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Browse entries in the PDBbind-CN Database

HEADER    HYDROLASE                               22-SEP-15   5DWA              
TITLE     CRYSTAL STRUCTURE OF PRE-SPECIFIC RESTRICTION ENDONUCLEASE AGEI-DNA   
TITLE    2 COMPLEX                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYPE-2 RESTRICTION ENZYME AGEI;                            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: R.AGEI,ENDONUCLEASE AGEI,TYPE II RESTRICTION ENZYME AGEI;   
COMPND   5 EC: 3.1.21.4;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: DNA (5'-D(*TP*CP*GP*AP*CP*CP*GP*GP*TP*CP*G*)-3');          
COMPND   9 CHAIN: C, D;                                                         
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THALASSOBIUS GELATINOVORUS;                     
SOURCE   3 ORGANISM_TAXID: 53501;                                               
SOURCE   4 GENE: AGEIR;                                                         
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: ER2566;                                    
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PRRS-AGEIRM;                              
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  13 ORGANISM_TAXID: 32630                                                
KEYWDS    RESTRICTION ENDONUCLEASE, PD-(D/E)XK NUCLEASE, PROTEIN-DNA COMPLEX,   
KEYWDS   2 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.TAMULAITIENE,V.JOVAISAITE,S.GRAZULIS,V.SIKSNYS                      
REVDAT   4   17-JUL-19 5DWA    1       REMARK                                   
REVDAT   3   03-MAY-17 5DWA    1       JRNL                                     
REVDAT   2   11-JAN-17 5DWA    1       JRNL                                     
REVDAT   1   05-OCT-16 5DWA    0                                                
JRNL        AUTH   G.TAMULAITIENE,V.JOVAISAITE,G.TAMULAITIS,I.SONGAILIENE,      
JRNL        AUTH 2 E.MANAKOVA,M.ZAREMBA,S.GRAZULIS,S.Y.XU,V.SIKSNYS             
JRNL        TITL   RESTRICTION ENDONUCLEASE AGEI IS A MONOMER WHICH DIMERIZES   
JRNL        TITL 2 TO CLEAVE DNA.                                               
JRNL        REF    NUCLEIC ACIDS RES.            V.  45  3547 2017              
JRNL        REFN                   ESSN 1362-4962                               
JRNL        PMID   28039325                                                     
JRNL        DOI    10.1093/NAR/GKW1310                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.3                                         
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.27                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.280                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 84472                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.155                           
REMARK   3   R VALUE            (WORKING SET) : 0.152                           
REMARK   3   FREE R VALUE                     : 0.185                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.060                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 8036                            
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 40.2850 -  4.6585    1.00     4983   533  0.1559 0.1521        
REMARK   3     2  4.6585 -  3.6984    1.00     5028   503  0.1293 0.1578        
REMARK   3     3  3.6984 -  3.2312    1.00     4968   578  0.1494 0.1870        
REMARK   3     4  3.2312 -  2.9358    1.00     4982   581  0.1667 0.1811        
REMARK   3     5  2.9358 -  2.7255    1.00     5006   531  0.1623 0.1775        
REMARK   3     6  2.7255 -  2.5648    1.00     4945   587  0.1607 0.1843        
REMARK   3     7  2.5648 -  2.4364    1.00     4943   581  0.1524 0.1906        
REMARK   3     8  2.4364 -  2.3303    1.00     5048   506  0.1556 0.2013        
REMARK   3     9  2.3303 -  2.2406    0.87     4340   488  0.1559 0.1821        
REMARK   3    10  2.2406 -  2.1633    0.83     4135   465  0.1498 0.1943        
REMARK   3    11  2.1633 -  2.0957    0.84     4215   460  0.1574 0.1878        
REMARK   3    12  2.0957 -  2.0358    0.85     4245   456  0.1602 0.1999        
REMARK   3    13  2.0358 -  1.9822    0.87     4366   456  0.1543 0.1815        
REMARK   3    14  1.9822 -  1.9338    0.89     4421   510  0.1486 0.2127        
REMARK   3    15  1.9338 -  1.8899    0.92     4600   457  0.1343 0.1833        
REMARK   3    16  1.8899 -  1.8496    0.94     4673   578  0.1371 0.1835        
REMARK   3    17  1.8496 -  1.8126    0.96     4764   547  0.1418 0.1947        
REMARK   3    18  1.8126 -  1.7784    0.98     4862   548  0.1380 0.2027        
REMARK   3    19  1.7784 -  1.7467    0.98     4905   541  0.1411 0.1895        
REMARK   3    20  1.7467 -  1.7171    0.99     5048   536  0.1492 0.1924        
REMARK   3    21  1.7171 -  1.6894    0.99     4878   506  0.1447 0.2109        
REMARK   3    22  1.6894 -  1.6634    0.99     4934   593  0.1444 0.2144        
REMARK   3    23  1.6634 -  1.6389    0.99     4922   567  0.1544 0.2179        
REMARK   3    24  1.6389 -  1.6158    0.99     4823   614  0.1493 0.2051        
REMARK   3    25  1.6158 -  1.5940    0.99     4946   528  0.1541 0.1932        
REMARK   3    26  1.5940 -  1.5733    0.99     4957   602  0.1624 0.2004        
REMARK   3    27  1.5733 -  1.5536    0.99     4976   542  0.1634 0.2104        
REMARK   3    28  1.5536 -  1.5349    0.99     4919   561  0.1677 0.2175        
REMARK   3    29  1.5349 -  1.5170    1.00     4930   582  0.1794 0.2245        
REMARK   3    30  1.5170 -  1.5000    0.99     4949   535  0.1944 0.2535        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.140            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.600           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.32                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.64                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           5110                                  
REMARK   3   ANGLE     :  1.022           7043                                  
REMARK   3   CHIRALITY :  0.040            763                                  
REMARK   3   PLANARITY :  0.005            868                                  
REMARK   3   DIHEDRAL  : 16.726           1948                                  
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 5DWA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-SEP-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000213871.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-DEC-08; 09-FEB-09               
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 5.5; 5.5                           
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; N                               
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG; ROTATING       
REMARK 200                                   ANODE                              
REMARK 200  BEAMLINE                       : X12; NULL                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL; RIGAKU MICROMAX-007 HF       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99985; 1.5418                    
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : MIRRORS; NULL                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; IMAGE PLATE                   
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD; RIGAKU       
REMARK 200                                   RAXIS IV++                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM 6.2.6                       
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.2.19                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 84560                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 79.809                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 8.200                              
REMARK 200  R MERGE                    (I) : 0.06200                            
REMARK 200  R SYM                      (I) : 0.06200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.19700                            
REMARK 200  R SYM FOR SHELL            (I) : 0.19700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: MLPHARE 6.0, MOLREP 6.0, DM 6.0                       
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M NACL, 0.1 M BIS-TRIS (PH 5.5),     
REMARK 280  19% PEG3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K.       
REMARK 280  0.2 M NACL, 0.1 M BIS-TRIS (PH 5.5), 19% PEG3350, VAPOR             
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       33.00150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       50.82750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.90300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       50.82750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       33.00150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.90300            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7710 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22680 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A   9    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B   9    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  23    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 120    CG   CD   CE   NZ                                   
REMARK 470     GLU B 157    OE1  OE2                                            
REMARK 470     GLU B 173    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 266    CG   OD1  OD2                                       
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   OG   SER B   192     O    HOH B   301              1.99            
REMARK 500   NE2  GLN B   148     O    HOH B   302              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    ALA A 172     -132.28     40.67                                   
REMARK 500    LYS A 200      113.61   -164.95                                   
REMARK 500    LYS A 200      115.28   -164.95                                   
REMARK 500    GLN A 265     -107.42   -106.13                                   
REMARK 500    ARG B   9      150.12    -46.45                                   
REMARK 500    LEU B  11       97.38    -67.51                                   
REMARK 500    CYS B  58       73.99   -119.32                                   
REMARK 500    VAL B  70      -68.41   -106.19                                   
REMARK 500    LYS B 200      118.90   -166.20                                   
REMARK 500    GLN B 265      -95.83   -115.18                                   
REMARK 500    GLN B 265      -98.73   -111.85                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5DWA A    1   278  UNP    Q9KHV6   T2A1_THAGE       1    278             
DBREF  5DWA B    1   278  UNP    Q9KHV6   T2A1_THAGE       1    278             
DBREF  5DWA C   -2     8  PDB    5DWA     5DWA            -2      8             
DBREF  5DWA D   -2     8  PDB    5DWA     5DWA            -2      8             
SEQRES   1 A  278  MET ARG LEU ASP LEU ASP PHE GLY ARG GLY LEU VAL ALA          
SEQRES   2 A  278  HIS VAL MET LEU ASP ASN VAL SER GLU GLU GLN TYR GLN          
SEQRES   3 A  278  GLN ILE SER ASP TYR PHE VAL PRO LEU VAL ASN LYS PRO          
SEQRES   4 A  278  LYS LEU LYS SER ARG ASP ALA ILE GLY GLN ALA PHE VAL          
SEQRES   5 A  278  MET ALA THR GLU VAL CYS PRO ASP ALA ASN PRO SER ASP          
SEQRES   6 A  278  LEU TRP HIS HIS VAL LEU TYR ARG ILE TYR ILE ARG GLU          
SEQRES   7 A  278  LYS ILE GLY THR ASP PRO SER GLN SER TRP VAL ARG THR          
SEQRES   8 A  278  SER GLY GLU ALA PHE GLU VAL ALA LEU VAL GLU ARG TYR          
SEQRES   9 A  278  ASN PRO VAL LEU ALA ARG HIS GLY ILE ARG LEU THR ALA          
SEQRES  10 A  278  LEU PHE LYS GLY GLN LYS GLY LEU ALA LEU THR ARG MET          
SEQRES  11 A  278  GLY VAL ALA ASP ARG VAL GLY SER ARG LYS VAL ASP VAL          
SEQRES  12 A  278  MET ILE GLU LYS GLN GLY GLY GLY ARG SER PRO ASP ALA          
SEQRES  13 A  278  GLU GLY PHE GLY VAL VAL GLY GLY ILE HIS ALA LYS VAL          
SEQRES  14 A  278  SER LEU ALA GLU ARG VAL SER ASP ASP ILE PRO ALA SER          
SEQRES  15 A  278  ARG ILE MET MET GLY GLU GLY LEU LEU SER VAL LEU SER          
SEQRES  16 A  278  THR LEU ASP VAL LYS SER PHE PRO PRO PRO HIS GLY ASP          
SEQRES  17 A  278  LEU VAL ASN ARG GLY GLU LEU GLY THR PRO ASP ARG PRO          
SEQRES  18 A  278  SER ASP LYS ARG ASN TYR ILE GLU GLY HIS GLY ASP PHE          
SEQRES  19 A  278  SER ALA CYS PHE SER TYR ASN LEU ARG THR SER PRO SER          
SEQRES  20 A  278  ASN ALA THR THR PRO SER GLY ARG HIS ILE TYR VAL SER          
SEQRES  21 A  278  GLY PHE SER GLY GLN ASP ASP GLU PHE THR ASP TYR LEU          
SEQRES  22 A  278  VAL ALA GLN LEU ALA                                          
SEQRES   1 B  278  MET ARG LEU ASP LEU ASP PHE GLY ARG GLY LEU VAL ALA          
SEQRES   2 B  278  HIS VAL MET LEU ASP ASN VAL SER GLU GLU GLN TYR GLN          
SEQRES   3 B  278  GLN ILE SER ASP TYR PHE VAL PRO LEU VAL ASN LYS PRO          
SEQRES   4 B  278  LYS LEU LYS SER ARG ASP ALA ILE GLY GLN ALA PHE VAL          
SEQRES   5 B  278  MET ALA THR GLU VAL CYS PRO ASP ALA ASN PRO SER ASP          
SEQRES   6 B  278  LEU TRP HIS HIS VAL LEU TYR ARG ILE TYR ILE ARG GLU          
SEQRES   7 B  278  LYS ILE GLY THR ASP PRO SER GLN SER TRP VAL ARG THR          
SEQRES   8 B  278  SER GLY GLU ALA PHE GLU VAL ALA LEU VAL GLU ARG TYR          
SEQRES   9 B  278  ASN PRO VAL LEU ALA ARG HIS GLY ILE ARG LEU THR ALA          
SEQRES  10 B  278  LEU PHE LYS GLY GLN LYS GLY LEU ALA LEU THR ARG MET          
SEQRES  11 B  278  GLY VAL ALA ASP ARG VAL GLY SER ARG LYS VAL ASP VAL          
SEQRES  12 B  278  MET ILE GLU LYS GLN GLY GLY GLY ARG SER PRO ASP ALA          
SEQRES  13 B  278  GLU GLY PHE GLY VAL VAL GLY GLY ILE HIS ALA LYS VAL          
SEQRES  14 B  278  SER LEU ALA GLU ARG VAL SER ASP ASP ILE PRO ALA SER          
SEQRES  15 B  278  ARG ILE MET MET GLY GLU GLY LEU LEU SER VAL LEU SER          
SEQRES  16 B  278  THR LEU ASP VAL LYS SER PHE PRO PRO PRO HIS GLY ASP          
SEQRES  17 B  278  LEU VAL ASN ARG GLY GLU LEU GLY THR PRO ASP ARG PRO          
SEQRES  18 B  278  SER ASP LYS ARG ASN TYR ILE GLU GLY HIS GLY ASP PHE          
SEQRES  19 B  278  SER ALA CYS PHE SER TYR ASN LEU ARG THR SER PRO SER          
SEQRES  20 B  278  ASN ALA THR THR PRO SER GLY ARG HIS ILE TYR VAL SER          
SEQRES  21 B  278  GLY PHE SER GLY GLN ASP ASP GLU PHE THR ASP TYR LEU          
SEQRES  22 B  278  VAL ALA GLN LEU ALA                                          
SEQRES   1 C   11   DT  DC  DG  DA  DC  DC  DG  DG  DT  DC  DG                  
SEQRES   1 D   11   DT  DC  DG  DA  DC  DC  DG  DG  DT  DC  DG                  
FORMUL   5  HOH   *524(H2 O)                                                    
HELIX    1 AA1 SER A   21  ASN A   37  1                                  17    
HELIX    2 AA2 LYS A   42  CYS A   58  1                                  17    
HELIX    3 AA3 ASN A   62  VAL A   70  1                                   9    
HELIX    4 AA4 VAL A   70  LYS A   79  1                                  10    
HELIX    5 AA5 ASP A   83  ARG A  110  1                                  28    
HELIX    6 AA6 GLN A  122  GLY A  131  1                                  10    
HELIX    7 AA7 GLU A  173  SER A  176  5                                   4    
HELIX    8 AA8 ASP A  177  GLU A  188  1                                  12    
HELIX    9 AA9 SER A  222  GLY A  230  1                                   9    
HELIX   10 AB1 ASP A  267  ALA A  278  1                                  12    
HELIX   11 AB2 SER B   21  ASN B   37  1                                  17    
HELIX   12 AB3 LYS B   42  CYS B   58  1                                  17    
HELIX   13 AB4 ASN B   62  VAL B   70  1                                   9    
HELIX   14 AB5 VAL B   70  LYS B   79  1                                  10    
HELIX   15 AB6 ASP B   83  ALA B  109  1                                  27    
HELIX   16 AB7 GLN B  122  MET B  130  1                                   9    
HELIX   17 AB8 GLY B  137  VAL B  141  5                                   5    
HELIX   18 AB9 ARG B  174  ASP B  177  5                                   4    
HELIX   19 AC1 ASP B  178  GLU B  188  1                                  11    
HELIX   20 AC2 SER B  222  GLY B  230  1                                   9    
HELIX   21 AC3 ASP B  267  ALA B  278  1                                  12    
SHEET    1 AA1 2 ARG A   2  GLY A   8  0                                        
SHEET    2 AA1 2 LEU A  11  MET A  16 -1  O  ALA A  13   N  LEU A   5           
SHEET    1 AA2 6 ILE A 113  ALA A 117  0                                        
SHEET    2 AA2 6 VAL A 143  GLN A 148 -1  O  MET A 144   N  THR A 116           
SHEET    3 AA2 6 PHE A 159  LYS A 168 -1  O  ILE A 165   N  VAL A 143           
SHEET    4 AA2 6 LEU A 191  THR A 196  1  O  VAL A 193   N  HIS A 166           
SHEET    5 AA2 6 ALA A 236  SER A 239  1  O  PHE A 238   N  LEU A 194           
SHEET    6 AA2 6 ILE A 257  VAL A 259  1  O  TYR A 258   N  CYS A 237           
SHEET    1 AA3 2 ARG B   2  ASP B   6  0                                        
SHEET    2 AA3 2 VAL B  12  MET B  16 -1  O  ALA B  13   N  LEU B   5           
SHEET    1 AA4 6 ILE B 113  ALA B 117  0                                        
SHEET    2 AA4 6 VAL B 143  GLN B 148 -1  O  GLU B 146   N  ARG B 114           
SHEET    3 AA4 6 PHE B 159  LYS B 168 -1  O  ILE B 165   N  VAL B 143           
SHEET    4 AA4 6 LEU B 191  THR B 196  1  O  VAL B 193   N  HIS B 166           
SHEET    5 AA4 6 ALA B 236  SER B 239  1  O  PHE B 238   N  LEU B 194           
SHEET    6 AA4 6 ILE B 257  VAL B 259  1  O  TYR B 258   N  CYS B 237           
CISPEP   1 PRO A  204    PRO A  205          0         5.87                     
CISPEP   2 ARG B    9    GLY B   10          0        -0.03                     
CISPEP   3 PRO B  204    PRO B  205          0        12.04                     
CRYST1   66.003   79.806  101.655  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015151  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012530  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009837        0.00000                         
ATOM      1  N   MET A   1      71.777  34.576 -11.497  1.00 23.94           N  
ANISOU    1  N   MET A   1     2752   3990   2354   -156    252     61       N  
ATOM      2  CA  MET A   1      71.149  34.749 -12.803  1.00 23.46           C  
ANISOU    2  CA  MET A   1     2592   3842   2479   -128    416    -79       C  
ATOM      3  C   MET A   1      70.237  35.968 -12.810  1.00 23.46           C  
ANISOU    3  C   MET A   1     2587   3873   2455     69    339   -136       C  
ATOM      4  O   MET A   1      69.812  36.439 -11.757  1.00 24.20           O  
ANISOU    4  O   MET A   1     2786   3903   2507    122    233   -342       O  
ATOM      5  CB  MET A   1      70.346  33.506 -13.184  1.00 23.10           C  
ANISOU    5  CB  MET A   1     2488   3775   2512   -264    567    -20       C  
ATOM      6  CG  MET A   1      69.134  33.273 -12.292  1.00 24.03           C  
ANISOU    6  CG  MET A   1     2605   3849   2675   -284    465   -102       C  
ATOM      7  SD  MET A   1      68.207  31.788 -12.697  1.00 25.74           S  
ANISOU    7  SD  MET A   1     2866   4089   2825   -336    408   -119       S  
ATOM      8  CE  MET A   1      67.310  32.325 -14.148  1.00 26.48           C  
ANISOU    8  CE  MET A   1     3068   4175   2818   -362    270     48       C  
ATOM      9  N   ARG A   2      69.936  36.477 -13.998  1.00 23.16           N  
ANISOU    9  N   ARG A   2     2532   3777   2490      2    396   -228       N  
ATOM     10  CA  ARG A   2      68.924  37.512 -14.124  1.00 22.06           C  
ANISOU   10  CA  ARG A   2     2442   3551   2390   -171    436   -109       C  
ATOM     11  C   ARG A   2      67.564  36.848 -14.270  1.00 22.92           C  
ANISOU   11  C   ARG A   2     2535   3635   2536   -263    463    -91       C  
ATOM     12  O   ARG A   2      67.337  36.077 -15.201  1.00 23.70           O  
ANISOU   12  O   ARG A   2     2598   3757   2652   -372    640   -208       O  
ATOM     13  CB  ARG A   2      69.194  38.432 -15.315  1.00 21.71           C  
ANISOU   13  CB  ARG A   2     2562   3486   2201   -375    446     26       C  
ATOM     14  CG  ARG A   2      68.247  39.623 -15.368  1.00 22.78           C  
ANISOU   14  CG  ARG A   2     2948   3531   2177   -589    429     -1       C  
ATOM     15  CD  ARG A   2      68.308  40.353 -16.694  1.00 24.12           C  
ANISOU   15  CD  ARG A   2     3335   3704   2125   -758    239   -185       C  
ATOM     16  NE  ARG A   2      67.537  39.656 -17.717  1.00 24.85           N  
ANISOU   16  NE  ARG A   2     3657   3718   2066   -736    490   -263       N  
ATOM     17  CZ  ARG A   2      67.523  39.994 -19.001  1.00 25.44           C  
ANISOU   17  CZ  ARG A   2     3728   3833   2106   -779    683   -289       C  
ATOM     18  NH1 ARG A   2      68.248  41.020 -19.428  1.00 26.42           N  
ANISOU   18  NH1 ARG A   2     3921   3909   2209   -906    614   -288       N  
ATOM     19  NH2 ARG A   2      66.786  39.302 -19.856  1.00 25.53           N  
ANISOU   19  NH2 ARG A   2     3669   3865   2165   -636    755   -397       N  
ATOM     20  N   LEU A   3      66.665  37.141 -13.338  1.00 23.22           N  
ANISOU   20  N   LEU A   3     2718   3587   2516   -209    490     34       N  
ATOM     21  CA  LEU A   3      65.306  36.625 -13.405  1.00 23.51           C  
ANISOU   21  CA  LEU A   3     2820   3531   2581   -331    713    -86       C  
ATOM     22  C   LEU A   3      64.415  37.522 -14.242  1.00 22.74           C  
ANISOU   22  C   LEU A   3     2649   3203   2788   -268    558   -192       C  
ATOM     23  O   LEU A   3      64.427  38.738 -14.081  1.00 23.80           O  
ANISOU   23  O   LEU A   3     2608   3269   3167    -95    381   -101       O  
ATOM     24  CB  LEU A   3      64.717  36.486 -12.001  1.00 25.38           C  
ANISOU   24  CB  LEU A   3     3246   3935   2463   -485    971   -204       C  
ATOM     25  CG  LEU A   3      64.652  35.080 -11.414  1.00 28.39           C  
ANISOU   25  CG  LEU A   3     3774   4380   2633   -443    915   -198       C  
ATOM     26  CD1 LEU A   3      64.017  35.133 -10.033  1.00 27.35           C  
ANISOU   26  CD1 LEU A   3     3644   4360   2389   -561   1157    -30       C  
ATOM     27  CD2 LEU A   3      63.873  34.153 -12.328  1.00 30.38           C  
ANISOU   27  CD2 LEU A   3     3996   4590   2958   -341    770   -230       C  
ATOM     28  N   ASP A   4      63.639  36.917 -15.133  1.00 22.89           N  
ANISOU   28  N   ASP A   4     2753   3048   2898   -233    418   -358       N  
ATOM     29  CA  ASP A   4      62.661  37.658 -15.914  1.00 25.10           C  
ANISOU   29  CA  ASP A   4     3161   3193   3182    -55    249   -514       C  
ATOM     30  C   ASP A   4      61.276  37.381 -15.356  1.00 26.18           C  
ANISOU   30  C   ASP A   4     3148   3124   3677    -81     56   -654       C  
ATOM     31  O   ASP A   4      60.804  36.245 -15.370  1.00 27.82           O  
ANISOU   31  O   ASP A   4     3279   3160   4130   -194    131   -567       O  
ATOM     32  CB  ASP A   4      62.738  37.272 -17.391  1.00 27.27           C  
ANISOU   32  CB  ASP A   4     3698   3635   3028    423    151   -366       C  
ATOM     33  CG  ASP A   4      64.123  37.463 -17.966  1.00 30.18           C  
ANISOU   33  CG  ASP A   4     4284   4114   3067    737    187   -207       C  
ATOM     34  OD1 ASP A   4      64.824  38.401 -17.531  1.00 31.39           O  
ANISOU   34  OD1 ASP A   4     4387   4396   3143    763    344   -139       O  
ATOM     35  OD2 ASP A   4      64.516  36.667 -18.847  1.00 32.05           O  
ANISOU   35  OD2 ASP A   4     4667   4381   3130   1066    181     22       O  
ATOM     36  N   LEU A   5      60.626  38.421 -14.852  1.00 25.64           N  
ANISOU   36  N   LEU A   5     3014   3042   3687    -28   -340   -425       N  
ATOM     37  CA  LEU A   5      59.345  38.250 -14.182  1.00 25.43           C  
ANISOU   37  CA  LEU A   5     2871   3095   3697   -248   -628   -479       C  
ATOM     38  C   LEU A   5      58.203  38.789 -15.018  1.00 27.85           C  
ANISOU   38  C   LEU A   5     3296   3380   3906   -198   -912   -425       C  
ATOM     39  O   LEU A   5      58.200  39.957 -15.399  1.00 28.42           O  
ANISOU   39  O   LEU A   5     3463   3479   3858    -88  -1068   -229       O  
ATOM     40  CB  LEU A   5      59.360  38.937 -12.817  1.00 25.00           C  
ANISOU   40  CB  LEU A   5     2781   3116   3601   -256   -470   -580       C  
ATOM     41  CG  LEU A   5      60.515  38.546 -11.892  1.00 24.89           C  
ANISOU   41  CG  LEU A   5     2698   3239   3519    -76   -474   -483       C  
ATOM     42  CD1 LEU A   5      60.373  39.241 -10.548  1.00 25.34           C  
ANISOU   42  CD1 LEU A   5     2717   3547   3363     25   -731   -510       C  
ATOM     43  CD2 LEU A   5      60.613  37.034 -11.738  1.00 25.94           C  
ANISOU   43  CD2 LEU A   5     2786   3448   3623   -105   -247   -247       C  
ATOM     44  N   ASP A   6      57.232  37.927 -15.295  1.00 29.96           N  
ANISOU   44  N   ASP A   6     3479   3695   4208   -204  -1108   -314       N  
ATOM     45  CA  ASP A   6      56.053  38.322 -16.049  1.00 32.21           C  
ANISOU   45  CA  ASP A   6     3887   3897   4454   -181  -1146   -298       C  
ATOM     46  C   ASP A   6      55.042  38.975 -15.120  1.00 30.53           C  
ANISOU   46  C   ASP A   6     3596   3657   4348    -52  -1005    324       C  
ATOM     47  O   ASP A   6      54.423  38.305 -14.293  1.00 30.57           O  
ANISOU   47  O   ASP A   6     3466   3583   4566    153   -928    805       O  
ATOM     48  CB  ASP A   6      55.433  37.113 -16.748  1.00 36.49           C  
ANISOU   48  CB  ASP A   6     4643   4384   4838   -172  -1233   -677       C  
ATOM     49  CG  ASP A   6      54.593  37.497 -17.955  1.00 40.93           C  
ANISOU   49  CG  ASP A   6     5377   4988   5185    -21  -1117  -1003       C  
ATOM     50  OD1 ASP A   6      53.987  38.590 -17.953  1.00 42.02           O  
ANISOU   50  OD1 ASP A   6     5419   5218   5330     28  -1201  -1101       O  
ATOM     51  OD2 ASP A   6      54.546  36.697 -18.913  1.00 42.85           O  
ANISOU   51  OD2 ASP A   6     5711   5220   5349     43   -998  -1136       O  
ATOM     52  N  APHE A   7      54.879  40.287 -15.255  0.60 28.77           N  
ANISOU   52  N  APHE A   7     3416   3423   4092   -188  -1009    431       N  
ATOM     53  N  BPHE A   7      54.869  40.285 -15.263  0.40 29.73           N  
ANISOU   53  N  BPHE A   7     3604   3526   4168   -105   -957    384       N  
ATOM     54  CA APHE A   7      53.881  41.010 -14.477  0.60 28.17           C  
ANISOU   54  CA APHE A   7     3311   3498   3896   -113  -1010    462       C  
ATOM     55  CA BPHE A   7      53.869  41.005 -14.485  0.40 29.55           C  
ANISOU   55  CA BPHE A   7     3624   3593   4009    -44   -918    406       C  
ATOM     56  C  APHE A   7      52.566  41.084 -15.248  0.60 29.73           C  
ANISOU   56  C  APHE A   7     3524   3825   3946    133  -1148    633       C  
ATOM     57  C  BPHE A   7      52.566  41.112 -15.268  0.40 30.32           C  
ANISOU   57  C  BPHE A   7     3681   3817   4025     63  -1062    557       C  
ATOM     58  O  APHE A   7      51.636  41.774 -14.836  0.60 31.24           O  
ANISOU   58  O  APHE A   7     3613   4263   3994    278  -1106    651       O  
ATOM     59  O  BPHE A   7      51.654  41.849 -14.892  0.40 31.49           O  
ANISOU   59  O  BPHE A   7     3766   4123   4076    119   -994    530       O  
ATOM     60  CB APHE A   7      54.375  42.422 -14.121  0.60 26.03           C  
ANISOU   60  CB APHE A   7     3125   3126   3639   -181   -803    323       C  
ATOM     61  CB BPHE A   7      54.383  42.392 -14.098  0.40 28.46           C  
ANISOU   61  CB BPHE A   7     3636   3364   3815    -28   -722    303       C  
ATOM     62  CG APHE A   7      55.280  42.470 -12.914  0.60 24.52           C  
ANISOU   62  CG APHE A   7     2856   2980   3480   -254   -458    154       C  
ATOM     63  CG BPHE A   7      55.293  42.384 -12.904  0.40 27.65           C  
ANISOU   63  CG BPHE A   7     3573   3273   3661     -4   -467    201       C  
ATOM     64  CD1APHE A   7      55.469  43.656 -12.218  0.60 23.25           C  
ANISOU   64  CD1APHE A   7     2642   2800   3393   -202   -140    179       C  
ATOM     65  CD1BPHE A   7      54.772  42.447 -11.624  0.40 27.28           C  
ANISOU   65  CD1BPHE A   7     3491   3275   3599     -3   -292    239       C  
ATOM     66  CD2APHE A   7      55.939  41.332 -12.476  0.60 24.63           C  
ANISOU   66  CD2APHE A   7     2808   3067   3482   -300   -307     93       C  
ATOM     67  CD2BPHE A   7      56.664  42.291 -13.058  0.40 27.47           C  
ANISOU   67  CD2BPHE A   7     3591   3250   3597     61   -312    151       C  
ATOM     68  CE1APHE A   7      56.293  43.702 -11.111  0.60 22.77           C  
ANISOU   68  CE1APHE A   7     2466   2828   3359   -193     76     59       C  
ATOM     69  CE1BPHE A   7      55.603  42.432 -10.522  0.40 27.66           C  
ANISOU   69  CE1BPHE A   7     3527   3376   3608      3   -234    224       C  
ATOM     70  CE2APHE A   7      56.766  41.374 -11.366  0.60 23.78           C  
ANISOU   70  CE2APHE A   7     2606   3006   3424   -313    -61    128       C  
ATOM     71  CE2BPHE A   7      57.495  42.276 -11.957  0.40 27.79           C  
ANISOU   71  CE2BPHE A   7     3601   3335   3625    128   -215    195       C  
ATOM     72  CZ APHE A   7      56.941  42.562 -10.685  0.60 23.46           C  
ANISOU   72  CZ APHE A   7     2506   3058   3348   -179    138    134       C  
ATOM     73  CZ BPHE A   7      56.965  42.346 -10.689  0.40 27.80           C  
ANISOU   73  CZ BPHE A   7     3552   3413   3597     89   -161    229       C  
ATOM     74  N   GLY A   8      52.494  40.365 -16.364  1.00 29.93           N  
ANISOU   74  N   GLY A   8     3604   3717   4052    -91  -1257    699       N  
ATOM     75  CA  GLY A   8      51.299  40.332 -17.184  1.00 30.36           C  
ANISOU   75  CA  GLY A   8     3667   3629   4238   -244  -1385    733       C  
ATOM     76  C   GLY A   8      51.181  41.517 -18.122  1.00 30.90           C  
ANISOU   76  C   GLY A   8     3749   3596   4398   -605  -1386    726       C  
ATOM     77  O   GLY A   8      51.868  42.521 -17.953  1.00 31.43           O  
ANISOU   77  O   GLY A   8     3694   3724   4525   -515  -1258    554       O  
ATOM     78  N   ARG A   9      50.310  41.383 -19.119  1.00 31.68           N  
ANISOU   78  N   ARG A   9     3881   3665   4491   -576  -1404    978       N  
ATOM     79  CA  ARG A   9      49.975  42.473 -20.034  1.00 32.18           C  
ANISOU   79  CA  ARG A   9     3885   3770   4570   -624  -1369    942       C  
ATOM     80  C   ARG A   9      51.196  43.070 -20.728  1.00 31.11           C  
ANISOU   80  C   ARG A   9     3521   3853   4447   -919  -1718    940       C  
ATOM     81  O   ARG A   9      51.279  44.285 -20.911  1.00 30.98           O  
ANISOU   81  O   ARG A   9     3484   3851   4435   -986  -1796   1357       O  
ATOM     82  CB  ARG A   9      49.217  43.577 -19.287  1.00 33.39           C  
ANISOU   82  CB  ARG A   9     4063   3918   4707   -284  -1197    842       C  
ATOM     83  N   GLY A  10      52.139  42.217 -21.111  1.00 30.64           N  
ANISOU   83  N   GLY A  10     3408   3862   4373  -1187  -1726    795       N  
ATOM     84  CA  GLY A  10      53.324  42.669 -21.814  1.00 30.26           C  
ANISOU   84  CA  GLY A  10     3461   3696   4340  -1080  -1759    662       C  
ATOM     85  C   GLY A  10      54.306  43.402 -20.918  1.00 29.40           C  
ANISOU   85  C   GLY A  10     3567   3359   4243   -789  -1749    542       C  
ATOM     86  O   GLY A  10      55.292  43.956 -21.407  1.00 28.67           O  
ANISOU   86  O   GLY A  10     3515   3165   4211   -607  -1719    717       O  
ATOM     87  N   LEU A  11      54.031  43.403 -19.614  1.00 29.19           N  
ANISOU   87  N   LEU A  11     3711   3259   4121   -748  -1509    414       N  
ATOM     88  CA  LEU A  11      54.937  43.979 -18.622  1.00 29.91           C  
ANISOU   88  CA  LEU A  11     3685   3549   4129   -473  -1277    360       C  
ATOM     89  C   LEU A  11      55.929  42.939 -18.125  1.00 29.69           C  
ANISOU   89  C   LEU A  11     3534   3725   4023   -445  -1337    163       C  
ATOM     90  O   LEU A  11      55.537  41.887 -17.619  1.00 29.04           O  
ANISOU   90  O   LEU A  11     3365   3597   4072   -486  -1420    150       O  
ATOM     91  CB  LEU A  11      54.161  44.546 -17.429  1.00 30.94           C  
ANISOU   91  CB  LEU A  11     3862   3693   4201   -463   -893    352       C  
ATOM     92  CG  LEU A  11      53.324  45.815 -17.578  1.00 32.12           C  
ANISOU   92  CG  LEU A  11     4116   3808   4278   -594   -541    251       C  
ATOM     93  CD1 LEU A  11      52.401  45.978 -16.380  1.00 32.81           C  
ANISOU   93  CD1 LEU A  11     4197   3924   4344   -665   -540     80       C  
ATOM     94  CD2 LEU A  11      54.227  47.027 -17.727  1.00 31.55           C  
ANISOU   94  CD2 LEU A  11     4167   3588   4231   -540   -453    372       C  
ATOM     95  N   VAL A  12      57.214  43.239 -18.269  1.00 30.01           N  
ANISOU   95  N   VAL A  12     3588   3910   3904   -210  -1187      4       N  
ATOM     96  CA  VAL A  12      58.267  42.370 -17.770  1.00 29.40           C  
ANISOU   96  CA  VAL A  12     3483   4008   3679   -123  -1177   -205       C  
ATOM     97  C   VAL A  12      59.144  43.155 -16.807  1.00 27.69           C  
ANISOU   97  C   VAL A  12     3301   3785   3434   -137  -1198     12       C  
ATOM     98  O   VAL A  12      59.416  44.330 -17.028  1.00 28.36           O  
ANISOU   98  O   VAL A  12     3246   3981   3550   -269  -1169    311       O  
ATOM     99  CB  VAL A  12      59.138  41.814 -18.912  1.00 31.49           C  
ANISOU   99  CB  VAL A  12     3819   4407   3739      6  -1069   -445       C  
ATOM    100  CG1 VAL A  12      60.048  40.702 -18.403  1.00 31.99           C  
ANISOU  100  CG1 VAL A  12     3937   4487   3729      4  -1054   -503       C  
ATOM    101  CG2 VAL A  12      58.265  41.316 -20.058  1.00 33.00           C  
ANISOU  101  CG2 VAL A  12     3942   4647   3950    -70  -1117   -487       C  
ATOM    102  N   ALA A  13      59.581  42.522 -15.730  1.00 25.94           N  
ANISOU  102  N   ALA A  13     3131   3519   3206      5  -1256   -143       N  
ATOM    103  CA  ALA A  13      60.602  43.152 -14.911  1.00 25.60           C  
ANISOU  103  CA  ALA A  13     3211   3441   3076     87  -1244    -97       C  
ATOM    104  C   ALA A  13      61.725  42.168 -14.647  1.00 25.17           C  
ANISOU  104  C   ALA A  13     3166   3409   2987    -93  -1099     82       C  
ATOM    105  O   ALA A  13      61.611  40.984 -14.952  1.00 25.53           O  
ANISOU  105  O   ALA A  13     3213   3381   3106   -177  -1029   -111       O  
ATOM    106  CB  ALA A  13      60.025  43.663 -13.624  1.00 26.62           C  
ANISOU  106  CB  ALA A  13     3454   3563   3095    446  -1180    -34       C  
ATOM    107  N   HIS A  14      62.816  42.673 -14.087  1.00 25.02           N  
ANISOU  107  N   HIS A  14     3218   3534   2755    -77  -1007    301       N  
ATOM    108  CA  HIS A  14      64.005  41.873 -13.881  1.00 25.21           C  
ANISOU  108  CA  HIS A  14     3164   3691   2722   -179   -806    474       C  
ATOM    109  C   HIS A  14      64.474  42.059 -12.460  1.00 22.88           C  
ANISOU  109  C   HIS A  14     2642   3519   2532   -269   -409    402       C  
ATOM    110  O   HIS A  14      64.276  43.117 -11.863  1.00 23.25           O  
ANISOU  110  O   HIS A  14     2633   3563   2640   -284   -429    418       O  
ATOM    111  CB  HIS A  14      65.103  42.265 -14.869  1.00 28.04           C  
ANISOU  111  CB  HIS A  14     3742   3994   2919    -76   -674    418       C  
ATOM    112  CG  HIS A  14      64.644  42.273 -16.292  1.00 31.24           C  
ANISOU  112  CG  HIS A  14     4354   4305   3211   -108   -462    392       C  
ATOM    113  ND1 HIS A  14      64.630  41.138 -17.074  1.00 32.99           N  
ANISOU  113  ND1 HIS A  14     4632   4477   3427    -66   -349    391       N  
ATOM    114  CD2 HIS A  14      64.156  43.271 -17.065  1.00 32.42           C  
ANISOU  114  CD2 HIS A  14     4564   4441   3313   -119   -390    449       C  
ATOM    115  CE1 HIS A  14      64.163  41.440 -18.273  1.00 33.23           C  
ANISOU  115  CE1 HIS A  14     4682   4539   3404     33   -428    509       C  
ATOM    116  NE2 HIS A  14      63.867  42.727 -18.292  1.00 33.59           N  
ANISOU  116  NE2 HIS A  14     4728   4604   3430    -68   -454    578       N  
ATOM    117  N   VAL A  15      65.071  41.012 -11.917  1.00 20.26           N  
ANISOU  117  N   VAL A  15     2081   3247   2371   -270   -302    443       N  
ATOM    118  CA  VAL A  15      65.710  41.097 -10.618  1.00 20.92           C  
ANISOU  118  CA  VAL A  15     2128   3424   2398   -270    -15    445       C  
ATOM    119  C   VAL A  15      66.837  40.073 -10.629  1.00 21.06           C  
ANISOU  119  C   VAL A  15     2143   3428   2431   -335     43    407       C  
ATOM    120  O   VAL A  15      66.728  39.026 -11.270  1.00 22.36           O  
ANISOU  120  O   VAL A  15     2385   3682   2430   -404    151    385       O  
ATOM    121  CB  VAL A  15      64.710  40.841  -9.452  1.00 21.67           C  
ANISOU  121  CB  VAL A  15     2274   3509   2452   -306    150    310       C  
ATOM    122  CG1 VAL A  15      64.218  39.402  -9.463  1.00 22.60           C  
ANISOU  122  CG1 VAL A  15     2421   3604   2563   -366    196    280       C  
ATOM    123  CG2 VAL A  15      65.349  41.185  -8.105  1.00 22.47           C  
ANISOU  123  CG2 VAL A  15     2319   3649   2570   -189    217     16       C  
ATOM    124  N  AMET A  16      67.927  40.394  -9.938  0.45 21.44           N  
ANISOU  124  N  AMET A  16     2213   3397   2536   -224     51    389       N  
ATOM    125  N  BMET A  16      67.934  40.371  -9.944  0.55 20.99           N  
ANISOU  125  N  BMET A  16     2133   3365   2477   -223    186    285       N  
ATOM    126  CA AMET A  16      69.039  39.465  -9.788  0.45 21.86           C  
ANISOU  126  CA AMET A  16     2322   3371   2611   -100    154    295       C  
ATOM    127  CA BMET A  16      69.046  39.429  -9.899  0.55 20.99           C  
ANISOU  127  CA BMET A  16     2223   3260   2491   -116    401     44       C  
ATOM    128  C  AMET A  16      68.688  38.365  -8.798  0.45 20.23           C  
ANISOU  128  C  AMET A  16     2089   3149   2447    224    214    100       C  
ATOM    129  C  BMET A  16      68.852  38.399  -8.792  0.55 20.56           C  
ANISOU  129  C  BMET A  16     2265   3151   2395     97    354    -34       C  
ATOM    130  O  AMET A  16      68.125  38.629  -7.734  0.45 18.95           O  
ANISOU  130  O  AMET A  16     1880   3031   2289    621     59    -78       O  
ATOM    131  O  BMET A  16      68.548  38.746  -7.651  0.55 20.60           O  
ANISOU  131  O  BMET A  16     2500   3094   2234    228    176   -241       O  
ATOM    132  CB AMET A  16      70.303  40.189  -9.316  0.45 24.39           C  
ANISOU  132  CB AMET A  16     2736   3665   2864   -238     61    355       C  
ATOM    133  CB BMET A  16      70.371  40.168  -9.711  0.55 22.56           C  
ANISOU  133  CB BMET A  16     2483   3418   2670   -194    478    -72       C  
