454    365   -215    -11       C  
ATOM   3877  C   THR B 436      47.580  22.129  -4.327  1.00  9.62           C  
ANISOU 3877  C   THR B 436     1249   1063   1344    318     75     -9       C  
ATOM   3878  O   THR B 436      46.625  21.588  -3.753  1.00 11.25           O  
ANISOU 3878  O   THR B 436     1268   1557   1450    213     91    -97       O  
ATOM   3879  CB  THR B 436      47.091  23.769  -6.140  1.00 13.56           C  
ANISOU 3879  CB  THR B 436     1992   1371   1787    517   -412    193       C  
ATOM   3880  OG1 THR B 436      45.757  23.958  -5.651  1.00 17.17           O  
ANISOU 3880  OG1 THR B 436     2034   1743   2748    731   -804   -364       O  
ATOM   3881  CG2 THR B 436      47.120  24.009  -7.643  1.00 15.96           C  
ANISOU 3881  CG2 THR B 436     2576   1504   1982    442   -404    483       C  
ATOM   3882  N   SER B 437      48.667  22.580  -3.702  1.00 10.18           N  
ANISOU 3882  N   SER B 437     1332   1070   1467    175   -177     47       N  
ATOM   3883  CA  SER B 437      48.775  22.648  -2.250  1.00  8.92           C  
ANISOU 3883  CA  SER B 437     1314    982   1092    302   -217    -33       C  
ATOM   3884  C   SER B 437      49.366  23.993  -1.856  1.00  9.85           C  
ANISOU 3884  C   SER B 437     1392   1084   1266    273    209     24       C  
ATOM   3885  O   SER B 437      50.331  24.468  -2.458  1.00 12.12           O  
ANISOU 3885  O   SER B 437     1773   1210   1622    132    495    -84       O  
ATOM   3886  CB  SER B 437      49.703  21.550  -1.717  1.00 10.49           C  
ANISOU 3886  CB  SER B 437     1310    986   1689    605   -178    -30       C  
ATOM   3887  OG  SER B 437      49.206  20.265  -2.032  1.00 11.03           O  
ANISOU 3887  OG  SER B 437     1433    978   1780    368   -182   -256       O  
ATOM   3888  N   THR B 438      48.808  24.596  -0.819  1.00 10.67           N  
ANISOU 3888  N   THR B 438     1310   1246   1497    317    -29   -346       N  
ATOM   3889  CA  THR B 438      49.451  25.739  -0.207  1.00 10.70           C  
ANISOU 3889  CA  THR B 438     1351   1180   1533    297    -52   -327       C  
ATOM   3890  C   THR B 438      50.717  25.255   0.506  1.00 10.71           C  
ANISOU 3890  C   THR B 438     1334   1177   1557    122      4    -60       C  
ATOM   3891  O   THR B 438      50.684  24.294   1.280  1.00 11.94           O  
ANISOU 3891  O   THR B 438     1474   1135   1927    101    -19    -80       O  
ATOM   3892  CB  THR B 438      48.500  26.451   0.758  1.00 12.25           C  
ANISOU 3892  CB  THR B 438     1572   1351   1729    504   -151   -545       C  
ATOM   3893  OG1 THR B 438      47.345  26.875   0.029  1.00 15.04           O  
ANISOU 3893  OG1 THR B 438     1623   2039   2051    791   -359   -379       O  
ATOM   3894  CG2 THR B 438      49.179  27.655   1.391  1.00 13.29           C  
ANISOU 3894  CG2 THR B 438     1845   1130   2073    330   -116   -445       C  
ATOM   3895  N   PHE B 439      51.835  25.919   0.233  1.00 10.98           N  
ANISOU 3895  N   PHE B 439     1147   1375   1649    290     19   -168       N  
ATOM   3896  CA  PHE B 439      53.136  25.466   0.704  1.00 10.02           C  
ANISOU 3896  CA  PHE B 439     1063   1043   1702    256   -129   -259       C  
ATOM   3897  C   PHE B 439      54.054  26.677   0.701  1.00 10.54           C  
ANISOU 3897  C   PHE B 439     1241   1091   1673     54   -107   -337       C  
ATOM   3898  O   PHE B 439      53.850  27.595  -0.090  1.00 12.10           O  
ANISOU 3898  O   PHE B 439     1395   1298   1902     59    -64    121       O  
ATOM   3899  CB  PHE B 439      53.661  24.385  -0.256  1.00 11.57           C  
ANISOU 3899  CB  PHE B 439     1485   1125   1785    430     15   -348       C  
ATOM   3900  CG  PHE B 439      55.010  23.828   0.117  1.00 11.01           C  
ANISOU 3900  CG  PHE B 439     1440    950   1792    426    154     24       C  
ATOM   3901  CD1 PHE B 439      55.115  22.726   0.957  1.00 11.56           C  
ANISOU 3901  CD1 PHE B 439     1534    938   1920    391   -131   -103       C  
ATOM   3902  CD2 PHE B 439      56.174  24.393  -0.384  1.00 11.48           C  
ANISOU 3902  CD2 PHE B 439     1449   1182   1732    450    472   -284       C  
ATOM   3903  CE1 PHE B 439      56.355  22.215   1.300  1.00 13.01           C  
ANISOU 3903  CE1 PHE B 439     1923   1126   1894    544     39     -9       C  
ATOM   3904  CE2 PHE B 439      57.410  23.889  -0.034  1.00 13.40           C  
ANISOU 3904  CE2 PHE B 439     1634   1050   2408    476     62   -110       C  
ATOM   3905  CZ  PHE B 439      57.501  22.799   0.804  1.00 13.67           C  
ANISOU 3905  CZ  PHE B 439     1760   1174   2261    376     32   -305       C  
ATOM   3906  N   PRO B 440      55.064  26.693   1.582  1.00  9.85           N  
ANISOU 3906  N   PRO B 440     1198    913   1631     44      3    -45       N  
ATOM   3907  CA  PRO B 440      55.972  27.843   1.649  1.00 10.25           C  
ANISOU 3907  CA  PRO B 440     1267   1011   1614   -106     36     22       C  
ATOM   3908  C   PRO B 440      57.011  27.892   0.521  1.00 10.86           C  
ANISOU 3908  C   PRO B 440     1224   1000   1901    169   -141    100       C  
ATOM   3909  O   PRO B 440      58.223  27.911   0.767  1.00 10.79           O  
ANISOU 3909  O   PRO B 440     1337    913   1850     91     26   -120       O  
ATOM   3910  CB  PRO B 440      56.635  27.681   3.017  1.00 11.05           C  
ANISOU 3910  CB  PRO B 440     1476   1108   1612    227    -55     -9       C  
ATOM   3911  CG  PRO B 440      56.637  26.183   3.232  1.00 11.61           C  
ANISOU 3911  CG  PRO B 440     1679    848   1882    407   -228    113       C  
ATOM   3912  CD  PRO B 440      55.292  25.751   2.695  1.00 10.43           C  
ANISOU 3912  CD  PRO B 440     1386   1199   1379    250   -364    391       C  
ATOM   3913  N   THR B 441      56.521  27.895  -0.715  1.00 10.53           N  
ANISOU 3913  N   THR B 441     1445    867   1689     97    168    108       N  
ATOM   3914  CA  THR B 441      57.299  28.370  -1.852  1.00 11.22           C  
ANISOU 3914  CA  THR B 441     1634    758   1869    180    -83    -30       C  
ATOM   3915  C   THR B 441      57.117  29.885  -1.834  1.00 11.74           C  
ANISOU 3915  C   THR B 441     1663    898   1898    308   -128    164       C  
ATOM   3916  O   THR B 441      56.158  30.431  -2.385  1.00 11.72           O  
ANISOU 3916  O   THR B 441     1646    764   2041    254     32     70       O  
ATOM   3917  CB  THR B 441      56.819  27.742  -3.182  1.00 10.93           C  
ANISOU 3917  CB  THR B 441     1282    819   2050    154    -49     53       C  
ATOM   3918  OG1 THR B 441      55.413  27.472  -3.103  1.00 11.95           O  
ANISOU 3918  OG1 THR B 441     1248   1232   2060    138     -9   -154       O  
ATOM   3919  CG2 THR B 441      57.559  26.426  -3.459  1.00 12.23           C  
ANISOU 3919  CG2 THR B 441     1832    960   1854    409    -19     81       C  
ATOM   3920  N   VAL B 442      58.019  30.562  -1.140  1.00 11.24           N  
ANISOU 3920  N   VAL B 442     1648    794   1827     51      8     83       N  
ATOM   3921  CA  VAL B 442      57.825  31.976  -0.831  1.00 12.92           C  
ANISOU 3921  CA  VAL B 442     1996    685   2229    145     59    -86       C  
ATOM   3922  C   VAL B 442      57.879  32.823  -2.098  1.00 13.18           C  
ANISOU 3922  C   VAL B 442     2130    808   2069    228     86     84       C  
ATOM   3923  O   VAL B 442      58.805  32.688  -2.902  1.00 14.91           O  
ANISOU 3923  O   VAL B 442     2275   1038   2350    255    311    222       O  
ATOM   3924  CB  VAL B 442      58.841  32.452   0.225  1.00 13.43           C  
ANISOU 3924  CB  VAL B 442     2088    679   2335   -184     40     42       C  
ATOM   3925  CG1 VAL B 442      58.736  33.959   0.454  1.00 13.45           C  
ANISOU 3925  CG1 VAL B 442     2204    618   2286     41     26    -53       C  
ATOM   3926  CG2 VAL B 442      58.611  31.701   1.534  1.00 13.98           C  
ANISOU 3926  CG2 VAL B 442     1996    964   2352    -98    149    107       C  
ATOM   3927  N   SER B 443      56.863  33.678  -2.251  1.00 13.14           N  
ANISOU 3927  N   SER B 443     2139    735   2117    252    -80    226       N  
ATOM   3928  CA  SER B 443      56.596  34.521  -3.436  1.00 14.57           C  
ANISOU 3928  CA  SER B 443     2121   1046   2368    146    221    233       C  
ATOM   3929  C   SER B 443      55.675  33.820  -4.435  1.00 14.56           C  
ANISOU 3929  C   SER B 443     2220   1011   2302    254    116    134       C  
ATOM   3930  O   SER B 443      55.222  34.422  -5.417  1.00 17.16           O  
ANISOU 3930  O   SER B 443     2581   1290   2650    500    -90    388       O  
ATOM   3931  CB  SER B 443      57.869  35.057  -4.126  1.00 15.27           C  
ANISOU 3931  CB  SER B 443     2278   1118   2404    265    324    511       C  
ATOM   3932  OG  SER B 443      58.462  34.097  -4.990  1.00 16.63           O  
ANISOU 3932  OG  SER B 443     2563   1214   2542    386    579     62       O  
ATOM   3933  N   ASN B 444      55.376  32.550  -4.172  1.00 14.60           N  
ANISOU 3933  N   ASN B 444     2078   1383   2086    172     82     62       N  
ATOM   3934  CA  ASN B 444      54.497  31.787  -5.042  1.00 13.90           C  
ANISOU 3934  CA  ASN B 444     2205   1435   1642    367    222    265       C  
ATOM   3935  C   ASN B 444      53.993  30.542  -4.306  1.00 12.41           C  
ANISOU 3935  C   ASN B 444     1981   1243   1491    284    -54    103       C  
ATOM   3936  O   ASN B 444      54.332  29.414  -4.677  1.00 13.17           O  
ANISOU 3936  O   ASN B 444     1948   1263   1792    293    -11    -10       O  
ATOM   3937  CB  ASN B 444      55.265  31.412  -6.308  1.00 16.16           C  
ANISOU 3937  CB  ASN B 444     2598   1579   1962    300    113    278       C  
ATOM   3938  CG  ASN B 444      54.386  30.849  -7.385  1.00 17.88           C  
ANISOU 3938  CG  ASN B 444     2935   1673   2185    390    -59    129       C  
ATOM   3939  OD1 ASN B 444      53.161  30.793  -7.250  1.00 19.24           O  
ANISOU 3939  OD1 ASN B 444     3024   1961   2325    277   -423     54       O  
ATOM   3940  ND2 ASN B 444      55.007  30.442  -8.485  1.00 19.38           N  
ANISOU 3940  ND2 ASN B 444     3221   1721   2421    385   -135    -88       N  
ATOM   3941  N   PRO B 445      53.184  30.751  -3.250  1.00 12.55           N  
ANISOU 3941  N   PRO B 445     1928   1183   1657    494     76     72       N  
ATOM   3942  CA  PRO B 445      52.921  29.700  -2.254  1.00 12.02           C  
ANISOU 3942  CA  PRO B 445     1911   1132   1525    277    104    118       C  
ATOM   3943  C   PRO B 445      51.813  28.721  -2.631  1.00 12.68           C  
ANISOU 3943  C   PRO B 445     1924   1210   1685    226    -18    354       C  
ATOM   3944  O   PRO B 445      50.976  28.363  -1.794  1.00 15.31           O  
ANISOU 3944  O   PRO B 445     2288   1526   2004    269    108    368       O  
ATOM   3945  CB  PRO B 445      52.526  30.502  -1.012  1.00 13.70           C  
ANISOU 3945  CB  PRO B 445     2077   1295   1833    659    -14   -135       C  
ATOM   3946  CG  PRO B 445      51.865  31.737  -1.573  1.00 14.42           C  
ANISOU 3946  CG  PRO B 445     2103   1319   2057    794    -50    192       C  
ATOM   3947  CD  PRO B 445      52.632  32.057  -2.837  1.00 13.80           C  
ANISOU 3947  CD  PRO B 445     2044   1304   1896    524    466    196       C  
ATOM   3948  N   LYS B 446      51.819  28.286  -3.883  1.00 12.25           N  
ANISOU 3948  N   LYS B 446     1930    991   1733    156    -13    -39       N  
ATOM   3949  CA  LYS B 446      50.855  27.313  -4.374  1.00 13.39           C  
ANISOU 3949  CA  LYS B 446     2005   1220   1860    436    203     94       C  
ATOM   3950  C   LYS B 446      51.574  26.359  -5.310  1.00 12.53           C  
ANISOU 3950  C   LYS B 446     1799   1013   1949    229    319    -58       C  
ATOM   3951  O   LYS B 446      51.963  26.738  -6.418  1.00 13.92           O  
ANISOU 3951  O   LYS B 446     2141   1070   2079    393    476     28       O  
ATOM   3952  CB  LYS B 446      49.703  28.001  -5.114  1.00 15.78           C  
ANISOU 3952  CB  LYS B 446     2207   1809   1980    403    453   -239       C  
ATOM   3953  CG  LYS B 446      48.661  27.016  -5.603  1.00 19.66           C  
ANISOU 3953  CG  LYS B 446     2476   2169   2825    173    106   -543       C  
ATOM   3954  CD  LYS B 446      47.339  27.679  -5.929  1.00 26.31           C  
ANISOU 3954  CD  LYS B 446     2995   2995   4006    594   -146   -808       C  
ATOM   3955  CE  LYS B 446      47.397  28.435  -7.236  1.00 30.85           C  
ANISOU 3955  CE  LYS B 446     3316   3588   4815   1078   -144   -944       C  
ATOM   3956  NZ  LYS B 446      46.062  29.003  -7.569  1.00 35.21           N  
ANISOU 3956  NZ  LYS B 446     3548   4139   5690   1194   -607   -725       N  
ATOM   3957  N   VAL B 447      51.765  25.123  -4.857  1.00 11.13           N  
ANISOU 3957  N   VAL B 447     1397    969   1864    208    302     26       N  
ATOM   3958  CA  VAL B 447      52.550  24.152  -5.621  1.00 10.70           C  
ANISOU 3958  CA  VAL B 447     1225   1032   1809    365     -4   -177       C  
ATOM   3959  C   VAL B 447      51.640  23.293  -6.493  1.00 10.00           C  
ANISOU 3959  C   VAL B 447     1220    939   1640    167    137    251       C  
ATOM   3960  O   VAL B 447      50.771  22.596  -5.979  1.00  9.45           O  
ANISOU 3960  O   VAL B 447     1167    958   1464    194     88     98       O  
ATOM   3961  CB  VAL B 447      53.369  23.228  -4.696  1.00 10.26           C  
ANISOU 3961  CB  VAL B 447     1174   1008   1717    220     70     47       C  
ATOM   3962  CG1 VAL B 447      53.988  22.082  -5.500  1.00 10.81           C  
ANISOU 3962  CG1 VAL B 447     1256   1070   1779    476     84   -190       C  
ATOM   3963  CG2 VAL B 447      54.439  24.023  -3.950  1.00 12.25           C  
ANISOU 3963  CG2 VAL B 447     1418   1201   2034    -69   -490    -85       C  
ATOM   3964  N   PRO B 448      51.819  23.360  -7.819  1.00 10.91           N  
ANISOU 3964  N   PRO B 448     1364   1063   1719     56     65     57       N  
ATOM   3965  CA  PRO B 448      51.021  22.540  -8.737  1.00 10.66           C  
ANISOU 3965  CA  PRO B 448     1560   1033   1457    291     76    109       C  
ATOM   3966  C   PRO B 448      51.671  21.188  -9.020  1.00  9.85           C  
ANISOU 3966  C   PRO B 448     1247    898   1596    136    -81    -94       C  
ATOM   3967  O   PRO B 448      52.899  21.101  -9.090  1.00 10.88           O  
ANISOU 3967  O   PRO B 448     1219   1145   1770     95     -1    -48       O  
ATOM   3968  CB  PRO B 448      51.016  23.384 -10.006  1.00 11.35           C  
ANISOU 3968  CB  PRO B 448     1659   1198   1453     46     61    258       C  
ATOM   3969  CG  PRO B 448      52.389  24.025 -10.000  1.00 12.47           C  
ANISOU 3969  CG  PRO B 448     1664   1249   1823    115    164     74       C  
ATOM   3970  CD  PRO B 448      52.743  24.254  -8.542  1.00 11.39           C  
ANISOU 3970  CD  PRO B 448     1811   1178   1338     63    310     92       C  
ATOM   3971  N   CYS B 449      50.858  20.148  -9.158  1.00  9.77           N  
ANISOU 3971  N   CYS B 449     1257    864   1591    431     71    -92       N  
ATOM   3972  CA  CYS B 449      51.359  18.842  -9.606  1.00 10.13           C  
ANISOU 3972  CA  CYS B 449     1359    824   1666    304    -43    101       C  
ATOM   3973  C   CYS B 449      50.359  18.215 -10.574  1.00  9.62           C  
ANISOU 3973  C   CYS B 449     1252   1112   1289    -15    141   -118       C  
ATOM   3974  O   CYS B 449      49.209  18.647 -10.648  1.00 11.15           O  
ANISOU 3974  O   CYS B 449     1310   1276   1651    442    111     34       O  
ATOM   3975  CB  CYS B 449      51.633  17.913  -8.412  1.00 10.60           C  
ANISOU 3975  CB  CYS B 449     1262   1051   1714    261    159    312       C  
ATOM   3976  SG  CYS B 449      50.174  17.283  -7.563  1.00 10.40           S  
ANISOU 3976  SG  CYS B 449     1263   1155   1534    225    -68     86       S  
ATOM   3977  N   THR B 450      50.782  17.198 -11.318  1.00  9.27           N  
ANISOU 3977  N   THR B 450     1543    932   1045    242    127   -137       N  
ATOM   3978  CA  THR B 450      49.897  16.613 -12.323  1.00 10.48           C  
ANISOU 3978  CA  THR B 450     1581   1271   1131    201     65   -133       C  
ATOM   3979  C   THR B 450      49.117  15.366 -11.865  1.00  9.61           C  
ANISOU 3979  C   THR B 450     1479   1019   1151    212    -18    -11       C  
ATOM   3980  O   THR B 450      48.191  14.931 -12.544  1.00 11.89           O  
ANISOU 3980  O   THR B 450     1810   1208   1500     43   -492     28       O  
ATOM   3981  CB  THR B 450      50.617  16.390 -13.681  1.00 11.68           C  
ANISOU 3981  CB  THR B 450     1481   1389   1566    379     -3   -150       C  
ATOM   3982  OG1 THR B 450      51.932  15.872 -13.452  1.00 12.34           O  
ANISOU 3982  OG1 THR B 450     1412   1638   1637    448     54   -358       O  
ATOM   3983  CG2 THR B 450      50.750  17.718 -14.431  1.00 13.61           C  
ANISOU 3983  CG2 THR B 450     1585   1503   2084    426    235    408       C  
ATOM   3984  N   LEU B 451      49.467  14.817 -10.702  1.00 10.19           N  
ANISOU 3984  N   LEU B 451     1377   1147   1347    -13     94    164       N  
ATOM   3985  CA  LEU B 451      48.698  13.720 -10.096  1.00 10.05           C  
ANISOU 3985  CA  LEU B 451     1499    928   1390    191    158    178       C  
ATOM   3986  C   LEU B 451      48.834  13.739  -8.590  1.00 10.42           C  
ANISOU 3986  C   LEU B 451     1411   1092   1454     66    -51    195       C  
ATOM   3987  O   LEU B 451      49.916  13.987  -8.074  1.00 11.18           O  
ANISOU 3987  O   LEU B 451     1318   1260   1670     45   -173     89       O  
ATOM   3988  CB  LEU B 451      49.212  12.349 -10.558  1.00 12.33           C  
ANISOU 3988  CB  LEU B 451     1622   1181   1881    227    -60   -148       C  
ATOM   3989  CG  LEU B 451      48.824  11.781 -11.918  1.00 15.58           C  
ANISOU 3989  CG  LEU B 451     1909   1491   2519    407   -683   -452       C  
ATOM   3990  CD1 LEU B 451      49.479  10.406 -12.092  1.00 17.85           C  
ANISOU 3990  CD1 LEU B 451     2122   1441   3218    596   -620   -678       C  
ATOM   3991  CD2 LEU B 451      47.305  11.694 -12.077  1.00 14.97           C  
ANISOU 3991  CD2 LEU B 451     1688   1727   2273    -42   -767   -243       C  
ATOM   3992  N   PRO B 452      47.749  13.418  -7.876  1.00 10.31           N  
ANISOU 3992  N   PRO B 452     1143   1288   1486     76   -182    148       N  
ATOM   3993  CA  PRO B 452      47.900  13.192  -6.433  1.00 11.46           C  
ANISOU 3993  CA  PRO B 452     1127   1676   1552    386   -219    646       C  
ATOM   3994  C   PRO B 452      48.798  11.983  -6.179  1.00  9.16           C  
ANISOU 3994  C   PRO B 452      950   1188   1340    102    -86    336       C  
ATOM   3995  O   PRO B 452      48.785  11.031  -6.964  1.00 10.06           O  
ANISOU 3995  O   PRO B 452     1130   1084   1608     84    -22     25       O  
ATOM   3996  CB  PRO B 452      46.471  12.881  -5.968  1.00 12.98           C  
ANISOU 3996  CB  PRO B 452     1130   1939   1862    603    -21    425       C  
ATOM   3997  CG  PRO B 452      45.578  13.434  -7.075  1.00 13.28           C  
ANISOU 3997  CG  PRO B 452     1272   2088   1685    636     76    683       C  
ATOM   3998  CD  PRO B 452      46.361  13.225  -8.333  1.00 11.97           C  
ANISOU 3998  CD  PRO B 452      952   2087   1509    324    218    232       C  
ATOM   3999  N   GLN B 453      49.556  12.014  -5.094  1.00  9.02           N  
ANISOU 3999  N   GLN B 453      818   1165   1445    204    -99    227       N  
ATOM   4000  CA  GLN B 453      50.495  10.932  -4.835  1.00  8.62           C  
ANISOU 4000  CA  GLN B 453      791    965   1517    164   -283     85       C  
ATOM   4001  C   GLN B 453      49.783   9.585  -4.729  1.00  9.12           C  
ANISOU 4001  C   GLN B 453      856   1062   1546     20   -155     64       C  
ATOM   4002  O   GLN B 453      50.291   8.570  -5.201  1.00 10.44           O  
ANISOU 4002  O   GLN B 453     1295    997   1673    194   -164   -141       O  
ATOM   4003  CB  GLN B 453      51.328  11.191  -3.577  1.00  8.72           C  
ANISOU 4003  CB  GLN B 453      962   1073   1276    297   -115    106       C  
ATOM   4004  CG  GLN B 453      52.358  10.094  -3.315  1.00  9.53           C  
ANISOU 4004  CG  GLN B 453      973   1189   1460    317   -160    145       C  
ATOM   4005  CD  GLN B 453      53.383   9.994  -4.430  1.00 10.46           C  
ANISOU 4005  CD  GLN B 453     1193   1197   1585    211     95     51       C  
ATOM   4006  OE1 GLN B 453      53.679  10.984  -5.100  1.00 11.05           O  
ANISOU 4006  OE1 GLN B 453     1154   1286   1756    131      2    168       O  
ATOM   4007  NE2 GLN B 453      53.935   8.797  -4.632  1.00 11.53           N  
ANISOU 4007  NE2 GLN B 453     1418   1084   1878    310   -275      3       N  
ATOM   4008  N   GLU B 454      48.612   9.572  -4.101  1.00  9.87           N  
ANISOU 4008  N   GLU B 454     1080    998   1672   -128   -196    265       N  
ATOM   4009  CA  GLU B 454      47.905   8.314  -3.892  1.00  9.42           C  
ANISOU 4009  CA  GLU B 454     1250   1351    979    -48     56    155       C  
ATOM   4010  C   GLU B 454      47.379   7.703  -5.199  1.00  9.39           C  
ANISOU 4010  C   GLU B 454     1312   1142   1114      6   -136     45       C  
ATOM   4011  O   GLU B 454      47.155   6.501  -5.265  1.00 11.38           O  
ANISOU 4011  O   GLU B 454     1327   1100   1895   -148   -175   -108       O  
ATOM   4012  CB  GLU B 454      46.814   8.447  -2.823  1.00 10.83           C  
ANISOU 4012  CB  GLU B 454     1452   1380   1282   -313     22   -103       C  
ATOM   4013  CG  GLU B 454      47.357   8.556  -1.382  1.00 11.78           C  
ANISOU 4013  CG  GLU B 454     1769   1166   1539   -336    -55   -181       C  
ATOM   4014  CD  GLU B 454      47.913   9.943  -1.026  1.00 10.83           C  
ANISOU 4014  CD  GLU B 454     1376   1411   1328   -204   -134    -90       C  
ATOM   4015  OE1 GLU B 454      47.753  10.897  -1.813  1.00 11.17           O  
ANISOU 4015  OE1 GLU B 454     1541   1262   1442    -72    -65     46       O  
ATOM   4016  OE2 GLU B 454      48.507  10.082   0.062  1.00 12.13           O  
ANISOU 4016  OE2 GLU B 454     1686   1320   1603     97    -84   -222       O  
ATOM   4017  N   PHE B 455      47.209   8.512  -6.240  1.00 10.60           N  
ANISOU 4017  N   PHE B 455     1395   1447   1184    163   -235    109       N  
ATOM   4018  CA  PHE B 455      46.944   7.962  -7.568  1.00 10.95           C  
ANISOU 4018  CA  PHE B 455     1363   1453   1345    177   -221    188       C  
ATOM   4019  C   PHE B 455      48.154   7.151  -8.026  1.00 10.64           C  
ANISOU 4019  C   PHE B 455     1166   1385   1491   -200   -417     16       C  
ATOM   4020  O   PHE B 455      48.000   6.086  -8.625  1.00 11.62           O  
ANISOU 4020  O   PHE B 455     1506   1123   1787   -281   -271    -95       O  
ATOM   4021  CB  PHE B 455      46.701   9.068  -8.596  1.00 11.68           C  
ANISOU 4021  CB  PHE B 455     1345   1553   1541     92   -184    324       C  
ATOM   4022  CG  PHE B 455      45.262   9.500  -8.725  1.00 11.53           C  
ANISOU 4022  CG  PHE B 455     1440   1487   1455    -94   -214     87       C  
ATOM   4023  CD1 PHE B 455      44.553   9.965  -7.628  1.00 14.34           C  
ANISOU 4023  CD1 PHE B 455     1312   2156   1980    119   -169    220       C  
ATOM   4024  CD2 PHE B 455      44.637   9.492  -9.963  1.00 13.18           C  
ANISOU 4024  CD2 PHE B 455     1446   1673   1888    -83   -510    189       C  
ATOM   4025  CE1 PHE B 455      43.242  10.387  -7.759  1.00 15.55           C  
ANISOU 4025  CE1 PHE B 455     1532   2302   2075    152   -371     43       C  
ATOM   4026  CE2 PHE B 455      43.330   9.923 -10.104  1.00 14.86           C  
ANISOU 4026  CE2 PHE B 455     1651   1746   2247    -33   -274    -21       C  
ATOM   4027  CZ  PHE B 455      42.631  10.371  -9.004  1.00 15.06           C  
ANISOU 4027  CZ  PHE B 455     1541   1968   2212     98   -220     75       C  
ATOM   4028  N   VAL B 456      49.356   7.662  -7.763  1.00 11.56           N  
ANISOU 4028  N   VAL B 456     1137   1716   1540   -101    113    -10       N  
ATOM   4029  CA  VAL B 456      50.579   6.984  -8.181  1.00 11.92           C  
ANISOU 4029  CA  VAL B 456     1158   1672   1697   -531     62   -174       C  
ATOM   4030  C   VAL B 456      50.672   5.597  -7.553  1.00 10.73           C  
ANISOU 4030  C   VAL B 456     1239   1490   1348   -229     70    -59       C  
ATOM   4031  O   VAL B 456      50.870   4.600  -8.259  1.00 12.83           O  
ANISOU 4031  O   VAL B 456     1585   1503   1787    -26     25   -499       O  
ATOM   4032  CB  VAL B 456      51.852   7.783  -7.808  1.00 13.28           C  
ANISOU 4032  CB  VAL B 456     1399   1726   1920   -394    176   -349       C  
ATOM   4033  CG1 VAL B 456      53.109   6.993  -8.172  1.00 14.34           C  
ANISOU 4033  CG1 VAL B 456     1254   1926   2267   -477    251   -444       C  
ATOM   4034  CG2 VAL B 456      51.861   9.139  -8.505  1.00 14.10           C  
ANISOU 4034  CG2 VAL B 456     1736   1671   1951   -338      7   -169       C  
ATOM   4035  N   SER B 457      50.537   5.524  -6.230  1.00 11.54           N  
ANISOU 4035  N   SER B 457     1337   1356   1692    -46   -125    -75       N  
ATOM   4036  CA  SER B 457      50.646   4.233  -5.554  1.00 11.61           C  
ANISOU 4036  CA  SER B 457     1340   1409   1661   -156   -253    -69       C  
ATOM   4037  C   SER B 457      49.500   3.312  -5.960  1.00 12.60           C  
ANISOU 4037  C   SER B 457     1348   1676   1761    155   -268    -83       C  
ATOM   4038  O   SER B 457      49.674   2.104  -6.047  1.00 13.43           O  
ANISOU 4038  O   SER B 457     1671   1485   1946    192   -358   -125       O  
ATOM   4039  CB  SER B 457      50.712   4.384  -4.030  1.00 12.94           C  
ANISOU 4039  CB  SER B 457     1533   1567   1815    -32   -365   -208       C  
ATOM   4040  OG  SER B 457      49.660   5.190  -3.526  1.00 12.70           O  
ANISOU 4040  OG  SER B 457     1460   1481   1882    294    -42      8       O  
ATOM   4041  N   HIS B 458      48.329   3.888  -6.211  1.00 11.28           N  
ANISOU 4041  N   HIS B 458     1266   1351   1670   -132    -77    -20       N  
ATOM   4042  CA  HIS B 458      47.194   3.101  -6.669  1.00 11.27           C  
ANISOU 4042  CA  HIS B 458     1281   1485   1517    -37   -123    -61       C  
ATOM   4043  C   HIS B 458      47.519   2.412  -7.997  1.00 11.97           C  
ANISOU 4043  C   HIS B 458     1611   1155   1783   -146   -362     16       C  
ATOM   4044  O   HIS B 458      47.313   1.206  -8.148  1.00 13.37           O  
ANISOU 4044  O   HIS B 458     1796   1221   2062   -200   -491   -232       O  
ATOM   4045  CB  HIS B 458      45.951   3.987  -6.813  1.00 11.60           C  
ANISOU 4045  CB  HIS B 458      961   1403   2043   -457   -381    318       C  
ATOM   4046  CG  HIS B 458      44.695   3.226  -7.100  1.00 13.19           C  
ANISOU 4046  CG  HIS B 458     1208   1577   2227   -648   -393    364       C  
ATOM   4047  ND1 HIS B 458      44.001   2.544  -6.125  1.00 18.10           N  
ANISOU 4047  ND1 HIS B 458     1600   2403   2875   -863   -482    892       N  
ATOM   4048  CD2 HIS B 458      44.006   3.044  -8.252  1.00 14.65           C  
ANISOU 4048  CD2 HIS B 458     1338   1873   2355   -459   -740    134       C  
ATOM   4049  CE1 HIS B 458      42.936   1.976  -6.662  1.00 18.77           C  
ANISOU 4049  CE1 HIS B 458     1740   2382   3008   -617   -624    692       C  
ATOM   4050  NE2 HIS B 458      42.918   2.258  -7.952  1.00 15.76           N  
ANISOU 4050  NE2 HIS B 458     1587   2018   2384   -415   -514    473       N  
ATOM   4051  N   PHE B 459      48.036   3.166  -8.962  1.00 11.72           N  
ANISOU 4051  N   PHE B 459     1582   1377   1494   -151   -230     -9       N  
ATOM   4052  CA  PHE B 459      48.334   2.583 -10.274  1.00 12.52           C  
ANISOU 4052  CA  PHE B 459     1795   1446   1517     -8   -290     21       C  
ATOM   4053  C   PHE B 459      49.482   1.568 -10.190  1.00 13.22           C  
ANISOU 4053  C   PHE B 459     1714   1380   1929   -228   -270   -149       C  
ATOM   4054  O   PHE B 459      49.451   0.536 -10.856  1.00 14.77           O  
ANISOU 4054  O   PHE B 459     2121   1382   2107   -109   -320   -492       O  
ATOM   4055  CB  PHE B 459      48.655   3.670 -11.304  1.00 12.88           C  
ANISOU 4055  CB  PHE B 459     1654   1476   1764   -270   -329     67       C  
ATOM   4056  CG  PHE B 459      47.531   4.640 -11.545  1.00 12.40           C  
ANISOU 4056  CG  PHE B 459     1683   1525   1504   -168   -264    135       C  
ATOM   4057  CD1 PHE B 459      46.213   4.266 -11.331  1.00 13.81           C  
ANISOU 4057  CD1 PHE B 459     1649   1648   1951   -230   -281     66       C  
ATOM   4058  CD2 PHE B 459      47.797   5.931 -11.988  1.00 13.13           C  
ANISOU 4058  CD2 PHE B 459     1941   1508   1540    -48   -286     19       C  
ATOM   4059  CE1 PHE B 459      45.175   5.160 -11.559  1.00 14.16           C  
ANISOU 4059  CE1 PHE B 459     1935   1366   2079   -159   -192     11       C  
ATOM   4060  CE2 PHE B 459      46.772   6.832 -12.217  1.00 13.68           C  
ANISOU 4060  CE2 PHE B 459     1796   1643   1758   -211    -82     11       C  
ATOM   4061  CZ  PHE B 459      45.452   6.444 -12.001  1.00 14.67           C  
ANISOU 4061  CZ  PHE B 459     1789   1817   1969   -410   -172    -69       C  
ATOM   4062  N   VAL B 460      50.491   1.861  -9.373  1.00 13.09           N  
ANISOU 4062  N   VAL B 460     1402   1594   1978   -174   -316   -165       N  
ATOM   4063  CA  VAL B 460      51.587   0.922  -9.176  1.00 14.63           C  
ANISOU 4063  CA  VAL B 460     1633   1602   2323    -91   -606   -165       C  
ATOM   4064  C   VAL B 460      51.048  -0.376  -8.584  1.00 15.50           C  
ANISOU 4064  C   VAL B 460     1993   1651   2243    114   -370   -175       C  
ATOM   4065  O   VAL B 460      51.432  -1.471  -8.999  1.00 17.55           O  
ANISOU 4065  O   VAL B 460     2361   1522   2786    126   -497   -428       O  
ATOM   4066  CB  VAL B 460      52.689   1.500  -8.264  1.00 15.12           C  
ANISOU 4066  CB  VAL B 460     1657   1320   2766     19   -677   -295       C  
ATOM   4067  CG1 VAL B 460      53.687   0.411  -7.896  1.00 18.41           C  
ANISOU 4067  CG1 VAL B 460     1864   1629   3500    393   -691   -110       C  
ATOM   4068  CG2 VAL B 460      53.386   2.679  -8.951  1.00 15.52           C  
ANISOU 4068  CG2 VAL B 460     1769   1636   2491    127   -313     40       C  
ATOM   4069  N   ASN B 461      50.137  -0.250  -7.627  1.00 14.54           N  
ANISOU 4069  N   ASN B 461     2051   1361   2113   -327   -490     68       N  
ATOM   4070  CA  ASN B 461      49.529  -1.420  -7.002  1.00 14.50           C  
ANISOU 4070  CA  ASN B 461     2071   1581   1855   -498   -468    203       C  
ATOM   4071  C   ASN B 461      48.699  -2.259  -7.980  1.00 16.37           C  
ANISOU 4071  C   ASN B 461     2325   1380   2514   -124   -743   -130       C  
ATOM   4072  O   ASN B 461      48.809  -3.485  -8.013  1.00 18.54           O  
ANISOU 4072  O   ASN B 461     2687   1371   2987    173   -991   -320       O  
ATOM   4073  CB  ASN B 461      48.649  -0.998  -5.831  1.00 15.73           C  
ANISOU 4073  CB  ASN B 461     2436   1629   1912   -472   -366    451       C  
ATOM   4074  CG  ASN B 461      48.263  -2.165  -4.958  1.00 18.06           C  
ANISOU 4074  CG  ASN B 461     2644   1827   2392   -555   -364    300       C  
ATOM   4075  OD1 ASN B 461      49.030  -2.574  -4.092  1.00 19.77           O  
ANISOU 4075  OD1 ASN B 461     2808   2093   2611   -476   -865    482       O  
ATOM   4076  ND2 ASN B 461      47.080  -2.722  -5.190  1.00 20.31           N  
ANISOU 4076  ND2 ASN B 461     2709   2180   2829   -509   -430    144       N  
ATOM   4077  N   GLU B 462      47.870  -1.591  -8.778  1.00 15.22           N  
ANISOU 4077  N   GLU B 462     2340   1092   2349   -274   -651    -33       N  
ATOM   4078  CA  GLU B 462      46.916  -2.276  -9.642  1.00 16.51           C  
ANISOU 4078  CA  GLU B 462     2374   1516   2382   -312   -969   -131       C  
ATOM   4079  C   GLU B 462      47.544  -2.863 -10.900  1.00 16.88           C  
ANISOU 4079  C   GLU B 462     2573   1633   2207   -184   -691   -143       C  
ATOM   4080  O   GLU B 462      47.191  -3.969 -11.310  1.00 17.79           O  
ANISOU 4080  O   GLU B 462     2957   1460   2340     85   -741   -250       O  
ATOM   4081  CB  GLU B 462      45.792  -1.318 -10.037  1.00 17.08           C  
ANISOU 4081  CB  GLU B 462     2465   1774   2250   -279   -993     -6       C  
ATOM   4082  CG  GLU B 462      44.969  -0.834  -8.870  1.00 19.63           C  
ANISOU 4082  CG  GLU B 462     2857   2043   2559   -420   -672    285       C  
ATOM   4083  CD  GLU B 462      44.320  -1.978  -8.135  1.00 22.65           C  
ANISOU 4083  CD  GLU B 462     3047   2615   2945   -490   -954    269       C  
ATOM   4084  OE1 GLU B 462      43.304  -2.509  -8.631  1.00 23.97           O  
ANISOU 4084  OE1 GLU B 462     3168   2456   3481   -636   -808    407       O  
ATOM   4085  OE2 GLU B 462      44.841  -2.366  -7.072  1.00 25.26           O  
ANISOU 4085  OE2 GLU B 462     3092   3128   3378   -602  -1037    719       O  
ATOM   4086  N   GLN B 463      48.453  -2.120 -11.526  1.00 17.03           N  
ANISOU 4086  N   GLN B 463     2671   1465   2333   -434   -700   -222       N  
ATOM   4087  CA  GLN B 463      49.037  -2.558 -12.792  1.00 19.85           C  
ANISOU 4087  CA  GLN B 463     2969   2165   2409   -200   -713   -715       C  
ATOM   4088  C   GLN B 463      47.943  -2.942 -13.780  1.00 19.32           C  
ANISOU 4088  C   GLN B 463     2998   1774   2569   -197   -770   -164       C  
ATOM   4089  O   GLN B 463      48.059  -3.943 -14.485  1.00 20.94           O  
ANISOU 4089  O   GLN B 463     3140   1954   2863    -46   -778   -625       O  
ATOM   4090  CB  GLN B 463      49.960  -3.760 -12.570  1.00 22.57           C  
ANISOU 4090  CB  GLN B 463     3178   2539   2858   -358   -832   -925       C  
ATOM   4091  CG  GLN B 463      51.097  -3.512 -11.591  1.00 27.07           C  
ANISOU 4091  CG  GLN B 463     3593   3209   3481   -228   -538   -898       C  
ATOM   4092  CD  GLN B 463      52.269  -2.815 -12.238  1.00 29.91           C  
ANISOU 4092  CD  GLN B 463     3918   3416   4028    -77   -392  -1014       C  
ATOM   4093  OE1 GLN B 463      52.841  -3.312 -13.208  1.00 32.18           O  
ANISOU 4093  OE1 GLN B 463     3995   3772   4459    -74   -345  -1345       O  
ATOM   4094  NE2 GLN B 463      52.631  -1.652 -11.709  1.00 29.99           N  
ANISOU 4094  NE2 GLN B 463     4048   3276   4070     84   -256   -379       N  
ATOM   4095  N   ALA B 464      46.875  -2.152 -13.823  1.00 18.07           N  
ANISOU 4095  N   ALA B 464     2878   1572   2415   -202  -1085     28       N  
ATOM   4096  CA  ALA B 464      45.741  -2.449 -14.691  1.00 18.22           C  
ANISOU 4096  CA  ALA B 464     3088   1591   2243   -159   -984   -166       C  
ATOM   4097  C   ALA B 464      46.087  -2.147 -16.140  1.00 19.23           C  
ANISOU 4097  C   ALA B 464     3394   1607   2303    -96   -978   -239       C  
ATOM   4098  O   ALA B 464      46.540  -1.049 -16.449  1.00 19.11           O  
ANISOU 4098  O   ALA B 464     3177   1712   2371   -391   -791   -209       O  
ATOM   4099  CB  ALA B 464      44.521  -1.646 -14.261  1.00 19.38           C  
ANISOU 4099  CB  ALA B 464     2993   1767   2603   -152   -879   -148       C  
ATOM   4100  N   PRO B 465      45.879  -3.120 -17.039  1.00 20.43           N  
ANISOU 4100  N   PRO B 465     3835   1458   2470    -46   -965   -307       N  
ATOM   4101  CA  PRO B 465      46.165  -2.826 -18.446  1.00 20.71           C  
ANISOU 4101  CA  PRO B 465     3807   1663   2399   -133  -1028   -626       C  
ATOM   4102  C   PRO B 465      45.368  -1.627 -18.956  1.00 20.72           C  
ANISOU 4102  C   PRO B 465     3597   1728   2547   -319   -948   -404       C  
ATOM   4103  O   PRO B 465      44.184  -1.467 -18.635  1.00 21.58           O  
ANISOU 4103  O   PRO B 465     3458   2048   2691   -274  -1035   -180       O  
ATOM   4104  CB  PRO B 465      45.723  -4.103 -19.166  1.00 23.57           C  
ANISOU 4104  CB  PRO B 465     4237   1935   2782    106  -1350   -763       C  
ATOM   4105  CG  PRO B 465      45.865  -5.171 -18.140  1.00 24.51           C  
ANISOU 4105  CG  PRO B 465     4402   1817   3092     96  -1018   -456       C  
ATOM   4106  CD  PRO B 465      45.498  -4.529 -16.832  1.00 21.88           C  
ANISOU 4106  CD  PRO B 465     4146   1598   2570    -41   -849   -686       C  
ATOM   4107  N   THR B 466      46.029  -0.787 -19.744  1.00 20.47           N  
ANISOU 4107  N   THR B 466     3470   1854   2454   -386   -897   -226       N  
ATOM   4108  CA  THR B 466      45.390   0.385 -20.332  1.00 20.14           C  
ANISOU 4108  CA  THR B 466     3260   2211   2181   -497  -1034   -202       C  
ATOM   4109  C   THR B 466      44.646  -0.022 -21.604  1.00 21.70           C  
ANISOU 4109  C   THR B 466     3579   2723   1942   -538  -1140   -248       C  
ATOM   4110  O   THR B 466      45.263  -0.343 -22.621  1.00 25.93           O  
ANISOU 4110  O   THR B 466     3771   3670   2412   -257   -867   -647       O  
ATOM   4111  CB  THR B 466      46.436   1.468 -20.640  1.00 20.24           C  
ANISOU 4111  CB  THR B 466     3025   2093   2571   -503   -875     11       C  
ATOM   4112  OG1 THR B 466      47.172   1.755 -19.446  1.00 20.48           O  
ANISOU 4112  OG1 THR B 466     2832   2155   2795   -396   -919   -353       O  
ATOM   4113  CG2 THR B 466      45.770   2.753 -21.137  1.00 20.80           C  
ANISOU 4113  CG2 THR B 466     2893   1929   3079   -633   -790    469       C  
ATOM   4114  N   ARG B 467      43.317  -0.014 -21.540  1.00 23.56           N  
ANISOU 4114  N   ARG B 467     3768   2888   2296   -326  -1373   -276       N  
ATOM   4115  CA  ARG B 467      42.503  -0.605 -22.603  1.00 24.53           C  
ANISOU 4115  CA  ARG B 467     3918   3033   2367   -646  -1499   -260       C  
ATOM   4116  C   ARG B 467      41.875   0.411 -23.556  1.00 24.73           C  
ANISOU 4116  C   ARG B 467     3951   2942   2504   -537  -1600   -176       C  
ATOM   4117  O   ARG B 467      41.106   0.045 -24.446  1.00 28.94           O  
ANISOU 4117  O   ARG B 467     4231   3431   3334   -534  -1816   -241       O  
ATOM   4118  CB  ARG B 467      41.419  -1.510 -22.010  1.00 28.21           C  
ANISOU 4118  CB  ARG B 467     4355   3478   2884   -985  -1682   -190       C  
ATOM   4119  CG  ARG B 467      41.961  -2.644 -21.153  1.00 32.49           C  
ANISOU 4119  CG  ARG B 467     4857   4077   3410   -930  -1980      2       C  
ATOM   4120  CD  ARG B 467      40.881  -3.662 -20.820  1.00 40.46           C  
ANISOU 4120  CD  ARG B 467     5494   4934   4944   -385  -1425    236       C  
ATOM   4121  NE  ARG B 467      41.261  -4.521 -19.701  1.00 46.74           N  
ANISOU 4121  NE  ARG B 467     6037   5655   6066    125   -934    242       N  
ATOM   4122  CZ  ARG B 467      42.055  -5.583 -19.804  1.00 51.14           C  
ANISOU 4122  CZ  ARG B 467     6397   6314   6719    545   -629    279       C  
ATOM   4123  NH1 ARG B 467      42.565  -5.923 -20.981  1.00 53.17           N  
ANISOU 4123  NH1 ARG B 467     6533   6570   7099    781   -425    295       N  
ATOM   4124  NH2 ARG B 467      42.342  -6.303 -18.729  1.00 52.28           N  
ANISOU 4124  NH2 ARG B 467     6529   6572   6763    675   -639    197       N  
ATOM   4125  N   GLY B 468      42.203   1.682 -23.370  1.00 23.54           N  
ANISOU 4125  N   GLY B 468     3696   2724   2523   -540  -1221    279       N  
ATOM   4126  CA  GLY B 468      41.735   2.723 -24.268  1.00 22.83           C  
ANISOU 4126  CA  GLY B 468     3585   2678   2409   -402  -1103     60       C  
ATOM   4127  C   GLY B 468      42.736   3.857 -24.313  1.00 21.98           C  
ANISOU 4127  C   GLY B 468     3497   2644   2210    -54  -1046      7       C  
ATOM   4128  O   GLY B 468      43.719   3.857 -23.570  1.00 22.38           O  
ANISOU 4128  O   GLY B 468     3374   2646   2484    -17   -920   -179       O  
ATOM   4129  N   ASP B 469      42.493   4.833 -25.176  1.00 23.19           N  
ANISOU 4129  N   ASP B 469     3587   2644   2580     77   -692     21       N  
ATOM   4130  CA  ASP B 469      43.423   5.943 -25.317  1.00 24.05           C  
ANISOU 4130  CA  ASP B 469     3768   2745   2625    313   -471    261       C  
ATOM   4131  C   ASP B 469      43.211   7.010 -24.250  1.00 21.77           C  
ANISOU 4131  C   ASP B 469     3169   2603   2497    115   -345   -137       C  
ATOM   4132  O   ASP B 469      44.053   7.884 -24.060  1.00 22.65           O  
ANISOU 4132  O   ASP B 469     3003   2650   2952   -166   -333   -400       O  
ATOM   4133  CB  ASP B 469      43.352   6.527 -26.725  1.00 29.11           C  
ANISOU 4133  CB  ASP B 469     4453   3085   3520    647    -97    243       C  
ATOM   4134  CG  ASP B 469      43.928   5.581 -27.766  1.00 35.20           C  
ANISOU 4134  CG  ASP B 469     5044   3901   4427   1142    173     77       C  
ATOM   4135  OD1 ASP B 469      44.898   4.858 -27.440  1.00 37.32           O  
ANISOU 4135  OD1 ASP B 469     5314   4137   4727   1251    332    165       O  
ATOM   4136  OD2 ASP B 469      43.411   5.545 -28.899  1.00 38.10           O  
ANISOU 4136  OD2 ASP B 469     5228   4162   5085   1151     70   -450       O  
ATOM   4137  N   ALA B 470      42.087   6.928 -23.546  1.00 18.07           N  
ANISOU 4137  N   ALA B 470     2598   2227   2041   -183   -460   -297       N  
ATOM   4138  CA  ALA B 470      41.833   7.831 -22.430  1.00 18.94           C  
ANISOU 4138  CA  ALA B 470     2350   2244   2601   -287   -513   -228       C  
ATOM   4139  C   ALA B 470      40.814   7.234 -21.480  1.00 18.36           C  
ANISOU 4139  C   ALA B 470     2227   2343   2406   -259   -673    -92       C  
ATOM   4140  O   ALA B 470      39.986   6.412 -21.877  1.00 19.51           O  
ANISOU 4140  O   ALA B 470     2428   2307   2676   -358   -954    -31       O  
ATOM   4141  CB  ALA B 470      41.367   9.199 -22.925  1.00 19.26           C  
ANISOU 4141  CB  ALA B 470     2330   2235   2754   -298   -322   -139       C  
ATOM   4142  N   ALA B 471      40.887   7.650 -20.221  1.00 17.69           N  
ANISOU 4142  N   ALA B 471     1858   2320   2541   -378   -237    -93       N  
ATOM   4143  CA  ALA B 471      39.946   7.206 -19.202  1.00 17.76           C  
ANISOU 4143  CA  ALA B 471     1936   2128   2682   -193   -224    -73       C  
ATOM   4144  C   ALA B 471      39.023   8.348 -18.809  1.00 17.59           C  
ANISOU 4144  C   ALA B 471     1850   2181   2652   -145    -95     18       C  
ATOM   4145  O   ALA B 471      39.482   9.415 -18.394  1.00 18.37           O  
ANISOU 4145  O   ALA B 471     1895   1955   3128   -109   -209   -184       O  
ATOM   4146  CB  ALA B 471      40.686   6.685 -17.986  1.00 18.25           C  
ANISOU 4146  CB  ALA B 471     2127   1835   2970   -148   -153     98       C  
ATOM   4147  N   LEU B 472      37.722   8.121 -18.949  1.00 16.39           N  
ANISOU 4147  N   LEU B 472     1960   2502   1763     84    -76    220       N  
ATOM   4148  CA  LEU B 472      36.732   9.104 -18.548  1.00 16.39           C  
ANISOU 4148  CA  LEU B 472     1789   2517   1922   -316   -518     97       C  
ATOM   4149  C   LEU B 472      36.484   8.981 -17.053  1.00 16.07           C  
ANISOU 4149  C   LEU B 472     1764   2447   1895   -259   -207    121       C  
ATOM   4150  O   LEU B 472      36.154   7.898 -16.560  1.00 17.55           O  
ANISOU 4150  O   LEU B 472     2065   2404   2199   -340   -352    345       O  
ATOM   4151  CB  LEU B 472      35.428   8.893 -19.312  1.00 17.81           C  
ANISOU 4151  CB  LEU B 472     1673   2681   2412   -495   -638     10       C  
ATOM   4152  CG  LEU B 472      34.244   9.766 -18.906  1.00 20.12           C  
ANISOU 4152  CG  LEU B 472     1984   2889   2772    -99   -764    191       C  
ATOM   4153  CD1 LEU B 472      34.540  11.232 -19.188  1.00 21.51           C  
ANISOU 4153  CD1 LEU B 472     2166   2870   3136    148  -1053     26       C  
ATOM   4154  CD2 LEU B 472      32.983   9.321 -19.636  1.00 20.89           C  
ANISOU 4154  CD2 LEU B 472     1992   2962   2982   -192  -1105    270       C  
ATOM   4155  N   LEU B 473      36.650  10.091 -16.339  1.00 15.54           N  
ANISOU 4155  N   LEU B 473     1639   2390   1873    -27    -82    175       N  
ATOM   4156  CA  LEU B 473      36.390  10.137 -14.904  1.00 16.27           C  
ANISOU 4156  CA  LEU B 473     1628   2439   2115    145   -181   -100       C  
ATOM   4157  C   LEU B 473      35.243  11.086 -14.601  1.00 17.97           C  
ANISOU 4157  C   LEU B 473     1661   2863   2304    318   -251    125       C  
ATOM   4158  O   LEU B 473      35.051  12.086 -15.298  1.00 18.38           O  
ANISOU 4158  O   LEU B 473     1803   2959   2222    312   -339    406       O  
ATOM   4159  CB  LEU B 473      37.626  10.623 -14.134  1.00 15.91           C  
ANISOU 4159  CB  LEU B 473     1664   2313   2067    196   -470     -4       C  
ATOM   4160  CG  LEU B 473      38.977   9.948 -14.345  1.00 16.59           C  
ANISOU 4160  CG  LEU B 473     1689   2115   2497    161   -637    169       C  
ATOM   4161  CD1 LEU B 473      39.998  10.572 -13.411  1.00 16.30           C  
ANISOU 4161  CD1 LEU B 473     1840   2099   2254    -51   -693    -92       C  
ATOM   4162  CD2 LEU B 473      38.895   8.444 -14.109  1.00 18.27           C  
ANISOU 4162  CD2 LEU B 473     1991   1748   3201    -15   -428    266       C  
ATOM   4163  N   HIS B 474      34.481  10.764 -13.563  1.00 17.67           N  
ANISOU 4163  N   HIS B 474     1478   3035   2201    183   -135    -52       N  
ATOM   4164  CA  HIS B 474      33.586  11.728 -12.944  1.00 18.18           C  
ANISOU 4164  CA  HIS B 474     1216   3298   2394   -208   -279    136       C  
ATOM   4165  C   HIS B 474      34.161  12.160 -11.599  1.00 18.20           C  
ANISOU 4165  C   HIS B 474     1415   3256   2242    214   -387    154       C  
ATOM   4166  O   HIS B 474      34.771  11.359 -10.897  1.00 20.24           O  
ANISOU 4166  O   HIS B 474     2034   3268   2387    755   -521    337       O  
ATOM   4167  CB  HIS B 474      32.202  11.119 -12.723  1.00 19.88           C  
ANISOU 4167  CB  HIS B 474     1242   3712   2598   -297   -580    374       C  
ATOM   4168  CG  HIS B 474      31.397  10.958 -13.974  1.00 22.72           C  
ANISOU 4168  CG  HIS B 474     1690   4142   2800   -119   -731    398       C  
ATOM   4169  ND1 HIS B 474      31.822  11.414 -15.204  1.00 25.50           N  
ANISOU 4169  ND1 HIS B 474     1957   4373   3359    149   -889    171       N  
ATOM   4170  CD2 HIS B 474      30.180  10.401 -14.178  1.00 24.70           C  
ANISOU 4170  CD2 HIS B 474     1729   4199   3458   -335  -1106    335       C  
ATOM   4171  CE1 HIS B 474      30.902  11.138 -16.113  1.00 25.60           C  
ANISOU 4171  CE1 HIS B 474     1683   4446   3597   -125   -788    312       C  
ATOM   4172  NE2 HIS B 474      29.898  10.520 -15.517  1.00 27.80           N  
ANISOU 4172  NE2 HIS B 474     2031   4554   3977     60  -1367   -139       N  
ATOM   4173  N   TYR B 475      33.978  13.430 -11.257  1.00 18.09           N  
ANISOU 4173  N   TYR B 475     1567   3073   2233    252   -263     47       N  
ATOM   4174  CA  TYR B 475      34.342  13.951  -9.945  1.00 16.72           C  
ANISOU 4174  CA  TYR B 475     1392   3068   1894    176    -93    178       C  
ATOM   4175  C   TYR B 475      33.047  14.128  -9.168  1.00 19.54           C  
ANISOU 4175  C   TYR B 475     1401   3729   2294    312    281    413       C  
ATOM   4176  O   TYR B 475      32.242  15.008  -9.481  1.00 21.88           O  
ANISOU 4176  O   TYR B 475     1393   3798   3122    454    -19    653       O  
ATOM   4177  CB  TYR B 475      35.081  15.277 -10.107  1.00 18.11           C  
ANISOU 4177  CB  TYR B 475     1505   3145   2230    256   -180     62       C  
ATOM   4178  CG  TYR B 475      35.582  15.910  -8.830  1.00 15.87           C  
ANISOU 4178  CG  TYR B 475     1335   3042   1654    339   -295     79       C  
ATOM   4179  CD1 TYR B 475      36.596  15.319  -8.088  1.00 15.29           C  
ANISOU 4179  CD1 TYR B 475     1192   3055   1560    179   -131    242       C  
ATOM   4180  CD2 TYR B 475      35.074  17.127  -8.391  1.00 18.24           C  
ANISOU 4180  CD2 TYR B 475     1632   3149   2147    648     47    271       C  
ATOM   4181  CE1 TYR B 475      37.061  15.910  -6.927  1.00 16.17           C  
ANISOU 4181  CE1 TYR B 475     1374   3118   1651    473    -99    283       C  
ATOM   4182  CE2 TYR B 475      35.535  17.726  -7.239  1.00 16.98           C  
ANISOU 4182  CE2 TYR B 475     1610   3056   1786    517   -582     25       C  
ATOM   4183  CZ  TYR B 475      36.529  17.115  -6.508  1.00 16.25           C  
ANISOU 4183  CZ  TYR B 475     1468   3029   1678    465   -401    313       C  
ATOM   4184  OH  TYR B 475      37.003  17.704  -5.358  1.00 17.81           O  
ANISOU 4184  OH  TYR B 475     1623   3097   2048    591   -493    389       O  
ATOM   4185  N   VAL B 476      32.843  13.275  -8.167  1.00 20.67           N  
ANISOU 4185  N   VAL B 476     1269   4299   2284    151    234    278       N  
ATOM   4186  CA  VAL B 476      31.526  13.093  -7.563  1.00 23.39           C  
ANISOU 4186  CA  VAL B 476     1616   4710   2561    -53     82   -218       C  
ATOM   4187  C   VAL B 476      31.441  13.624  -6.131  1.00 24.25           C  
ANISOU 4187  C   VAL B 476     1656   5159   2400   -226    307     79       C  
ATOM   4188  O   VAL B 476      32.373  13.483  -5.338  1.00 24.61           O  
ANISOU 4188  O   VAL B 476     1473   5389   2489   -203     70     96       O  
ATOM   4189  CB  VAL B 476      31.127  11.604  -7.579  1.00 25.07           C  
ANISOU 4189  CB  VAL B 476     1877   4543   3105   -475    315   -420       C  
ATOM   4190  CG1 VAL B 476      29.767  11.413  -6.949  1.00 28.44           C  
ANISOU 4190  CG1 VAL B 476     2270   4961   3574    -44     81   -287       C  
ATOM   4191  CG2 VAL B 476      31.129  11.068  -9.006  1.00 25.17           C  
ANISOU 4191  CG2 VAL B 476     2082   4589   2890   -502    266   -464       C  
ATOM   4192  N   ASP B 477      30.315  14.250  -5.813  1.00 28.28           N  
ANISOU 4192  N   ASP B 477     2136   5607   3000   -271    419    -35       N  
ATOM   4193  CA  ASP B 477      30.055  14.692  -4.454  1.00 32.91           C  
ANISOU 4193  CA  ASP B 477     2912   6087   3503   -148    495     -8       C  
ATOM   4194  C   ASP B 477      29.997  13.471  -3.544  1.00 33.26           C  
ANISOU 4194  C   ASP B 477     3159   6422   3057   -805    702    444       C  
ATOM   4195  O   ASP B 477      29.295  12.505  -3.838  1.00 32.86           O  
ANISOU 4195  O   ASP B 477     3157   6166   3163   -938    563    576       O  
ATOM   4196  CB  ASP B 477      28.741  15.467  -4.392  1.00 38.68           C  
ANISOU 4196  CB  ASP B 477     3638   6607   4451    628    847   -330       C  
ATOM   4197  CG  ASP B 477      28.501  16.091  -3.036  1.00 44.71           C  
ANISOU 4197  CG  ASP B 477     4374   6994   5619   1219    776   -610       C  
ATOM   4198  OD1 ASP B 477      28.595  17.333  -2.928  1.00 46.82           O  
ANISOU 4198  OD1 ASP B 477     4691   7049   6049   1655    534   -934       O  
ATOM   4199  OD2 ASP B 477      28.228  15.338  -2.077  1.00 46.74           O  
ANISOU 4199  OD2 ASP B 477     4555   7198   6004   1232   1024   -492       O  
ATOM   4200  N   PRO B 478      30.739  13.512  -2.430  1.00 34.94           N  
ANISOU 4200  N   PRO B 478     3583   6690   3003  -1141    578    446       N  
ATOM   4201  CA  PRO B 478      30.919  12.357  -1.544  1.00 38.97           C  
ANISOU 4201  CA  PRO B 478     4061   6928   3819  -1074    451    366       C  
ATOM   4202  C   PRO B 478      29.645  12.001  -0.792  1.00 42.28           C  
ANISOU 4202  C   PRO B 478     4521   7241   4301  -1106    653    466       C  
ATOM   4203  O   PRO B 478      29.492  10.869  -0.332  1.00 43.28           O  
ANISOU 4203  O   PRO B 478     4638   7118   4686  -1285    594    195       O  
ATOM   4204  CB  PRO B 478      31.989  12.842  -0.563  1.00 39.47           C  
ANISOU 4204  CB  PRO B 478     4124   7040   3832   -901     30    322       C  
ATOM   4205  CG  PRO B 478      31.798  14.318  -0.512  1.00 38.06           C  
ANISOU 4205  CG  PRO B 478     4027   6916   3519  -1051     18    328       C  
ATOM   4206  CD  PRO B 478      31.418  14.714  -1.916  1.00 36.06           C  
ANISOU 4206  CD  PRO B 478     3820   6765   3117  -1143    231    450       C  
ATOM   4207  N   ASP B 479      28.740  12.966  -0.671  1.00 45.05           N  
ANISOU 4207  N   ASP B 479     4716   7706   4694  -1068   1092    808       N  
ATOM   4208  CA  ASP B 479      27.512  12.772   0.090  1.00 50.41           C  
ANISOU 4208  CA  ASP B 479     5136   8233   5783   -679   1074    814       C  
ATOM   4209  C   ASP B 479      26.330  12.483  -0.827  1.00 52.16           C  
ANISOU 4209  C   ASP B 479     4983   8323   6512   -959   1092   1164       C  
ATOM   4210  O   ASP B 479      25.622  11.489  -0.653  1.00 53.51           O  
ANISOU 4210  O   ASP B 479     5136   8329   6866  -1063    972   1413       O  
ATOM   4211  CB  ASP B 479      27.218  14.009   0.937  1.00 53.84           C  
ANISOU 4211  CB  ASP B 479     5727   8541   6188   -114    985    492       C  
ATOM   4212  CG  ASP B 479      28.417  14.457   1.749  1.00 56.81           C  
ANISOU 4212  CG  ASP B 479     6279   8747   6557    376    882     40       C  
ATOM   4213  OD1 ASP B 479      28.700  15.674   1.767  1.00 58.73           O  
ANISOU 4213  OD1 ASP B 479     6494   8756   7065    512    835   -167       O  
ATOM   4214  OD2 ASP B 479      29.077  13.592   2.367  1.00 56.64           O  
ANISOU 4214  OD2 ASP B 479     6490   8772   6258    616    856    -56       O  
ATOM   4215  N   THR B 480      26.124  13.360  -1.803  1.00 52.44           N  
ANISOU 4215  N   THR B 480     4728   8516   6681  -1170   1090   1037       N  
ATOM   4216  CA  THR B 480      24.982  13.262  -2.703  1.00 52.86           C  
ANISOU 4216  CA  THR B 480     4590   8682   6812  -1119    982    723       C  
ATOM   4217  C   THR B 480      25.243  12.310  -3.865  1.00 52.03           C  
ANISOU 4217  C   THR B 480     4582   8403   6783  -1254    556    696       C  
ATOM   4218  O   THR B 480      24.310  11.835  -4.504  1.00 50.83           O  
ANISOU 4218  O   THR B 480     4466   8099   6746  -1624    665    954       O  
ATOM   4219  CB  THR B 480      24.599  14.641  -3.274  1.00 53.92           C  
ANISOU 4219  CB  THR B 480     4401   9191   6893  -1028   1202    308       C  
ATOM   4220  OG1 THR B 480      25.634  15.103  -4.153  1.00 53.76           O  
ANISOU 4220  OG1 THR B 480     4140   9387   6899  -1071   1308    112       O  
ATOM   4221  CG2 THR B 480      24.406  15.650  -2.150  1.00 53.82           C  
ANISOU 4221  CG2 THR B 480     4382   9351   6716  -1031   1352    222       C  
ATOM   4222  N   HIS B 481      26.515  12.038  -4.138  1.00 50.99           N  
ANISOU 4222  N   HIS B 481     4644   8060   6670  -1117    163    634       N  
ATOM   4223  CA  HIS B 481      26.893  11.180  -5.257  1.00 51.40           C  
ANISOU 4223  CA  HIS B 481     4809   7932   6788   -690   -271    520       C  
ATOM   4224  C   HIS B 481      26.565  11.822  -6.605  1.00 46.57           C  
ANISOU 4224  C   HIS B 481     4139   7406   6150  -1117   -524    550       C  
ATOM   4225  O   HIS B 481      26.512  11.143  -7.629  1.00 47.42           O  
ANISOU 4225  O   HIS B 481     4196   7410   6411  -1204   -650    516       O  
ATOM   4226  CB  HIS B 481      26.233   9.801  -5.143  1.00 55.85           C  
ANISOU 4226  CB  HIS B 481     5635   8044   7539    224   -518    390       C  
ATOM   4227  CG  HIS B 481      26.789   8.957  -4.040  1.00 60.35           C  
ANISOU 4227  CG  HIS B 481     6343   8370   8215   1104   -660    335       C  
ATOM   4228  ND1 HIS B 481      26.504   9.186  -2.711  1.00 61.96           N  
ANISOU 4228  ND1 HIS B 481     6637   8459   8445   1498   -700    290       N  
ATOM   4229  CD2 HIS B 481      27.620   7.888  -4.067  1.00 62.17           C  
ANISOU 4229  CD2 HIS B 481     6631   8483   8506   1511   -696    342       C  
ATOM   4230  CE1 HIS B 481      27.133   8.291  -1.967  1.00 62.86           C  
ANISOU 4230  CE1 HIS B 481     6768   8576   8538   1673   -744    356       C  
ATOM   4231  NE2 HIS B 481      27.817   7.492  -2.766  1.00 63.06           N  
ANISOU 4231  NE2 HIS B 481     6771   8587   8602   1675   -752    382       N  
ATOM   4232  N   ARG B 482      26.350  13.133  -6.593  1.00 43.36           N  
ANISOU 4232  N   ARG B 482     3621   7223   5629  -1024   -396    820       N  
ATOM   4233  CA  ARG B 482      26.122  13.887  -7.821  1.00 43.12           C  
ANISOU 4233  CA  ARG B 482     3506   7255   5623   -467   -154   1003       C  
ATOM   4234  C   ARG B 482      27.427  14.091  -8.578  1.00 37.35           C  
ANISOU 4234  C   ARG B 482     2924   6683   4584   -292   -430    847       C  
ATOM   4235  O   ARG B 482      28.450  14.421  -7.978  1.00 34.90           O  
ANISOU 4235  O   ARG B 482     2537   6556   4168   -520   -804    619       O  
ATOM   4236  CB  ARG B 482      25.518  15.255  -7.503  1.00 49.40           C  
ANISOU 4236  CB  ARG B 482     4074   7839   6856     56     55   1030       C  
ATOM   4237  CG  ARG B 482      24.016  15.264  -7.290  1.00 55.09           C  
ANISOU 4237  CG  ARG B 482     4727   8283   7920    612    163    979       C  
ATOM   4238  CD  ARG B 482      23.527  16.666  -6.942  1.00 59.27           C  
ANISOU 4238  CD  ARG B 482     5236   8569   8715    820    231    872       C  
ATOM   4239  NE  ARG B 482      24.122  17.685  -7.804  1.00 61.87           N  
ANISOU 4239  NE  ARG B 482     5637   8660   9211   1052    187    759       N  
ATOM   4240  CZ  ARG B 482      25.177  18.426  -7.472  1.00 63.05           C  
ANISOU 4240  CZ  ARG B 482     5823   8671   9460   1244     74    699       C  
ATOM   4241  NH1 ARG B 482      25.758  18.266  -6.289  1.00 63.57           N  
ANISOU 4241  NH1 ARG B 482     5900   8741   9512   1351     67    750       N  
ATOM   4242  NH2 ARG B 482      25.650  19.329  -8.321  1.00 63.23           N  
ANISOU 4242  NH2 ARG B 482     5856   8671   9495   1256     31    619       N  
ATOM   4243  N   ASN B 483      27.386  13.903  -9.893  1.00 35.26           N  
ANISOU 4243  N   ASN B 483     2693   6478   4227     97   -377    744       N  
ATOM   4244  CA  ASN B 483      28.532  14.204 -10.743  1.00 31.60           C  
ANISOU 4244  CA  ASN B 483     2322   5959   3724    297   -578    565       C  
ATOM   4245  C   ASN B 483      28.769  15.709 -10.814  1.00 31.29           C  
ANISOU 4245  C   ASN B 483     2358   5791   3738    921   -329    752       C  
ATOM   4246  O   ASN B 483      27.884  16.463 -11.223  1.00 35.07           O  
ANISOU 4246  O   ASN B 483     2761   6115   4450   1505   -485    836       O  
ATOM   4247  CB  ASN B 483      28.331  13.632 -12.147  1.00 32.05           C  
ANISOU 4247  CB  ASN B 483     2399   5630   4149    216   -628    117       C  
ATOM   4248  CG  ASN B 483      29.500  13.920 -13.067  1.00 33.94           C  
ANISOU 4248  CG  ASN B 483     2704   5522   4668    537   -484     37       C  
ATOM   4249  OD1 ASN B 483      30.625  14.123 -12.613  1.00 34.46           O  
ANISOU 4249  OD1 ASN B 483     2532   5290   5271    203     60    -41       O  
ATOM   4250  ND2 ASN B 483      29.240  13.937 -14.368  1.00 34.34           N  
ANISOU 4250  ND2 ASN B 483     3044   5406   4596    790   -140     84       N  
ATOM   4251  N   LEU B 484      29.960  16.146 -10.415  1.00 28.97           N  
ANISOU 4251  N   LEU B 484     2447   5438   3123   1126     44    519       N  
ATOM   4252  CA  LEU B 484      30.277  17.570 -10.378  1.00 29.03           C  
ANISOU 4252  CA  LEU B 484     2601   5284   3144   1374    413    423       C  
ATOM   4253  C   LEU B 484      31.067  18.027 -11.600  1.00 28.00           C  
ANISOU 4253  C   LEU B 484     2643   4967   3028   1507    418    234       C  
ATOM   4254  O   LEU B 484      31.216  19.224 -11.836  1.00 28.72           O  
ANISOU 4254  O   LEU B 484     2873   4989   3050   1596    338    169       O  
ATOM   4255  CB  LEU B 484      31.057  17.913  -9.109  1.00 28.00           C  
ANISOU 4255  CB  LEU B 484     2832   5322   2485   1606    422    155       C  
ATOM   4256  CG  LEU B 484      30.427  17.494  -7.782  1.00 29.98           C  
ANISOU 4256  CG  LEU B 484     2871   5420   3098   1555    557    162       C  
ATOM   4257  CD1 LEU B 484      31.391  17.758  -6.634  1.00 30.34           C  
ANISOU 4257  CD1 LEU B 484     3148   5353   3026   1503    417   -112       C  
ATOM   4258  CD2 LEU B 484      29.103  18.217  -7.566  1.00 31.79           C  
ANISOU 4258  CD2 LEU B 484     2835   5565   3677   1576    742    113       C  
ATOM   4259  N   GLY B 485      31.581  17.076 -12.372  1.00 26.45           N  
ANISOU 4259  N   GLY B 485     2404   4608   3037   1333    260    522       N  
ATOM   4260  CA  GLY B 485      32.338  17.412 -13.563  1.00 25.25           C  
ANISOU 4260  CA  GLY B 485     2253   4216   3124   1221    296    394       C  
ATOM   4261  C   GLY B 485      33.049  16.217 -14.159  1.00 21.81           C  
ANISOU 4261  C   GLY B 485     1894   3872   2521    715   -134    478       C  
ATOM   4262  O   GLY B 485      33.408  15.286 -13.439  1.00 21.86           O  
ANISOU 4262  O   GLY B 485     2193   3718   2395    834   -382    573       O  
ATOM   4263  N   GLU B 486      33.250  16.246 -15.474  1.00 22.74           N  
ANISOU 4263  N   GLU B 486     1873   3898   2868    569    378    542       N  
ATOM   4264  CA  GLU B 486      33.931  15.166 -16.182  1.00 21.28           C  
ANISOU 4264  CA  GLU B 486     1799   3793   2494    414   -213    457       C  
ATOM   4265  C   GLU B 486      35.386  15.530 -16.444  1.00 19.73           C  
ANISOU 4265  C   GLU B 486     1873   3174   2449    451   -412    201       C  
ATOM   4266  O   GLU B 486      35.711  16.695 -16.677  1.00 19.51           O  
ANISOU 4266  O   GLU B 486     1961   2947   2506    714   -314    187       O  
ATOM   4267  CB  GLU B 486      33.231  14.855 -17.515  1.00 23.78           C  
ANISOU 4267  CB  GLU B 486     1997   4305   2733    125   -549    520       C  
ATOM   4268  CG  GLU B 486      31.827  14.264 -17.393  1.00 29.94           C  
ANISOU 4268  CG  GLU B 486     2386   4934   4055    106   -599    681       C  
ATOM   4269  CD  GLU B 486      31.355  13.586 -18.677  1.00 36.16           C  
ANISOU 4269  CD  GLU B 486     2969   5582   5188    240   -503    943       C  
ATOM   4270  OE1 GLU B 486      31.785  14.000 -19.778  1.00 37.65           O  
ANISOU 4270  OE1 GLU B 486     2996   5729   5580    285   -580    934       O  
ATOM   4271  OE2 GLU B 486      30.555  12.628 -18.586  1.00 39.05           O  
ANISOU 4271  OE2 GLU B 486     3664   5928   5246    866   -660    864       O  
ATOM   4272  N   PHE B 487      36.252  14.521 -16.402  1.00 16.20           N  
ANISOU 4272  N   PHE B 487     1432   2836   1887    455   -354     39       N  
ATOM   4273  CA  PHE B 487      37.672  14.687 -16.671  1.00 15.23           C  
ANISOU 4273  CA  PHE B 487     1626   2384   1775    101   -176    123       C  
ATOM   4274  C   PHE B 487      38.159  13.547 -17.559  1.00 15.27           C  
ANISOU 4274  C   PHE B 487     1745   2236   1821    195   -316    -25       C  
ATOM   4275  O   PHE B 487      37.574  12.461 -17.567  1.00 17.05           O  
ANISOU 4275  O   PHE B 487     1893   2393   2191    -21   -374    -10       O  
ATOM   4276  CB  PHE B 487      38.469  14.675 -15.365  1.00 15.45           C  
ANISOU 4276  CB  PHE B 487     1828   2458   1585    211   -318    -48       C  
ATOM   4277  CG  PHE B 487      38.138  15.806 -14.437  1.00 14.89           C  
ANISOU 4277  CG  PHE B 487     1855   2357   1446     52   -243    135       C  
ATOM   4278  CD1 PHE B 487      38.945  16.928 -14.379  1.00 17.28           C  
ANISOU 4278  CD1 PHE B 487     1960   2421   2182    113    -98   -196       C  
ATOM   4279  CD2 PHE B 487      37.020  15.745 -13.620  1.00 16.81           C  
ANISOU 4279  CD2 PHE B 487     1967   2747   1672    445    -21     44       C  
ATOM   4280  CE1 PHE B 487      38.644  17.976 -13.517  1.00 18.03           C  
ANISOU 4280  CE1 PHE B 487     2022   2518   2308    301     85   -100       C  
ATOM   4281  CE2 PHE B 487      36.712  16.784 -12.758  1.00 18.47           C  
ANISOU 4281  CE2 PHE B 487     2061   2658   2297    450    -93    209       C  
ATOM   4282  CZ  PHE B 487      37.524  17.900 -12.706  1.00 17.49           C  
ANISOU 4282  CZ  PHE B 487     2009   2790   1847    370    412    404       C  
ATOM   4283  N   LYS B 488      39.233  13.791 -18.302  1.00 15.17           N  
ANISOU 4283  N   LYS B 488     1540   2201   2021    281   -171    -75       N  
ATOM   4284  CA  LYS B 488      39.878  12.736 -19.080  1.00 16.04           C  
ANISOU 4284  CA  LYS B 488     1744   2440   1911      9   -325   -192       C  
ATOM   4285  C   LYS B 488      41.278  12.503 -18.533  1.00 15.57           C  
ANISOU 4285  C   LYS B 488     1722   2403   1789   -110   -575   -207       C  
ATOM   4286  O   LYS B 488      42.029  13.452 -18.321  1.00 19.22           O  
ANISOU 4286  O   LYS B 488     1833   2158   3312    -77   -626   -160       O  
ATOM   4287  CB  LYS B 488      39.954  13.118 -20.561  1.00 18.73           C  
ANISOU 4287  CB  LYS B 488     1974   2809   2333   -115   -799   -128       C  
ATOM   4288  CG  LYS B 488      38.649  12.925 -21.317  1.00 21.44           C  
ANISOU 4288  CG  LYS B 488     2295   3198   2653    221   -752   -117       C  
ATOM   4289  CD  LYS B 488      38.649  13.670 -22.650  1.00 22.14           C  
ANISOU 4289  CD  LYS B 488     2715   3294   2404    702   -681    -43       C  
ATOM   4290  CE  LYS B 488      39.674  13.101 -23.632  1.00 22.04           C  
ANISOU 4290  CE  LYS B 488     2995   3132   2247    667   -818    529       C  
ATOM   4291  NZ  LYS B 488      39.546  13.734 -24.983  1.00 21.88           N  
ANISOU 4291  NZ  LYS B 488     3081   2766   2465    578  -1087   -148       N  
ATOM   4292  N   MET B 489      41.619  11.241 -18.298  1.00 14.80           N  
ANISOU 4292  N   MET B 489     1769   2163   1692   -180   -289     78       N  
ATOM   4293  CA  MET B 489      42.970  10.872 -17.896  1.00 15.64           C  
ANISOU 4293  CA  MET B 489     1910   2200   1832   -274   -419    392       C  
ATOM   4294  C   MET B 489      43.628  10.204 -19.076  1.00 15.94           C  
ANISOU 4294  C   MET B 489     2034   1888   2133   -155   -233    -93       C  
ATOM   4295  O   MET B 489      43.052   9.307 -19.675  1.00 21.04           O  
ANISOU 4295  O   MET B 489     2177   2275   3540   -342    246   -802       O  
ATOM   4296  CB  MET B 489      42.960   9.864 -16.751  1.00 19.44           C  