ATOM    134  CG AMET A  16      70.824  41.249 -10.268  0.45 27.38           C  
ANISOU  134  CG AMET A  16     3227   3990   3186   -330    141    364       C  
ATOM    135  CG BMET A  16      70.712  41.106 -10.860  0.55 24.04           C  
ANISOU  135  CG BMET A  16     2844   3527   2762   -230    589    -60       C  
ATOM    136  SD AMET A  16      71.095  40.614 -11.930  0.45 30.06           S  
ANISOU  136  SD AMET A  16     3663   4251   3508   -569    276    314       S  
ATOM    137  SD BMET A  16      70.825  40.252 -12.446  0.55 25.40           S  
ANISOU  137  SD BMET A  16     3153   3589   2909   -608    654     75       S  
ATOM    138  CE AMET A  16      69.814  41.494 -12.816  0.45 30.33           C  
ANISOU  138  CE AMET A  16     3673   4276   3576   -571    229    282       C  
ATOM    139  CE BMET A  16      72.153  39.102 -12.103  0.55 25.10           C  
ANISOU  139  CE BMET A  16     3107   3550   2880   -552    619    178       C  
ATOM    140  N   LEU A  17      69.024  37.133  -9.154  1.00 19.81           N  
ANISOU  140  N   LEU A  17     2094   3040   2391    144    424     49       N  
ATOM    141  CA  LEU A  17      68.882  36.017  -8.237  1.00 20.06           C  
ANISOU  141  CA  LEU A  17     2098   3177   2348     -8    459     -6       C  
ATOM    142  C   LEU A  17      70.252  35.373  -8.057  1.00 21.11           C  
ANISOU  142  C   LEU A  17     2136   3413   2469     73    399     39       C  
ATOM    143  O   LEU A  17      70.649  34.491  -8.829  1.00 21.77           O  
ANISOU  143  O   LEU A  17     1932   3809   2529    -62    627    106       O  
ATOM    144  CB  LEU A  17      67.857  35.012  -8.763  1.00 19.04           C  
ANISOU  144  CB  LEU A  17     2225   2993   2014     40    610    -77       C  
ATOM    145  CG  LEU A  17      67.551  33.807  -7.876  1.00 21.19           C  
ANISOU  145  CG  LEU A  17     2576   3270   2205    137    705   -160       C  
ATOM    146  CD1 LEU A  17      66.874  34.266  -6.586  1.00 21.39           C  
ANISOU  146  CD1 LEU A  17     2536   3392   2198    182    877    -86       C  
ATOM    147  CD2 LEU A  17      66.692  32.792  -8.623  1.00 22.42           C  
ANISOU  147  CD2 LEU A  17     2820   3449   2250    185    479   -195       C  
ATOM    148  N   ASP A  18      70.973  35.845  -7.043  1.00 21.51           N  
ANISOU  148  N   ASP A  18     2098   3607   2467    133    402    283       N  
ATOM    149  CA  ASP A  18      72.352  35.438  -6.788  1.00 23.40           C  
ANISOU  149  CA  ASP A  18     2278   3796   2815     82    392    134       C  
ATOM    150  C   ASP A  18      72.484  33.966  -6.431  1.00 22.47           C  
ANISOU  150  C   ASP A  18     2029   3804   2706     97    472     15       C  
ATOM    151  O   ASP A  18      71.642  33.411  -5.725  1.00 22.22           O  
ANISOU  151  O   ASP A  18     2154   3753   2537    -12    397    103       O  
ATOM    152  CB  ASP A  18      72.946  36.284  -5.660  1.00 26.98           C  
ANISOU  152  CB  ASP A  18     2814   4006   3431    -88    356     70       C  
ATOM    153  CG  ASP A  18      72.848  37.768  -5.933  1.00 31.13           C  
ANISOU  153  CG  ASP A  18     3548   4310   3969   -122    348    144       C  
ATOM    154  OD1 ASP A  18      73.184  38.186  -7.060  1.00 32.39           O  
ANISOU  154  OD1 ASP A  18     3902   4191   4212   -304    257    441       O  
ATOM    155  OD2 ASP A  18      72.432  38.515  -5.023  1.00 33.73           O  
ANISOU  155  OD2 ASP A  18     3919   4568   4328   -147    347     61       O  
ATOM    156  N   ASN A  19      73.559  33.350  -6.922  1.00 22.88           N  
ANISOU  156  N   ASN A  19     1946   3933   2814   -128    327   -101       N  
ATOM    157  CA  ASN A  19      73.888  31.949  -6.649  1.00 21.72           C  
ANISOU  157  CA  ASN A  19     1756   3982   2513    -97    210      8       C  
ATOM    158  C   ASN A  19      72.792  30.968  -7.047  1.00 21.06           C  
ANISOU  158  C   ASN A  19     1838   3941   2224      3    120    -37       C  
ATOM    159  O   ASN A  19      72.588  29.940  -6.398  1.00 23.01           O  
ANISOU  159  O   ASN A  19     2303   4174   2265    246     -2   -279       O  
ATOM    160  CB  ASN A  19      74.252  31.777  -5.175  1.00 23.33           C  
ANISOU  160  CB  ASN A  19     1742   4330   2791   -164    392     51       C  
ATOM    161  CG  ASN A  19      75.558  32.462  -4.829  1.00 25.96           C  
ANISOU  161  CG  ASN A  19     2227   4646   2990    -33    648    121       C  
ATOM    162  OD1 ASN A  19      76.624  32.058  -5.301  1.00 27.67           O  
ANISOU  162  OD1 ASN A  19     2503   4818   3192    156    906    219       O  
ATOM    163  ND2 ASN A  19      75.483  33.518  -4.033  1.00 26.13           N  
ANISOU  163  ND2 ASN A  19     2273   4699   2955     28    832    169       N  
ATOM    164  N   VAL A  20      72.091  31.303  -8.124  1.00 20.37           N  
ANISOU  164  N   VAL A  20     1770   3956   2015     -8    316   -340       N  
ATOM    165  CA  VAL A  20      71.183  30.380  -8.785  1.00 20.13           C  
ANISOU  165  CA  VAL A  20     1755   3938   1957     -4    313   -232       C  
ATOM    166  C   VAL A  20      71.482  30.434 -10.271  1.00 22.08           C  
ANISOU  166  C   VAL A  20     2106   4227   2057     11    455   -133       C  
ATOM    167  O   VAL A  20      71.420  31.500 -10.875  1.00 23.29           O  
ANISOU  167  O   VAL A  20     2300   4365   2183    -49    298      2       O  
ATOM    168  CB  VAL A  20      69.702  30.733  -8.549  1.00 19.43           C  
ANISOU  168  CB  VAL A  20     1659   3738   1983    -66    372   -230       C  
ATOM    169  CG1 VAL A  20      68.795  29.749  -9.283  1.00 19.47           C  
ANISOU  169  CG1 VAL A  20     1737   3652   2008   -300    355    -89       C  
ATOM    170  CG2 VAL A  20      69.388  30.749  -7.062  1.00 19.07           C  
ANISOU  170  CG2 VAL A  20     1626   3715   1903    -67    463   -292       C  
ATOM    171  N   SER A  21      71.824  29.294 -10.852  1.00 23.34           N  
ANISOU  171  N   SER A  21     2482   4304   2082   -133    452   -258       N  
ATOM    172  CA  SER A  21      72.075  29.237 -12.285  1.00 24.54           C  
ANISOU  172  CA  SER A  21     2614   4529   2179     43    625   -326       C  
ATOM    173  C   SER A  21      70.776  28.950 -13.022  1.00 24.28           C  
ANISOU  173  C   SER A  21     2757   4424   2045    315    811   -148       C  
ATOM    174  O   SER A  21      69.800  28.487 -12.422  1.00 23.65           O  
ANISOU  174  O   SER A  21     2634   4182   2168    279    626    -98       O  
ATOM    175  CB  SER A  21      73.118  28.168 -12.610  1.00 26.09           C  
ANISOU  175  CB  SER A  21     2656   4791   2465     93    545   -318       C  
ATOM    176  OG  SER A  21      72.610  26.871 -12.367  1.00 27.59           O  
ANISOU  176  OG  SER A  21     2888   5040   2555    277    414   -200       O  
ATOM    177  N   GLU A  22      70.764  29.212 -14.325  1.00 26.23           N  
ANISOU  177  N   GLU A  22     3296   4557   2112    237    973     78       N  
ATOM    178  CA  GLU A  22      69.625  28.844 -15.157  1.00 28.50           C  
ANISOU  178  CA  GLU A  22     3758   4728   2343    171   1024     12       C  
ATOM    179  C   GLU A  22      69.294  27.364 -14.994  1.00 26.93           C  
ANISOU  179  C   GLU A  22     3626   4321   2286    403    941   -173       C  
ATOM    180  O   GLU A  22      68.128  26.982 -14.940  1.00 26.45           O  
ANISOU  180  O   GLU A  22     3599   4279   2170    435   1022   -307       O  
ATOM    181  CB  GLU A  22      69.903  29.161 -16.631  1.00 31.52           C  
ANISOU  181  CB  GLU A  22     4223   5092   2662     87   1045    148       C  
ATOM    182  CG  GLU A  22      69.839  30.638 -16.985  1.00 36.28           C  
ANISOU  182  CG  GLU A  22     4740   5660   3384    -22   1154    223       C  
ATOM    183  CD  GLU A  22      68.420  31.120 -17.240  1.00 39.66           C  
ANISOU  183  CD  GLU A  22     5142   6012   3913    -54   1136    293       C  
ATOM    184  OE1 GLU A  22      67.477  30.312 -17.101  1.00 41.15           O  
ANISOU  184  OE1 GLU A  22     5274   6209   4152   -100   1213    352       O  
ATOM    185  OE2 GLU A  22      68.246  32.307 -17.589  1.00 40.94           O  
ANISOU  185  OE2 GLU A  22     5268   6216   4073    -50   1064    213       O  
ATOM    186  N  AGLU A  23      70.325  26.532 -14.895  0.55 27.17           N  
ANISOU  186  N  AGLU A  23     3635   4289   2400    379    915   -137       N  
ATOM    187  N  BGLU A  23      70.338  26.543 -14.916  0.45 26.72           N  
ANISOU  187  N  BGLU A  23     3557   4211   2385    398    777     -8       N  
ATOM    188  CA AGLU A  23      70.128  25.089 -14.802  0.55 27.56           C  
ANISOU  188  CA AGLU A  23     3598   4284   2589    403   1023    -92       C  
ATOM    189  CA BGLU A  23      70.198  25.096 -14.780  0.45 26.74           C  
ANISOU  189  CA BGLU A  23     3481   4124   2555    435    715    146       C  
ATOM    190  C  AGLU A  23      69.554  24.679 -13.447  0.55 25.49           C  
ANISOU  190  C  AGLU A  23     3270   4015   2401    539    949      0       C  
ATOM    191  C  BGLU A  23      69.547  24.709 -13.457  0.45 25.17           C  
ANISOU  191  C  BGLU A  23     3217   3944   2401    523    796    126       C  
ATOM    192  O  AGLU A  23      68.707  23.790 -13.375  0.55 24.02           O  
ANISOU  192  O  AGLU A  23     3105   3741   2280    618    981     67       O  
ATOM    193  O  BGLU A  23      68.652  23.868 -13.415  0.45 24.00           O  
ANISOU  193  O  BGLU A  23     3066   3709   2343    544    821    216       O  
ATOM    194  CB AGLU A  23      71.444  24.352 -15.061  0.55 29.69           C  
ANISOU  194  CB AGLU A  23     3818   4462   3001    368   1312   -236       C  
ATOM    195  CB BGLU A  23      71.567  24.421 -14.901  0.45 28.26           C  
ANISOU  195  CB BGLU A  23     3650   4144   2944    445    656    220       C  
ATOM    196  CG AGLU A  23      72.211  24.848 -16.281  0.55 31.93           C  
ANISOU  196  CG AGLU A  23     4010   4687   3435    367   1529   -371       C  
ATOM    197  CG BGLU A  23      71.567  22.954 -14.519  0.45 29.96           C  
ANISOU  197  CG BGLU A  23     3833   4205   3346    436    531    242       C  
ATOM    198  CD AGLU A  23      73.329  25.804 -15.917  0.55 34.12           C  
ANISOU  198  CD AGLU A  23     4231   4927   3807    348   1640   -411       C  
ATOM    199  CD BGLU A  23      72.964  22.401 -14.325  0.45 31.75           C  
ANISOU  199  CD BGLU A  23     4044   4301   3718    354    399    290       C  
ATOM    200  OE1AGLU A  23      74.391  25.329 -15.465  0.55 36.14           O  
ANISOU  200  OE1AGLU A  23     4491   5150   4090    351   1598   -474       O  
ATOM    201  OE1BGLU A  23      73.938  23.175 -14.451  0.45 32.55           O  
ANISOU  201  OE1BGLU A  23     4224   4320   3825    193    322    205       O  
ATOM    202  OE2AGLU A  23      73.142  27.029 -16.078  0.55 33.64           O  
ANISOU  202  OE2AGLU A  23     4058   4857   3866    429   1893   -388       O  
ATOM    203  OE2BGLU A  23      73.087  21.191 -14.044  0.45 32.13           O  
ANISOU  203  OE2BGLU A  23     4006   4308   3894    559    325    351       O  
ATOM    204  N   GLN A  24      70.020  25.324 -12.382  1.00 24.44           N  
ANISOU  204  N   GLN A  24     3137   3932   2219    583    851      1       N  
ATOM    205  CA  GLN A  24      69.486  25.062 -11.048  1.00 23.62           C  
ANISOU  205  CA  GLN A  24     2877   3867   2231    522    698   -112       C  
ATOM    206  C   GLN A  24      68.032  25.505 -10.961  1.00 22.39           C  
ANISOU  206  C   GLN A  24     2910   3399   2199    435    429    -72       C  
ATOM    207  O   GLN A  24      67.196  24.814 -10.379  1.00 21.54           O  
ANISOU  207  O   GLN A  24     2885   3105   2193    245    314   -191       O  
ATOM    208  CB  GLN A  24      70.319  25.773  -9.986  1.00 24.53           C  
ANISOU  208  CB  GLN A  24     2665   4113   2543    663    557   -163       C  
ATOM    209  CG  GLN A  24      71.662  25.115  -9.715  1.00 25.51           C  
ANISOU  209  CG  GLN A  24     2613   4212   2867    760    503    -42       C  
ATOM    210  CD  GLN A  24      72.590  25.998  -8.902  1.00 26.35           C  
ANISOU  210  CD  GLN A  24     2619   4370   3022    605    536     15       C  
ATOM    211  OE1 GLN A  24      72.502  27.226  -8.948  1.00 25.42           O  
ANISOU  211  OE1 GLN A  24     2444   4128   3086    363    595    -59       O  
ATOM    212  NE2 GLN A  24      73.491  25.373  -8.153  1.00 27.09           N  
ANISOU  212  NE2 GLN A  24     2681   4578   3034    888    561    161       N  
ATOM    213  N   TYR A  25      67.741  26.661 -11.551  1.00 20.73           N  
ANISOU  213  N   TYR A  25     2692   3087   2097    442    417   -181       N  
ATOM    214  CA  TYR A  25      66.375  27.173 -11.610  1.00 18.86           C  
ANISOU  214  CA  TYR A  25     2330   2861   1975    350    353   -160       C  
ATOM    215  C   TYR A  25      65.458  26.166 -12.306  1.00 18.66           C  
ANISOU  215  C   TYR A  25     2199   3020   1869    391    305   -406       C  
ATOM    216  O   TYR A  25      64.373  25.855 -11.812  1.00 17.97           O  
ANISOU  216  O   TYR A  25     1871   2988   1968    664    214   -298       O  
ATOM    217  CB  TYR A  25      66.332  28.535 -12.324  1.00 18.54           C  
ANISOU  217  CB  TYR A  25     2371   2724   1950    425    309    -63       C  
ATOM    218  CG  TYR A  25      64.955  29.166 -12.342  1.00 18.10           C  
ANISOU  218  CG  TYR A  25     2216   2604   2056    463    245     70       C  
ATOM    219  CD1 TYR A  25      64.590  30.120 -11.404  1.00 17.38           C  
ANISOU  219  CD1 TYR A  25     2185   2355   2064    519    353     21       C  
ATOM    220  CD2 TYR A  25      64.010  28.788 -13.288  1.00 19.11           C  
ANISOU  220  CD2 TYR A  25     2100   2769   2392    464    -40    -36       C  
ATOM    221  CE1 TYR A  25      63.330  30.690 -11.421  1.00 18.30           C  
ANISOU  221  CE1 TYR A  25     2133   2548   2274    419    205    226       C  
ATOM    222  CE2 TYR A  25      62.747  29.347 -13.305  1.00 19.43           C  
ANISOU  222  CE2 TYR A  25     2009   2776   2597    424     97   -182       C  
ATOM    223  CZ  TYR A  25      62.410  30.294 -12.369  1.00 19.33           C  
ANISOU  223  CZ  TYR A  25     2067   2665   2611    437    131     17       C  
ATOM    224  OH  TYR A  25      61.150  30.855 -12.396  1.00 21.54           O  
ANISOU  224  OH  TYR A  25     2351   2792   3042    240     97     18       O  
ATOM    225  N   GLN A  26      65.891  25.646 -13.450  1.00 18.73           N  
ANISOU  225  N   GLN A  26     2255   3179   1683    314    158   -467       N  
ATOM    226  CA  GLN A  26      65.077  24.661 -14.163  1.00 19.91           C  
ANISOU  226  CA  GLN A  26     2645   3238   1683    475    328   -580       C  
ATOM    227  C   GLN A  26      64.861  23.394 -13.342  1.00 19.93           C  
ANISOU  227  C   GLN A  26     2670   3104   1799    786    378   -465       C  
ATOM    228  O   GLN A  26      63.790  22.801 -13.387  1.00 19.72           O  
ANISOU  228  O   GLN A  26     2665   2907   1921    687    309   -523       O  
ATOM    229  CB  GLN A  26      65.713  24.310 -15.515  1.00 21.44           C  
ANISOU  229  CB  GLN A  26     2966   3517   1662    433     80   -556       C  
ATOM    230  CG  GLN A  26      64.776  23.552 -16.449  1.00 23.02           C  
ANISOU  230  CG  GLN A  26     3290   3634   1824    359   -169   -382       C  
ATOM    231  CD  GLN A  26      63.577  24.387 -16.868  1.00 25.39           C  
ANISOU  231  CD  GLN A  26     3693   3837   2117    281   -340   -180       C  
ATOM    232  OE1 GLN A  26      63.730  25.474 -17.419  1.00 28.24           O  
ANISOU  232  OE1 GLN A  26     4006   4184   2539    225   -451     66       O  
ATOM    233  NE2 GLN A  26      62.378  23.883 -16.602  1.00 24.84           N  
ANISOU  233  NE2 GLN A  26     3728   3863   1846    474   -118   -417       N  
ATOM    234  N  AGLN A  27      65.882  23.006 -12.589  0.48 20.50           N  
ANISOU  234  N  AGLN A  27     2767   3109   1911    691    393   -201       N  
ATOM    235  N  BGLN A  27      65.882  22.982 -12.593  0.52 20.45           N  
ANISOU  235  N  BGLN A  27     2759   3132   1877    796    434   -194       N  
ATOM    236  CA AGLN A  27      65.811  21.840 -11.723  0.48 21.37           C  
ANISOU  236  CA AGLN A  27     2919   3074   2127    597    248   -216       C  
ATOM    237  CA BGLN A  27      65.763  21.810 -11.725  0.52 21.21           C  
ANISOU  237  CA BGLN A  27     2887   3095   2076    830    336   -241       C  
ATOM    238  C  AGLN A  27      64.728  22.028 -10.662  0.48 20.13           C  
ANISOU  238  C  AGLN A  27     2917   2749   1983    461    171   -394       C  
ATOM    239  C  BGLN A  27      64.679  22.037 -10.680  0.52 19.78           C  
ANISOU  239  C  BGLN A  27     2863   2701   1950    660    147   -416       C  
ATOM    240  O  AGLN A  27      63.931  21.129 -10.398  0.48 19.52           O  
ANISOU  240  O  AGLN A  27     2923   2706   1787    130    261   -278       O  
ATOM    241  O  BGLN A  27      63.845  21.167 -10.430  0.52 18.69           O  
ANISOU  241  O  BGLN A  27     2791   2565   1745    460    146   -317       O  
ATOM    242  CB AGLN A  27      67.173  21.603 -11.075  0.48 23.51           C  
ANISOU  242  CB AGLN A  27     3083   3347   2501    724    189    -71       C  
ATOM    243  CB BGLN A  27      67.089  21.499 -11.028  0.52 23.45           C  
ANISOU  243  CB BGLN A  27     3048   3444   2420   1155    455   -156       C  
ATOM    244  CG AGLN A  27      67.338  20.283 -10.365  0.48 25.45           C  
ANISOU  244  CG AGLN A  27     3360   3468   2841    603     90    -28       C  
ATOM    245  CG BGLN A  27      68.201  21.006 -11.934  0.52 25.67           C  
ANISOU  245  CG BGLN A  27     3372   3652   2730   1212    528   -183       C  
ATOM    246  CD AGLN A  27      68.761  20.086  -9.887  0.48 27.55           C  
ANISOU  246  CD AGLN A  27     3659   3617   3190    409    -72     42       C  
ATOM    247  CD BGLN A  27      69.517  20.868 -11.195  0.52 28.53           C  
ANISOU  247  CD BGLN A  27     3670   4044   3127   1025    556    -99       C  
ATOM    248  OE1AGLN A  27      69.594  20.986  -9.998  0.48 27.76           O  
ANISOU  248  OE1AGLN A  27     3725   3551   3272    425   -283    -62       O  
ATOM    249  OE1BGLN A  27      70.549  21.368 -11.640  0.52 30.49           O  
ANISOU  249  OE1BGLN A  27     3960   4227   3400    863    425   -100       O  
ATOM    250  NE2AGLN A  27      69.052  18.905  -9.365  0.48 28.75           N  
ANISOU  250  NE2AGLN A  27     3867   3672   3385    259    -14     79       N  
ATOM    251  NE2BGLN A  27      69.485  20.190 -10.054  0.52 29.52           N  
ANISOU  251  NE2BGLN A  27     3691   4209   3316   1006    474     90       N  
ATOM    252  N   ILE A  28      64.704  23.218 -10.070  1.00 19.02           N  
ANISOU  252  N   ILE A  28     2767   2516   1943    558    103   -555       N  
ATOM    253  CA  ILE A  28      63.712  23.563  -9.064  1.00 18.10           C  
ANISOU  253  CA  ILE A  28     2332   2551   1995    661    -86   -319       C  
ATOM    254  C   ILE A  28      62.329  23.613  -9.705  1.00 18.66           C  
ANISOU  254  C   ILE A  28     2537   2476   2078    629     60   -219       C  
ATOM    255  O   ILE A  28      61.363  23.078  -9.166  1.00 18.29           O  
ANISOU  255  O   ILE A  28     2653   2241   2055    684    248   -292       O  
ATOM    256  CB  ILE A  28      64.040  24.912  -8.403  1.00 17.36           C  
ANISOU  256  CB  ILE A  28     2143   2510   1944    738     96   -482       C  
ATOM    257  CG1 ILE A  28      65.350  24.811  -7.614  1.00 18.70           C  
ANISOU  257  CG1 ILE A  28     2170   2713   2224    656      4   -290       C  
ATOM    258  CG2 ILE A  28      62.899  25.358  -7.485  1.00 17.37           C  
ANISOU  258  CG2 ILE A  28     2117   2439   2044    894    241   -515       C  
ATOM    259  CD1 ILE A  28      65.953  26.154  -7.218  1.00 19.84           C  
ANISOU  259  CD1 ILE A  28     2404   2845   2289    329     95   -325       C  
ATOM    260  N  ASER A  29      62.247  24.247 -10.870  0.62 16.99           N  
ANISOU  260  N  ASER A  29     2321   2249   1885    718    -38    -57       N  
ATOM    261  N  BSER A  29      62.246  24.259 -10.867  0.38 18.36           N  
ANISOU  261  N  BSER A  29     2448   2434   2094    664     42   -212       N  
ATOM    262  CA ASER A  29      60.984  24.353 -11.586  0.62 17.96           C  
ANISOU  262  CA ASER A  29     2414   2519   1890    700   -103    -55       C  
ATOM    263  CA BSER A  29      60.986  24.353 -11.603  0.38 19.51           C  
ANISOU  263  CA BSER A  29     2531   2664   2218    705     56   -259       C  
ATOM    264  C  ASER A  29      60.436  22.974 -11.951  0.62 19.31           C  
ANISOU  264  C  ASER A  29     2514   2622   2202    635     55   -179       C  
ATOM    265  C  BSER A  29      60.432  22.974 -11.956  0.38 19.99           C  
ANISOU  265  C  BSER A  29     2593   2686   2318    643    108   -271       C  
ATOM    266  O  ASER A  29      59.246  22.711 -11.786  0.62 19.19           O  
ANISOU  266  O  ASER A  29     2418   2591   2283    421     62   -127       O  
ATOM    267  O  BSER A  29      59.237  22.718 -11.789  0.38 19.87           O  
ANISOU  267  O  BSER A  29     2526   2676   2349    509     87   -249       O  
ATOM    268  CB ASER A  29      61.156  25.207 -12.844  0.62 18.16           C  
ANISOU  268  CB ASER A  29     2429   2718   1753    849   -158    246       C  
ATOM    269  CB BSER A  29      61.170  25.179 -12.881  0.38 20.43           C  
ANISOU  269  CB BSER A  29     2565   2876   2319    889     79   -157       C  
ATOM    270  OG ASER A  29      59.907  25.427 -13.473  0.62 20.00           O  
ANISOU  270  OG ASER A  29     2614   3189   1794    804    -50    435       O  
ATOM    271  OG BSER A  29      61.591  26.495 -12.577  0.38 21.99           O  
ANISOU  271  OG BSER A  29     2696   3159   2499    972    160   -121       O  
ATOM    272  N   ASP A  30      61.309  22.093 -12.433  1.00 20.27           N  
ANISOU  272  N   ASP A  30     2761   2616   2327    680    126   -196       N  
ATOM    273  CA  ASP A  30      60.905  20.748 -12.837  1.00 21.00           C  
ANISOU  273  CA  ASP A  30     2898   2741   2341    536    323   -279       C  
ATOM    274  C   ASP A  30      60.343  19.919 -11.684  1.00 20.25           C  
ANISOU  274  C   ASP A  30     2855   2476   2361    711    473   -326       C  
ATOM    275  O   ASP A  30      59.485  19.059 -11.891  1.00 21.70           O  
ANISOU  275  O   ASP A  30     3160   2514   2571    606    469   -333       O  
ATOM    276  CB  ASP A  30      62.081  19.994 -13.469  1.00 22.36           C  
ANISOU  276  CB  ASP A  30     3169   2949   2376    659    460   -352       C  
ATOM    277  CG  ASP A  30      62.447  20.523 -14.849  1.00 25.25           C  
ANISOU  277  CG  ASP A  30     3586   3413   2594    439    483   -485       C  
ATOM    278  OD1 ASP A  30      61.657  21.303 -15.421  1.00 26.75           O  
ANISOU  278  OD1 ASP A  30     3794   3686   2685    213    372   -549       O  
ATOM    279  OD2 ASP A  30      63.524  20.146 -15.359  1.00 26.64           O  
ANISOU  279  OD2 ASP A  30     3872   3423   2828    361    623   -684       O  
ATOM    280  N   TYR A  31      60.837  20.168 -10.476  1.00 18.35           N  
ANISOU  280  N   TYR A  31     2715   2084   2172    838    546   -245       N  
ATOM    281  CA  TYR A  31      60.326  19.476  -9.295  1.00 18.12           C  
ANISOU  281  CA  TYR A  31     2708   1954   2223    824    407   -175       C  
ATOM    282  C   TYR A  31      58.997  20.076  -8.840  1.00 18.13           C  
ANISOU  282  C   TYR A  31     2675   1986   2228    820    318   -314       C  
ATOM    283  O   TYR A  31      58.050  19.363  -8.527  1.00 20.32           O  
ANISOU  283  O   TYR A  31     2903   2335   2483    625    347   -293       O  
ATOM    284  CB  TYR A  31      61.345  19.534  -8.157  1.00 18.61           C  
ANISOU  284  CB  TYR A  31     2911   1852   2308    743    295     53       C  
ATOM    285  CG  TYR A  31      60.857  18.916  -6.868  1.00 19.73           C  
ANISOU  285  CG  TYR A  31     3296   1851   2350    637    415    134       C  
ATOM    286  CD1 TYR A  31      60.618  17.553  -6.781  1.00 21.33           C  
ANISOU  286  CD1 TYR A  31     3691   1968   2447    513    502    245       C  
ATOM    287  CD2 TYR A  31      60.640  19.692  -5.738  1.00 20.34           C  
ANISOU  287  CD2 TYR A  31     3536   1909   2286    540    327    235       C  
ATOM    288  CE1 TYR A  31      60.173  16.974  -5.599  1.00 23.36           C  
ANISOU  288  CE1 TYR A  31     3964   2285   2628    479    523    120       C  
ATOM    289  CE2 TYR A  31      60.195  19.124  -4.554  1.00 22.30           C  
ANISOU  289  CE2 TYR A  31     3765   2223   2484    375    295    164       C  
ATOM    290  CZ  TYR A  31      59.963  17.766  -4.494  1.00 23.56           C  
ANISOU  290  CZ  TYR A  31     3990   2381   2580    413    452    232       C  
ATOM    291  OH  TYR A  31      59.525  17.200  -3.320  1.00 24.81           O  
ANISOU  291  OH  TYR A  31     4171   2509   2747    146    643    284       O  
ATOM    292  N   PHE A  32      58.934  21.401  -8.844  1.00 16.88           N  
ANISOU  292  N   PHE A  32     2538   1727   2148    593     82   -416       N  
ATOM    293  CA  PHE A  32      57.826  22.123  -8.220  1.00 16.02           C  
ANISOU  293  CA  PHE A  32     2253   1752   2083    391     53   -407       C  
ATOM    294  C   PHE A  32      56.586  22.259  -9.110  1.00 16.96           C  
ANISOU  294  C   PHE A  32     2388   1893   2162    215     80   -241       C  
ATOM    295  O   PHE A  32      55.471  22.048  -8.645  1.00 17.11           O  
ANISOU  295  O   PHE A  32     2177   1879   2445    396    -48   -148       O  
ATOM    296  CB  PHE A  32      58.325  23.503  -7.784  1.00 15.47           C  
ANISOU  296  CB  PHE A  32     2154   1588   2135    348    100   -445       C  
ATOM    297  CG  PHE A  32      57.290  24.365  -7.105  1.00 14.29           C  
ANISOU  297  CG  PHE A  32     2019   1449   1962    152    110   -308       C  
ATOM    298  CD1 PHE A  32      56.498  23.871  -6.080  1.00 15.09           C  
ANISOU  298  CD1 PHE A  32     2144   1475   2115    262    -72   -135       C  
ATOM    299  CD2 PHE A  32      57.154  25.699  -7.472  1.00 15.33           C  
ANISOU  299  CD2 PHE A  32     2256   1582   1987    155    156   -242       C  
ATOM    300  CE1 PHE A  32      55.570  24.687  -5.445  1.00 15.61           C  
ANISOU  300  CE1 PHE A  32     2247   1558   2128    158     79    -96       C  
ATOM    301  CE2 PHE A  32      56.233  26.521  -6.844  1.00 15.01           C  
ANISOU  301  CE2 PHE A  32     2369   1420   1915     20     15   -265       C  
ATOM    302  CZ  PHE A  32      55.438  26.021  -5.838  1.00 15.64           C  
ANISOU  302  CZ  PHE A  32     2428   1512   2002    -12    159   -160       C  
ATOM    303  N   VAL A  33      56.775  22.603 -10.382  1.00 17.28           N  
ANISOU  303  N   VAL A  33     2420   1980   2165    341   -206   -308       N  
ATOM    304  CA  VAL A  33      55.637  22.824 -11.272  1.00 19.07           C  
ANISOU  304  CA  VAL A  33     2523   2405   2318     65   -181   -430       C  
ATOM    305  C   VAL A  33      54.630  21.665 -11.260  1.00 19.27           C  
ANISOU  305  C   VAL A  33     2413   2382   2526     57   -206   -670       C  
ATOM    306  O   VAL A  33      53.433  21.907 -11.102  1.00 19.38           O  
ANISOU  306  O   VAL A  33     2478   2271   2613    149   -407   -683       O  
ATOM    307  CB  VAL A  33      56.092  23.096 -12.725  1.00 19.62           C  
ANISOU  307  CB  VAL A  33     2605   2469   2382    -77   -371   -245       C  
ATOM    308  CG1 VAL A  33      54.907  23.019 -13.679  1.00 20.87           C  
ANISOU  308  CG1 VAL A  33     2740   2656   2534     17   -335   -459       C  
ATOM    309  CG2 VAL A  33      56.767  24.460 -12.822  1.00 19.62           C  
ANISOU  309  CG2 VAL A  33     2585   2462   2406    -89   -257    -93       C  
ATOM    310  N   PRO A  34      55.098  20.406 -11.393  1.00 19.88           N  
ANISOU  310  N   PRO A  34     2470   2307   2775    111   -157   -617       N  
ATOM    311  CA  PRO A  34      54.096  19.333 -11.414  1.00 21.20           C  
ANISOU  311  CA  PRO A  34     2655   2352   3048     94   -148   -706       C  
ATOM    312  C   PRO A  34      53.366  19.136 -10.087  1.00 21.07           C  
ANISOU  312  C   PRO A  34     2432   2454   3122   -162   -167   -618       C  
ATOM    313  O   PRO A  34      52.378  18.406 -10.045  1.00 23.46           O  
ANISOU  313  O   PRO A  34     2762   2813   3340   -340   -214   -516       O  
ATOM    314  CB  PRO A  34      54.921  18.081 -11.752  1.00 22.72           C  
ANISOU  314  CB  PRO A  34     2892   2455   3287    235     15   -825       C  
ATOM    315  CG  PRO A  34      56.190  18.578 -12.321  1.00 23.81           C  
ANISOU  315  CG  PRO A  34     3038   2726   3284    430    168   -785       C  
ATOM    316  CD  PRO A  34      56.455  19.877 -11.617  1.00 21.22           C  
ANISOU  316  CD  PRO A  34     2689   2398   2974    352     61   -794       C  
ATOM    317  N   LEU A  35      53.841  19.779  -9.022  1.00 19.47           N  
ANISOU  317  N   LEU A  35     2162   2320   2916    201    -20   -426       N  
ATOM    318  CA  LEU A  35      53.228  19.626  -7.709  1.00 18.16           C  
ANISOU  318  CA  LEU A  35     2012   2073   2816    285   -159   -312       C  
ATOM    319  C   LEU A  35      52.125  20.651  -7.467  1.00 17.29           C  
ANISOU  319  C   LEU A  35     2011   1836   2721    132    -86   -276       C  
ATOM    320  O   LEU A  35      51.270  20.450  -6.602  1.00 17.44           O  
ANISOU  320  O   LEU A  35     2060   1850   2718    246     12   -169       O  
ATOM    321  CB  LEU A  35      54.282  19.753  -6.605  1.00 18.89           C  
ANISOU  321  CB  LEU A  35     2122   2156   2898    400    -24    -78       C  
ATOM    322  CG  LEU A  35      55.473  18.797  -6.657  1.00 18.49           C  
ANISOU  322  CG  LEU A  35     1953   2141   2930    362   -135   -138       C  
ATOM    323  CD1 LEU A  35      56.386  19.035  -5.453  1.00 19.26           C  
ANISOU  323  CD1 LEU A  35     1899   2524   2894    269   -257   -207       C  
ATOM    324  CD2 LEU A  35      55.000  17.349  -6.698  1.00 19.08           C  
ANISOU  324  CD2 LEU A  35     2150   2092   3009    258    -34    -43       C  
ATOM    325  N   VAL A  36      52.168  21.753  -8.214  1.00 16.04           N  
ANISOU  325  N   VAL A  36     1948   1757   2390    274   -152   -409       N  
ATOM    326  CA  VAL A  36      51.300  22.903  -7.947  1.00 15.31           C  
ANISOU  326  CA  VAL A  36     1899   1642   2276    283   -232   -212       C  
ATOM    327  C   VAL A  36      49.823  22.534  -8.076  1.00 16.68           C  
ANISOU  327  C   VAL A  36     2018   1985   2334    161   -313   -367       C  
ATOM    328  O   VAL A  36      48.989  22.966  -7.279  1.00 17.04           O  
ANISOU  328  O   VAL A  36     2036   2051   2388    155   -227   -224       O  
ATOM    329  CB  VAL A  36      51.634  24.078  -8.892  1.00 14.19           C  
ANISOU  329  CB  VAL A  36     1539   1536   2318    386   -190    -95       C  
ATOM    330  CG1 VAL A  36      50.626  25.216  -8.744  1.00 14.04           C  
ANISOU  330  CG1 VAL A  36     1511   1487   2336    388   -267   -276       C  
ATOM    331  CG2 VAL A  36      53.042  24.585  -8.624  1.00 15.19           C  
ANISOU  331  CG2 VAL A  36     1562   1953   2257    422   -283   -395       C  
ATOM    332  N   ASN A  37      49.512  21.706  -9.069  1.00 17.93           N  
ANISOU  332  N   ASN A  37     2155   2206   2450    -40   -641   -599       N  
ATOM    333  CA  ASN A  37      48.138  21.289  -9.314  1.00 19.37           C  
ANISOU  333  CA  ASN A  37     2463   2345   2551     71   -554   -393       C  
ATOM    334  C   ASN A  37      47.961  19.783  -9.195  1.00 18.60           C  
ANISOU  334  C   ASN A  37     2378   2112   2579     82   -644   -535       C  
ATOM    335  O   ASN A  37      46.988  19.233  -9.708  1.00 20.59           O  
ANISOU  335  O   ASN A  37     2669   2360   2793   -179   -831   -305       O  
ATOM    336  CB  ASN A  37      47.682  21.749 -10.702  1.00 19.57           C  
ANISOU  336  CB  ASN A  37     2569   2301   2566     13   -458   -274       C  
ATOM    337  CG  ASN A  37      47.803  23.252 -10.891  1.00 20.03           C  
ANISOU  337  CG  ASN A  37     2656   2259   2696    113   -297   -306       C  
ATOM    338  OD1 ASN A  37      47.048  24.023 -10.301  1.00 19.85           O  
ANISOU  338  OD1 ASN A  37     2528   2268   2748    342   -443   -295       O  
ATOM    339  ND2 ASN A  37      48.747  23.671 -11.723  1.00 21.36           N  
ANISOU  339  ND2 ASN A  37     2887   2503   2727    189   -264   -433       N  
ATOM    340  N   LYS A  38      48.893  19.120  -8.511  1.00 18.75           N  
ANISOU  340  N   LYS A  38     2459   1959   2705    304   -450   -555       N  
ATOM    341  CA  LYS A  38      48.873  17.662  -8.410  1.00 20.21           C  
ANISOU  341  CA  LYS A  38     2493   2103   3083    160   -478   -650       C  
ATOM    342  C   LYS A  38      47.709  17.204  -7.556  1.00 21.17           C  
ANISOU  342  C   LYS A  38     2601   2233   3208    -82   -662   -630       C  
ATOM    343  O   LYS A  38      47.542  17.665  -6.429  1.00 21.12           O  
ANISOU  343  O   LYS A  38     2621   2352   3050     26   -484   -547       O  
ATOM    344  CB  LYS A  38      50.186  17.132  -7.825  1.00 21.04           C  
ANISOU  344  CB  LYS A  38     2604   2067   3325    244   -584   -780       C  
ATOM    345  CG  LYS A  38      50.303  15.610  -7.830  1.00 24.35           C  
ANISOU  345  CG  LYS A  38     2897   2534   3820    254   -618   -896       C  
ATOM    346  CD  LYS A  38      51.655  15.170  -7.289  1.00 25.76           C  
ANISOU  346  CD  LYS A  38     2969   2665   4156    436   -605   -897       C  
ATOM    347  CE  LYS A  38      51.863  13.675  -7.434  1.00 28.51           C  
ANISOU  347  CE  LYS A  38     3171   3232   4429    487   -543   -762       C  
ATOM    348  NZ  LYS A  38      53.270  13.312  -7.111  1.00 30.58           N  
ANISOU  348  NZ  LYS A  38     3412   3576   4629    416   -645   -575       N  
ATOM    349  N   PRO A  39      46.884  16.297  -8.093  1.00 22.54           N  
ANISOU  349  N   PRO A  39     2638   2568   3359   -323   -918   -661       N  
ATOM    350  CA  PRO A  39      45.768  15.784  -7.293  1.00 22.52           C  
ANISOU  350  CA  PRO A  39     2827   2344   3386   -738   -969   -434       C  
ATOM    351  C   PRO A  39      46.199  15.178  -5.952  1.00 24.94           C  
ANISOU  351  C   PRO A  39     3245   2591   3640   -706  -1005   -268       C  
ATOM    352  O   PRO A  39      47.241  14.514  -5.875  1.00 26.38           O  
ANISOU  352  O   PRO A  39     3383   2791   3848   -890   -862   -388       O  
ATOM    353  CB  PRO A  39      45.157  14.718  -8.208  1.00 24.00           C  
ANISOU  353  CB  PRO A  39     2952   2652   3516   -740   -928   -381       C  
ATOM    354  CG  PRO A  39      45.438  15.232  -9.585  1.00 24.14           C  
ANISOU  354  CG  PRO A  39     2885   2789   3497   -626  -1000   -546       C  
ATOM    355  CD  PRO A  39      46.807  15.860  -9.500  1.00 22.13           C  
ANISOU  355  CD  PRO A  39     2589   2419   3402   -612  -1016   -586       C  
ATOM    356  N  ALYS A  40      45.387  15.422  -4.919  0.53 25.34           N  
ANISOU  356  N  ALYS A  40     3430   2582   3614   -673   -934   -104       N  
ATOM    357  N  BLYS A  40      45.398  15.434  -4.920  0.47 25.03           N  
ANISOU  357  N  BLYS A  40     3381   2542   3589   -677   -866   -179       N  
ATOM    358  CA ALYS A  40      45.574  14.893  -3.557  0.53 26.36           C  
ANISOU  358  CA ALYS A  40     3657   2667   3691   -693   -908    -40       C  
ATOM    359  CA BLYS A  40      45.578  14.875  -3.578  0.47 25.64           C  
ANISOU  359  CA BLYS A  40     3543   2560   3638   -704   -782   -181       C  
ATOM    360  C  ALYS A  40      46.800  15.441  -2.831  0.53 25.01           C  
ANISOU  360  C  ALYS A  40     3513   2491   3500   -781   -835     14       C  
ATOM    361  C  BLYS A  40      46.833  15.392  -2.870  0.47 24.52           C  
ANISOU  361  C  BLYS A  40     3444   2400   3471   -800   -793    -66       C  
ATOM    362  O  ALYS A  40      47.136  14.977  -1.739  0.53 26.90           O  
ANISOU  362  O  ALYS A  40     3709   2863   3651  -1035   -879    118       O  
ATOM    363  O  BLYS A  40      47.216  14.865  -1.827  0.47 26.13           O  
ANISOU  363  O  BLYS A  40     3622   2685   3622  -1045   -880     32       O  
ATOM    364  CB ALYS A  40      45.661  13.365  -3.574  0.53 28.47           C  
ANISOU  364  CB ALYS A  40     3883   2981   3955   -684   -907   -124       C  
ATOM    365  CB BLYS A  40      45.612  13.337  -3.622  0.47 27.08           C  
ANISOU  365  CB BLYS A  40     3652   2783   3854   -698   -644   -371       C  
ATOM    366  CG ALYS A  40      44.501  12.667  -4.249  0.53 30.09           C  
ANISOU  366  CG ALYS A  40     4088   3250   4095   -657   -853   -118       C  
ATOM    367  CG BLYS A  40      44.569  12.678  -4.524  0.47 28.19           C  
ANISOU  367  CG BLYS A  40     3750   2993   3968   -659   -425   -482       C  
ATOM    368  CD ALYS A  40      44.904  11.247  -4.603  0.53 31.12           C  
ANISOU  368  CD ALYS A  40     4251   3424   4150   -645   -772   -126       C  
ATOM    369  CD BLYS A  40      43.169  13.237  -4.309  0.47 29.01           C  
ANISOU  369  CD BLYS A  40     3830   3158   4032   -686   -215   -570       C  
ATOM    370  CE ALYS A  40      43.723  10.430  -5.082  0.53 31.81           C  
ANISOU  370  CE ALYS A  40     4356   3526   4203   -654   -688   -145       C  
ATOM    371  CE BLYS A  40      42.623  12.913  -2.932  0.47 29.83           C  
ANISOU  371  CE BLYS A  40     3952   3319   4062   -587    -88   -683       C  
ATOM    372  NZ ALYS A  40      43.806  10.076  -6.530  0.53 32.09           N  
ANISOU  372  NZ ALYS A  40     4430   3562   4199   -579   -687   -183       N  
ATOM    373  NZ BLYS A  40      41.255  13.473  -2.770  0.47 30.47           N  
ANISOU  373  NZ BLYS A  40     4030   3453   4096   -518    -14   -647       N  
ATOM    374  N   LEU A  41      47.472  16.414  -3.429  1.00 21.41           N  
ANISOU  374  N   LEU A  41     3063   1857   3215   -560   -652   -277       N  
ATOM    375  CA  LEU A  41      48.636  17.007  -2.782  1.00 18.34           C  
ANISOU  375  CA  LEU A  41     2443   1658   2867     54   -585   -367       C  
ATOM    376  C   LEU A  41      48.302  18.409  -2.311  1.00 16.92           C  
ANISOU  376  C   LEU A  41     2439   1453   2536   -148   -736   -430       C  
ATOM    377  O   LEU A  41      48.076  19.295  -3.129  1.00 17.67           O  
ANISOU  377  O   LEU A  41     2813   1435   2465    107   -785     31       O  
ATOM    378  CB  LEU A  41      49.838  17.036  -3.725  1.00 18.72           C  
ANISOU  378  CB  LEU A  41     2312   1783   3018    253   -522   -461       C  
ATOM    379  CG  LEU A  41      51.102  17.665  -3.124  1.00 18.81           C  
ANISOU  379  CG  LEU A  41     2239   1869   3040    425   -370   -296       C  
ATOM    380  CD1 LEU A  41      51.598  16.878  -1.910  1.00 19.50           C  
ANISOU  380  CD1 LEU A  41     2240   2079   3089    732   -430   -268       C  
ATOM    381  CD2 LEU A  41      52.190  17.788  -4.172  1.00 18.16           C  
ANISOU  381  CD2 LEU A  41     2173   1798   2928    592   -112   -457       C  
ATOM    382  N   LYS A  42      48.244  18.599  -0.999  1.00 16.89           N  
ANISOU  382  N   LYS A  42     2470   1483   2464   -146   -425   -457       N  
ATOM    383  CA  LYS A  42      48.036  19.939  -0.445  1.00 15.26           C  
ANISOU  383  CA  LYS A  42     2293   1175   2329     83   -194   -203       C  
ATOM    384  C   LYS A  42      49.178  20.838  -0.867  1.00 14.27           C  
ANISOU  384  C   LYS A  42     2180   1083   2160    289   -174   -222       C  
ATOM    385  O   LYS A  42      50.334  20.444  -0.844  1.00 16.15           O  
ANISOU  385  O   LYS A  42     2414   1420   2304    130   -161   -227       O  
ATOM    386  CB  LYS A  42      47.934  19.892   1.077  1.00 16.38           C  
ANISOU  386  CB  LYS A  42     2246   1399   2577    -96    196   -245       C  
ATOM    387  CG  LYS A  42      46.720  19.117   1.596  1.00 17.93           C  
ANISOU  387  CG  LYS A  42     2219   1689   2904   -400     50   -203       C  
ATOM    388  CD  LYS A  42      46.654  19.109   3.116  1.00 21.09           C  
ANISOU  388  CD  LYS A  42     2680   2170   3164   -419    -97     18       C  
ATOM    389  CE  LYS A  42      47.689  18.181   3.722  1.00 24.30           C  
ANISOU  389  CE  LYS A  42     3300   2468   3465   -589   -322   -121       C  
ATOM    390  NZ  LYS A  42      47.440  16.769   3.310  1.00 26.26           N  
ANISOU  390  NZ  LYS A  42     3645   2549   3784   -804   -323     39       N  
ATOM    391  N   SER A  43      48.864  22.068  -1.246  1.00 13.34           N  
ANISOU  391  N   SER A  43     1935    946   2188     98    -35     -8       N  
ATOM    392  CA  SER A  43      49.923  22.943  -1.708  1.00 13.46           C  
ANISOU  392  CA  SER A  43     1954   1029   2131    -35   -208    215       C  
ATOM    393  C   SER A  43      50.880  23.340  -0.590  1.00 13.60           C  
ANISOU  393  C   SER A  43     1907   1323   1938    139     76     37       C  
ATOM    394  O   SER A  43      52.021  23.703  -0.867  1.00 14.47           O  
ANISOU  394  O   SER A  43     2065   1413   2018     74     73    -62       O  
ATOM    395  CB  SER A  43      49.339  24.185  -2.363  1.00 14.30           C  
ANISOU  395  CB  SER A  43     2002   1294   2138   -199   -467    270       C  
ATOM    396  OG  SER A  43      48.852  23.845  -3.639  1.00 16.81           O  
ANISOU  396  OG  SER A  43     2334   1597   2457     77   -678     81       O  
ATOM    397  N   ARG A  44      50.446  23.269   0.666  1.00 13.31           N  
ANISOU  397  N   ARG A  44     1782   1388   1888    123    -30    125       N  
ATOM    398  CA  ARG A  44      51.378  23.558   1.751  1.00 13.34           C  
ANISOU  398  CA  ARG A  44     1670   1530   1867    -37     -2     88       C  
ATOM    399  C   ARG A  44      52.523  22.547   1.708  1.00 13.60           C  
ANISOU  399  C   ARG A  44     1713   1606   1848    102   -127     26       C  
ATOM    400  O   ARG A  44      53.671  22.880   2.004  1.00 14.51           O  
ANISOU  400  O   ARG A  44     1739   1804   1970     30    -44    -23       O  
ATOM    401  CB  ARG A  44      50.688  23.552   3.128  1.00 12.79           C  
ANISOU  401  CB  ARG A  44     1532   1435   1893   -155    251    228       C  
ATOM    402  CG  ARG A  44      50.224  22.196   3.636  1.00 13.75           C  
ANISOU  402  CG  ARG A  44     1784   1510   1928   -379    396    274       C  
ATOM    403  CD  ARG A  44      49.614  22.345   5.009  1.00 15.56           C  
ANISOU  403  CD  ARG A  44     2144   1710   2059   -580    578    366       C  
ATOM    404  NE  ARG A  44      49.295  21.055   5.621  1.00 17.58           N  
ANISOU  404  NE  ARG A  44     2458   2073   2147   -652    175    281       N  
ATOM    405  CZ  ARG A  44      48.262  20.864   6.433  1.00 18.24           C  
ANISOU  405  CZ  ARG A  44     2647   2140   2143   -859     86    226       C  
ATOM    406  NH1 ARG A  44      47.441  21.866   6.711  1.00 17.93           N  
ANISOU  406  NH1 ARG A  44     2680   2230   1901   -764    -56    130       N  
ATOM    407  NH2 ARG A  44      48.039  19.662   6.952  1.00 18.87           N  
ANISOU  407  NH2 ARG A  44     2707   2200   2262  -1050   -197     87       N  
ATOM    408  N   ASP A  45      52.208  21.328   1.284  1.00 13.39           N  
ANISOU  408  N   ASP A  45     1832   1339   1917     27      8   -109       N  
ATOM    409  CA  ASP A  45      53.223  20.290   1.126  1.00 14.80           C  
ANISOU  409  CA  ASP A  45     1951   1430   2241    129   -114    -86       C  
ATOM    410  C   ASP A  45      54.054  20.472  -0.141  1.00 15.25           C  
ANISOU  410  C   ASP A  45     2022   1529   2242    277   -128     74       C  
ATOM    411  O   ASP A  45      55.276  20.294  -0.127  1.00 17.14           O  
ANISOU  411  O   ASP A  45     2392   1732   2389    542   -168    -35       O  
ATOM    412  CB  ASP A  45      52.568  18.904   1.131  1.00 15.69           C  
ANISOU  412  CB  ASP A  45     1891   1570   2498   -167    -78    161       C  
ATOM    413  CG  ASP A  45      52.033  18.531   2.484  1.00 17.80           C  
ANISOU  413  CG  ASP A  45     2129   1873   2761   -104   -242    160       C  
ATOM    414  OD1 ASP A  45      52.692  18.871   3.490  1.00 18.57           O  
ANISOU  414  OD1 ASP A  45     2286   1970   2798   -298   -221     63       O  
ATOM    415  OD2 ASP A  45      50.955  17.905   2.548  1.00 19.46           O  
ANISOU  415  OD2 ASP A  45     2073   2338   2981   -111   -412    282       O  
ATOM    416  N   ALA A  46      53.400  20.842  -1.239  1.00 14.72           N  
ANISOU  416  N   ALA A  46     1906   1472   2214    210    -64    -50       N  
ATOM    417  CA  ALA A  46      54.109  21.148  -2.474  1.00 14.36           C  
ANISOU  417  CA  ALA A  46     1798   1590   2069    170   -324   -217       C  
ATOM    418  C   ALA A  46      55.131  22.272  -2.275  1.00 14.07           C  
ANISOU  418  C   ALA A  46     1671   1561   2114    216   -234   -235       C  
ATOM    419  O   ALA A  46      56.297  22.135  -2.630  1.00 15.05           O  
ANISOU  419  O   ALA A  46     1868   1682   2168    335   -126   -301       O  
ATOM    420  CB  ALA A  46      53.117  21.517  -3.565  1.00 14.22           C  
ANISOU  420  CB  ALA A  46     1708   1854   1839    359   -432   -213       C  
ATOM    421  N   ILE A  47      54.690  23.389  -1.709  1.00 13.35           N  
ANISOU  421  N   ILE A  47     1902   1330   1839    100   -295    -43       N  
ATOM    422  CA  ILE A  47      55.568  24.535  -1.526  1.00 13.10           C  
ANISOU  422  CA  ILE A  47     1741   1430   1805    223   -248      3       C  
ATOM    423  C   ILE A  47      56.628  24.247  -0.466  1.00 12.59           C  
ANISOU  423  C   ILE A  47     1664   1357   1764    209    -30    131       C  
ATOM    424  O   ILE A  47      57.807  24.555  -0.649  1.00 13.68           O  
ANISOU  424  O   ILE A  47     1628   1667   1901    129    139    171       O  
ATOM    425  CB  ILE A  47      54.754  25.782  -1.140  1.00 12.38           C  
ANISOU  425  CB  ILE A  47     1713   1303   1689    204   -213    -59       C  
ATOM    426  CG1 ILE A  47      53.748  26.139  -2.236  1.00 12.29           C  
ANISOU  426  CG1 ILE A  47     1560   1335   1776    395   -167    -44       C  
ATOM    427  CG2 ILE A  47      55.666  26.976  -0.853  1.00 12.56           C  
ANISOU  427  CG2 ILE A  47     1687   1346   1740      1   -481     43       C  
ATOM    428  CD1 ILE A  47      52.625  27.017  -1.727  1.00 12.60           C  
ANISOU  428  CD1 ILE A  47     1588   1399   1798    175    -76    -55       C  
ATOM    429  N   GLY A  48      56.202  23.624   0.633  1.00 12.33           N  
ANISOU  429  N   GLY A  48     1708   1411   1566    426     40    174       N  
ATOM    430  CA  GLY A  48      57.102  23.309   1.727  1.00 13.28           C  
ANISOU  430  CA  GLY A  48     1656   1518   1872    440   -147     83       C  
ATOM    431  C   GLY A  48      58.228  22.401   1.284  1.00 14.10           C  
ANISOU  431  C   GLY A  48     1640   1653   2064    276      4    -37       C  
ATOM    432  O   GLY A  48      59.405  22.684   1.541  1.00 14.65           O  
ANISOU  432  O   GLY A  48     1642   1835   2088    149    215   -217       O  
ATOM    433  N   GLN A  49      57.874  21.314   0.606  1.00 15.65           N  
ANISOU  433  N   GLN A  49     2028   1677   2240    478    -51      8       N  
ATOM    434  CA  GLN A  49      58.885  20.364   0.150  1.00 16.39           C  
ANISOU  434  CA  GLN A  49     2097   1711   2418    555   -153    -36       C  
ATOM    435  C   GLN A  49      59.734  20.965  -0.963  1.00 15.89           C  
ANISOU  435  C   GLN A  49     2101   1779   2159    657   -334     34       C  
ATOM    436  O   GLN A  49      60.944  20.751  -1.002  1.00 17.20           O  
ANISOU  436  O   GLN A  49     2174   2227   2135    390   -279     30       O  
ATOM    437  CB  GLN A  49      58.242  19.045  -0.306  1.00 18.81           C  
ANISOU  437  CB  GLN A  49     2441   2042   2664    400   -174   -120       C  
ATOM    438  CG  GLN A  49      57.564  18.245   0.812  1.00 21.00           C  
ANISOU  438  CG  GLN A  49     2788   2321   2870    315   -289    105       C  
ATOM    439  CD  GLN A  49      58.470  17.973   2.016  1.00 24.68           C  
ANISOU  439  CD  GLN A  49     3208   2866   3304    284    -82     50       C  
ATOM    440  OE1 GLN A  49      59.685  17.815   1.881  1.00 27.07           O  
ANISOU  440  OE1 GLN A  49     3565   3176   3545    281   -136    195       O  
ATOM    441  NE2 GLN A  49      57.872  17.923   3.203  1.00 24.96           N  
ANISOU  441  NE2 GLN A  49     3206   2905   3371    257     32    -69       N  
ATOM    442  N   ALA A  50      59.124  21.753  -1.854  1.00 15.36           N  
ANISOU  442  N   ALA A  50     2144   1698   1993    521   -170    -15       N  
ATOM    443  CA  ALA A  50      59.902  22.414  -2.889  1.00 15.48           C  
ANISOU  443  CA  ALA A  50     2333   1693   1857    589   -285     85       C  
ATOM    444  C   ALA A  50      60.919  23.394  -2.300  1.00 15.64           C  
ANISOU  444  C   ALA A  50     2051   2009   1882    401    -85   -133       C  
ATOM    445  O   ALA A  50      62.011  23.578  -2.842  1.00 16.37           O  
ANISOU  445  O   ALA A  50     2056   2121   2043    323     13   -279       O  
ATOM    446  CB  ALA A  50      58.988  23.125  -3.861  1.00 16.47           C  
ANISOU  446  CB  ALA A  50     2696   1641   1921    747   -470    304       C  
ATOM    447  N   PHE A  51      60.571  24.029  -1.188  1.00 14.15           N  
ANISOU  447  N   PHE A  51     1949   1628   1800    535      4   -113       N  
ATOM    448  CA  PHE A  51      61.504  24.951  -0.562  1.00 13.51           C  
ANISOU  448  CA  PHE A  51     1790   1494   1847    392     57   -207       C  
ATOM    449  C   PHE A  51      62.706  24.216   0.022  1.00 13.12           C  
ANISOU  449  C   PHE A  51     1811   1379   1795    298    159     26       C  
ATOM    450  O   PHE A  51      63.847  24.664  -0.106  1.00 14.64           O  
ANISOU  450  O   PHE A  51     1801   1928   1832    274    221    -57       O  
ATOM    451  CB  PHE A  51      60.802  25.774   0.525  1.00 13.08           C  
ANISOU  451  CB  PHE A  51     1714   1389   1868    289    153   -373       C  
ATOM    452  CG  PHE A  51      61.685  26.812   1.165  1.00 12.12           C  
ANISOU  452  CG  PHE A  51     1411   1435   1759    -96     39     47       C  
ATOM    453  CD1 PHE A  51      62.307  27.784   0.390  1.00 13.61           C  
ANISOU  453  CD1 PHE A  51     1442   1755   1973     28     28    -37       C  
ATOM    454  CD2 PHE A  51      61.874  26.837   2.541  1.00 13.27           C  
ANISOU  454  CD2 PHE A  51     1488   1657   1895    -46   -140    102       C  
ATOM    455  CE1 PHE A  51      63.115  28.751   0.977  1.00 13.36           C  
ANISOU  455  CE1 PHE A  51     1154   1883   2040     33    119    -11       C  
ATOM    456  CE2 PHE A  51      62.678  27.797   3.136  1.00 13.15           C  
ANISOU  456  CE2 PHE A  51     1344   1804   1848    -92   -105     23       C  
ATOM    457  CZ  PHE A  51      63.296  28.762   2.353  1.00 12.44           C  
ANISOU  457  CZ  PHE A  51     1145   1758   1826     -9     93    -62       C  
ATOM    458  N   VAL A  52      62.448  23.089   0.675  1.00 14.40           N  
ANISOU  458  N   VAL A  52     1881   1676   1915    519    121    207       N  
ATOM    459  CA  VAL A  52      63.526  22.278   1.229  1.00 15.54           C  
ANISOU  459  CA  VAL A  52     1951   1806   2146    648    253    155       C  
ATOM    460  C   VAL A  52      64.428  21.777   0.099  1.00 16.64           C  
ANISOU  460  C   VAL A  52     1978   2142   2203    589    239    -33       C  
ATOM    461  O   VAL A  52      65.658  21.804   0.207  1.00 19.57           O  
ANISOU  461  O   VAL A  52     2274   2791   2370    635     46   -258       O  
ATOM    462  CB  VAL A  52      62.968  21.099   2.030  1.00 15.50           C  
ANISOU  462  CB  VAL A  52     1817   1974   2099    494    370    170       C  
ATOM    463  CG1 VAL A  52      64.081  20.152   2.457  1.00 17.00           C  
ANISOU  463  CG1 VAL A  52     1813   2382   2266    397    127    348       C  
ATOM    464  CG2 VAL A  52      62.218  21.603   3.254  1.00 15.42           C  
ANISOU  464  CG2 VAL A  52     1826   1926   2105    408    410    -83       C  
ATOM    465  N   MET A  53      63.802  21.357  -0.994  1.00 16.80           N  
ANISOU  465  N   MET A  53     2159   1968   2254    535    158     32       N  
ATOM    466  CA  MET A  53      64.533  20.937  -2.181  1.00 16.53           C  
ANISOU  466  CA  MET A  53     2195   1923   2162    551    118   -130       C  
ATOM    467  C   MET A  53      65.337  22.091  -2.776  1.00 16.52           C  
ANISOU  467  C   MET A  53     2035   2160   2081    644    180     85       C  
ATOM    468  O   MET A  53      66.526  21.946  -3.064  1.00 17.51           O  
ANISOU  468  O   MET A  53     2309   2328   2017    516    242    -80       O  
ATOM    469  CB  MET A  53      63.565  20.358  -3.221  1.00 17.71           C  
ANISOU  469  CB  MET A  53     2441   2082   2205    653     23   -156       C  
ATOM    470  CG  MET A  53      64.223  19.858  -4.506  1.00 17.44           C  
ANISOU  470  CG  MET A  53     2393   2046   2187    953    -83     63       C  
ATOM    471  SD  MET A  53      64.262  21.145  -5.764  1.00 19.77           S  
ANISOU  471  SD  MET A  53     2782   2433   2295    908      4   -184       S  
ATOM    472  CE  MET A  53      64.860  20.189  -7.165  1.00 21.14           C  
ANISOU  472  CE  MET A  53     2988   2659   2385    710    164   -493       C  
ATOM    473  N   ALA A  54      64.696  23.245  -2.949  1.00 15.88           N  
ANISOU  473  N   ALA A  54     2031   1925   2078    648    397     68       N  
ATOM    474  CA  ALA A  54      65.360  24.370  -3.611  1.00 15.88           C  
ANISOU  474  CA  ALA A  54     1949   2174   1911    664    133    184       C  
ATOM    475  C   ALA A  54      66.571  24.873  -2.837  1.00 15.88           C  
ANISOU  475  C   ALA A  54     1834   2358   1841    673    180    -44       C  
ATOM    476  O   ALA A  54      67.572  25.268  -3.433  1.00 16.87           O  
ANISOU  476  O   ALA A  54     1782   2511   2115    747    -82     -7       O  
ATOM    477  CB  ALA A  54      64.373  25.522  -3.838  1.00 16.27           C  
ANISOU  477  CB  ALA A  54     2069   2194   1919    985    134    128       C  
ATOM    478  N   THR A  55      66.472  24.883  -1.508  1.00 15.68           N  
ANISOU  478  N   THR A  55     1885   2346   1728    813     19   -225       N  
ATOM    479  CA  THR A  55      67.582  25.348  -0.694  1.00 16.63           C  
ANISOU  479  CA  THR A  55     1849   2573   1896    764     87   -273       C  
ATOM    480  C   THR A  55      68.723  24.342  -0.664  1.00 18.07           C  
ANISOU  480  C   THR A  55     2235   2595   2038    712     34   -246       C  
ATOM    481  O   THR A  55      69.861  24.702  -0.372  1.00 19.96           O  
ANISOU  481  O   THR A  55     2295   2813   2478    524     83    -77       O  
ATOM    482  CB  THR A  55      67.141  25.655   0.750  1.00 17.39           C  
ANISOU  482  CB  THR A  55     1886   2710   2011    733    262    -43       C  
ATOM    483  OG1 THR A  55      66.420  24.540   1.284  1.00 18.17           O  
ANISOU  483  OG1 THR A  55     1890   2823   2193    412    342    185       O  
ATOM    484  CG2 THR A  55      66.250  26.888   0.767  1.00 17.83           C  
ANISOU  484  CG2 THR A  55     2007   2789   1979    764    296   -128       C  
ATOM    485  N   GLU A  56      68.423  23.087  -0.972  1.00 19.14           N  
ANISOU  485  N   GLU A  56     2404   2703   2165   1062    139   -108       N  
ATOM    486  CA  GLU A  56      69.479  22.093  -1.065  1.00 21.21           C  
ANISOU  486  CA  GLU A  56     2230   3232   2598   1293    -25    -73       C  
ATOM    487  C   GLU A  56      70.129  22.136  -2.450  1.00 19.33           C  
ANISOU  487  C   GLU A  56     1824   2846   2675   1304    -26     10       C  
ATOM    488  O   GLU A  56      71.334  21.935  -2.574  1.00 21.42           O  
ANISOU  488  O   GLU A  56     1786   3232   3122   1306     51      2       O  
ATOM    489  CB  GLU A  56      68.930  20.707  -0.732  1.00 24.76           C  
ANISOU  489  CB  GLU A  56     2861   3654   2892   1257     81   -152       C  
ATOM    490  CG  GLU A  56      68.657  20.550   0.769  1.00 30.03           C  
ANISOU  490  CG  GLU A  56     3662   4286   3463    963    212   -327       C  
ATOM    491  CD  GLU A  56      68.019  19.228   1.137  1.00 35.91           C  
ANISOU  491  CD  GLU A  56     4650   4981   4012    558    103   -467       C  
ATOM    492  OE1 GLU A  56      67.825  18.384   0.239  1.00 39.34           O  
ANISOU  492  OE1 GLU A  56     5163   5434   4352    252    103   -456       O  
ATOM    493  OE2 GLU A  56      67.714  19.032   2.332  1.00 37.72           O  
ANISOU  493  OE2 GLU A  56     5001   5174   4157    426     -6   -456       O  
ATOM    494  N   VAL A  57      69.346  22.442  -3.483  1.00 20.05           N  
ANISOU  494  N   VAL A  57     2025   2982   2611   1244    197     60       N  
ATOM    495  CA  VAL A  57      69.896  22.632  -4.827  1.00 19.40           C  
ANISOU  495  CA  VAL A  57     1989   2941   2441   1070    171     99       C  
ATOM    496  C   VAL A  57      70.754  23.891  -4.885  1.00 19.18           C  
ANISOU  496  C   VAL A  57     1837   2985   2465   1131    389     95       C  
ATOM    497  O   VAL A  57      71.798  23.922  -5.537  1.00 20.81           O  
ANISOU  497  O   VAL A  57     2230   3058   2619   1014    426     -7       O  
ATOM    498  CB  VAL A  57      68.781  22.738  -5.895  1.00 20.14           C  
ANISOU  498  CB  VAL A  57     2224   3093   2335    692     63    -12       C  
ATOM    499  CG1 VAL A  57      69.356  23.142  -7.257  1.00 20.96           C  
ANISOU  499  CG1 VAL A  57     2255   3343   2367    689     23   -153       C  
ATOM    500  CG2 VAL A  57      68.027  21.435  -5.996  1.00 19.39           C  
ANISOU  500  CG2 VAL A  57     2241   2807   2321    639    145   -121       C  
ATOM    501  N   CYS A  58      70.302  24.934  -4.195  1.00 19.28           N  
ANISOU  501  N   CYS A  58     2000   2980   2345   1112    147     83       N  
ATOM    502  CA  CYS A  58      70.989  26.218  -4.192  1.00 19.24           C  
ANISOU  502  CA  CYS A  58     2009   3085   2216    719    132    163       C  
ATOM    503  C   CYS A  58      71.314  26.668  -2.775  1.00 19.81           C  
ANISOU  503  C   CYS A  58     2026   3187   2316    771    255    160       C  
ATOM    504  O   CYS A  58      70.705  27.608  -2.255  1.00 18.84           O  
ANISOU  504  O   CYS A  58     1811   3103   2243    788    411    319       O  
ATOM    505  CB  CYS A  58      70.140  27.276  -4.896  1.00 19.78           C  
ANISOU  505  CB  CYS A  58     2188   3129   2199    585    206    152       C  
ATOM    506  SG  CYS A  58      69.784  26.865  -6.624  1.00 20.88           S  
ANISOU  506  SG  CYS A  58     2401   3226   2305    494    151    -24       S  
ATOM    507  N   PRO A  59      72.293  26.011  -2.144  1.00 20.55           N  
ANISOU  507  N   PRO A  59     2195   3172   2440    954    198    107       N  
ATOM    508  CA  PRO A  59      72.576  26.288  -0.731  1.00 21.20           C  
ANISOU  508  CA  PRO A  59     2156   3418   2482    799    191     88       C  
ATOM    509  C   PRO A  59      73.189  27.662  -0.464  1.00 21.08           C  
ANISOU  509  C   PRO A  59     2066   3470   2474    645    510    119       C  
ATOM    510  O   PRO A  59      73.157  28.118   0.681  1.00 21.24           O  
ANISOU  510  O   PRO A  59     1953   3576   2540    433    417    166       O  
ATOM    511  CB  PRO A  59      73.557  25.177  -0.351  1.00 22.08           C  
ANISOU  511  CB  PRO A  59     2240   3630   2519   1023    -26    226       C  
ATOM    512  CG  PRO A  59      74.211  24.786  -1.638  1.00 20.97           C  
ANISOU  512  CG  PRO A  59     2031   3449   2486   1173    -22    125       C  
ATOM    513  CD  PRO A  59      73.181  24.975  -2.706  1.00 20.50           C  
ANISOU  513  CD  PRO A  59     2078   3241   2469   1097    158    -39       C  
ATOM    514  N   ASP A  60      73.736  28.312  -1.487  1.00 22.31           N  
ANISOU  514  N   ASP A  60     2138   3748   2590    624    446     39       N  
ATOM    515  CA  ASP A  60      74.347  29.621  -1.294  1.00 22.96           C  
ANISOU  515  CA  ASP A  60     2030   3981   2713    625    530    118       C  
ATOM    516  C   ASP A  60      73.401  30.752  -1.665  1.00 21.56           C  
ANISOU  516  C   ASP A  60     1976   3667   2548    352    478     97       C  
ATOM    517  O   ASP A  60      73.716  31.928  -1.471  1.00 23.00           O  
ANISOU  517  O   ASP A  60     2101   3811   2826    544    507     66       O  
ATOM    518  CB  ASP A  60      75.637  29.730  -2.105  1.00 25.75           C  
ANISOU  518  CB  ASP A  60     2232   4468   3084    919    735     61       C  
ATOM    519  CG  ASP A  60      76.708  28.783  -1.612  1.00 30.96           C  
ANISOU  519  CG  ASP A  60     2970   5170   3624    982    867    -42       C  
ATOM    520  OD1 ASP A  60      76.719  28.479  -0.400  1.00 33.06           O  
ANISOU  520  OD1 ASP A  60     3286   5469   3807   1101    913    -53       O  
ATOM    521  OD2 ASP A  60      77.537  28.341  -2.434  1.00 33.28           O  
ANISOU  521  OD2 ASP A  60     3273   5424   3947   1049    921   -179       O  
ATOM    522  N   ALA A  61      72.240  30.393  -2.199  1.00 18.79           N  
ANISOU  522  N   ALA A  61     1661   3330   2148    352    410    156       N  
ATOM    523  CA  ALA A  61      71.255  31.386  -2.586  1.00 17.07           C  
ANISOU  523  CA  ALA A  61     1573   2933   1981    191    147    111       C  
ATOM    524  C   ALA A  61      70.557  31.910  -1.343  1.00 16.94           C  
ANISOU  524  C   ALA A  61     1597   2719   2121    146    353    131       C  
ATOM    525  O   ALA A  61      70.546  31.245  -0.303  1.00 17.34           O  
ANISOU  525  O   ALA A  61     1832   2773   1983    190    430    171       O  
ATOM    526  CB  ALA A  61      70.253  30.799  -3.559  1.00 16.45           C  
ANISOU  526  CB  ALA A  61     1476   2775   1998    254     12     26       C  
ATOM    527  N   ASN A  62      69.989  33.101  -1.452  1.00 16.66           N  
ANISOU  527  N   ASN A  62     1549   2661   2121    231    445     -4       N  
ATOM    528  CA  ASN A  62      69.190  33.667  -0.381  1.00 16.47           C  
ANISOU  528  CA  ASN A  62     1763   2443   2051     60    592     86       C  
ATOM    529  C   ASN A  62      67.874  32.891  -0.287  1.00 15.83           C  
ANISOU  529  C   ASN A  62     1780   2307   1929    -77    544     27       C  
ATOM    530  O   ASN A  62      67.062  32.917  -1.211  1.00 15.45           O  
ANISOU  530  O   ASN A  62     1760   2255   1854     48    191     20       O  
ATOM    531  CB  ASN A  62      68.953  35.163  -0.636  1.00 15.95           C  
ANISOU  531  CB  ASN A  62     1814   2254   1993     85    576    208       C  
ATOM    532  CG  ASN A  62      68.236  35.854   0.508  1.00 16.58           C  
ANISOU  532  CG  ASN A  62     1887   2295   2117     23    366    254       C  
ATOM    533  OD1 ASN A  62      67.570  35.210   1.323  1.00 15.97           O  
ANISOU  533  OD1 ASN A  62     1680   2271   2118     65    502    215       O  
ATOM    534  ND2 ASN A  62      68.373  37.176   0.578  1.00 16.16           N  
ANISOU  534  ND2 ASN A  62     1911   2151   2080    -33    275    275       N  
ATOM    535  N   PRO A  63      67.659  32.190   0.839  1.00 15.59           N  
ANISOU  535  N   PRO A  63     1836   2299   1789    113    339    -34       N  
ATOM    536  CA  PRO A  63      66.452  31.367   0.957  1.00 13.53           C  
ANISOU  536  CA  PRO A  63     1436   2138   1567    103    438     67       C  
ATOM    537  C   PRO A  63      65.186  32.193   0.760  1.00 13.58           C  
ANISOU  537  C   PRO A  63     1531   1982   1646     93    447    109       C  
ATOM    538  O   PRO A  63      64.242  31.768   0.101  1.00 14.00           O  
ANISOU  538  O   PRO A  63     1680   1983   1655     61    404    119       O  
ATOM    539  CB  PRO A  63      66.541  30.821   2.388  1.00 14.30           C  
ANISOU  539  CB  PRO A  63     1485   2230   1719    103    400    -65       C  
ATOM    540  CG  PRO A  63      68.006  30.842   2.710  1.00 14.51           C  
ANISOU  540  CG  PRO A  63     1498   2345   1670    207    358   -109       C  
ATOM    541  CD  PRO A  63      68.530  32.075   2.019  1.00 14.46           C  
ANISOU  541  CD  PRO A  63     1674   2192   1630     30    328    -50       C  
ATOM    542  N   SER A  64      65.189  33.398   1.306  1.00 13.42           N  
ANISOU  542  N   SER A  64     1546   1917   1637     98    335    -51       N  
ATOM    543  CA  SER A  64      64.035  34.278   1.170  1.00 13.26           C  
ANISOU  543  CA  SER A  64     1542   1857   1637    150     94    162       C  
ATOM    544  C   SER A  64      63.770  34.617  -0.300  1.00 12.95           C  
ANISOU  544  C   SER A  64     1422   1964   1536     64    172    200       C  
ATOM    545  O   SER A  64      62.614  34.719  -0.714  1.00 13.51           O  
ANISOU  545  O   SER A  64     1520   2024   1588   -107   -118    105       O  
ATOM    546  CB  SER A  64      64.240  35.549   1.989  1.00 11.87           C  
ANISOU  546  CB  SER A  64     1257   1586   1668    140     37     38       C  
ATOM    547  OG  SER A  64      63.061  36.327   2.041  1.00 12.10           O  
ANISOU  547  OG  SER A  64     1165   1618   1813     -4     75    105       O  
ATOM    548  N   ASP A  65      64.838  34.770  -1.082  1.00 13.82           N  
ANISOU  548  N   ASP A  65     1649   1953   1651    -38    280    210       N  
ATOM    549  CA  ASP A  65      64.702  35.021  -2.517  1.00 14.50           C  
ANISOU  549  CA  ASP A  65     1625   2170   1713   -287    397    209       C  
ATOM    550  C   ASP A  65      64.190  33.788  -3.258  1.00 14.21           C  
ANISOU  550  C   ASP A  65     1813   2030   1558    190    295    233       C  
ATOM    551  O   ASP A  65      63.424  33.913  -4.209  1.00 15.25           O  
ANISOU  551  O   ASP A  65     2077   2255   1462     47    227    125       O  
ATOM    552  CB  ASP A  65      66.038  35.472  -3.127  1.00 16.11           C  
ANISOU  552  CB  ASP A  65     1686   2453   1981   -430    692    123       C  
ATOM    553  CG  ASP A  65      66.354  36.929  -2.842  1.00 19.07           C  
ANISOU  553  CG  ASP A  65     2000   2739   2507   -516    491    158       C  
ATOM    554  OD1 ASP A  65      65.706  37.533  -1.966  1.00 19.45           O  
ANISOU  554  OD1 ASP A  65     1988   2544   2859   -161    251     87       O  
ATOM    555  OD2 ASP A  65      67.265  37.471  -3.499  1.00 21.06           O  
ANISOU  555  OD2 ASP A  65     2399   2875   2727   -736    529     64       O  
ATOM    556  N   LEU A  66      64.589  32.595  -2.819  1.00 13.85           N  
ANISOU  556  N   LEU A  66     1644   1993   1626    409    436     71       N  
ATOM    557  CA  LEU A  66      64.071  31.388  -3.447  1.00 13.45           C  
ANISOU  557  CA  LEU A  66     1498   2010   1603    303    312    -63       C  
ATOM    558  C   LEU A  66      62.574  31.282  -3.207  1.00 13.32           C  
ANISOU  558  C   LEU A  66     1473   1972   1618    351    409   -205       C  
ATOM    559  O   LEU A  66      61.818  30.869  -4.079  1.00 15.19           O  
ANISOU  559  O   LEU A  66     1895   2174   1704     86    305   -387       O  
ATOM    560  CB  LEU A  66      64.772  30.137  -2.925  1.00 14.32           C  
ANISOU  560  CB  LEU A  66     1440   2281   1720    528    403   -101       C  
ATOM    561  CG  LEU A  66      66.241  29.973  -3.311  1.00 15.54           C  
ANISOU  561  CG  LEU A  66     1527   2800   1576    609    374    142       C  
ATOM    562  CD1 LEU A  66      66.829  28.764  -2.613  1.00 16.77           C  
ANISOU  562  CD1 LEU A  66     1696   2807   1869    657     79    223       C  
ATOM    563  CD2 LEU A  66      66.364  29.829  -4.825  1.00 17.44           C  
ANISOU  563  CD2 LEU A  66     2074   3080   1471    708    506    396       C  
ATOM    564  N   TRP A  67      62.142  31.652  -2.009  1.00 13.24           N  
ANISOU  564  N   TRP A  67     1407   1903   1719    152    248    -93       N  
ATOM    565  CA  TRP A  67      60.721  31.612  -1.700  1.00 11.84           C  
ANISOU  565  CA  TRP A  67     1197   1733   1567    108    376      2       C  
ATOM    566  C   TRP A  67      59.955  32.652  -2.508  1.00 12.75           C  
ANISOU  566  C   TRP A  67     1450   1711   1682   -184    163    -16       C  
ATOM    567  O   TRP A  67      58.930  32.352  -3.120  1.00 14.14           O  
ANISOU  567  O   TRP A  67     1761   1907   1703     13    225   -369       O  
ATOM    568  CB  TRP A  67      60.508  31.850  -0.208  1.00 11.58           C  
ANISOU  568  CB  TRP A  67     1099   1689   1610   -150    333    -68       C  
ATOM    569  CG  TRP A  67      59.122  31.652   0.290  1.00 11.39           C  
ANISOU  569  CG  TRP A  67     1210   1679   1440     19     62     73       C  
ATOM    570  CD1 TRP A  67      58.094  32.549   0.271  1.00 11.79           C  
ANISOU  570  CD1 TRP A  67     1510   1494   1476   -180    182     30       C  
ATOM    571  CD2 TRP A  67      58.622  30.476   0.926  1.00 10.22           C  
ANISOU  571  CD2 TRP A  67      995   1452   1437    -79   -106    171       C  
ATOM    572  NE1 TRP A  67      56.972  31.996   0.858  1.00 10.48           N  
ANISOU  572  NE1 TRP A  67     1252   1260   1469    -76     58    -25       N  
ATOM    573  CE2 TRP A  67      57.276  30.724   1.266  1.00 10.87           C  
ANISOU  573  CE2 TRP A  67     1261   1380   1489     18    -43    121       C  
ATOM    574  CE3 TRP A  67      59.191  29.237   1.251  1.00 10.80           C  
ANISOU  574  CE3 TRP A  67     1237   1308   1559      3     64     34       C  
ATOM    575  CZ2 TRP A  67      56.483  29.760   1.913  1.00 11.41           C  
ANISOU  575  CZ2 TRP A  67     1288   1332   1717     44    -21    -27       C  
ATOM    576  CZ3 TRP A  67      58.409  28.292   1.903  1.00 11.20           C  
ANISOU  576  CZ3 TRP A  67     1031   1511   1715    -53     34     29       C  
ATOM    577  CH2 TRP A  67      57.066  28.562   2.230  1.00 11.70           C  
ANISOU  577  CH2 TRP A  67     1111   1539   1795      6    132    -19       C  
ATOM    578  N   HIS A  68      60.461  33.884  -2.492  1.00 12.32           N  
ANISOU  578  N   HIS A  68     1305   1539   1836    -89      3    -94       N  
ATOM    579  CA  HIS A  68      59.725  35.022  -3.018  1.00 13.11           C  
ANISOU  579  CA  HIS A  68     1811   1507   1665   -247     88   -106       C  
ATOM    580  C   HIS A  68      59.856  35.199  -4.522  1.00 13.53           C  
ANISOU  580  C   HIS A  68     1630   1893   1617   -100     13   -149       C  
ATOM    581  O   HIS A  68      58.873  35.530  -5.181  1.00 13.82           O  
ANISOU  581  O   HIS A  68     1328   2286   1638    -86     23   -146       O  
ATOM    582  CB  HIS A  68      60.181  36.305  -2.311  1.00 14.24           C  
ANISOU  582  CB  HIS A  68     2286   1393   1730   -258    293    -44       C  
ATOM    583  CG  HIS A  68      59.468  37.537  -2.769  1.00 17.17           C  
ANISOU  583  CG  HIS A  68     2845   1772   1905    100    410     82       C  
ATOM    584  ND1 HIS A  68      58.097  37.662  -2.730  1.00 18.36           N  
ANISOU  584  ND1 HIS A  68     3151   1852   1973    476    424    199       N  
ATOM    585  CD2 HIS A  68      59.940  38.699  -3.279  1.00 19.69           C  
ANISOU  585  CD2 HIS A  68     3432   1999   2050    246    495     93       C  
ATOM    586  CE1 HIS A  68      57.754  38.849  -3.199  1.00 20.05           C  
ANISOU  586  CE1 HIS A  68     3606   1844   2167    168    508    186       C  
ATOM    587  NE2 HIS A  68      58.854  39.497  -3.538  1.00 21.13           N  
ANISOU  587  NE2 HIS A  68     3790   2027   2210    256    589    273       N  
ATOM    588  N   HIS A  69      61.060  35.007  -5.060  1.00 13.54           N  
ANISOU  588  N   HIS A  69     1812   1669   1663    128    244    -64       N  
ATOM    589  CA  HIS A  69      61.287  35.256  -6.485  1.00 13.47           C  
ANISOU  589  CA  HIS A  69     1570   1836   1713    218    173     71       C  
ATOM    590  C   HIS A  69      61.131  34.000  -7.333  1.00 14.24           C  
ANISOU  590  C   HIS A  69     1584   2062   1763    119    123    166       C  
ATOM    591  O   HIS A  69      60.971  34.104  -8.548  1.00 15.80           O  
ANISOU  591  O   HIS A  69     1876   2269   1858     75    306    158       O  
ATOM    592  CB  HIS A  69      62.683  35.857  -6.740  1.00 14.20           C  
ANISOU  592  CB  HIS A  69     1618   2003   1773    -49    307     45       C  
ATOM    593  CG  HIS A  69      62.843  37.263  -6.251  1.00 15.47           C  
ANISOU  593  CG  HIS A  69     1890   2114   1876    -45    288    382       C  
ATOM    594  ND1 HIS A  69      61.877  38.228  -6.421  1.00 16.69           N  
ANISOU  594  ND1 HIS A  69     2173   2174   1994    -40    200    207       N  
ATOM    595  CD2 HIS A  69      63.872  37.870  -5.612  1.00 17.02           C  
ANISOU  595  CD2 HIS A  69     2260   2332   1877   -266    174    297       C  
ATOM    596  CE1 HIS A  69      62.293  39.366  -5.900  1.00 17.68           C  
ANISOU  596  CE1 HIS A  69     2364   2311   2042      0     67     83       C  
ATOM    597  NE2 HIS A  69      63.504  39.177  -5.403  1.00 17.95           N  
ANISOU  597  NE2 HIS A  69     2323   2472   2025   -242     12    221       N  
ATOM    598  N   VAL A  70      61.180  32.819  -6.712  1.00 13.48           N  
ANISOU  598  N   VAL A  70     1591   1753   1778      6    156     45       N  
ATOM    599  CA  VAL A  70      61.063  31.576  -7.481  1.00 14.09           C  
ANISOU  599  CA  VAL A  70     1717   1714   1922    200    259    -90       C  
ATOM    600  C   VAL A  70      59.749  30.855  -7.198  1.00 13.74           C  
ANISOU  600  C   VAL A  70     1978   1549   1695    214    244   -132       C  
ATOM    601  O   VAL A  70      58.881  30.796  -8.062  1.00 15.68           O  
ANISOU  601  O   VAL A  70     2300   1897   1762    280    190   -229       O  
ATOM    602  CB  VAL A  70      62.243  30.615  -7.207  1.00 14.65           C  
ANISOU  602  CB  VAL A  70     1629   1949   1989    -81    364   -345       C  
ATOM    603  CG1 VAL A  70      62.095  29.322  -8.027  1.00 15.37           C  
ANISOU  603  CG1 VAL A  70     1772   2148   1920    245    331   -161       C  
ATOM    604  CG2 VAL A  70      63.557  31.305  -7.515  1.00 15.35           C  
ANISOU  604  CG2 VAL A  70     1569   2254   2008   -146    393   -285       C  
ATOM    605  N   LEU A  71      59.582  30.332  -5.984  1.00 13.32           N  
ANISOU  605  N   LEU A  71     1726   1598   1737    171    240     64       N  
ATOM    606  CA  LEU A  71      58.393  29.540  -5.661  1.00 12.67           C  
ANISOU  606  CA  LEU A  71     1641   1594   1579    142    218    187       C  
ATOM    607  C   LEU A  71      57.093  30.341  -5.787  1.00 12.14           C  
ANISOU  607  C   LEU A  71     1507   1334   1772    153    196     -1       C  
ATOM    608  O   LEU A  71      56.147  29.893  -6.421  1.00 12.67           O  
ANISOU  608  O   LEU A  71     1347   1490   1975    189    159    -88       O  
ATOM    609  CB  LEU A  71      58.508  28.941  -4.247  1.00 12.98           C  
ANISOU  609  CB  LEU A  71     1669   1776   1487    305     21    134       C  
ATOM    610  CG  LEU A  71      59.672  27.971  -3.998  1.00 14.02           C  
ANISOU  610  CG  LEU A  71     1816   1905   1605    294     79   -108       C  
ATOM    611  CD1 LEU A  71      59.589  27.342  -2.603  1.00 15.11           C  
ANISOU  611  CD1 LEU A  71     2117   1878   1745    181     91     11       C  
ATOM    612  CD2 LEU A  71      59.730  26.883  -5.079  1.00 14.88           C  
ANISOU  612  CD2 LEU A  71     1880   2032   1741    398    175   -236       C  
ATOM    613  N   TYR A  72      57.063  31.535  -5.197  1.00 11.92           N  
ANISOU  613  N   TYR A  72     1540   1178   1813    276    342    -58       N  
ATOM    614  CA  TYR A  72      55.912  32.429  -5.328  1.00 12.35           C  
ANISOU  614  CA  TYR A  72     1674   1252   1767    217     98    -59       C  
ATOM    615  C   TYR A  72      55.526  32.681  -6.771  1.00 12.54           C  
ANISOU  615  C   TYR A  72     1533   1472   1759    228    108    117       C  
ATOM    616  O   TYR A  72      54.365  32.563  -7.153  1.00 13.39           O  
ANISOU  616  O   TYR A  72     1746   1534   1808     93    -93     14       O  
ATOM    617  CB  TYR A  72      56.247  33.750  -4.651  1.00 12.42           C  
ANISOU  617  CB  TYR A  72     1841    966   1911    133     11   -233       C  
ATOM    618  CG  TYR A  72      55.258  34.887  -4.776  1.00 11.65           C  
ANISOU  618  CG  TYR A  72     1591    906   1931     57    120   -175       C  
ATOM    619  CD1 TYR A  72      53.913  34.729  -4.454  1.00 11.98           C  
ANISOU  619  CD1 TYR A  72     1591   1173   1788    -96     -7   -274       C  
ATOM    620  CD2 TYR A  72      55.704  36.158  -5.112  1.00 13.20           C  
ANISOU  620  CD2 TYR A  72     1647   1132   2237    122    118    -18       C  
ATOM    621  CE1 TYR A  72      53.031  35.800  -4.521  1.00 12.14           C  
ANISOU  621  CE1 TYR A  72     1695   1127   1791    -76    197    -11       C  
ATOM    622  CE2 TYR A  72      54.839  37.218  -5.183  1.00 13.16           C  
ANISOU  622  CE2 TYR A  72     1581   1157   2263    125    101     79       C  
ATOM    623  CZ  TYR A  72      53.516  37.048  -4.875  1.00 12.68           C  
ANISOU  623  CZ  TYR A  72     1612   1114   2091      7     98      7       C  
ATOM    624  OH  TYR A  72      52.683  38.141  -4.933  1.00 13.48           O  
ANISOU  624  OH  TYR A  72     1850   1124   2148     22    146    -48       O  
ATOM    625  N  AARG A  73      56.524  33.041  -7.568  0.56 12.03           N  
ANISOU  625  N  AARG A  73     1471   1356   1742    232    217    237       N  