ANISOU 4296  CB  MET B 489     2482   2579   2323   -415   -344    848       C  
ATOM   4297  CG  MET B 489      42.739  10.421 -15.386  1.00 22.82           C  
ANISOU 4297  CG  MET B 489     3056   2595   3018     95     30    332       C  
ATOM   4298  SD  MET B 489      43.576   9.392 -14.157  1.00 20.35           S  
ANISOU 4298  SD  MET B 489     3409   2581   1741    477    139    454       S  
ATOM   4299  CE  MET B 489      45.191  10.152 -14.155  1.00 24.28           C  
ANISOU 4299  CE  MET B 489     3410   2825   2989    499   -230   -103       C  
ATOM   4300  N   TYR B 490      44.838  10.629 -19.402  1.00 13.63           N  
ANISOU 4300  N   TYR B 490     1698   1576   1904   -306   -189    170       N  
ATOM   4301  CA  TYR B 490      45.560  10.039 -20.513  1.00 13.85           C  
ANISOU 4301  CA  TYR B 490     1825   1648   1789   -169   -199     80       C  
ATOM   4302  C   TYR B 490      46.574   9.022 -19.990  1.00 14.75           C  
ANISOU 4302  C   TYR B 490     1977   1500   2128   -268   -297     42       C  
ATOM   4303  O   TYR B 490      46.986   9.096 -18.835  1.00 14.97           O  
ANISOU 4303  O   TYR B 490     2030   1552   2105   -141   -473    162       O  
ATOM   4304  CB  TYR B 490      46.226  11.132 -21.351  1.00 15.34           C  
ANISOU 4304  CB  TYR B 490     2007   1640   2181    -82   -324    541       C  
ATOM   4305  CG  TYR B 490      45.234  11.989 -22.112  1.00 16.46           C  
ANISOU 4305  CG  TYR B 490     2358   1857   2039    207   -344    243       C  
ATOM   4306  CD1 TYR B 490      44.912  11.702 -23.436  1.00 17.43           C  
ANISOU 4306  CD1 TYR B 490     2615   2217   1788    316   -501    261       C  
ATOM   4307  CD2 TYR B 490      44.612  13.077 -21.505  1.00 17.44           C  
ANISOU 4307  CD2 TYR B 490     2393   1940   2293    315   -281    427       C  
ATOM   4308  CE1 TYR B 490      44.005  12.478 -24.135  1.00 19.28           C  
ANISOU 4308  CE1 TYR B 490     2832   2306   2186    870   -477     68       C  
ATOM   4309  CE2 TYR B 490      43.698  13.863 -22.200  1.00 17.29           C  
ANISOU 4309  CE2 TYR B 490     2387   2243   1937    288   -271     99       C  
ATOM   4310  CZ  TYR B 490      43.403  13.558 -23.516  1.00 18.67           C  
ANISOU 4310  CZ  TYR B 490     2642   2481   1969    778   -542    230       C  
ATOM   4311  OH  TYR B 490      42.500  14.324 -24.227  1.00 20.83           O  
ANISOU 4311  OH  TYR B 490     3043   2717   2152    933   -801   -267       O  
ATOM   4312  N   PRO B 491      46.964   8.064 -20.842  1.00 14.92           N  
ANISOU 4312  N   PRO B 491     2209   1624   1836    -30   -605   -191       N  
ATOM   4313  CA  PRO B 491      47.866   6.964 -20.477  1.00 15.69           C  
ANISOU 4313  CA  PRO B 491     2264   1642   2056    311   -479   -276       C  
ATOM   4314  C   PRO B 491      49.171   7.448 -19.848  1.00 14.98           C  
ANISOU 4314  C   PRO B 491     2250   1587   1855    185   -275    -55       C  
ATOM   4315  O   PRO B 491      49.732   6.742 -19.009  1.00 14.89           O  
ANISOU 4315  O   PRO B 491     2265   1454   1937    223   -384     99       O  
ATOM   4316  CB  PRO B 491      48.142   6.286 -21.822  1.00 16.28           C  
ANISOU 4316  CB  PRO B 491     2278   1742   2164    141   -608   -297       C  
ATOM   4317  CG  PRO B 491      46.895   6.537 -22.623  1.00 17.93           C  
ANISOU 4317  CG  PRO B 491     2440   1769   2601     73   -715   -446       C  
ATOM   4318  CD  PRO B 491      46.472   7.937 -22.228  1.00 16.89           C  
ANISOU 4318  CD  PRO B 491     2526   1627   2262    319   -800   -569       C  
ATOM   4319  N   GLU B 492      49.634   8.632 -20.245  1.00 14.78           N  
ANISOU 4319  N   GLU B 492     2243   1518   1853   -154   -330   -254       N  
ATOM   4320  CA  GLU B 492      50.869   9.217 -19.721  1.00 15.16           C  
ANISOU 4320  CA  GLU B 492     2293   1881   1586   -257   -401   -260       C  
ATOM   4321  C   GLU B 492      50.781   9.639 -18.252  1.00 15.18           C  
ANISOU 4321  C   GLU B 492     2212   1801   1755   -214   -139    154       C  
ATOM   4322  O   GLU B 492      51.796   9.973 -17.634  1.00 17.21           O  
ANISOU 4322  O   GLU B 492     2181   2464   1893   -575   -261     52       O  
ATOM   4323  CB  GLU B 492      51.292  10.411 -20.574  1.00 16.48           C  
ANISOU 4323  CB  GLU B 492     2479   2201   1581   -461    125    140       C  
ATOM   4324  CG  GLU B 492      51.720  10.052 -21.987  1.00 19.16           C  
ANISOU 4324  CG  GLU B 492     2675   2837   1767    -44     86   -268       C  
ATOM   4325  CD  GLU B 492      50.552   9.838 -22.942  1.00 21.17           C  
ANISOU 4325  CD  GLU B 492     2985   3208   1849    260     80   -543       C  
ATOM   4326  OE1 GLU B 492      49.386  10.114 -22.578  1.00 20.83           O  
ANISOU 4326  OE1 GLU B 492     2861   2856   2198    380   -100    225       O  
ATOM   4327  OE2 GLU B 492      50.807   9.393 -24.076  1.00 26.22           O  
ANISOU 4327  OE2 GLU B 492     3294   3983   2686    337    -90   -745       O  
ATOM   4328  N   GLY B 493      49.575   9.628 -17.698  1.00 13.39           N  
ANISOU 4328  N   GLY B 493     2187   1362   1538    104    -64    -41       N  
ATOM   4329  CA  GLY B 493      49.397   9.897 -16.284  1.00 13.69           C  
ANISOU 4329  CA  GLY B 493     1975   1390   1834    -81   -218    -45       C  
ATOM   4330  C   GLY B 493      49.160  11.354 -15.946  1.00 14.02           C  
ANISOU 4330  C   GLY B 493     2052   1393   1881    -71   -460    126       C  
ATOM   4331  O   GLY B 493      49.852  11.933 -15.113  1.00 16.60           O  
ANISOU 4331  O   GLY B 493     2476   1478   2351     47  -1013   -147       O  
ATOM   4332  N   TYR B 494      48.180  11.952 -16.604  1.00 12.85           N  
ANISOU 4332  N   TYR B 494     1706   1477   1700     92   -121    -57       N  
ATOM   4333  CA  TYR B 494      47.736  13.293 -16.264  1.00 12.84           C  
ANISOU 4333  CA  TYR B 494     1426   1424   2029     -7     72   -188       C  
ATOM   4334  C   TYR B 494      46.273  13.404 -16.664  1.00 11.72           C  
ANISOU 4334  C   TYR B 494     1357   1601   1494    151   -178   -245       C  
ATOM   4335  O   TYR B 494      45.740  12.527 -17.352  1.00 13.35           O  
ANISOU 4335  O   TYR B 494     1399   1863   1810   -116   -141   -349       O  
ATOM   4336  CB  TYR B 494      48.577  14.360 -16.970  1.00 12.78           C  
ANISOU 4336  CB  TYR B 494     1627   1495   1732    -35   -172    -69       C  
ATOM   4337  CG  TYR B 494      48.390  14.393 -18.466  1.00 13.72           C  
ANISOU 4337  CG  TYR B 494     1890   1872   1451    -96   -114     47       C  
ATOM   4338  CD1 TYR B 494      47.550  15.329 -19.055  1.00 15.24           C  
ANISOU 4338  CD1 TYR B 494     2022   2099   1668   -354    -72    531       C  
ATOM   4339  CD2 TYR B 494      49.040  13.478 -19.288  1.00 14.58           C  
ANISOU 4339  CD2 TYR B 494     2169   1854   1516   -398    316     38       C  
ATOM   4340  CE1 TYR B 494      47.370  15.356 -20.427  1.00 17.02           C  
ANISOU 4340  CE1 TYR B 494     2209   2483   1774   -303     54    301       C  
ATOM   4341  CE2 TYR B 494      48.872  13.502 -20.660  1.00 16.19           C  
ANISOU 4341  CE2 TYR B 494     2551   2017   1584   -347     85     82       C  
ATOM   4342  CZ  TYR B 494      48.034  14.441 -21.223  1.00 16.66           C  
ANISOU 4342  CZ  TYR B 494     2583   2329   1418   -467   -110    361       C  
ATOM   4343  OH  TYR B 494      47.860  14.473 -22.591  1.00 19.73           O  
ANISOU 4343  OH  TYR B 494     2974   2820   1700   -405     12    175       O  
ATOM   4344  N   MET B 495      45.637  14.487 -16.235  1.00 12.78           N  
ANISOU 4344  N   MET B 495     1464   1675   1717    385    -95    114       N  
ATOM   4345  CA  MET B 495      44.208  14.662 -16.389  1.00 13.54           C  
ANISOU 4345  CA  MET B 495     1656   1867   1621    373     51    193       C  
ATOM   4346  C   MET B 495      43.928  15.992 -17.090  1.00 14.29           C  
ANISOU 4346  C   MET B 495     1764   1853   1812    261   -283    140       C  
ATOM   4347  O   MET B 495      44.667  16.961 -16.905  1.00 13.46           O  
ANISOU 4347  O   MET B 495     1727   1611   1776    230   -234     75       O  
ATOM   4348  CB  MET B 495      43.596  14.687 -14.990  1.00 19.11           C  
ANISOU 4348  CB  MET B 495     1989   2491   2782    210    409    567       C  
ATOM   4349  CG  MET B 495      42.115  14.504 -14.910  1.00 21.22           C  
ANISOU 4349  CG  MET B 495     2383   2770   2909    432     54    519       C  
ATOM   4350  SD  MET B 495      41.646  14.458 -13.171  1.00 16.43           S  
ANISOU 4350  SD  MET B 495     2119   2451   1672   -165   -113    142       S  
ATOM   4351  CE  MET B 495      42.493  13.014 -12.542  1.00 19.87           C  
ANISOU 4351  CE  MET B 495     2267   2589   2693    -47    163    -77       C  
ATOM   4352  N   THR B 496      42.868  16.044 -17.894  1.00 14.20           N  
ANISOU 4352  N   THR B 496     1694   2054   1648    398   -220    127       N  
ATOM   4353  CA  THR B 496      42.429  17.306 -18.482  1.00 14.92           C  
ANISOU 4353  CA  THR B 496     1710   2398   1562    298   -393     44       C  
ATOM   4354  C   THR B 496      40.953  17.556 -18.205  1.00 15.63           C  
ANISOU 4354  C   THR B 496     1865   2254   1818    192   -301    -21       C  
ATOM   4355  O   THR B 496      40.213  16.653 -17.821  1.00 15.38           O  
ANISOU 4355  O   THR B 496     1779   2323   1742    248   -273    -51       O  
ATOM   4356  CB  THR B 496      42.615  17.334 -20.009  1.00 15.78           C  
ANISOU 4356  CB  THR B 496     1822   2451   1721    147   -161   -141       C  
ATOM   4357  OG1 THR B 496      41.766  16.346 -20.598  1.00 15.19           O  
ANISOU 4357  OG1 THR B 496     1850   2366   1555     77   -179     10       O  
ATOM   4358  CG2 THR B 496      44.065  17.064 -20.395  1.00 16.80           C  
ANISOU 4358  CG2 THR B 496     1839   2699   1843    360    -94    -66       C  
ATOM   4359  N   CYS B 497      40.534  18.799 -18.408  1.00 16.45           N  
ANISOU 4359  N   CYS B 497     1911   2551   1788    529   -376    -41       N  
ATOM   4360  CA  CYS B 497      39.128  19.160 -18.337  1.00 17.93           C  
ANISOU 4360  CA  CYS B 497     2374   2814   1625    745   -444     15       C  
ATOM   4361  C   CYS B 497      38.856  20.176 -19.435  1.00 18.10           C  
ANISOU 4361  C   CYS B 497     2426   2756   1693    861   -198     69       C  
ATOM   4362  O   CYS B 497      39.779  20.624 -20.110  1.00 18.49           O  
ANISOU 4362  O   CYS B 497     2471   2680   1874    874   -262    141       O  
ATOM   4363  CB  CYS B 497      38.803  19.770 -16.975  1.00 21.43           C  
ANISOU 4363  CB  CYS B 497     3043   3229   1870    994   -455   -137       C  
ATOM   4364  SG  CYS B 497      39.541  21.400 -16.708  1.00 25.22           S  
ANISOU 4364  SG  CYS B 497     3993   3421   2169   1354   -579   -523       S  
ATOM   4365  N   VAL B 498      37.590  20.529 -19.623  1.00 19.87           N  
ANISOU 4365  N   VAL B 498     2431   2853   2265    982   -326    214       N  
ATOM   4366  CA  VAL B 498      37.240  21.640 -20.492  1.00 21.29           C  
ANISOU 4366  CA  VAL B 498     2854   3003   2233   1030   -519     46       C  
ATOM   4367  C   VAL B 498      36.647  22.739 -19.622  1.00 24.04           C  
ANISOU 4367  C   VAL B 498     3176   3130   2826   1060   -155    166       C  
ATOM   4368  O   VAL B 498      35.501  22.637 -19.190  1.00 27.44           O  
ANISOU 4368  O   VAL B 498     3165   3132   4127    854    252      4       O  
ATOM   4369  CB  VAL B 498      36.236  21.215 -21.580  1.00 24.79           C  
ANISOU 4369  CB  VAL B 498     3143   3277   2998   1239   -903    328       C  
ATOM   4370  CG1 VAL B 498      35.665  22.438 -22.287  1.00 27.41           C  
ANISOU 4370  CG1 VAL B 498     3458   3560   3396   1424  -1143    481       C  
ATOM   4371  CG2 VAL B 498      36.911  20.279 -22.580  1.00 26.41           C  
ANISOU 4371  CG2 VAL B 498     3552   3389   3092   1098   -810    256       C  
ATOM   4372  N   PRO B 499      37.442  23.781 -19.329  1.00 26.93           N  
ANISOU 4372  N   PRO B 499     3704   3436   3092   1320   -275    -78       N  
ATOM   4373  CA  PRO B 499      36.981  24.889 -18.484  1.00 32.17           C  
ANISOU 4373  CA  PRO B 499     4214   3922   4088   1492    140    -89       C  
ATOM   4374  C   PRO B 499      35.777  25.599 -19.093  1.00 41.40           C  
ANISOU 4374  C   PRO B 499     4894   4796   6041   1703    215     98       C  
ATOM   4375  O   PRO B 499      35.720  25.767 -20.311  1.00 42.91           O  
ANISOU 4375  O   PRO B 499     4911   4728   6663   1953    128    577       O  
ATOM   4376  CB  PRO B 499      38.184  25.835 -18.457  1.00 31.35           C  
ANISOU 4376  CB  PRO B 499     4182   3718   4009   1459   -180   -440       C  
ATOM   4377  CG  PRO B 499      39.352  24.979 -18.762  1.00 29.45           C  
ANISOU 4377  CG  PRO B 499     3906   3497   3786   1382   -596   -245       C  
ATOM   4378  CD  PRO B 499      38.853  23.941 -19.721  1.00 26.37           C  
ANISOU 4378  CD  PRO B 499     3757   3256   3005   1156   -736   -362       C  
ATOM   4379  N   ASN B 500      34.835  26.011 -18.251  1.00 47.93           N  
ANISOU 4379  N   ASN B 500     5476   5466   7269   1616    441    -68       N  
ATOM   4380  CA  ASN B 500      33.601  26.637 -18.717  1.00 53.92           C  
ANISOU 4380  CA  ASN B 500     6085   6130   8270   1391    396   -145       C  
ATOM   4381  C   ASN B 500      33.354  28.037 -18.144  1.00 53.98           C  
ANISOU 4381  C   ASN B 500     6207   6340   7963   1154    355   -503       C  
ATOM   4382  O   ASN B 500      34.286  28.703 -17.691  1.00 55.87           O  
ANISOU 4382  O   ASN B 500     6293   6492   8441   1221    485   -565       O  
ATOM   4383  CB  ASN B 500      32.404  25.722 -18.442  1.00 58.76           C  
ANISOU 4383  CB  ASN B 500     6510   6467   9350   1364    440    -48       C  
ATOM   4384  CG  ASN B 500      32.474  25.064 -17.075  1.00 62.63           C  
ANISOU 4384  CG  ASN B 500     6890   6689  10217   1303    533    -75       C  
ATOM   4385  OD1 ASN B 500      32.958  25.655 -16.110  1.00 63.92           O  
ANISOU 4385  OD1 ASN B 500     7052   6705  10529   1292    573   -153       O  
ATOM   4386  ND2 ASN B 500      31.995  23.827 -16.991  1.00 63.74           N  
ANISOU 4386  ND2 ASN B 500     6990   6763  10464   1263    570     -8       N  
ATOM   4387  N   ALA B 501      32.093  28.471 -18.175  1.00 52.14           N  
ANISOU 4387  N   ALA B 501     6242   6318   7251    889    137   -579       N  
ATOM   4388  CA  ALA B 501      31.704  29.813 -17.732  1.00 49.11           C  
ANISOU 4388  CA  ALA B 501     6209   6131   6318    573      4   -523       C  
ATOM   4389  C   ALA B 501      32.155  30.089 -16.307  1.00 47.86           C  
ANISOU 4389  C   ALA B 501     6148   5920   6115    218     40   -218       C  
ATOM   4390  O   ALA B 501      33.059  30.895 -16.074  1.00 49.14           O  
ANISOU 4390  O   ALA B 501     6174   5919   6576    128    -71   -324       O  
ATOM   4391  CB  ALA B 501      30.200  29.994 -17.853  1.00 48.16           C  
ANISOU 4391  CB  ALA B 501     6255   5978   6065    598     39   -441       C  
ATOM   4392  N   GLY B 502      31.505  29.437 -15.348  1.00 46.80           N  
ANISOU 4392  N   GLY B 502     6117   5878   5785    267    -66    -65       N  
ATOM   4393  CA  GLY B 502      32.020  29.424 -13.995  1.00 45.48           C  
ANISOU 4393  CA  GLY B 502     6015   5774   5489    356   -236    -33       C  
ATOM   4394  C   GLY B 502      33.436  28.914 -14.131  1.00 45.43           C  
ANISOU 4394  C   GLY B 502     5994   5607   5661    563   -328    -67       C  
ATOM   4395  O   GLY B 502      33.665  27.943 -14.855  1.00 46.85           O  
ANISOU 4395  O   GLY B 502     6183   5709   5910    677   -347   -123       O  
ATOM   4396  N   GLY B 503      34.385  29.580 -13.478  1.00 44.64           N  
ANISOU 4396  N   GLY B 503     5790   5417   5754    820   -337     84       N  
ATOM   4397  CA  GLY B 503      35.786  29.205 -13.578  1.00 44.05           C  
ANISOU 4397  CA  GLY B 503     5516   5265   5955   1120    -95    344       C  
ATOM   4398  C   GLY B 503      35.961  27.699 -13.673  1.00 42.69           C  
ANISOU 4398  C   GLY B 503     5299   5065   5855   1347     66    716       C  
ATOM   4399  O   GLY B 503      35.119  26.943 -13.185  1.00 44.94           O  
ANISOU 4399  O   GLY B 503     5519   5103   6451   1243    161    785       O  
ATOM   4400  N   GLY B 504      37.045  27.263 -14.307  1.00 37.42           N  
ANISOU 4400  N   GLY B 504     4800   4820   4597   1786     31    870       N  
ATOM   4401  CA  GLY B 504      37.321  25.845 -14.466  1.00 30.93           C  
ANISOU 4401  CA  GLY B 504     4229   4342   3182   1864   -156   1023       C  
ATOM   4402  C   GLY B 504      37.242  25.045 -13.177  1.00 28.58           C  
ANISOU 4402  C   GLY B 504     3699   4227   2931   1799   -127    667       C  
ATOM   4403  O   GLY B 504      36.433  25.334 -12.294  1.00 29.73           O  
ANISOU 4403  O   GLY B 504     3490   4445   3361   2014   -175    464       O  
ATOM   4404  N   PRO B 505      38.095  24.025 -13.053  1.00 25.72           N  
ANISOU 4404  N   PRO B 505     3468   3714   2591   1676   -153    483       N  
ATOM   4405  CA  PRO B 505      38.018  23.119 -11.902  1.00 24.25           C  
ANISOU 4405  CA  PRO B 505     3394   3511   2309   1556   -296    282       C  
ATOM   4406  C   PRO B 505      38.307  23.818 -10.573  1.00 23.34           C  
ANISOU 4406  C   PRO B 505     3099   3239   2530   1510     51    219       C  
ATOM   4407  O   PRO B 505      38.001  23.271  -9.516  1.00 20.81           O  
ANISOU 4407  O   PRO B 505     2743   2920   2245   1230    128    397       O  
ATOM   4408  CB  PRO B 505      39.099  22.079 -12.205  1.00 24.61           C  
ANISOU 4408  CB  PRO B 505     3436   3443   2470   1618    309    -56       C  
ATOM   4409  CG  PRO B 505      40.055  22.782 -13.104  1.00 25.12           C  
ANISOU 4409  CG  PRO B 505     3579   3409   2554   1554    151    235       C  
ATOM   4410  CD  PRO B 505      39.216  23.695 -13.948  1.00 25.21           C  
ANISOU 4410  CD  PRO B 505     3540   3587   2452   1507    314    392       C  
ATOM   4411  N   GLN B 506      38.878  25.016 -10.628  1.00 22.21           N  
ANISOU 4411  N   GLN B 506     3278   3067   2094   1737   -114   -171       N  
ATOM   4412  CA  GLN B 506      39.221  25.750  -9.416  1.00 24.59           C  
ANISOU 4412  CA  GLN B 506     3521   3335   2487   2003     27    235       C  
ATOM   4413  C   GLN B 506      37.992  26.111  -8.585  1.00 25.53           C  
ANISOU 4413  C   GLN B 506     3640   3391   2670   1906    -88     55       C  
ATOM   4414  O   GLN B 506      38.097  26.360  -7.383  1.00 26.53           O  
ANISOU 4414  O   GLN B 506     3870   3373   2837   1857    -53   -121       O  
ATOM   4415  CB  GLN B 506      40.013  27.013  -9.762  1.00 29.96           C  
ANISOU 4415  CB  GLN B 506     3851   3693   3840   2134     82    683       C  
ATOM   4416  CG  GLN B 506      41.306  26.756 -10.519  1.00 34.21           C  
ANISOU 4416  CG  GLN B 506     4324   4275   4398   2211    -77    885       C  
ATOM   4417  CD  GLN B 506      41.242  27.127 -11.997  1.00 32.83           C  
ANISOU 4417  CD  GLN B 506     4238   4548   3686   2376     94    941       C  
ATOM   4418  OE1 GLN B 506      40.226  26.912 -12.670  1.00 31.84           O  
ANISOU 4418  OE1 GLN B 506     4264   4714   3118   2022   -412    828       O  
ATOM   4419  NE2 GLN B 506      42.344  27.684 -12.512  1.00 27.12           N  
ANISOU 4419  NE2 GLN B 506     3720   3969   2615   2153   1025    924       N  
ATOM   4420  N   THR B 507      36.829  26.140  -9.229  1.00 25.50           N  
ANISOU 4420  N   THR B 507     3500   3431   2756   1989    140    502       N  
ATOM   4421  CA  THR B 507      35.596  26.517  -8.552  1.00 27.63           C  
ANISOU 4421  CA  THR B 507     3358   3709   3429   1966    162    778       C  
ATOM   4422  C   THR B 507      34.876  25.324  -7.937  1.00 26.21           C  
ANISOU 4422  C   THR B 507     3122   3756   3079   1963    371    587       C  
ATOM   4423  O   THR B 507      33.871  25.484  -7.240  1.00 29.61           O  
ANISOU 4423  O   THR B 507     3200   4008   4042   1956    866    573       O  
ATOM   4424  CB  THR B 507      34.627  27.226  -9.519  1.00 31.19           C  
ANISOU 4424  CB  THR B 507     3599   4089   4161   2135    206    886       C  
ATOM   4425  OG1 THR B 507      34.210  26.307 -10.539  1.00 33.26           O  
ANISOU 4425  OG1 THR B 507     3749   4382   4504   2085   -223    806       O  
ATOM   4426  CG2 THR B 507      35.303  28.426 -10.167  1.00 34.65           C  
ANISOU 4426  CG2 THR B 507     3829   4334   5000   2278    344    914       C  
ATOM   4427  N   LEU B 508      35.391  24.124  -8.191  1.00 24.03           N  
ANISOU 4427  N   LEU B 508     2897   3574   2657   1767    -22    583       N  
ATOM   4428  CA  LEU B 508      34.770  22.913  -7.670  1.00 21.94           C  
ANISOU 4428  CA  LEU B 508     2655   3519   2163   1525    161    278       C  
ATOM   4429  C   LEU B 508      35.100  22.723  -6.192  1.00 20.36           C  
ANISOU 4429  C   LEU B 508     2415   3359   1961   1329    -40    -44       C  
ATOM   4430  O   LEU B 508      36.164  23.137  -5.726  1.00 21.98           O  
ANISOU 4430  O   LEU B 508     2528   3489   2335   1361    -22     80       O  
ATOM   4431  CB  LEU B 508      35.240  21.690  -8.469  1.00 20.71           C  
ANISOU 4431  CB  LEU B 508     2544   3444   1879   1361    148   -123       C  
ATOM   4432  CG  LEU B 508      34.815  21.659  -9.940  1.00 23.36           C  
ANISOU 4432  CG  LEU B 508     2565   3977   2332   1321   -328      3       C  
ATOM   4433  CD1 LEU B 508      35.481  20.502 -10.675  1.00 23.92           C  
ANISOU 4433  CD1 LEU B 508     2922   3885   2279   1427   -130    -60       C  
ATOM   4434  CD2 LEU B 508      33.295  21.583 -10.065  1.00 27.23           C  
ANISOU 4434  CD2 LEU B 508     2762   4356   3229   1183    -55   -216       C  
ATOM   4435  N   PRO B 509      34.184  22.094  -5.445  1.00 20.60           N  
ANISOU 4435  N   PRO B 509     2041   3458   2329   1317     60   -130       N  
ATOM   4436  CA  PRO B 509      34.505  21.702  -4.072  1.00 20.16           C  
ANISOU 4436  CA  PRO B 509     1814   3409   2436   1086   -118    142       C  
ATOM   4437  C   PRO B 509      35.720  20.779  -4.108  1.00 18.21           C  
ANISOU 4437  C   PRO B 509     1760   3101   2057   1102    -16   -143       C  
ATOM   4438  O   PRO B 509      35.917  20.071  -5.097  1.00 19.96           O  
ANISOU 4438  O   PRO B 509     1843   3286   2455   1097   -263     -3       O  
ATOM   4439  CB  PRO B 509      33.262  20.925  -3.628  1.00 23.16           C  
ANISOU 4439  CB  PRO B 509     1890   3729   3181    998     25    431       C  
ATOM   4440  CG  PRO B 509      32.173  21.355  -4.563  1.00 26.10           C  
ANISOU 4440  CG  PRO B 509     2463   3950   3503   1141   -135    138       C  
ATOM   4441  CD  PRO B 509      32.852  21.626  -5.863  1.00 23.71           C  
ANISOU 4441  CD  PRO B 509     2230   3797   2981   1172    121    217       C  
ATOM   4442  N   ILE B 510      36.521  20.787  -3.050  1.00 16.84           N  
ANISOU 4442  N   ILE B 510     1290   2897   2212    862    -34    339       N  
ATOM   4443  CA  ILE B 510      37.756  20.009  -3.052  1.00 16.76           C  
ANISOU 4443  CA  ILE B 510     1362   2848   2157    775    -63    383       C  
ATOM   4444  C   ILE B 510      37.622  18.659  -2.348  1.00 16.66           C  
ANISOU 4444  C   ILE B 510     1412   3031   1886    702    144    139       C  
ATOM   4445  O   ILE B 510      38.604  17.922  -2.227  1.00 17.55           O  
ANISOU 4445  O   ILE B 510     1403   2979   2286    758    -31    370       O  
ATOM   4446  CB  ILE B 510      38.931  20.802  -2.438  1.00 16.36           C  
ANISOU 4446  CB  ILE B 510     1791   2932   1493    628     -9    254       C  
ATOM   4447  CG1 ILE B 510      38.672  21.089  -0.960  1.00 17.91           C  
ANISOU 4447  CG1 ILE B 510     1701   3245   1858    568   -243     -4       C  
ATOM   4448  CG2 ILE B 510      39.165  22.096  -3.219  1.00 19.44           C  
ANISOU 4448  CG2 ILE B 510     2257   3142   1987    752    -69    757       C  
ATOM   4449  CD1 ILE B 510      39.871  21.679  -0.247  1.00 19.39           C  
ANISOU 4449  CD1 ILE B 510     2179   3296   1890    623   -255    180       C  
ATOM   4450  N   ASN B 511      36.411  18.330  -1.902  1.00 17.65           N  
ANISOU 4450  N   ASN B 511     1630   3114   1961    590    -83    317       N  
ATOM   4451  CA  ASN B 511      36.181  17.087  -1.168  1.00 19.19           C  
ANISOU 4451  CA  ASN B 511     1754   3234   2302    413    281    205       C  
ATOM   4452  C   ASN B 511      35.477  16.011  -1.993  1.00 19.38           C  
ANISOU 4452  C   ASN B 511     1617   3229   2517    369    -54    302       C  
ATOM   4453  O   ASN B 511      34.909  15.063  -1.448  1.00 19.14           O  
ANISOU 4453  O   ASN B 511     1712   3221   2340    259   -206    299       O  
ATOM   4454  CB  ASN B 511      35.416  17.353   0.133  1.00 21.64           C  
ANISOU 4454  CB  ASN B 511     1989   3703   2530    639    706    322       C  
ATOM   4455  CG  ASN B 511      34.002  17.849  -0.109  1.00 24.29           C  
ANISOU 4455  CG  ASN B 511     2163   4066   2998    715   1028    414       C  
ATOM   4456  OD1 ASN B 511      33.678  18.338  -1.190  1.00 24.02           O  
ANISOU 4456  OD1 ASN B 511     2018   4053   3055    557    707    -80       O  
ATOM   4457  ND2 ASN B 511      33.155  17.729   0.906  1.00 28.00           N  
ANISOU 4457  ND2 ASN B 511     2547   4373   3718    882   1092    798       N  
ATOM   4458  N   GLY B 512      35.521  16.165  -3.311  1.00 17.83           N  
ANISOU 4458  N   GLY B 512     1429   3034   2309    406   -129     57       N  
ATOM   4459  CA  GLY B 512      34.930  15.195  -4.211  1.00 17.62           C  
ANISOU 4459  CA  GLY B 512     1342   2921   2432    388   -214    261       C  
ATOM   4460  C   GLY B 512      35.792  13.959  -4.394  1.00 16.22           C  
ANISOU 4460  C   GLY B 512     1359   2770   2034    131   -435    219       C  
ATOM   4461  O   GLY B 512      36.969  13.926  -4.005  1.00 17.11           O  
ANISOU 4461  O   GLY B 512     1527   2716   2256    128   -482    353       O  
ATOM   4462  N   VAL B 513      35.200  12.942  -5.007  1.00 17.17           N  
ANISOU 4462  N   VAL B 513     1428   2841   2256    -14   -179    271       N  
ATOM   4463  CA  VAL B 513      35.884  11.686  -5.263  1.00 17.82           C  
ANISOU 4463  CA  VAL B 513     1655   2852   2264   -296   -146    493       C  
ATOM   4464  C   VAL B 513      35.908  11.408  -6.761  1.00 16.85           C  
ANISOU 4464  C   VAL B 513     1469   2805   2127   -216    -53    595       C  
ATOM   4465  O   VAL B 513      34.877  11.481  -7.429  1.00 17.75           O  
ANISOU 4465  O   VAL B 513     1273   3115   2357   -183   -354    331       O  
ATOM   4466  CB  VAL B 513      35.178  10.529  -4.534  1.00 19.96           C  
ANISOU 4466  CB  VAL B 513     1986   3201   2398   -330   -105    764       C  
ATOM   4467  CG1 VAL B 513      35.822   9.194  -4.895  1.00 21.46           C  
ANISOU 4467  CG1 VAL B 513     2323   2993   2837   -201   -100   1033       C  
ATOM   4468  CG2 VAL B 513      35.214  10.759  -3.030  1.00 19.63           C  
ANISOU 4468  CG2 VAL B 513     2183   3375   1898   -350   -131    691       C  
ATOM   4469  N   PHE B 514      37.083  11.101  -7.298  1.00 15.61           N  
ANISOU 4469  N   PHE B 514     1353   2648   1930     26    -51    377       N  
ATOM   4470  CA  PHE B 514      37.175  10.750  -8.706  1.00 15.52           C  
ANISOU 4470  CA  PHE B 514     1364   2302   2231   -126     46    356       C  
ATOM   4471  C   PHE B 514      36.749   9.308  -8.891  1.00 15.58           C  
ANISOU 4471  C   PHE B 514     1435   2355   2129   -323   -395    374       C  
ATOM   4472  O   PHE B 514      37.117   8.437  -8.099  1.00 16.21           O  
ANISOU 4472  O   PHE B 514     1571   2392   2195   -132   -227    384       O  
ATOM   4473  CB  PHE B 514      38.596  10.936  -9.235  1.00 15.38           C  
ANISOU 4473  CB  PHE B 514     1341   2305   2197    -24     22    418       C  
ATOM   4474  CG  PHE B 514      39.043  12.366  -9.290  1.00 14.80           C  
ANISOU 4474  CG  PHE B 514     1369   2215   2037     70   -239    372       C  
ATOM   4475  CD1 PHE B 514      38.776  13.144 -10.409  1.00 14.74           C  
ANISOU 4475  CD1 PHE B 514     1334   2246   2020    -94   -263     49       C  
ATOM   4476  CD2 PHE B 514      39.734  12.933  -8.232  1.00 16.12           C  
ANISOU 4476  CD2 PHE B 514     1136   2331   2659     43   -276   -179       C  
ATOM   4477  CE1 PHE B 514      39.185  14.463 -10.469  1.00 16.43           C  
ANISOU 4477  CE1 PHE B 514     1355   2119   2769    -50    -42    267       C  
ATOM   4478  CE2 PHE B 514      40.153  14.250  -8.284  1.00 15.84           C  
ANISOU 4478  CE2 PHE B 514     1308   2510   2200    224    -88    345       C  
ATOM   4479  CZ  PHE B 514      39.875  15.019  -9.401  1.00 16.19           C  
ANISOU 4479  CZ  PHE B 514     1380   2351   2421     48     -4   -159       C  
ATOM   4480  N   VAL B 515      35.966   9.059  -9.936  1.00 15.93           N  
ANISOU 4480  N   VAL B 515     1504   2511   2036   -383   -325    -67       N  
ATOM   4481  CA  VAL B 515      35.488   7.716 -10.231  1.00 17.65           C  
ANISOU 4481  CA  VAL B 515     1699   2830   2177   -550    -54    108       C  
ATOM   4482  C   VAL B 515      35.691   7.410 -11.708  1.00 17.39           C  
ANISOU 4482  C   VAL B 515     1712   2560   2335   -525   -229    146       C  
ATOM   4483  O   VAL B 515      35.275   8.188 -12.564  1.00 17.22           O  
ANISOU 4483  O   VAL B 515     1675   2634   2232   -252   -264    497       O  
ATOM   4484  CB  VAL B 515      33.986   7.570  -9.891  1.00 20.51           C  
ANISOU 4484  CB  VAL B 515     2032   3203   2556   -739    238     39       C  
ATOM   4485  CG1 VAL B 515      33.518   6.150 -10.154  1.00 21.10           C  
ANISOU 4485  CG1 VAL B 515     2275   3216   2525   -959     50   -169       C  
ATOM   4486  CG2 VAL B 515      33.724   7.954  -8.437  1.00 21.86           C  
ANISOU 4486  CG2 VAL B 515     2064   3563   2678   -581    361    472       C  
ATOM   4487  N   PHE B 516      36.343   6.285 -11.997  1.00 16.64           N  
ANISOU 4487  N   PHE B 516     1828   2445   2050   -584   -402    264       N  
ATOM   4488  CA  PHE B 516      36.507   5.803 -13.364  1.00 17.83           C  
ANISOU 4488  CA  PHE B 516     1926   2545   2304   -696   -615    255       C  
ATOM   4489  C   PHE B 516      35.175   5.325 -13.931  1.00 19.68           C  
ANISOU 4489  C   PHE B 516     2156   2818   2502   -824   -512    652       C  
ATOM   4490  O   PHE B 516      34.511   4.464 -13.343  1.00 21.49           O  
ANISOU 4490  O   PHE B 516     2443   3155   2567   -950   -509    410       O  
ATOM   4491  CB  PHE B 516      37.528   4.665 -13.407  1.00 18.38           C  
ANISOU 4491  CB  PHE B 516     2264   2329   2391   -227   -661    270       C  
ATOM   4492  CG  PHE B 516      37.647   3.998 -14.749  1.00 18.69           C  
ANISOU 4492  CG  PHE B 516     2432   2220   2447   -314   -637    423       C  
ATOM   4493  CD1 PHE B 516      38.125   4.692 -15.847  1.00 19.24           C  
ANISOU 4493  CD1 PHE B 516     2291   2522   2495   -371   -891     23       C  
ATOM   4494  CD2 PHE B 516      37.316   2.663 -14.903  1.00 19.13           C  
ANISOU 4494  CD2 PHE B 516     2828   2101   2337   -318   -685    176       C  
ATOM   4495  CE1 PHE B 516      38.253   4.074 -17.078  1.00 19.16           C  
ANISOU 4495  CE1 PHE B 516     2363   2399   2518   -509   -847     71       C  
ATOM   4496  CE2 PHE B 516      37.443   2.034 -16.129  1.00 19.30           C  
ANISOU 4496  CE2 PHE B 516     2900   2212   2221   -281   -582    383       C  
ATOM   4497  CZ  PHE B 516      37.911   2.744 -17.221  1.00 19.28           C  
ANISOU 4497  CZ  PHE B 516     2692   2358   2274   -348   -715   -183       C  
ATOM   4498  N   ILE B 517      34.791   5.891 -15.070  1.00 18.60           N  
ANISOU 4498  N   ILE B 517     1869   2825   2374   -878   -839    552       N  
ATOM   4499  CA  ILE B 517      33.534   5.552 -15.721  1.00 20.10           C  
ANISOU 4499  CA  ILE B 517     2056   3048   2534   -757   -733    426       C  
ATOM   4500  C   ILE B 517      33.758   4.568 -16.861  1.00 20.07           C  
ANISOU 4500  C   ILE B 517     2201   2958   2467  -1194   -648    324       C  
ATOM   4501  O   ILE B 517      33.114   3.521 -16.929  1.00 22.80           O  
ANISOU 4501  O   ILE B 517     2530   3185   2949   -976   -628    336       O  
ATOM   4502  CB  ILE B 517      32.865   6.810 -16.288  1.00 20.75           C  
ANISOU 4502  CB  ILE B 517     1797   3537   2551   -525   -877    288       C  
ATOM   4503  CG1 ILE B 517      32.634   7.838 -15.177  1.00 20.96           C  
ANISOU 4503  CG1 ILE B 517     1904   3571   2489   -544   -525    342       C  
ATOM   4504  CG2 ILE B 517      31.553   6.458 -16.977  1.00 21.76           C  
ANISOU 4504  CG2 ILE B 517     1601   3782   2885   -522   -817    469       C  
ATOM   4505  CD1 ILE B 517      31.815   7.308 -14.012  1.00 22.82           C  
ANISOU 4505  CD1 ILE B 517     1984   3795   2889   -337   -327    364       C  
ATOM   4506  N   SER B 518      34.675   4.905 -17.760  1.00 19.94           N  