ATOM    626  N  BARG A  73      56.509  33.011  -7.591  0.44 12.91           N  
ANISOU  626  N  BARG A  73     1574   1498   1832    200    287    181       N  
ATOM    627  CA AARG A  73      56.287  33.417  -8.954  0.56 13.85           C  
ANISOU  627  CA AARG A  73     1673   1722   1869   -147     56    455       C  
ATOM    628  CA BARG A  73      56.205  33.441  -8.944  0.44 15.04           C  
ANISOU  628  CA BARG A  73     1821   1892   2003   -137    278    373       C  
ATOM    629  C  AARG A  73      55.799  32.247  -9.786  0.56 15.02           C  
ANISOU  629  C  AARG A  73     1912   1906   1890     64    -12    380       C  
ATOM    630  C  BARG A  73      55.830  32.260  -9.843  0.44 15.30           C  
ANISOU  630  C  BARG A  73     1889   2001   1926     46    150    322       C  
ATOM    631  O  AARG A  73      54.865  32.380 -10.578  0.56 17.18           O  
ANISOU  631  O  AARG A  73     2079   2337   2111    278   -259    329       O  
ATOM    632  O  BARG A  73      54.984  32.394 -10.730  0.44 16.57           O  
ANISOU  632  O  BARG A  73     1876   2378   2043    163     18    295       O  
ATOM    633  CB AARG A  73      57.560  33.992  -9.570  0.56 15.97           C  
ANISOU  633  CB AARG A  73     1850   2055   2163   -216      4    418       C  
ATOM    634  CB BARG A  73      57.390  34.217  -9.513  0.44 17.80           C  
ANISOU  634  CB BARG A  73     2147   2237   2380   -308    413    398       C  
ATOM    635  CG AARG A  73      57.956  35.324  -8.989  0.56 16.26           C  
ANISOU  635  CG AARG A  73     1939   1883   2355     13    -62    595       C  
ATOM    636  CG BARG A  73      57.982  35.203  -8.515  0.44 19.50           C  
ANISOU  636  CG BARG A  73     2431   2269   2708   -418    583    441       C  
ATOM    637  CD AARG A  73      56.886  36.377  -9.207  0.56 18.50           C  
ANISOU  637  CD AARG A  73     2198   2267   2564   -174    132    402       C  
ATOM    638  CD BARG A  73      58.443  36.468  -9.204  0.44 20.97           C  
ANISOU  638  CD BARG A  73     2725   2332   2910   -576    767    484       C  
ATOM    639  NE AARG A  73      57.235  37.606  -8.507  0.56 20.22           N  
ANISOU  639  NE AARG A  73     2404   2559   2721   -280    130    365       N  
ATOM    640  NE BARG A  73      57.792  37.679  -8.710  0.44 21.85           N  
ANISOU  640  NE BARG A  73     3025   2187   3090   -733    932    497       N  
ATOM    641  CZ AARG A  73      56.491  38.706  -8.492  0.56 18.17           C  
ANISOU  641  CZ AARG A  73     2154   2229   2522    -76    139    608       C  
ATOM    642  CZ BARG A  73      58.175  38.355  -7.632  0.44 21.41           C  
ANISOU  642  CZ BARG A  73     3186   1781   3169   -591    897    636       C  
ATOM    643  NH1AARG A  73      55.336  38.747  -9.141  0.56 18.80           N  
ANISOU  643  NH1AARG A  73     2405   2190   2550   -230    460    610       N  
ATOM    644  NH1BARG A  73      59.187  37.920  -6.902  0.44 19.45           N  
ANISOU  644  NH1BARG A  73     2842   1473   3076   -414    820    689       N  
ATOM    645  NH2AARG A  73      56.902  39.763  -7.816  0.56 18.40           N  
ANISOU  645  NH2AARG A  73     1923   2637   2430   -186   -212    792       N  
ATOM    646  NH2BARG A  73      57.529  39.456  -7.273  0.44 21.59           N  
ANISOU  646  NH2BARG A  73     3320   1630   3254   -390    887    819       N  
ATOM    647  N   ILE A  74      56.443  31.102  -9.612  1.00 14.75           N  
ANISOU  647  N   ILE A  74     1992   1827   1786    196    142    151       N  
ATOM    648  CA  ILE A  74      56.048  29.907 -10.333  1.00 16.08           C  
ANISOU  648  CA  ILE A  74     2072   2186   1853     71    165    -14       C  
ATOM    649  C   ILE A  74      54.634  29.487  -9.926  1.00 15.23           C  
ANISOU  649  C   ILE A  74     1846   2323   1619    294    240     44       C  
ATOM    650  O   ILE A  74      53.814  29.139 -10.771  1.00 16.04           O  
ANISOU  650  O   ILE A  74     1817   2385   1891    127    280      3       O  
ATOM    651  CB  ILE A  74      57.043  28.751 -10.095  1.00 17.10           C  
ANISOU  651  CB  ILE A  74     2168   2320   2008    235    122    -42       C  
ATOM    652  CG1 ILE A  74      58.390  29.084 -10.747  1.00 18.06           C  
ANISOU  652  CG1 ILE A  74     2039   2514   2310    261     60     25       C  
ATOM    653  CG2 ILE A  74      56.501  27.458 -10.657  1.00 17.71           C  
ANISOU  653  CG2 ILE A  74     2387   2421   1921    146    190   -325       C  
ATOM    654  CD1 ILE A  74      59.471  28.047 -10.521  1.00 18.39           C  
ANISOU  654  CD1 ILE A  74     2091   2362   2536    386     28    -33       C  
ATOM    655  N   TYR A  75      54.350  29.526  -8.625  1.00 13.99           N  
ANISOU  655  N   TYR A  75     1715   2165   1436    139    388     29       N  
ATOM    656  CA  TYR A  75      53.028  29.169  -8.132  1.00 13.33           C  
ANISOU  656  CA  TYR A  75     1741   2024   1297    187     86   -128       C  
ATOM    657  C   TYR A  75      51.953  30.068  -8.748  1.00 15.15           C  
ANISOU  657  C   TYR A  75     2065   2151   1539    -35   -129   -271       C  
ATOM    658  O   TYR A  75      50.940  29.584  -9.258  1.00 16.00           O  
ANISOU  658  O   TYR A  75     2083   2388   1607     93   -261   -261       O  
ATOM    659  CB  TYR A  75      53.000  29.249  -6.602  1.00 12.68           C  
ANISOU  659  CB  TYR A  75     1678   1874   1264     -6    115   -117       C  
ATOM    660  CG  TYR A  75      51.742  28.692  -5.985  1.00 11.63           C  
ANISOU  660  CG  TYR A  75     1588   1528   1303     63   -117     29       C  
ATOM    661  CD1 TYR A  75      51.689  27.367  -5.570  1.00 12.54           C  
ANISOU  661  CD1 TYR A  75     1658   1560   1545   -197   -120     63       C  
ATOM    662  CD2 TYR A  75      50.611  29.484  -5.805  1.00 11.96           C  
ANISOU  662  CD2 TYR A  75     1604   1611   1327     50   -137   -158       C  
ATOM    663  CE1 TYR A  75      50.550  26.836  -5.008  1.00 12.73           C  
ANISOU  663  CE1 TYR A  75     1614   1615   1609   -104    -71     30       C  
ATOM    664  CE2 TYR A  75      49.457  28.965  -5.228  1.00 11.88           C  
ANISOU  664  CE2 TYR A  75     1647   1466   1400     21     -6   -220       C  
ATOM    665  CZ  TYR A  75      49.437  27.635  -4.831  1.00 12.55           C  
ANISOU  665  CZ  TYR A  75     1697   1468   1604     11    -11   -153       C  
ATOM    666  OH  TYR A  75      48.316  27.077  -4.262  1.00 14.10           O  
ANISOU  666  OH  TYR A  75     1935   1484   1938    -28     85     72       O  
ATOM    667  N   ILE A  76      52.181  31.376  -8.707  1.00 15.92           N  
ANISOU  667  N   ILE A  76     2337   1991   1720      6   -317   -184       N  
ATOM    668  CA  ILE A  76      51.246  32.334  -9.290  1.00 18.04           C  
ANISOU  668  CA  ILE A  76     2618   2283   1954    243   -398   -113       C  
ATOM    669  C   ILE A  76      51.012  32.091 -10.790  1.00 18.33           C  
ANISOU  669  C   ILE A  76     2517   2526   1922    229   -378    103       C  
ATOM    670  O   ILE A  76      49.885  32.231 -11.273  1.00 20.41           O  
ANISOU  670  O   ILE A  76     2530   3178   2047    -89   -479     23       O  
ATOM    671  CB  ILE A  76      51.744  33.786  -9.059  1.00 20.86           C  
ANISOU  671  CB  ILE A  76     2977   2632   2317    886   -530   -195       C  
ATOM    672  CG1 ILE A  76      51.716  34.125  -7.567  1.00 23.85           C  
ANISOU  672  CG1 ILE A  76     3066   3422   2575    417   -227   -181       C  
ATOM    673  CG2 ILE A  76      50.914  34.789  -9.860  1.00 22.85           C  
ANISOU  673  CG2 ILE A  76     3281   2798   2601   1112   -609   -191       C  
ATOM    674  CD1 ILE A  76      50.357  33.980  -6.933  1.00 24.35           C  
ANISOU  674  CD1 ILE A  76     3039   3636   2579     77   -319   -219       C  
ATOM    675  N   ARG A  77      52.061  31.710 -11.517  1.00 16.63           N  
ANISOU  675  N   ARG A  77     2546   2279   1495    258   -170     96       N  
ATOM    676  CA  ARG A  77      51.944  31.449 -12.952  1.00 18.60           C  
ANISOU  676  CA  ARG A  77     2775   2770   1522    255   -253     46       C  
ATOM    677  C   ARG A  77      51.195  30.160 -13.241  1.00 18.49           C  
ANISOU  677  C   ARG A  77     2803   2659   1563    481   -443   -172       C  
ATOM    678  O   ARG A  77      50.385  30.086 -14.170  1.00 20.86           O  
ANISOU  678  O   ARG A  77     3148   2877   1901    517   -517   -334       O  
ATOM    679  CB  ARG A  77      53.328  31.373 -13.595  1.00 19.75           C  
ANISOU  679  CB  ARG A  77     2910   3141   1452     84    101     -9       C  
ATOM    680  CG  ARG A  77      53.278  31.093 -15.106  1.00 23.24           C  
ANISOU  680  CG  ARG A  77     3300   3663   1867    270    295    -45       C  
ATOM    681  CD  ARG A  77      54.657  30.898 -15.715  1.00 25.82           C  
ANISOU  681  CD  ARG A  77     3636   3812   2363    448    396     46       C  
ATOM    682  NE  ARG A  77      55.234  29.594 -15.398  1.00 27.13           N  
ANISOU  682  NE  ARG A  77     3803   3906   2598    697    422     55       N  
ATOM    683  CZ  ARG A  77      56.444  29.428 -14.875  1.00 29.26           C  
ANISOU  683  CZ  ARG A  77     4217   4044   2855    442     66     35       C  
ATOM    684  NH1 ARG A  77      57.198  30.484 -14.607  1.00 30.46           N  
ANISOU  684  NH1 ARG A  77     4474   4032   3069    518     75   -126       N  
ATOM    685  NH2 ARG A  77      56.902  28.210 -14.620  1.00 29.67           N  
ANISOU  685  NH2 ARG A  77     4261   4068   2943    439   -107    205       N  
ATOM    686  N   GLU A  78      51.464  29.143 -12.434  1.00 17.00           N  
ANISOU  686  N   GLU A  78     2428   2610   1420    534    -78   -251       N  
ATOM    687  CA  GLU A  78      51.026  27.792 -12.756  1.00 17.19           C  
ANISOU  687  CA  GLU A  78     2431   2563   1536    397   -232   -496       C  
ATOM    688  C   GLU A  78      49.708  27.341 -12.137  1.00 16.36           C  
ANISOU  688  C   GLU A  78     2142   2494   1581    496   -298   -758       C  
ATOM    689  O   GLU A  78      49.076  26.415 -12.639  1.00 17.92           O  
ANISOU  689  O   GLU A  78     2448   2274   2087    293   -258   -643       O  
ATOM    690  CB  GLU A  78      52.122  26.803 -12.365  1.00 18.90           C  
ANISOU  690  CB  GLU A  78     2540   2819   1821    512    -39   -364       C  
ATOM    691  CG  GLU A  78      53.416  27.007 -13.124  1.00 20.23           C  
ANISOU  691  CG  GLU A  78     2770   3135   1782    422    284   -321       C  
ATOM    692  CD  GLU A  78      53.308  26.545 -14.568  1.00 23.40           C  
ANISOU  692  CD  GLU A  78     3179   3551   2159    215    340   -538       C  
ATOM    693  OE1 GLU A  78      52.428  25.707 -14.853  1.00 26.11           O  
ANISOU  693  OE1 GLU A  78     3519   4072   2330     98    288   -721       O  
ATOM    694  OE2 GLU A  78      54.100  27.018 -15.403  1.00 24.25           O  
ANISOU  694  OE2 GLU A  78     3413   3460   2340     67    474   -305       O  
ATOM    695  N   LYS A  79      49.280  27.972 -11.046  1.00 16.00           N  
ANISOU  695  N   LYS A  79     2032   2354   1693    645   -169   -549       N  
ATOM    696  CA  LYS A  79      48.089  27.500 -10.347  1.00 14.95           C  
ANISOU  696  CA  LYS A  79     1896   2128   1658    461   -158   -358       C  
ATOM    697  C   LYS A  79      46.828  27.589 -11.218  1.00 17.13           C  
ANISOU  697  C   LYS A  79     2101   2270   2139    157   -331   -284       C  
ATOM    698  O   LYS A  79      46.509  28.642 -11.761  1.00 17.36           O  
ANISOU  698  O   LYS A  79     2252   2286   2055    209   -463    -90       O  
ATOM    699  CB  LYS A  79      47.891  28.292  -9.045  1.00 14.58           C  
ANISOU  699  CB  LYS A  79     2081   1800   1659    442    -76   -266       C  
ATOM    700  CG  LYS A  79      46.856  27.689  -8.118  1.00 14.05           C  
ANISOU  700  CG  LYS A  79     2080   1563   1697    529    -24   -125       C  
ATOM    701  CD  LYS A  79      47.356  26.378  -7.522  1.00 16.48           C  
ANISOU  701  CD  LYS A  79     2534   1764   1964    292     92   -340       C  
ATOM    702  CE  LYS A  79      46.383  25.768  -6.525  1.00 16.76           C  
ANISOU  702  CE  LYS A  79     2425   1771   2173    353    252   -209       C  
ATOM    703  NZ  LYS A  79      47.034  24.664  -5.755  1.00 18.24           N  
ANISOU  703  NZ  LYS A  79     2589   1912   2428    399    459    -44       N  
ATOM    704  N   ILE A  80      46.115  26.474 -11.338  1.00 17.56           N  
ANISOU  704  N   ILE A  80     2085   2227   2360    276   -538   -673       N  
ATOM    705  CA  ILE A  80      44.922  26.410 -12.179  1.00 19.25           C  
ANISOU  705  CA  ILE A  80     2367   2428   2521    436   -661   -784       C  
ATOM    706  C   ILE A  80      43.641  26.264 -11.356  1.00 18.59           C  
ANISOU  706  C   ILE A  80     2220   2302   2540    490   -721   -746       C  
ATOM    707  O   ILE A  80      43.620  25.580 -10.336  1.00 20.10           O  
ANISOU  707  O   ILE A  80     2506   2484   2649    281   -587   -516       O  
ATOM    708  CB  ILE A  80      45.017  25.227 -13.182  1.00 21.83           C  
ANISOU  708  CB  ILE A  80     2696   2860   2739    525   -536  -1057       C  
ATOM    709  CG1 ILE A  80      46.272  25.366 -14.043  1.00 25.73           C  
ANISOU  709  CG1 ILE A  80     3155   3443   3177    689   -245   -899       C  
ATOM    710  CG2 ILE A  80      43.784  25.154 -14.069  1.00 22.24           C  
ANISOU  710  CG2 ILE A  80     2937   2854   2659    636   -773  -1204       C  
ATOM    711  CD1 ILE A  80      46.339  26.660 -14.812  1.00 27.46           C  
ANISOU  711  CD1 ILE A  80     3347   3748   3340    846    -65   -822       C  
ATOM    712  N   GLY A  81      42.580  26.940 -11.790  1.00 18.75           N  
ANISOU  712  N   GLY A  81     2229   2285   2612    364   -694   -993       N  
ATOM    713  CA  GLY A  81      41.250  26.670 -11.278  1.00 19.48           C  
ANISOU  713  CA  GLY A  81     2257   2485   2658    608   -407  -1075       C  
ATOM    714  C   GLY A  81      40.874  27.394 -10.004  1.00 21.43           C  
ANISOU  714  C   GLY A  81     2353   2914   2876    201   -391  -1003       C  
ATOM    715  O   GLY A  81      39.833  27.120  -9.405  1.00 23.74           O  
ANISOU  715  O   GLY A  81     2397   3394   3230    222   -280   -968       O  
ATOM    716  N   THR A  82      41.728  28.320  -9.591  1.00 18.97           N  
ANISOU  716  N   THR A  82     2173   2386   2650    -94   -485  -1084       N  
ATOM    717  CA  THR A  82      41.527  29.043  -8.346  1.00 18.09           C  
ANISOU  717  CA  THR A  82     2121   2208   2542     82   -280   -685       C  
ATOM    718  C   THR A  82      42.426  30.279  -8.382  1.00 16.95           C  
ANISOU  718  C   THR A  82     2165   1940   2334    -24   -311   -509       C  
ATOM    719  O   THR A  82      43.446  30.278  -9.071  1.00 17.76           O  
ANISOU  719  O   THR A  82     2314   1914   2519   -205   -460   -494       O  
ATOM    720  CB  THR A  82      41.834  28.141  -7.114  1.00 18.79           C  
ANISOU  720  CB  THR A  82     2153   2326   2662   -221    -81   -622       C  
ATOM    721  OG1 THR A  82      41.336  28.747  -5.918  1.00 18.37           O  
ANISOU  721  OG1 THR A  82     2144   2136   2699   -508    -44   -473       O  
ATOM    722  CG2 THR A  82      43.328  27.867  -6.976  1.00 19.14           C  
ANISOU  722  CG2 THR A  82     2034   2502   2735   -239   -128   -634       C  
ATOM    723  N   ASP A  83      42.041  31.345  -7.682  1.00 13.86           N  
ANISOU  723  N   ASP A  83     1846   1590   1832    124   -402   -170       N  
ATOM    724  CA  ASP A  83      42.811  32.587  -7.754  1.00 13.21           C  
ANISOU  724  CA  ASP A  83     1762   1469   1790    174   -271   -242       C  
ATOM    725  C   ASP A  83      44.226  32.361  -7.243  1.00 13.47           C  
ANISOU  725  C   ASP A  83     1608   1824   1685    -25   -108   -211       C  
ATOM    726  O   ASP A  83      44.401  32.002  -6.090  1.00 13.30           O  
ANISOU  726  O   ASP A  83     1809   1767   1478    215   -240    -64       O  
ATOM    727  CB  ASP A  83      42.159  33.699  -6.943  1.00 14.77           C  
ANISOU  727  CB  ASP A  83     1892   1530   2191    -86    -17   -108       C  
ATOM    728  CG  ASP A  83      42.916  35.000  -7.068  1.00 16.72           C  
ANISOU  728  CG  ASP A  83     2384   1691   2278    141    -39    -14       C  
ATOM    729  OD1 ASP A  83      42.896  35.597  -8.165  1.00 19.24           O  
ANISOU  729  OD1 ASP A  83     2915   2194   2201    317   -201    -35       O  
ATOM    730  OD2 ASP A  83      43.556  35.408  -6.083  1.00 15.53           O  
ANISOU  730  OD2 ASP A  83     2291   1471   2138    160    -41    -50       O  
ATOM    731  N   PRO A  84      45.237  32.570  -8.098  1.00 13.53           N  
ANISOU  731  N   PRO A  84     1617   1910   1615    -37   -183   -334       N  
ATOM    732  CA  PRO A  84      46.605  32.229  -7.686  1.00 12.21           C  
ANISOU  732  CA  PRO A  84     1413   1769   1458    -86   -181   -429       C  
ATOM    733  C   PRO A  84      47.091  33.017  -6.460  1.00 11.75           C  
ANISOU  733  C   PRO A  84     1451   1393   1619    -54    -18   -155       C  
ATOM    734  O   PRO A  84      47.674  32.427  -5.553  1.00 12.90           O  
ANISOU  734  O   PRO A  84     1721   1397   1781    -25    -70    -24       O  
ATOM    735  CB  PRO A  84      47.437  32.569  -8.926  1.00 13.44           C  
ANISOU  735  CB  PRO A  84     1602   2114   1389   -106   -293   -283       C  
ATOM    736  CG  PRO A  84      46.467  32.414 -10.089  1.00 14.40           C  
ANISOU  736  CG  PRO A  84     1722   2267   1481    -83    -97   -356       C  
ATOM    737  CD  PRO A  84      45.130  32.856  -9.541  1.00 14.11           C  
ANISOU  737  CD  PRO A  84     1611   2193   1558   -132   -102   -421       C  
ATOM    738  N   SER A  85      46.845  34.323  -6.421  1.00 10.70           N  
ANISOU  738  N   SER A  85     1161   1283   1622    -73     44   -107       N  
ATOM    739  CA  SER A  85      47.339  35.114  -5.298  1.00 10.18           C  
ANISOU  739  CA  SER A  85     1245   1038   1584    -78     84     -9       C  
ATOM    740  C   SER A  85      46.682  34.739  -3.971  1.00 10.13           C  
ANISOU  740  C   SER A  85     1186   1252   1411   -213     61   -138       C  
ATOM    741  O   SER A  85      47.349  34.627  -2.946  1.00 10.40           O  
ANISOU  741  O   SER A  85     1265   1390   1294    129     55   -180       O  
ATOM    742  CB  SER A  85      47.134  36.610  -5.554  1.00 11.43           C  
ANISOU  742  CB  SER A  85     1519   1038   1786     16    151    128       C  
ATOM    743  OG  SER A  85      48.053  37.094  -6.514  1.00 13.22           O  
ANISOU  743  OG  SER A  85     1988   1314   1719     35      2     37       O  
ATOM    744  N   GLN A  86      45.371  34.554  -3.975  1.00 10.58           N  
ANISOU  744  N   GLN A  86     1143   1371   1504   -293    144   -265       N  
ATOM    745  CA  GLN A  86      44.691  34.214  -2.727  1.00 10.67           C  
ANISOU  745  CA  GLN A  86     1063   1171   1820   -121     77    -17       C  
ATOM    746  C   GLN A  86      44.949  32.760  -2.319  1.00 11.32           C  
ANISOU  746  C   GLN A  86     1252   1255   1794     -5    -76   -179       C  
ATOM    747  O   GLN A  86      44.998  32.441  -1.133  1.00 11.83           O  
ANISOU  747  O   GLN A  86     1360   1431   1704    -56   -114   -200       O  
ATOM    748  CB  GLN A  86      43.193  34.506  -2.839  1.00 10.87           C  
ANISOU  748  CB  GLN A  86     1134   1179   1817   -102   -232    -41       C  
ATOM    749  CG  GLN A  86      42.863  36.008  -2.966  1.00 11.62           C  
ANISOU  749  CG  GLN A  86     1552   1138   1726     58   -297    -42       C  
ATOM    750  CD  GLN A  86      42.985  36.751  -1.644  1.00 11.35           C  
ANISOU  750  CD  GLN A  86     1514   1070   1727    101    123    -71       C  
ATOM    751  OE1 GLN A  86      44.091  36.991  -1.153  1.00 12.90           O  
ANISOU  751  OE1 GLN A  86     1757   1463   1680      3    -19   -150       O  
ATOM    752  NE2 GLN A  86      41.843  37.102  -1.048  1.00 12.59           N  
ANISOU  752  NE2 GLN A  86     1586   1148   2049    180    364    137       N  
ATOM    753  N   SER A  87      45.120  31.886  -3.310  1.00 10.75           N  
ANISOU  753  N   SER A  87     1253   1031   1800    111    -43   -362       N  
ATOM    754  CA  SER A  87      45.550  30.524  -3.035  1.00 11.31           C  
ANISOU  754  CA  SER A  87     1348   1076   1873    176   -241   -544       C  
ATOM    755  C   SER A  87      46.923  30.518  -2.363  1.00 12.19           C  
ANISOU  755  C   SER A  87     1559   1136   1939     23    -80   -313       C  
ATOM    756  O   SER A  87      47.137  29.818  -1.375  1.00 12.04           O  
ANISOU  756  O   SER A  87     1532   1172   1870    -45    -27    -83       O  
ATOM    757  CB  SER A  87      45.578  29.712  -4.327  1.00 11.79           C  
ANISOU  757  CB  SER A  87     1643    923   1913     71   -206   -556       C  
ATOM    758  OG  SER A  87      46.035  28.386  -4.087  1.00 12.93           O  
ANISOU  758  OG  SER A  87     1642   1070   2199     -8   -176   -488       O  
ATOM    759  N   TRP A  88      47.834  31.318  -2.897  1.00 12.69           N  
ANISOU  759  N   TRP A  88     1487   1259   2075   -262   -212   -344       N  
ATOM    760  CA  TRP A  88      49.152  31.475  -2.305  1.00 11.14           C  
ANISOU  760  CA  TRP A  88     1486   1059   1687   -387    -65      2       C  
ATOM    761  C   TRP A  88      49.078  31.938  -0.849  1.00 11.03           C  
ANISOU  761  C   TRP A  88     1553   1045   1592   -190   -163    -10       C  
ATOM    762  O   TRP A  88      49.797  31.413   0.001  1.00 12.01           O  
ANISOU  762  O   TRP A  88     1704   1247   1613   -255   -219    174       O  
ATOM    763  CB  TRP A  88      49.982  32.455  -3.141  1.00 10.91           C  
ANISOU  763  CB  TRP A  88     1346   1220   1580   -551    -94    159       C  
ATOM    764  CG  TRP A  88      51.311  32.783  -2.531  1.00 10.95           C  
ANISOU  764  CG  TRP A  88     1259   1371   1533   -245   -103    -34       C  
ATOM    765  CD1 TRP A  88      51.649  33.943  -1.875  1.00 10.01           C  
ANISOU  765  CD1 TRP A  88     1247   1249   1306   -308   -163   -257       C  
ATOM    766  CD2 TRP A  88      52.486  31.964  -2.524  1.00 10.94           C  
ANISOU  766  CD2 TRP A  88     1457   1310   1387     72     61    -89       C  
ATOM    767  NE1 TRP A  88      52.955  33.886  -1.456  1.00 10.70           N  
ANISOU  767  NE1 TRP A  88     1432   1302   1331     61     30    148       N  
ATOM    768  CE2 TRP A  88      53.494  32.685  -1.844  1.00 10.24           C  
ANISOU  768  CE2 TRP A  88     1393   1189   1311    110    160    -24       C  
ATOM    769  CE3 TRP A  88      52.786  30.686  -3.018  1.00 11.95           C  
ANISOU  769  CE3 TRP A  88     1539   1605   1395    363    128   -258       C  
ATOM    770  CZ2 TRP A  88      54.779  32.171  -1.643  1.00 12.01           C  
ANISOU  770  CZ2 TRP A  88     1654   1538   1373    184    113   -183       C  
ATOM    771  CZ3 TRP A  88      54.066  30.178  -2.822  1.00 11.88           C  
ANISOU  771  CZ3 TRP A  88     1625   1580   1309     92   -103   -257       C  
ATOM    772  CH2 TRP A  88      55.048  30.922  -2.142  1.00 12.28           C  
ANISOU  772  CH2 TRP A  88     1729   1512   1423    -37     -3   -289       C  
ATOM    773  N   VAL A  89      48.214  32.910  -0.543  1.00  9.97           N  
ANISOU  773  N   VAL A  89     1419    982   1386    -91    -50   -203       N  
ATOM    774  CA  VAL A  89      48.063  33.350   0.848  1.00 11.92           C  
ANISOU  774  CA  VAL A  89     1908   1177   1446    -32    155    -51       C  
ATOM    775  C   VAL A  89      47.692  32.172   1.749  1.00 12.15           C  
ANISOU  775  C   VAL A  89     1905   1196   1514   -211     32     -5       C  
ATOM    776  O   VAL A  89      48.293  31.973   2.801  1.00 13.57           O  
ANISOU  776  O   VAL A  89     2187   1335   1636   -417     50    134       O  
ATOM    777  CB  VAL A  89      46.989  34.440   0.991  1.00 11.91           C  
ANISOU  777  CB  VAL A  89     2072   1126   1329     26    282   -122       C  
ATOM    778  CG1 VAL A  89      46.753  34.773   2.460  1.00 12.47           C  
ANISOU  778  CG1 VAL A  89     2369   1196   1174   -275    343   -265       C  
ATOM    779  CG2 VAL A  89      47.385  35.683   0.200  1.00 10.31           C  
ANISOU  779  CG2 VAL A  89     1829    827   1261   -162    195    154       C  
ATOM    780  N   ARG A  90      46.717  31.382   1.300  1.00 10.82           N  
ANISOU  780  N   ARG A  90     1598    955   1558   -257    175    -68       N  
ATOM    781  CA  ARG A  90      46.154  30.317   2.121  1.00 11.94           C  
ANISOU  781  CA  ARG A  90     1601   1174   1763   -196    135     23       C  
ATOM    782  C   ARG A  90      47.115  29.143   2.296  1.00 11.95           C  
ANISOU  782  C   ARG A  90     1436   1334   1771   -164    -85    114       C  
ATOM    783  O   ARG A  90      47.116  28.485   3.344  1.00 14.20           O  
ANISOU  783  O   ARG A  90     2010   1387   1998   -151   -238    246       O  
ATOM    784  CB  ARG A  90      44.840  29.844   1.500  1.00 12.50           C  
ANISOU  784  CB  ARG A  90     1458   1287   2004   -348    376     63       C  
ATOM    785  CG  ARG A  90      44.239  28.619   2.172  1.00 13.69           C  
ANISOU  785  CG  ARG A  90     1678   1322   2203   -337    290    -25       C  
ATOM    786  CD  ARG A  90      43.836  28.885   3.617  1.00 15.39           C  
ANISOU  786  CD  ARG A  90     1857   1690   2300   -703    124     17       C  
ATOM    787  NE  ARG A  90      43.222  27.678   4.176  1.00 16.87           N  
ANISOU  787  NE  ARG A  90     2028   1722   2660   -788    186    111       N  
ATOM    788  CZ  ARG A  90      43.750  26.925   5.134  1.00 18.90           C  
ANISOU  788  CZ  ARG A  90     2057   2041   3082   -882     -4    387       C  
ATOM    789  NH1 ARG A  90      44.897  27.266   5.705  1.00 20.32           N  
ANISOU  789  NH1 ARG A  90     2120   2394   3208   -917   -210    530       N  
ATOM    790  NH2 ARG A  90      43.110  25.828   5.538  1.00 21.03           N  
ANISOU  790  NH2 ARG A  90     2433   2260   3298   -629     77    234       N  
ATOM    791  N   THR A  91      47.941  28.885   1.286  1.00 11.94           N  
ANISOU  791  N   THR A  91     1312   1310   1914    153     42    142       N  
ATOM    792  CA  THR A  91      48.807  27.699   1.315  1.00 12.65           C  
ANISOU  792  CA  THR A  91     1284   1474   2049    199     67    131       C  
ATOM    793  C   THR A  91      50.254  27.962   1.747  1.00 12.62           C  
ANISOU  793  C   THR A  91     1429   1325   2041    -61    -79     56       C  
ATOM    794  O   THR A  91      50.897  27.088   2.328  1.00 13.60           O  
ANISOU  794  O   THR A  91     1450   1698   2019    -23   -300    195       O  
ATOM    795  CB  THR A  91      48.832  27.013  -0.059  1.00 13.08           C  
ANISOU  795  CB  THR A  91     1209   1590   2169     48   -319    117       C  
ATOM    796  OG1 THR A  91      49.308  27.931  -1.055  1.00 13.32           O  
ANISOU  796  OG1 THR A  91     1220   1587   2255     -6   -261   -144       O  
ATOM    797  CG2 THR A  91      47.433  26.543  -0.424  1.00 14.10           C  
ANISOU  797  CG2 THR A  91     1164   1775   2420    292   -231    162       C  
ATOM    798  N   SER A  92      50.775  29.158   1.482  1.00 11.36           N  
ANISOU  798  N   SER A  92     1275   1054   1987   -339    -23    290       N  
ATOM    799  CA  SER A  92      52.203  29.400   1.699  1.00 11.10           C  
ANISOU  799  CA  SER A  92     1291   1243   1685   -347     -2    161       C  
ATOM    800  C   SER A  92      52.586  29.602   3.168  1.00 12.77           C  
ANISOU  800  C   SER A  92     1729   1395   1727   -266      8     65       C  
ATOM    801  O   SER A  92      53.700  29.283   3.559  1.00 13.97           O  
ANISOU  801  O   SER A  92     1993   1443   1875   -307    -54    207       O  
ATOM    802  CB  SER A  92      52.667  30.600   0.859  1.00 11.62           C  
ANISOU  802  CB  SER A  92     1391   1210   1812   -101     74    132       C  
ATOM    803  OG  SER A  92      52.104  31.821   1.320  1.00 12.13           O  
ANISOU  803  OG  SER A  92     1582   1199   1829      4     28     89       O  
ATOM    804  N   GLY A  93      51.666  30.114   3.975  1.00 13.19           N  
ANISOU  804  N   GLY A  93     2000   1301   1710    -57    170     40       N  
ATOM    805  CA  GLY A  93      51.918  30.280   5.398  1.00 14.21           C  
ANISOU  805  CA  GLY A  93     2143   1468   1788   -373    211    -37       C  
ATOM    806  C   GLY A  93      52.146  28.934   6.047  1.00 14.25           C  
ANISOU  806  C   GLY A  93     1895   1646   1872   -338     71   -188       C  
ATOM    807  O   GLY A  93      53.149  28.710   6.727  1.00 14.79           O  
ANISOU  807  O   GLY A  93     1822   1879   1919   -241    119   -179       O  
ATOM    808  N   GLU A  94      51.215  28.016   5.809  1.00 13.50           N  
ANISOU  808  N   GLU A  94     1893   1346   1891   -343    125    -35       N  
ATOM    809  CA  GLU A  94      51.370  26.667   6.329  1.00 12.40           C  
ANISOU  809  CA  GLU A  94     1471   1219   2022   -328     96    224       C  
ATOM    810  C   GLU A  94      52.555  25.950   5.683  1.00 13.10           C  
ANISOU  810  C   GLU A  94     1509   1640   1827   -301    188    261       C  
ATOM    811  O   GLU A  94      53.186  25.088   6.303  1.00 12.33           O  
ANISOU  811  O   GLU A  94     1554   1388   1744   -152    -29    373       O  
ATOM    812  CB  GLU A  94      50.080  25.870   6.130  1.00 13.49           C  
ANISOU  812  CB  GLU A  94     1491   1431   2205   -255    142    -56       C  
ATOM    813  CG  GLU A  94      48.930  26.439   6.958  1.00 16.11           C  
ANISOU  813  CG  GLU A  94     1732   1906   2484    -29    473   -171       C  
ATOM    814  CD  GLU A  94      47.719  25.531   7.032  1.00 18.90           C  
ANISOU  814  CD  GLU A  94     2047   2447   2688    -13    399   -143       C  
ATOM    815  OE1 GLU A  94      47.590  24.636   6.175  1.00 18.78           O  
ANISOU  815  OE1 GLU A  94     2167   2416   2552     10    290    224       O  
ATOM    816  OE2 GLU A  94      46.903  25.712   7.970  1.00 22.46           O  
ANISOU  816  OE2 GLU A  94     2215   3299   3020   -268    272   -352       O  
ATOM    817  N   ALA A  95      52.883  26.306   4.448  1.00 12.82           N  
ANISOU  817  N   ALA A  95     1189   1861   1821    -82    191    194       N  
ATOM    818  CA  ALA A  95      54.027  25.678   3.796  1.00 11.23           C  
ANISOU  818  CA  ALA A  95     1051   1586   1631     -9    144    261       C  
ATOM    819  C   ALA A  95      55.332  25.993   4.523  1.00 11.56           C  
ANISOU  819  C   ALA A  95     1255   1469   1669    -81    -88     89       C  
ATOM    820  O   ALA A  95      56.219  25.151   4.582  1.00 12.24           O  
ANISOU  820  O   ALA A  95     1429   1420   1803     87    -48    107       O  
ATOM    821  CB  ALA A  95      54.119  26.110   2.342  1.00 11.79           C  
ANISOU  821  CB  ALA A  95     1283   1675   1522   -149    439    248       C  
ATOM    822  N   PHE A  96      55.470  27.199   5.070  1.00 11.84           N  
ANISOU  822  N   PHE A  96     1475   1490   1534    -87   -127   -152       N  
ATOM    823  CA  PHE A  96      56.703  27.526   5.779  1.00 11.76           C  
ANISOU  823  CA  PHE A  96     1526   1333   1609    -49    -95   -111       C  
ATOM    824  C   PHE A  96      56.807  26.702   7.077  1.00 11.65           C  
ANISOU  824  C   PHE A  96     1501   1345   1582     17    -35    129       C  
ATOM    825  O   PHE A  96      57.891  26.237   7.446  1.00 12.06           O  
ANISOU  825  O   PHE A  96     1472   1332   1779   -117    -15     60       O  
ATOM    826  CB  PHE A  96      56.775  29.035   6.046  1.00 12.45           C  
ANISOU  826  CB  PHE A  96     1766   1264   1702   -242   -106   -240       C  
ATOM    827  CG  PHE A  96      58.035  29.472   6.738  1.00 12.09           C  
ANISOU  827  CG  PHE A  96     1540   1401   1654   -379    -18   -134       C  
ATOM    828  CD1 PHE A  96      59.275  29.005   6.340  1.00 13.19           C  
ANISOU  828  CD1 PHE A  96     1559   1602   1853   -383   -172    -46       C  
ATOM    829  CD2 PHE A  96      57.969  30.373   7.786  1.00 12.84           C  
ANISOU  829  CD2 PHE A  96     1791   1526   1561   -457    -57     -6       C  
ATOM    830  CE1 PHE A  96      60.431  29.428   6.987  1.00 13.32           C  
ANISOU  830  CE1 PHE A  96     1587   1670   1804    -46   -137    -89       C  
ATOM    831  CE2 PHE A  96      59.116  30.798   8.444  1.00 12.85           C  
ANISOU  831  CE2 PHE A  96     1663   1697   1523   -376   -142    -46       C  
ATOM    832  CZ  PHE A  96      60.349  30.324   8.045  1.00 13.72           C  
ANISOU  832  CZ  PHE A  96     1742   1766   1704   -176   -316     37       C  
ATOM    833  N   GLU A  97      55.681  26.507   7.760  1.00 11.28           N  
ANISOU  833  N   GLU A  97     1520   1215   1550    314    166    165       N  
ATOM    834  CA  GLU A  97      55.642  25.580   8.900  1.00 11.89           C  
ANISOU  834  CA  GLU A  97     1507   1355   1654    332    243     35       C  
ATOM    835  C   GLU A  97      56.105  24.175   8.494  1.00 12.63           C  
ANISOU  835  C   GLU A  97     1616   1435   1750     17     84    116       C  
ATOM    836  O   GLU A  97      56.932  23.566   9.178  1.00 12.77           O  
ANISOU  836  O   GLU A  97     1504   1537   1813     19    144    196       O  
ATOM    837  CB  GLU A  97      54.242  25.493   9.484  1.00 12.41           C  
ANISOU  837  CB  GLU A  97     1645   1307   1764    486    241   -173       C  
ATOM    838  CG  GLU A  97      53.685  26.833   9.942  1.00 14.57           C  
ANISOU  838  CG  GLU A  97     1618   1870   2048    471    284    -56       C  
ATOM    839  CD  GLU A  97      52.268  26.670  10.439  1.00 18.88           C  
ANISOU  839  CD  GLU A  97     2009   2835   2331    453    194    194       C  
ATOM    840  OE1 GLU A  97      52.088  26.052  11.505  1.00 20.00           O  
ANISOU  840  OE1 GLU A  97     2251   3139   2210    -74    166    331       O  
ATOM    841  OE2 GLU A  97      51.333  27.117   9.748  1.00 22.25           O  
ANISOU  841  OE2 GLU A  97     2398   3422   2634    570     99    267       O  
ATOM    842  N   VAL A  98      55.552  23.657   7.397  1.00 12.45           N  
ANISOU  842  N   VAL A  98     1644   1364   1721     78   -118     38       N  
ATOM    843  CA  VAL A  98      55.960  22.346   6.877  1.00 12.27           C  
ANISOU  843  CA  VAL A  98     1637   1252   1774    -29   -199     72       C  
ATOM    844  C   VAL A  98      57.465  22.296   6.655  1.00 12.58           C  
ANISOU  844  C   VAL A  98     1743   1290   1749     59   -142    137       C  
ATOM    845  O   VAL A  98      58.128  21.342   7.044  1.00 13.75           O  
ANISOU  845  O   VAL A  98     1984   1412   1829    528   -161     -3       O  
ATOM    846  CB  VAL A  98      55.241  22.007   5.551  1.00 13.02           C  
ANISOU  846  CB  VAL A  98     1599   1331   2016    104   -139   -156       C  
ATOM    847  CG1 VAL A  98      55.889  20.788   4.871  1.00 13.86           C  
ANISOU  847  CG1 VAL A  98     1838   1234   2193    270   -316   -229       C  
ATOM    848  CG2 VAL A  98      53.772  21.744   5.799  1.00 13.66           C  
ANISOU  848  CG2 VAL A  98     1420   1487   2285     20    -69     81       C  
ATOM    849  N   ALA A  99      58.002  23.332   6.027  1.00 12.05           N  
ANISOU  849  N   ALA A  99     1727   1248   1604   -237    -28      9       N  
ATOM    850  CA  ALA A  99      59.423  23.379   5.711  1.00 12.82           C  
ANISOU  850  CA  ALA A  99     1733   1444   1692     79   -130    144       C  
ATOM    851  C   ALA A  99      60.294  23.441   6.972  1.00 12.20           C  
ANISOU  851  C   ALA A  99     1582   1398   1656    137    -88   -131       C  
ATOM    852  O   ALA A  99      61.330  22.782   7.031  1.00 12.42           O  
ANISOU  852  O   ALA A  99     1466   1543   1710    115    -18   -111       O  
ATOM    853  CB  ALA A  99      59.719  24.565   4.802  1.00 13.35           C  
ANISOU  853  CB  ALA A  99     1828   1488   1756     57   -188    171       C  
ATOM    854  N   LEU A 100      59.885  24.220   7.974  1.00 12.03           N  
ANISOU  854  N   LEU A 100     1491   1385   1693    -19    -29   -113       N  
ATOM    855  CA  LEU A 100      60.644  24.306   9.222  1.00 13.18           C  
ANISOU  855  CA  LEU A 100     1665   1501   1840    146    -68   -194       C  
ATOM    856  C   LEU A 100      60.754  22.937   9.896  1.00 12.56           C  
ANISOU  856  C   LEU A 100     1609   1617   1545     -8   -145   -170       C  
ATOM    857  O   LEU A 100      61.832  22.539  10.345  1.00 12.98           O  
ANISOU  857  O   LEU A 100     1478   1828   1625     19    -12    -30       O  
ATOM    858  CB  LEU A 100      60.004  25.303  10.191  1.00 14.15           C  
ANISOU  858  CB  LEU A 100     1815   1522   2038    231    156   -199       C  
ATOM    859  CG  LEU A 100      60.246  26.772   9.879  1.00 13.91           C  
ANISOU  859  CG  LEU A 100     1518   1548   2221    279     88   -125       C  
ATOM    860  CD1 LEU A 100      59.349  27.619  10.782  1.00 15.36           C  
ANISOU  860  CD1 LEU A 100     1780   1597   2458    419    418   -280       C  
ATOM    861  CD2 LEU A 100      61.711  27.122  10.087  1.00 13.87           C  
ANISOU  861  CD2 LEU A 100     1315   1766   2187    183   -180   -120       C  
ATOM    862  N   VAL A 101      59.634  22.222   9.960  1.00 12.49           N  
ANISOU  862  N   VAL A 101     1728   1471   1547    147    -85   -178       N  
ATOM    863  CA  VAL A 101      59.588  20.912  10.601  1.00 12.92           C  
ANISOU  863  CA  VAL A 101     1631   1519   1757    283    112     40       C  
ATOM    864  C   VAL A 101      60.431  19.902   9.822  1.00 15.04           C  
ANISOU  864  C   VAL A 101     2026   1695   1993    293    -20     79       C  
ATOM    865  O   VAL A 101      61.230  19.159  10.411  1.00 15.37           O  
ANISOU  865  O   VAL A 101     2010   1692   2138    494    196    373       O  
ATOM    866  CB  VAL A 101      58.143  20.402  10.718  1.00 12.97           C  
ANISOU  866  CB  VAL A 101     1563   1357   2010    316    270    261       C  
ATOM    867  CG1 VAL A 101      58.115  18.949  11.195  1.00 14.35           C  
ANISOU  867  CG1 VAL A 101     1805   1343   2303    246    180    422       C  
ATOM    868  CG2 VAL A 101      57.342  21.287  11.653  1.00 12.75           C  
ANISOU  868  CG2 VAL A 101     1380   1541   1923    469    290    100       C  
ATOM    869  N   GLU A 102      60.273  19.903   8.501  1.00 14.71           N  
ANISOU  869  N   GLU A 102     2122   1660   1807    290     72   -113       N  
ATOM    870  CA  GLU A 102      61.010  18.981   7.634  1.00 15.64           C  
ANISOU  870  CA  GLU A 102     2291   1621   2030    463     75    -98       C  
ATOM    871  C   GLU A 102      62.521  19.196   7.733  1.00 16.04           C  
ANISOU  871  C   GLU A 102     2255   1885   1952    340    141    104       C  
ATOM    872  O   GLU A 102      63.295  18.233   7.804  1.00 17.37           O  
ANISOU  872  O   GLU A 102     2325   2210   2064    749    433   -307       O  
ATOM    873  CB  GLU A 102      60.552  19.140   6.181  1.00 18.61           C  
ANISOU  873  CB  GLU A 102     2685   1927   2459    438     99   -470       C  
ATOM    874  CG  GLU A 102      61.232  18.196   5.190  1.00 21.20           C  
ANISOU  874  CG  GLU A 102     2897   2266   2890    579    -30   -369       C  
ATOM    875  CD  GLU A 102      60.728  16.775   5.299  1.00 23.72           C  
ANISOU  875  CD  GLU A 102     2977   2656   3379    665   -246   -297       C  
ATOM    876  OE1 GLU A 102      59.502  16.579   5.452  1.00 25.68           O  
ANISOU  876  OE1 GLU A 102     3170   2977   3612    599   -225    -56       O  
ATOM    877  OE2 GLU A 102      61.561  15.849   5.240  1.00 24.79           O  
ANISOU  877  OE2 GLU A 102     3004   2829   3587    702   -273   -416       O  
ATOM    878  N  AARG A 103      62.921  20.464   7.749  0.44 15.05           N  
ANISOU  878  N  AARG A 103     2004   1928   1786    178    147     57       N  
ATOM    879  N  BARG A 103      62.941  20.457   7.749  0.56 14.69           N  
ANISOU  879  N  BARG A 103     1887   1885   1810     99    206    158       N  
ATOM    880  CA AARG A 103      64.329  20.856   7.743  0.44 15.87           C  
ANISOU  880  CA AARG A 103     1963   2256   1812    228    136    107       C  
ATOM    881  CA BARG A 103      64.366  20.774   7.737  0.56 15.37           C  
ANISOU  881  CA BARG A 103     1752   2206   1884    182    244    289       C  
ATOM    882  C  AARG A 103      65.031  20.597   9.072  0.44 16.49           C  
ANISOU  882  C  AARG A 103     2085   2342   1840    297     98     91       C  
ATOM    883  C  BARG A 103      65.025  20.525   9.088  0.56 16.37           C  
ANISOU  883  C  BARG A 103     2037   2346   1839    354    160    234       C  
ATOM    884  O  AARG A 103      66.173  20.132   9.102  0.44 17.38           O  
ANISOU  884  O  AARG A 103     2268   2409   1927    382    140    141       O  
ATOM    885  O  BARG A 103      66.141  20.005   9.148  0.56 17.21           O  
ANISOU  885  O  BARG A 103     2315   2360   1863    593    218    405       O  
ATOM    886  CB AARG A 103      64.449  22.341   7.377  0.44 16.30           C  
ANISOU  886  CB AARG A 103     1868   2461   1864     98    186     71       C  
ATOM    887  CB BARG A 103      64.594  22.229   7.310  0.56 15.26           C  
ANISOU  887  CB BARG A 103     1424   2319   2058     34    404    314       C  
ATOM    888  CG AARG A 103      65.728  23.021   7.839  0.44 17.32           C  
ANISOU  888  CG AARG A 103     1968   2694   1919    102     97    -62       C  
ATOM    889  CG BARG A 103      66.063  22.642   7.230  0.56 16.60           C  
ANISOU  889  CG BARG A 103     1509   2540   2259     28    326    222       C  
ATOM    890  CD AARG A 103      66.942  22.527   7.074  0.44 17.80           C  
ANISOU  890  CD AARG A 103     1914   2764   2085     43     65    -56       C  
ATOM    891  CD BARG A 103      66.486  23.413   8.473  0.56 17.19           C  
ANISOU  891  CD BARG A 103     1593   2536   2403     37    300    130       C  
ATOM    892  NE AARG A 103      68.156  23.234   7.475  0.44 18.22           N  
ANISOU  892  NE AARG A 103     1923   2758   2243     84     35    -45       N  
ATOM    893  NE BARG A 103      67.869  23.887   8.421  0.56 17.24           N  
ANISOU  893  NE BARG A 103     1681   2488   2382      7    277     93       N  
ATOM    894  CZ AARG A 103      68.973  22.825   8.440  0.44 18.98           C  
ANISOU  894  CZ AARG A 103     2096   2690   2426    139     61     94       C  
ATOM    895  CZ BARG A 103      68.899  23.262   8.983  0.56 17.27           C  
ANISOU  895  CZ BARG A 103     1819   2425   2317    211    386     82       C  
ATOM    896  NH1AARG A 103      68.708  21.708   9.105  0.44 18.65           N  
ANISOU  896  NH1AARG A 103     2090   2480   2516    320    143     95       N  
ATOM    897  NH1BARG A 103      68.712  22.122   9.636  0.56 17.53           N  
ANISOU  897  NH1BARG A 103     1876   2569   2214    244    415     30       N  
ATOM    898  NH2AARG A 103      70.057  23.529   8.738  0.44 19.36           N  
ANISOU  898  NH2AARG A 103     2194   2657   2504     59    -32     97       N  
ATOM    899  NH2BARG A 103      70.119  23.774   8.890  0.56 18.09           N  
ANISOU  899  NH2BARG A 103     1947   2526   2400    408    427    147       N  
ATOM    900  N   TYR A 104      64.347  20.907  10.168  1.00 16.06           N  
ANISOU  900  N   TYR A 104     2027   2247   1827    382     62     46       N  
ATOM    901  CA  TYR A 104      64.973  20.869  11.480  1.00 13.97           C  
ANISOU  901  CA  TYR A 104     1795   1782   1732    639    142     90       C  
ATOM    902  C   TYR A 104      64.794  19.605  12.302  1.00 15.26           C  
ANISOU  902  C   TYR A 104     1833   2025   1940    373    138    155       C  
ATOM    903  O   TYR A 104      65.658  19.305  13.116  1.00 16.23           O  
ANISOU  903  O   TYR A 104     1892   2144   2132    525   -267    546       O  
ATOM    904  CB  TYR A 104      64.490  22.068  12.291  1.00 13.64           C  
ANISOU  904  CB  TYR A 104     1855   1500   1829    384     74     14       C  
ATOM    905  CG  TYR A 104      65.199  23.331  11.887  1.00 13.90           C  
ANISOU  905  CG  TYR A 104     1728   1627   1926    169     12    176       C  
ATOM    906  CD1 TYR A 104      66.572  23.441  12.032  1.00 14.48           C  
ANISOU  906  CD1 TYR A 104     1709   1633   2162    -14    -29    127       C  
ATOM    907  CD2 TYR A 104      64.505  24.410  11.352  1.00 14.25           C  
ANISOU  907  CD2 TYR A 104     1765   1677   1973    148   -102    143       C  
ATOM    908  CE1 TYR A 104      67.245  24.591  11.666  1.00 16.00           C  
ANISOU  908  CE1 TYR A 104     1866   1879   2332    150     -3    367       C  
ATOM    909  CE2 TYR A 104      65.170  25.568  10.989  1.00 15.04           C  
ANISOU  909  CE2 TYR A 104     1779   1890   2044    159    -34    396       C  
ATOM    910  CZ  TYR A 104      66.541  25.653  11.149  1.00 16.35           C  
ANISOU  910  CZ  TYR A 104     1950   1943   2320    135    -37    538       C  
ATOM    911  OH  TYR A 104      67.217  26.798  10.794  1.00 18.66           O  
ANISOU  911  OH  TYR A 104     2049   2274   2768    161     54    582       O  
ATOM    912  N   ASN A 105      63.701  18.871  12.123  1.00 14.39           N  
ANISOU  912  N   ASN A 105     1822   1708   1938    491    262    175       N  
ATOM    913  CA  ASN A 105      63.492  17.706  12.981  1.00 15.65           C  
ANISOU  913  CA  ASN A 105     1861   1963   2124    819    264    287       C  
ATOM    914  C   ASN A 105      64.593  16.642  12.914  1.00 17.88           C  
ANISOU  914  C   ASN A 105     2211   2167   2415    739    409    296       C  
ATOM    915  O   ASN A 105      64.936  16.086  13.951  1.00 17.01           O  
ANISOU  915  O   ASN A 105     1989   2259   2215    791    199    796       O  
ATOM    916  CB  ASN A 105      62.129  17.067  12.707  1.00 16.11           C  
ANISOU  916  CB  ASN A 105     2000   1929   2192    644    352     65       C  
ATOM    917  CG  ASN A 105      61.058  17.600  13.649  1.00 16.08           C  
ANISOU  917  CG  ASN A 105     1869   2063   2178    501    261    106       C  
ATOM    918  OD1 ASN A 105      61.350  18.427  14.502  1.00 17.14           O  
ANISOU  918  OD1 ASN A 105     1945   2261   2307    313    177     63       O  
ATOM    919  ND2 ASN A 105      59.829  17.130  13.503  1.00 15.72           N  
ANISOU  919  ND2 ASN A 105     1715   2063   2195    574    169    216       N  
ATOM    920  N   PRO A 106      65.161  16.365  11.722  1.00 19.02           N  
ANISOU  920  N   PRO A 106     2511   2159   2559   1134    514    257       N  
ATOM    921  CA  PRO A 106      66.248  15.374  11.731  1.00 22.09           C  
ANISOU  921  CA  PRO A 106     2687   2685   3021   1278    528    287       C  
ATOM    922  C   PRO A 106      67.436  15.768  12.619  1.00 23.69           C  
ANISOU  922  C   PRO A 106     2744   2752   3505   1278    230    602       C  
ATOM    923  O   PRO A 106      67.964  14.926  13.347  1.00 27.30           O  
ANISOU  923  O   PRO A 106     3017   3284   4071   1152    116    713       O  
ATOM    924  CB  PRO A 106      66.668  15.308  10.259  1.00 22.07           C  
ANISOU  924  CB  PRO A 106     2769   2728   2890   1262    538     31       C  
ATOM    925  CG  PRO A 106      65.440  15.676   9.507  1.00 21.48           C  
ANISOU  925  CG  PRO A 106     2885   2555   2722   1239    563   -227       C  
ATOM    926  CD  PRO A 106      64.764  16.727  10.348  1.00 20.21           C  
ANISOU  926  CD  PRO A 106     2736   2319   2625   1055    519     11       C  
ATOM    927  N   VAL A 107      67.845  17.030  12.565  1.00 22.94           N  
ANISOU  927  N   VAL A 107     2627   2604   3484   1105    232    463       N  
ATOM    928  CA  VAL A 107      68.981  17.497  13.344  1.00 23.01           C  
ANISOU  928  CA  VAL A 107     2708   2502   3534    712    229    570       C  
ATOM    929  C   VAL A 107      68.628  17.609  14.823  1.00 21.78           C  
ANISOU  929  C   VAL A 107     2431   2437   3409    588    -94    517       C  
ATOM    930  O   VAL A 107      69.426  17.264  15.694  1.00 23.74           O  
ANISOU  930  O   VAL A 107     2455   2912   3654    564   -229    378       O  
ATOM    931  CB  VAL A 107      69.487  18.856  12.813  1.00 26.16           C  
ANISOU  931  CB  VAL A 107     3170   2982   3787    299    262    608       C  
ATOM    932  CG1 VAL A 107      70.590  19.413  13.702  1.00 27.54           C  
ANISOU  932  CG1 VAL A 107     3361   3241   3861    254    308    605       C  
ATOM    933  CG2 VAL A 107      69.972  18.702  11.380  1.00 27.72           C  
ANISOU  933  CG2 VAL A 107     3403   3202   3927    242    257    607       C  
ATOM    934  N   LEU A 108      67.418  18.073  15.109  1.00 19.73           N  
ANISOU  934  N   LEU A 108     2092   2388   3017    626   -102    590       N  
ATOM    935  CA  LEU A 108      66.986  18.252  16.487  1.00 18.19           C  
ANISOU  935  CA  LEU A 108     1966   2270   2675    561     48    690       C  
ATOM    936  C   LEU A 108      66.760  16.914  17.203  1.00 19.13           C  
ANISOU  936  C   LEU A 108     2075   2433   2759    339     47    650       C  
ATOM    937  O   LEU A 108      66.937  16.825  18.418  1.00 18.67           O  
ANISOU  937  O   LEU A 108     1934   2483   2677    378   -128    725       O  
ATOM    938  CB  LEU A 108      65.720  19.103  16.530  1.00 16.07           C  
ANISOU  938  CB  LEU A 108     1751   2046   2310    424     88    551       C  
ATOM    939  CG  LEU A 108      65.936  20.570  16.173  1.00 16.33           C  
ANISOU  939  CG  LEU A 108     1882   2110   2214     83   -190    273       C  
ATOM    940  CD1 LEU A 108      64.600  21.275  16.100  1.00 16.03           C  
ANISOU  940  CD1 LEU A 108     1790   2024   2275    471    -68    251       C  
ATOM    941  CD2 LEU A 108      66.849  21.223  17.202  1.00 17.57           C  
ANISOU  941  CD2 LEU A 108     2308   2238   2129   -114   -161    344       C  
ATOM    942  N   ALA A 109      66.390  15.883  16.449  1.00 19.33           N  
ANISOU  942  N   ALA A 109     2207   2394   2746    367    -13    699       N  
ATOM    943  CA  ALA A 109      66.118  14.566  17.031  1.00 20.61           C  
ANISOU  943  CA  ALA A 109     2467   2570   2796    601    101    768       C  
ATOM    944  C   ALA A 109      67.336  13.997  17.751  1.00 21.71           C  
ANISOU  944  C   ALA A 109     2505   2823   2920    950    204    404       C  
ATOM    945  O   ALA A 109      67.192  13.271  18.733  1.00 21.84           O  
ANISOU  945  O   ALA A 109     2601   2895   2802    823    118    108       O  
ATOM    946  CB  ALA A 109      65.641  13.601  15.969  1.00 21.61           C  
ANISOU  946  CB  ALA A 109     2697   2620   2893    476    112    909       C  
ATOM    947  N  AARG A 110      68.529  14.334  17.267  0.44 23.05           N  
ANISOU  947  N  AARG A 110     2661   3085   3013   1029    281    392       N  
ATOM    948  N  BARG A 110      68.523  14.341  17.262  0.56 23.09           N  
ANISOU  948  N  BARG A 110     2644   3076   3051   1028    363    344       N  
ATOM    949  CA AARG A 110      69.778  13.905  17.903  0.44 24.14           C  
ANISOU  949  CA AARG A 110     2743   3286   3143   1027    305    487       C  
ATOM    950  CA BARG A 110      69.771  13.901  17.878  0.56 24.11           C  
ANISOU  950  CA BARG A 110     2703   3240   3218   1010    453    426       C  
ATOM    951  C  AARG A 110      69.894  14.419  19.330  0.44 23.15           C  
ANISOU  951  C  AARG A 110     2523   3170   3104   1067     78    632       C  
ATOM    952  C  BARG A 110      69.926  14.443  19.299  0.56 23.01           C  
ANISOU  952  C  BARG A 110     2452   3167   3124   1087    180    601       C  
ATOM    953  O  AARG A 110      70.611  13.845  20.156  0.44 24.27           O  
ANISOU  953  O  AARG A 110     2561   3419   3243   1283    -55    566       O  
ATOM    954  O  BARG A 110      70.700  13.903  20.094  0.56 24.34           O  
ANISOU  954  O  BARG A 110     2428   3533   3288   1346    102    444       O  
ATOM    955  CB AARG A 110      70.981  14.387  17.094  0.44 26.12           C  
ANISOU  955  CB AARG A 110     3032   3585   3308   1040    509    268       C  
ATOM    956  CB BARG A 110      70.965  14.333  17.024  0.56 26.03           C  
ANISOU  956  CB BARG A 110     3013   3401   3477    998    743    122       C  
ATOM    957  CG AARG A 110      71.052  13.815  15.704  0.44 27.91           C  
ANISOU  957  CG AARG A 110     3326   3832   3447   1029    706    205       C  
ATOM    958  CG BARG A 110      70.780  14.102  15.539  0.56 27.84           C  
ANISOU  958  CG BARG A 110     3353   3499   3725    917    989     24       C  
ATOM    959  CD AARG A 110      71.990  14.618  14.830  0.44 28.91           C  
ANISOU  959  CD AARG A 110     3470   3929   3584   1165    818    195       C  
ATOM    960  CD BARG A 110      72.116  14.081  14.801  0.56 29.06           C  
ANISOU  960  CD BARG A 110     3573   3509   3959    896   1102    -70       C  
ATOM    961  NE AARG A 110      71.632  14.498  13.422  0.44 28.78           N  
ANISOU  961  NE AARG A 110     3398   3916   3621   1442    990    223       N  
ATOM    962  NE BARG A 110      72.647  15.416  14.534  0.56 29.79           N  
ANISOU  962  NE BARG A 110     3728   3510   4083    867   1122   -132       N  
ATOM    963  CZ AARG A 110      71.970  15.383  12.493  0.44 28.40           C  
ANISOU  963  CZ AARG A 110     3342   3755   3693   1735   1057    315       C  
ATOM    964  CZ BARG A 110      73.522  16.047  15.310  0.56 31.02           C  
ANISOU  964  CZ BARG A 110     3908   3682   4198    865   1105   -167       C  
ATOM    965  NH1AARG A 110      72.678  16.454  12.827  0.44 28.86           N  
ANISOU  965  NH1AARG A 110     3397   3878   3692   1676   1150    276       N  
ATOM    966  NH1BARG A 110      73.976  15.477  16.417  0.56 31.74           N  
ANISOU  966  NH1BARG A 110     4012   3826   4223    906   1066   -171       N  
ATOM    967  NH2AARG A 110      71.601  15.198  11.232  0.44 28.05           N  
ANISOU  967  NH2AARG A 110     3250   3626   3783   1878    994    437       N  
ATOM    968  NH2BARG A 110      73.949  17.255  14.978  0.56 31.27           N  
ANISOU  968  NH2BARG A 110     3950   3671   4259    835   1114   -296       N  
ATOM    969  N   HIS A 111      69.187  15.506  19.616  1.00 22.40           N  
ANISOU  969  N   HIS A 111     2332   3113   3068    818    150    635       N  
ATOM    970  CA  HIS A 111      69.243  16.134  20.931  1.00 22.61           C  
ANISOU  970  CA  HIS A 111     2465   2904   3224    790   -112    494       C  
ATOM    971  C   HIS A 111      67.930  15.988  21.702  1.00 21.70           C  
ANISOU  971  C   HIS A 111     2387   2915   2945    899   -151    539       C  
ATOM    972  O   HIS A 111      67.696  16.691  22.687  1.00 22.60           O  
ANISOU  972  O   HIS A 111     2560   3149   2879    935   -335    365       O  
ATOM    973  CB  HIS A 111      69.603  17.616  20.783  1.00 25.11           C  
ANISOU  973  CB  HIS A 111     2806   3075   3657    412   -149    226       C  
ATOM    974  CG  HIS A 111      70.858  17.847  20.004  1.00 28.43           C  
ANISOU  974  CG  HIS A 111     3211   3593   3999    188   -136     30       C  
ATOM    975  ND1 HIS A 111      72.107  17.819  20.585  1.00 30.33           N  
ANISOU  975  ND1 HIS A 111     3411   3962   4152     49   -203    -13       N  
ATOM    976  CD2 HIS A 111      71.059  18.095  18.688  1.00 30.06           C  
ANISOU  976  CD2 HIS A 111     3370   3877   4175    208   -164   -188       C  
ATOM    977  CE1 HIS A 111      73.024  18.046  19.662  1.00 31.51           C  
ANISOU  977  CE1 HIS A 111     3505   4240   4227      4   -265    -89       C  
ATOM    978  NE2 HIS A 111      72.414  18.218  18.502  1.00 31.96           N  
ANISOU  978  NE2 HIS A 111     3609   4250   4284     31   -183   -280       N  
ATOM    979  N   GLY A 112      67.071  15.091  21.228  1.00 19.42           N  
ANISOU  979  N   GLY A 112     2175   2434   2769    918     60    607       N  
ATOM    980  CA  GLY A 112      65.782  14.846  21.854  1.00 19.66           C  
ANISOU  980  CA  GLY A 112     2255   2536   2678    939    194    582       C  
ATOM    981  C   GLY A 112      64.784  15.985  21.726  1.00 18.22           C  
ANISOU  981  C   GLY A 112     2168   2263   2490    750    112    686       C  
ATOM    982  O   GLY A 112      63.850  16.100  22.523  1.00 19.48           O  
ANISOU  982  O   GLY A 112     2426   2385   2591    810    215    828       O  
ATOM    983  N   ILE A 113      64.975  16.826  20.717  1.00 16.95           N  
ANISOU  983  N   ILE A 113     1884   2090   2467    632    -15    373       N  
ATOM    984  CA  ILE A 113      64.100  17.968  20.491  1.00 15.53           C  
ANISOU  984  CA  ILE A 113     1618   1941   2341    555   -128    388       C  
ATOM    985  C   ILE A 113      63.274  17.715  19.242  1.00 14.20           C  
ANISOU  985  C   ILE A 113     1538   1757   2102    581     23    350       C  
ATOM    986  O   ILE A 113      63.766  17.136  18.271  1.00 14.62           O  
ANISOU  986  O   ILE A 113     1758   1831   1967    414     19    260       O  
ATOM    987  CB  ILE A 113      64.907  19.273  20.366  1.00 15.56           C  
ANISOU  987  CB  ILE A 113     1394   2197   2321    541   -293    482       C  
ATOM    988  CG1 ILE A 113      65.705  19.520  21.645  1.00 16.79           C  
ANISOU  988  CG1 ILE A 113     1599   2399   2383    220   -108    429       C  
ATOM    989  CG2 ILE A 113      63.995  20.475  20.081  1.00 14.70           C  
ANISOU  989  CG2 ILE A 113     1438   1882   2266    464   -257    518       C  
ATOM    990  CD1 ILE A 113      66.863  20.471  21.458  1.00 18.05           C  
ANISOU  990  CD1 ILE A 113     1763   2611   2484      3    -28    473       C  
ATOM    991  N   ARG A 114      62.011  18.133  19.272  1.00 14.13           N  
ANISOU  991  N   ARG A 114     1364   1968   2037    624     19    336       N  
ATOM    992  CA  ARG A 114      61.091  17.855  18.184  1.00 15.12           C  
ANISOU  992  CA  ARG A 114     1573   1910   2262    429    -31    294       C  
ATOM    993  C   ARG A 114      60.124  18.999  17.949  1.00 13.46           C  
ANISOU  993  C   ARG A 114     1504   1649   1960    404    -22    312       C  
ATOM    994  O   ARG A 114      59.558  19.537  18.900  1.00 14.19           O  
ANISOU  994  O   ARG A 114     1752   1783   1857    498    -10    286       O  
ATOM    995  CB  ARG A 114      60.309  16.568  18.466  1.00 17.47           C  
ANISOU  995  CB  ARG A 114     1838   2226   2573    -97    -99    218       C  
ATOM    996  CG  ARG A 114      59.407  16.127  17.314  1.00 19.26           C  
ANISOU  996  CG  ARG A 114     2191   2382   2745   -262   -133    192       C  
ATOM    997  CD  ARG A 114      58.651  14.851  17.667  1.00 20.88           C  
ANISOU  997  CD  ARG A 114     2516   2550   2866   -391    113    333       C  
ATOM    998  NE  ARG A 114      57.734  15.045  18.785  1.00 23.26           N  
ANISOU  998  NE  ARG A 114     2887   2706   3245   -139    340    108       N  
ATOM    999  CZ  ARG A 114      57.170  14.051  19.465  1.00 24.80           C  
ANISOU  999  CZ  ARG A 114     3365   2762   3296   -330    586   -108       C  
ATOM   1000  NH1 ARG A 114      57.433  12.792  19.136  1.00 26.05           N  
ANISOU 1000  NH1 ARG A 114     3669   2786   3445   -261    444   -120       N  
ATOM   1001  NH2 ARG A 114      56.338  14.313  20.465  1.00 25.13           N  
ANISOU 1001  NH2 ARG A 114     3402   3007   3137   -470    680   -148       N  
ATOM   1002  N   LEU A 115      59.964  19.367  16.681  1.00 12.73           N  
ANISOU 1002  N   LEU A 115     1353   1577   1905    418   -125    430       N  
ATOM   1003  CA  LEU A 115      58.983  20.355  16.252  1.00 12.60           C  
ANISOU 1003  CA  LEU A 115     1252   1705   1830    -58    -18    374       C  
ATOM   1004  C   LEU A 115      57.731  19.689  15.688  1.00 13.17           C  
ANISOU 1004  C   LEU A 115     1370   1847   1787     46    -16    173       C  
ATOM   1005  O   LEU A 115      57.807  18.668  15.010  1.00 14.25           O  
ANISOU 1005  O   LEU A 115     1820   1612   1984    258     11    -75       O  
ATOM   1006  CB  LEU A 115      59.586  21.264  15.179  1.00 11.79           C  
ANISOU 1006  CB  LEU A 115     1017   1706   1758     76    267    292       C  
ATOM   1007  CG  LEU A 115      60.922  21.948  15.486  1.00 12.63           C  
ANISOU 1007  CG  LEU A 115     1164   1894   1742    -53    320     13       C  
ATOM   1008  CD1 LEU A 115      61.339  22.814  14.315  1.00 13.53           C  
ANISOU 1008  CD1 LEU A 115     1424   1912   1806    -35    271    146       C  
ATOM   1009  CD2 LEU A 115      60.866  22.779  16.770  1.00 13.45           C  
ANISOU 1009  CD2 LEU A 115     1345   2045   1719     33    335   -285       C  
ATOM   1010  N   THR A 116      56.584  20.312  15.919  1.00 12.58           N  
ANISOU 1010  N   THR A 116     1390   1751   1639     -8    178    445       N  
ATOM   1011  CA  THR A 116      55.327  19.834  15.378  1.00 12.75           C  
ANISOU 1011  CA  THR A 116     1455   1514   1873     94    -36    362       C  
ATOM   1012  C   THR A 116      54.477  21.020  14.927  1.00 13.29           C  
ANISOU 1012  C   THR A 116     1666   1569   1813     18     57    224       C  
ATOM   1013  O   THR A 116      54.168  21.899  15.733  1.00 13.08           O  
ANISOU 1013  O   THR A 116     1839   1642   1489   -236    -28    -91       O  
ATOM   1014  CB  THR A 116      54.543  19.019  16.414  1.00 15.74           C  
ANISOU 1014  CB  THR A 116     1954   1694   2334    -80   -326    571       C  
ATOM   1015  OG1 THR A 116      55.354  17.935  16.889  1.00 18.20           O  
ANISOU 1015  OG1 THR A 116     2501   1995   2420    -31   -208    658       O  
ATOM   1016  CG2 THR A 116      53.266  18.468  15.798  1.00 16.41           C  
ANISOU 1016  CG2 THR A 116     1947   1867   2422   -351   -403    675       C  
ATOM   1017  N   ALA A 117      54.111  21.056  13.649  1.00 12.66           N  
ANISOU 1017  N   ALA A 117     1639   1288   1882    257    -75    229       N  
ATOM   1018  CA  ALA A 117      53.242  22.126  13.136  1.00 12.99           C  
ANISOU 1018  CA  ALA A 117     1505   1594   1836    449    -34     -4       C  
ATOM   1019  C   ALA A 117      51.840  21.955  13.701  1.00 13.46           C  
ANISOU 1019  C   ALA A 117     1341   1643   2131    -92   -199   -227       C  
ATOM   1020  O   ALA A 117      51.300  20.845  13.715  1.00 14.68           O  
ANISOU 1020  O   ALA A 117     1547   1826   2204   -279   -301      7       O  
ATOM   1021  CB  ALA A 117      53.217  22.126  11.611  1.00 13.42           C  
ANISOU 1021  CB  ALA A 117     2006   1454   1639    477     20   -120       C  
ATOM   1022  N   LEU A 118      51.260  23.047  14.193  1.00 12.12           N  
ANISOU 1022  N   LEU A 118     1112   1395   2098    289      2   -119       N  
ATOM   1023  CA  LEU A 118      49.963  22.953  14.857  1.00 13.58           C  
ANISOU 1023  CA  LEU A 118     1315   1842   2003    244    -77   -241       C  
ATOM   1024  C   LEU A 118      48.848  23.204  13.845  1.00 16.01           C  
ANISOU 1024  C   LEU A 118     1866   2029   2188     24   -206   -144       C  
ATOM   1025  O   LEU A 118      48.221  24.262  13.815  1.00 17.32           O  
ANISOU 1025  O   LEU A 118     1998   2146   2438    177   -221     12       O  
ATOM   1026  CB  LEU A 118      49.885  23.922  16.040  1.00 14.12           C  
ANISOU 1026  CB  LEU A 118     1487   1921   1957    256    -77     41       C  
ATOM   1027  CG  LEU A 118      50.926  23.656  17.132  1.00 14.39           C  
ANISOU 1027  CG  LEU A 118     1716   1870   1882     39    -74     86       C  
ATOM   1028  CD1 LEU A 118      50.814  24.672  18.256  1.00 14.54           C  
ANISOU 1028  CD1 LEU A 118     1871   1946   1706   -152     -8     -5       C  
ATOM   1029  CD2 LEU A 118      50.757  22.239  17.668  1.00 14.46           C  
ANISOU 1029  CD2 LEU A 118     1540   1899   2054    -77    136    222       C  
ATOM   1030  N   PHE A 119      48.614  22.209  13.000  1.00 17.25           N  
ANISOU 1030  N   PHE A 119     2170   2321   2063   -232   -292   -170       N  
ATOM   1031  CA  PHE A 119      47.585  22.319  11.979  1.00 19.29           C  
ANISOU 1031  CA  PHE A 119     2212   2714   2404    -89   -215   -193       C  
ATOM   1032  C   PHE A 119      46.231  21.968  12.574  1.00 21.98           C  
ANISOU 1032  C   PHE A 119     2358   3207   2785    -51   -401     11       C  
ATOM   1033  O   PHE A 119      46.126  21.699  13.769  1.00 21.06           O  
ANISOU 1033  O   PHE A 119     2350   3043   2611     -6   -331   -145       O  
ATOM   1034  CB  PHE A 119      47.929  21.421  10.792  1.00 18.77           C  
ANISOU 1034  CB  PHE A 119     2325   2492   2316    -87   -208   -499       C  
ATOM   1035  CG  PHE A 119      49.112  21.904  10.012  1.00 19.60           C  
ANISOU 1035  CG  PHE A 119     2523   2647   2278   -187   -247   -566       C  
ATOM   1036  CD1 PHE A 119      49.321  23.265   9.826  1.00 19.92           C  
ANISOU 1036  CD1 PHE A 119     2716   2651   2200   -141   -129   -421       C  
ATOM   1037  CD2 PHE A 119      50.017  21.013   9.460  1.00 19.53           C  
ANISOU 1037  CD2 PHE A 119     2360   2726   2335    114   -282   -382       C  
ATOM   1038  CE1 PHE A 119      50.410  23.725   9.109  1.00 20.74           C  
ANISOU 1038  CE1 PHE A 119     2857   2807   2217    -44   -149   -324       C  
ATOM   1039  CE2 PHE A 119      51.112  21.470   8.737  1.00 20.72           C  
ANISOU 1039  CE2 PHE A 119     2692   2785   2395     63   -373   -233       C  
ATOM   1040  CZ  PHE A 119      51.306  22.823   8.560  1.00 21.35           C  
ANISOU 1040  CZ  PHE A 119     2888   2926   2300    -62   -331   -285       C  
ATOM   1041  N   LYS A 120      45.198  21.972  11.741  1.00 26.15           N  
ANISOU 1041  N   LYS A 120     2611   3988   3336    -69   -360    270       N  
ATOM   1042  CA  LYS A 120      43.831  21.854  12.236  1.00 29.39           C  
ANISOU 1042  CA  LYS A 120     2943   4620   3603   -108   -537    283       C  
ATOM   1043  C   LYS A 120      43.620  20.649  13.151  1.00 28.17           C  
ANISOU 1043  C   LYS A 120     2635   4748   3323   -235   -497     46       C  
ATOM   1044  O   LYS A 120      43.932  19.513  12.788  1.00 29.01           O  
ANISOU 1044  O   LYS A 120     2584   5021   3417   -139   -439     25       O  
ATOM   1045  CB  LYS A 120      42.867  21.784  11.060  1.00 32.84           C  
ANISOU 1045  CB  LYS A 120     3475   5021   3980    124   -759    439       C  
ATOM   1046  CG  LYS A 120      41.589  22.542  11.295  1.00 36.56           C  
ANISOU 1046  CG  LYS A 120     4114   5286   4493    230   -695    430       C  
ATOM   1047  CD  LYS A 120      41.167  23.233  10.027  1.00 38.85           C  
ANISOU 1047  CD  LYS A 120     4461   5419   4883    293   -613    432       C  
ATOM   1048  CE  LYS A 120      39.901  24.015  10.242  1.00 40.06           C  
ANISOU 1048  CE  LYS A 120     4687   5446   5087    374   -546    482       C  
ATOM   1049  NZ  LYS A 120      39.836  25.155   9.296  1.00 40.91           N  
ANISOU 1049  NZ  LYS A 120     4797   5572   5176    340   -426    399       N  
ATOM   1050  N   GLY A 121      43.101  20.909  14.345  1.00 26.51           N  
ANISOU 1050  N   GLY A 121     2435   4554   3082   -436   -524   -136       N  
ATOM   1051  CA  GLY A 121      42.789  19.840  15.275  1.00 25.62           C  
ANISOU 1051  CA  GLY A 121     2364   4316   3054   -548   -444   -211       C  
ATOM   1052  C   GLY A 121      43.852  19.611  16.333  1.00 24.99           C  
ANISOU 1052  C   GLY A 121     2507   4006   2984   -662   -253   -122       C  
ATOM   1053  O   GLY A 121      43.608  18.926  17.325  1.00 26.51           O  
ANISOU 1053  O   GLY A 121     2898   4151   3025   -506    -84    -25       O  
ATOM   1054  N   GLN A 122      45.029  20.193  16.133  1.00 22.12           N  
ANISOU 1054  N   GLN A 122     2070   3501   2833   -760    -94   -235       N  
ATOM   1055  CA  GLN A 122      46.156  19.959  17.033  1.00 20.44           C  
ANISOU 1055  CA  GLN A 122     2167   2961   2639   -466   -217    -55       C  
ATOM   1056  C   GLN A 122      46.361  21.059  18.069  1.00 19.53           C  
ANISOU 1056  C   GLN A 122     2339   2630   2453   -317    -71    175       C  
ATOM   1057  O   GLN A 122      47.028  20.842  19.083  1.00 18.89           O  
ANISOU 1057  O   GLN A 122     2329   2628   2221   -294   -136    247       O  
ATOM   1058  CB  GLN A 122      47.448  19.807  16.231  1.00 20.74           C  
ANISOU 1058  CB  GLN A 122     2302   2844   2734   -207   -242   -290       C  
ATOM   1059  CG  GLN A 122      47.537  18.562  15.393  1.00 21.97           C  
ANISOU 1059  CG  GLN A 122     2429   2902   3015   -190   -238   -355       C  
ATOM   1060  CD  GLN A 122      48.780  18.569  14.537  1.00 25.16           C  
ANISOU 1060  CD  GLN A 122     2727   3541   3291   -163   -347   -194       C  
ATOM   1061  OE1 GLN A 122      49.874  18.261  15.010  1.00 28.49           O  
ANISOU 1061  OE1 GLN A 122     2984   4260   3581   -103   -578   -224       O  
ATOM   1062  NE2 GLN A 122      48.626  18.939  13.274  1.00 24.24           N  
ANISOU 1062  NE2 GLN A 122     2729   3321   3160   -384   -339    -28       N  
ATOM   1063  N   LYS A 123      45.809  22.238  17.825  1.00 19.27           N  
ANISOU 1063  N   LYS A 123     2495   2321   2507   -283   -151    390       N  
ATOM   1064  CA  LYS A 123      46.197  23.390  18.624  1.00 19.87           C  
ANISOU 1064  CA  LYS A 123     2679   2259   2612   -113   -453    469       C  
ATOM   1065  C   LYS A 123      45.652  23.350  20.057  1.00 19.43           C  
ANISOU 1065  C   LYS A 123     2503   2282   2600   -157   -414    223       C  
ATOM   1066  O   LYS A 123      46.352  23.740  20.990  1.00 19.57           O  
ANISOU 1066  O   LYS A 123     2715   2042   2678    -37   -571    231       O  
ATOM   1067  CB  LYS A 123      45.767  24.684  17.923  1.00 20.63           C  
ANISOU 1067  CB  LYS A 123     2815   2191   2833     64   -569    588       C  
ATOM   1068  CG  LYS A 123      46.420  25.914  18.498  1.00 22.04           C  
ANISOU 1068  CG  LYS A 123     2898   2431   3044    192   -415    492       C  
ATOM   1069  CD  LYS A 123      46.329  27.108  17.545  1.00 21.84           C  
ANISOU 1069  CD  LYS A 123     2790   2445   3062    130    107    608       C  
ATOM   1070  CE  LYS A 123      47.414  27.091  16.470  1.00 20.69           C  
ANISOU 1070  CE  LYS A 123     2519   2289   3053    244    238    562       C  
ATOM   1071  NZ  LYS A 123      47.402  28.376  15.702  1.00 20.41           N  
ANISOU 1071  NZ  LYS A 123     2477   2296   2982    231    130    343       N  
ATOM   1072  N   GLY A 124      44.422  22.868  20.230  1.00 19.37           N  
ANISOU 1072  N   GLY A 124     2417   2436   2508    -96     86    293       N  
ATOM   1073  CA  GLY A 124      43.791  22.836  21.541  1.00 19.18           C  
ANISOU 1073  CA  GLY A 124     2148   2661   2479     17     10    216       C  
ATOM   1074  C   GLY A 124      44.590  22.084  22.589  1.00 18.36           C  
ANISOU 1074  C   GLY A 124     1881   2703   2393    -28    219    188       C  
ATOM   1075  O   GLY A 124      44.801  22.586  23.692  1.00 18.70           O  
ANISOU 1075  O   GLY A 124     1814   2946   2346    -62    -12     -2       O  
ATOM   1076  N   LEU A 125      45.046  20.887  22.241  1.00 17.49           N  
ANISOU 1076  N   LEU A 125     1817   2486   2343    -47    513    315       N  
ATOM   1077  CA  LEU A 125      45.830  20.080  23.171  1.00 16.93           C  
ANISOU 1077  CA  LEU A 125     1908   2222   2303     76    396    236       C  
ATOM   1078  C   LEU A 125      47.200  20.699  23.401  1.00 15.47           C  
ANISOU 1078  C   LEU A 125     1658   2182   2037    179    520    274       C  
ATOM   1079  O   LEU A 125      47.685  20.765  24.535  1.00 14.84           O  
ANISOU 1079  O   LEU A 125     1807   2147   1685     20    366    219       O  
ATOM   1080  CB  LEU A 125      45.967  18.642  22.652  1.00 17.31           C  
ANISOU 1080  CB  LEU A 125     2061   2071   2445    -39    396    161       C  
ATOM   1081  CG  LEU A 125      46.852  17.704  23.475  1.00 18.92           C  
ANISOU 1081  CG  LEU A 125     2411   2145   2631   -162    481      1       C  
ATOM   1082  CD1 LEU A 125      46.281  17.484  24.868  1.00 19.46           C  
ANISOU 1082  CD1 LEU A 125     2612   2329   2453   -230    383    276       C  
ATOM   1083  CD2 LEU A 125      47.002  16.377  22.754  1.00 19.58           C  
ANISOU 1083  CD2 LEU A 125     2508   2050   2879   -156    500    -78       C  
ATOM   1084  N   ALA A 126      47.811  21.188  22.326  1.00 14.01           N  
ANISOU 1084  N   ALA A 126     1369   1953   2002    142    355    169       N  
ATOM   1085  CA  ALA A 126      49.123  21.801  22.432  1.00 12.48           C  
ANISOU 1085  CA  ALA A 126     1069   1856   1816     69    472    306       C  
ATOM   1086  C   ALA A 126      49.101  23.001  23.379  1.00 14.33           C  
ANISOU 1086  C   ALA A 126     1476   2089   1881     42    206    324       C  
ATOM   1087  O   ALA A 126      49.966  23.125  24.248  1.00 14.49           O  
ANISOU 1087  O   ALA A 126     1630   2042   1833   -240    235    456       O  
ATOM   1088  CB  ALA A 126      49.624  22.212  21.054  1.00 14.11           C  
ANISOU 1088  CB  ALA A 126     1318   2153   1890    -50    506    377       C  
ATOM   1089  N   LEU A 127      48.108  23.878  23.217  1.00 15.57           N  
ANISOU 1089  N   LEU A 127     1791   2265   1860      1    185    356       N  
ATOM   1090  CA  LEU A 127      47.983  25.058  24.068  1.00 15.61           C  
ANISOU 1090  CA  LEU A 127     1929   2231   1770   -126    116    250       C  
ATOM   1091  C   LEU A 127      47.709  24.657  25.521  1.00 14.87           C  
ANISOU 1091  C   LEU A 127     1783   2145   1724   -293    250    263       C  
ATOM   1092  O   LEU A 127      48.213  25.287  26.447  1.00 15.70           O  
ANISOU 1092  O   LEU A 127     1958   2225   1782   -351    206    -63       O  
ATOM   1093  CB  LEU A 127      46.877  25.988  23.558  1.00 16.33           C  
ANISOU 1093  CB  LEU A 127     2025   2224   1955    -34     17    232       C  
ATOM   1094  CG  LEU A 127      47.175  26.607  22.189  1.00 18.52           C  
ANISOU 1094  CG  LEU A 127     2368   2492   2176     31    221    275       C  
ATOM   1095  CD1 LEU A 127      46.047  27.525  21.735  1.00 19.76           C  
ANISOU 1095  CD1 LEU A 127     2648   2573   2287    513    295    287       C  
ATOM   1096  CD2 LEU A 127      48.502  27.353  22.223  1.00 19.11           C  
ANISOU 1096  CD2 LEU A 127     2443   2544   2271   -420    474    376       C  
ATOM   1097  N   THR A 128      46.917  23.605  25.704  1.00 14.35           N  
ANISOU 1097  N   THR A 128     1597   2026   1830   -185    339    427       N  
ATOM   1098  CA  THR A 128      46.618  23.109  27.043  1.00 15.52           C  
ANISOU 1098  CA  THR A 128     1690   2110   2096   -362    414    355       C  
ATOM   1099  C   THR A 128      47.879  22.610  27.722  1.00 15.85           C  
ANISOU 1099  C   THR A 128     1751   2165   2108   -160    443    463       C  
ATOM   1100  O   THR A 128      48.129  22.913  28.897  1.00 18.50           O  
ANISOU 1100  O   THR A 128     2082   2568   2377   -188    338    522       O  
ATOM   1101  CB  THR A 128      45.579  21.984  27.007  1.00 15.94           C  
ANISOU 1101  CB  THR A 128     1641   2268   2147   -360    569    486       C  
ATOM   1102  OG1 THR A 128      44.362  22.489  26.445  1.00 16.97           O  
ANISOU 1102  OG1 THR A 128     1713   2582   2155   -422    359    190       O  
ATOM   1103  CG2 THR A 128      45.318  21.442  28.420  1.00 16.16           C  
ANISOU 1103  CG2 THR A 128     1699   2372   2068   -218    491    645       C  
ATOM   1104  N   ARG A 129      48.674  21.848  26.981  1.00 16.58           N  
ANISOU 1104  N   ARG A 129     1889   2157   2254    -25    446    385       N  
ATOM   1105  CA  ARG A 129      49.925  21.326  27.512  1.00 15.80           C  
ANISOU 1105  CA  ARG A 129     1755   2072   2174    116    312    213       C  
ATOM   1106  C   ARG A 129      50.919  22.454  27.765  1.00 17.12           C  
ANISOU 1106  C   ARG A 129     1971   2251   2282    126    291    385       C  
ATOM   1107  O   ARG A 129      51.724  22.372  28.688  1.00 19.08           O  
ANISOU 1107  O   ARG A 129     2298   2487   2466      6    171    504       O  
ATOM   1108  CB  ARG A 129      50.507  20.278  26.560  1.00 15.72           C  
ANISOU 1108  CB  ARG A 129     1833   2042   2099     51    299    265       C  
ATOM   1109  CG  ARG A 129      49.632  19.036  26.425  1.00 16.00           C  
ANISOU 1109  CG  ARG A 129     2022   1945   2111    106    299    271       C  
ATOM   1110  CD  ARG A 129      50.152  18.106  25.342  1.00 15.60           C  
ANISOU 1110  CD  ARG A 129     1938   1922   2069    213    379    351       C  
ATOM   1111  NE  ARG A 129      51.492  17.617  25.656  1.00 15.81           N  
ANISOU 1111  NE  ARG A 129     2011   1948   2049    324    295    433       N  
ATOM   1112  CZ  ARG A 129      52.516  17.609  24.805  1.00 17.56           C  
ANISOU 1112  CZ  ARG A 129     2198   2271   2205    432    221    315       C  
ATOM   1113  NH1 ARG A 129      52.375  18.086  23.571  1.00 18.53           N  
ANISOU 1113  NH1 ARG A 129     2362   2519   2160    320    348    354       N  
ATOM   1114  NH2 ARG A 129      53.695  17.144  25.196  1.00 17.61           N  
ANISOU 1114  NH2 ARG A 129     2002   2327   2360    286    119    126       N  
ATOM   1115  N   MET A 130      50.841  23.519  26.963  1.00 16.88           N  
ANISOU 1115  N   MET A 130     1982   2106   2325    179    316    486       N  
ATOM   1116  CA  MET A 130      51.669  24.705  27.165  1.00 17.11           C  
ANISOU 1116  CA  MET A 130     2084   2117   2302    266    190    332       C  
ATOM   1117  C   MET A 130      51.288  25.479  28.413  1.00 17.71           C  
ANISOU 1117  C   MET A 130     2221   2058   2451   -114    148     74       C  
ATOM   1118  O   MET A 130      52.093  26.242  28.949  1.00 19.11           O  