ANISOU 4506  N   SER B 518     2239   3070   2268  -1068   -632    119       N  
ATOM   4507  CA  SER B 518      34.880   4.100 -18.951  1.00 20.71           C  
ANISOU 4507  CA  SER B 518     2366   3239   2263  -1159   -762    143       C  
ATOM   4508  C   SER B 518      36.138   4.474 -19.713  1.00 20.51           C  
ANISOU 4508  C   SER B 518     2524   2945   2322   -908   -569    350       C  
ATOM   4509  O   SER B 518      36.616   5.605 -19.636  1.00 20.02           O  
ANISOU 4509  O   SER B 518     2539   2777   2290   -774   -530    222       O  
ATOM   4510  CB  SER B 518      33.684   4.263 -19.890  1.00 23.91           C  
ANISOU 4510  CB  SER B 518     2655   4005   2423   -972   -711   -724       C  
ATOM   4511  OG  SER B 518      33.863   3.493 -21.060  1.00 29.61           O  
ANISOU 4511  OG  SER B 518     2996   4723   3531   -581   -759   -166       O  
ATOM   4512  N   TRP B 519      36.664   3.513 -20.464  1.00 20.69           N  
ANISOU 4512  N   TRP B 519     2584   2918   2357   -649   -491    332       N  
ATOM   4513  CA  TRP B 519      37.676   3.821 -21.463  1.00 20.04           C  
ANISOU 4513  CA  TRP B 519     2607   2647   2358   -655   -953      2       C  
ATOM   4514  C   TRP B 519      36.996   4.512 -22.634  1.00 20.61           C  
ANISOU 4514  C   TRP B 519     2719   2789   2322   -654   -780    171       C  
ATOM   4515  O   TRP B 519      35.946   4.068 -23.103  1.00 23.61           O  
ANISOU 4515  O   TRP B 519     2672   3225   3072   -739   -989    335       O  
ATOM   4516  CB  TRP B 519      38.398   2.556 -21.932  1.00 20.69           C  
ANISOU 4516  CB  TRP B 519     2809   2555   2495   -455   -650    -80       C  
ATOM   4517  CG  TRP B 519      39.255   1.941 -20.867  1.00 20.04           C  
ANISOU 4517  CG  TRP B 519     3020   2454   2141   -309   -638    331       C  
ATOM   4518  CD1 TRP B 519      39.012   0.786 -20.179  1.00 22.29           C  
ANISOU 4518  CD1 TRP B 519     3235   2578   2656   -131   -618    170       C  
ATOM   4519  CD2 TRP B 519      40.485   2.459 -20.355  1.00 19.68           C  
ANISOU 4519  CD2 TRP B 519     2938   2346   2192   -301   -844     94       C  
ATOM   4520  NE1 TRP B 519      40.023   0.548 -19.278  1.00 23.08           N  
ANISOU 4520  NE1 TRP B 519     3168   2601   2998   -188   -758     -9       N  
ATOM   4521  CE2 TRP B 519      40.938   1.565 -19.364  1.00 20.59           C  
ANISOU 4521  CE2 TRP B 519     3004   2269   2550   -320   -751    272       C  
ATOM   4522  CE3 TRP B 519      41.252   3.593 -20.642  1.00 19.50           C  
ANISOU 4522  CE3 TRP B 519     2828   2208   2372   -245   -692   -154       C  
ATOM   4523  CZ2 TRP B 519      42.123   1.767 -18.662  1.00 20.72           C  
ANISOU 4523  CZ2 TRP B 519     2960   2395   2517    -50   -784    111       C  
ATOM   4524  CZ3 TRP B 519      42.423   3.798 -19.936  1.00 20.32           C  
ANISOU 4524  CZ3 TRP B 519     2825   2403   2491    -52   -540   -108       C  
ATOM   4525  CH2 TRP B 519      42.850   2.887 -18.961  1.00 20.70           C  
ANISOU 4525  CH2 TRP B 519     2831   2361   2672    -33   -602    120       C  
ATOM   4526  N   VAL B 520      37.591   5.608 -23.088  1.00 20.08           N  
ANISOU 4526  N   VAL B 520     2862   2679   2086   -593   -762    414       N  
ATOM   4527  CA  VAL B 520      37.059   6.353 -24.217  1.00 21.51           C  
ANISOU 4527  CA  VAL B 520     2959   2912   2303   -662   -795    331       C  
ATOM   4528  C   VAL B 520      38.161   6.703 -25.206  1.00 21.16           C  
ANISOU 4528  C   VAL B 520     3267   2895   1879   -494   -708    456       C  
ATOM   4529  O   VAL B 520      39.358   6.540 -24.925  1.00 22.09           O  
ANISOU 4529  O   VAL B 520     3289   2822   2281   -264   -401    358       O  
ATOM   4530  CB  VAL B 520      36.340   7.655 -23.774  1.00 22.16           C  
ANISOU 4530  CB  VAL B 520     2865   3110   2445   -841   -701    229       C  
ATOM   4531  CG1 VAL B 520      35.156   7.333 -22.866  1.00 23.32           C  
ANISOU 4531  CG1 VAL B 520     2933   3323   2605   -782   -508    401       C  
ATOM   4532  CG2 VAL B 520      37.314   8.606 -23.077  1.00 20.74           C  
ANISOU 4532  CG2 VAL B 520     2884   2896   2101   -816   -490     41       C  
ATOM   4533  N   SER B 521      37.741   7.191 -26.366  1.00 22.87           N  
ANISOU 4533  N   SER B 521     3620   2908   2159   -449   -648    299       N  
ATOM   4534  CA  SER B 521      38.653   7.657 -27.392  1.00 23.53           C  
ANISOU 4534  CA  SER B 521     3786   3153   2002   -527   -663    123       C  
ATOM   4535  C   SER B 521      39.448   8.865 -26.899  1.00 22.33           C  
ANISOU 4535  C   SER B 521     3563   3139   1783   -510   -468    358       C  
ATOM   4536  O   SER B 521      38.980   9.620 -26.045  1.00 21.61           O  
ANISOU 4536  O   SER B 521     3410   3017   1784   -445   -484    106       O  
ATOM   4537  CB  SER B 521      37.855   8.032 -28.641  1.00 25.98           C  
ANISOU 4537  CB  SER B 521     4074   3487   2311   -731   -940      9       C  
ATOM   4538  OG  SER B 521      38.650   8.764 -29.541  1.00 27.92           O  
ANISOU 4538  OG  SER B 521     4317   3300   2989   -741  -1081    275       O  
ATOM   4539  N   ARG B 522      40.649   9.054 -27.440  1.00 22.20           N  
ANISOU 4539  N   ARG B 522     3419   3216   1801   -366   -462    111       N  
ATOM   4540  CA  ARG B 522      41.440  10.227 -27.094  1.00 25.29           C  
ANISOU 4540  CA  ARG B 522     3569   3300   2738   -172   -255     26       C  
ATOM   4541  C   ARG B 522      40.714  11.480 -27.564  1.00 22.99           C  
ANISOU 4541  C   ARG B 522     3421   3177   2136   -303   -203     55       C  
ATOM   4542  O   ARG B 522      41.019  12.587 -27.121  1.00 23.84           O  
ANISOU 4542  O   ARG B 522     3481   3001   2574   -269   -223   -373       O  
ATOM   4543  CB  ARG B 522      42.842  10.155 -27.711  1.00 31.75           C  
ANISOU 4543  CB  ARG B 522     4004   3889   4168    185     38    418       C  
ATOM   4544  CG  ARG B 522      42.869  10.233 -29.227  1.00 38.54           C  
ANISOU 4544  CG  ARG B 522     4499   4426   5716    531    241    444       C  
ATOM   4545  CD  ARG B 522      44.289  10.095 -29.761  1.00 44.82           C  
ANISOU 4545  CD  ARG B 522     5078   4873   7076    970    176    540       C  
ATOM   4546  NE  ARG B 522      45.143  11.206 -29.353  1.00 49.07           N  
ANISOU 4546  NE  ARG B 522     5577   5280   7785   1396     48    747       N  
ATOM   4547  CZ  ARG B 522      45.553  12.176 -30.165  1.00 51.53           C  
ANISOU 4547  CZ  ARG B 522     5930   5682   7965   1827   -211    781       C  
ATOM   4548  NH1 ARG B 522      45.199  12.178 -31.443  1.00 51.67           N  
ANISOU 4548  NH1 ARG B 522     6078   5771   7783   2022   -250    815       N  
ATOM   4549  NH2 ARG B 522      46.328  13.145 -29.698  1.00 53.12           N  
ANISOU 4549  NH2 ARG B 522     6089   5733   8359   2031   -244    762       N  
ATOM   4550  N   TYR B 523      39.740  11.291 -28.453  1.00 21.72           N  
ANISOU 4550  N   TYR B 523     3221   3031   2000   -335   -158    270       N  
ATOM   4551  CA  TYR B 523      39.001  12.402 -29.040  1.00 20.73           C  
ANISOU 4551  CA  TYR B 523     3100   3031   1743   -338   -130    161       C  
ATOM   4552  C   TYR B 523      37.662  12.636 -28.356  1.00 22.25           C  
ANISOU 4552  C   TYR B 523     3048   3194   2212   -140   -141    325       C  
ATOM   4553  O   TYR B 523      36.866  13.465 -28.803  1.00 24.30           O  
ANISOU 4553  O   TYR B 523     3177   3609   2445    306    -53    304       O  
ATOM   4554  CB  TYR B 523      38.777  12.153 -30.532  1.00 22.14           C  
ANISOU 4554  CB  TYR B 523     3185   3143   2082   -195   -142    257       C  
ATOM   4555  CG  TYR B 523      40.038  11.785 -31.275  1.00 24.37           C  
ANISOU 4555  CG  TYR B 523     3376   3534   2350     69     27    495       C  
ATOM   4556  CD1 TYR B 523      40.292  10.467 -31.636  1.00 27.01           C  
ANISOU 4556  CD1 TYR B 523     3481   3727   3055    109     31    520       C  
ATOM   4557  CD2 TYR B 523      40.978  12.749 -31.608  1.00 25.53           C  
ANISOU 4557  CD2 TYR B 523     3375   3805   2519     99    120    739       C  
ATOM   4558  CE1 TYR B 523      41.445  10.121 -32.317  1.00 27.11           C  
ANISOU 4558  CE1 TYR B 523     3567   3903   2830    182     62    326       C  
ATOM   4559  CE2 TYR B 523      42.137  12.412 -32.287  1.00 27.88           C  
ANISOU 4559  CE2 TYR B 523     3460   4075   3059    324    177    651       C  
ATOM   4560  CZ  TYR B 523      42.364  11.096 -32.638  1.00 28.93           C  
ANISOU 4560  CZ  TYR B 523     3579   4065   3349    271    370    711       C  
ATOM   4561  OH  TYR B 523      43.511  10.756 -33.315  1.00 33.10           O  
ANISOU 4561  OH  TYR B 523     3799   4402   4375    473    464    697       O  
ATOM   4562  N   TYR B 524      37.413  11.901 -27.277  1.00 21.27           N  
ANISOU 4562  N   TYR B 524     2923   3046   2112   -137   -117    299       N  
ATOM   4563  CA  TYR B 524      36.172  12.052 -26.527  1.00 22.01           C  
ANISOU 4563  CA  TYR B 524     2911   3357   2095    279   -272    586       C  
ATOM   4564  C   TYR B 524      35.937  13.510 -26.147  1.00 23.37           C  
ANISOU 4564  C   TYR B 524     3008   3461   2411    547   -361    333       C  
ATOM   4565  O   TYR B 524      36.830  14.181 -25.621  1.00 23.05           O  
ANISOU 4565  O   TYR B 524     3092   3181   2484    660   -611     83       O  
ATOM   4566  CB  TYR B 524      36.191  11.174 -25.279  1.00 23.39           C  
ANISOU 4566  CB  TYR B 524     2825   3881   2180    133   -230   1101       C  
ATOM   4567  CG  TYR B 524      34.909  11.215 -24.482  1.00 26.96           C  
ANISOU 4567  CG  TYR B 524     2875   4751   2616    416   -132   1144       C  
ATOM   4568  CD1 TYR B 524      33.862  10.351 -24.773  1.00 28.68           C  
ANISOU 4568  CD1 TYR B 524     2826   5028   3044    380   -183   1243       C  
ATOM   4569  CD2 TYR B 524      34.745  12.113 -23.433  1.00 27.99           C  
ANISOU 4569  CD2 TYR B 524     2933   5171   2532    517   -170   1039       C  
ATOM   4570  CE1 TYR B 524      32.687  10.384 -24.048  1.00 31.42           C  
ANISOU 4570  CE1 TYR B 524     2940   5360   3639    379    -91   1200       C  
ATOM   4571  CE2 TYR B 524      33.570  12.154 -22.703  1.00 29.87           C  
ANISOU 4571  CE2 TYR B 524     2991   5520   2839    453     17   1333       C  
ATOM   4572  CZ  TYR B 524      32.546  11.285 -23.014  1.00 31.81           C  
ANISOU 4572  CZ  TYR B 524     2990   5641   3454    427    207   1436       C  
ATOM   4573  OH  TYR B 524      31.375  11.320 -22.288  1.00 34.93           O  
ANISOU 4573  OH  TYR B 524     3233   5971   4066    748    118   1620       O  
ATOM   4574  N   GLN B 525      34.725  13.990 -26.404  1.00 24.00           N  
ANISOU 4574  N   GLN B 525     2999   3737   2384    698   -595    580       N  
ATOM   4575  CA  GLN B 525      34.377  15.387 -26.163  1.00 23.74           C  
ANISOU 4575  CA  GLN B 525     2751   3938   2329    741   -588    646       C  
ATOM   4576  C   GLN B 525      33.813  15.617 -24.765  1.00 24.83           C  
ANISOU 4576  C   GLN B 525     2626   4120   2688    724   -436    493       C  
ATOM   4577  O   GLN B 525      32.720  15.146 -24.442  1.00 25.57           O  
ANISOU 4577  O   GLN B 525     2633   4189   2892    540   -302    318       O  
ATOM   4578  CB  GLN B 525      33.365  15.858 -27.209  1.00 26.49           C  
ANISOU 4578  CB  GLN B 525     2954   4197   2913    985   -689    661       C  
ATOM   4579  CG  GLN B 525      32.911  17.296 -27.037  1.00 27.11           C  
ANISOU 4579  CG  GLN B 525     3144   4294   2861    959   -243    939       C  
ATOM   4580  CD  GLN B 525      34.030  18.289 -27.276  1.00 28.55           C  
ANISOU 4580  CD  GLN B 525     3338   4656   2853   1181    117   1068       C  
ATOM   4581  OE1 GLN B 525      34.537  18.414 -28.393  1.00 30.32           O  
ANISOU 4581  OE1 GLN B 525     3454   4802   3262   1163    438   1065       O  
ATOM   4582  NE2 GLN B 525      34.425  19.000 -26.224  1.00 27.89           N  
ANISOU 4582  NE2 GLN B 525     3311   4557   2730   1178    -83    918       N  
ATOM   4583  N   LEU B 526      34.561  16.346 -23.943  1.00 23.09           N  
ANISOU 4583  N   LEU B 526     2562   3969   2240    846   -279    202       N  
ATOM   4584  CA  LEU B 526      34.100  16.744 -22.618  1.00 24.98           C  
ANISOU 4584  CA  LEU B 526     2624   4250   2615   1048   -347    323       C  
ATOM   4585  C   LEU B 526      33.133  17.914 -22.722  1.00 27.68           C  
ANISOU 4585  C   LEU B 526     2769   4585   3161   1200   -235    455       C  
ATOM   4586  O   LEU B 526      33.167  18.663 -23.700  1.00 28.71           O  
ANISOU 4586  O   LEU B 526     2900   4687   3320   1237   -182    391       O  
ATOM   4587  CB  LEU B 526      35.284  17.145 -21.739  1.00 23.57           C  
ANISOU 4587  CB  LEU B 526     2573   3932   2451    971   -828    260       C  
ATOM   4588  CG  LEU B 526      36.226  16.020 -21.312  1.00 24.68           C  
ANISOU 4588  CG  LEU B 526     2718   3780   2879    967   -537    523       C  
ATOM   4589  CD1 LEU B 526      37.471  16.585 -20.645  1.00 24.52           C  
ANISOU 4589  CD1 LEU B 526     2712   3739   2865    755   -758   -192       C  
ATOM   4590  CD2 LEU B 526      35.494  15.069 -20.385  1.00 28.34           C  
ANISOU 4590  CD2 LEU B 526     3011   3963   3792   1023   -351    666       C  
ATOM   4591  OXT LEU B 526      32.303  18.142 -21.840  1.00 29.60           O  
ANISOU 4591  OXT LEU B 526     2873   4720   3654   1334     -3    645       O  
TER    4592      LEU B 526                                                      
HETATM 4593  C1  FUC A 601      67.706  19.121  23.349  1.00 24.62           C  
ANISOU 4593  C1  FUC A 601     2724   2866   3765    285   -727   -958       C  
HETATM 4594  C2  FUC A 601      67.568  20.445  22.724  1.00 22.35           C  
ANISOU 4594  C2  FUC A 601     2710   2312   3469    -42   -621  -1240       C  
HETATM 4595  C3  FUC A 601      68.677  21.337  23.131  1.00 23.65           C  
ANISOU 4595  C3  FUC A 601     2766   2538   3681    -27   -261   -919       C  
HETATM 4596  C4  FUC A 601      70.015  20.759  22.839  1.00 23.99           C  
ANISOU 4596  C4  FUC A 601     2832   2705   3579    -29   -378  -1117       C  
HETATM 4597  C5  FUC A 601      70.154  19.347  23.378  1.00 23.99           C  
ANISOU 4597  C5  FUC A 601     2582   2754   3779     79   -647   -945       C  
HETATM 4598  C6  FUC A 601      71.430  18.717  22.970  1.00 24.53           C  
ANISOU 4598  C6  FUC A 601     2550   2860   3910    279   -553  -1207       C  
HETATM 4599  O2  FUC A 601      66.343  21.006  23.103  1.00 25.32           O  
ANISOU 4599  O2  FUC A 601     2512   2529   4577      7    -52   -854       O  
HETATM 4600  O3  FUC A 601      68.540  22.590  22.540  1.00 25.54           O  
ANISOU 4600  O3  FUC A 601     3110   2236   4359     57    184   -409       O  
HETATM 4601  O4  FUC A 601      70.230  20.749  21.469  1.00 24.68           O  
ANISOU 4601  O4  FUC A 601     2996   2851   3528    153   -286   -840       O  
HETATM 4602  O5  FUC A 601      69.051  18.516  23.001  1.00 23.73           O  
ANISOU 4602  O5  FUC A 601     2542   2958   3516     12   -946  -1220       O  
HETATM 4603  C1  GAL A 602      68.410  17.849  26.467  1.00 22.16           C  
ANISOU 4603  C1  GAL A 602     2615   3291   2513    187   -911   -325       C  
HETATM 4604  C2  GAL A 602      67.395  17.981  25.353  1.00 21.49           C  
ANISOU 4604  C2  GAL A 602     2659   3056   2451    214  -1011   -354       C  
HETATM 4605  C3  GAL A 602      66.003  17.850  25.852  1.00 19.57           C  
ANISOU 4605  C3  GAL A 602     2415   2626   2395     89   -961   -297       C  
HETATM 4606  C4  GAL A 602      65.818  16.666  26.619  1.00 19.39           C  
ANISOU 4606  C4  GAL A 602     2671   2644   2053    345   -776   -376       C  
HETATM 4607  C5  GAL A 602      66.808  16.630  27.738  1.00 20.68           C  
ANISOU 4607  C5  GAL A 602     2863   2938   2056    342  -1036   -172       C  
HETATM 4608  C6  GAL A 602      66.738  15.436  28.577  1.00 22.62           C  
ANISOU 4608  C6  GAL A 602     3084   3369   2142    379  -1404   -343       C  
HETATM 4609  O2  GAL A 602      67.578  19.246  24.723  1.00 25.31           O  
ANISOU 4609  O2  GAL A 602     2852   3017   3747    298   -985   -160       O  
HETATM 4610  O3  GAL A 602      65.080  17.921  24.747  1.00 18.79           O  
ANISOU 4610  O3  GAL A 602     2034   2158   2947    -37   -768   -454       O  
HETATM 4611  O4  GAL A 602      65.966  15.489  25.761  1.00 18.29           O  
ANISOU 4611  O4  GAL A 602     2544   2485   1920    393   -699   -817       O  
HETATM 4612  O5  GAL A 602      68.196  16.707  27.204  1.00 21.82           O  
ANISOU 4612  O5  GAL A 602     2695   3059   2535    407   -858   -750       O  
HETATM 4613  O6  GAL A 602      67.520  15.432  29.678  1.00 26.12           O  
ANISOU 4613  O6  GAL A 602     3572   3464   2887    620  -1214   -262       O  
HETATM 4614  C1  NDG A 603      73.423  18.443  27.730  1.00 41.48           C  
ANISOU 4614  C1  NDG A 603     4017   5777   5966    337  -2068   -539       C  
HETATM 4615  C2  NDG A 603      72.728  17.092  27.855  1.00 38.85           C  
ANISOU 4615  C2  NDG A 603     3833   5595   5334    251  -2485   -978       C  
HETATM 4616  C3  NDG A 603      71.735  16.951  26.811  1.00 32.56           C  
ANISOU 4616  C3  NDG A 603     3134   4872   4364     26  -1920  -1043       C  
HETATM 4617  C4  NDG A 603      70.780  17.984  26.915  1.00 31.06           C  
ANISOU 4617  C4  NDG A 603     3102   4698   4002     45  -1867   -941       C  
HETATM 4618  C5  NDG A 603      71.447  19.356  26.799  1.00 35.85           C  
ANISOU 4618  C5  NDG A 603     3459   5221   4942    123  -2139  -1109       C  
HETATM 4619  C6  NDG A 603      70.466  20.440  27.010  1.00 38.37           C  
ANISOU 4619  C6  NDG A 603     3848   5263   5466    401  -1790  -1366       C  
HETATM 4620  C7  NDG A 603      73.865  15.060  28.901  1.00 49.82           C  
ANISOU 4620  C7  NDG A 603     5078   6670   7179   1302  -2356   -366       C  
HETATM 4621  C8  NDG A 603      74.797  14.023  28.811  1.00 50.74           C  
ANISOU 4621  C8  NDG A 603     5065   6876   7336   1453  -2698   -171       C  
HETATM 4622  O   NDG A 603      72.502  19.497  27.770  1.00 38.39           O  
ANISOU 4622  O   NDG A 603     3619   5465   5501    -71  -2335  -1101       O  
HETATM 4623  O3  NDG A 603      71.089  15.591  26.872  1.00 29.57           O  
ANISOU 4623  O3  NDG A 603     2707   4731   3797    416  -1524  -1297       O  
HETATM 4624  O4  NDG A 603      69.704  17.827  25.936  1.00 26.40           O  
ANISOU 4624  O4  NDG A 603     2654   3861   3516   -144  -1028   -868       O  
HETATM 4625  O6  NDG A 603      69.853  20.518  28.331  1.00 39.82           O  
ANISOU 4625  O6  NDG A 603     4148   5321   5661    430  -1796  -1870       O  
HETATM 4626  O7  NDG A 603      73.182  15.177  29.925  1.00 52.09           O  
ANISOU 4626  O7  NDG A 603     5412   6876   7502   1312  -2138   -256       O  
HETATM 4627  N2  NDG A 603      73.705  15.989  27.795  1.00 44.84           N  
ANISOU 4627  N2  NDG A 603     4579   6132   6326    927  -2392   -577       N  
HETATM 4628  O1L NDG A 603      74.122  18.499  26.569  1.00 44.68           O  
ANISOU 4628  O1L NDG A 603     4399   6058   6517    630  -1848   -200       O  
HETATM 4629  C1  FUC A 604      71.586  14.627  25.969  1.00 27.36           C  
ANISOU 4629  C1  FUC A 604     2327   4719   3350    469  -1327   -854       C  
HETATM 4630  C2  FUC A 604      71.158  13.268  26.456  1.00 25.99           C  
ANISOU 4630  C2  FUC A 604     2325   4551   2998    740  -1248   -618       C  
HETATM 4631  C3  FUC A 604      69.687  13.173  26.454  1.00 24.76           C  
ANISOU 4631  C3  FUC A 604     2400   4289   2717    681  -1233   -765       C  
HETATM 4632  C4  FUC A 604      69.130  13.446  25.160  1.00 24.67           C  
ANISOU 4632  C4  FUC A 604     2381   4289   2701    757   -906   -814       C  
HETATM 4633  C5  FUC A 604      69.594  14.748  24.620  1.00 24.69           C  
ANISOU 4633  C5  FUC A 604     2122   4465   2792    393  -1129   -651       C  
HETATM 4634  C6  FUC A 604      69.180  14.928  23.249  1.00 25.13           C  
ANISOU 4634  C6  FUC A 604     1924   4496   3127    138  -1160   -407       C  
HETATM 4635  O2  FUC A 604      71.671  13.041  27.763  1.00 27.25           O  
ANISOU 4635  O2  FUC A 604     2371   4789   3193    937  -1071   -532       O  
HETATM 4636  O3  FUC A 604      69.274  11.873  26.937  1.00 26.70           O  
ANISOU 4636  O3  FUC A 604     2600   4329   3215   1065  -1078   -772       O  
HETATM 4637  O4  FUC A 604      69.483  12.401  24.225  1.00 25.09           O  
ANISOU 4637  O4  FUC A 604     2564   4052   2916   1011   -837   -829       O  
HETATM 4638  O5  FUC A 604      71.087  14.881  24.689  1.00 26.33           O  
ANISOU 4638  O5  FUC A 604     2046   4537   3422    192  -1221   -744       O  
HETATM 4639  C1  FUC B 601      67.190  33.370   2.680  1.00 26.76           C  
ANISOU 4639  C1  FUC B 601     3742   2627   3798   -581   -546   -925       C  
HETATM 4640  C2  FUC B 601      67.870  32.729   3.697  1.00 27.06           C  
ANISOU 4640  C2  FUC B 601     3475   3115   3690   -529   -125   -576       C  
HETATM 4641  C3  FUC B 601      68.430  33.596   4.800  1.00 27.19           C  
ANISOU 4641  C3  FUC B 601     3589   3333   3409   -751   -587   -728       C  
HETATM 4642  C4  FUC B 601      67.479  34.581   5.356  1.00 26.88           C  
ANISOU 4642  C4  FUC B 601     3637   3201   3376  -1010   -204   -185       C  
HETATM 4643  C5  FUC B 601      66.602  35.108   4.271  1.00 30.49           C  
ANISOU 4643  C5  FUC B 601     4048   3513   4024   -468   -297   -182       C  
HETATM 4644  C6  FUC B 601      65.499  35.922   4.806  1.00 33.18           C  
ANISOU 4644  C6  FUC B 601     4214   3775   4617   -114   -353    -39       C  
HETATM 4645  O2  FUC B 601      68.917  32.274   2.965  1.00 23.77           O  
ANISOU 4645  O2  FUC B 601     3049   2489   3493   -595     45   -519       O  
HETATM 4646  O3  FUC B 601      68.900  32.765   5.768  1.00 30.26           O  
ANISOU 4646  O3  FUC B 601     3945   3699   3851   -520   -362   -651       O  
HETATM 4647  O4  FUC B 601      66.632  34.037   6.292  1.00 28.72           O  
ANISOU 4647  O4  FUC B 601     3567   3899   3444   -569   -349   -133       O  
HETATM 4648  O5  FUC B 601      66.089  34.060   3.465  1.00 27.31           O  
ANISOU 4648  O5  FUC B 601     3889   2829   3659  -1128    118   -593       O  
HETATM 4649  C1  GAL B 602      67.467  35.884   0.386  1.00 19.34           C  
ANISOU 4649  C1  GAL B 602     3338   1211   2797   -609   -208    -12       C  
HETATM 4650  C2  GAL B 602      67.381  34.379   0.600  1.00 20.82           C  
ANISOU 4650  C2  GAL B 602     3383   1434   3092   -380   -527   -495       C  
HETATM 4651  C3  GAL B 602      67.829  33.621  -0.599  1.00 18.44           C  
ANISOU 4651  C3  GAL B 602     3016   1209   2782   -522   -315    -26       C  
HETATM 4652  C4  GAL B 602      67.238  34.082  -1.794  1.00 18.62           C  
ANISOU 4652  C4  GAL B 602     2860   1291   2922   -672   -128     42       C  
HETATM 4653  C5  GAL B 602      67.407  35.569  -1.901  1.00 19.01           C  
ANISOU 4653  C5  GAL B 602     3110   1176   2935   -459    237    232       C  
HETATM 4654  C6  GAL B 602      66.741  36.162  -3.044  1.00 19.88           C  
ANISOU 4654  C6  GAL B 602     3246   1132   3174   -460    118    598       C  
HETATM 4655  O2  GAL B 602      68.074  34.049   1.785  1.00 25.23           O  
ANISOU 4655  O2  GAL B 602     3867   2000   3719   -184   -726   -451       O  
HETATM 4656  O3  GAL B 602      67.597  32.202  -0.432  1.00 19.03           O  
ANISOU 4656  O3  GAL B 602     2651   1496   3083   -621   -617    -63       O  
HETATM 4657  O4  GAL B 602      65.843  33.741  -1.823  1.00 17.22           O  
ANISOU 4657  O4  GAL B 602     2680   1049   2815   -595     35   -119       O  
HETATM 4658  O5  GAL B 602      66.806  36.171  -0.727  1.00 19.02           O  
ANISOU 4658  O5  GAL B 602     3117   1202   2906   -550     87    -52       O  
HETATM 4659  O6  GAL B 602      67.011  37.495  -3.244  1.00 22.78           O  
ANISOU 4659  O6  GAL B 602     3744   1301   3608   -228    281    662       O  
HETATM 4660  C1  NDG B 603      67.332  40.178   3.199  1.00 31.20           C  
ANISOU 4660  C1  NDG B 603     4163   1993   5697   -840    334   -639       C  
HETATM 4661  C2  NDG B 603      66.284  40.082   2.143  1.00 28.77           C  
ANISOU 4661  C2  NDG B 603     4099   1739   5093   -791    149   -745       C  
HETATM 4662  C3  NDG B 603      65.997  38.647   1.883  1.00 25.28           C  
ANISOU 4662  C3  NDG B 603     3725   1461   4417   -787    297   -308       C  
HETATM 4663  C4  NDG B 603      67.187  37.929   1.658  1.00 24.10           C  
ANISOU 4663  C4  NDG B 603     3709   1517   3932   -712    158   -686       C  
HETATM 4664  C5  NDG B 603      68.199  38.122   2.773  1.00 27.56           C  
ANISOU 4664  C5  NDG B 603     3835   1858   4778   -888     46   -727       C  
HETATM 4665  C6  NDG B 603      69.487  37.517   2.523  1.00 29.42           C  
ANISOU 4665  C6  NDG B 603     3886   2199   5094   -828    213   -476       C  
HETATM 4666  C7  NDG B 603      64.577  41.862   1.970  1.00 35.20           C  
ANISOU 4666  C7  NDG B 603     4595   1987   6792   -121    423   -902       C  
HETATM 4667  C8  NDG B 603      63.454  42.485   2.451  1.00 36.82           C  
ANISOU 4667  C8  NDG B 603     4655   2068   7267    -67    458   -748       C  
HETATM 4668  O   NDG B 603      68.467  39.509   2.898  1.00 29.39           O  
ANISOU 4668  O   NDG B 603     4020   1919   5226   -877    142   -905       O  
HETATM 4669  O3  NDG B 603      65.076  38.480   0.737  1.00 23.43           O  
ANISOU 4669  O3  NDG B 603     3417   1390   4094   -786    373    -51       O  
HETATM 4670  O4  NDG B 603      66.907  36.501   1.469  1.00 21.58           O  
ANISOU 4670  O4  NDG B 603     3554   1457   3189   -665    118   -451       O  
HETATM 4671  O6  NDG B 603      70.148  37.866   1.308  1.00 33.85           O  
ANISOU 4671  O6  NDG B 603     3976   2909   5974   -622    148   -508       O  
HETATM 4672  O7  NDG B 603      65.089  42.266   0.958  1.00 37.67           O  
ANISOU 4672  O7  NDG B 603     4745   2242   7324      0    313   -616       O  
HETATM 4673  N2  NDG B 603      65.105  40.739   2.659  1.00 31.38           N  
ANISOU 4673  N2  NDG B 603     4393   1866   5662   -407     92  -1076       N  
HETATM 4674  O1L NDG B 603      66.869  39.785   4.374  1.00 34.52           O  
ANISOU 4674  O1L NDG B 603     4331   2680   6105   -616    343   -815       O  
HETATM 4675  C1  FUC B 604      63.707  38.364   0.929  1.00 22.24           C  
ANISOU 4675  C1  FUC B 604     3414   1154   3882   -492    287    -35       C  
HETATM 4676  C2  FUC B 604      62.997  38.470  -0.370  1.00 21.23           C  
ANISOU 4676  C2  FUC B 604     3343   1094   3627   -407    324    178       C  
HETATM 4677  C3  FUC B 604      63.313  37.343  -1.260  1.00 20.23           C  
ANISOU 4677  C3  FUC B 604     3169   1125   3391   -409    398     71       C  
HETATM 4678  C4  FUC B 604      62.984  36.093  -0.618  1.00 19.92           C  
ANISOU 4678  C4  FUC B 604     2868   1255   3446   -391    611     21       C  
HETATM 4679  C5  FUC B 604      63.679  36.000   0.663  1.00 19.29           C  
ANISOU 4679  C5  FUC B 604     3056   1134   3137   -506    646     61       C  
HETATM 4680  C6  FUC B 604      63.360  34.787   1.399  1.00 20.17           C  
ANISOU 4680  C6  FUC B 604     3149   1099   3415   -365    577   -253       C  
HETATM 4681  O2  FUC B 604      63.392  39.694  -0.977  1.00 24.23           O  
ANISOU 4681  O2  FUC B 604     3516   1377   4314   -374    480    554       O  
HETATM 4682  O3  FUC B 604      62.562  37.495  -2.445  1.00 21.17           O  
ANISOU 4682  O3  FUC B 604     3203   1399   3440   -379    295    311       O  
HETATM 4683  O4  FUC B 604      61.595  36.030  -0.444  1.00 20.56           O  
ANISOU 4683  O4  FUC B 604     2741   1427   3642   -207    591     -6       O  
HETATM 4684  O5  FUC B 604      63.360  37.161   1.525  1.00 20.33           O  
ANISOU 4684  O5  FUC B 604     3292   1157   3275   -286    715   -429       O  
HETATM 4685  O   HOH A 701      45.513  32.608  19.617  1.00 15.95           O  
ANISOU 4685  O   HOH A 701     2075   2039   1946    863   -118     12       O  
HETATM 4686  O   HOH A 702      65.435  -5.236   8.813  1.00 15.01           O  
ANISOU 4686  O   HOH A 702     1691   1220   2791    202    -70     71       O  
HETATM 4687  O   HOH A 703      50.825   1.960  14.035  1.00 16.64           O  
ANISOU 4687  O   HOH A 703     1917   1948   2457    827   -413   -632       O  
HETATM 4688  O   HOH A 704      48.951  -8.188  -2.169  1.00 13.57           O  
ANISOU 4688  O   HOH A 704     2040   1292   1822    -29   -196     35       O  
HETATM 4689  O   HOH A 705      50.926  -5.571  13.388  1.00 12.11           O  
ANISOU 4689  O   HOH A 705     1332   1115   2155   -255   -386    215       O  
HETATM 4690  O   HOH A 706      62.976  21.778  17.244  1.00 23.69           O  
ANISOU 4690  O   HOH A 706     1965   2353   4684    276   -519   1214       O  
HETATM 4691  O   HOH A 707      47.199  19.682  14.462  1.00 11.13           O  
ANISOU 4691  O   HOH A 707     1146   1071   2012    188     25    226       O  
HETATM 4692  O   HOH A 708      44.639  16.722  10.622  1.00 11.62           O  
ANISOU 4692  O   HOH A 708     1565   1194   1654    220   -196   -130       O  
HETATM 4693  O   HOH A 709      51.681  12.255  28.069  1.00 16.99           O  
ANISOU 4693  O   HOH A 709     2312   2134   2008    -85     26    -93       O  
HETATM 4694  O   HOH A 710      56.094  22.043  25.816  1.00 12.97           O  
ANISOU 4694  O   HOH A 710     1934   1088   1904    260   -315   -177       O  
HETATM 4695  O   HOH A 711      49.051   6.931  10.456  1.00 11.48           O  
ANISOU 4695  O   HOH A 711     1483   1089   1789     58     54    -71       O  
HETATM 4696  O   HOH A 712      47.654  -0.958  13.509  1.00 14.49           O  
ANISOU 4696  O   HOH A 712     2220   1273   2011    278    -69    -44       O  
HETATM 4697  O   HOH A 713      52.989   9.299  15.349  1.00 10.78           O  
ANISOU 4697  O   HOH A 713     1157   1024   1915    104     52    -84       O  
HETATM 4698  O   HOH A 714      43.705  11.097  27.183  1.00 27.98           O  
ANISOU 4698  O   HOH A 714     2744   3789   4097    299    299   1515       O  
HETATM 4699  O   HOH A 715      46.484  -9.281  -1.292  1.00 12.61           O  
ANISOU 4699  O   HOH A 715     1866   1270   1655   -184   -328    260       O  
HETATM 4700  O   HOH A 716      66.961  11.167  23.987  1.00 19.85           O  
ANISOU 4700  O   HOH A 716     2260   2608   2673   1023   -640   -707       O  
HETATM 4701  O   HOH A 717      53.798 -20.728   9.140  1.00 16.88           O  
ANISOU 4701  O   HOH A 717     2669   1763   1980   -294   -282    188       O  
HETATM 4702  O   HOH A 718      63.835   3.420   7.522  1.00 22.26           O  
ANISOU 4702  O   HOH A 718     1442   1598   5418     48   -374   -753       O  
HETATM 4703  O   HOH A 719      50.808  32.146   8.604  1.00 13.12           O  
ANISOU 4703  O   HOH A 719     1834   1274   1876    419     16    -85       O  
HETATM 4704  O   HOH A 720      52.968  20.746  25.588  1.00 12.86           O  
ANISOU 4704  O   HOH A 720     1926   1219   1740    604   -315   -157       O  
HETATM 4705  O   HOH A 721      63.327  14.227  10.506  1.00 22.22           O  
ANISOU 4705  O   HOH A 721     3037   3301   2102   1216    -96     35       O  
HETATM 4706  O   HOH A 722      63.245   0.874   3.068  1.00 18.85           O  
ANISOU 4706  O   HOH A 722     2758   1437   2968   -128    863   -412       O  
HETATM 4707  O   HOH A 723      56.234  28.912  26.745  1.00 18.63           O  
ANISOU 4707  O   HOH A 723     2553   1948   2577    988   -778   -576       O  
HETATM 4708  O   HOH A 724      64.859   0.221  11.930  1.00 20.97           O  
ANISOU 4708  O   HOH A 724     3696   1617   2653    858   -755   -199       O  
HETATM 4709  O   HOH A 725      49.681 -19.686  15.241  1.00 15.02           O  
ANISOU 4709  O   HOH A 725     2377   1269   2062   -526   -119    -71       O  
HETATM 4710  O   HOH A 726      52.102   7.170   0.419  1.00 11.15           O  
ANISOU 4710  O   HOH A 726     1102   1365   1768   -112     51      2       O  
HETATM 4711  O   HOH A 727      61.012  10.439  27.698  1.00 15.57           O  
ANISOU 4711  O   HOH A 727     2158   1699   2058    517   -491   -148       O  
HETATM 4712  O   HOH A 728      46.897  28.035   4.293  1.00 16.06           O  
ANISOU 4712  O   HOH A 728     2006   1928   2169    426   -202    -94       O  
HETATM 4713  O   HOH A 729      46.817  25.206   3.831  1.00 14.01           O  
ANISOU 4713  O   HOH A 729     1833   1860   1630     60    -57     82       O  
HETATM 4714  O   HOH A 730      58.678   8.469  26.440  1.00 16.38           O  
ANISOU 4714  O   HOH A 730     2423   1723   2077    552   -545   -134       O  
HETATM 4715  O   HOH A 731      51.211  35.541  -1.121  1.00 20.96           O  
ANISOU 4715  O   HOH A 731     3149   2085   2729    772    118    415       O  
HETATM 4716  O   HOH A 732      55.418   7.013  22.770  1.00 14.59           O  
ANISOU 4716  O   HOH A 732     2028   1149   2366    392      3    352       O  