ANISOU 1118  O   MET A 130     2309   2331   2622   -344    132    199       O  
ATOM   1119  CB  MET A 130      51.564  25.650  25.966  1.00 17.33           C  
ANISOU 1119  CB  MET A 130     2064   2285   2235    210    226    365       C  
ATOM   1120  CG  MET A 130      52.413  25.276  24.786  1.00 18.96           C  
ANISOU 1120  CG  MET A 130     2236   2691   2277    328    276    332       C  
ATOM   1121  SD  MET A 130      52.281  26.550  23.524  1.00 20.34           S  
ANISOU 1121  SD  MET A 130     2453   2912   2363    349    511    462       S  
ATOM   1122  CE  MET A 130      53.034  25.702  22.141  1.00 20.51           C  
ANISOU 1122  CE  MET A 130     2621   2848   2326    379    573    163       C  
ATOM   1123  N   GLY A 131      50.043  25.310  28.848  1.00 17.24           N  
ANISOU 1123  N   GLY A 131     2217   1940   2392     37    281     62       N  
ATOM   1124  CA  GLY A 131      49.522  26.047  29.981  1.00 18.26           C  
ANISOU 1124  CA  GLY A 131     2374   2143   2421     68    119     56       C  
ATOM   1125  C   GLY A 131      49.029  27.427  29.599  1.00 18.41           C  
ANISOU 1125  C   GLY A 131     2520   2110   2366     16    152    -93       C  
ATOM   1126  O   GLY A 131      48.997  28.321  30.440  1.00 20.86           O  
ANISOU 1126  O   GLY A 131     2950   2342   2634    126    -76   -249       O  
ATOM   1127  N   VAL A 132      48.649  27.608  28.334  1.00 17.04           N  
ANISOU 1127  N   VAL A 132     2125   2025   2326    -42    297     79       N  
ATOM   1128  CA  VAL A 132      48.189  28.915  27.859  1.00 16.39           C  
ANISOU 1128  CA  VAL A 132     2014   1865   2349   -164    512      7       C  
ATOM   1129  C   VAL A 132      46.811  28.884  27.197  1.00 15.88           C  
ANISOU 1129  C   VAL A 132     2011   1814   2208   -282    521    366       C  
ATOM   1130  O   VAL A 132      46.380  29.871  26.599  1.00 17.36           O  
ANISOU 1130  O   VAL A 132     2106   2022   2468    -86    237    409       O  
ATOM   1131  CB  VAL A 132      49.191  29.560  26.848  1.00 18.03           C  
ANISOU 1131  CB  VAL A 132     2222   1959   2668   -357    180   -158       C  
ATOM   1132  CG1 VAL A 132      50.539  29.821  27.505  1.00 19.76           C  
ANISOU 1132  CG1 VAL A 132     2414   2282   2814   -528    -15   -285       C  
ATOM   1133  CG2 VAL A 132      49.347  28.711  25.589  1.00 17.90           C  
ANISOU 1133  CG2 VAL A 132     2289   1745   2769   -275    208   -306       C  
ATOM   1134  N   ALA A 133      46.102  27.769  27.309  1.00 16.04           N  
ANISOU 1134  N   ALA A 133     1889   1933   2273    -77    568    112       N  
ATOM   1135  CA  ALA A 133      44.789  27.657  26.684  1.00 16.37           C  
ANISOU 1135  CA  ALA A 133     1791   2022   2409    102    568    250       C  
ATOM   1136  C   ALA A 133      43.807  28.660  27.269  1.00 16.64           C  
ANISOU 1136  C   ALA A 133     1820   2221   2282    231    657    255       C  
ATOM   1137  O   ALA A 133      43.833  28.916  28.470  1.00 18.71           O  
ANISOU 1137  O   ALA A 133     2121   2777   2211    -90    673    147       O  
ATOM   1138  CB  ALA A 133      44.248  26.246  26.848  1.00 17.44           C  
ANISOU 1138  CB  ALA A 133     1849   2039   2740   -240    451    419       C  
ATOM   1139  N   ASP A 134      42.956  29.215  26.404  1.00 16.31           N  
ANISOU 1139  N   ASP A 134     1691   2023   2484    123    557    394       N  
ATOM   1140  CA  ASP A 134      41.899  30.163  26.780  1.00 17.39           C  
ANISOU 1140  CA  ASP A 134     1936   1989   2681   -244    761    213       C  
ATOM   1141  C   ASP A 134      42.393  31.503  27.313  1.00 20.66           C  
ANISOU 1141  C   ASP A 134     2420   2437   2991   -445    779    -89       C  
ATOM   1142  O   ASP A 134      41.646  32.232  27.958  1.00 24.63           O  
ANISOU 1142  O   ASP A 134     2969   2828   3559   -307    666   -352       O  
ATOM   1143  CB  ASP A 134      40.966  29.521  27.810  1.00 17.73           C  
ANISOU 1143  CB  ASP A 134     1946   2130   2661   -205    675      4       C  
ATOM   1144  CG  ASP A 134      40.339  28.262  27.287  1.00 18.70           C  
ANISOU 1144  CG  ASP A 134     2172   2285   2648   -428    461    297       C  
ATOM   1145  OD1 ASP A 134      39.563  28.363  26.311  1.00 20.61           O  
ANISOU 1145  OD1 ASP A 134     2235   2587   3008   -349    441    487       O  
ATOM   1146  OD2 ASP A 134      40.634  27.179  27.831  1.00 18.61           O  
ANISOU 1146  OD2 ASP A 134     2320   2248   2503   -465    437    203       O  
ATOM   1147  N   ARG A 135      43.644  31.836  27.040  1.00 20.11           N  
ANISOU 1147  N   ARG A 135     2651   2248   2740   -767    954     -6       N  
ATOM   1148  CA  ARG A 135      44.115  33.189  27.314  1.00 21.77           C  
ANISOU 1148  CA  ARG A 135     2969   2475   2829   -845    971    -94       C  
ATOM   1149  C   ARG A 135      43.963  34.036  26.062  1.00 22.73           C  
ANISOU 1149  C   ARG A 135     3101   2462   3075   -617   1089   -103       C  
ATOM   1150  O   ARG A 135      44.145  33.544  24.951  1.00 23.50           O  
ANISOU 1150  O   ARG A 135     3253   2678   2998   -780   1287   -207       O  
ATOM   1151  CB  ARG A 135      45.564  33.170  27.783  1.00 23.47           C  
ANISOU 1151  CB  ARG A 135     3304   2705   2909  -1128    749     -8       C  
ATOM   1152  CG  ARG A 135      45.753  32.386  29.064  1.00 26.67           C  
ANISOU 1152  CG  ARG A 135     3711   3223   3198  -1151    586    256       C  
ATOM   1153  CD  ARG A 135      47.200  32.359  29.482  1.00 29.39           C  
ANISOU 1153  CD  ARG A 135     4069   3654   3444   -948    445    208       C  
ATOM   1154  NE  ARG A 135      47.422  31.424  30.576  1.00 31.99           N  
ANISOU 1154  NE  ARG A 135     4394   4064   3697   -854    413    -22       N  
ATOM   1155  CZ  ARG A 135      48.277  31.628  31.570  1.00 33.19           C  
ANISOU 1155  CZ  ARG A 135     4493   4277   3841   -762    537   -393       C  
ATOM   1156  NH1 ARG A 135      48.984  32.748  31.615  1.00 33.35           N  
ANISOU 1156  NH1 ARG A 135     4421   4323   3926   -620    865   -678       N  
ATOM   1157  NH2 ARG A 135      48.419  30.717  32.523  1.00 34.20           N  
ANISOU 1157  NH2 ARG A 135     4633   4447   3916   -687    465   -461       N  
ATOM   1158  N   VAL A 136      43.620  35.307  26.248  1.00 23.32           N  
ANISOU 1158  N   VAL A 136     3098   2438   3325   -139   1171    -33       N  
ATOM   1159  CA  VAL A 136      43.359  36.210  25.132  1.00 24.55           C  
ANISOU 1159  CA  VAL A 136     3071   2766   3490    208   1176     97       C  
ATOM   1160  C   VAL A 136      44.574  36.349  24.215  1.00 22.70           C  
ANISOU 1160  C   VAL A 136     2519   2579   3526    -89   1168    325       C  
ATOM   1161  O   VAL A 136      45.615  36.851  24.636  1.00 24.84           O  
ANISOU 1161  O   VAL A 136     2947   2743   3749   -138   1128    412       O  
ATOM   1162  CB  VAL A 136      42.945  37.605  25.639  1.00 27.35           C  
ANISOU 1162  CB  VAL A 136     3494   3192   3706    483   1141    218       C  
ATOM   1163  CG1 VAL A 136      42.626  38.522  24.469  1.00 27.74           C  
ANISOU 1163  CG1 VAL A 136     3586   3197   3757    639    922    371       C  
ATOM   1164  CG2 VAL A 136      41.749  37.489  26.572  1.00 28.34           C  
ANISOU 1164  CG2 VAL A 136     3677   3355   3737    528   1149    431       C  
ATOM   1165  N   GLY A 137      44.430  35.877  22.978  1.00 20.23           N  
ANISOU 1165  N   GLY A 137     1916   2514   3258    245   1189    334       N  
ATOM   1166  CA  GLY A 137      45.471  35.969  21.965  1.00 19.02           C  
ANISOU 1166  CA  GLY A 137     1868   2205   3152    266    998    185       C  
ATOM   1167  C   GLY A 137      46.429  34.786  21.854  1.00 18.44           C  
ANISOU 1167  C   GLY A 137     1886   2162   2958    159    514    403       C  
ATOM   1168  O   GLY A 137      47.247  34.734  20.929  1.00 18.67           O  
ANISOU 1168  O   GLY A 137     1689   2317   3089    195    325    147       O  
ATOM   1169  N  ASER A 138      46.318  33.826  22.769  0.63 17.06           N  
ANISOU 1169  N  ASER A 138     1925   1980   2577     39    300    449       N  
ATOM   1170  N  BSER A 138      46.317  33.832  22.773  0.37 18.75           N  
ANISOU 1170  N  BSER A 138     2003   2277   2846    100    458    475       N  
ATOM   1171  CA ASER A 138      47.299  32.739  22.854  0.63 16.60           C  
ANISOU 1171  CA ASER A 138     2043   1850   2416    101    206    335       C  
ATOM   1172  CA BSER A 138      47.286  32.740  22.860  0.37 19.66           C  
ANISOU 1172  CA BSER A 138     2186   2433   2852     94    456    478       C  
ATOM   1173  C  ASER A 138      47.300  31.776  21.660  0.63 16.28           C  
ANISOU 1173  C  ASER A 138     1840   1935   2411     67    105    365       C  
ATOM   1174  C  BSER A 138      47.214  31.711  21.728  0.37 19.30           C  
ANISOU 1174  C  BSER A 138     2092   2464   2778     77    506    505       C  
ATOM   1175  O  ASER A 138      48.264  31.038  21.465  0.63 16.99           O  
ANISOU 1175  O  ASER A 138     1956   1987   2510    152     29    424       O  
ATOM   1176  O  BSER A 138      48.035  30.798  21.679  0.37 19.52           O  
ANISOU 1176  O  BSER A 138     2079   2578   2758     17    662    599       O  
ATOM   1177  CB ASER A 138      47.084  31.940  24.145  0.63 17.10           C  
ANISOU 1177  CB ASER A 138     2318   1856   2322    125    236    395       C  
ATOM   1178  CB BSER A 138      47.133  32.016  24.201  0.37 21.04           C  
ANISOU 1178  CB BSER A 138     2446   2600   2947     37    410    536       C  
ATOM   1179  OG ASER A 138      45.858  31.234  24.106  0.63 16.37           O  
ANISOU 1179  OG ASER A 138     2172   1790   2259     55    441    369       O  
ATOM   1180  OG BSER A 138      47.806  32.714  25.233  0.37 21.48           O  
ANISOU 1180  OG BSER A 138     2477   2639   3045      8    481    556       O  
ATOM   1181  N  AARG A 139      46.245  31.783  20.852  0.63 16.30           N  
ANISOU 1181  N  AARG A 139     1692   2034   2468     25    305    456       N  
ATOM   1182  N  BARG A 139      46.252  31.837  20.820  0.37 19.26           N  
ANISOU 1182  N  BARG A 139     2092   2400   2824    131    467    445       N  
ATOM   1183  CA AARG A 139      46.181  30.877  19.702  0.63 17.82           C  
ANISOU 1183  CA AARG A 139     1791   2275   2704     62    333    493       C  
ATOM   1184  CA BARG A 139      46.173  30.889  19.710  0.37 20.06           C  
ANISOU 1184  CA BARG A 139     2203   2455   2963    154    407    381       C  
ATOM   1185  C  AARG A 139      47.207  31.180  18.614  0.63 16.89           C  
ANISOU 1185  C  AARG A 139     1727   2002   2686     85    307    151       C  
ATOM   1186  C  BARG A 139      47.214  31.175  18.632  0.37 18.01           C  
ANISOU 1186  C  BARG A 139     1947   2098   2797    165    369    153       C  
ATOM   1187  O  AARG A 139      47.505  30.318  17.782  0.63 17.74           O  
ANISOU 1187  O  AARG A 139     1886   2039   2817     -9    238   -223       O  
ATOM   1188  O  BARG A 139      47.533  30.298  17.826  0.37 18.65           O  
ANISOU 1188  O  BARG A 139     2055   2139   2890    159    339    -53       O  
ATOM   1189  CB AARG A 139      44.784  30.899  19.077  0.63 21.05           C  
ANISOU 1189  CB AARG A 139     2209   2741   3049     52    444    685       C  
ATOM   1190  CB BARG A 139      44.775  30.891  19.081  0.37 23.19           C  
ANISOU 1190  CB BARG A 139     2654   2860   3298    141    418    465       C  
ATOM   1191  CG AARG A 139      43.674  30.493  20.032  0.63 25.99           C  
ANISOU 1191  CG AARG A 139     2880   3448   3546    -26    293    516       C  
ATOM   1192  CG BARG A 139      43.727  30.128  19.873  0.37 27.02           C  
ANISOU 1192  CG BARG A 139     3243   3357   3665     99    329    376       C  
ATOM   1193  CD AARG A 139      42.519  29.830  19.294  0.63 30.39           C  
ANISOU 1193  CD AARG A 139     3469   4039   4037     59     63    345       C  
ATOM   1194  CD BARG A 139      42.415  30.047  19.109  0.37 30.48           C  
ANISOU 1194  CD BARG A 139     3763   3854   3965     98    256    260       C  
ATOM   1195  NE AARG A 139      42.402  28.409  19.613  0.63 34.05           N  
ANISOU 1195  NE AARG A 139     3947   4574   4416     37    -78    189       N  
ATOM   1196  NE BARG A 139      41.272  30.412  19.941  0.37 33.22           N  
ANISOU 1196  NE BARG A 139     4224   4192   4207    112    194    108       N  
ATOM   1197  CZ AARG A 139      42.482  27.430  18.716  0.63 35.58           C  
ANISOU 1197  CZ AARG A 139     4118   4745   4655    142   -176     15       C  
ATOM   1198  CZ BARG A 139      40.006  30.333  19.544  0.37 34.84           C  
ANISOU 1198  CZ BARG A 139     4522   4338   4378    128    107     62       C  
ATOM   1199  NH1AARG A 139      42.673  27.710  17.435  0.63 36.96           N  
ANISOU 1199  NH1AARG A 139     4182   4967   4894    162   -214     66       N  
ATOM   1200  NH1BARG A 139      39.721  29.893  18.327  0.37 35.58           N  
ANISOU 1200  NH1BARG A 139     4692   4394   4432     88     72     50       N  
ATOM   1201  NH2AARG A 139      42.360  26.169  19.098  0.63 36.09           N  
ANISOU 1201  NH2AARG A 139     4272   4730   4709    223   -216    -54       N  
ATOM   1202  NH2BARG A 139      39.025  30.687  20.362  0.37 35.48           N  
ANISOU 1202  NH2BARG A 139     4603   4434   4445    223     57     26       N  
ATOM   1203  N   LYS A 140      47.748  32.394  18.620  1.00 15.57           N  
ANISOU 1203  N   LYS A 140     1701   1683   2531    137    397     81       N  
ATOM   1204  CA  LYS A 140      48.678  32.802  17.560  1.00 15.75           C  
ANISOU 1204  CA  LYS A 140     1874   1805   2305    110    463    -10       C  
ATOM   1205  C   LYS A 140      50.084  32.287  17.846  1.00 15.95           C  
ANISOU 1205  C   LYS A 140     1983   1754   2322     41    138   -205       C  
ATOM   1206  O   LYS A 140      50.990  33.041  18.229  1.00 16.78           O  
ANISOU 1206  O   LYS A 140     2322   1772   2280    283    285     36       O  
ATOM   1207  CB  LYS A 140      48.682  34.329  17.382  1.00 17.14           C  
ANISOU 1207  CB  LYS A 140     2078   2381   2055   -247    515    118       C  
ATOM   1208  CG  LYS A 140      49.494  34.849  16.189  1.00 19.12           C  
ANISOU 1208  CG  LYS A 140     2366   3023   1875   -403    318   -101       C  
ATOM   1209  CD  LYS A 140      49.116  34.171  14.868  1.00 21.36           C  
ANISOU 1209  CD  LYS A 140     2693   3616   1807   -443    347    156       C  
ATOM   1210  CE  LYS A 140      49.573  35.025  13.674  1.00 22.33           C  
ANISOU 1210  CE  LYS A 140     2665   4085   1735   -473    575   -109       C  
ATOM   1211  NZ  LYS A 140      49.547  34.277  12.389  1.00 24.79           N  
ANISOU 1211  NZ  LYS A 140     2934   4440   2043   -546    527   -169       N  
ATOM   1212  N   VAL A 141      50.240  30.978  17.672  1.00 16.40           N  
ANISOU 1212  N   VAL A 141     1859   1930   2441    359    -33   -347       N  
ATOM   1213  CA  VAL A 141      51.537  30.312  17.708  1.00 16.11           C  
ANISOU 1213  CA  VAL A 141     1749   2110   2260    266   -118   -227       C  
ATOM   1214  C   VAL A 141      51.409  29.142  16.747  1.00 14.46           C  
ANISOU 1214  C   VAL A 141     1533   1783   2177    330     10   -100       C  
ATOM   1215  O   VAL A 141      50.334  28.551  16.640  1.00 15.43           O  
ANISOU 1215  O   VAL A 141     1441   2086   2336     87     98   -129       O  
ATOM   1216  CB  VAL A 141      51.924  29.876  19.139  1.00 18.80           C  
ANISOU 1216  CB  VAL A 141     2046   2747   2350    285     -3   -254       C  
ATOM   1217  CG1 VAL A 141      50.926  28.879  19.705  1.00 18.78           C  
ANISOU 1217  CG1 VAL A 141     2189   2755   2191    276      8   -256       C  
ATOM   1218  CG2 VAL A 141      53.339  29.326  19.165  1.00 18.83           C  
ANISOU 1218  CG2 VAL A 141     1902   2994   2258    440   -146   -289       C  
ATOM   1219  N   ASP A 142      52.478  28.823  16.025  1.00 12.26           N  
ANISOU 1219  N   ASP A 142     1392   1378   1887    263     51   -333       N  
ATOM   1220  CA  ASP A 142      52.346  27.955  14.855  1.00 11.43           C  
ANISOU 1220  CA  ASP A 142     1354   1105   1885    -21    -34   -138       C  
ATOM   1221  C   ASP A 142      52.923  26.551  14.991  1.00 11.99           C  
ANISOU 1221  C   ASP A 142     1390   1317   1850    -29     15     37       C  
ATOM   1222  O   ASP A 142      52.313  25.587  14.544  1.00 13.87           O  
ANISOU 1222  O   ASP A 142     1763   1381   2126   -155     26     -6       O  
ATOM   1223  CB  ASP A 142      52.982  28.663  13.656  1.00 12.16           C  
ANISOU 1223  CB  ASP A 142     1417   1220   1983   -159    -78    159       C  
ATOM   1224  CG  ASP A 142      52.436  30.056  13.474  1.00 15.02           C  
ANISOU 1224  CG  ASP A 142     1565   1805   2338     66   -321    258       C  
ATOM   1225  OD1 ASP A 142      51.197  30.194  13.443  1.00 17.62           O  
ANISOU 1225  OD1 ASP A 142     1601   2172   2921    223   -457    167       O  
ATOM   1226  OD2 ASP A 142      53.232  31.009  13.405  1.00 16.43           O  
ANISOU 1226  OD2 ASP A 142     2005   1902   2336   -132   -346    294       O  
ATOM   1227  N   VAL A 143      54.106  26.447  15.572  1.00 11.14           N  
ANISOU 1227  N   VAL A 143     1289   1292   1653     74    -23     73       N  
ATOM   1228  CA  VAL A 143      54.796  25.168  15.651  1.00 11.44           C  
ANISOU 1228  CA  VAL A 143     1433   1428   1485    376    114     75       C  
ATOM   1229  C   VAL A 143      55.212  24.950  17.105  1.00 11.11           C  
ANISOU 1229  C   VAL A 143     1509   1198   1515     10   -101    235       C  
ATOM   1230  O   VAL A 143      55.787  25.838  17.732  1.00 13.55           O  
ANISOU 1230  O   VAL A 143     2016   1533   1598   -229   -401    255       O  
ATOM   1231  CB  VAL A 143      56.027  25.132  14.715  1.00 13.91           C  
ANISOU 1231  CB  VAL A 143     1810   1720   1756    468     -3    100       C  
ATOM   1232  CG1 VAL A 143      56.746  23.801  14.811  1.00 13.33           C  
ANISOU 1232  CG1 VAL A 143     1668   1449   1949    623     53    -34       C  
ATOM   1233  CG2 VAL A 143      55.650  25.471  13.259  1.00 14.26           C  
ANISOU 1233  CG2 VAL A 143     2019   1779   1620    791    -79    144       C  
ATOM   1234  N   MET A 144      54.909  23.792  17.673  1.00 11.93           N  
ANISOU 1234  N   MET A 144     1372   1524   1639     51    128    460       N  
ATOM   1235  CA  MET A 144      55.309  23.591  19.058  1.00 12.89           C  
ANISOU 1235  CA  MET A 144     1239   1622   2039    113    102    455       C  
ATOM   1236  C   MET A 144      56.693  22.953  19.119  1.00 13.15           C  
ANISOU 1236  C   MET A 144     1563   1589   1845    224    -59    168       C  
ATOM   1237  O   MET A 144      57.121  22.279  18.178  1.00 13.41           O  
ANISOU 1237  O   MET A 144     1616   1684   1796     63    -68    -27       O  
ATOM   1238  CB  MET A 144      54.258  22.772  19.825  1.00 16.98           C  
ANISOU 1238  CB  MET A 144     1664   1839   2948    -29     71    952       C  
ATOM   1239  CG  MET A 144      54.309  21.278  19.677  1.00 21.65           C  
ANISOU 1239  CG  MET A 144     1903   2475   3848   -304    451   1031       C  
ATOM   1240  SD  MET A 144      53.213  20.475  20.886  1.00 23.13           S  
ANISOU 1240  SD  MET A 144     1874   2526   4386   -146    375   1534       S  
ATOM   1241  CE  MET A 144      52.795  19.023  19.940  1.00 23.98           C  
ANISOU 1241  CE  MET A 144     2016   2542   4555   -180    306   1574       C  
ATOM   1242  N   ILE A 145      57.408  23.243  20.203  1.00 12.54           N  
ANISOU 1242  N   ILE A 145     1414   1640   1712    443   -233    367       N  
ATOM   1243  CA  ILE A 145      58.728  22.681  20.450  1.00 13.06           C  
ANISOU 1243  CA  ILE A 145     1577   1684   1701    115    100    283       C  
ATOM   1244  C   ILE A 145      58.619  21.786  21.668  1.00 13.39           C  
ANISOU 1244  C   ILE A 145     1652   1785   1652     59     63    362       C  
ATOM   1245  O   ILE A 145      58.066  22.210  22.690  1.00 12.97           O  
ANISOU 1245  O   ILE A 145     1699   1544   1686    203    -11    545       O  
ATOM   1246  CB  ILE A 145      59.799  23.760  20.701  1.00 11.99           C  
ANISOU 1246  CB  ILE A 145     1254   1486   1816    150     34    280       C  
ATOM   1247  CG1 ILE A 145      59.721  24.881  19.657  1.00 12.38           C  
ANISOU 1247  CG1 ILE A 145     1564   1296   1843    120    -81    302       C  
ATOM   1248  CG2 ILE A 145      61.194  23.127  20.740  1.00 12.09           C  
ANISOU 1248  CG2 ILE A 145      989   1561   2044    468    113    129       C  
ATOM   1249  CD1 ILE A 145      60.540  26.109  20.046  1.00 13.20           C  
ANISOU 1249  CD1 ILE A 145     1694   1403   1917    -97     32    228       C  
ATOM   1250  N   GLU A 146      59.133  20.563  21.543  1.00 13.22           N  
ANISOU 1250  N   GLU A 146     1477   1946   1600    241     33    443       N  
ATOM   1251  CA  GLU A 146      59.110  19.587  22.631  1.00 14.47           C  
ANISOU 1251  CA  GLU A 146     1534   2022   1943    117    -48    350       C  
ATOM   1252  C   GLU A 146      60.498  19.033  22.889  1.00 15.52           C  
ANISOU 1252  C   GLU A 146     1727   2092   2077    241    -60    462       C  
ATOM   1253  O   GLU A 146      61.339  18.995  21.991  1.00 16.06           O  
ANISOU 1253  O   GLU A 146     1869   2054   2181    440   -109    417       O  
ATOM   1254  CB  GLU A 146      58.155  18.442  22.311  1.00 15.32           C  
ANISOU 1254  CB  GLU A 146     1688   2162   1970     19     81    204       C  
ATOM   1255  CG  GLU A 146      56.690  18.828  22.263  1.00 16.50           C  
ANISOU 1255  CG  GLU A 146     1780   2449   2042     67    325    288       C  
ATOM   1256  CD  GLU A 146      55.816  17.674  21.825  1.00 17.24           C  
ANISOU 1256  CD  GLU A 146     1947   2448   2155    103    531    406       C  
ATOM   1257  OE1 GLU A 146      56.031  17.149  20.712  1.00 17.95           O  
ANISOU 1257  OE1 GLU A 146     2146   2299   2375    -61    300    377       O  
ATOM   1258  OE2 GLU A 146      54.922  17.275  22.601  1.00 19.60           O  
ANISOU 1258  OE2 GLU A 146     2046   3015   2386    311    547    352       O  
ATOM   1259  N   LYS A 147      60.716  18.576  24.117  1.00 16.30           N  
ANISOU 1259  N   LYS A 147     1840   2144   2210    519    -85    560       N  
ATOM   1260  CA  LYS A 147      61.990  18.002  24.521  1.00 18.35           C  
ANISOU 1260  CA  LYS A 147     2075   2452   2447    615     12    669       C  
ATOM   1261  C   LYS A 147      61.730  16.689  25.238  1.00 19.94           C  
ANISOU 1261  C   LYS A 147     2363   2589   2626    935    266    722       C  
ATOM   1262  O   LYS A 147      60.929  16.640  26.166  1.00 20.04           O  
ANISOU 1262  O   LYS A 147     2357   2691   2566    676    465    925       O  
ATOM   1263  CB  LYS A 147      62.749  18.970  25.427  1.00 19.91           C  
ANISOU 1263  CB  LYS A 147     2377   2675   2514    634    -86    545       C  
ATOM   1264  CG  LYS A 147      63.936  18.367  26.166  1.00 22.33           C  
ANISOU 1264  CG  LYS A 147     2738   2976   2770    711     -9    661       C  
ATOM   1265  CD  LYS A 147      65.174  18.314  25.295  1.00 24.75           C  
ANISOU 1265  CD  LYS A 147     3097   3322   2985    839   -111    681       C  
ATOM   1266  CE  LYS A 147      66.391  17.875  26.097  1.00 27.34           C  
ANISOU 1266  CE  LYS A 147     3388   3688   3312    618    -36    420       C  
ATOM   1267  NZ  LYS A 147      67.647  18.060  25.320  1.00 29.16           N  
ANISOU 1267  NZ  LYS A 147     3653   3930   3498    559    120    172       N  
ATOM   1268  N   GLN A 148      62.384  15.619  24.804  1.00 20.15           N  
ANISOU 1268  N   GLN A 148     2452   2464   2741   1101    276   1129       N  
ATOM   1269  CA  GLN A 148      62.206  14.331  25.471  1.00 21.32           C  
ANISOU 1269  CA  GLN A 148     2654   2533   2912   1019    260   1307       C  
ATOM   1270  C   GLN A 148      62.823  14.386  26.863  1.00 23.10           C  
ANISOU 1270  C   GLN A 148     2865   2979   2935   1019    162   1241       C  
ATOM   1271  O   GLN A 148      63.989  14.752  27.018  1.00 23.89           O  
ANISOU 1271  O   GLN A 148     2816   3320   2939   1072     74   1038       O  
ATOM   1272  CB  GLN A 148      62.821  13.209  24.648  1.00 22.76           C  
ANISOU 1272  CB  GLN A 148     2929   2597   3121    979    277   1366       C  
ATOM   1273  CG  GLN A 148      62.482  11.824  25.170  1.00 25.58           C  
ANISOU 1273  CG  GLN A 148     3355   2839   3523    832    351   1086       C  
ATOM   1274  CD  GLN A 148      62.883  10.745  24.198  1.00 27.77           C  
ANISOU 1274  CD  GLN A 148     3522   3102   3929    657    337   1003       C  
ATOM   1275  OE1 GLN A 148      63.977  10.782  23.636  1.00 28.33           O  
ANISOU 1275  OE1 GLN A 148     3379   3307   4077    629    318    958       O  
ATOM   1276  NE2 GLN A 148      61.989   9.787  23.971  1.00 29.42           N  
ANISOU 1276  NE2 GLN A 148     3795   3299   4083    494    405   1118       N  
ATOM   1277  N   GLY A 149      62.029  14.050  27.875  1.00 24.54           N  
ANISOU 1277  N   GLY A 149     3122   3200   3002   1005    240   1184       N  
ATOM   1278  CA  GLY A 149      62.490  14.115  29.250  1.00 25.73           C  
ANISOU 1278  CA  GLY A 149     3348   3425   3002    898    265   1067       C  
ATOM   1279  C   GLY A 149      62.508  15.516  29.835  1.00 27.44           C  
ANISOU 1279  C   GLY A 149     3512   3826   3086   1074    179    975       C  
ATOM   1280  O   GLY A 149      62.987  15.730  30.950  1.00 29.29           O  
ANISOU 1280  O   GLY A 149     3756   4105   3267   1052    -67    892       O  
ATOM   1281  N   GLY A 150      61.987  16.481  29.084  1.00 26.42           N  
ANISOU 1281  N   GLY A 150     3353   3736   2951   1187    204    987       N  
ATOM   1282  CA  GLY A 150      61.911  17.850  29.557  1.00 27.02           C  
ANISOU 1282  CA  GLY A 150     3446   3968   2853   1154    190    912       C  
ATOM   1283  C   GLY A 150      60.530  18.438  29.347  1.00 25.70           C  
ANISOU 1283  C   GLY A 150     3235   3835   2695   1184    241    912       C  
ATOM   1284  O   GLY A 150      59.608  17.736  28.940  1.00 25.45           O  
ANISOU 1284  O   GLY A 150     3066   3855   2748   1088    286   1052       O  
ATOM   1285  N   GLY A 151      60.387  19.726  29.638  1.00 25.23           N  
ANISOU 1285  N   GLY A 151     3232   3794   2560   1120    150    832       N  
ATOM   1286  CA  GLY A 151      59.149  20.430  29.371  1.00 24.87           C  
ANISOU 1286  CA  GLY A 151     3250   3636   2564    945    350    883       C  
ATOM   1287  C   GLY A 151      57.989  20.037  30.255  1.00 24.49           C  
ANISOU 1287  C   GLY A 151     3327   3423   2553    884    584   1218       C  
ATOM   1288  O   GLY A 151      58.173  19.409  31.302  1.00 26.62           O  
ANISOU 1288  O   GLY A 151     3676   3708   2732    812    608   1339       O  
ATOM   1289  N   ARG A 152      56.786  20.409  29.840  1.00 24.40           N  
ANISOU 1289  N   ARG A 152     3263   3372   2637    674    633   1075       N  
ATOM   1290  CA  ARG A 152      55.606  20.131  30.644  1.00 24.83           C  
ANISOU 1290  CA  ARG A 152     3381   3397   2657    680    821    978       C  
ATOM   1291  C   ARG A 152      54.629  19.222  29.903  1.00 23.00           C  
ANISOU 1291  C   ARG A 152     3054   3234   2450    758    838   1167       C  
ATOM   1292  O   ARG A 152      54.629  19.155  28.671  1.00 21.98           O  
ANISOU 1292  O   ARG A 152     3016   3023   2312    685    832   1079       O  
ATOM   1293  CB  ARG A 152      54.928  21.439  31.070  1.00 28.77           C  
ANISOU 1293  CB  ARG A 152     3994   3855   3082    529    564    614       C  
ATOM   1294  CG  ARG A 152      54.582  22.359  29.927  1.00 30.96           C  
ANISOU 1294  CG  ARG A 152     4459   4187   3117    336    306    347       C  
ATOM   1295  CD  ARG A 152      54.295  23.789  30.386  1.00 32.97           C  
ANISOU 1295  CD  ARG A 152     4889   4460   3180    172     -2     85       C  
ATOM   1296  NE  ARG A 152      55.519  24.526  30.700  1.00 33.39           N  
ANISOU 1296  NE  ARG A 152     5082   4565   3040    150   -282    -82       N  
ATOM   1297  CZ  ARG A 152      55.570  25.834  30.938  1.00 33.28           C  
ANISOU 1297  CZ  ARG A 152     5175   4583   2888    209   -444    -94       C  
ATOM   1298  NH1 ARG A 152      54.463  26.568  30.899  1.00 32.82           N  
ANISOU 1298  NH1 ARG A 152     5212   4531   2725    423   -701     -7       N  
ATOM   1299  NH2 ARG A 152      56.732  26.412  31.211  1.00 32.96           N  
ANISOU 1299  NH2 ARG A 152     5081   4567   2875    189   -440   -195       N  
ATOM   1300  N   SER A 153      53.825  18.490  30.671  1.00 23.11           N  
ANISOU 1300  N   SER A 153     3027   3086   2666    634    914   1368       N  
ATOM   1301  CA  SER A 153      52.852  17.541  30.129  1.00 23.59           C  
ANISOU 1301  CA  SER A 153     2938   3321   2704    759    874   1231       C  
ATOM   1302  C   SER A 153      53.409  16.578  29.076  1.00 23.85           C  
ANISOU 1302  C   SER A 153     2987   3259   2817    845    791   1319       C  
ATOM   1303  O   SER A 153      52.916  16.543  27.951  1.00 24.28           O  
ANISOU 1303  O   SER A 153     3016   3487   2723   1034    655   1044       O  
ATOM   1304  CB  SER A 153      51.664  18.301  29.537  1.00 24.77           C  
ANISOU 1304  CB  SER A 153     2891   3805   2716    905    814    861       C  
ATOM   1305  OG  SER A 153      51.005  19.051  30.541  1.00 27.68           O  
ANISOU 1305  OG  SER A 153     3211   4297   3009    850    566    639       O  
ATOM   1306  N   PRO A 154      54.419  15.768  29.444  1.00 24.58           N  
ANISOU 1306  N   PRO A 154     3041   3216   3082    801    686   1555       N  
ATOM   1307  CA  PRO A 154      55.028  14.860  28.458  1.00 25.33           C  
ANISOU 1307  CA  PRO A 154     3123   3088   3413    945    752   1549       C  
ATOM   1308  C   PRO A 154      54.020  13.907  27.811  1.00 26.15           C  
ANISOU 1308  C   PRO A 154     3201   2938   3795    843    971   1330       C  
ATOM   1309  O   PRO A 154      53.093  13.454  28.490  1.00 27.07           O  
ANISOU 1309  O   PRO A 154     3348   3012   3927    873   1020   1150       O  
ATOM   1310  CB  PRO A 154      56.059  14.082  29.288  1.00 25.82           C  
ANISOU 1310  CB  PRO A 154     3197   3184   3429   1060    668   1604       C  
ATOM   1311  CG  PRO A 154      55.603  14.230  30.712  1.00 26.50           C  
ANISOU 1311  CG  PRO A 154     3302   3306   3460    999    590   1548       C  
ATOM   1312  CD  PRO A 154      54.985  15.589  30.792  1.00 26.12           C  
ANISOU 1312  CD  PRO A 154     3237   3356   3331    941    499   1532       C  
ATOM   1313  N   ASP A 155      54.176  13.627  26.517  1.00 27.61           N  
ANISOU 1313  N   ASP A 155     3278   2985   4229    839    921   1070       N  
ATOM   1314  CA  ASP A 155      53.274  12.697  25.846  1.00 28.87           C  
ANISOU 1314  CA  ASP A 155     3433   2985   4551    598    947    958       C  
ATOM   1315  C   ASP A 155      53.704  11.259  26.129  1.00 31.16           C  
ANISOU 1315  C   ASP A 155     3758   3091   4991    550    977   1021       C  
ATOM   1316  O   ASP A 155      54.549  11.023  26.992  1.00 30.94           O  
ANISOU 1316  O   ASP A 155     3746   2892   5120    371   1146   1233       O  
ATOM   1317  CB  ASP A 155      53.196  12.966  24.328  1.00 29.24           C  
ANISOU 1317  CB  ASP A 155     3468   3058   4583    416    872    555       C  
ATOM   1318  CG  ASP A 155      54.530  12.779  23.600  1.00 29.16           C  
ANISOU 1318  CG  ASP A 155     3581   2985   4515    151    975    319       C  
ATOM   1319  OD1 ASP A 155      55.476  12.174  24.150  1.00 26.89           O  
ANISOU 1319  OD1 ASP A 155     3412   2332   4475    187    943    267       O  
ATOM   1320  OD2 ASP A 155      54.620  13.241  22.441  1.00 31.04           O  
ANISOU 1320  OD2 ASP A 155     3787   3442   4567    262    975    123       O  
ATOM   1321  N   ALA A 156      53.123  10.314  25.401  1.00 33.59           N  
ANISOU 1321  N   ALA A 156     4133   3388   5242    627    842    806       N  
ATOM   1322  CA  ALA A 156      53.387   8.896  25.621  1.00 35.82           C  
ANISOU 1322  CA  ALA A 156     4514   3686   5411    510    750    855       C  
ATOM   1323  C   ALA A 156      54.867   8.535  25.456  1.00 37.03           C  
ANISOU 1323  C   ALA A 156     4652   3863   5556    512    782    994       C  
ATOM   1324  O   ALA A 156      55.354   7.603  26.098  1.00 37.33           O  
ANISOU 1324  O   ALA A 156     4659   3909   5618    332    865   1206       O  
ATOM   1325  CB  ALA A 156      52.533   8.059  24.680  1.00 37.11           C  
ANISOU 1325  CB  ALA A 156     4692   3970   5440    407    650    763       C  
ATOM   1326  N   GLU A 157      55.579   9.273  24.607  1.00 37.93           N  
ANISOU 1326  N   GLU A 157     4789   4000   5621    594    752    842       N  
ATOM   1327  CA  GLU A 157      56.990   8.995  24.345  1.00 38.71           C  
ANISOU 1327  CA  GLU A 157     4958   4189   5560    661    609    766       C  
ATOM   1328  C   GLU A 157      57.928   9.810  25.235  1.00 35.29           C  
ANISOU 1328  C   GLU A 157     4444   3703   5263    834    668    949       C  
ATOM   1329  O   GLU A 157      59.148   9.712  25.107  1.00 35.91           O  
ANISOU 1329  O   GLU A 157     4401   3797   5446    652    727    946       O  
ATOM   1330  CB  GLU A 157      57.331   9.276  22.882  1.00 43.01           C  
ANISOU 1330  CB  GLU A 157     5740   4815   5787    523    456    575       C  
ATOM   1331  CG  GLU A 157      56.279   8.845  21.883  1.00 46.56           C  
ANISOU 1331  CG  GLU A 157     6393   5329   5968    401    363    381       C  
ATOM   1332  CD  GLU A 157      56.212   9.789  20.694  1.00 49.08           C  
ANISOU 1332  CD  GLU A 157     6852   5665   6131    388    401    199       C  
ATOM   1333  OE1 GLU A 157      56.827   9.483  19.648  1.00 49.60           O  
ANISOU 1333  OE1 GLU A 157     6970   5733   6143    407    491     81       O  
ATOM   1334  OE2 GLU A 157      55.552  10.846  20.815  1.00 49.57           O  
ANISOU 1334  OE2 GLU A 157     6980   5683   6170    417    445    164       O  
ATOM   1335  N   GLY A 158      57.364  10.625  26.120  1.00 30.66           N  
ANISOU 1335  N   GLY A 158     3887   3046   4717    932    748   1106       N  
ATOM   1336  CA  GLY A 158      58.169  11.408  27.041  1.00 27.77           C  
ANISOU 1336  CA  GLY A 158     3592   2722   4238    978    798   1450       C  
ATOM   1337  C   GLY A 158      58.503  12.818  26.566  1.00 25.79           C  
ANISOU 1337  C   GLY A 158     3377   2551   3872    696    940   1351       C  
ATOM   1338  O   GLY A 158      59.284  13.517  27.204  1.00 25.27           O  
ANISOU 1338  O   GLY A 158     3410   2453   3740    669   1034   1488       O  
ATOM   1339  N   PHE A 159      57.919  13.230  25.445  1.00 23.35           N  
ANISOU 1339  N   PHE A 159     3042   2303   3527    775   1077    952       N  
ATOM   1340  CA  PHE A 159      58.167  14.575  24.926  1.00 21.59           C  
ANISOU 1340  CA  PHE A 159     2888   2136   3178    858    771    827       C  
ATOM   1341  C   PHE A 159      57.253  15.590  25.611  1.00 20.85           C  
ANISOU 1341  C   PHE A 159     2890   2087   2946    674    568    742       C  
ATOM   1342  O   PHE A 159      56.036  15.517  25.467  1.00 20.79           O  
ANISOU 1342  O   PHE A 159     2687   2122   3090    360    727    541       O  
ATOM   1343  CB  PHE A 159      57.959  14.628  23.415  1.00 22.12           C  
ANISOU 1343  CB  PHE A 159     2876   2185   3342    755    551    789       C  
ATOM   1344  CG  PHE A 159      59.043  13.958  22.626  1.00 21.64           C  
ANISOU 1344  CG  PHE A 159     2569   2278   3374    654    347    725       C  
ATOM   1345  CD1 PHE A 159      60.105  14.690  22.124  1.00 20.96           C  
ANISOU 1345  CD1 PHE A 159     2227   2428   3309    581    253    791       C  
ATOM   1346  CD2 PHE A 159      58.999  12.593  22.380  1.00 23.71           C  
ANISOU 1346  CD2 PHE A 159     2821   2580   3609    356    421    472       C  
ATOM   1347  CE1 PHE A 159      61.102  14.083  21.390  1.00 21.00           C  
ANISOU 1347  CE1 PHE A 159     2141   2482   3355    459    303    785       C  
ATOM   1348  CE2 PHE A 159      59.996  11.976  21.644  1.00 23.34           C  
ANISOU 1348  CE2 PHE A 159     2647   2579   3643    351    490    483       C  
ATOM   1349  CZ  PHE A 159      61.050  12.727  21.146  1.00 22.31           C  
ANISOU 1349  CZ  PHE A 159     2397   2559   3522    489    438    563       C  
ATOM   1350  N   GLY A 160      57.847  16.533  26.338  1.00 19.76           N  
ANISOU 1350  N   GLY A 160     2856   2106   2548    657    279    736       N  
ATOM   1351  CA  GLY A 160      57.098  17.599  26.984  1.00 17.64           C  
ANISOU 1351  CA  GLY A 160     2519   1953   2231    655    212    834       C  
ATOM   1352  C   GLY A 160      57.295  18.916  26.252  1.00 16.90           C  
ANISOU 1352  C   GLY A 160     2215   2045   2159    429    217    564       C  
ATOM   1353  O   GLY A 160      58.342  19.139  25.647  1.00 16.10           O  
ANISOU 1353  O   GLY A 160     2030   2026   2060    389    104    467       O  
ATOM   1354  N  AVAL A 161      56.295  19.788  26.322  0.65 16.32           N  
ANISOU 1354  N  AVAL A 161     2067   1968   2165    426    174    550       N  
ATOM   1355  N  BVAL A 161      56.299  19.793  26.313  0.35 16.47           N  
ANISOU 1355  N  BVAL A 161     2193   2070   1993    361    247    520       N  
ATOM   1356  CA AVAL A 161      56.345  21.063  25.606  0.65 16.01           C  
ANISOU 1356  CA AVAL A 161     1954   1965   2164    335    173    520       C  
ATOM   1357  CA BVAL A 161      56.377  21.039  25.559  0.35 16.25           C  
ANISOU 1357  CA BVAL A 161     2181   2145   1848    264    301    474       C  
ATOM   1358  C  AVAL A 161      57.254  22.070  26.304  0.65 16.13           C  
ANISOU 1358  C  AVAL A 161     2147   2134   1848    176    239    238       C  
ATOM   1359  C  BVAL A 161      57.241  22.071  26.287  0.35 16.01           C  
ANISOU 1359  C  BVAL A 161     2178   2158   1746    192    237    271       C  
ATOM   1360  O  AVAL A 161      57.183  22.247  27.524  0.65 17.36           O  
ANISOU 1360  O  AVAL A 161     2420   2353   1822   -134    326    310       O  
ATOM   1361  O  BVAL A 161      57.153  22.238  27.506  0.35 16.80           O  
ANISOU 1361  O  BVAL A 161     2344   2284   1756     -7    260    306       O  
ATOM   1362  CB AVAL A 161      54.949  21.690  25.453  0.65 16.50           C  
ANISOU 1362  CB AVAL A 161     1789   2058   2423    217    195    558       C  
ATOM   1363  CB BVAL A 161      54.968  21.623  25.258  0.35 16.67           C  
ANISOU 1363  CB BVAL A 161     2239   2335   1758    193    500    482       C  
ATOM   1364  CG1AVAL A 161      55.001  22.858  24.466  0.65 13.04           C  