HETATM 4717  O   HOH A 733      48.284  10.862  18.023  1.00 11.76           O  
ANISOU 4717  O   HOH A 733     1350   1381   1738     44     20     53       O  
HETATM 4718  O   HOH A 734      48.926  15.802  29.421  1.00 15.16           O  
ANISOU 4718  O   HOH A 734     2310   1565   1883    367    -82     54       O  
HETATM 4719  O   HOH A 735      46.323  -5.294  -3.755  1.00 20.98           O  
ANISOU 4719  O   HOH A 735     3281   2262   2428   -780   -869    615       O  
HETATM 4720  O   HOH A 736      55.686  -8.622  19.617  1.00 13.90           O  
ANISOU 4720  O   HOH A 736     1526   1872   1881    -64   -167    370       O  
HETATM 4721  O   HOH A 737      42.158  24.866  18.966  1.00 26.69           O  
ANISOU 4721  O   HOH A 737     3087   3270   3783    184   1041  -1465       O  
HETATM 4722  O   HOH A 738      48.652   6.160   2.538  1.00 14.85           O  
ANISOU 4722  O   HOH A 738     1789   1633   2218   -106     75    -39       O  
HETATM 4723  O   HOH A 739      51.419   2.681  22.525  1.00 16.47           O  
ANISOU 4723  O   HOH A 739     2705   1548   2006   -295     -5    178       O  
HETATM 4724  O   HOH A 740      43.277  23.485   3.131  1.00 30.95           O  
ANISOU 4724  O   HOH A 740     5418   3422   2917   1329    709    606       O  
HETATM 4725  O   HOH A 741      54.612 -16.933  11.356  1.00 16.44           O  
ANISOU 4725  O   HOH A 741     2550   1818   1878    -66   -692    -92       O  
HETATM 4726  O   HOH A 742      54.708 -24.257  10.939  1.00 15.42           O  
ANISOU 4726  O   HOH A 742     1964   1265   2629   -350   -182    244       O  
HETATM 4727  O   HOH A 743      58.579   7.757  29.173  1.00 19.83           O  
ANISOU 4727  O   HOH A 743     3524   1877   2131   1013   -486   -257       O  
HETATM 4728  O   HOH A 744      61.619  -3.287  -3.189  1.00 17.61           O  
ANISOU 4728  O   HOH A 744     2274   1997   2421    140    234    135       O  
HETATM 4729  O   HOH A 745      59.410  27.661  28.151  1.00 29.63           O  
ANISOU 4729  O   HOH A 745     4171   4987   2099   -854   -350   -601       O  
HETATM 4730  O   HOH A 746      61.868  32.921  10.120  1.00 16.42           O  
ANISOU 4730  O   HOH A 746     2481   1250   2509     18   -103    -56       O  
HETATM 4731  O   HOH A 747      52.275  13.455  21.358  1.00 13.54           O  
ANISOU 4731  O   HOH A 747     1809   1527   1809    525   -131   -152       O  
HETATM 4732  O   HOH A 748      47.818  17.022  13.522  1.00 12.15           O  
ANISOU 4732  O   HOH A 748     1662    988   1966    388    -47    -72       O  
HETATM 4733  O   HOH A 749      44.610  -0.893  14.112  1.00 12.97           O  
ANISOU 4733  O   HOH A 749     1661   1168   2099    -47   -140     42       O  
HETATM 4734  O   HOH A 750      65.503  29.001   7.009  1.00 16.27           O  
ANISOU 4734  O   HOH A 750     2040   1691   2449     87    -77   -303       O  
HETATM 4735  O   HOH A 751      38.023  -6.842   5.966  1.00 17.14           O  
ANISOU 4735  O   HOH A 751     1551   1849   3110   -459   -311    -40       O  
HETATM 4736  O   HOH A 752      53.389  20.747  28.375  1.00 13.52           O  
ANISOU 4736  O   HOH A 752     1766   1643   1726    550   -180   -323       O  
HETATM 4737  O   HOH A 753      67.509   1.774   7.403  1.00 19.00           O  
ANISOU 4737  O   HOH A 753     2175   1784   3259   -318    371   -179       O  
HETATM 4738  O   HOH A 754      42.089  -1.534  16.587  1.00 17.39           O  
ANISOU 4738  O   HOH A 754     2208   1741   2656   -211    200   -266       O  
HETATM 4739  O   HOH A 755      52.629   9.391  27.917  1.00 18.67           O  
ANISOU 4739  O   HOH A 755     2607   2346   2139   -125      4     44       O  
HETATM 4740  O   HOH A 756      53.036  -9.945  21.044  1.00 18.81           O  
ANISOU 4740  O   HOH A 756     3053   1929   2164    133   -376   -346       O  
HETATM 4741  O   HOH A 757      52.798  -5.827   0.562  1.00 12.93           O  
ANISOU 4741  O   HOH A 757     1890    736   2285   -176   -516    139       O  
HETATM 4742  O   HOH A 758      61.477  25.453  21.980  1.00 14.89           O  
ANISOU 4742  O   HOH A 758     1983   1516   2158    -96   -357   -336       O  
HETATM 4743  O   HOH A 759      40.849   8.578  12.814  1.00 24.37           O  
ANISOU 4743  O   HOH A 759     2639   2093   4528   -571   1381  -1095       O  
HETATM 4744  O   HOH A 760      58.199   4.519  -1.849  1.00 12.41           O  
ANISOU 4744  O   HOH A 760     1445   1359   1910    341    -84    296       O  
HETATM 4745  O   HOH A 761      45.380   9.214  26.446  1.00 22.11           O  
ANISOU 4745  O   HOH A 761     2890   2882   2628   -396    614   -375       O  
HETATM 4746  O   HOH A 762      47.328  36.471  25.533  1.00 20.19           O  
ANISOU 4746  O   HOH A 762     2478   2359   2832    922    -75   -455       O  
HETATM 4747  O   HOH A 763      55.746  20.953  29.957  1.00 16.58           O  
ANISOU 4747  O   HOH A 763     2154   2268   1876    333   -125   -390       O  
HETATM 4748  O   HOH A 764      40.555  24.224  15.460  1.00 20.46           O  
ANISOU 4748  O   HOH A 764     1587   2865   3323    626   -511  -1043       O  
HETATM 4749  O   HOH A 765      40.257  10.927   7.436  1.00 19.37           O  
ANISOU 4749  O   HOH A 765     2265   2281   2814    180    -29    248       O  
HETATM 4750  O   HOH A 766      54.192  13.507   7.264  1.00 14.95           O  
ANISOU 4750  O   HOH A 766     1848   1691   2142    345    -11    299       O  
HETATM 4751  O   HOH A 767      38.857 -16.188   1.945  1.00 23.56           O  
ANISOU 4751  O   HOH A 767     3358   1809   3784    213  -1961   -550       O  
HETATM 4752  O   HOH A 768      65.464   5.716   7.601  1.00 16.48           O  
ANISOU 4752  O   HOH A 768     2185   1660   2415   -262     15   -499       O  
HETATM 4753  O   HOH A 769      47.731   9.399  10.772  1.00 14.43           O  
ANISOU 4753  O   HOH A 769     1789   1218   2476    207     25      1       O  
HETATM 4754  O   HOH A 770      57.573  34.296   5.034  1.00 20.96           O  
ANISOU 4754  O   HOH A 770     2374   1560   4030    474    198    666       O  
HETATM 4755  O   HOH A 771      39.301  -3.267   3.245  1.00 17.65           O  
ANISOU 4755  O   HOH A 771     1629   2207   2870   -539   -528    518       O  
HETATM 4756  O   HOH A 772      65.041  21.526  19.299  1.00 23.48           O  
ANISOU 4756  O   HOH A 772     3328   1526   4067    -47   1248   -331       O  
HETATM 4757  O   HOH A 773      57.179  23.313  30.125  1.00 18.54           O  
ANISOU 4757  O   HOH A 773     3026   2121   1897    437   -395   -358       O  
HETATM 4758  O   HOH A 774      60.962   2.581  23.614  1.00 24.67           O  
ANISOU 4758  O   HOH A 774     2995   3485   2893   1864   -418   -244       O  
HETATM 4759  O   HOH A 775      35.870 -11.558  12.341  1.00 26.86           O  
ANISOU 4759  O   HOH A 775     2781   3149   4274   -693    549   -113       O  
HETATM 4760  O   HOH A 776      62.584  20.296  26.833  1.00 18.82           O  
ANISOU 4760  O   HOH A 776     2004   1957   3189    284   -389   -335       O  
HETATM 4761  O   HOH A 777      63.484  25.491  10.966  1.00 18.86           O  
ANISOU 4761  O   HOH A 777     2409   1700   3055    308    104    -52       O  
HETATM 4762  O   HOH A 778      60.872  -5.775  -4.064  1.00 18.78           O  
ANISOU 4762  O   HOH A 778     2903   1760   2472    -60    -62    190       O  
HETATM 4763  O   HOH A 779      40.199  -5.348  -1.271  1.00 25.90           O  
ANISOU 4763  O   HOH A 779     2752   2454   4635     12   -976    477       O  
HETATM 4764  O   HOH A 780      64.111  26.200   8.324  1.00 20.08           O  
ANISOU 4764  O   HOH A 780     2168   1599   3861    359    560    385       O  
HETATM 4765  O   HOH A 781      53.617  26.264  31.976  1.00 25.77           O  
ANISOU 4765  O   HOH A 781     3132   3288   3369     65    -34  -1162       O  
HETATM 4766  O   HOH A 782      51.654  17.756   5.300  1.00 18.20           O  
ANISOU 4766  O   HOH A 782     3031   1646   2238    470    -56     73       O  
HETATM 4767  O   HOH A 783      40.910  16.398   9.071  1.00 23.76           O  
ANISOU 4767  O   HOH A 783     3114   2874   3039    241   -215   -539       O  
HETATM 4768  O   HOH A 784      54.349  -6.758  21.505  1.00 20.71           O  
ANISOU 4768  O   HOH A 784     2558   2318   2991    600    231    424       O  
HETATM 4769  O   HOH A 785      39.283 -12.318  15.281  1.00 22.24           O  
ANISOU 4769  O   HOH A 785     3006   2516   2928   -556    496     30       O  
HETATM 4770  O   HOH A 786      43.074  30.102  14.780  1.00 30.01           O  
ANISOU 4770  O   HOH A 786     3777   4568   3056   2294    382    386       O  
HETATM 4771  O   HOH A 787      61.737 -14.937  13.038  1.00 20.34           O  
ANISOU 4771  O   HOH A 787     2914   1146   3669   -182   -467    516       O  
HETATM 4772  O   HOH A 788      62.437  23.970  27.787  1.00 25.96           O  
ANISOU 4772  O   HOH A 788     2550   4104   3208    501  -1067  -1263       O  
HETATM 4773  O   HOH A 789      38.083  17.371  14.003  1.00 21.51           O  
ANISOU 4773  O   HOH A 789     2563   2714   2897    880    347   -684       O  
HETATM 4774  O   HOH A 790      51.261   4.881  28.284  1.00 24.30           O  
ANISOU 4774  O   HOH A 790     3740   3116   2377    775    389    884       O  
HETATM 4775  O   HOH A 791      50.980 -17.977  22.756  1.00 28.58           O  
ANISOU 4775  O   HOH A 791     5002   2596   3260   -577    -34   -232       O  
HETATM 4776  O   HOH A 792      54.885  37.529   3.313  1.00 29.89           O  
ANISOU 4776  O   HOH A 792     6312   2313   2733  -1299    918   -147       O  
HETATM 4777  O   HOH A 793      67.056  -2.608   6.673  1.00 23.39           O  
ANISOU 4777  O   HOH A 793     1902   1773   5211     65    454   -533       O  
HETATM 4778  O   HOH A 794      33.163  -6.100   7.940  1.00 24.24           O  
ANISOU 4778  O   HOH A 794     2201   2766   4241   -583    -61   -174       O  
HETATM 4779  O   HOH A 795      37.436  -5.203  10.118  1.00 21.12           O  
ANISOU 4779  O   HOH A 795     2552   2388   3083   -687     22     76       O  
HETATM 4780  O   HOH A 796      41.080  -4.672   1.391  1.00 16.66           O  
ANISOU 4780  O   HOH A 796     1995   1490   2845   -109   -477    393       O  
HETATM 4781  O   HOH A 797      63.307  22.673  25.544  1.00 23.07           O  
ANISOU 4781  O   HOH A 797     2314   2468   3983    362   -771   -455       O  
HETATM 4782  O   HOH A 798      43.566  13.833   6.506  1.00 16.26           O  
ANISOU 4782  O   HOH A 798     2454   1597   2127    295      5   -136       O  
HETATM 4783  O   HOH A 799      56.599  36.146  10.999  1.00 28.12           O  
ANISOU 4783  O   HOH A 799     3618   2744   4320    242   -891  -1313       O  
HETATM 4784  O   HOH A 800      55.713 -18.970   8.407  1.00 24.68           O  
ANISOU 4784  O   HOH A 800     2602   2678   4097    -99   -623   1789       O  
HETATM 4785  O   HOH A 801      63.549  24.625  23.689  1.00 24.18           O  
ANISOU 4785  O   HOH A 801     2392   3143   3653     82  -1331    321       O  
HETATM 4786  O   HOH A 802      58.149  10.464  33.466  1.00 28.24           O  
ANISOU 4786  O   HOH A 802     4502   4296   1931   1666   -427     23       O  
HETATM 4787  O   HOH A 803      53.565  23.470  32.124  1.00 25.29           O  
ANISOU 4787  O   HOH A 803     4351   2861   2395    549   -770   -660       O  
HETATM 4788  O   HOH A 804      37.012 -17.640  10.640  1.00 28.18           O  
ANISOU 4788  O   HOH A 804     3826   2498   4383  -1332   -132   -177       O  
HETATM 4789  O   HOH A 805      40.421  20.292   2.985  1.00 20.11           O  
ANISOU 4789  O   HOH A 805     2706   3131   1802    436   -327   -230       O  
HETATM 4790  O   HOH A 806      64.606  30.269  10.291  1.00 25.50           O  
ANISOU 4790  O   HOH A 806     2645   3113   3930    -13   -412   -202       O  
HETATM 4791  O   HOH A 807      62.385   7.229   4.244  1.00 17.32           O  
ANISOU 4791  O   HOH A 807     1913   1547   3119   -549    645   -224       O  
HETATM 4792  O   HOH A 808      59.719  37.819  -2.363  1.00 24.32           O  
ANISOU 4792  O   HOH A 808     3156   2619   3465    128    368    736       O  
HETATM 4793  O   HOH A 809      58.629  13.291  10.847  1.00 20.98           O  
ANISOU 4793  O   HOH A 809     2513   1994   3465    249   -512  -1234       O  
HETATM 4794  O   HOH A 810      61.916  -1.810  -5.514  1.00 29.35           O  
ANISOU 4794  O   HOH A 810     4830   2974   3348    985   1007    248       O  
HETATM 4795  O   HOH A 811      66.415  -7.434   2.312  1.00 29.18           O  
ANISOU 4795  O   HOH A 811     2759   2529   5797    -29   1503     33       O  
HETATM 4796  O   HOH A 812      52.581  -8.012  22.996  1.00 21.79           O  
ANISOU 4796  O   HOH A 812     2676   2707   2896    181   -227   -243       O  
HETATM 4797  O   HOH A 813      63.163  17.370  28.919  1.00 21.94           O  
ANISOU 4797  O   HOH A 813     3166   2294   2874    587   -931   -292       O  
HETATM 4798  O   HOH A 814      63.371   1.423  -0.593  1.00 26.69           O  
ANISOU 4798  O   HOH A 814     2474   2830   4836   -173    602   -265       O  
HETATM 4799  O   HOH A 815      43.103  17.734   7.326  1.00 20.46           O  
ANISOU 4799  O   HOH A 815     2475   2000   3298   -143    590   -300       O  
HETATM 4800  O   HOH A 816      43.906  27.134  15.070  1.00 29.88           O  
ANISOU 4800  O   HOH A 816     3618   4143   3590   1001   -806   -389       O  
HETATM 4801  O   HOH A 817      61.851 -17.663   4.549  1.00 24.04           O  
ANISOU 4801  O   HOH A 817     2724   2722   3688    355   -105    187       O  
HETATM 4802  O   HOH A 818      47.946  24.002  26.586  1.00 27.85           O  
ANISOU 4802  O   HOH A 818     3850   2471   4261   1252  -2002  -1042       O  
HETATM 4803  O   HOH A 819      60.091  33.673  21.968  1.00 24.61           O  
ANISOU 4803  O   HOH A 819     2519   3525   3305    537   -756   -682       O  
HETATM 4804  O   HOH A 820      40.255   2.487  23.506  1.00 35.42           O  
ANISOU 4804  O   HOH A 820     4762   3826   4868    -84   1761    287       O  
HETATM 4805  O   HOH A 821      59.610 -17.616   7.726  1.00 29.87           O  
ANISOU 4805  O   HOH A 821     3915   4983   2452     93   -649    485       O  
HETATM 4806  O   HOH A 822      42.910  27.646   9.004  1.00 22.51           O  
ANISOU 4806  O   HOH A 822     2274   2573   3706    487     37     32       O  
HETATM 4807  O   HOH A 823      62.657  31.221  13.314  1.00 23.45           O  
ANISOU 4807  O   HOH A 823     3438   2121   3349      6   -961   -116       O  
HETATM 4808  O   HOH A 824      51.846  27.423  30.089  1.00 32.87           O  
ANISOU 4808  O   HOH A 824     4778   3990   3722   1132    -48    370       O  
HETATM 4809  O   HOH A 825      50.308 -15.345  21.895  1.00 29.53           O  
ANISOU 4809  O   HOH A 825     5350   2678   3192  -1779    806   -283       O  
HETATM 4810  O   HOH A 826      56.622   5.951  29.728  1.00 33.58           O  
ANISOU 4810  O   HOH A 826     6076   3948   2736  -1313    833   -684       O  
HETATM 4811  O   HOH A 827      44.719 -10.172  -3.194  1.00 36.76           O  
ANISOU 4811  O   HOH A 827     4444   5185   4336  -1237  -1313  -1550       O  
HETATM 4812  O   HOH A 828      43.102 -21.221   3.141  1.00 30.66           O  
ANISOU 4812  O   HOH A 828     5565   2302   3781   1054   -370   -112       O  
HETATM 4813  O   HOH A 829      39.595  18.641   8.493  1.00 27.12           O  
ANISOU 4813  O   HOH A 829     3376   4042   2885   -129   -350     21       O  
HETATM 4814  O   HOH A 830      55.521 -20.815  -2.229  1.00 27.66           O  
ANISOU 4814  O   HOH A 830     4989   2313   3205  -1365   -112   -511       O  
HETATM 4815  O   HOH A 831      39.336 -14.508  16.760  1.00 34.61           O  
ANISOU 4815  O   HOH A 831     5657   2909   4584      7   1129    706       O  
HETATM 4816  O   HOH A 832      36.983   5.682   8.726  1.00 30.17           O  
ANISOU 4816  O   HOH A 832     2311   4047   5105   -301  -1025   2202       O  
HETATM 4817  O   HOH A 833      39.141   5.376  17.491  1.00 26.02           O  
ANISOU 4817  O   HOH A 833     2593   4314   2978  -1428   1155  -1148       O  
HETATM 4818  O   HOH A 834      44.768  15.713   7.965  1.00 17.88           O  
ANISOU 4818  O   HOH A 834     2338   2246   2209    193    -80   -338       O  
HETATM 4819  O   HOH A 835      51.598   1.204  26.105  1.00 35.10           O  
ANISOU 4819  O   HOH A 835     5134   3405   4798   -741   1171   1062       O  
HETATM 4820  O   HOH A 836      54.196  37.981  -3.732  1.00 36.30           O  
ANISOU 4820  O   HOH A 836     6359   3618   3813   -556    757    300       O  
HETATM 4821  O   HOH A 837      62.375   0.978  -5.792  1.00 23.77           O  
ANISOU 4821  O   HOH A 837     3246   2655   3130    502    478    350       O  
HETATM 4822  O   HOH A 838      55.751  22.236  33.329  1.00 31.12           O  
ANISOU 4822  O   HOH A 838     4936   3261   3625    962  -1072   -766       O  
HETATM 4823  O   HOH A 839      45.545  37.040   6.032  1.00 35.15           O  
ANISOU 4823  O   HOH A 839     5114   4487   3755   2794    238   -169       O  
HETATM 4824  O   HOH A 840      69.381   2.062   9.722  1.00 29.85           O  
ANISOU 4824  O   HOH A 840     3669   3179   4492   -175    743   -651       O  
HETATM 4825  O   HOH A 841      62.484   0.313  19.027  1.00 30.87           O  
ANISOU 4825  O   HOH A 841     4948   3355   3425   1721    241    918       O  
HETATM 4826  O   HOH A 842      48.709   7.879  28.840  1.00 32.52           O  
ANISOU 4826  O   HOH A 842     5101   4375   2879   -163   1414     48       O  
HETATM 4827  O   HOH A 843      49.829  14.723  31.704  1.00 26.52           O  
ANISOU 4827  O   HOH A 843     3977   3602   2496    657   -133    328       O  
HETATM 4828  O   HOH A 844      49.119  34.285  -2.644  1.00 28.05           O  
ANISOU 4828  O   HOH A 844     3575   3040   4042    481   -198    522       O  
HETATM 4829  O   HOH A 845      37.440  10.297  31.314  1.00 30.08           O  
ANISOU 4829  O   HOH A 845     3675   4456   3296   -841    528    655       O  
HETATM 4830  O   HOH A 846      52.387  14.242  32.131  1.00 23.35           O  
ANISOU 4830  O   HOH A 846     3550   2595   2728    166    236    144       O  
HETATM 4831  O   HOH A 847      55.764  21.906   8.852  1.00 20.46           O  
ANISOU 4831  O   HOH A 847     2623   1950   3199    572   -225     36       O  
HETATM 4832  O   HOH A 848      40.961 -21.964   8.641  1.00 28.44           O  
ANISOU 4832  O   HOH A 848     4377   1917   4511  -1151   -405    699       O  
HETATM 4833  O   HOH A 849      66.069  22.075  25.600  1.00 28.24           O  
ANISOU 4833  O   HOH A 849     2962   3534   4233    737   -908  -1241       O  
HETATM 4834  O   HOH A 850      38.855  13.295   6.976  1.00 23.68           O  
ANISOU 4834  O   HOH A 850     3141   2457   3399    462    269    308       O  
HETATM 4835  O   HOH A 851      38.278  22.000   3.129  1.00 35.57           O  
ANISOU 4835  O   HOH A 851     5370   4928   3217   1781   -331    -29       O  
HETATM 4836  O   HOH A 852      51.369  19.140  35.172  1.00 28.67           O  
ANISOU 4836  O   HOH A 852     4131   4381   2379   1074   -315   -628       O  
HETATM 4837  O   HOH A 853      53.813  11.817  31.748  1.00 33.15           O  
ANISOU 4837  O   HOH A 853     4158   3059   5376    553   2073   -392       O  
HETATM 4838  O   HOH A 854      51.691 -18.847  -1.270  1.00 27.55           O  
ANISOU 4838  O   HOH A 854     4898   3281   2287   -827   -101   -892       O  
HETATM 4839  O   HOH A 855      73.035  20.805  20.658  1.00 32.62           O  
ANISOU 4839  O   HOH A 855     3967   3639   4788   -512  -1052    -41       O  
HETATM 4840  O   HOH A 856      45.483  32.561   9.205  1.00 31.35           O  
ANISOU 4840  O   HOH A 856     4681   4699   2529   -308   -192    465       O  
HETATM 4841  O   HOH A 857      40.989  15.092   6.762  1.00 24.07           O  
ANISOU 4841  O   HOH A 857     3046   2800   3299    865   -333   -453       O  
HETATM 4842  O   HOH A 858      60.753  36.310  16.926  1.00 32.95           O  
ANISOU 4842  O   HOH A 858     3072   4636   4810    351   -595    402       O  
HETATM 4843  O   HOH A 859      44.955  34.197   3.301  1.00 31.68           O  
ANISOU 4843  O   HOH A 859     3229   3276   5531   1058  -1575      9       O  
HETATM 4844  O   HOH A 860      49.077  -0.226  18.053  1.00 17.99           O  
ANISOU 4844  O   HOH A 860     2442   1766   2628    -63    -77     65       O  
HETATM 4845  O   HOH A 861      68.272  12.750  30.166  1.00 36.36           O  
ANISOU 4845  O   HOH A 861     3883   5186   4746    430  -2118   -326       O  
HETATM 4846  O   HOH A 862      64.813  29.034  16.205  1.00 37.72           O  
ANISOU 4846  O   HOH A 862     5658   3732   4941   -512   1493   -669       O  
HETATM 4847  O   HOH A 863      35.419  22.897  16.274  1.00 37.58           O  
ANISOU 4847  O   HOH A 863     5688   2579   6010   1144   2035    -79       O  
HETATM 4848  O   HOH A 864      39.716  26.493  11.367  1.00 27.86           O  
ANISOU 4848  O   HOH A 864     2906   2926   4754    426    961   -719       O  
HETATM 4849  O   HOH A 865      44.312  27.550  12.803  1.00 36.13           O  
ANISOU 4849  O   HOH A 865     4283   5570   3875    163    132   1704       O  
HETATM 4850  O   HOH A 866      64.427 -10.761  -1.670  1.00 26.41           O  
ANISOU 4850  O   HOH A 866     3750   2697   3585   1195    621   -310       O  
HETATM 4851  O   HOH A 867      43.999 -16.514  17.144  1.00 24.10           O  
ANISOU 4851  O   HOH A 867     2655   2673   3829   -786    423   -247       O  
HETATM 4852  O   HOH A 868      70.530   4.757  20.945  1.00 33.21           O  
ANISOU 4852  O   HOH A 868     4422   3752   4444   -140    185     38       O  
HETATM 4853  O   HOH A 869      63.779 -15.735   3.513  1.00 29.83           O  
ANISOU 4853  O   HOH A 869     3294   2462   5578    522    199    134       O  
HETATM 4854  O   HOH A 870      37.436  19.776  10.389  1.00 30.61           O  
ANISOU 4854  O   HOH A 870     4486   3844   3301   -859  -1112   -210       O  
HETATM 4855  O   HOH A 871      58.311  22.331   8.112  1.00 23.26           O  
ANISOU 4855  O   HOH A 871     2879   1968   3990   -303    567    107       O  
HETATM 4856  O   HOH A 872      62.840  36.875   6.939  1.00 30.85           O  
ANISOU 4856  O   HOH A 872     5451   2210   4060   -516  -1196   -934       O  
HETATM 4857  O   HOH A 873      60.977  39.958   3.935  1.00 30.27           O  
ANISOU 4857  O   HOH A 873     4382   2716   4403    272  -1341   -492       O  
HETATM 4858  O   HOH A 874      59.373  -5.622  -6.446  1.00 27.04           O  
ANISOU 4858  O   HOH A 874     4467   2892   2913     31   -478    -99       O  
HETATM 4859  O   HOH A 875      63.853 -14.696  10.502  1.00 27.61           O  
ANISOU 4859  O   HOH A 875     5116   1482   3893    407   -545    234       O  
HETATM 4860  O   HOH A 876      54.722   1.556  28.236  1.00 36.38           O  
ANISOU 4860  O   HOH A 876     4980   4868   3973   -975    474   1318       O  
HETATM 4861  O   HOH A 877      44.373  26.126  26.791  1.00 25.51           O  
ANISOU 4861  O   HOH A 877     3351   3096   3244   1312   -180    -76       O  
HETATM 4862  O   HOH A 878      62.136  29.640  15.575  1.00 29.38           O  
ANISOU 4862  O   HOH A 878     5586   2289   3287  -1444   -636    121       O  
HETATM 4863  O   HOH A 879      38.818   6.605  24.357  1.00 28.68           O  
ANISOU 4863  O   HOH A 879     3604   4060   3234   -799    613    -47       O  
HETATM 4864  O   HOH A 880      49.170  16.014  33.929  1.00 37.44           O  
ANISOU 4864  O   HOH A 880     5087   4589   4548    318    853   -998       O  
HETATM 4865  O   HOH A 881      58.421 -18.591  18.697  1.00 34.20           O  
ANISOU 4865  O   HOH A 881     4586   3969   4439   -724   -986    529       O  
HETATM 4866  O   HOH A 882      68.520  24.831  18.072  1.00 41.04           O  
ANISOU 4866  O   HOH A 882     5585   4788   5218   -616  -1236  -1942       O  
HETATM 4867  O   HOH A 883      56.068 -18.420  19.908  1.00 34.61           O  
ANISOU 4867  O   HOH A 883     4702   5307   3139   1516   -361    299       O  
HETATM 4868  O   HOH A 884      59.041   8.026  34.007  1.00 40.90           O  
ANISOU 4868  O   HOH A 884     5350   5025   5166   -788   -447   1021       O  
HETATM 4869  O   HOH A 885      63.964  25.180  19.481  1.00 36.78           O  
ANISOU 4869  O   HOH A 885     4981   5220   3774    686   -686   -113       O  
HETATM 4870  O   HOH A 886      41.903 -14.763  18.177  1.00 33.26           O  
ANISOU 4870  O   HOH A 886     4208   4312   4116  -1111   -266  -1002       O  
HETATM 4871  O   HOH A 887      47.817  36.952  28.255  1.00 34.25           O  
ANISOU 4871  O   HOH A 887     4167   4664   4181   1575   -500   -208       O  
HETATM 4872  O   HOH A 888      46.207  37.052  30.543  1.00 37.14           O  
ANISOU 4872  O   HOH A 888     5268   4754   4089    857    703   -989       O  
HETATM 4873  O   HOH A 889      55.309 -22.024   2.102  1.00 36.31           O  
ANISOU 4873  O   HOH A 889     4812   2535   6448  -1074    813   1049       O  
HETATM 4874  O   HOH A 890      38.268  24.167  16.902  1.00 26.03           O  
ANISOU 4874  O   HOH A 890     3641   3037   3210    519    -55   -986       O  
HETATM 4875  O   HOH A 891      48.982  -9.258  -4.737  1.00 30.68           O  
ANISOU 4875  O   HOH A 891     6592   2557   2507    337     30   -250       O  
HETATM 4876  O   HOH A 892      42.631  -4.424  20.069  1.00 29.44           O  
ANISOU 4876  O   HOH A 892     4088   3635   3463   -801    141    138       O  
HETATM 4877  O   HOH A 893      42.803  28.343   6.309  1.00 35.14           O  
ANISOU 4877  O   HOH A 893     4592   4255   4504   1035    421   1025       O  
HETATM 4878  O   HOH A 894      56.451 -19.113  11.559  1.00 38.87           O  
ANISOU 4878  O   HOH A 894     5546   4669   4553   1180   -553  -1271       O  
HETATM 4879  O   HOH A 895      49.383  37.775  22.554  1.00 32.58           O  
ANISOU 4879  O   HOH A 895     4918   2068   5392   -315   1004   -788       O  
HETATM 4880  O   HOH A 896      36.810   8.461   9.205  1.00 36.05           O  
ANISOU 4880  O   HOH A 896     3315   3814   6569    326    113  -1498       O  
HETATM 4881  O   HOH A 897      36.124  13.821  25.498  1.00 34.01           O  
ANISOU 4881  O   HOH A 897     2993   6237   3693   -933    693   -631       O  
HETATM 4882  O   HOH A 898      61.365  18.300  31.037  1.00 30.92           O  
ANISOU 4882  O   HOH A 898     4276   4055   3417     -7  -1715   -455       O  
HETATM 4883  O   HOH A 899      64.127  34.198  10.556  1.00 39.08           O  
ANISOU 4883  O   HOH A 899     4807   4638   5403  -1608  -1495    -98       O  
HETATM 4884  O   HOH A 900      55.496  39.014  12.977  1.00 43.65           O  
ANISOU 4884  O   HOH A 900     5956   4647   5983   -123     87    911       O  
HETATM 4885  O   HOH A 901      65.810  23.389  21.339  1.00 33.66           O  
ANISOU 4885  O   HOH A 901     4109   3198   5483   -445   -907  -1084       O  
HETATM 4886  O   HOH A 902      36.395   3.906  14.211  1.00 32.79           O  
ANISOU 4886  O   HOH A 902     3082   4070   5306    123    516   -198       O  
HETATM 4887  O   HOH A 903      53.540  38.444  15.907  1.00 32.72           O  
ANISOU 4887  O   HOH A 903     3912   3017   5503   -557     63    497       O  
HETATM 4888  O   HOH A 904      51.287  27.835  27.187  1.00 23.88           O  
ANISOU 4888  O   HOH A 904     3045   2895   3134     77    145   -388       O  
HETATM 4889  O   HOH A 905      61.906  34.040  15.079  1.00 35.64           O  
ANISOU 4889  O   HOH A 905     3957   4757   4828  -1328   -250    866       O  
HETATM 4890  O   HOH A 906      43.374   0.303  -2.937  1.00 32.12           O  
ANISOU 4890  O   HOH A 906     4007   4494   3704   -108   -386   -369       O  
HETATM 4891  O   HOH A 907      35.171   7.313  23.028  1.00 43.60           O  
ANISOU 4891  O   HOH A 907     5365   5623   5576   -200   1048   -348       O  
HETATM 4892  O   HOH A 908      51.631  39.255   1.485  1.00 33.04           O  
ANISOU 4892  O   HOH A 908     5527   3025   4000    361    702    855       O  
HETATM 4893  O   HOH A 909      70.289  15.195  29.517  1.00 36.83           O  
ANISOU 4893  O   HOH A 909     4052   5927   4014    616  -1069   -751       O  
HETATM 4894  O   HOH A 910      35.582  22.529  19.150  1.00 37.89           O  
ANISOU 4894  O   HOH A 910     5786   4659   3949  -1076    303   -106       O  
HETATM 4895  O   HOH A 911      38.758  15.438  10.517  1.00 34.43           O  
ANISOU 4895  O   HOH A 911     4383   4025   4675    924    258   -226       O  
HETATM 4896  O   HOH A 912      53.998  15.241  33.941  1.00 37.54           O  
ANISOU 4896  O   HOH A 912     5694   4043   4524    659   -683    968       O  
HETATM 4897  O   HOH A 913      43.647  -7.164  21.434  1.00 32.86           O  
ANISOU 4897  O   HOH A 913     3190   3278   6015   -824   -135   -138       O  
HETATM 4898  O   HOH A 914      39.061   8.906  16.081  1.00 32.86           O  
ANISOU 4898  O   HOH A 914     2042   4771   5671   -171    453    -82       O  
HETATM 4899  O   HOH A 915      45.163  29.833   5.454  1.00 35.13           O  
ANISOU 4899  O   HOH A 915     3932   4279   5137   1014    573   -884       O  
HETATM 4900  O   HOH A 916      40.080  -4.146  20.396  1.00 33.33           O  
ANISOU 4900  O   HOH A 916     4121   3816   4728  -1040    495   -505       O  
HETATM 4901  O   HOH A 917      36.996  17.344  11.477  1.00 33.29           O  
ANISOU 4901  O   HOH A 917     3540   4834   4274    976    140   -239       O  
HETATM 4902  O   HOH A 918      51.009  38.227  24.911  1.00 37.02           O  
ANISOU 4902  O   HOH A 918     4060   3632   6374    398   -690  -1176       O  
HETATM 4903  O   HOH A 919      41.782  -4.031  23.680  1.00 35.96           O  
ANISOU 4903  O   HOH A 919     5098   3805   4760  -1417   1413    137       O  
HETATM 4904  O   HOH A 920      67.460   1.780  13.839  1.00 32.93           O  
ANISOU 4904  O   HOH A 920     5114   2959   4438   1257   1285   -323       O  
HETATM 4905  O   HOH A 921      62.985  -6.244  -5.483  1.00 37.96           O  
ANISOU 4905  O   HOH A 921     4844   4740   4839    845   1747    881       O  
HETATM 4906  O   HOH A 922      60.760  -7.066  -8.343  1.00 40.46           O  
ANISOU 4906  O   HOH A 922     6057   4833   4484    717   1010   -844       O  
HETATM 4907  O   HOH A 923      66.820  21.236  28.143  1.00 37.04           O  
ANISOU 4907  O   HOH A 923     4599   4892   4582   -283   -583   -782       O  
HETATM 4908  O   HOH A 924      42.614  -9.728  17.802  1.00 31.38           O  
ANISOU 4908  O   HOH A 924     3964   3875   4084   -421   -225   1206       O  
HETATM 4909  O   HOH A 925      54.951  21.671  35.987  1.00 46.13           O  
ANISOU 4909  O   HOH A 925     6172   6408   4945    329    -34    324       O  
HETATM 4910  O   HOH A 926      32.557  -2.708   4.388  1.00 43.10           O  
ANISOU 4910  O   HOH A 926     4859   5539   5978   -466    595     62       O  
HETATM 4911  O   HOH A 927      36.595   4.880   0.915  1.00 37.39           O  
ANISOU 4911  O   HOH A 927     4273   4765   5169   1967   -608    606       O  
HETATM 4912  O   HOH A 928      67.582  12.395  32.548  1.00 39.41           O  
ANISOU 4912  O   HOH A 928     5175   5038   4759   1848  -1150    183       O  
HETATM 4913  O   HOH A 929      50.545  38.228  14.099  1.00 35.95           O  
ANISOU 4913  O   HOH A 929     4888   3969   4801    616   -182   1208       O  
HETATM 4914  O   HOH A 930      39.489  -2.380  16.937  1.00 34.01           O  
ANISOU 4914  O   HOH A 930     4269   2237   6416    204   1408    967       O  
HETATM 4915  O   HOH A 931      68.825  -1.392  12.987  1.00 42.23           O  
ANISOU 4915  O   HOH A 931     4632   6085   5329   -278    813    170       O  
HETATM 4916  O   HOH A 932      50.427  38.197  -0.683  1.00 33.99           O  
ANISOU 4916  O   HOH A 932     5004   2891   5018   1490   -405     53       O  
HETATM 4917  O   HOH A 933      38.712  10.314   9.663  1.00 27.25           O  
ANISOU 4917  O   HOH A 933     3357   3245   3752   -656   1203   -331       O  
HETATM 4918  O   HOH A 934      47.317 -20.712  22.929  1.00 44.78           O  
ANISOU 4918  O   HOH A 934     6154   5689   5169  -1066   1205    700       O  
HETATM 4919  O   HOH A 935      37.793  15.937  35.334  1.00 30.42           O  
ANISOU 4919  O   HOH A 935     3613   4801   3145    996    554     87       O  
HETATM 4920  O   HOH A 936      43.075  13.962  36.316  1.00 38.83           O  
ANISOU 4920  O   HOH A 936     5465   4665   4623   -649    224   -111       O  
HETATM 4921  O   HOH A 937      37.570  13.004   9.388  1.00 38.07           O  
ANISOU 4921  O   HOH A 937     4551   5694   4220    166    153   -601       O  
HETATM 4922  O   HOH A 938      36.337  -4.934  12.743  1.00 36.86           O  
ANISOU 4922  O   HOH A 938     5140   4043   4823   -228   1269   -217       O  
HETATM 4923  O   HOH A 939      53.616   7.734  29.914  1.00 36.63           O  
ANISOU 4923  O   HOH A 939     4941   5452   3524   -414   -807   1569       O  
HETATM 4924  O   HOH A 940      64.480 -15.027   0.777  1.00 36.31           O  
ANISOU 4924  O   HOH A 940     4006   4097   5694   -263    785   -543       O  
HETATM 4925  O   HOH A 941      59.545  -2.687  -7.266  1.00 39.48           O  
ANISOU 4925  O   HOH A 941     5789   4892   4318    711   -362   -603       O  
HETATM 4926  O   HOH A 942      57.739  27.915  30.953  1.00 40.50           O  
ANISOU 4926  O   HOH A 942     4998   4170   6220  -1238  -1328    -26       O  