ANISOU 1364  CG1AVAL A 161     1067   1652   2235    237    201    976       C  
ATOM   1365  CG1BVAL A 161      54.137  20.615  24.483  0.35 17.94           C  
ANISOU 1365  CG1BVAL A 161     2425   2447   1946    160    420    481       C  
ATOM   1366  CG2AVAL A 161      53.957  20.659  24.982  0.65 18.64           C  
ANISOU 1366  CG2AVAL A 161     2131   2312   2638     90    319    505       C  
ATOM   1367  CG2BVAL A 161      54.249  22.036  26.519  0.35 14.88           C  
ANISOU 1367  CG2BVAL A 161     2035   2238   1382    203    728    685       C  
ATOM   1368  N   VAL A 162      58.100  22.741  25.525  1.00 15.05           N  
ANISOU 1368  N   VAL A 162     1974   2037   1709    368     74    190       N  
ATOM   1369  CA  VAL A 162      59.049  23.698  26.078  1.00 15.28           C  
ANISOU 1369  CA  VAL A 162     1917   2229   1659    438   -135    153       C  
ATOM   1370  C   VAL A 162      58.904  25.079  25.445  1.00 14.96           C  
ANISOU 1370  C   VAL A 162     2165   1953   1565    301   -231    279       C  
ATOM   1371  O   VAL A 162      59.535  26.040  25.887  1.00 17.58           O  
ANISOU 1371  O   VAL A 162     2672   2045   1963    146   -115    209       O  
ATOM   1372  CB  VAL A 162      60.500  23.229  25.887  1.00 16.92           C  
ANISOU 1372  CB  VAL A 162     1912   2767   1751    463   -160    379       C  
ATOM   1373  CG1 VAL A 162      60.784  21.985  26.722  1.00 17.41           C  
ANISOU 1373  CG1 VAL A 162     2052   2598   1966    533   -391    455       C  
ATOM   1374  CG2 VAL A 162      60.772  22.955  24.415  1.00 18.23           C  
ANISOU 1374  CG2 VAL A 162     1824   3299   1805    279    115    155       C  
ATOM   1375  N   GLY A 163      58.101  25.166  24.387  1.00 14.33           N  
ANISOU 1375  N   GLY A 163     2075   1830   1540     49   -193    469       N  
ATOM   1376  CA  GLY A 163      57.845  26.450  23.768  1.00 15.21           C  
ANISOU 1376  CA  GLY A 163     2266   1972   1543    -54   -222    424       C  
ATOM   1377  C   GLY A 163      57.205  26.342  22.404  1.00 13.18           C  
ANISOU 1377  C   GLY A 163     1854   1797   1359      8   -126    268       C  
ATOM   1378  O   GLY A 163      56.647  25.311  22.041  1.00 12.04           O  
ANISOU 1378  O   GLY A 163     1626   1682   1266    -46     57     33       O  
ATOM   1379  N   GLY A 164      57.270  27.429  21.645  1.00 12.11           N  
ANISOU 1379  N   GLY A 164     1773   1840    990    -36     47    509       N  
ATOM   1380  CA  GLY A 164      56.667  27.423  20.333  1.00 12.14           C  
ANISOU 1380  CA  GLY A 164     1801   1646   1168   -201    249    510       C  
ATOM   1381  C   GLY A 164      57.319  28.414  19.416  1.00 11.74           C  
ANISOU 1381  C   GLY A 164     1710   1472   1280    -20    -73    211       C  
ATOM   1382  O   GLY A 164      58.075  29.296  19.833  1.00 13.04           O  
ANISOU 1382  O   GLY A 164     1951   1543   1460   -293   -249    501       O  
ATOM   1383  N  AILE A 165      57.052  28.228  18.124  0.73 10.64           N  
ANISOU 1383  N  AILE A 165     1546   1383   1114    186     15    492       N  
ATOM   1384  N  BILE A 165      56.994  28.285  18.150  0.27 12.52           N  
ANISOU 1384  N  BILE A 165     1849   1588   1319    -19    -28    315       N  
ATOM   1385  CA AILE A 165      57.557  29.087  17.052  0.73 10.52           C  
ANISOU 1385  CA AILE A 165     1623   1061   1314    168     85    246       C  
ATOM   1386  CA BILE A 165      57.509  29.240  17.216  0.27 13.35           C  
ANISOU 1386  CA BILE A 165     2043   1548   1482    -50     82    203       C  
ATOM   1387  C  AILE A 165      56.418  29.883  16.409  0.73 12.04           C  
ANISOU 1387  C  AILE A 165     1881   1301   1393    293    -34     84       C  
ATOM   1388  C  BILE A 165      56.393  29.910  16.471  0.27 12.76           C  
ANISOU 1388  C  BILE A 165     2030   1425   1392     91     39    220       C  
ATOM   1389  O  AILE A 165      55.384  29.310  16.063  0.73 12.53           O  
ANISOU 1389  O  AILE A 165     1942   1251   1569    164     51    120       O  
ATOM   1390  O  BILE A 165      55.370  29.306  16.138  0.27 12.66           O  
ANISOU 1390  O  BILE A 165     2027   1363   1422    -45    110    330       O  
ATOM   1391  CB AILE A 165      58.274  28.262  15.962  0.73 10.05           C  
ANISOU 1391  CB AILE A 165     1501    765   1554    201    125    191       C  
ATOM   1392  CB BILE A 165      58.489  28.580  16.273  0.27 14.94           C  
ANISOU 1392  CB BILE A 165     2239   1697   1740   -107    209     55       C  
ATOM   1393  CG1AILE A 165      59.394  27.417  16.581  0.73 11.13           C  
ANISOU 1393  CG1AILE A 165     1242   1152   1834    348    -73    -50       C  
ATOM   1394  CG1BILE A 165      58.582  29.307  14.940  0.27 15.58           C  
ANISOU 1394  CG1BILE A 165     2272   1802   1847    -20    437     -7       C  
ATOM   1395  CG2AILE A 165      58.824  29.176  14.874  0.73 11.79           C  
ANISOU 1395  CG2AILE A 165     1705   1102   1673    239    312    -96       C  
ATOM   1396  CG2BILE A 165      58.136  27.163  16.079  0.27 16.37           C  
ANISOU 1396  CG2BILE A 165     2444   1886   1890    -99    139    -89       C  
ATOM   1397  CD1AILE A 165      60.111  26.542  15.572  0.73 12.06           C  
ANISOU 1397  CD1AILE A 165     1238   1140   2206    523    -58   -167       C  
ATOM   1398  CD1BILE A 165      59.705  28.801  14.184  0.27 15.93           C  
ANISOU 1398  CD1BILE A 165     2261   1898   1893    -34    609     24       C  
ATOM   1399  N   HIS A 166      56.606  31.202  16.290  1.00 12.06           N  
ANISOU 1399  N   HIS A 166     2016   1264   1303    282     14    337       N  
ATOM   1400  CA  HIS A 166      55.777  32.059  15.469  1.00 11.62           C  
ANISOU 1400  CA  HIS A 166     1731   1169   1514    482    -54    200       C  
ATOM   1401  C   HIS A 166      56.442  32.117  14.117  1.00 12.64           C  
ANISOU 1401  C   HIS A 166     2040   1253   1509    109    -27    300       C  
ATOM   1402  O   HIS A 166      57.505  32.726  13.982  1.00 13.77           O  
ANISOU 1402  O   HIS A 166     2009   1492   1730    -60     72    230       O  
ATOM   1403  CB  HIS A 166      55.675  33.435  16.111  1.00 12.92           C  
ANISOU 1403  CB  HIS A 166     1904   1391   1614    348     27    -97       C  
ATOM   1404  CG  HIS A 166      55.231  33.366  17.530  1.00 12.95           C  
ANISOU 1404  CG  HIS A 166     1722   1598   1599    125     30   -229       C  
ATOM   1405  ND1 HIS A 166      53.907  33.464  17.895  1.00 14.97           N  
ANISOU 1405  ND1 HIS A 166     1769   2042   1877     76    -91   -129       N  
ATOM   1406  CD2 HIS A 166      55.924  33.138  18.674  1.00 13.24           C  
ANISOU 1406  CD2 HIS A 166     1840   1587   1605    272    118   -135       C  
ATOM   1407  CE1 HIS A 166      53.805  33.321  19.205  1.00 13.87           C  
ANISOU 1407  CE1 HIS A 166     1638   1933   1697   -178   -275   -227       C  
ATOM   1408  NE2 HIS A 166      55.013  33.109  19.699  1.00 12.53           N  
ANISOU 1408  NE2 HIS A 166     1606   1535   1619    164   -171    -89       N  
ATOM   1409  N   ALA A 167      55.844  31.443  13.137  1.00 13.51           N  
ANISOU 1409  N   ALA A 167     2295   1363   1474   -166    -16    145       N  
ATOM   1410  CA  ALA A 167      56.445  31.292  11.821  1.00 14.15           C  
ANISOU 1410  CA  ALA A 167     2486   1553   1337   -183   -177    283       C  
ATOM   1411  C   ALA A 167      55.765  32.250  10.865  1.00 16.35           C  
ANISOU 1411  C   ALA A 167     2829   1812   1570   -491   -335    356       C  
ATOM   1412  O   ALA A 167      54.543  32.235  10.736  1.00 19.13           O  
ANISOU 1412  O   ALA A 167     2885   2347   2034   -791   -603    724       O  
ATOM   1413  CB  ALA A 167      56.313  29.858  11.327  1.00 14.10           C  
ANISOU 1413  CB  ALA A 167     2360   1601   1398    -93     -4     77       C  
ATOM   1414  N   LYS A 168      56.545  33.120  10.237  1.00 15.95           N  
ANISOU 1414  N   LYS A 168     2977   1731   1354   -366   -165    203       N  
ATOM   1415  CA  LYS A 168      55.972  34.090   9.313  1.00 15.51           C  
ANISOU 1415  CA  LYS A 168     3036   1487   1371     28    -24    214       C  
ATOM   1416  C   LYS A 168      56.858  34.208   8.099  1.00 14.65           C  
ANISOU 1416  C   LYS A 168     2681   1493   1394     26    -61    266       C  
ATOM   1417  O   LYS A 168      58.046  34.477   8.225  1.00 15.34           O  
ANISOU 1417  O   LYS A 168     2587   1680   1560    206    -86     63       O  
ATOM   1418  CB  LYS A 168      55.821  35.476   9.955  1.00 17.08           C  
ANISOU 1418  CB  LYS A 168     3151   1750   1588   -186    125     44       C  
ATOM   1419  CG  LYS A 168      55.289  35.472  11.373  1.00 17.92           C  
ANISOU 1419  CG  LYS A 168     3009   1927   1872   -424    136     -3       C  
ATOM   1420  CD  LYS A 168      54.781  36.839  11.764  1.00 20.01           C  
ANISOU 1420  CD  LYS A 168     2981   2259   2362   -396    -10    156       C  
ATOM   1421  CE  LYS A 168      53.393  37.098  11.193  1.00 19.96           C  
ANISOU 1421  CE  LYS A 168     2912   2217   2455   -304   -216    251       C  
ATOM   1422  NZ  LYS A 168      52.354  36.244  11.841  1.00 20.56           N  
ANISOU 1422  NZ  LYS A 168     2967   2234   2609   -124   -138    277       N  
ATOM   1423  N   VAL A 169      56.290  34.010   6.923  1.00 13.43           N  
ANISOU 1423  N   VAL A 169     2537   1162   1404   -381    -11    360       N  
ATOM   1424  CA  VAL A 169      57.042  34.296   5.709  1.00 13.58           C  
ANISOU 1424  CA  VAL A 169     2424   1389   1348   -480      9    282       C  
ATOM   1425  C   VAL A 169      57.437  35.771   5.679  1.00 12.48           C  
ANISOU 1425  C   VAL A 169     1993   1352   1398    -56   -112    291       C  
ATOM   1426  O   VAL A 169      58.587  36.112   5.407  1.00 13.85           O  
ANISOU 1426  O   VAL A 169     2221   1483   1560      4    -31     61       O  
ATOM   1427  CB  VAL A 169      56.236  33.959   4.460  1.00 13.95           C  
ANISOU 1427  CB  VAL A 169     2747   1226   1329   -521     11    161       C  
ATOM   1428  CG1 VAL A 169      56.895  34.564   3.208  1.00 14.12           C  
ANISOU 1428  CG1 VAL A 169     2711   1304   1350   -340     65    136       C  
ATOM   1429  CG2 VAL A 169      56.065  32.449   4.333  1.00 15.72           C  
ANISOU 1429  CG2 VAL A 169     3204   1268   1502   -199     56    344       C  
ATOM   1430  N   SER A 170      56.478  36.627   6.009  1.00 11.85           N  
ANISOU 1430  N   SER A 170     1876   1094   1532   -237    -13    288       N  
ATOM   1431  CA  SER A 170      56.676  38.069   5.960  1.00 11.48           C  
ANISOU 1431  CA  SER A 170     1683   1232   1448    -39    159    133       C  
ATOM   1432  C   SER A 170      56.074  38.677   7.206  1.00 12.57           C  
ANISOU 1432  C   SER A 170     2153   1218   1405   -389    224    -66       C  
ATOM   1433  O   SER A 170      55.102  38.159   7.743  1.00 12.70           O  
ANISOU 1433  O   SER A 170     2255   1163   1408   -416      7    -26       O  
ATOM   1434  CB  SER A 170      56.039  38.667   4.700  1.00 11.79           C  
ANISOU 1434  CB  SER A 170     1359   1468   1654     -4    285    283       C  
ATOM   1435  OG  SER A 170      54.685  38.255   4.557  1.00 11.98           O  
ANISOU 1435  OG  SER A 170     1261   1560   1730    -32    240     17       O  
ATOM   1436  N   LEU A 171      56.642  39.792   7.655  1.00 14.34           N  
ANISOU 1436  N   LEU A 171     2576   1359   1514   -266    377   -182       N  
ATOM   1437  CA  LEU A 171      56.253  40.366   8.938  1.00 14.67           C  
ANISOU 1437  CA  LEU A 171     2321   1534   1719   -401    281   -267       C  
ATOM   1438  C   LEU A 171      55.120  41.379   8.814  1.00 15.26           C  
ANISOU 1438  C   LEU A 171     2340   1591   1868   -444    288    -76       C  
ATOM   1439  O   LEU A 171      54.143  41.297   9.563  1.00 16.14           O  
ANISOU 1439  O   LEU A 171     2390   1840   1902   -310    217     63       O  
ATOM   1440  CB  LEU A 171      57.468  41.005   9.609  1.00 14.65           C  
ANISOU 1440  CB  LEU A 171     2144   1670   1751   -174    105   -205       C  
ATOM   1441  CG  LEU A 171      58.615  40.044   9.926  1.00 15.03           C  
ANISOU 1441  CG  LEU A 171     2110   1643   1957   -201   -152    -16       C  
ATOM   1442  CD1 LEU A 171      59.744  40.771  10.653  1.00 17.81           C  
ANISOU 1442  CD1 LEU A 171     2295   2151   2321   -544   -264   -203       C  
ATOM   1443  CD2 LEU A 171      58.118  38.843  10.752  1.00 16.21           C  
ANISOU 1443  CD2 LEU A 171     2258   1783   2119   -236    -58    115       C  
ATOM   1444  N   ALA A 172      55.246  42.309   7.858  1.00 15.67           N  
ANISOU 1444  N   ALA A 172     2482   1628   1845   -409    113     84       N  
ATOM   1445  CA  ALA A 172      54.312  43.437   7.715  1.00 17.17           C  
ANISOU 1445  CA  ALA A 172     2594   1894   2034   -481   -174     -5       C  
ATOM   1446  C   ALA A 172      53.965  43.969   9.098  1.00 18.31           C  
ANISOU 1446  C   ALA A 172     2793   1929   2236   -276     71    167       C  
ATOM   1447  O   ALA A 172      54.862  44.170   9.909  1.00 19.61           O  
ANISOU 1447  O   ALA A 172     2905   2030   2518   -316   -217     61       O  
ATOM   1448  CB  ALA A 172      53.055  43.030   6.946  1.00 18.07           C  
ANISOU 1448  CB  ALA A 172     2614   2274   1980   -490   -434    -18       C  
ATOM   1449  N   GLU A 173      52.690  44.187   9.395  1.00 16.61           N  
ANISOU 1449  N   GLU A 173     2715   1463   2132    -22    297    163       N  
ATOM   1450  CA  GLU A 173      52.343  44.459  10.789  1.00 17.97           C  
ANISOU 1450  CA  GLU A 173     2965   1781   2081    113    271    131       C  
ATOM   1451  C   GLU A 173      51.653  43.249  11.388  1.00 16.99           C  
ANISOU 1451  C   GLU A 173     2748   1685   2023    -66     15     -6       C  
ATOM   1452  O   GLU A 173      51.174  43.280  12.522  1.00 18.80           O  
ANISOU 1452  O   GLU A 173     3100   1867   2175    212   -103    141       O  
ATOM   1453  CB  GLU A 173      51.457  45.698  10.919  1.00 19.97           C  
ANISOU 1453  CB  GLU A 173     3196   2017   2375   -172    445     54       C  
ATOM   1454  CG  GLU A 173      52.212  47.014  10.784  1.00 22.72           C  
ANISOU 1454  CG  GLU A 173     3435   2708   2488   -356    529    -31       C  
ATOM   1455  CD  GLU A 173      53.355  47.156  11.775  1.00 24.37           C  
ANISOU 1455  CD  GLU A 173     3635   3012   2612   -404    736      8       C  
ATOM   1456  OE1 GLU A 173      53.293  46.583  12.888  1.00 26.95           O  
ANISOU 1456  OE1 GLU A 173     4101   3213   2926   -522    381    188       O  
ATOM   1457  OE2 GLU A 173      54.332  47.846  11.431  1.00 24.08           O  
ANISOU 1457  OE2 GLU A 173     3532   2929   2689   -245    783   -198       O  
ATOM   1458  N   ARG A 174      51.622  42.173  10.617  1.00 15.02           N  
ANISOU 1458  N   ARG A 174     2468   1378   1862   -318   -156    116       N  
ATOM   1459  CA  ARG A 174      50.985  40.947  11.063  1.00 14.66           C  
ANISOU 1459  CA  ARG A 174     2188   1551   1833   -535    -78     99       C  
ATOM   1460  C   ARG A 174      51.766  40.290  12.197  1.00 15.24           C  
ANISOU 1460  C   ARG A 174     2049   1622   2120   -460     16    332       C  
ATOM   1461  O   ARG A 174      51.207  39.518  12.969  1.00 15.72           O  
ANISOU 1461  O   ARG A 174     2030   1754   2189   -485    -81    365       O  
ATOM   1462  CB  ARG A 174      50.824  39.994   9.883  1.00 15.87           C  
ANISOU 1462  CB  ARG A 174     2291   1856   1882   -474    100    139       C  
ATOM   1463  CG  ARG A 174      49.668  40.381   8.981  1.00 15.87           C  
ANISOU 1463  CG  ARG A 174     2252   1851   1927   -252    -17    220       C  
ATOM   1464  CD  ARG A 174      49.600  39.509   7.751  1.00 14.99           C  
ANISOU 1464  CD  ARG A 174     2133   1571   1990   -225    242     80       C  
ATOM   1465  NE  ARG A 174      50.590  39.897   6.757  1.00 14.47           N  
ANISOU 1465  NE  ARG A 174     1893   1581   2025   -334    211     82       N  
ATOM   1466  CZ  ARG A 174      51.773  39.317   6.598  1.00 13.88           C  
ANISOU 1466  CZ  ARG A 174     1962   1306   2005    -50    113    182       C  
ATOM   1467  NH1 ARG A 174      52.120  38.268   7.343  1.00 14.91           N  
ANISOU 1467  NH1 ARG A 174     1915   1510   2239    146   -412    358       N  
ATOM   1468  NH2 ARG A 174      52.607  39.769   5.671  1.00 13.54           N  
ANISOU 1468  NH2 ARG A 174     1673   1535   1936   -354    164     33       N  
ATOM   1469  N   VAL A 175      53.042  40.629  12.336  1.00 16.38           N  
ANISOU 1469  N   VAL A 175     2067   1884   2272   -148   -102    383       N  
ATOM   1470  CA  VAL A 175      53.831  40.068  13.420  1.00 16.43           C  
ANISOU 1470  CA  VAL A 175     2136   1765   2340   -111   -204    351       C  
ATOM   1471  C   VAL A 175      53.316  40.599  14.768  1.00 16.33           C  
ANISOU 1471  C   VAL A 175     2365   1389   2453    248   -185    367       C  
ATOM   1472  O   VAL A 175      53.506  39.969  15.811  1.00 15.70           O  
ANISOU 1472  O   VAL A 175     2111   1535   2321    -72   -196    311       O  
ATOM   1473  CB  VAL A 175      55.342  40.359  13.228  1.00 16.77           C  
ANISOU 1473  CB  VAL A 175     2167   1888   2316   -384   -394    520       C  
ATOM   1474  CG1 VAL A 175      55.620  41.856  13.291  1.00 17.64           C  
ANISOU 1474  CG1 VAL A 175     2266   2017   2418   -281   -333    454       C  
ATOM   1475  CG2 VAL A 175      56.175  39.608  14.274  1.00 16.93           C  
ANISOU 1475  CG2 VAL A 175     2069   2139   2226   -106   -381    546       C  
ATOM   1476  N  ASER A 176      52.649  41.751  14.743  0.50 18.06           N  
ANISOU 1476  N  ASER A 176     2699   1579   2585    327     26    321       N  
ATOM   1477  N  BSER A 176      52.641  41.747  14.749  0.50 17.74           N  
ANISOU 1477  N  BSER A 176     2646   1593   2503    413    -62    409       N  
ATOM   1478  CA ASER A 176      52.035  42.285  15.953  0.50 18.83           C  
ANISOU 1478  CA ASER A 176     2890   1635   2631    309    199    146       C  
ATOM   1479  CA BSER A 176      52.058  42.273  15.977  0.50 18.21           C  
ANISOU 1479  CA BSER A 176     2797   1633   2490    459      5    331       C  
ATOM   1480  C  ASER A 176      50.960  41.341  16.494  0.50 18.53           C  
ANISOU 1480  C  ASER A 176     2946   1760   2334    247    181    209       C  
ATOM   1481  C  BSER A 176      50.952  41.346  16.498  0.50 18.23           C  
ANISOU 1481  C  BSER A 176     2908   1752   2266    321     96    307       C  
ATOM   1482  O  ASER A 176      50.691  41.331  17.699  0.50 19.63           O  
ANISOU 1482  O  ASER A 176     3181   1991   2284    264    119    171       O  
ATOM   1483  O  BSER A 176      50.655  41.350  17.696  0.50 19.40           O  
ANISOU 1483  O  BSER A 176     3169   1966   2236    337     51    260       O  
ATOM   1484  CB ASER A 176      51.444  43.672  15.689  0.50 20.77           C  
ANISOU 1484  CB ASER A 176     3078   1928   2887    243    368    -24       C  
ATOM   1485  CB BSER A 176      51.521  43.693  15.763  0.50 19.50           C  
ANISOU 1485  CB BSER A 176     2902   1888   2621    529    -36    349       C  
ATOM   1486  OG ASER A 176      52.436  44.554  15.199  0.50 21.83           O  
ANISOU 1486  OG ASER A 176     3142   2132   3019    159    511   -247       O  
ATOM   1487  OG BSER A 176      50.378  43.694  14.929  0.50 19.92           O  
ANISOU 1487  OG BSER A 176     2853   2117   2601    592   -180    314       O  
ATOM   1488  N   ASP A 177      50.369  40.541  15.606  1.00 18.23           N  
ANISOU 1488  N   ASP A 177     2841   1811   2273    286    -29    192       N  
ATOM   1489  CA  ASP A 177      49.385  39.523  16.001  1.00 18.07           C  
ANISOU 1489  CA  ASP A 177     2759   1990   2117    194   -267    159       C  
ATOM   1490  C   ASP A 177      50.000  38.516  16.966  1.00 17.49           C  
ANISOU 1490  C   ASP A 177     2276   2248   2123    249   -240    176       C  
ATOM   1491  O   ASP A 177      49.307  37.948  17.810  1.00 18.60           O  
ANISOU 1491  O   ASP A 177     2174   2539   2355     69    -77    -64       O  
ATOM   1492  CB  ASP A 177      48.833  38.742  14.795  1.00 19.56           C  
ANISOU 1492  CB  ASP A 177     2974   2309   2149    387   -273    -42       C  
ATOM   1493  CG  ASP A 177      48.108  39.613  13.791  1.00 22.34           C  
ANISOU 1493  CG  ASP A 177     3443   2669   2375    456   -317   -268       C  
ATOM   1494  OD1 ASP A 177      47.977  40.834  14.016  1.00 24.18           O  
ANISOU 1494  OD1 ASP A 177     3550   3046   2593    344   -217   -241       O  
ATOM   1495  OD2 ASP A 177      47.663  39.059  12.760  1.00 23.96           O  
ANISOU 1495  OD2 ASP A 177     3554   2953   2598    350   -506    -84       O  
ATOM   1496  N   ASP A 178      51.298  38.273  16.806  1.00 15.88           N  
ANISOU 1496  N   ASP A 178     1885   2085   2062    211   -167    331       N  
ATOM   1497  CA  ASP A 178      52.007  37.275  17.608  1.00 15.43           C  
ANISOU 1497  CA  ASP A 178     1954   1857   2051     80   -324    107       C  
ATOM   1498  C   ASP A 178      52.477  37.795  18.950  1.00 14.62           C  
ANISOU 1498  C   ASP A 178     1997   1644   1912      7     -1     81       C  
ATOM   1499  O   ASP A 178      52.786  37.016  19.835  1.00 15.77           O  
ANISOU 1499  O   ASP A 178     2198   1756   2039    -12    -19    189       O  
ATOM   1500  CB  ASP A 178      53.231  36.757  16.857  1.00 16.20           C  
ANISOU 1500  CB  ASP A 178     1997   1960   2197    -84   -306   -138       C  
ATOM   1501  CG  ASP A 178      52.868  36.014  15.596  1.00 18.39           C  
ANISOU 1501  CG  ASP A 178     2362   2270   2356   -273   -201    -42       C  
ATOM   1502  OD1 ASP A 178      52.740  34.769  15.666  1.00 19.23           O  
ANISOU 1502  OD1 ASP A 178     2334   2274   2699    -38   -103   -113       O  
ATOM   1503  OD2 ASP A 178      52.715  36.678  14.548  1.00 19.60           O  
ANISOU 1503  OD2 ASP A 178     2495   2558   2394   -485   -157   -135       O  
ATOM   1504  N   ILE A 179      52.558  39.110  19.107  1.00 15.48           N  
ANISOU 1504  N   ILE A 179     2199   1571   2113    -48    -80     73       N  
ATOM   1505  CA  ILE A 179      53.175  39.658  20.309  1.00 15.35           C  
ANISOU 1505  CA  ILE A 179     2304   1498   2029    -65     49    113       C  
ATOM   1506  C   ILE A 179      52.420  39.310  21.605  1.00 16.27           C  
ANISOU 1506  C   ILE A 179     2354   1722   2105    146    120     50       C  
ATOM   1507  O   ILE A 179      53.043  38.881  22.570  1.00 16.97           O  
ANISOU 1507  O   ILE A 179     2478   1893   2076    185      2    -79       O  
ATOM   1508  CB  ILE A 179      53.344  41.186  20.184  1.00 17.30           C  
ANISOU 1508  CB  ILE A 179     2546   1728   2300   -474    -29    163       C  
ATOM   1509  CG1 ILE A 179      54.417  41.490  19.143  1.00 19.24           C  
ANISOU 1509  CG1 ILE A 179     2799   1924   2588   -558    -55    318       C  
ATOM   1510  CG2 ILE A 179      53.721  41.804  21.517  1.00 18.34           C  
ANISOU 1510  CG2 ILE A 179     2733   1935   2299   -169   -152    216       C  
ATOM   1511  CD1 ILE A 179      54.510  42.969  18.779  1.00 19.96           C  
ANISOU 1511  CD1 ILE A 179     2971   1790   2823   -637     28    298       C  
ATOM   1512  N   PRO A 180      51.081  39.450  21.630  1.00 16.31           N  
ANISOU 1512  N   PRO A 180     2101   1972   2123    -96    328     85       N  
ATOM   1513  CA  PRO A 180      50.450  39.074  22.905  1.00 18.14           C  
ANISOU 1513  CA  PRO A 180     2250   2213   2429   -150    373     68       C  
ATOM   1514  C   PRO A 180      50.624  37.590  23.238  1.00 17.31           C  
ANISOU 1514  C   PRO A 180     2217   2096   2264   -279    500    -72       C  
ATOM   1515  O   PRO A 180      50.918  37.273  24.383  1.00 18.29           O  
ANISOU 1515  O   PRO A 180     2407   2186   2355    -58    296   -268       O  
ATOM   1516  CB  PRO A 180      48.974  39.428  22.682  1.00 19.27           C  
ANISOU 1516  CB  PRO A 180     2295   2354   2672    -44    364    154       C  
ATOM   1517  CG  PRO A 180      49.008  40.512  21.640  1.00 19.16           C  
ANISOU 1517  CG  PRO A 180     2315   2233   2735    -66    389    166       C  
ATOM   1518  CD  PRO A 180      50.119  40.100  20.719  1.00 17.18           C  
ANISOU 1518  CD  PRO A 180     2158   1967   2402    -15    318    168       C  
ATOM   1519  N   ALA A 181      50.474  36.706  22.256  1.00 15.74           N  
ANISOU 1519  N   ALA A 181     1974   1923   2083   -130    460    103       N  
ATOM   1520  CA  ALA A 181      50.717  35.283  22.487  1.00 15.69           C  
ANISOU 1520  CA  ALA A 181     2074   1811   2078   -211    173     49       C  
ATOM   1521  C   ALA A 181      52.135  35.057  22.989  1.00 15.30           C  
ANISOU 1521  C   ALA A 181     2109   1754   1952   -177    136     60       C  
ATOM   1522  O   ALA A 181      52.361  34.289  23.920  1.00 15.50           O  
ANISOU 1522  O   ALA A 181     2232   1627   2031    128    281    -76       O  
ATOM   1523  CB  ALA A 181      50.476  34.481  21.214  1.00 14.79           C  
ANISOU 1523  CB  ALA A 181     2023   1605   1991   -228   -154     77       C  
ATOM   1524  N   SER A 182      53.092  35.736  22.370  1.00 15.00           N  
ANISOU 1524  N   SER A 182     1906   1985   1807   -193     11    -84       N  
ATOM   1525  CA  SER A 182      54.489  35.540  22.708  1.00 13.79           C  
ANISOU 1525  CA  SER A 182     1575   1885   1779   -156    351    -36       C  
ATOM   1526  C   SER A 182      54.784  35.976  24.136  1.00 14.83           C  
ANISOU 1526  C   SER A 182     1944   1780   1909   -137    451   -172       C  
ATOM   1527  O   SER A 182      55.488  35.283  24.868  1.00 15.08           O  
ANISOU 1527  O   SER A 182     2081   1872   1775    -90    263     -1       O  
ATOM   1528  CB  SER A 182      55.385  36.295  21.728  1.00 14.68           C  
ANISOU 1528  CB  SER A 182     1706   1919   1953   -151    268     69       C  
ATOM   1529  OG  SER A 182      56.746  36.016  21.992  1.00 14.31           O  
ANISOU 1529  OG  SER A 182     1679   2016   1743   -130      6    101       O  
ATOM   1530  N   ARG A 183      54.253  37.127  24.527  1.00 15.30           N  
ANISOU 1530  N   ARG A 183     2154   1681   1978    -83    451   -369       N  
ATOM   1531  CA  ARG A 183      54.459  37.610  25.882  1.00 17.59           C  
ANISOU 1531  CA  ARG A 183     2783   1836   2064   -287    104   -511       C  
ATOM   1532  C   ARG A 183      53.863  36.650  26.901  1.00 18.56           C  
ANISOU 1532  C   ARG A 183     2896   2150   2008   -259    357   -362       C  
ATOM   1533  O   ARG A 183      54.447  36.406  27.956  1.00 19.77           O  
ANISOU 1533  O   ARG A 183     3245   2426   1841    -96    339   -458       O  
ATOM   1534  CB  ARG A 183      53.848  38.998  26.050  1.00 19.14           C  
ANISOU 1534  CB  ARG A 183     3237   1750   2286   -345    -84   -515       C  
ATOM   1535  CG  ARG A 183      54.604  40.086  25.335  1.00 22.48           C  
ANISOU 1535  CG  ARG A 183     3554   2411   2577   -223   -212   -399       C  
ATOM   1536  CD  ARG A 183      53.937  41.430  25.560  1.00 23.97           C  
ANISOU 1536  CD  ARG A 183     3663   2601   2842    121   -339   -439       C  
ATOM   1537  NE  ARG A 183      54.605  42.493  24.820  1.00 24.54           N  
ANISOU 1537  NE  ARG A 183     3618   2675   3030    304   -345   -500       N  
ATOM   1538  CZ  ARG A 183      54.141  43.734  24.721  1.00 25.43           C  
ANISOU 1538  CZ  ARG A 183     3663   2708   3291    480   -193   -395       C  
ATOM   1539  NH1 ARG A 183      53.006  44.068  25.322  1.00 25.81           N  
ANISOU 1539  NH1 ARG A 183     3485   2884   3436    764   -247   -377       N  
ATOM   1540  NH2 ARG A 183      54.813  44.639  24.028  1.00 25.37           N  
ANISOU 1540  NH2 ARG A 183     3768   2527   3343    194   -165   -221       N  
ATOM   1541  N   ILE A 184      52.697  36.099  26.576  1.00 17.65           N  
ANISOU 1541  N   ILE A 184     2623   2102   1980   -235    383   -144       N  
ATOM   1542  CA  ILE A 184      52.043  35.140  27.461  1.00 18.81           C  
ANISOU 1542  CA  ILE A 184     2668   2446   2031     16    566   -144       C  
ATOM   1543  C   ILE A 184      52.905  33.886  27.607  1.00 17.94           C  
ANISOU 1543  C   ILE A 184     2727   2385   1705    153    600    -36       C  
ATOM   1544  O   ILE A 184      53.139  33.402  28.716  1.00 20.71           O  
ANISOU 1544  O   ILE A 184     3102   2780   1987    149    545    151       O  
ATOM   1545  CB  ILE A 184      50.640  34.777  26.937  1.00 19.68           C  
ANISOU 1545  CB  ILE A 184     2507   2557   2415     65    561    -52       C  
ATOM   1546  CG1 ILE A 184      49.688  35.960  27.139  1.00 20.86           C  
ANISOU 1546  CG1 ILE A 184     2427   2765   2735    107    259   -101       C  
ATOM   1547  CG2 ILE A 184      50.094  33.539  27.633  1.00 19.84           C  
ANISOU 1547  CG2 ILE A 184     2668   2423   2449    147    606    -47       C  
ATOM   1548  CD1 ILE A 184      48.412  35.886  26.308  1.00 22.32           C  
ANISOU 1548  CD1 ILE A 184     2468   3078   2935     85    220   -262       C  
ATOM   1549  N   MET A 185      53.390  33.366  26.482  1.00 16.15           N  
ANISOU 1549  N   MET A 185     2452   2224   1460    -40    262   -172       N  
ATOM   1550  CA  MET A 185      54.266  32.205  26.509  1.00 15.25           C  
ANISOU 1550  CA  MET A 185     2210   2195   1390      7    123   -196       C  
ATOM   1551  C   MET A 185      55.534  32.426  27.336  1.00 16.49           C  
ANISOU 1551  C   MET A 185     2380   2297   1590     -6     27   -364       C  
ATOM   1552  O   MET A 185      55.897  31.584  28.154  1.00 17.44           O  
ANISOU 1552  O   MET A 185     2504   2406   1718     10    -65   -213       O  
ATOM   1553  CB  MET A 185      54.645  31.805  25.085  1.00 13.98           C  
ANISOU 1553  CB  MET A 185     2088   1862   1359    -16    107   -353       C  
ATOM   1554  CG  MET A 185      53.474  31.297  24.277  1.00 15.63           C  
ANISOU 1554  CG  MET A 185     2102   2168   1671   -202    -30   -415       C  
ATOM   1555  SD  MET A 185      53.846  31.125  22.517  1.00 15.68           S  
ANISOU 1555  SD  MET A 185     1857   2253   1846     32     19    -85       S  
ATOM   1556  CE  MET A 185      55.148  29.899  22.599  1.00 15.80           C  
ANISOU 1556  CE  MET A 185     1819   2167   2015    421   -109   -273       C  
ATOM   1557  N   MET A 186      56.211  33.547  27.118  1.00 17.55           N  
ANISOU 1557  N   MET A 186     2485   2524   1660   -112     16   -441       N  
ATOM   1558  CA  MET A 186      57.455  33.826  27.824  1.00 18.82           C  
ANISOU 1558  CA  MET A 186     2593   2830   1729   -304     -4   -395       C  
ATOM   1559  C   MET A 186      57.175  33.993  29.314  1.00 21.19           C  
ANISOU 1559  C   MET A 186     2885   3303   1862   -287     73   -332       C  
ATOM   1560  O   MET A 186      57.978  33.583  30.149  1.00 22.45           O  
ANISOU 1560  O   MET A 186     2932   3633   1965   -474   -187   -242       O  
ATOM   1561  CB  MET A 186      58.138  35.073  27.240  1.00 18.40           C  
ANISOU 1561  CB  MET A 186     2464   2799   1729   -539    -56   -517       C  
ATOM   1562  CG  MET A 186      58.519  34.925  25.762  1.00 18.82           C  
ANISOU 1562  CG  MET A 186     2323   2947   1881   -588    158   -313       C  
ATOM   1563  SD  MET A 186      59.222  36.404  25.013  1.00 20.76           S  
ANISOU 1563  SD  MET A 186     2583   3162   2144   -617    291   -287       S  
ATOM   1564  CE  MET A 186      60.842  36.408  25.770  1.00 20.03           C  
ANISOU 1564  CE  MET A 186     2387   2955   2267   -436    207   -386       C  
ATOM   1565  N   GLY A 187      56.017  34.569  29.632  1.00 21.69           N  
ANISOU 1565  N   GLY A 187     3125   3393   1723   -159    445   -484       N  
ATOM   1566  CA  GLY A 187      55.596  34.720  31.018  1.00 22.46           C  
ANISOU 1566  CA  GLY A 187     3401   3589   1543    117    128   -367       C  
ATOM   1567  C   GLY A 187      55.382  33.387  31.713  1.00 23.33           C  
ANISOU 1567  C   GLY A 187     3564   3776   1525    191     78   -115       C  
ATOM   1568  O   GLY A 187      55.513  33.290  32.936  1.00 25.62           O  
ANISOU 1568  O   GLY A 187     4081   3994   1659    316      7    -58       O  
ATOM   1569  N   GLU A 188      55.044  32.359  30.944  1.00 22.92           N  
ANISOU 1569  N   GLU A 188     3191   3825   1694    -14   -142    -35       N  
ATOM   1570  CA  GLU A 188      54.851  31.020  31.494  1.00 24.22           C  
ANISOU 1570  CA  GLU A 188     3257   3952   1995   -130     64    116       C  
ATOM   1571  C   GLU A 188      56.102  30.167  31.338  1.00 23.41           C  
ANISOU 1571  C   GLU A 188     3222   3882   1790   -236     17    367       C  
ATOM   1572  O   GLU A 188      56.041  28.937  31.400  1.00 24.31           O  
ANISOU 1572  O   GLU A 188     3452   3889   1894   -213    208    655       O  
ATOM   1573  CB  GLU A 188      53.652  30.332  30.831  1.00 27.14           C  
ANISOU 1573  CB  GLU A 188     3547   4153   2611    -10    521    190       C  
ATOM   1574  CG  GLU A 188      52.328  31.067  31.024  1.00 31.18           C  
ANISOU 1574  CG  GLU A 188     4070   4546   3230     66    663    213       C  
ATOM   1575  CD  GLU A 188      51.955  31.256  32.489  1.00 34.33           C  
ANISOU 1575  CD  GLU A 188     4465   4850   3730    358    858    147       C  
ATOM   1576  OE1 GLU A 188      52.373  30.437  33.334  1.00 35.03           O  
ANISOU 1576  OE1 GLU A 188     4441   4866   4003    307    980    203       O  
ATOM   1577  OE2 GLU A 188      51.235  32.229  32.797  1.00 36.35           O  
ANISOU 1577  OE2 GLU A 188     4868   5060   3885    576    943    -15       O  
ATOM   1578  N   GLY A 189      57.239  30.825  31.134  1.00 21.40           N  
ANISOU 1578  N   GLY A 189     2768   3828   1533   -219   -146    330       N  
ATOM   1579  CA  GLY A 189      58.512  30.132  31.064  1.00 21.06           C  
ANISOU 1579  CA  GLY A 189     2783   3549   1672    -53   -136    395       C  
ATOM   1580  C   GLY A 189      58.707  29.291  29.818  1.00 19.59           C  
ANISOU 1580  C   GLY A 189     2469   3283   1691    -38   -180    341       C  
ATOM   1581  O   GLY A 189      59.498  28.353  29.819  1.00 22.04           O  
ANISOU 1581  O   GLY A 189     2547   3776   2050    -27   -357    300       O  
ATOM   1582  N   LEU A 190      57.990  29.628  28.750  1.00 17.09           N  
ANISOU 1582  N   LEU A 190     2204   2841   1449   -263   -185     70       N  
ATOM   1583  CA  LEU A 190      58.149  28.913  27.491  1.00 15.96           C  
ANISOU 1583  CA  LEU A 190     2049   2472   1543   -171   -105    -24       C  
ATOM   1584  C   LEU A 190      59.043  29.678  26.518  1.00 16.52           C  
ANISOU 1584  C   LEU A 190     2296   2340   1642   -218    -29     69       C  
ATOM   1585  O   LEU A 190      59.075  30.908  26.529  1.00 17.27           O  
ANISOU 1585  O   LEU A 190     2437   2274   1852    -11     52     67       O  
ATOM   1586  CB  LEU A 190      56.785  28.671  26.844  1.00 16.25           C  
ANISOU 1586  CB  LEU A 190     1957   2573   1642      8     98     69       C  
ATOM   1587  CG  LEU A 190      55.808  27.773  27.606  1.00 17.29           C  
ANISOU 1587  CG  LEU A 190     2224   2514   1830    162    197    327       C  
ATOM   1588  CD1 LEU A 190      54.386  28.005  27.121  1.00 19.13           C  
ANISOU 1588  CD1 LEU A 190     2393   2898   1980     29     11    332       C  
ATOM   1589  CD2 LEU A 190      56.184  26.309  27.432  1.00 18.52           C  
ANISOU 1589  CD2 LEU A 190     2587   2467   1984    162    340    366       C  
ATOM   1590  N   LEU A 191      59.773  28.952  25.680  1.00 14.90           N  
ANISOU 1590  N   LEU A 191     2116   2189   1355   -187    154    378       N  
ATOM   1591  CA  LEU A 191      60.474  29.598  24.575  1.00 15.40           C  
ANISOU 1591  CA  LEU A 191     2101   2116   1635     83   -108    250       C  
ATOM   1592  C   LEU A 191      59.446  30.094  23.567  1.00 14.46           C  
ANISOU 1592  C   LEU A 191     1918   1998   1578    -97    -34    158       C  
ATOM   1593  O   LEU A 191      58.487  29.388  23.251  1.00 14.61           O  
ANISOU 1593  O   LEU A 191     1845   2009   1698   -260   -111    347       O  
ATOM   1594  CB  LEU A 191      61.460  28.638  23.910  1.00 17.31           C  
ANISOU 1594  CB  LEU A 191     2213   2267   2097    210   -154    115       C  
ATOM   1595  CG  LEU A 191      62.704  28.264  24.713  1.00 20.43           C  
ANISOU 1595  CG  LEU A 191     2399   2719   2645    249    -61    -96       C  
ATOM   1596  CD1 LEU A 191      63.560  27.295  23.927  1.00 21.09           C  
ANISOU 1596  CD1 LEU A 191     2361   2848   2803    591     17    -81       C  
ATOM   1597  CD2 LEU A 191      63.486  29.514  25.063  1.00 23.50           C  
ANISOU 1597  CD2 LEU A 191     2638   3240   3051    -18   -226   -242       C  
ATOM   1598  N   SER A 192      59.639  31.316  23.085  1.00 13.27           N  
ANISOU 1598  N   SER A 192     1816   1858   1369      0   -115      3       N  
ATOM   1599  CA  SER A 192      58.758  31.873  22.062  1.00 12.76           C  
ANISOU 1599  CA  SER A 192     1708   1638   1502    -87    132     37       C  
ATOM   1600  C   SER A 192      59.609  32.470  20.951  1.00 13.02           C  
ANISOU 1600  C   SER A 192     1833   1691   1423    -59    157    -51       C  
ATOM   1601  O   SER A 192      60.096  33.595  21.061  1.00 14.68           O  
ANISOU 1601  O   SER A 192     1988   1888   1703   -239     43   -203       O  
ATOM   1602  CB  SER A 192      57.826  32.924  22.660  1.00 14.43           C  
ANISOU 1602  CB  SER A 192     1892   1917   1672    -25     20    103       C  
ATOM   1603  OG  SER A 192      56.975  33.475  21.668  1.00 15.09           O  
ANISOU 1603  OG  SER A 192     1973   1946   1813    -16   -167    -15       O  
ATOM   1604  N   VAL A 193      59.797  31.701  19.883  1.00 11.40           N  
ANISOU 1604  N   VAL A 193     1498   1622   1211     -5    276      6       N  
ATOM   1605  CA  VAL A 193      60.736  32.075  18.834  1.00 11.91           C  
ANISOU 1605  CA  VAL A 193     1493   1772   1259     26    137    202       C  
ATOM   1606  C   VAL A 193      59.993  32.645  17.637  1.00 12.26           C  
ANISOU 1606  C   VAL A 193     1670   1636   1353   -252    129    383       C  
ATOM   1607  O   VAL A 193      58.956  32.120  17.243  1.00 13.78           O  
ANISOU 1607  O   VAL A 193     1602   1932   1702   -408     57    371       O  
ATOM   1608  CB  VAL A 193      61.578  30.856  18.413  1.00 14.62           C  
ANISOU 1608  CB  VAL A 193     1786   2344   1426    327    250    433       C  
ATOM   1609  CG1 VAL A 193      62.532  31.200  17.285  1.00 15.92           C  
ANISOU 1609  CG1 VAL A 193     1845   2472   1733    134    338    326       C  
ATOM   1610  CG2 VAL A 193      62.358  30.313  19.624  1.00 16.47           C  
ANISOU 1610  CG2 VAL A 193     1985   2771   1501    302    -11    415       C  