HETATM 4927  O   HOH A 943      55.953 -19.003  22.501  1.00 44.74           O  
ANISOU 4927  O   HOH A 943     5379   6544   5075    258   -516    597       O  
HETATM 4928  O   HOH A 944      38.688   2.928  18.474  1.00 35.10           O  
ANISOU 4928  O   HOH A 944     4024   4400   4912   -615    433    357       O  
HETATM 4929  O   HOH A 945      43.115 -19.266  -1.255  1.00 38.52           O  
ANISOU 4929  O   HOH A 945     6041   4442   4154   -247     31    876       O  
HETATM 4930  O   HOH A 946      39.281  -3.372  22.680  1.00 40.48           O  
ANISOU 4930  O   HOH A 946     5152   4838   5388  -2239    627    327       O  
HETATM 4931  O   HOH A 947      35.604  12.538  32.048  1.00 44.98           O  
ANISOU 4931  O   HOH A 947     5660   6224   5207   -359   -364    -17       O  
HETATM 4932  O   HOH A 948      61.319  36.190  19.514  1.00 31.44           O  
ANISOU 4932  O   HOH A 948     3544   2597   5804    407   -768   -404       O  
HETATM 4933  O   HOH A 949      59.089  22.403  31.783  1.00 41.63           O  
ANISOU 4933  O   HOH A 949     4945   6123   4750   -148  -2161   -281       O  
HETATM 4934  O   HOH A 950      45.347   6.763  27.818  1.00 42.08           O  
ANISOU 4934  O   HOH A 950     5976   5899   4114   -252    113    673       O  
HETATM 4935  O   HOH A 951      39.796   4.231  25.584  1.00 35.55           O  
ANISOU 4935  O   HOH A 951     4446   4737   4322     61    625    678       O  
HETATM 4936  O   HOH A 952      34.412   4.837   9.674  1.00 40.02           O  
ANISOU 4936  O   HOH A 952     3814   4984   6408    295     38     32       O  
HETATM 4937  O   HOH A 953      50.857 -14.498  24.598  1.00 48.98           O  
ANISOU 4937  O   HOH A 953     6571   6277   5763    218   -158   -681       O  
HETATM 4938  O   HOH A 954      42.370  32.399   8.604  1.00 45.72           O  
ANISOU 4938  O   HOH A 954     6373   5417   5581    558   -568   -117       O  
HETATM 4939  O   HOH A 955      57.944 -22.622   9.383  1.00 41.96           O  
ANISOU 4939  O   HOH A 955     5260   4972   5709    -23    -56    104       O  
HETATM 4940  O   HOH A 956      46.625 -11.627  -4.955  1.00 38.88           O  
ANISOU 4940  O   HOH A 956     5360   5432   3979   -137  -1077    632       O  
HETATM 4941  O   HOH A 957      61.064  41.493  -0.352  1.00 35.01           O  
ANISOU 4941  O   HOH A 957     5472   2890   4941   -161    125    962       O  
HETATM 4942  O   HOH A 958      57.856   0.320  26.837  1.00 37.96           O  
ANISOU 4942  O   HOH A 958     5514   3680   5227    444  -1107    818       O  
HETATM 4943  O   HOH A 959      57.624  36.574   6.660  1.00 38.61           O  
ANISOU 4943  O   HOH A 959     4776   4879   5015  -2150   1621  -1882       O  
HETATM 4944  O   HOH A 960      37.135  18.505  35.986  1.00 32.56           O  
ANISOU 4944  O   HOH A 960     4596   4408   3366    406    881   -146       O  
HETATM 4945  O   HOH A 961      37.562  -3.937  15.262  1.00 42.26           O  
ANISOU 4945  O   HOH A 961     5126   5952   4980   -314   -245    807       O  
HETATM 4946  O   HOH A 962      63.395  20.887  15.242  1.00 25.72           O  
ANISOU 4946  O   HOH A 962     1823   1781   6168    130     23    146       O  
HETATM 4947  O   HOH A 963      47.700  33.998  19.002  1.00 24.22           O  
ANISOU 4947  O   HOH A 963     2444   2275   4481    995    813    902       O  
HETATM 4948  O   HOH A 964      40.548  14.843  14.669  1.00 28.76           O  
ANISOU 4948  O   HOH A 964     4664   1980   4281    -26   2463      5       O  
HETATM 4949  O   HOH A 965      66.953  -8.836   5.865  1.00 34.03           O  
ANISOU 4949  O   HOH A 965     2196   4371   6364   -314    -45   -476       O  
HETATM 4950  O   HOH A 966      55.432 -22.657   7.876  1.00 29.76           O  
ANISOU 4950  O   HOH A 966     3326   3562   4419   -569   -307  -1621       O  
HETATM 4951  O   HOH A 967      42.614  25.768  20.687  1.00 28.15           O  
ANISOU 4951  O   HOH A 967     3081   3699   3914   1477    -96   -515       O  
HETATM 4952  O   HOH A 968      57.501  30.023  28.936  1.00 29.06           O  
ANISOU 4952  O   HOH A 968     4284   3682   3073    660   -421  -1077       O  
HETATM 4953  O   HOH A 969      44.069  12.090  29.142  1.00 31.72           O  
ANISOU 4953  O   HOH A 969     4182   2829   5040    732   1465   1049       O  
HETATM 4954  O   HOH A 970      42.488  29.787  12.456  1.00 35.15           O  
ANISOU 4954  O   HOH A 970     4239   4368   4746   1650   -741   -217       O  
HETATM 4955  O   HOH A 971      59.086  25.953  29.849  1.00 33.63           O  
ANISOU 4955  O   HOH A 971     3775   4432   4572    513    255  -1826       O  
HETATM 4956  O   HOH A 972      46.186  30.856   7.665  1.00 30.49           O  
ANISOU 4956  O   HOH A 972     3651   3239   4695     -2    -64   -685       O  
HETATM 4957  O   HOH A 973      56.512  13.996   5.016  1.00 33.06           O  
ANISOU 4957  O   HOH A 973     3691   3914   4956    355   -756   1359       O  
HETATM 4958  O   HOH A 974      38.700  13.795  13.132  1.00 37.89           O  
ANISOU 4958  O   HOH A 974     3528   4870   5997   1285   1825    389       O  
HETATM 4959  O   HOH A 975      63.578 -13.272  -1.199  1.00 33.33           O  
ANISOU 4959  O   HOH A 975     4965   3611   4088   -350   1527   -488       O  
HETATM 4960  O   HOH A 976      49.420 -23.327  19.380  1.00 33.50           O  
ANISOU 4960  O   HOH A 976     4365   5270   3092    334    637   -300       O  
HETATM 4961  O   HOH A 977      63.567  12.310   8.933  1.00 33.67           O  
ANISOU 4961  O   HOH A 977     3345   3699   5749   -413   -362  -1574       O  
HETATM 4962  O   HOH A 978      51.596  22.057  33.661  1.00 34.38           O  
ANISOU 4962  O   HOH A 978     4771   3639   4654    347    -18   -684       O  
HETATM 4963  O   HOH A 979      41.460  29.917   9.629  1.00 38.10           O  
ANISOU 4963  O   HOH A 979     4297   4744   5436   1290    924  -1034       O  
HETATM 4964  O   HOH A 980      43.709  -5.518  -4.563  1.00 38.23           O  
ANISOU 4964  O   HOH A 980     4893   5660   3972    228   -284    940       O  
HETATM 4965  O   HOH A 981      42.208 -10.609  -2.797  1.00 31.37           O  
ANISOU 4965  O   HOH A 981     4959   3651   3308   -602   -916   -131       O  
HETATM 4966  O   HOH A 982      50.911  -7.984  26.257  1.00 40.65           O  
ANISOU 4966  O   HOH A 982     5342   5530   4571   1219   -179    914       O  
HETATM 4967  O   HOH A 983      36.444   1.270  14.768  1.00 32.91           O  
ANISOU 4967  O   HOH A 983     2773   4583   5146   -463    103    433       O  
HETATM 4968  O   HOH A 984      56.553  -1.786  -6.604  1.00 36.74           O  
ANISOU 4968  O   HOH A 984     6005   3882   4073    -89   -554   1358       O  
HETATM 4969  O   HOH A 985      60.713  35.124  25.381  1.00 41.78           O  
ANISOU 4969  O   HOH A 985     6227   4073   5573   -966   -265   -139       O  
HETATM 4970  O   HOH A 986      54.573  37.764  22.227  1.00 43.35           O  
ANISOU 4970  O   HOH A 986     5524   5478   5469  -1853   -180  -1167       O  
HETATM 4971  O   HOH A 987      56.556  38.522  -3.459  1.00 39.44           O  
ANISOU 4971  O   HOH A 987     5427   4617   4939    504   -113    601       O  
HETATM 4972  O   HOH A 988      36.506  21.017  34.894  1.00 37.78           O  
ANISOU 4972  O   HOH A 988     5273   4738   4342    964    612    -35       O  
HETATM 4973  O   HOH A 989      59.123  32.180  28.630  1.00 43.32           O  
ANISOU 4973  O   HOH A 989     6291   5107   5060   -684   -292   -749       O  
HETATM 4974  O   HOH A 990      34.576   0.987   7.280  1.00 41.16           O  
ANISOU 4974  O   HOH A 990     4683   5200   5756   -325    558    449       O  
HETATM 4975  O   HOH A 991      67.072 -11.111  -0.784  1.00 43.93           O  
ANISOU 4975  O   HOH A 991     5463   5687   5540   -277    468    703       O  
HETATM 4976  O   HOH A 992      50.623  -7.338  29.086  1.00 41.21           O  
ANISOU 4976  O   HOH A 992     5431   5355   4871    411    -81    144       O  
HETATM 4977  O   HOH A 993      55.948 -20.683   5.723  1.00 37.79           O  
ANISOU 4977  O   HOH A 993     5450   4616   4292    237  -1000   1093       O  
HETATM 4978  O   HOH A 994      47.377 -11.824  25.011  1.00 49.56           O  
ANISOU 4978  O   HOH A 994     6242   5783   6804    523    -15   -649       O  
HETATM 4979  O   HOH A 995      66.777  29.678  20.269  1.00 40.81           O  
ANISOU 4979  O   HOH A 995     4622   5325   5558   1098    292    468       O  
HETATM 4980  O   HOH A 996      67.160   8.729  30.286  1.00 46.94           O  
ANISOU 4980  O   HOH A 996     5516   5269   7050     83   -254    549       O  
HETATM 4981  O   HOH A 997      60.329   5.809  30.272  1.00 43.35           O  
ANISOU 4981  O   HOH A 997     5757   5762   4953     76   -608   1114       O  
HETATM 4982  O   HOH A 998      41.221 -13.218  -2.989  1.00 47.74           O  
ANISOU 4982  O   HOH A 998     6070   6020   6047    -27   -864   -773       O  
HETATM 4983  O   HOH A 999      47.048  -7.297  -5.779  1.00 35.07           O  
ANISOU 4983  O   HOH A 999     5453   3417   4453   -336   -595   -382       O  
HETATM 4984  O   HOH A1000      38.828   8.766   5.365  1.00 36.37           O  
ANISOU 4984  O   HOH A1000     5017   4828   3975   -514    146   1342       O  
HETATM 4985  O   HOH A1001      48.992   3.219  28.717  1.00 37.30           O  
ANISOU 4985  O   HOH A1001     5887   4099   4184   -445    734   -633       O  
HETATM 4986  O   HOH A1002      33.524  -0.920   6.226  1.00 46.19           O  
ANISOU 4986  O   HOH A1002     5496   5774   6279    749   -172    796       O  
HETATM 4987  O   HOH A1003      38.327  18.315   6.634  1.00 44.11           O  
ANISOU 4987  O   HOH A1003     5994   5189   5576    303    702   -826       O  
HETATM 4988  O   HOH A1004      55.658  41.169  -0.330  1.00 38.78           O  
ANISOU 4988  O   HOH A1004     5819   3211   5704   -635  -1164    610       O  
HETATM 4989  O   HOH A1005      34.762 -16.452   4.738  1.00 44.91           O  
ANISOU 4989  O   HOH A1005     5972   5353   5738  -1520   -271   -180       O  
HETATM 4990  O   HOH A1006      34.679  20.872  32.594  1.00 47.91           O  
ANISOU 4990  O   HOH A1006     5747   6192   6264   1371    293    263       O  
HETATM 4991  O   HOH A1007      49.229  17.782  37.203  1.00 38.33           O  
ANISOU 4991  O   HOH A1007     3734   6390   4439   1073   -882  -1107       O  
HETATM 4992  O   HOH A1008      36.838 -13.329  -0.007  1.00 47.36           O  
ANISOU 4992  O   HOH A1008     6920   5306   5768  -1093   -770   -896       O  
HETATM 4993  O   HOH A1009      51.695   5.487  21.546  1.00 19.71           O  
ANISOU 4993  O   HOH A1009     3611   1550   2328   -694    278    143       O  
HETATM 4994  O   HOH A1010      60.694 -11.791  24.914  1.00 42.99           O  
ANISOU 4994  O   HOH A1010     5831   5542   4962    166   -427   1044       O  
HETATM 4995  O   HOH A1011      61.179 -11.078  27.307  1.00 37.54           O  
ANISOU 4995  O   HOH A1011     3477   5728   5057  -1134  -1327    654       O  
HETATM 4996  O   HOH A1012      43.436  -3.368  28.259  1.00 39.32           O  
ANISOU 4996  O   HOH A1012     5702   4302   4934   -242   1112    627       O  
HETATM 4997  O   HOH A1013      53.561  40.506  11.174  1.00 41.71           O  
ANISOU 4997  O   HOH A1013     5817   4141   5891   -709   -145   -433       O  
HETATM 4998  O   HOH A1014      63.294 -19.845  -6.176  1.00 46.50           O  
ANISOU 4998  O   HOH A1014     6038   5220   6409   -497    899    -96       O  
HETATM 4999  O   HOH A1015      64.633  19.708  29.217  1.00 42.86           O  
ANISOU 4999  O   HOH A1015     5835   5178   5271   -238     46  -1337       O  
HETATM 5000  O   HOH A1016      45.697   4.274  27.472  1.00 41.37           O  
ANISOU 5000  O   HOH A1016     5816   5338   4563    401    894  -1806       O  
HETATM 5001  O   HOH A1017      49.209 -18.884  24.819  1.00 47.54           O  
ANISOU 5001  O   HOH A1017     6681   5875   5505    227    580    486       O  
HETATM 5002  O   HOH A1018      47.886 -17.317  25.646  1.00 51.29           O  
ANISOU 5002  O   HOH A1018     6583   6624   6282   -157    190    -25       O  
HETATM 5003  O   HOH A1019      56.512 -15.169   9.339  1.00 24.98           O  
ANISOU 5003  O   HOH A1019     3421   2261   3807   -827    444   -195       O  
HETATM 5004  O   HOH A1020      53.116 -21.426  -0.955  1.00 32.71           O  
ANISOU 5004  O   HOH A1020     5064   3304   4060  -1361   1112   -772       O  
HETATM 5005  O   HOH A1021      64.631  -3.513  -2.721  1.00 40.22           O  
ANISOU 5005  O   HOH A1021     4763   5322   5197    661   1299    192       O  
HETATM 5006  O   HOH A1022      49.522  38.507   6.588  1.00 34.73           O  
ANISOU 5006  O   HOH A1022     4328   3715   5152    604  -1405  -1210       O  
HETATM 5007  O   HOH A1023      41.010 -18.769  -2.614  1.00 40.21           O  
ANISOU 5007  O   HOH A1023     6025   4543   4711  -2277    392    875       O  
HETATM 5008  O   HOH A1024      48.365  33.786   9.845  1.00  7.89           O  
ANISOU 5008  O   HOH A1024     1289    835    873    559      2    -21       O  
HETATM 5009  O   HOH A1025      51.254  20.038   6.918  1.00 20.07           O  
ANISOU 5009  O   HOH A1025     2877   2372   2377    446    167    -98       O  
HETATM 5010  O   HOH A1026      37.966  15.521  16.544  1.00 28.92           O  
ANISOU 5010  O   HOH A1026     4123   3467   3397   -411    389    507       O  
HETATM 5011  O   HOH A1027      67.966  26.772  13.451  1.00 43.92           O  
ANISOU 5011  O   HOH A1027     5956   5750   4982  -1018    648   -180       O  
HETATM 5012  O   HOH A1028      64.353   3.525  25.069  1.00 39.24           O  
ANISOU 5012  O   HOH A1028     5440   4272   5195   1657    546    497       O  
HETATM 5013  O   HOH A1029      74.816  17.344  23.576  1.00 42.18           O  
ANISOU 5013  O   HOH A1029     4547   5611   5867     85  -1923   -827       O  
HETATM 5014  O   HOH A1030      50.552  30.306  31.357  1.00 43.79           O  
ANISOU 5014  O   HOH A1030     5877   5781   4980    933    293   1362       O  
HETATM 5015  O   HOH A1031      53.975 -14.197  22.115  1.00 46.94           O  
ANISOU 5015  O   HOH A1031     5778   6315   5741   -997   -859    811       O  
HETATM 5016  O   HOH A1032      37.000   7.413   6.445  1.00 38.61           O  
ANISOU 5016  O   HOH A1032     4598   4880   5190    497   -240   1269       O  
HETATM 5017  O   HOH A1033      51.428  41.878   1.704  1.00 47.72           O  
ANISOU 5017  O   HOH A1033     6475   5347   6308     38    -63    557       O  
HETATM 5018  O   HOH A1034      48.947  21.440   5.591  1.00 20.91           O  
ANISOU 5018  O   HOH A1034     2186   2809   2948    755   -450   -325       O  
HETATM 5019  O   HOH A1035      56.396 -21.358  12.349  1.00 32.76           O  
ANISOU 5019  O   HOH A1035     4250   3316   4882   -447   -861    -12       O  
HETATM 5020  O   HOH A1036      48.681   1.133  26.822  1.00 34.82           O  
ANISOU 5020  O   HOH A1036     5648   4627   2954   -440    516    577       O  
HETATM 5021  O   HOH A1037      64.626 -10.270  -4.325  1.00 40.99           O  
ANISOU 5021  O   HOH A1037     5954   5733   3887   1401   1376    621       O  
HETATM 5022  O   HOH A1038      47.455 -26.025  16.670  1.00 32.27           O  
ANISOU 5022  O   HOH A1038     4009   3607   4644   -847     49    927       O  
HETATM 5023  O   HOH A1039      38.655   9.536  12.029  1.00 44.57           O  
ANISOU 5023  O   HOH A1039     4825   6085   6023    398    312    127       O  
HETATM 5024  O   HOH A1040      66.022  27.707  18.026  1.00 43.30           O  
ANISOU 5024  O   HOH A1040     5288   5781   5384   -284   -302   -921       O  
HETATM 5025  O   HOH A1041      69.089 -15.434   6.333  1.00 51.71           O  
ANISOU 5025  O   HOH A1041     6653   6611   6381    742    237    -90       O  
HETATM 5026  O   HOH A1042      65.857   6.467  26.518  1.00 33.33           O  
ANISOU 5026  O   HOH A1042     3329   5583   3751   1482   -137   1479       O  
HETATM 5027  O   HOH A1043      63.854  -7.830  -7.115  1.00 41.84           O  
ANISOU 5027  O   HOH A1043     5237   5070   5588    123   2298  -1541       O  
HETATM 5028  O   HOH A1044      54.883  15.444  36.257  1.00 48.56           O  
ANISOU 5028  O   HOH A1044     6576   6112   5761   -665    -22   -660       O  
HETATM 5029  O   HOH A1045      54.229  39.203   8.280  1.00 44.67           O  
ANISOU 5029  O   HOH A1045     5910   4169   6892   -163   -137   -393       O  
HETATM 5030  O   HOH A1046      58.795  35.172   8.996  1.00 41.91           O  
ANISOU 5030  O   HOH A1046     5159   5018   5745   1006   -472   -744       O  
HETATM 5031  O   HOH A1047      40.208  -7.286  -4.312  1.00 43.33           O  
ANISOU 5031  O   HOH A1047     6384   5730   4347   -717   -858   -788       O  
HETATM 5032  O   HOH A1048      69.645 -18.734   7.167  1.00 47.07           O  
ANISOU 5032  O   HOH A1048     5672   6232   5979    -98   -190    105       O  
HETATM 5033  O   HOH A1049      56.532  32.071  32.460  1.00 52.64           O  
ANISOU 5033  O   HOH A1049     6842   6727   6430    147    -91   -436       O  
HETATM 5034  O   HOH A1050      61.015  16.321  33.053  1.00 38.66           O  
ANISOU 5034  O   HOH A1050     5154   4961   4573   -168  -1366    375       O  
HETATM 5035  O   HOH A1051      46.896 -23.314  16.484  1.00 37.38           O  
ANISOU 5035  O   HOH A1051     5060   4971   4170  -1517  -1697    711       O  
HETATM 5036  O   HOH A1052      60.959  29.754  17.135  1.00 36.30           O  
ANISOU 5036  O   HOH A1052     3943   4527   5320   -898   -555   -282       O  
HETATM 5037  O   HOH A1053      67.830  24.320  24.352  1.00 37.08           O  
ANISOU 5037  O   HOH A1053     4305   4823   4959    191    -87   -210       O  
HETATM 5038  O   HOH A1054      74.595  16.192  25.704  1.00 47.93           O  
ANISOU 5038  O   HOH A1054     5561   5672   6979   -340    183    -25       O  
HETATM 5039  O   HOH A1055      60.844  -2.428  23.612  1.00 41.30           O  
ANISOU 5039  O   HOH A1055     5458   5096   5136    437  -1158    345       O  
HETATM 5040  O   HOH A1056      57.467 -23.058   7.204  1.00 43.55           O  
ANISOU 5040  O   HOH A1056     5223   5242   6082   -599    122   -183       O  
HETATM 5041  O   HOH A1057      64.351  -6.858  -8.847  1.00 47.97           O  
ANISOU 5041  O   HOH A1057     5976   6870   5380    127    885   -288       O  
HETATM 5042  O   HOH A1058      38.322  -3.108  19.159  1.00 39.93           O  
ANISOU 5042  O   HOH A1058     4577   5339   5253  -1465   1088    117       O  
HETATM 5043  O   HOH A1059      55.795  18.317  35.725  1.00 47.45           O  
ANISOU 5043  O   HOH A1059     6532   6409   5086   -152   -970   -217       O  
HETATM 5044  O   HOH A1060      67.639  -9.337   0.921  1.00 51.61           O  
ANISOU 5044  O   HOH A1060     6217   6474   6919    331    972   -611       O  
HETATM 5045  O   HOH A1061      48.720  36.385   9.713  1.00 42.75           O  
ANISOU 5045  O   HOH A1061     5543   6046   4654   -255    772   -341       O  
HETATM 5046  O   HOH A1062      35.676  14.963  32.256  1.00 51.61           O  
ANISOU 5046  O   HOH A1062     6203   7053   6351    362    517     30       O  
HETATM 5047  O   HOH A1063      33.800  21.852  10.869  1.00 49.36           O  
ANISOU 5047  O   HOH A1063     5981   6477   6297   -189   -655   -863       O  
HETATM 5048  O   HOH A1064      35.053   5.994   4.797  1.00 52.00           O  
ANISOU 5048  O   HOH A1064     7007   6308   6442    157   -298     37       O  
HETATM 5049  O   HOH A1065      60.119  42.584   4.106  1.00 47.79           O  
ANISOU 5049  O   HOH A1065     6067   5785   6307    313   -739   -441       O  
HETATM 5050  O   HOH A1066      49.182 -11.311  -5.798  1.00 46.97           O  
ANISOU 5050  O   HOH A1066     6513   6056   5278    355     61    120       O  
HETATM 5051  O   HOH A1067      47.751  38.190  -0.893  1.00 48.68           O  
ANISOU 5051  O   HOH A1067     6189   6095   6210    495    234    -99       O  
HETATM 5052  O   HOH A1068      45.991 -15.011  -2.943  1.00 40.45           O  
ANISOU 5052  O   HOH A1068     5896   5170   4303   -919   -647  -1299       O  
HETATM 5053  O   HOH A1069      45.520  35.141   0.327  1.00 51.13           O  
ANISOU 5053  O   HOH A1069     6429   6710   6289    640   -554    169       O  
HETATM 5054  O   HOH A1070      31.840  -2.369   9.000  1.00 44.71           O  
ANISOU 5054  O   HOH A1070     4964   5990   6033    490    351  -1155       O  
HETATM 5055  O   HOH A1071      49.822  40.913  10.711  1.00 47.18           O  
ANISOU 5055  O   HOH A1071     5978   5591   6357    622   -327    526       O  
HETATM 5056  O   HOH A1072      59.478  40.596  -2.391  1.00 48.45           O  
ANISOU 5056  O   HOH A1072     6641   5118   6648    670   -627    446       O  
HETATM 5057  O   HOH A1073      60.917  -2.763  17.672  1.00 47.26           O  
ANISOU 5057  O   HOH A1073     5376   5807   6774    634   -143    651       O  
HETATM 5058  O   HOH A1074      63.612 -19.268  -8.854  1.00 43.17           O  
ANISOU 5058  O   HOH A1074     5829   5023   5549   -247    917    142       O  
HETATM 5059  O   HOH A1075      54.726  39.121  19.188  1.00 45.84           O  
ANISOU 5059  O   HOH A1075     6014   4984   6419   -584   -100  -1030       O  
HETATM 5060  O   HOH A1076      43.978  31.697   2.901  1.00 51.72           O  
ANISOU 5060  O   HOH A1076     6099   6256   7294    236   -619     93       O  
HETATM 5061  O   HOH A1077      37.950   3.478  27.948  1.00 52.11           O  
ANISOU 5061  O   HOH A1077     6425   6564   6808   -354    438    486       O  
HETATM 5062  O   HOH A1078      63.613  36.716   9.325  1.00 50.18           O  
ANISOU 5062  O   HOH A1078     6784   6217   6063   -151    182   -481       O  
HETATM 5063  O   HOH A1079      46.091  39.493   0.291  1.00 51.38           O  
ANISOU 5063  O   HOH A1079     6549   6422   6550    167   -145    579       O  
HETATM 5064  O   HOH A1080      31.745   1.373   3.514  1.00 50.68           O  
ANISOU 5064  O   HOH A1080     6099   6719   6439    211    185   -639       O  
HETATM 5065  O   HOH A1081      59.746  29.189  32.251  1.00 52.43           O  
ANISOU 5065  O   HOH A1081     6696   6802   6423   -152   -558   -492       O  
HETATM 5066  O   HOH A1082      46.670   3.357  -1.827  1.00 38.32           O  
ANISOU 5066  O   HOH A1082     5220   3876   5465  -1436  -2171   -325       O  
HETATM 5067  O   HOH A1083      40.057  15.930  36.874  1.00 28.71           O  
ANISOU 5067  O   HOH A1083     3739   3883   3284     45   -209   -769       O  
HETATM 5068  O   HOH A1084      57.305  19.651   4.795  1.00 32.69           O  
ANISOU 5068  O   HOH A1084     3420   4034   4966   -498    237   1180       O  
HETATM 5069  O   HOH A1085      68.410  23.703  13.385  1.00 33.53           O  
ANISOU 5069  O   HOH A1085     3990   4678   4072   -496   -695  -1144       O  
HETATM 5070  O   HOH A1086      49.037  26.288  27.340  1.00 34.93           O  
ANISOU 5070  O   HOH A1086     4228   4260   4783   -182    301    -51       O  
HETATM 5071  O   HOH A1087      49.911  30.097  27.919  1.00 33.82           O  
ANISOU 5071  O   HOH A1087     5540   3440   3868   1133  -1578   -622       O  
HETATM 5072  O   HOH A1088      53.576  20.101   8.729  1.00 29.37           O  
ANISOU 5072  O   HOH A1088     4215   2157   4786    691    -55   -223       O  
HETATM 5073  O   HOH A1089      37.905  23.240  35.378  1.00 36.19           O  
ANISOU 5073  O   HOH A1089     5033   4860   3856   1161   -110    981       O  
HETATM 5074  O   HOH A1090      61.102   6.627  32.424  1.00 36.51           O  
ANISOU 5074  O   HOH A1090     5135   3897   4840   -574    712   -311       O  
HETATM 5075  O   HOH A1091      40.304 -21.624  22.405  1.00 36.34           O  
ANISOU 5075  O   HOH A1091     5868   4418   3519  -2014    478   -681       O  
HETATM 5076  O   HOH A1092      40.658 -16.648  -0.747  1.00 37.36           O  
ANISOU 5076  O   HOH A1092     4431   6165   3599      1   -997    -29       O  
HETATM 5077  O   HOH A1093      64.268  26.772  25.345  1.00 42.63           O  
ANISOU 5077  O   HOH A1093     5145   4331   6721    716  -1431    657       O  
HETATM 5078  O   HOH A1094      58.132 -19.224   9.292  1.00 44.84           O  
ANISOU 5078  O   HOH A1094     5739   6290   5009   -613   -297  -1022       O  
HETATM 5079  O   HOH A1095      40.489 -10.557  16.987  1.00 45.14           O  
ANISOU 5079  O   HOH A1095     6381   5195   5574   -247   -464   -226       O  
HETATM 5080  O   HOH A1096      58.344  18.023  35.937  1.00 53.68           O  
ANISOU 5080  O   HOH A1096     6976   6868   6551   -536    101   -493       O  
HETATM 5081  O   HOH A1097      34.743  13.916  34.208  1.00 48.96           O  
ANISOU 5081  O   HOH A1097     6279   6449   5874    229   -709    822       O  
HETATM 5082  O   HOH A1098      69.915 -15.379  10.911  1.00 48.12           O  
ANISOU 5082  O   HOH A1098     6067   5924   6293    966  -1135     83       O  
HETATM 5083  O   HOH A1099      50.960  16.984  35.646  1.00 50.61           O  
ANISOU 5083  O   HOH A1099     6134   6571   6524   -160   -179    -70       O  
HETATM 5084  O   HOH A1100      35.251  20.717   9.504  1.00 50.29           O  
ANISOU 5084  O   HOH A1100     5833   6334   6942   -109   -620   -347       O  
HETATM 5085  O   HOH A1101      41.527 -12.002  17.955  1.00 52.94           O  
ANISOU 5085  O   HOH A1101     7205   6570   6338    121    596    212       O  
HETATM 5086  O   HOH A1102      66.002  -6.724  -7.043  1.00 50.35           O  
ANISOU 5086  O   HOH A1102     6217   6334   6579   -709    659     85       O  
HETATM 5087  O   HOH A1103      46.261  36.494  33.031  1.00 53.47           O  
ANISOU 5087  O   HOH A1103     7005   6750   6560   -138   -101    103       O  
HETATM 5088  O   HOH A1104      34.039  12.976  23.951  1.00 45.37           O  
ANISOU 5088  O   HOH A1104     5702   6090   5444    764    659   -317       O  
HETATM 5089  O   HOH A1105      48.389 -16.470  -4.067  1.00 53.62           O  
ANISOU 5089  O   HOH A1105     7022   6724   6626    221   -158   -330       O  
HETATM 5090  O   HOH A1106      62.883 -17.916   7.181  1.00 53.81           O  
ANISOU 5090  O   HOH A1106     6967   6861   6618    328   -893    567       O  
HETATM 5091  O   HOH A1107      66.846 -13.767   1.276  1.00 47.21           O  
ANISOU 5091  O   HOH A1107     5757   5955   6224    148   -192   -186       O  
HETATM 5092  O   HOH A1108      31.377  -4.387   5.935  1.00 53.17           O  
ANISOU 5092  O   HOH A1108     6518   6801   6882    196   -469    -48       O  
HETATM 5093  O   HOH A1109      54.160  40.577  15.510  1.00 54.57           O  
ANISOU 5093  O   HOH A1109     7093   6690   6951    182     74    414       O  
HETATM 5094  O   HOH A1110      35.195  -2.278  15.795  1.00 48.30           O  
ANISOU 5094  O   HOH A1110     5984   6422   5946   1013    316     45       O  
HETATM 5095  O   HOH A1111      61.992  27.977  28.011  1.00 49.03           O  
ANISOU 5095  O   HOH A1111     6087   6575   5966   -584   -969   1317       O  
HETATM 5096  O   HOH B 701      38.724  22.683  -6.848  1.00 24.48           O  
ANISOU 5096  O   HOH B 701     3175   3746   2379   2001    345    214       O  
HETATM 5097  O   HOH B 702      77.335   8.547   9.640  1.00 10.81           O  
ANISOU 5097  O   HOH B 702      803   1188   2114    274   -128    140       O  
HETATM 5098  O   HOH B 703      60.773   5.581 -10.095  1.00 32.08           O  
ANISOU 5098  O   HOH B 703     2147   4657   5385    319   -403  -2974       O  
HETATM 5099  O   HOH B 704      63.942  31.251  -8.447  1.00 15.75           O  
ANISOU 5099  O   HOH B 704     2336   1368   2280   -283     -7     38       O  
HETATM 5100  O   HOH B 705      68.979  11.542  -2.221  1.00 10.55           O  
ANISOU 5100  O   HOH B 705     1218   1069   1722    172   -108   -102       O  
HETATM 5101  O   HOH B 706      59.248  17.668  -5.907  1.00  9.84           O  
ANISOU 5101  O   HOH B 706     1163    785   1791     92     91    -15       O  
HETATM 5102  O   HOH B 707      57.631  22.500   5.414  1.00 24.60           O  
ANISOU 5102  O   HOH B 707     3065   2411   3869    706    819    975       O  
HETATM 5103  O   HOH B 708      74.671   9.809  10.675  1.00 14.01           O  
ANISOU 5103  O   HOH B 708     1196   1640   2487    363   -396   -166       O  
HETATM 5104  O   HOH B 709      65.436   7.383  -3.005  1.00 12.11           O  
ANISOU 5104  O   HOH B 709     1333   1141   2128     97   -131     43       O  
HETATM 5105  O   HOH B 710      49.395   3.304 -19.171  1.00 20.75           O  
ANISOU 5105  O   HOH B 710     3147   2588   2148   -577   -628   -204       O  
HETATM 5106  O   HOH B 711      69.313  14.469 -16.342  1.00 38.19           O  
ANISOU 5106  O   HOH B 711     3432   6340   4736   1486   -546  -2592       O  
HETATM 5107  O   HOH B 712      79.335  22.535  12.881  1.00 33.06           O  
ANISOU 5107  O   HOH B 712     5024   3123   4415   1198   -689   -235       O  
HETATM 5108  O   HOH B 713      51.302   6.931  -2.191  1.00 13.42           O  
ANISOU 5108  O   HOH B 713     1674   1515   1909    -14   -105   -119       O  
HETATM 5109  O   HOH B 714      63.250  15.304  -9.020  1.00 11.16           O  
ANISOU 5109  O   HOH B 714     1315   1048   1877     46    138     22       O  
HETATM 5110  O   HOH B 715      46.090  23.998 -17.679  1.00 15.35           O  
ANISOU 5110  O   HOH B 715     2181   1614   2035      1    -39    -95       O  
HETATM 5111  O   HOH B 716      44.794  12.077   4.558  1.00 12.36           O  
ANISOU 5111  O   HOH B 716     1624   1426   1647    383    150    217       O  
HETATM 5112  O   HOH B 717      75.246   9.516 -13.651  1.00 21.23           O  
ANISOU 5112  O   HOH B 717     2037   2752   3278    292    885    -83       O  
HETATM 5113  O   HOH B 718      46.965  16.279 -14.586  1.00 13.54           O  
ANISOU 5113  O   HOH B 718     1955   1501   1689    398   -513    -55       O  
HETATM 5114  O   HOH B 719      58.083  13.461   2.269  1.00 14.61           O  
ANISOU 5114  O   HOH B 719     1851   1471   2229    534    159    173       O  
HETATM 5115  O   HOH B 720      72.344  12.915  17.736  1.00 19.78           O  
ANISOU 5115  O   HOH B 720     3056   1946   2514   1073   -762   -341       O  
HETATM 5116  O   HOH B 721      51.640  13.221 -13.545  1.00 13.02           O  
ANISOU 5116  O   HOH B 721     1401   1611   1936     22     54    -18       O  
HETATM 5117  O   HOH B 722      66.904  20.916  17.414  1.00 15.27           O  
ANISOU 5117  O   HOH B 722     1814   1335   2653    222   -322   -257       O  
HETATM 5118  O   HOH B 723      66.727   5.432  -8.745  1.00 19.64           O  
ANISOU 5118  O   HOH B 723     2375   2287   2800    487    320    352       O  
HETATM 5119  O   HOH B 724      49.326  23.683 -18.790  1.00 16.54           O  
ANISOU 5119  O   HOH B 724     2348   1691   2246    141    -64    519       O  
HETATM 5120  O   HOH B 725      69.749  33.281  -4.273  1.00 21.03           O  
ANISOU 5120  O   HOH B 725     2764   1950   3275   -644    152    154       O  
HETATM 5121  O   HOH B 726      53.302  15.775 -10.457  1.00 13.77           O  
ANISOU 5121  O   HOH B 726     1449   1371   2410    322    243     64       O  
HETATM 5122  O   HOH B 727      52.850  11.127 -15.421  1.00 13.23           O  
ANISOU 5122  O   HOH B 727     1627   1395   2005     77   -146     86       O  
HETATM 5123  O   HOH B 728      49.919   8.276   1.505  1.00 11.48           O  
ANISOU 5123  O   HOH B 728     1410   1448   1502    102     21   -283       O  
HETATM 5124  O   HOH B 729      60.465  24.279 -10.524  1.00 16.52           O  
ANISOU 5124  O   HOH B 729     2530   1801   1944    487    -80    111       O  
HETATM 5125  O   HOH B 730      64.457  22.890  10.870  1.00 15.58           O  
ANISOU 5125  O   HOH B 730     1806   1758   2354    192   -175    -83       O  
HETATM 5126  O   HOH B 731      55.993  11.546  -6.342  1.00 17.21           O  
ANISOU 5126  O   HOH B 731     1631   3365   1541   -727   -144    657       O  
HETATM 5127  O   HOH B 732      74.955  24.679  -6.997  1.00 15.77           O  
ANISOU 5127  O   HOH B 732     1493   1833   2667   -245    337    123       O  
HETATM 5128  O   HOH B 733      62.119   8.284 -16.125  1.00 22.23           O  
ANISOU 5128  O   HOH B 733     2397   2941   3106   -397   1227  -1070       O  
HETATM 5129  O   HOH B 734      46.786   0.659 -12.833  1.00 18.64           O  
ANISOU 5129  O   HOH B 734     3317   1512   2254    -54   -660   -218       O  
HETATM 5130  O   HOH B 735      54.303  10.428 -18.522  1.00 15.62           O  
ANISOU 5130  O   HOH B 735     2322   1465   2148    -36     -8   -364       O  
HETATM 5131  O   HOH B 736      66.232  11.621  -2.965  1.00 11.55           O  
ANISOU 5131  O   HOH B 736     1061   1230   2097    148    -85   -286       O  
HETATM 5132  O   HOH B 737      70.413   4.506   8.776  1.00 16.17           O  
ANISOU 5132  O   HOH B 737     1846   1573   2726     40    -14   -295       O  
HETATM 5133  O   HOH B 738      61.196  33.969  -2.375  1.00 17.21           O  
ANISOU 5133  O   HOH B 738     2152   1411   2975    110    188    214       O  
HETATM 5134  O   HOH B 739      37.181   5.747  -7.510  1.00 16.94           O  
ANISOU 5134  O   HOH B 739     1811   2465   2161   -261   -147    391       O  
HETATM 5135  O   HOH B 740      62.419  28.838 -10.334  1.00 18.00           O  
ANISOU 5135  O   HOH B 740     2198   1633   3009    379    465    575       O  
HETATM 5136  O   HOH B 741      73.109  26.935   3.990  1.00 15.05           O  
ANISOU 5136  O   HOH B 741     1790   1572   2355   -672   -392    -78       O  
HETATM 5137  O   HOH B 742      44.132   1.060 -11.666  1.00 18.82           O  
ANISOU 5137  O   HOH B 742     2480   2112   2558      1   -476   -256       O  
HETATM 5138  O   HOH B 743      65.725  24.914 -13.731  1.00 17.35           O  
ANISOU 5138  O   HOH B 743     2392   1920   2280   -368    258   -458       O  
HETATM 5139  O   HOH B 744      43.082  19.392   1.954  1.00 20.49           O  
ANISOU 5139  O   HOH B 744     1667   4076   2042     86    -29   -228       O  
HETATM 5140  O   HOH B 745      39.445  10.246  -5.869  1.00 15.44           O  
ANISOU 5140  O   HOH B 745     1504   2058   2304     54   -712    293       O  
HETATM 5141  O   HOH B 746      75.183   6.659  -4.013  1.00 19.44           O  
ANISOU 5141  O   HOH B 746     1997   1775   3613    -97    624    101       O  
HETATM 5142  O   HOH B 747      75.251  27.478  -6.706  1.00 19.39           O  
ANISOU 5142  O   HOH B 747     2027   2096   3243   -770    455     39       O  
HETATM 5143  O   HOH B 748      45.721   1.375 -17.234  1.00 17.87           O  
ANISOU 5143  O   HOH B 748     2531   1818   2440   -344   -543   -166       O  
HETATM 5144  O   HOH B 749      67.906   4.471   7.345  1.00 15.10           O  
ANISOU 5144  O   HOH B 749     1974   1589   2175   -293    248    -55       O  
HETATM 5145  O   HOH B 750      58.501  11.028  -5.384  1.00 18.78           O  
ANISOU 5145  O   HOH B 750     1447   2362   3325    531    285   1083       O  
HETATM 5146  O   HOH B 751      73.936  25.236  -3.219  1.00 14.74           O  
ANISOU 5146  O   HOH B 751     1411   1630   2559   -304    -27   -196       O  
HETATM 5147  O   HOH B 752      57.879  21.213 -15.130  1.00 21.79           O  
ANISOU 5147  O   HOH B 752     3876   2058   2346   -739    582   -347       O  
HETATM 5148  O   HOH B 753      61.211   9.842   4.545  1.00 17.03           O  
ANISOU 5148  O   HOH B 753     1906   1864   2700     12   -228    389       O  
HETATM 5149  O   HOH B 754      73.720  22.774  -5.387  1.00 15.50           O  
ANISOU 5149  O   HOH B 754     1636   1671   2581   -122    273    -47       O  
HETATM 5150  O   HOH B 755      75.205   1.816  11.888  1.00 32.97           O  
ANISOU 5150  O   HOH B 755     4547   2419   5559   1113  -1485   -548       O  
HETATM 5151  O   HOH B 756      54.217  16.848 -15.227  1.00 14.74           O  
ANISOU 5151  O   HOH B 756     1846   1707   2047     27    -18   -103       O  
HETATM 5152  O   HOH B 757      65.848  20.909  14.281  1.00 21.70           O  
ANISOU 5152  O   HOH B 757     2730   2254   3262    927   -882   -431       O  
HETATM 5153  O   HOH B 758      68.469  23.968 -12.684  1.00 21.17           O  
ANISOU 5153  O   HOH B 758     3329   2477   2238  -1105    777   -355       O  
HETATM 5154  O   HOH B 759      68.558   5.364 -10.912  1.00 26.03           O  
ANISOU 5154  O   HOH B 759     3612   3235   3044    214    594   -515       O  
HETATM 5155  O   HOH B 760      65.701  20.301  -7.265  1.00 19.79           O  
ANISOU 5155  O   HOH B 760     2651   2011   2857   -155   -680    116       O  
HETATM 5156  O   HOH B 761      74.054  17.921  20.596  1.00 27.53           O  
ANISOU 5156  O   HOH B 761     2508   3265   4686   -837  -1388   -387       O  
HETATM 5157  O   HOH B 762      37.499   4.420 -10.013  1.00 17.83           O  
ANISOU 5157  O   HOH B 762     1873   2538   2361   -144   -331    676       O  
HETATM 5158  O   HOH B 763      74.809  31.258   0.037  1.00 26.90           O  
ANISOU 5158  O   HOH B 763     3407   2281   4532   -789    475   -476       O  
HETATM 5159  O   HOH B 764      65.289  -0.684   1.527  1.00 19.19           O  
ANISOU 5159  O   HOH B 764     2316   1606   3368   -425     39     78       O  
HETATM 5160  O   HOH B 765      48.751  -1.440 -20.459  1.00 24.87           O  
ANISOU 5160  O   HOH B 765     3072   2830   3547    347   -382  -1129       O  
HETATM 5161  O   HOH B 766      47.036  23.017 -20.290  1.00 20.19           O  
ANISOU 5161  O   HOH B 766     2292   2048   3331    317    790    604       O  
HETATM 5162  O   HOH B 767      72.772  19.510  15.933  1.00 18.76           O  
ANISOU 5162  O   HOH B 767     2089   2273   2765   -155   -833   -179       O  
HETATM 5163  O   HOH B 768      58.564  34.780  -7.574  1.00 23.10           O  
ANISOU 5163  O   HOH B 768     4374   1909   2495   1054    712    264       O  
HETATM 5164  O   HOH B 769      60.985   4.531  -2.684  1.00 16.41           O  
ANISOU 5164  O   HOH B 769     1727   2095   2413     80   -112    286       O  
HETATM 5165  O   HOH B 770      62.507  24.265 -17.416  1.00 25.50           O  
ANISOU 5165  O   HOH B 770     3612   3622   2456    440    506    652       O  
HETATM 5166  O   HOH B 771      53.373  35.548  -2.978  1.00 20.23           O  
ANISOU 5166  O   HOH B 771     3104   1924   2658    667    -63    154       O  
HETATM 5167  O   HOH B 772      72.041  22.696 -12.456  1.00 19.00           O  
ANISOU 5167  O   HOH B 772     2561   1742   2915     35   -100    -99       O  
HETATM 5168  O   HOH B 773      79.958  25.220  -0.009  1.00 26.08           O  
ANISOU 5168  O   HOH B 773     1718   2682   5508   -576    -94    523       O  
HETATM 5169  O   HOH B 774      76.880   9.707  -4.715  1.00 25.24           O  
ANISOU 5169  O   HOH B 774     2129   3014   4446   -436   1232   -430       O  
HETATM 5170  O   HOH B 775      73.863  20.102 -13.505  1.00 19.96           O  
ANISOU 5170  O   HOH B 775     2079   2318   3185    176    692   -211       O  
HETATM 5171  O   HOH B 776      55.290  29.144 -11.125  1.00 21.10           O  
ANISOU 5171  O   HOH B 776     2784   2540   2691   1010   -225   -130       O  
HETATM 5172  O   HOH B 777      48.737  23.384   3.130  1.00 17.05           O  
ANISOU 5172  O   HOH B 777     1915   2088   2475    -79    264   -281       O  
HETATM 5173  O   HOH B 778      69.781   3.622  -7.609  1.00 23.34           O  
ANISOU 5173  O   HOH B 778     2424   2874   3569    160    231   -722       O  
HETATM 5174  O   HOH B 779      36.957  14.886   2.585  1.00 23.47           O  
ANISOU 5174  O   HOH B 779     2536   3987   2395    300    368    328       O  
HETATM 5175  O   HOH B 780      55.729  25.790 -21.805  1.00 28.98           O  
ANISOU 5175  O   HOH B 780     4002   2520   4487   -163    739    743       O  
HETATM 5176  O   HOH B 781      64.794   2.815   4.488  1.00 16.89           O  
ANISOU 5176  O   HOH B 781     1938   1982   2496     98    384    300       O  
HETATM 5177  O   HOH B 782      65.115  14.885   6.976  1.00 19.01           O  
ANISOU 5177  O   HOH B 782     1919   2042   3263    313    -18     59       O  
HETATM 5178  O   HOH B 783      39.469   2.398  -6.107  1.00 21.72           O  
ANISOU 5178  O   HOH B 783     3590   2170   2493   -637   -782    272       O  
HETATM 5179  O   HOH B 784      59.752  20.567 -12.588  1.00 23.07           O  
ANISOU 5179  O   HOH B 784     2329   4044   2393  -1256    -54    232       O  
HETATM 5180  O   HOH B 785      69.882  21.962  15.810  1.00 28.47           O  
ANISOU 5180  O   HOH B 785     3010   2866   4941   -131    -42   -560       O  
HETATM 5181  O   HOH B 786      78.549  19.170  -6.677  1.00 29.32           O  
ANISOU 5181  O   HOH B 786     2014   3241   5884    426     98    814       O  
HETATM 5182  O   HOH B 787      58.455  19.200   1.967  1.00 19.68           O  
ANISOU 5182  O   HOH B 787     1987   1798   3691   -108   -580   -585       O  
HETATM 5183  O   HOH B 788      71.906   4.349  19.012  1.00 34.81           O  
ANISOU 5183  O   HOH B 788     5042   3754   4428    618   -622    912       O  
HETATM 5184  O   HOH B 789      63.407  30.432 -12.432  1.00 21.23           O  
ANISOU 5184  O   HOH B 789     1957   2756   3351   -169     97   1287       O  
HETATM 5185  O   HOH B 790      67.190   1.438   4.800  1.00 19.39           O  
ANISOU 5185  O   HOH B 790     2335   2350   2680    333   -154    244       O  
HETATM 5186  O   HOH B 791      63.334  29.127 -14.969  1.00 32.49           O  
ANISOU 5186  O   HOH B 791     5173   3226   3944   -614   -602    609       O  
HETATM 5187  O   HOH B 792      84.961  15.788   3.413  1.00 28.11           O  
ANISOU 5187  O   HOH B 792     1603   3191   5886    256   -202   -111       O  
HETATM 5188  O   HOH B 793      68.028  32.693 -13.360  1.00 25.97           O  
ANISOU 5188  O   HOH B 793     3671   2339   3856   -722    918    852       O  
HETATM 5189  O   HOH B 794      66.867  22.016  11.902  1.00 19.57           O  
ANISOU 5189  O   HOH B 794     2221   2661   2552    484   -411   -315       O  
HETATM 5190  O   HOH B 795      52.271  14.842 -24.280  1.00 33.85           O  
ANISOU 5190  O   HOH B 795     5165   3621   4076   -206    -87  -1185       O  
HETATM 5191  O   HOH B 796      41.572  17.080   4.719  1.00 22.30           O  
ANISOU 5191  O   HOH B 796     2693   2887   2892    532     25   -370       O  
HETATM 5192  O   HOH B 797      51.723  28.690  -8.340  1.00 24.03           O  
ANISOU 5192  O   HOH B 797     3596   2290   3244     64   -200    697       O  
HETATM 5193  O   HOH B 798      57.684   1.240 -12.248  1.00 24.42           O  
ANISOU 5193  O   HOH B 798     3986   1612   3679    885  -1019   -135       O  
HETATM 5194  O   HOH B 799      63.383  16.046 -21.823  1.00 32.35           O  
ANISOU 5194  O   HOH B 799     3507   5410   3373    513   1887    191       O  
HETATM 5195  O   HOH B 800      71.524  35.198   0.557  1.00 29.45           O  
ANISOU 5195  O   HOH B 800     4222   2960   4006   -804    -15     20       O  
HETATM 5196  O   HOH B 801      71.815   5.241 -19.995  1.00 27.03           O  
ANISOU 5196  O   HOH B 801     2845   3093   4330    138    533    -94       O  
HETATM 5197  O   HOH B 802      32.691  12.357 -27.676  1.00 35.49           O  
ANISOU 5197  O   HOH B 802     4077   4814   4592   -635  -1318   -283       O  
HETATM 5198  O   HOH B 803      66.727  18.882 -17.046  1.00 31.46           O  
ANISOU 5198  O   HOH B 803     4085   4474   3395   -831   1207  -1438       O  
HETATM 5199  O   HOH B 804      78.789  28.766   0.390  1.00 34.51           O  
ANISOU 5199  O   HOH B 804     4313   4339   4461  -2473    312    467       O  
HETATM 5200  O   HOH B 805      70.334   9.664  25.324  1.00 29.56           O  
ANISOU 5200  O   HOH B 805     4250   3079   3903    378   -645  -1155       O  
HETATM 5201  O   HOH B 806      34.710  14.041   1.240  1.00 24.41           O  
ANISOU 5201  O   HOH B 806     1901   4173   3199    646    107    818       O  
HETATM 5202  O   HOH B 807      76.858  28.467  -4.640  1.00 23.68           O  
ANISOU 5202  O   HOH B 807     2466   2733   3797   -934    405    124       O  
HETATM 5203  O   HOH B 808      69.330  27.848 -14.107  1.00 28.81           O  
ANISOU 5203  O   HOH B 808     3222   3705   4020    206    825  -1174       O  
HETATM 5204  O   HOH B 809      73.034   3.909   8.270  1.00 31.53           O  
ANISOU 5204  O   HOH B 809     2666   4862   4450   1062    108    450       O  
HETATM 5205  O   HOH B 810      64.385  16.384   9.112  1.00 21.36           O  
ANISOU 5205  O   HOH B 810     2443   3056   2615   -238    -95     -4       O  
HETATM 5206  O   HOH B 811      72.078  32.890  -6.037  1.00 26.46           O  
ANISOU 5206  O   HOH B 811     3398   1936   4719   -798    238   -147       O  
HETATM 5207  O   HOH B 812      56.281  14.119 -24.484  1.00 30.43           O  
ANISOU 5207  O   HOH B 812     4586   4186   2788   1094   -447  -1279       O  
HETATM 5208  O   HOH B 813      65.081  38.498  -4.954  1.00 27.74           O  
ANISOU 5208  O   HOH B 813     4922   1559   4059   -898    154     32       O  
HETATM 5209  O   HOH B 814      29.825  21.257 -10.654  1.00 35.49           O  
ANISOU 5209  O   HOH B 814     3798   5230   4457   1965   -480   -678       O  
HETATM 5210  O   HOH B 815      59.363   4.285  -4.859  1.00 22.23           O  
ANISOU 5210  O   HOH B 815     1816   4390   2241   1048     85     37       O  
HETATM 5211  O   HOH B 816      45.470  22.725 -23.828  1.00 28.86           O  
ANISOU 5211  O   HOH B 816     2658   5177   3128    527   -566   -998       O  
HETATM 5212  O   HOH B 817      76.494   8.547   0.008  1.00 26.28           O  
ANISOU 5212  O   HOH B 817     3611   2325   4048    825    365    430       O  
HETATM 5213  O   HOH B 818      72.873  22.205  13.442  1.00 25.54           O  
ANISOU 5213  O   HOH B 818     3090   3102   3513   -597  -1002    303       O  
HETATM 5214  O   HOH B 819      48.569  29.746  -1.900  1.00 25.14           O  
ANISOU 5214  O   HOH B 819     2840   3494   3216    311    239   -394       O  
HETATM 5215  O   HOH B 820      58.416  22.859 -19.806  1.00 28.38           O  
ANISOU 5215  O   HOH B 820     3843   2849   4092   -367    359     90       O  
HETATM 5216  O   HOH B 821      80.048  25.207   8.112  1.00 25.10           O  
ANISOU 5216  O   HOH B 821     2899   2626   4013  -1163   -805    398       O  
HETATM 5217  O   HOH B 822      70.462  27.665   6.580  1.00 30.40           O  
ANISOU 5217  O   HOH B 822     3715   3678   4158   -620    230     -1       O  
HETATM 5218  O   HOH B 823      37.167  17.299 -24.898  1.00 24.76           O  
ANISOU 5218  O   HOH B 823     2653   3804   2951    405   -421   -343       O  
HETATM 5219  O   HOH B 824      63.430  39.402   4.881  1.00 35.38           O  
ANISOU 5219  O   HOH B 824     4871   3035   5536    682   -632  -1212       O  
HETATM 5220  O   HOH B 825      75.758   2.973 -21.371  1.00 29.24           O  
ANISOU 5220  O   HOH B 825     3195   2229   5685    571   1084   1376       O  
HETATM 5221  O   HOH B 826      42.200  -1.095 -10.724  1.00 31.11           O  
ANISOU 5221  O   HOH B 826     4570   3244   4004    643  -1698   -306       O  
HETATM 5222  O   HOH B 827      75.084   3.679  -0.268  1.00 31.34           O  
ANISOU 5222  O   HOH B 827     2000   5363   4543     65     80    -41       O  
HETATM 5223  O   HOH B 828      74.048   4.475   3.528  1.00 28.89           O  
ANISOU 5223  O   HOH B 828     3436   3368   4173    991   -242   -941       O  
HETATM 5224  O   HOH B 829      35.546  18.940 -18.265  1.00 24.78           O  
ANISOU 5224  O   HOH B 829     2490   3466   3459    764    350    714       O  
HETATM 5225  O   HOH B 830      73.800  29.943  10.031  1.00 36.02           O  
ANISOU 5225  O   HOH B 830     4529   4061   5095    984   -226  -1078       O  
HETATM 5226  O   HOH B 831      45.959   8.619 -25.769  1.00 30.34           O  
ANISOU 5226  O   HOH B 831     3648   5445   2435    -48   -199    -17       O  
HETATM 5227  O   HOH B 832      77.720  26.471 -13.559  1.00 36.41           O  
ANISOU 5227  O   HOH B 832     4215   4253   5367   -785   2203    998       O  
HETATM 5228  O   HOH B 833      44.851  21.342   3.041  1.00 19.15           O  
ANISOU 5228  O   HOH B 833     2321   2452   2504    370    127   -325       O  
HETATM 5229  O   HOH B 834      54.801   8.927 -20.794  1.00 25.66           O  
ANISOU 5229  O   HOH B 834     3161   3972   2616    541   -283   -229       O  
HETATM 5230  O   HOH B 835      69.246  34.852 -11.605  1.00 33.67           O  
ANISOU 5230  O   HOH B 835     5088   3289   4417   -229     58    530       O  
HETATM 5231  O   HOH B 836      51.947  34.720  -5.378  1.00 26.02           O  
ANISOU 5231  O   HOH B 836     4187   2776   2923    311    -11    246       O  
HETATM 5232  O   HOH B 837      76.388  22.466  13.440  1.00 36.15           O  
ANISOU 5232  O   HOH B 837     5826   3984   3924   -873   -205   -927       O  
HETATM 5233  O   HOH B 838      72.862  23.223  10.673  1.00 31.28           O  
ANISOU 5233  O   HOH B 838     4134   3262   4489  -1612  -1984    792       O  
HETATM 5234  O   HOH B 839      66.172  39.358  -7.155  1.00 33.72           O  
ANISOU 5234  O   HOH B 839     5214   2734   4865    295   1058    746       O  
HETATM 5235  O   HOH B 840      53.900  13.079 -22.105  1.00 28.47           O  
ANISOU 5235  O   HOH B 840     3602   2940   4273   -220    565   -544       O  
HETATM 5236  O   HOH B 841      81.290  10.996   1.183  1.00 35.07           O  
ANISOU 5236  O   HOH B 841     3633   5621   4070   1066    621    360       O  
HETATM 5237  O   HOH B 842      43.458  15.306 -26.692  1.00 30.12           O  
ANISOU 5237  O   HOH B 842     4406   4515   2522   1395    124    232       O  
HETATM 5238  O   HOH B 843      73.022  11.984 -18.646  1.00 27.36           O  
ANISOU 5238  O   HOH B 843     2369   4010   4014    193    727   -773       O  
HETATM 5239  O   HOH B 844      64.071  10.287   4.660  1.00 19.65           O  
ANISOU 5239  O   HOH B 844     2109   2379   2976    594   -121    431       O  
HETATM 5240  O   HOH B 845      71.568  33.998  -8.632  1.00 32.37           O  
ANISOU 5240  O   HOH B 845     4449   3148   4703  -1396    151   -271       O  
HETATM 5241  O   HOH B 846      48.889  31.815  -3.773  1.00 32.01           O  
ANISOU 5241  O   HOH B 846     4250   2798   5114    463   -637    333       O  
HETATM 5242  O   HOH B 847      77.393  15.720  14.497  1.00 28.82           O  
ANISOU 5242  O   HOH B 847     2991   3450   4510   -949   -476   -111       O  
HETATM 5243  O   HOH B 848      81.837  12.573   3.462  1.00 29.46           O  
ANISOU 5243  O   HOH B 848     2995   3851   4345    802    287   -272       O  
HETATM 5244  O   HOH B 849      66.130   9.256 -20.759  1.00 26.68           O  
ANISOU 5244  O   HOH B 849     2684   4450   3001    323    396  -1182       O  
HETATM 5245  O   HOH B 850      35.498  22.625  -0.941  1.00 33.38           O  
ANISOU 5245  O   HOH B 850     3203   5820   3661   1756   -134  -1386       O  
HETATM 5246  O   HOH B 851      38.803  18.705 -26.986  1.00 28.85           O  
ANISOU 5246  O   HOH B 851     3257   3894   3810    329     66    779       O  
HETATM 5247  O   HOH B 852      53.384   6.560 -21.679  1.00 38.97           O  
ANISOU 5247  O   HOH B 852     6561   4274   3973    727    119     10       O  
HETATM 5248  O   HOH B 853      78.929  26.801  -7.867  1.00 33.57           O  
ANISOU 5248  O   HOH B 853     3140   3773   5842  -1691    431    306       O  
HETATM 5249  O   HOH B 854      77.409  30.697  12.728  1.00 37.37           O  
ANISOU 5249  O   HOH B 854     5033   4642   4524   -375    178   -626       O  
HETATM 5250  O   HOH B 855      63.114  34.948 -13.768  1.00 36.97           O  
ANISOU 5250  O   HOH B 855     4893   5458   3695  -1180   -438    613       O  
HETATM 5251  O   HOH B 856      63.038   6.076  -1.897  1.00 22.71           O  
ANISOU 5251  O   HOH B 856     2836   2810   2983   -482   -228    113       O  
HETATM 5252  O   HOH B 857      65.979  22.790 -17.348  1.00 33.98           O  
ANISOU 5252  O   HOH B 857     4950   4985   2975  -1264   1638   -416       O  
HETATM 5253  O   HOH B 858      50.970  32.069  -6.043  1.00 30.63           O  
ANISOU 5253  O   HOH B 858     3200   4026   4410   1047   -869   -505       O  
HETATM 5254  O   HOH B 859      68.823  30.034   9.981  1.00 37.82           O  
ANISOU 5254  O   HOH B 859     4984   4132   5252   -995     62   -410       O  
HETATM 5255  O   HOH B 860      65.213  27.392  11.912  1.00 36.41           O  
ANISOU 5255  O   HOH B 860     5597   3659   4579  -2187    940  -1268       O  
HETATM 5256  O   HOH B 861      65.446   3.191  -9.032  1.00 34.70           O  
ANISOU 5256  O   HOH B 861     4696   3519   4967   -699    890  -1208       O  
HETATM 5257  O   HOH B 862      75.257   8.596  -6.738  1.00 28.63           O  
ANISOU 5257  O   HOH B 862     2990   4550   3336   -356    378    -60       O  
HETATM 5258  O   HOH B 863      71.376   7.722 -16.464  1.00 33.87           O  
ANISOU 5258  O   HOH B 863     3466   4064   5338   -779    941   -332       O  
HETATM 5259  O   HOH B 864      33.008  19.175 -19.255  1.00 34.10           O  
ANISOU 5259  O   HOH B 864     3649   5360   3948   1143     44    529       O  
HETATM 5260  O   HOH B 865      59.651  37.348  -7.468  1.00 37.52           O  
ANISOU 5260  O   HOH B 865     5341   3970   4944   -111    147   1002       O  
HETATM 5261  O   HOH B 866      34.942   4.575  -6.620  1.00 34.45           O  
ANISOU 5261  O   HOH B 866     3749   4556   4784  -1081   -113   1630       O  
HETATM 5262  O   HOH B 867      63.093   2.506  -3.392  1.00 33.81           O  
ANISOU 5262  O   HOH B 867     3868   3505   5472    227   -119   1832       O  
HETATM 5263  O   HOH B 868      50.863  29.677 -16.809  1.00 32.53           O  
ANISOU 5263  O   HOH B 868     4277   3891   4193   -365   -523    101       O  
HETATM 5264  O   HOH B 869      31.004  13.171 -25.689  1.00 43.57           O  
ANISOU 5264  O   HOH B 869     4997   6210   5347   -266  -1083    492       O  
HETATM 5265  O   HOH B 870      71.280  14.203 -19.020  1.00 30.18           O  
ANISOU 5265  O   HOH B 870     2277   3674   5517    234     84    136       O  
HETATM 5266  O   HOH B 871      49.578  -4.394 -16.774  1.00 38.01           O  
ANISOU 5266  O   HOH B 871     5057   4873   4510   -290    602  -1427       O  
HETATM 5267  O   HOH B 872      73.614  -1.974  -1.269  1.00 37.25           O  
ANISOU 5267  O   HOH B 872     4351   3560   6241   1312   1353     89       O  
HETATM 5268  O   HOH B 873      78.836  18.984 -12.546  1.00 29.49           O  
ANISOU 5268  O   HOH B 873     3810   3067   4329   -725   1268   -270       O  
HETATM 5269  O   HOH B 874      36.814  13.408   4.929  1.00 31.43           O  
ANISOU 5269  O   HOH B 874     2834   5111   3997   -162    395    892       O  
HETATM 5270  O   HOH B 875      60.180  21.121 -20.277  1.00 35.84           O  
ANISOU 5270  O   HOH B 875     5882   2806   4929    451   1523   1359       O  
HETATM 5271  O   HOH B 876      43.800  24.064 -29.982  1.00 36.56           O  
ANISOU 5271  O   HOH B 876     4937   4155   4800  -1019   -340    648       O  
HETATM 5272  O   HOH B 877      32.997  15.126   2.932  1.00 43.35           O  
ANISOU 5272  O   HOH B 877     5428   5622   5419    952    619   -201       O  
HETATM 5273  O   HOH B 878      78.668   3.726  12.728  1.00 38.14           O  
ANISOU 5273  O   HOH B 878     3957   4806   5728   1418   -114    461       O  
HETATM 5274  O   HOH B 879      85.361  20.560   7.754  1.00 37.20           O  
ANISOU 5274  O   HOH B 879     4706   4936   4491  -1523  -1048   -388       O  
HETATM 5275  O   HOH B 880      36.505  17.735   4.055  1.00 40.46           O  
ANISOU 5275  O   HOH B 880     4722   6094   4558   -280   1842   -109       O  
HETATM 5276  O   HOH B 881      75.046   9.354  19.176  1.00 31.43           O  
ANISOU 5276  O   HOH B 881     2414   5892   3635  -1234   -626     67       O  
HETATM 5277  O   HOH B 882      34.730   7.241 -27.008  1.00 33.35           O  
ANISOU 5277  O   HOH B 882     3925   5117   3629   -672  -1339   -335       O  
HETATM 5278  O   HOH B 883      55.036  10.597 -23.125  1.00 29.49           O  
ANISOU 5278  O   HOH B 883     3167   4917   3122    187   -179   -737       O  
HETATM 5279  O   HOH B 884      76.837   6.141   8.074  1.00 33.01           O  
ANISOU 5279  O   HOH B 884     4479   3949   4112   -666    -67    543       O  
HETATM 5280  O   HOH B 885      75.264  31.013   3.825  1.00 36.52           O  
ANISOU 5280  O   HOH B 885     4433   3440   6001  -1051  -1545   -317       O  
HETATM 5281  O   HOH B 886      48.533  12.210 -24.048  1.00 30.21           O  
ANISOU 5281  O   HOH B 886     4479   3649   3350    506    844    189       O  
HETATM 5282  O   HOH B 887      75.551  12.084  18.746  1.00 42.38           O  
ANISOU 5282  O   HOH B 887     5816   4989   5295   -716   -229   -887       O  
HETATM 5283  O   HOH B 888      43.698  29.697 -18.051  1.00 39.19           O  
ANISOU 5283  O   HOH B 888     4808   4294   5786   1472    -89    351       O  
HETATM 5284  O   HOH B 889      65.367  27.056 -15.334  1.00 30.58           O  
ANISOU 5284  O   HOH B 889     5682   2666   3271   -511    226    491       O  
HETATM 5285  O   HOH B 890      76.227   5.865  -1.506  1.00 31.72           O  
ANISOU 5285  O   HOH B 890     2575   5051   4427    273    103   1189       O  
HETATM 5286  O   HOH B 891      74.754  14.333  17.789  1.00 32.29           O  
ANISOU 5286  O   HOH B 891     3897   5168   3202  -1587    457  -1000       O  
HETATM 5287  O   HOH B 892      46.363   3.671 -24.882  1.00 35.19           O  
ANISOU 5287  O   HOH B 892     4957   4395   4018   -119   -426   -392       O  
HETATM 5288  O   HOH B 893      63.212  40.042  -3.791  1.00 30.49           O  
ANISOU 5288  O   HOH B 893     4541   2716   4327    377    329    503       O  
HETATM 5289  O   HOH B 894      78.880  11.562  17.052  1.00 41.85           O  
ANISOU 5289  O   HOH B 894     4892   6082   4926    689  -1614   -958       O  
HETATM 5290  O   HOH B 895      70.175   1.267  -4.529  1.00 34.94           O  
ANISOU 5290  O   HOH B 895     5739   3512   4024  -2162   -411    522       O  
HETATM 5291  O   HOH B 896      64.940   4.222  -1.274  1.00 25.95           O  
ANISOU 5291  O   HOH B 896     1996   3880   3983    358   -684  -1210       O  
HETATM 5292  O   HOH B 897      69.513   2.973 -10.384  1.00 38.11           O  
ANISOU 5292  O   HOH B 897     5368   5078   4035    255    761   -186       O  
HETATM 5293  O   HOH B 898      40.456   4.294 -27.062  1.00 32.86           O  
ANISOU 5293  O   HOH B 898     4628   4140   3715   -168  -1493   -479       O  
HETATM 5294  O   HOH B 899      59.626  24.454 -17.790  1.00 27.74           O  
ANISOU 5294  O   HOH B 899     3858   4266   2414   -359    114    -15       O  
HETATM 5295  O   HOH B 900      60.563  32.436 -15.327  1.00 44.43           O  
ANISOU 5295  O   HOH B 900     6485   4850   5546   -214    194    942       O  
HETATM 5296  O   HOH B 901      33.884  11.544   1.996  1.00 31.43           O  
ANISOU 5296  O   HOH B 901     3198   4663   4079    -14    175   1065       O  
HETATM 5297  O   HOH B 902      60.455   8.434 -18.623  1.00 32.63           O  
ANISOU 5297  O   HOH B 902     4291   3996   4111   1079     19   -359       O  
HETATM 5298  O   HOH B 903      53.442   9.228 -24.985  1.00 38.80           O  
ANISOU 5298  O   HOH B 903     4884   5879   3980    200    -10   -713       O  
HETATM 5299  O   HOH B 904      68.554  11.166 -22.752  1.00 33.80           O  
ANISOU 5299  O   HOH B 904     4610   4776   3457   1585    -76    110       O  
HETATM 5300  O   HOH B 905      35.446   0.839 -20.368  1.00 34.80           O  
ANISOU 5300  O   HOH B 905     4589   3302   5331  -1661    137   -347       O  
HETATM 5301  O   HOH B 906      40.742  25.536  -3.706  1.00 34.57           O  
ANISOU 5301  O   HOH B 906     5445   3920   3768   1996   -440    164       O  
HETATM 5302  O   HOH B 907      71.341  34.320  -2.014  1.00 35.41           O  
ANISOU 5302  O   HOH B 907     4273   4424   4758  -1192    688   -965       O  
HETATM 5303  O   HOH B 908      62.205  32.513 -13.252  1.00 30.61           O  
ANISOU 5303  O   HOH B 908     5324   2731   3574    731    593     44       O  
HETATM 5304  O   HOH B 909      79.226   8.408  11.547  1.00 32.32           O  
ANISOU 5304  O   HOH B 909     3608   4132   4538    424   -744    255       O  
HETATM 5305  O   HOH B 910      73.659   1.384   9.558  1.00 42.74           O  
ANISOU 5305  O   HOH B 910     5371   5144   5724    942    254   -654       O  
HETATM 5306  O   HOH B 911      65.483   3.508  -4.223  1.00 32.23           O  
ANISOU 5306  O   HOH B 911     3121   3515   5610   -731    -55   -737       O  
HETATM 5307  O   HOH B 912      37.865   7.913 -32.311  1.00 42.70           O  
ANISOU 5307  O   HOH B 912     5774   5097   5352   -954    439    907       O  
HETATM 5308  O   HOH B 913      52.639  -3.470  -7.876  1.00 35.62           O  
ANISOU 5308  O   HOH B 913     5322   3297   4914   1455   1371   1099       O  
HETATM 5309  O   HOH B 914      82.052   9.999  11.171  1.00 47.69           O  
ANISOU 5309  O   HOH B 914     5496   6265   6358   1524   -100    740       O  
HETATM 5310  O   HOH B 915      81.236  26.553  -6.187  1.00 41.31           O  
ANISOU 5310  O   HOH B 915     4694   4836   6166   -695    634   -862       O  
HETATM 5311  O   HOH B 916      72.028  26.518 -13.726  1.00 30.12           O  
ANISOU 5311  O   HOH B 916     3752   4456   3234     80   -192     84       O  
HETATM 5312  O   HOH B 917      35.979  10.696   3.925  1.00 41.49           O  
ANISOU 5312  O   HOH B 917     4519   5531   5715    483    722   1406       O  
HETATM 5313  O   HOH B 918      80.529  22.018  -3.173  1.00 35.40           O  
ANISOU 5313  O   HOH B 918     2799   6126   4526    434   1185    570       O  
HETATM 5314  O   HOH B 919      32.034  20.970 -13.731  1.00 39.66           O  
ANISOU 5314  O   HOH B 919     5538   4888   4644    660    -18    151       O  
HETATM 5315  O   HOH B 920      60.680   5.211 -16.086  1.00 31.60           O  
ANISOU 5315  O   HOH B 920     3607   3554   4845    778    548   -589       O  
HETATM 5316  O   HOH B 921      58.416  24.629 -21.855  1.00 37.95           O  
ANISOU 5316  O   HOH B 921     4819   4235   5366   -944    805    417       O  
HETATM 5317  O   HOH B 922      89.167  19.584   2.349  1.00 47.78           O  
ANISOU 5317  O   HOH B 922     5715   6246   6193    525  -1174    239       O  
HETATM 5318  O   HOH B 923      78.343  29.551  -1.900  1.00 33.20           O  
ANISOU 5318  O   HOH B 923     3080   4570   4964  -1248     94   -160       O  
HETATM 5319  O   HOH B 924      83.101  27.232   7.086  1.00 36.35           O  
ANISOU 5319  O   HOH B 924     3443   5507   4860    -68  -1270    548       O  
HETATM 5320  O   HOH B 925      75.495   7.780   2.195  1.00 31.84           O  
ANISOU 5320  O   HOH B 925     3560   4372   4164    242    693     75       O  
HETATM 5321  O   HOH B 926      36.602  25.486  -4.276  1.00 46.54           O  
ANISOU 5321  O   HOH B 926     5918   5514   6252    117     22   -877       O  
HETATM 5322  O   HOH B 927      81.384  27.476   0.345  1.00 34.79           O  
ANISOU 5322  O   HOH B 927     3976   3195   6047  -1316     86   -351       O  
HETATM 5323  O   HOH B 928      67.435  -1.088   4.191  1.00 34.28           O  
ANISOU 5323  O   HOH B 928     5483   3056   4485  -1225   1441   -936       O  
HETATM 5324  O   HOH B 929      56.079  33.974  -8.972  1.00 34.84           O  
ANISOU 5324  O   HOH B 929     4580   4347   4308  -1475   -480   1396       O  
HETATM 5325  O   HOH B 930      60.231   1.227 -10.993  1.00 32.74           O  
ANISOU 5325  O   HOH B 930     4099   3461   4878    580   -822  -1878       O  
HETATM 5326  O   HOH B 931      84.355  13.314   4.173  1.00 34.71           O  
ANISOU 5326  O   HOH B 931     2491   4672   6024    146    279    825       O  
HETATM 5327  O   HOH B 932      55.548   4.674 -21.761  1.00 46.59           O  
ANISOU 5327  O   HOH B 932     6027   5439   6234    605    745   -501       O  
HETATM 5328  O   HOH B 933      77.182   5.529   3.156  1.00 39.76           O  
ANISOU 5328  O   HOH B 933     4685   5281   5142   1047   -770   -257       O  
HETATM 5329  O   HOH B 934      82.691  12.557  10.617  1.00 40.49           O  
ANISOU 5329  O   HOH B 934     4845   5381   5156    330  -1220    643       O  
HETATM 5330  O   HOH B 935      71.595   6.618  24.782  1.00 37.46           O  
ANISOU 5330  O   HOH B 935     5067   4320   4845    906   -756   1225       O  
HETATM 5331  O   HOH B 936      70.707   2.265   5.801  1.00 38.30           O  
ANISOU 5331  O   HOH B 936     4836   4609   5107   -583    162    185       O  
HETATM 5332  O   HOH B 937      73.043  28.908 -13.127  1.00 32.90           O  
ANISOU 5332  O   HOH B 937     3744   4098   4658    720    346    132       O  
HETATM 5333  O   HOH B 938      36.211   1.985 -10.150  1.00 38.54           O  
ANISOU 5333  O   HOH B 938     4724   3806   6114  -2104    655   -442       O  
HETATM 5334  O   HOH B 939      76.581   1.400   0.324  1.00 43.11           O  
ANISOU 5334  O   HOH B 939     5266   5730   5384    438   -395   -132       O  
HETATM 5335  O   HOH B 940      82.883  16.086  11.092  1.00 39.08           O  
ANISOU 5335  O   HOH B 940     5082   4873   4894   -485  -1493   -342       O  
HETATM 5336  O   HOH B 941      69.843  32.033 -15.246  1.00 43.01           O  
ANISOU 5336  O   HOH B 941     6180   5094   5067   -195    662     54       O  
HETATM 5337  O   HOH B 942      67.238  -2.986   0.422  1.00 39.87           O  
ANISOU 5337  O   HOH B 942     5132   3955   6060   -160    964    755       O  
HETATM 5338  O   HOH B 943      73.553   3.980 -21.942  1.00 38.48           O  
ANISOU 5338  O   HOH B 943     4487   4628   5504  -1091    945    692       O  
HETATM 5339  O   HOH B 944      45.657  28.351   1.725  1.00 36.25           O  
ANISOU 5339  O   HOH B 944     3693   4959   5119   -973   -519    -94       O  
HETATM 5340  O   HOH B 945      41.120  25.179  -0.301  1.00 38.17           O  
ANISOU 5340  O   HOH B 945     5122   4403   4979   2157    763   -590       O  
HETATM 5341  O   HOH B 946      57.796   0.281  -7.761  1.00 41.77           O  
ANISOU 5341  O   HOH B 946     6639   4417   4814    290   -160    633       O  
HETATM 5342  O   HOH B 947      55.073  -3.310  -7.207  1.00 43.01           O  
ANISOU 5342  O   HOH B 947     5625   5329   5388   -128  -1060    -86       O  
HETATM 5343  O   HOH B 948      57.068  29.077 -17.405  1.00 38.19           O  
ANISOU 5343  O   HOH B 948     4961   5371   4176   -121   -330   1053       O  
HETATM 5344  O   HOH B 949      76.661   5.437  19.544  1.00 40.93           O  
ANISOU 5344  O   HOH B 949     5210   5534   4807    509   -972    256       O  
HETATM 5345  O   HOH B 950      41.715  25.340 -31.635  1.00 49.19           O  
ANISOU 5345  O   HOH B 950     6421   5921   6348   -151   -261     45       O  
HETATM 5346  O   HOH B 951      34.194   9.735 -28.698  1.00 49.37           O  
ANISOU 5346  O   HOH B 951     6121   6149   6488    183   -557   -824       O  
HETATM 5347  O   HOH B 952      87.053  16.534   5.347  1.00 40.91           O  
ANISOU 5347  O   HOH B 952     3797   5878   5870   -107  -1247   -309       O  
HETATM 5348  O   HOH B 953      73.148   2.608   5.046  1.00 49.06           O  
ANISOU 5348  O   HOH B 953     6115   6198   6326    680   -533    712       O  
HETATM 5349  O   HOH B 954      72.898  24.548 -14.704  1.00 44.77           O  
ANISOU 5349  O   HOH B 954     5553   5104   6353    235    371    756       O  
HETATM 5350  O   HOH B 955      52.702  -2.026 -19.557  1.00 46.19           O  
ANISOU 5350  O   HOH B 955     5957   5138   6455    549    345   -727       O  
HETATM 5351  O   HOH B 956      80.189  19.219  -9.030  1.00 35.02           O  
ANISOU 5351  O   HOH B 956     3787   4402   5115   -361   1278  -1021       O  
HETATM 5352  O   HOH B 957      58.602  14.193 -25.728  1.00 41.21           O  
ANISOU 5352  O   HOH B 957     5351   5748   4559    772    731  -1041       O  
HETATM 5353  O   HOH B 958      55.184  21.999   5.322  1.00 38.19           O  
ANISOU 5353  O   HOH B 958     5294   3716   5498   -304    415  -2139       O  
HETATM 5354  O   HOH B 959      68.999  -2.500   2.758  1.00 47.86           O  
ANISOU 5354  O   HOH B 959     6119   5943   6121    435    698   -484       O  
HETATM 5355  O   HOH B 960      65.941  33.706 -14.808  1.00 43.70           O  
ANISOU 5355  O   HOH B 960     5565   5853   5186    -28   -593    606       O  
HETATM 5356  O   HOH B 961      60.210   2.335  -6.721  1.00 21.73           O  
ANISOU 5356  O   HOH B 961     3508   2272   2477    -28    -26    -95       O  
HETATM 5357  O   HOH B 962      61.255   2.966  -9.209  1.00 23.28           O  
ANISOU 5357  O   HOH B 962     3213   3277   2355    -40    271   -498       O  
HETATM 5358  O   HOH B 963      69.519   8.829 -24.465  1.00 41.11           O  
ANISOU 5358  O   HOH B 963     4932   5913   4773    226    -29   -495       O  
HETATM 5359  O   HOH B 964      72.210  30.865   1.060  1.00 21.01           O  
ANISOU 5359  O   HOH B 964     2546   2166   3270   -624   -260   -382       O  
HETATM 5360  O   HOH B 965      71.184  31.239  -1.494  1.00 19.99           O  
ANISOU 5360  O   HOH B 965     2604   1795   3197   -193   -257   -216       O  
HETATM 5361  O   HOH B 966      72.826  29.709   3.483  1.00 23.77           O  
ANISOU 5361  O   HOH B 966     3697   1395   3937   -201   -670   -164       O  
HETATM 5362  O   HOH B 967      40.222  24.684  -6.074  1.00 23.81           O  
ANISOU 5362  O   HOH B 967     2833   3445   2769   1349     64    485       O  
HETATM 5363  O   HOH B 968      62.888   5.725 -15.275  1.00 21.69           O  
ANISOU 5363  O   HOH B 968     2468   2132   3640   -365    704  -1010       O  
HETATM 5364  O   HOH B 969      68.640  17.266 -16.486  1.00 26.77           O  
ANISOU 5364  O   HOH B 969     3819   3631   2721   -726    416   -336       O  
HETATM 5365  O   HOH B 970      61.976   6.575 -13.078  1.00 22.71           O  
ANISOU 5365  O   HOH B 970     2714   2453   3462    358    506   -540       O  
HETATM 5366  O   HOH B 971      44.763  25.232   2.215  1.00 29.51           O  
ANISOU 5366  O   HOH B 971     3221   4302   3690   -147  -1079   -281       O  
HETATM 5367  O   HOH B 972      74.187   7.956 -15.776  1.00 27.02           O  
ANISOU 5367  O   HOH B 972     2332   4817   3117    225    920    -42       O  
HETATM 5368  O   HOH B 973      80.514  24.603  11.557  1.00 32.22           O  
ANISOU 5368  O   HOH B 973     4696   2863   4683   -204  -1379   -539       O  
HETATM 5369  O   HOH B 974      46.187  25.600  -3.484  1.00 30.83           O  
ANISOU 5369  O   HOH B 974     4541   3846   3326   1580   1081   1037       O  
HETATM 5370  O   HOH B 975      67.601  28.352   5.221  1.00 33.76           O  
ANISOU 5370  O   HOH B 975     2398   7855   2572    365   -375   -487       O  
HETATM 5371  O   HOH B 976      74.666   5.836   7.764  1.00 35.55           O  
ANISOU 5371  O   HOH B 976     4036   3391   6078      0   -159  -1034       O  
HETATM 5372  O   HOH B 977      51.096   3.659 -21.201  1.00 39.82           O  
ANISOU 5372  O   HOH B 977     4701   5435   4993    225     54   -497       O  
HETATM 5373  O   HOH B 978      55.727  30.983 -13.039  1.00 38.67           O  
ANISOU 5373  O   HOH B 978     5717   4261   4716     85    763   -480       O  
HETATM 5374  O   HOH B 979      41.609   6.879 -29.294  1.00 40.79           O  
ANISOU 5374  O   HOH B 979     5562   4590   5345   1278    920   -431       O  
HETATM 5375  O   HOH B 980      45.099   0.077  -4.865  1.00 33.41           O  
ANISOU 5375  O   HOH B 980     3903   3468   5323    428    -40    865       O  
HETATM 5376  O   HOH B 981      82.907  27.937   2.547  1.00 31.65           O  
ANISOU 5376  O   HOH B 981     2645   4405   4974   -506    -27    438       O  
HETATM 5377  O   HOH B 982      79.978  17.228 -11.192  1.00 42.20           O  
ANISOU 5377  O   HOH B 982     4786   5748   5498    -16    444    -62       O  
HETATM 5378  O   HOH B 983      52.677  24.338 -25.732  1.00 42.99           O  
ANISOU 5378  O   HOH B 983     6209   5414   4710   1047   -484    211       O  
HETATM 5379  O   HOH B 984      33.783   4.287   0.059  1.00 46.27           O  
ANISOU 5379  O   HOH B 984     5446   6304   5830    266    751    770       O  
HETATM 5380  O   HOH B 985      55.917  -0.069 -10.810  1.00 40.16           O  
ANISOU 5380  O   HOH B 985     4688   4888   5681    500   -122    418       O  
HETATM 5381  O   HOH B 986      73.572  21.322  17.671  1.00 38.89           O  
ANISOU 5381  O   HOH B 986     5422   4126   5227  -1355  -1208   -728       O  
HETATM 5382  O   HOH B 987      63.599  11.119 -21.008  1.00 37.62           O  
ANISOU 5382  O   HOH B 987     4132   6152   4011    510    830  -1119       O  
HETATM 5383  O   HOH B 988      73.893   5.221 -15.953  1.00 43.80           O  
ANISOU 5383  O   HOH B 988     5409   5929   5304   -859   1443      2       O  
HETATM 5384  O   HOH B 989      62.232  13.157 -21.459  1.00 41.82           O  
ANISOU 5384  O   HOH B 989     4806   5751   5331    130    352   -621       O  
HETATM 5385  O   HOH B 990      66.282  -5.217  -0.395  1.00 48.26           O  
ANISOU 5385  O   HOH B 990     6208   5668   6459    308    191   -247       O  
HETATM 5386  O   HOH B 991      54.341  13.969 -26.270  1.00 41.85           O  
ANISOU 5386  O   HOH B 991     5688   5577   4635    283   -101   -231       O  
HETATM 5387  O   HOH B 992      36.786   0.187 -12.146  1.00 36.58           O  
ANISOU 5387  O   HOH B 992     4301   4517   5080   -709   -514    154       O  
HETATM 5388  O   HOH B 993      62.089  16.909 -24.428  1.00 45.08           O  
ANISOU 5388  O   HOH B 993     5667   6190   5269    489   1646    -86       O  
HETATM 5389  O   HOH B 994      84.871  18.852  10.015  1.00 37.54           O  
ANISOU 5389  O   HOH B 994     4274   4739   5249   -667   -358    -27       O  
HETATM 5390  O   HOH B 995      59.346  20.521 -23.970  1.00 45.07           O  
ANISOU 5390  O   HOH B 995     5862   5497   5765   -509    136    678       O  
HETATM 5391  O   HOH B 996      78.079  30.954   2.296  1.00 47.37           O  
ANISOU 5391  O   HOH B 996     6613   5680   5703    206     64    -48       O  
HETATM 5392  O   HOH B 997      37.999   8.605   2.888  1.00 41.23           O  
ANISOU 5392  O   HOH B 997     5424   5754   4486    358   -497    976       O  
HETATM 5393  O   HOH B 998      48.728   7.774 -25.152  1.00 42.64           O  
ANISOU 5393  O   HOH B 998     5402   5914   4884   -700    180   -903       O  
HETATM 5394  O   HOH B 999      36.461   1.866  -5.811  1.00 40.09           O  
ANISOU 5394  O   HOH B 999     4874   5217   5142   -304   -783   -316       O  
HETATM 5395  O   HOH B1000      79.001   7.038  15.189  1.00 41.36           O  
ANISOU 5395  O   HOH B1000     4901   5004   5809    554   -280     57       O  
HETATM 5396  O   HOH B1001      70.121   0.652   7.577  1.00 45.97           O  
ANISOU 5396  O   HOH B1001     5355   5484   6625    572   -114   -134       O  
HETATM 5397  O   HOH B1002      75.488  31.122 -11.775  1.00 47.38           O  
ANISOU 5397  O   HOH B1002     6771   5402   5830   -200    252   1169       O  
HETATM 5398  O   HOH B1003      42.131  17.895 -27.167  1.00 23.10           O  
ANISOU 5398  O   HOH B1003     2801   3055   2919    -25   -483    241       O  
HETATM 5399  O   HOH B1004      55.549  37.043  -6.260  1.00 34.87           O  
ANISOU 5399  O   HOH B1004     5305   3287   4656   1095    340   1462       O  
HETATM 5400  O   HOH B1005      53.421  34.278  -7.973  1.00 40.56           O  
ANISOU 5400  O   HOH B1005     5680   5150   4579   -232    598    729       O  
HETATM 5401  O   HOH B1006      31.821  18.163 -17.051  1.00 40.14           O  
ANISOU 5401  O   HOH B1006     4688   5812   4752   2156    380   1499       O  
HETATM 5402  O   HOH B1007      41.074  24.513   2.149  1.00 46.54           O  
ANISOU 5402  O   HOH B1007     6043   6100   5540     48   -362   -996       O  
HETATM 5403  O   HOH B1008      74.765   3.437  19.763  1.00 48.55           O  
ANISOU 5403  O   HOH B1008     6228   5707   6512    743   -310    500       O  
HETATM 5404  O   HOH B1009      54.879  26.375 -24.454  1.00 50.37           O  
ANISOU 5404  O   HOH B1009     7042   6236   5860     63    241    327       O  
HETATM 5405  O   HOH B1010      81.283  15.831  14.533  1.00 42.28           O  
ANISOU 5405  O   HOH B1010     5512   4983   5569    275   -848    278       O  
HETATM 5406  O   HOH B1011      53.427  -1.549 -15.078  1.00 42.32           O  
ANISOU 5406  O   HOH B1011     4881   5495   5702   1371    148      3       O  
HETATM 5407  O   HOH B1012      77.492   6.229  -5.173  1.00 41.30           O  
ANISOU 5407  O   HOH B1012     4399   5574   5717    398   2207   -513       O  
HETATM 5408  O   HOH B1013      32.122   1.026 -21.237  1.00 46.30           O  
ANISOU 5408  O   HOH B1013     5686   5240   6664   -182    -65    179       O  
HETATM 5409  O   HOH B1014      61.663   1.547 -13.859  1.00 40.36           O  
ANISOU 5409  O   HOH B1014     4999   4616   5720   1098   -472  -1088       O  
HETATM 5410  O   HOH B1015      73.006   1.676 -22.412  1.00 40.67           O  
ANISOU 5410  O   HOH B1015     5397   4749   5305    954   1170     57       O  
HETATM 5411  O   HOH B1016      71.454   7.378 -23.722  1.00 38.69           O  
ANISOU 5411  O   HOH B1016     4706   5756   4238   -258   -126   -296       O  
HETATM 5412  O   HOH B1017      35.424  21.603 -16.257  1.00 42.85           O  
ANISOU 5412  O   HOH B1017     5402   5550   5327    758    102   -523       O  
HETATM 5413  O   HOH B1018      71.156   2.075  18.003  1.00 43.38           O  
ANISOU 5413  O   HOH B1018     4903   5417   6162    365   -781    925       O  
HETATM 5414  O   HOH B1019      32.570   6.118 -25.729  1.00 50.78           O  
ANISOU 5414  O   HOH B1019     6232   6882   6179   -242  -1096    102       O  
HETATM 5415  O   HOH B1020      60.091  16.938   2.087  1.00 17.59           O  
ANISOU 5415  O   HOH B1020     2270   1925   2489    125   -290   -387       O  
HETATM 5416  O   HOH B1021      39.861  -1.678 -17.379  1.00 27.78           O  
ANISOU 5416  O   HOH B1021     5757   2232   2564   -934  -1104     75       O  
HETATM 5417  O   HOH B1022      58.937  16.851   4.695  1.00 24.89           O  
ANISOU 5417  O   HOH B1022     2321   3808   3328    -93    313    775       O  
HETATM 5418  O   HOH B1023      42.243  -3.057 -17.519  1.00 28.40           O  
ANISOU 5418  O   HOH B1023     3778   3581   3432  -1152   -997    577       O  
HETATM 5419  O   HOH B1024      47.446  22.400   1.052  1.00 25.56           O  
ANISOU 5419  O   HOH B1024     3227   2486   3997    970   -273   -819       O  
HETATM 5420  O   HOH B1025      47.964  22.201 -28.409  1.00 44.91           O  
ANISOU 5420  O   HOH B1025     5429   6099   5535   -119    939   -198       O  
HETATM 5421  O   HOH B1026      46.745  11.504 -26.265  1.00 37.35           O  
ANISOU 5421  O   HOH B1026     5464   5219   3509    284    575     47       O  
HETATM 5422  O   HOH B1027      42.973  28.831  -9.908  1.00 35.15           O  
ANISOU 5422  O   HOH B1027     4583   4099   4671    350    -45  -1145       O  
HETATM 5423  O   HOH B1028      72.969   6.135 -25.459  1.00 35.57           O  
ANISOU 5423  O   HOH B1028     3965   5676   3873    712   -149    121       O  
HETATM 5424  O   HOH B1029      59.277  27.294 -17.334  1.00 31.92           O  
ANISOU 5424  O   HOH B1029     4032   3876   4218    -50    116    226       O  
HETATM 5425  O   HOH B1030      86.132  15.543   0.980  1.00 46.38           O  
ANISOU 5425  O   HOH B1030     5589   5887   6145    727   1074   -347       O  
HETATM 5426  O   HOH B1031      32.175  13.742 -30.132  1.00 47.27           O  
ANISOU 5426  O   HOH B1031     5431   6666   5861    -17   -448   -174       O  
HETATM 5427  O   HOH B1032      53.372  29.741 -17.684  1.00 41.33           O  
ANISOU 5427  O   HOH B1032     5324   5359   5021    314    820   -985       O  
HETATM 5428  O   HOH B1033      32.692  21.470 -24.141  1.00 42.04           O  
ANISOU 5428  O   HOH B1033     5064   5692   5217    987    -79   -392       O  
HETATM 5429  O   HOH B1034      68.209  24.895 -16.939  1.00 43.89           O  
ANISOU 5429  O   HOH B1034     5798   5637   5241   -573    791   -463       O  
HETATM 5430  O   HOH B1035      76.716   4.219  -7.367  1.00 46.78           O  
ANISOU 5430  O   HOH B1035     5335   6696   5742    740   -260     29       O  
HETATM 5431  O   HOH B1036      55.595  28.335 -21.246  1.00 52.68           O  
ANISOU 5431  O   HOH B1036     6687   6208   7119   -160    414    123       O  
HETATM 5432  O   HOH B1037      42.431  29.479  -7.793  1.00 42.74           O  
ANISOU 5432  O   HOH B1037     5329   5507   5402    600   -251    285       O  
HETATM 5433  O   HOH B1038      42.735  26.855  -0.256  1.00 52.57           O  
ANISOU 5433  O   HOH B1038     6840   6502   6630    -45   -517   -200       O  
HETATM 5434  O   HOH B1039      65.550  24.997   6.457  1.00 27.46           O  
ANISOU 5434  O   HOH B1039     3395   3209   3829   1569  -1376  -1596       O  
HETATM 5435  O   HOH B1040      57.484   4.628 -18.969  1.00 37.09           O  
ANISOU 5435  O   HOH B1040     5285   3909   4897   1382     -9  -1293       O  
HETATM 5436  O   HOH B1041      35.366  19.304 -14.918  1.00 36.67           O  
ANISOU 5436  O   HOH B1041     5445   4877   3612   -265    348   -271       O  
HETATM 5437  O   HOH B1042      91.515  22.022   1.256  1.00 38.87           O  
ANISOU 5437  O   HOH B1042     4487   4833   5448     34   -223   -296       O  
HETATM 5438  O   HOH B1043      71.962   4.795 -26.659  1.00 37.85           O  
ANISOU 5438  O   HOH B1043     3990   4103   6287   1654    108    475       O  
HETATM 5439  O   HOH B1044      68.618   0.946  16.787  1.00 35.14           O  
ANISOU 5439  O   HOH B1044     4767   3423   5162    885  -1153     60       O  
HETATM 5440  O   HOH B1045      43.382  -3.270  -5.027  1.00 46.26           O  
ANISOU 5440  O   HOH B1045     6000   6965   4611    -65    275    139       O  
HETATM 5441  O   HOH B1046      76.724  30.970  -5.171  1.00 40.52           O  
ANISOU 5441  O   HOH B1046     5474   4189   5733   -847    383    380       O  
HETATM 5442  O   HOH B1047      67.133  25.529   5.566  1.00 27.29           O  
ANISOU 5442  O   HOH B1047     4362   2932   3074   1245  -1079   -790       O  
HETATM 5443  O   HOH B1048      44.233  26.050  -6.980  1.00 28.85           O  
ANISOU 5443  O   HOH B1048     3085   3286   4590    878   -578    584       O  
HETATM 5444  O   HOH B1049      78.978   8.299  17.840  1.00 48.96           O  
ANISOU 5444  O   HOH B1049     5980   6570   6053   -394   -396   -379       O  
HETATM 5445  O   HOH B1050      37.865  25.524 -22.748  1.00 35.90           O  
ANISOU 5445  O   HOH B1050     5151   4245   4245   2103   -206   -313       O  
HETATM 5446  O   HOH B1051      47.346  21.287   2.565  1.00 34.39           O  
ANISOU 5446  O   HOH B1051     4586   3822   4659   -958    704  -1011       O  
HETATM 5447  O   HOH B1052      44.339  -5.211  -7.308  1.00 43.00           O  
ANISOU 5447  O   HOH B1052     6282   5269   4788   -500   -716   1257       O  
HETATM 5448  O   HOH B1053      31.441  11.322   3.144  1.00 50.17           O  
ANISOU 5448  O   HOH B1053     5787   6934   6342    159    842    328       O  
HETATM 5449  O   HOH B1054      44.752  30.179  -5.080  1.00 49.26           O  
ANISOU 5449  O   HOH B1054     6073   5969   6672    110   -726   -230       O  
HETATM 5450  O   HOH B1055      73.661  34.072   4.014  1.00 49.56           O  
ANISOU 5450  O   HOH B1055     6345   6016   6469   -204   -325    -14       O  
HETATM 5451  O   HOH B1056      49.027  18.852   4.519  1.00 18.58           O  
ANISOU 5451  O   HOH B1056     2010   3202   1846    155    -63   -620       O  
HETATM 5452  O   HOH B1057      65.161   7.596   5.001  1.00 21.73           O  
ANISOU 5452  O   HOH B1057     2282   1802   4173    269     99   -371       O  
HETATM 5453  O   HOH B1058      81.040  15.249  -4.907  1.00 42.99           O  
ANISOU 5453  O   HOH B1058     5781   5640   4913   -435    561   -112       O  
HETATM 5454  O   HOH B1059      62.406   3.854 -13.544  1.00 34.68           O  
ANISOU 5454  O   HOH B1059     4871   3441   4866    225    640    292       O  
HETATM 5455  O   HOH B1060      69.875  25.618 -14.233  1.00 36.50           O  
ANISOU 5455  O   HOH B1060     4362   4602   4903  -1855    759    985       O  
HETATM 5456  O   HOH B1061      30.231  21.924  -7.943  1.00 39.35           O  
ANISOU 5456  O   HOH B1061     4288   5559   5103    734   -478    292       O  
HETATM 5457  O   HOH B1062      64.949   5.556   4.999  1.00 34.81           O  
ANISOU 5457  O   HOH B1062     3772   4582   4870   -110   -194   -282       O  
HETATM 5458  O   HOH B1063      30.957  24.397  -7.643  1.00 51.71           O  
ANISOU 5458  O   HOH B1063     5880   6814   6951    585   -210    186       O  
HETATM 5459  O   HOH B1064      58.954   2.259 -14.841  1.00 35.90           O  
ANISOU 5459  O   HOH B1064     4569   3495   5577   1074    234   -544       O  
HETATM 5460  O   HOH B1065      61.306  13.085 -23.548  1.00 49.04           O  
ANISOU 5460  O   HOH B1065     5659   6329   6646    725    225    694       O  
HETATM 5461  O   HOH B1066      35.420  23.499 -15.445  1.00 49.19           O  
ANISOU 5461  O   HOH B1066     6476   6245   5969   -151   1057    102       O  
HETATM 5462  O   HOH B1067      70.346  24.657 -17.071  1.00 47.62           O  
ANISOU 5462  O   HOH B1067     6762   5645   5686    367   -226    -17       O  
HETATM 5463  O   HOH B1068      79.102   7.880  -3.135  1.00 47.97           O  
ANISOU 5463  O   HOH B1068     6124   5674   6426   -158    454   -853       O  
HETATM 5464  O   HOH B1069      63.552   1.666  -8.668  1.00 40.38           O  
ANISOU 5464  O   HOH B1069     4988   4652   5703    571   -386  -1358       O  
HETATM 5465  O   HOH B1070      58.813   3.572 -16.387  1.00 39.16           O  
ANISOU 5465  O   HOH B1070     4544   5440   4893   -259   -143  -1497       O  
HETATM 5466  O   HOH B1071      82.279  17.379  -5.308  1.00 45.20           O  
ANISOU 5466  O   HOH B1071     5301   6297   5574    465   1136    230       O  
HETATM 5467  O   HOH B1072      39.575  -0.195  -7.163  1.00 45.63           O  
ANISOU 5467  O   HOH B1072     6341   5545   5449   -374    128    591       O  
HETATM 5468  O   HOH B1073      58.111  32.762 -12.573  1.00 46.32           O  
ANISOU 5468  O   HOH B1073     6253   5617   5728    229    122    121       O  
HETATM 5469  O   HOH B1074      69.016   0.998  -6.744  1.00 48.44           O  
ANISOU 5469  O   HOH B1074     6377   6057   5969    116    681   -286       O  
HETATM 5470  O   HOH B1075      67.931  27.924 -16.071  1.00 46.93           O  
ANISOU 5470  O   HOH B1075     5755   6359   5716   -745    584   -156       O  
HETATM 5471  O   HOH B1076      38.389  26.027  -2.519  1.00 51.25           O  
ANISOU 5471  O   HOH B1076     6258   6421   6794    775    -43    -22       O  
HETATM 5472  O   HOH B1077      65.345  30.973 -16.242  1.00 46.28           O  
ANISOU 5472  O   HOH B1077     6318   5845   5422     59     65    664       O  
HETATM 5473  O   HOH B1078      45.471  -8.032 -15.471  1.00 52.04           O  
ANISOU 5473  O   HOH B1078     6634   6302   6835    316   -109   -160       O  
HETATM 5474  O   HOH B1079      81.008  30.476   7.120  1.00 51.18           O  
ANISOU 5474  O   HOH B1079     6114   6600   6732   -623   -234   -739       O  
HETATM 5475  O   HOH B1080      75.964  -1.089  -1.155  1.00 47.60           O  
ANISOU 5475  O   HOH B1080     6001   5738   6345   1000    126    222       O  
HETATM 5476  O   HOH B1081      65.243  35.786   8.236  1.00 47.73           O  
ANISOU 5476  O   HOH B1081     6200   5696   6237    548    287  -1024       O  
HETATM 5477  O   HOH B1082      59.433  16.558 -26.424  1.00 50.10           O  
ANISOU 5477  O   HOH B1082     6350   6604   6080    738    543   -459       O  
HETATM 5478  O   HOH B1083      62.508  22.661 -19.829  1.00 44.63           O  
ANISOU 5478  O   HOH B1083     6034   5505   5416   -470    262    371       O  
HETATM 5479  O   HOH B1084      30.359  21.215  -1.235  1.00 50.28           O  
ANISOU 5479  O   HOH B1084     6278   6640   6185    639    279   -285       O  
HETATM 5480  O   HOH B1085      31.126  19.120  -1.865  1.00 43.89           O  
ANISOU 5480  O   HOH B1085     4890   5981   5805   -421   -398    742       O  
HETATM 5481  O   HOH B1086      41.770  -2.517 -25.702  1.00 48.19           O  
ANISOU 5481  O   HOH B1086     6624   6014   5673   -145   -122   -900       O  
HETATM 5482  O   HOH B1087      64.338  46.605   1.675  1.00 49.21           O  
ANISOU 5482  O   HOH B1087     6451   5622   6625    -64   -474    295       O  
HETATM 5483  O   HOH B1088      75.175  17.212  17.778  1.00 46.43           O  
ANISOU 5483  O   HOH B1088     5966   6239   5435     22   -287   -630       O  
HETATM 5484  O   HOH B1089      72.794  31.565   7.850  1.00 51.89           O  
ANISOU 5484  O   HOH B1089     6844   6163   6710    -44   -142   -309       O  
HETATM 5485  O   HOH B1090      68.103  39.379 -13.037  1.00 48.76           O  
ANISOU 5485  O   HOH B1090     6653   6199   5673   -597   -519   1329       O  
HETATM 5486  O   HOH B1091      49.523  -4.090 -19.360  1.00 50.32           O  
ANISOU 5486  O   HOH B1091     6400   6201   6519    110    290    175       O  
HETATM 5487  O   HOH B1092      63.685  26.456 -17.750  1.00 46.30           O  
ANISOU 5487  O   HOH B1092     5942   5851   5799  -1203    218    586       O  
HETATM 5488  O   HOH B1093      63.943   6.027 -17.355  1.00 51.81           O  
ANISOU 5488  O   HOH B1093     6364   6750   6571    258   -232   -450       O  
HETATM 5489  O   HOH B1094      70.875  29.855 -15.428  1.00 49.67           O  
ANISOU 5489  O   HOH B1094     6526   6080   6267    331    666    118       O  
HETATM 5490  O   HOH B1095      72.412   0.474   5.926  1.00 52.75           O  
ANISOU 5490  O   HOH B1095     6874   6303   6865    -21    220    289       O  
HETATM 5491  O   HOH B1096      79.830   5.756   8.849  1.00 55.12           O  
ANISOU 5491  O   HOH B1096     6884   6935   7123    280   -182    215       O  
HETATM 5492  O   HOH B1097      75.662  22.829  17.556  1.00 50.88           O  
ANISOU 5492  O   HOH B1097     6433   6617   6281  -1080    -36   -717       O  
HETATM 5493  O   HOH B1098      38.204  -3.606 -17.847  1.00 51.19           O  
ANISOU 5493  O   HOH B1098     6300   6698   6450   -710   -394     53       O  
HETATM 5494  O   HOH B1099      64.417  19.290 -19.304  1.00 45.68           O  
ANISOU 5494  O   HOH B1099     6077   5437   5840   -312    475     78       O  
HETATM 5495  O   HOH B1100      35.108  22.249 -25.962  1.00 51.36           O  
ANISOU 5495  O   HOH B1100     6719   6811   5982    -76    -87    476       O  
HETATM 5496  O   HOH B1101      47.185   1.354  -2.474  1.00 46.40           O  
ANISOU 5496  O   HOH B1101     6284   6051   5296   -226    358   -425       O  
HETATM 5497  O   HOH B1102      55.149  12.421   3.878  1.00 42.43           O  
ANISOU 5497  O   HOH B1102     5378   5139   5605    387    -20    428       O  
HETATM 5498  O   HOH B1103      71.416  30.467   5.606  1.00 45.34           O  
ANISOU 5498  O   HOH B1103     6376   5652   5198    931    473    941       O  
HETATM 5499  O   HOH B1104      68.017  25.408 -14.190  1.00 39.21           O  
ANISOU 5499  O   HOH B1104     4906   4887   5106   -927    654    934       O  
HETATM 5500  O   HOH B1105      51.693  -2.671 -16.376  1.00 46.97           O  
ANISOU 5500  O   HOH B1105     6407   5497   5942     99   -406     26       O  
HETATM 5501  O   HOH B1106      42.227  25.416 -26.557  1.00 45.19           O  
ANISOU 5501  O   HOH B1106     5949   5299   5921   -230    442   -465       O  
HETATM 5502  O   HOH B1107      75.272  30.970  -8.308  1.00 44.55           O  
ANISOU 5502  O   HOH B1107     6045   4840   6040  -1008    380   -912       O  
HETATM 5503  O   HOH B1108      43.442  27.378   2.485  1.00 49.50           O  
ANISOU 5503  O   HOH B1108     6293   6038   6476   -136  -1124     40       O  
HETATM 5504  O   HOH B1109      46.554  15.440 -26.303  1.00 49.05           O  
ANISOU 5504  O   HOH B1109     6171   6673   5791    483   -623    785       O  
HETATM 5505  O   HOH B1110      38.664   1.311 -25.758  1.00 49.07           O  
ANISOU 5505  O   HOH B1110     6094   6947   5603   -410   -403   -737       O  
HETATM 5506  O   HOH B1111      75.122  31.224  -6.437  1.00 49.30           O  
ANISOU 5506  O   HOH B1111     6279   6199   6252  -1380    148    653       O  
HETATM 5507  O   HOH B1112      35.884  24.730 -25.295  1.00 48.08           O  
ANISOU 5507  O   HOH B1112     6122   6328   5819    771   -336    528       O  
HETATM 5508  O   HOH B1113      52.123  -4.682 -15.593  1.00 47.43           O  
ANISOU 5508  O   HOH B1113     6059   5701   6262    470    334   -444       O  
HETATM 5509  O   HOH B1114      75.836  32.029  10.130  1.00 51.19           O  
ANISOU 5509  O   HOH B1114     6130   6231   7088    -76   -299   -672       O  
CONECT 4593 4594 4602 4609                                                      
CONECT 4594 4593 4595 4599                                                      
CONECT 4595 4594 4596 4600                                                      
CONECT 4596 4595 4597 4601                                                      
CONECT 4597 4596 4598 4602                                                      
CONECT 4598 4597                                                                
CONECT 4599 4594                                                                
CONECT 4600 4595                                                                
CONECT 4601 4596                                                                
CONECT 4602 4593 4597                                                           
CONECT 4603 4604 4612 4624                                                      
CONECT 4604 4603 4605 4609                                                      
CONECT 4605 4604 4606 4610                                                      
CONECT 4606 4605 4607 4611                                                      
CONECT 4607 4606 4608 4612                                                      
CONECT 4608 4607 4613                                                           
CONECT 4609 4593 4604                                                           
CONECT 4610 4605                                                                
CONECT 4611 4606                                                                
CONECT 4612 4603 4607                                                           
CONECT 4613 4608                                                                
CONECT 4614 4615 4622 4628                                                      
CONECT 4615 4614 4616 4627                                                      
CONECT 4616 4615 4617 4623                                                      
CONECT 4617 4616 4618 4624                                                      
CONECT 4618 4617 4619 4622                                                      
CONECT 4619 4618 4625                                                           
CONECT 4620 4621 4626 4627                                                      
CONECT 4621 4620                                                                
CONECT 4622 4614 4618                                                           
CONECT 4623 4616 4629                                                           
CONECT 4624 4603 4617                                                           
CONECT 4625 4619                                                                
CONECT 4626 4620                                                                
CONECT 4627 4615 4620                                                           
CONECT 4628 4614                                                                
CONECT 4629 4623 4630 4638                                                      
CONECT 4630 4629 4631 4635                                                      
CONECT 4631 4630 4632 4636                                                      
CONECT 4632 4631 4633 4637                                                      
CONECT 4633 4632 4634 4638                                                      
CONECT 4634 4633                                                                
CONECT 4635 4630                                                                
CONECT 4636 4631                                                                
CONECT 4637 4632                                                                
CONECT 4638 4629 4633                                                           
CONECT 4639 4640 4648 4655                                                      
CONECT 4640 4639 4641 4645                                                      
CONECT 4641 4640 4642 4646                                                      
CONECT 4642 4641 4643 4647                                                      
CONECT 4643 4642 4644 4648                                                      
CONECT 4644 4643                                                                
CONECT 4645 4640                                                                
CONECT 4646 4641                                                                
CONECT 4647 4642                                                                
CONECT 4648 4639 4643                                                           
CONECT 4649 4650 4658 4670                                                      
CONECT 4650 4649 4651 4655                                                      
CONECT 4651 4650 4652 4656                                                      
CONECT 4652 4651 4653 4657                                                      
CONECT 4653 4652 4654 4658                                                      
CONECT 4654 4653 4659                                                           
CONECT 4655 4639 4650                                                           
CONECT 4656 4651                                                                
CONECT 4657 4652                                                                
CONECT 4658 4649 4653                                                           
CONECT 4659 4654                                                                
CONECT 4660 4661 4668 4674                                                      
CONECT 4661 4660 4662 4673                                                      
CONECT 4662 4661 4663 4669                                                      
CONECT 4663 4662 4664 4670                                                      
CONECT 4664 4663 4665 4668                                                      
CONECT 4665 4664 4671                                                           
CONECT 4666 4667 4672 4673                                                      
CONECT 4667 4666                                                                
CONECT 4668 4660 4664                                                           
CONECT 4669 4662 4675                                                           
CONECT 4670 4649 4663                                                           
CONECT 4671 4665                                                                
CONECT 4672 4666                                                                
CONECT 4673 4661 4666                                                           
CONECT 4674 4660                                                                
CONECT 4675 4669 4676 4684                                                      
CONECT 4676 4675 4677 4681                                                      
CONECT 4677 4676 4678 4682                                                      
CONECT 4678 4677 4679 4683                                                      
CONECT 4679 4678 4680 4684                                                      
CONECT 4680 4679                                                                
CONECT 4681 4676                                                                
CONECT 4682 4677                                                                
CONECT 4683 4678                                                                
CONECT 4684 4675 4679                                                           
MASTER      351    0    8   13   31    0   10    6 5507    2   92   48          
END