ATOM   1611  N   LEU A 194      60.512  33.743  17.087  1.00 12.50           N  
ANISOU 1611  N   LEU A 194     1873   1594   1282   -198    114    433       N  
ATOM   1612  CA  LEU A 194      60.047  34.258  15.805  1.00 12.70           C  
ANISOU 1612  CA  LEU A 194     2046   1391   1390   -142     47    319       C  
ATOM   1613  C   LEU A 194      60.960  33.730  14.703  1.00 12.99           C  
ANISOU 1613  C   LEU A 194     1935   1508   1494   -285    120     57       C  
ATOM   1614  O   LEU A 194      62.138  34.073  14.659  1.00 15.27           O  
ANISOU 1614  O   LEU A 194     1856   2054   1891   -330    163     54       O  
ATOM   1615  CB  LEU A 194      60.047  35.793  15.814  1.00 13.09           C  
ANISOU 1615  CB  LEU A 194     2237   1267   1471     59    -15    386       C  
ATOM   1616  CG  LEU A 194      59.552  36.467  14.534  1.00 14.46           C  
ANISOU 1616  CG  LEU A 194     2220   1370   1905   -396     60    372       C  
ATOM   1617  CD1 LEU A 194      58.093  36.124  14.286  1.00 16.94           C  
ANISOU 1617  CD1 LEU A 194     2444   1782   2210   -539   -112    355       C  
ATOM   1618  CD2 LEU A 194      59.748  37.982  14.621  1.00 14.81           C  
ANISOU 1618  CD2 LEU A 194     2252   1460   1914   -232    231    264       C  
ATOM   1619  N  ASER A 195      60.410  32.891  13.830  0.78 11.84           N  
ANISOU 1619  N  ASER A 195     1948   1287   1264   -304    166     74       N  
ATOM   1620  N  BSER A 195      60.457  32.865  13.833  0.22 12.67           N  
ANISOU 1620  N  BSER A 195     1919   1414   1481   -194    139     14       N  
ATOM   1621  CA ASER A 195      61.149  32.380  12.685  0.78 12.29           C  
ANISOU 1621  CA ASER A 195     2003   1344   1325   -164     56    129       C  
ATOM   1622  CA BSER A 195      61.261  32.473  12.685  0.22 13.05           C  
ANISOU 1622  CA BSER A 195     1980   1452   1527     35     91     13       C  
ATOM   1623  C  ASER A 195      60.539  32.985  11.441  0.78 12.79           C  
ANISOU 1623  C  ASER A 195     1909   1608   1342    -46     71     -3       C  
ATOM   1624  C  BSER A 195      60.579  32.929  11.426  0.22 12.54           C  
ANISOU 1624  C  BSER A 195     1947   1402   1417     66    137     99       C  
ATOM   1625  O  ASER A 195      59.322  32.942  11.270  0.78 14.35           O  
ANISOU 1625  O  ASER A 195     1961   1980   1513   -265    148     48       O  
ATOM   1626  O  BSER A 195      59.386  32.708  11.218  0.22 12.29           O  
ANISOU 1626  O  BSER A 195     1900   1338   1433     99    225    315       O  
ATOM   1627  CB ASER A 195      61.097  30.852  12.627  0.78 12.75           C  
ANISOU 1627  CB ASER A 195     1998   1475   1370   -167    -27    411       C  
ATOM   1628  CB BSER A 195      61.508  30.973  12.640  0.22 14.18           C  
ANISOU 1628  CB BSER A 195     2038   1667   1682    260    -32    -56       C  
ATOM   1629  OG ASER A 195      61.660  30.296  13.803  0.78 13.39           O  
ANISOU 1629  OG ASER A 195     2028   1789   1270    246    141    299       O  
ATOM   1630  OG BSER A 195      62.016  30.554  11.389  0.22 14.48           O  
ANISOU 1630  OG BSER A 195     2048   1709   1745    586    -71   -241       O  
ATOM   1631  N   THR A 196      61.363  33.573  10.582  1.00 12.69           N  
ANISOU 1631  N   THR A 196     2071   1396   1352     23    147     44       N  
ATOM   1632  CA  THR A 196      60.811  34.285   9.461  1.00 12.17           C  
ANISOU 1632  CA  THR A 196     1996   1291   1336    231    301    212       C  
ATOM   1633  C   THR A 196      61.692  34.203   8.237  1.00 13.23           C  
ANISOU 1633  C   THR A 196     2076   1477   1474    183    296    135       C  
ATOM   1634  O   THR A 196      62.905  34.068   8.343  1.00 13.13           O  
ANISOU 1634  O   THR A 196     2106   1426   1457     -3    208    282       O  
ATOM   1635  CB  THR A 196      60.556  35.767   9.845  1.00 13.75           C  
ANISOU 1635  CB  THR A 196     2008   1403   1815    -61    232     32       C  
ATOM   1636  OG1 THR A 196      59.858  36.424   8.780  1.00 14.35           O  
ANISOU 1636  OG1 THR A 196     2130   1442   1880    271    350    194       O  
ATOM   1637  CG2 THR A 196      61.872  36.508  10.185  1.00 14.47           C  
ANISOU 1637  CG2 THR A 196     2008   1404   2086    -20    339   -136       C  
ATOM   1638  N   LEU A 197      61.062  34.265   7.072  1.00 13.50           N  
ANISOU 1638  N   LEU A 197     2107   1519   1501    115    180    120       N  
ATOM   1639  CA  LEU A 197      61.804  34.439   5.833  1.00 14.21           C  
ANISOU 1639  CA  LEU A 197     2122   1672   1606   -182    377     64       C  
ATOM   1640  C   LEU A 197      62.042  35.923   5.565  1.00 13.27           C  
ANISOU 1640  C   LEU A 197     1747   1642   1652    121    408    110       C  
ATOM   1641  O   LEU A 197      62.785  36.271   4.637  1.00 14.48           O  
ANISOU 1641  O   LEU A 197     1756   2018   1728    -45    303    350       O  
ATOM   1642  CB  LEU A 197      61.059  33.799   4.661  1.00 14.58           C  
ANISOU 1642  CB  LEU A 197     2345   1435   1760    -93    273   -220       C  
ATOM   1643  CG  LEU A 197      60.903  32.285   4.778  1.00 15.05           C  
ANISOU 1643  CG  LEU A 197     2116   1588   2014    118    108   -268       C  
ATOM   1644  CD1 LEU A 197      60.183  31.760   3.563  1.00 16.82           C  
ANISOU 1644  CD1 LEU A 197     2321   2005   2066    -13    -87   -450       C  
ATOM   1645  CD2 LEU A 197      62.262  31.630   4.932  1.00 16.38           C  
ANISOU 1645  CD2 LEU A 197     2020   1919   2284    363    273   -284       C  
ATOM   1646  N   ASP A 198      61.405  36.780   6.366  1.00 13.73           N  
ANISOU 1646  N   ASP A 198     1822   1719   1677   -153    430    235       N  
ATOM   1647  CA  ASP A 198      61.533  38.242   6.255  1.00 14.24           C  
ANISOU 1647  CA  ASP A 198     1841   1872   1698   -238    329    317       C  
ATOM   1648  C   ASP A 198      61.417  38.673   4.794  1.00 13.41           C  
ANISOU 1648  C   ASP A 198     1737   1767   1591   -176    514    322       C  
ATOM   1649  O   ASP A 198      62.278  39.384   4.273  1.00 13.67           O  
ANISOU 1649  O   ASP A 198     1734   1955   1505    -88    447    383       O  
ATOM   1650  CB  ASP A 198      62.860  38.721   6.862  1.00 14.16           C  
ANISOU 1650  CB  ASP A 198     1898   1761   1723   -251    173    214       C  
ATOM   1651  CG  ASP A 198      62.933  40.250   7.015  1.00 15.68           C  
ANISOU 1651  CG  ASP A 198     1922   2030   2004   -294    162    156       C  
ATOM   1652  OD1 ASP A 198      61.876  40.917   7.022  1.00 16.80           O  
ANISOU 1652  OD1 ASP A 198     2324   2084   1977   -385    356    222       O  
ATOM   1653  OD2 ASP A 198      64.057  40.778   7.149  1.00 17.35           O  
ANISOU 1653  OD2 ASP A 198     2111   2228   2253   -232    192    211       O  
ATOM   1654  N   VAL A 199      60.367  38.202   4.132  1.00 13.69           N  
ANISOU 1654  N   VAL A 199     1938   1695   1568    103    434    200       N  
ATOM   1655  CA  VAL A 199      60.123  38.565   2.741  1.00 13.34           C  
ANISOU 1655  CA  VAL A 199     1778   1667   1625     45    520    636       C  
ATOM   1656  C   VAL A 199      59.495  39.946   2.629  1.00 15.35           C  
ANISOU 1656  C   VAL A 199     2054   1760   2016   -158    716    410       C  
ATOM   1657  O   VAL A 199      58.444  40.207   3.222  1.00 18.40           O  
ANISOU 1657  O   VAL A 199     2331   2131   2532    206   1044    598       O  
ATOM   1658  CB  VAL A 199      59.197  37.555   2.040  1.00 14.08           C  
ANISOU 1658  CB  VAL A 199     1811   1832   1707    253    284    655       C  
ATOM   1659  CG1 VAL A 199      58.762  38.087   0.656  1.00 14.95           C  
ANISOU 1659  CG1 VAL A 199     1800   2036   1845    342    446    729       C  
ATOM   1660  CG2 VAL A 199      59.877  36.207   1.900  1.00 14.41           C  
ANISOU 1660  CG2 VAL A 199     1776   1906   1793    526    102    419       C  
ATOM   1661  N   LYS A 200      60.141  40.826   1.870  1.00 13.68           N  
ANISOU 1661  N   LYS A 200     2047   1430   1723   -172    143    459       N  
ATOM   1662  CA  LYS A 200      59.507  42.054   1.394  1.00 13.60           C  
ANISOU 1662  CA  LYS A 200     1888   1540   1739   -133    280    498       C  
ATOM   1663  C   LYS A 200      60.332  42.652   0.282  1.00 13.24           C  
ANISOU 1663  C   LYS A 200     1724   1627   1681    -43    327    628       C  
ATOM   1664  O   LYS A 200      61.473  43.067   0.493  1.00 14.04           O  
ANISOU 1664  O   LYS A 200     1704   2039   1591   -205    203    422       O  
ATOM   1665  CB  LYS A 200      59.327  43.102   2.494  1.00 13.99           C  
ANISOU 1665  CB  LYS A 200     1891   1609   1815    -37    202    298       C  
ATOM   1666  CG  LYS A 200      58.671  44.413   2.016  1.00 13.23           C  
ANISOU 1666  CG  LYS A 200     1582   1638   1806    -24    222     66       C  
ATOM   1667  CD  LYS A 200      57.254  44.192   1.471  1.00 13.15           C  
ANISOU 1667  CD  LYS A 200     1561   1645   1790     97     93    173       C  
ATOM   1668  CE  LYS A 200      56.572  45.529   1.144  1.00 11.85           C  
ANISOU 1668  CE  LYS A 200     1494   1338   1669    -26    -93    209       C  
ATOM   1669  NZ  LYS A 200      55.162  45.347   0.668  1.00 11.52           N  
ANISOU 1669  NZ  LYS A 200     1539   1215   1624   -258     68    238       N  
ATOM   1670  N  ASER A 201      59.747  42.652  -0.909  0.33 12.86           N  
ANISOU 1670  N  ASER A 201     1756   1514   1617    -62    304    632       N  
ATOM   1671  N  BSER A 201      59.755  42.694  -0.909  0.67 12.21           N  
ANISOU 1671  N  BSER A 201     1719   1439   1481     26    299    602       N  
ATOM   1672  CA ASER A 201      60.256  43.411  -2.039  0.33 13.56           C  
ANISOU 1672  CA ASER A 201     1770   1570   1814   -113    288    578       C  
ATOM   1673  CA BSER A 201      60.341  43.451  -2.007  0.67 13.29           C  
ANISOU 1673  CA BSER A 201     1739   1561   1751   -104    314    574       C  
ATOM   1674  C  ASER A 201      59.255  44.505  -2.356  0.33 13.74           C  
ANISOU 1674  C  ASER A 201     1740   1725   1756      2    121    403       C  
ATOM   1675  C  BSER A 201      59.280  44.388  -2.541  0.67 14.93           C  
ANISOU 1675  C  BSER A 201     1738   2030   1905   -132    132    503       C  
ATOM   1676  O  ASER A 201      58.089  44.425  -1.977  0.33 13.54           O  
ANISOU 1676  O  ASER A 201     1814   1717   1613    135     94    342       O  
ATOM   1677  O  BSER A 201      58.091  44.079  -2.496  0.67 16.52           O  
ANISOU 1677  O  BSER A 201     1928   2334   2014   -418    197    682       O  
ATOM   1678  CB ASER A 201      60.470  42.523  -3.268  0.33 15.29           C  
ANISOU 1678  CB ASER A 201     1951   1734   2125   -105    136    494       C  
ATOM   1679  CB BSER A 201      60.861  42.534  -3.113  0.67 15.65           C  
ANISOU 1679  CB BSER A 201     2137   1831   1977    127     -6    223       C  
ATOM   1680  OG ASER A 201      61.516  41.588  -3.072  0.33 16.07           O  
ANISOU 1680  OG ASER A 201     2114   1631   2361   -260     76    457       O  
ATOM   1681  OG BSER A 201      59.810  42.122  -3.968  0.67 15.96           O  
ANISOU 1681  OG BSER A 201     2416   1653   1996   -191   -229     90       O  
ATOM   1682  N   PHE A 202      59.711  45.537  -3.047  1.00 14.12           N  
ANISOU 1682  N   PHE A 202     1809   1697   1859   -116     19    374       N  
ATOM   1683  CA  PHE A 202      58.792  46.498  -3.608  1.00 13.36           C  
ANISOU 1683  CA  PHE A 202     1730   1573   1773   -252     63    185       C  
ATOM   1684  C   PHE A 202      58.872  46.332  -5.118  1.00 14.95           C  
ANISOU 1684  C   PHE A 202     1740   2045   1897   -187    209    204       C  
ATOM   1685  O   PHE A 202      59.923  46.558  -5.713  1.00 16.69           O  
ANISOU 1685  O   PHE A 202     1814   2528   1998   -147     49    376       O  
ATOM   1686  CB  PHE A 202      59.139  47.918  -3.161  1.00 14.31           C  
ANISOU 1686  CB  PHE A 202     2063   1432   1944   -384    156    186       C  
ATOM   1687  CG  PHE A 202      58.890  48.164  -1.702  1.00 14.41           C  
ANISOU 1687  CG  PHE A 202     2090   1400   1988   -600     33    107       C  
ATOM   1688  CD1 PHE A 202      57.710  48.750  -1.280  1.00 15.12           C  
ANISOU 1688  CD1 PHE A 202     2060   1555   2130   -517    -11     61       C  
ATOM   1689  CD2 PHE A 202      59.825  47.794  -0.746  1.00 15.93           C  
ANISOU 1689  CD2 PHE A 202     2298   1669   2085   -404   -166    159       C  
ATOM   1690  CE1 PHE A 202      57.471  48.986   0.064  1.00 15.49           C  
ANISOU 1690  CE1 PHE A 202     2112   1757   2015   -587   -172    159       C  
ATOM   1691  CE2 PHE A 202      59.591  48.025   0.601  1.00 16.82           C  
ANISOU 1691  CE2 PHE A 202     2127   1937   2325   -593    -94    174       C  
ATOM   1692  CZ  PHE A 202      58.417  48.621   1.004  1.00 16.02           C  
ANISOU 1692  CZ  PHE A 202     2063   1877   2146   -548   -248      6       C  
ATOM   1693  N   PRO A 203      57.782  45.863  -5.736  1.00 14.38           N  
ANISOU 1693  N   PRO A 203     1800   1923   1738   -111    208     -7       N  
ATOM   1694  CA  PRO A 203      57.831  45.685  -7.184  1.00 14.30           C  
ANISOU 1694  CA  PRO A 203     1871   1861   1700    -88    100     38       C  
ATOM   1695  C   PRO A 203      57.674  47.029  -7.876  1.00 15.06           C  
ANISOU 1695  C   PRO A 203     2124   1940   1656    -61    378    209       C  
ATOM   1696  O   PRO A 203      57.069  47.941  -7.301  1.00 15.63           O  
ANISOU 1696  O   PRO A 203     2327   1974   1639   -165    411     69       O  
ATOM   1697  CB  PRO A 203      56.639  44.769  -7.465  1.00 15.25           C  
ANISOU 1697  CB  PRO A 203     1971   1953   1869   -243    246    -97       C  
ATOM   1698  CG  PRO A 203      55.650  45.129  -6.400  1.00 15.27           C  
ANISOU 1698  CG  PRO A 203     1968   1978   1855   -311    252   -127       C  
ATOM   1699  CD  PRO A 203      56.490  45.430  -5.168  1.00 14.75           C  
ANISOU 1699  CD  PRO A 203     1828   2032   1743   -414    113     26       C  
ATOM   1700  N   PRO A 204      58.220  47.163  -9.093  1.00 15.94           N  
ANISOU 1700  N   PRO A 204     2026   2235   1794    117    230    216       N  
ATOM   1701  CA  PRO A 204      57.879  48.367  -9.850  1.00 15.42           C  
ANISOU 1701  CA  PRO A 204     1830   2273   1756   -111    337    499       C  
ATOM   1702  C   PRO A 204      56.369  48.433 -10.009  1.00 15.69           C  
ANISOU 1702  C   PRO A 204     1676   2330   1955   -191    328    544       C  
ATOM   1703  O   PRO A 204      55.749  47.382 -10.187  1.00 16.45           O  
ANISOU 1703  O   PRO A 204     1921   2504   1824   -226    102    234       O  
ATOM   1704  CB  PRO A 204      58.580  48.149 -11.199  1.00 16.18           C  
ANISOU 1704  CB  PRO A 204     2090   2445   1612    -17    532    610       C  
ATOM   1705  CG  PRO A 204      58.837  46.653 -11.276  1.00 16.59           C  
ANISOU 1705  CG  PRO A 204     2123   2517   1664     95    471    531       C  
ATOM   1706  CD  PRO A 204      59.101  46.256  -9.846  1.00 15.67           C  
ANISOU 1706  CD  PRO A 204     1784   2501   1668    143    577    486       C  
ATOM   1707  N   PRO A 205      55.783  49.636  -9.966  1.00 15.91           N  
ANISOU 1707  N   PRO A 205     1607   2235   2204   -121     42    727       N  
ATOM   1708  CA  PRO A 205      56.420  50.957  -9.898  1.00 17.47           C  
ANISOU 1708  CA  PRO A 205     1960   2306   2372   -307   -184    883       C  
ATOM   1709  C   PRO A 205      56.707  51.479  -8.490  1.00 18.01           C  
ANISOU 1709  C   PRO A 205     2201   2210   2433   -546    -75    524       C  
ATOM   1710  O   PRO A 205      56.775  52.694  -8.292  1.00 19.84           O  
ANISOU 1710  O   PRO A 205     2547   2273   2718   -735   -108    591       O  
ATOM   1711  CB  PRO A 205      55.381  51.849 -10.573  1.00 17.45           C  
ANISOU 1711  CB  PRO A 205     1713   2509   2409   -429   -115    972       C  
ATOM   1712  CG  PRO A 205      54.079  51.231 -10.105  1.00 17.02           C  
ANISOU 1712  CG  PRO A 205     1719   2306   2443   -483     -1    912       C  
ATOM   1713  CD  PRO A 205      54.322  49.749 -10.137  1.00 17.02           C  
ANISOU 1713  CD  PRO A 205     1626   2508   2332   -218    107    731       C  
ATOM   1714  N   HIS A 206      56.868  50.583  -7.525  1.00 16.38           N  
ANISOU 1714  N   HIS A 206     2174   2021   2028   -490    -36    644       N  
ATOM   1715  CA  HIS A 206      57.005  50.983  -6.128  1.00 17.49           C  
ANISOU 1715  CA  HIS A 206     2330   2284   2030   -658   -211    346       C  
ATOM   1716  C   HIS A 206      58.411  50.769  -5.573  1.00 18.81           C  
ANISOU 1716  C   HIS A 206     2486   2478   2184   -529   -379    131       C  
ATOM   1717  O   HIS A 206      58.704  51.176  -4.445  1.00 21.78           O  
ANISOU 1717  O   HIS A 206     2852   2748   2676   -442   -376   -228       O  
ATOM   1718  CB  HIS A 206      56.001  50.212  -5.264  1.00 17.75           C  
ANISOU 1718  CB  HIS A 206     2321   2357   2068   -505    -51    344       C  
ATOM   1719  CG  HIS A 206      54.600  50.263  -5.781  1.00 18.96           C  
ANISOU 1719  CG  HIS A 206     2468   2762   1974   -357     -1    311       C  
ATOM   1720  ND1 HIS A 206      53.822  51.396  -5.711  1.00 19.74           N  
ANISOU 1720  ND1 HIS A 206     2562   2882   2055   -253   -144    161       N  
ATOM   1721  CD2 HIS A 206      53.837  49.314  -6.365  1.00 18.76           C  
ANISOU 1721  CD2 HIS A 206     2503   2770   1854   -413    117    251       C  
ATOM   1722  CE1 HIS A 206      52.638  51.145  -6.240  1.00 19.97           C  
ANISOU 1722  CE1 HIS A 206     2518   3004   2067   -502    -17     27       C  
ATOM   1723  NE2 HIS A 206      52.622  49.887  -6.646  1.00 20.29           N  
ANISOU 1723  NE2 HIS A 206     2589   3112   2009   -419    113    200       N  
ATOM   1724  N   GLY A 207      59.260  50.100  -6.340  1.00 16.85           N  
ANISOU 1724  N   GLY A 207     2361   2153   1889   -723   -104    562       N  
ATOM   1725  CA  GLY A 207      60.619  49.825  -5.919  1.00 18.21           C  
ANISOU 1725  CA  GLY A 207     2415   2514   1990   -569     85    604       C  
ATOM   1726  C   GLY A 207      61.388  49.031  -6.951  1.00 19.18           C  
ANISOU 1726  C   GLY A 207     2341   2772   2175   -649     -4    862       C  
ATOM   1727  O   GLY A 207      60.994  48.970  -8.122  1.00 19.81           O  
ANISOU 1727  O   GLY A 207     2298   3079   2149   -630    -93    983       O  
ATOM   1728  N   ASP A 208      62.486  48.416  -6.516  1.00 19.39           N  
ANISOU 1728  N   ASP A 208     2257   2803   2306   -446     57    884       N  
ATOM   1729  CA  ASP A 208      63.410  47.741  -7.422  1.00 19.12           C  
ANISOU 1729  CA  ASP A 208     2196   2931   2138   -461    196    602       C  
ATOM   1730  C   ASP A 208      63.438  46.220  -7.273  1.00 17.44           C  
ANISOU 1730  C   ASP A 208     2161   2597   1869   -388    255    407       C  
ATOM   1731  O   ASP A 208      64.382  45.571  -7.723  1.00 18.55           O  
ANISOU 1731  O   ASP A 208     2470   2596   1984   -527    171    354       O  
ATOM   1732  CB  ASP A 208      64.826  48.305  -7.229  1.00 20.18           C  
ANISOU 1732  CB  ASP A 208     2144   3147   2378   -621     93    743       C  
ATOM   1733  CG  ASP A 208      65.411  47.999  -5.852  1.00 20.96           C  
ANISOU 1733  CG  ASP A 208     2079   3178   2707   -360   -239    555       C  
ATOM   1734  OD1 ASP A 208      64.726  47.369  -5.014  1.00 19.42           O  
ANISOU 1734  OD1 ASP A 208     1833   3008   2537   -206   -213    550       O  
ATOM   1735  OD2 ASP A 208      66.567  48.404  -5.611  1.00 21.88           O  
ANISOU 1735  OD2 ASP A 208     2014   3351   2950   -318   -253    773       O  
ATOM   1736  N   LEU A 209      62.413  45.671  -6.619  1.00 15.67           N  
ANISOU 1736  N   LEU A 209     2020   2350   1585   -304    314    393       N  
ATOM   1737  CA  LEU A 209      62.237  44.220  -6.438  1.00 15.59           C  
ANISOU 1737  CA  LEU A 209     2003   2489   1433   -471    317    435       C  
ATOM   1738  C   LEU A 209      63.294  43.525  -5.580  1.00 15.87           C  
ANISOU 1738  C   LEU A 209     1879   2309   1843   -554     83    628       C  
ATOM   1739  O   LEU A 209      63.226  42.316  -5.389  1.00 18.61           O  
ANISOU 1739  O   LEU A 209     2133   2605   2332   -426     27    799       O  
ATOM   1740  CB  LEU A 209      62.177  43.502  -7.792  1.00 17.42           C  
ANISOU 1740  CB  LEU A 209     2152   2938   1527   -297    260    171       C  
ATOM   1741  CG  LEU A 209      60.821  43.449  -8.497  1.00 18.35           C  
ANISOU 1741  CG  LEU A 209     2222   3044   1704   -271    218    218       C  
ATOM   1742  CD1 LEU A 209      61.008  43.054  -9.958  1.00 20.26           C  
ANISOU 1742  CD1 LEU A 209     2502   3341   1855    -19    106    204       C  
ATOM   1743  CD2 LEU A 209      59.865  42.482  -7.801  1.00 18.95           C  
ANISOU 1743  CD2 LEU A 209     2316   2923   1961   -295    331    238       C  
ATOM   1744  N   VAL A 210      64.260  44.268  -5.059  1.00 15.41           N  
ANISOU 1744  N   VAL A 210     1900   2301   1653   -462    109    741       N  
ATOM   1745  CA  VAL A 210      65.254  43.658  -4.191  1.00 14.81           C  
ANISOU 1745  CA  VAL A 210     1713   2100   1815   -560    262    660       C  
ATOM   1746  C   VAL A 210      64.606  43.343  -2.842  1.00 14.40           C  
ANISOU 1746  C   VAL A 210     1841   1831   1801   -441    331    366       C  
ATOM   1747  O   VAL A 210      63.994  44.198  -2.213  1.00 14.25           O  
ANISOU 1747  O   VAL A 210     1919   1795   1700   -257    456    155       O  
ATOM   1748  CB  VAL A 210      66.488  44.563  -4.012  1.00 14.26           C  
ANISOU 1748  CB  VAL A 210     1704   2024   1689   -524    130    544       C  
ATOM   1749  CG1 VAL A 210      67.523  43.889  -3.129  1.00 15.71           C  
ANISOU 1749  CG1 VAL A 210     1738   2374   1858   -386    291    403       C  
ATOM   1750  CG2 VAL A 210      67.095  44.875  -5.382  1.00 16.46           C  
ANISOU 1750  CG2 VAL A 210     1889   2628   1736   -313    191    239       C  
ATOM   1751  N   ASN A 211      64.751  42.098  -2.413  1.00 14.81           N  
ANISOU 1751  N   ASN A 211     2000   1873   1756   -452    327    549       N  
ATOM   1752  CA  ASN A 211      64.059  41.587  -1.240  1.00 14.24           C  
ANISOU 1752  CA  ASN A 211     1961   1682   1770   -621     61    535       C  
ATOM   1753  C   ASN A 211      64.805  41.905   0.058  1.00 14.62           C  
ANISOU 1753  C   ASN A 211     1857   1903   1796   -604    160    469       C  
ATOM   1754  O   ASN A 211      65.516  41.061   0.611  1.00 14.81           O  
ANISOU 1754  O   ASN A 211     1653   2152   1822   -452    189    446       O  
ATOM   1755  CB  ASN A 211      63.859  40.089  -1.450  1.00 13.56           C  
ANISOU 1755  CB  ASN A 211     1880   1535   1736   -688    192    580       C  
ATOM   1756  CG  ASN A 211      63.229  39.390  -0.266  1.00 14.21           C  
ANISOU 1756  CG  ASN A 211     1790   1741   1870   -387    218    382       C  
ATOM   1757  OD1 ASN A 211      62.509  39.992   0.527  1.00 14.63           O  
ANISOU 1757  OD1 ASN A 211     1671   1989   1900   -207    263    466       O  
ATOM   1758  ND2 ASN A 211      63.492  38.098  -0.158  1.00 13.90           N  
ANISOU 1758  ND2 ASN A 211     1670   1755   1855   -338    128    271       N  
ATOM   1759  N   ARG A 212      64.627  43.134   0.535  1.00 15.02           N  
ANISOU 1759  N   ARG A 212     1931   1945   1831   -696    217    243       N  
ATOM   1760  CA  ARG A 212      65.403  43.638   1.656  1.00 15.46           C  
ANISOU 1760  CA  ARG A 212     2078   2020   1778   -714    101    356       C  
ATOM   1761  C   ARG A 212      64.769  43.326   3.006  1.00 16.23           C  
ANISOU 1761  C   ARG A 212     2163   2028   1974   -512    273    175       C  
ATOM   1762  O   ARG A 212      65.387  43.537   4.044  1.00 16.70           O  
ANISOU 1762  O   ARG A 212     2270   2109   1964   -398     67    247       O  
ATOM   1763  CB  ARG A 212      65.606  45.151   1.517  1.00 16.18           C  
ANISOU 1763  CB  ARG A 212     2031   2246   1871   -979     46    385       C  
ATOM   1764  CG  ARG A 212      66.370  45.519   0.265  1.00 18.01           C  
ANISOU 1764  CG  ARG A 212     2047   2701   2093   -859    157    547       C  
ATOM   1765  CD  ARG A 212      66.717  46.992   0.226  1.00 18.93           C  
ANISOU 1765  CD  ARG A 212     2235   2730   2228   -884    104    823       C  
ATOM   1766  NE  ARG A 212      67.550  47.272  -0.939  1.00 19.42           N  
ANISOU 1766  NE  ARG A 212     2342   2740   2296   -663    153    977       N  
ATOM   1767  CZ  ARG A 212      67.069  47.537  -2.150  1.00 18.77           C  
ANISOU 1767  CZ  ARG A 212     2237   2494   2402   -825    262    994       C  
ATOM   1768  NH1 ARG A 212      65.759  47.590  -2.352  1.00 19.01           N  
ANISOU 1768  NH1 ARG A 212     2232   2565   2425   -848    356    948       N  
ATOM   1769  NH2 ARG A 212      67.898  47.760  -3.162  1.00 18.94           N  
ANISOU 1769  NH2 ARG A 212     2310   2352   2533   -826    388    954       N  
ATOM   1770  N   GLY A 213      63.533  42.837   2.997  1.00 15.32           N  
ANISOU 1770  N   GLY A 213     2066   1978   1777   -623    438    196       N  
ATOM   1771  CA  GLY A 213      62.860  42.550   4.256  1.00 15.15           C  
ANISOU 1771  CA  GLY A 213     2193   1809   1755   -520    324    180       C  
ATOM   1772  C   GLY A 213      62.386  43.794   4.994  1.00 16.07           C  
ANISOU 1772  C   GLY A 213     2105   1980   2021   -471    229    246       C  
ATOM   1773  O   GLY A 213      62.437  44.904   4.462  1.00 18.50           O  
ANISOU 1773  O   GLY A 213     2487   2400   2142   -226    555    446       O  
ATOM   1774  N  AGLU A 214      61.947  43.611   6.235  0.54 15.83           N  
ANISOU 1774  N  AGLU A 214     1913   1927   2175   -536     90    227       N  
ATOM   1775  N  BGLU A 214      61.924  43.613   6.229  0.46 15.97           N  
ANISOU 1775  N  BGLU A 214     1933   2008   2127   -689     91     22       N  
ATOM   1776  CA AGLU A 214      61.264  44.669   6.971  0.54 17.55           C  
ANISOU 1776  CA AGLU A 214     2058   2168   2440   -261    236    275       C  
ATOM   1777  CA BGLU A 214      61.272  44.693   6.972  0.46 17.68           C  
ANISOU 1777  CA BGLU A 214     2078   2307   2335   -571    217   -133       C  
ATOM   1778  C  AGLU A 214      61.823  44.901   8.370  0.54 18.22           C  
ANISOU 1778  C  AGLU A 214     2264   2231   2426   -380    284    144       C  
ATOM   1779  C  BGLU A 214      61.835  44.928   8.365  0.46 18.18           C  
ANISOU 1779  C  BGLU A 214     2236   2302   2368   -541    255    -41       C  
ATOM   1780  O  AGLU A 214      61.133  45.448   9.229  0.54 19.77           O  
ANISOU 1780  O  AGLU A 214     2429   2559   2523    -89    321    -10       O  
ATOM   1781  O  BGLU A 214      61.152  45.493   9.220  0.46 19.52           O  
ANISOU 1781  O  BGLU A 214     2358   2595   2463   -266    275   -172       O  
ATOM   1782  CB AGLU A 214      59.768  44.348   7.063  0.54 19.15           C  
ANISOU 1782  CB AGLU A 214     2140   2407   2731     15    384    491       C  
ATOM   1783  CB BGLU A 214      59.767  44.420   7.098  0.46 19.42           C  
ANISOU 1783  CB BGLU A 214     2208   2638   2533   -574    377   -348       C  
ATOM   1784  CG AGLU A 214      59.090  44.292   5.710  0.54 20.85           C  
ANISOU 1784  CG AGLU A 214     2264   2675   2983    324    352    869       C  
ATOM   1785  CG BGLU A 214      59.014  44.419   5.786  0.46 21.23           C  
ANISOU 1785  CG BGLU A 214     2404   2934   2729   -533    478   -460       C  
ATOM   1786  CD AGLU A 214      57.633  43.877   5.769  0.54 22.88           C  
ANISOU 1786  CD AGLU A 214     2502   2898   3292    463    408   1060       C  
ATOM   1787  CD BGLU A 214      57.614  44.970   5.921  0.46 22.98           C  
ANISOU 1787  CD BGLU A 214     2642   3143   2947   -695    556   -649       C  
ATOM   1788  OE1AGLU A 214      57.353  42.659   5.775  0.54 23.36           O  
ANISOU 1788  OE1AGLU A 214     2549   3015   3310    413    636   1686       O  
ATOM   1789  OE1BGLU A 214      56.669  44.326   5.422  0.46 25.30           O  
ANISOU 1789  OE1BGLU A 214     2931   3497   3185   -418    690   -692       O  
ATOM   1790  OE2AGLU A 214      56.766  44.775   5.785  0.54 24.35           O  
ANISOU 1790  OE2AGLU A 214     2634   3085   3531    368    345    658       O  
ATOM   1791  OE2BGLU A 214      57.458  46.055   6.509  0.46 22.55           O  
ANISOU 1791  OE2BGLU A 214     2611   2987   2971  -1065    414   -754       O  
ATOM   1792  N   LEU A 215      63.067  44.498   8.597  1.00 17.33           N  
ANISOU 1792  N   LEU A 215     2209   2071   2304   -735    280    176       N  
ATOM   1793  CA  LEU A 215      63.657  44.615   9.921  1.00 18.59           C  
ANISOU 1793  CA  LEU A 215     2598   2221   2243   -925    296    143       C  
ATOM   1794  C   LEU A 215      64.656  45.765  10.065  1.00 20.13           C  
ANISOU 1794  C   LEU A 215     2968   2490   2189   -987    497    206       C  
ATOM   1795  O   LEU A 215      65.191  45.978  11.147  1.00 22.07           O  
ANISOU 1795  O   LEU A 215     3296   2935   2154  -1140    375   -157       O  
ATOM   1796  CB  LEU A 215      64.316  43.288  10.316  1.00 17.83           C  
ANISOU 1796  CB  LEU A 215     2415   2220   2138   -756    384    197       C  
ATOM   1797  CG  LEU A 215      63.304  42.225  10.751  1.00 16.73           C  
ANISOU 1797  CG  LEU A 215     2148   2167   2044   -486    657    -22       C  
ATOM   1798  CD1 LEU A 215      63.910  40.822  10.777  1.00 18.16           C  
ANISOU 1798  CD1 LEU A 215     2450   2244   2207   -165    388     17       C  
ATOM   1799  CD2 LEU A 215      62.744  42.597  12.130  1.00 16.96           C  
ANISOU 1799  CD2 LEU A 215     2118   2318   2010   -518    464   -179       C  
ATOM   1800  N   GLY A 216      64.897  46.516   8.993  1.00 19.47           N  
ANISOU 1800  N   GLY A 216     2815   2285   2295   -942    573    149       N  
ATOM   1801  CA  GLY A 216      65.792  47.660   9.084  1.00 19.93           C  
ANISOU 1801  CA  GLY A 216     2689   2350   2533   -874    393    214       C  
ATOM   1802  C   GLY A 216      67.178  47.279   9.571  1.00 20.77           C  
ANISOU 1802  C   GLY A 216     2742   2462   2687   -984     21    164       C  
ATOM   1803  O   GLY A 216      67.653  46.177   9.312  1.00 21.78           O  
ANISOU 1803  O   GLY A 216     2848   2677   2751   -809     48    193       O  
ATOM   1804  N   THR A 217      67.827  48.191  10.288  1.00 20.97           N  
ANISOU 1804  N   THR A 217     2632   2470   2865  -1255      7    150       N  
ATOM   1805  CA  THR A 217      69.160  47.949  10.822  1.00 21.63           C  
ANISOU 1805  CA  THR A 217     2644   2545   3030  -1242    -29    220       C  
ATOM   1806  C   THR A 217      69.179  48.355  12.289  1.00 23.03           C  
ANISOU 1806  C   THR A 217     2798   2856   3098  -1109   -151    266       C  
ATOM   1807  O   THR A 217      68.280  49.060  12.731  1.00 22.83           O  
ANISOU 1807  O   THR A 217     2791   2949   2934   -855   -182    350       O  
ATOM   1808  CB  THR A 217      70.228  48.750  10.057  1.00 21.69           C  
ANISOU 1808  CB  THR A 217     2664   2506   3070  -1334    -65    239       C  
ATOM   1809  OG1 THR A 217      69.990  50.148  10.258  1.00 24.26           O  
ANISOU 1809  OG1 THR A 217     2941   2904   3371  -1072   -127    -91       O  
ATOM   1810  CG2 THR A 217      70.188  48.430   8.562  1.00 21.25           C  
ANISOU 1810  CG2 THR A 217     2709   2425   2942  -1269   -272     51       C  
ATOM   1811  N   PRO A 218      70.192  47.910  13.054  1.00 25.70           N  
ANISOU 1811  N   PRO A 218     3134   3233   3398   -914   -160    -49       N  
ATOM   1812  CA  PRO A 218      70.287  48.404  14.435  1.00 27.07           C  
ANISOU 1812  CA  PRO A 218     3309   3519   3457  -1035   -110   -241       C  
ATOM   1813  C   PRO A 218      70.336  49.929  14.518  1.00 28.91           C  
ANISOU 1813  C   PRO A 218     3624   3737   3622  -1120    -95   -605       C  
ATOM   1814  O   PRO A 218      69.692  50.515  15.389  1.00 28.95           O  
ANISOU 1814  O   PRO A 218     3688   3877   3434  -1057   -116   -779       O  
ATOM   1815  CB  PRO A 218      71.596  47.793  14.930  1.00 26.34           C  
ANISOU 1815  CB  PRO A 218     3037   3550   3420   -996   -185   -243       C  
ATOM   1816  CG  PRO A 218      71.713  46.521  14.164  1.00 26.33           C  
ANISOU 1816  CG  PRO A 218     2994   3487   3525   -969   -127    -71       C  
ATOM   1817  CD  PRO A 218      71.159  46.828  12.794  1.00 26.09           C  
ANISOU 1817  CD  PRO A 218     3090   3334   3490   -958   -115    -58       C  
ATOM   1818  N   ASP A 219      71.080  50.557  13.610  1.00 30.22           N  
ANISOU 1818  N   ASP A 219     3859   3718   3904  -1441     -9   -610       N  
ATOM   1819  CA  ASP A 219      71.201  52.012  13.599  1.00 32.03           C  
ANISOU 1819  CA  ASP A 219     4192   3931   4046  -1365     68   -668       C  
ATOM   1820  C   ASP A 219      69.929  52.673  13.088  1.00 29.89           C  
ANISOU 1820  C   ASP A 219     4017   3530   3811  -1508    143   -545       C  
ATOM   1821  O   ASP A 219      69.622  53.810  13.442  1.00 30.18           O  
ANISOU 1821  O   ASP A 219     3977   3512   3977  -1470     83   -637       O  
ATOM   1822  CB  ASP A 219      72.389  52.451  12.742  1.00 36.01           C  
ANISOU 1822  CB  ASP A 219     4677   4568   4438  -1250    182   -780       C  
ATOM   1823  CG  ASP A 219      73.718  51.992  13.307  1.00 40.45           C  
ANISOU 1823  CG  ASP A 219     5305   5262   4801  -1086    359   -792       C  
ATOM   1824  OD1 ASP A 219      73.806  51.769  14.533  1.00 41.56           O  
ANISOU 1824  OD1 ASP A 219     5457   5447   4888  -1154    415   -728       O  
ATOM   1825  OD2 ASP A 219      74.680  51.857  12.522  1.00 42.72           O  
ANISOU 1825  OD2 ASP A 219     5535   5589   5108   -857    455   -843       O  
ATOM   1826  N   ARG A 220      69.185  51.958  12.254  1.00 27.95           N  
ANISOU 1826  N   ARG A 220     3890   3331   3399  -1607     32   -336       N  
ATOM   1827  CA  ARG A 220      67.981  52.519  11.659  1.00 26.97           C  
ANISOU 1827  CA  ARG A 220     3946   3101   3200  -1511     68   -168       C  
ATOM   1828  C   ARG A 220      66.848  51.498  11.706  1.00 25.17           C  
ANISOU 1828  C   ARG A 220     3838   2743   2984  -1386    230   -191       C  
ATOM   1829  O   ARG A 220      66.464  50.932  10.684  1.00 24.99           O  
ANISOU 1829  O   ARG A 220     3913   2653   2930  -1042    314   -163       O  
ATOM   1830  CB  ARG A 220      68.265  52.958  10.223  1.00 27.78           C  
ANISOU 1830  CB  ARG A 220     4167   3175   3214  -1149    -29    -99       C  
ATOM   1831  CG  ARG A 220      67.311  53.989   9.688  1.00 28.68           C  
ANISOU 1831  CG  ARG A 220     4436   3258   3203  -1014   -202     38       C  
ATOM   1832  CD  ARG A 220      67.856  54.605   8.413  1.00 30.13           C  
ANISOU 1832  CD  ARG A 220     4692   3373   3381   -849   -289    263       C  
ATOM   1833  NE  ARG A 220      66.847  55.415   7.745  1.00 30.43           N  
ANISOU 1833  NE  ARG A 220     4841   3209   3513  -1013   -452    448       N  
ATOM   1834  CZ  ARG A 220      67.020  55.995   6.563  1.00 28.82           C  
ANISOU 1834  CZ  ARG A 220     4647   2807   3494  -1217   -540    589       C  
ATOM   1835  NH1 ARG A 220      68.168  55.850   5.918  1.00 27.94           N  
ANISOU 1835  NH1 ARG A 220     4610   2574   3434  -1161   -624    530       N  
ATOM   1836  NH2 ARG A 220      66.042  56.713   6.030  1.00 28.95           N  
ANISOU 1836  NH2 ARG A 220     4448   2855   3698  -1202   -698    450       N  
ATOM   1837  N   PRO A 221      66.309  51.258  12.906  1.00 23.79           N  
ANISOU 1837  N   PRO A 221     3671   2572   2794  -1435    213   -375       N  
ATOM   1838  CA  PRO A 221      65.376  50.137  13.065  1.00 23.03           C  
ANISOU 1838  CA  PRO A 221     3425   2640   2684  -1521    271   -210       C  
ATOM   1839  C   PRO A 221      63.991  50.410  12.504  1.00 22.51           C  
ANISOU 1839  C   PRO A 221     3356   2532   2664  -1278    247   -265       C  
ATOM   1840  O   PRO A 221      63.538  51.550  12.451  1.00 25.12           O  
ANISOU 1840  O   PRO A 221     3603   2882   3059   -951    236   -281       O  
ATOM   1841  CB  PRO A 221      65.314  49.954  14.584  1.00 23.36           C  
ANISOU 1841  CB  PRO A 221     3501   2759   2615  -1398    194   -214       C  
ATOM   1842  CG  PRO A 221      65.593  51.319  15.123  1.00 24.26           C  
ANISOU 1842  CG  PRO A 221     3692   2823   2703  -1321    140   -207       C  
ATOM   1843  CD  PRO A 221      66.601  51.923  14.188  1.00 23.63           C  
ANISOU 1843  CD  PRO A 221     3579   2632   2768  -1480    215   -348       C  
ATOM   1844  N   SER A 222      63.329  49.346  12.063  1.00 20.71           N  
ANISOU 1844  N   SER A 222     3045   2385   2438  -1178    185   -175       N  
ATOM   1845  CA  SER A 222      61.908  49.414  11.778  1.00 19.18           C  
ANISOU 1845  CA  SER A 222     2918   1990   2379   -836    234    -71       C  
ATOM   1846  C   SER A 222      61.179  49.164  13.087  1.00 18.86           C  
ANISOU 1846  C   SER A 222     2903   1929   2333   -881     78   -102       C  
ATOM   1847  O   SER A 222      61.804  48.778  14.078  1.00 18.62           O  
ANISOU 1847  O   SER A 222     2904   1903   2270   -696     17     97       O  
ATOM   1848  CB  SER A 222      61.510  48.376  10.743  1.00 18.07           C  
ANISOU 1848  CB  SER A 222     2789   1834   2242   -516    343      5       C  
ATOM   1849  OG  SER A 222      61.652  47.079  11.300  1.00 19.38           O  
ANISOU 1849  OG  SER A 222     3026   2101   2237   -521    403     -1       O  
ATOM   1850  N   ASP A 223      59.868  49.362  13.109  1.00 19.00           N  
ANISOU 1850  N   ASP A 223     2995   1931   2293   -593    110   -294       N  
ATOM   1851  CA  ASP A 223      59.139  49.144  14.352  1.00 19.74           C  
ANISOU 1851  CA  ASP A 223     3056   2157   2287   -548    194   -144       C  
ATOM   1852  C   ASP A 223      59.204  47.671  14.747  1.00 20.07           C  
ANISOU 1852  C   ASP A 223     3006   2255   2363   -679    151   -245       C  
ATOM   1853  O   ASP A 223      59.174  47.338  15.928  1.00 20.24           O  
ANISOU 1853  O   ASP A 223     3015   2336   2340   -945    122    -67       O  
ATOM   1854  CB  ASP A 223      57.693  49.629  14.234  1.00 21.65           C  
ANISOU 1854  CB  ASP A 223     3220   2614   2392   -470     -7   -211       C  
ATOM   1855  CG  ASP A 223      56.905  48.890  13.181  1.00 23.28           C  
ANISOU 1855  CG  ASP A 223     3260   2826   2759   -261     17   -279       C  
ATOM   1856  OD1 ASP A 223      57.508  48.171  12.359  1.00 22.73           O  
ANISOU 1856  OD1 ASP A 223     3191   2645   2798   -219   -255   -369       O  
ATOM   1857  OD2 ASP A 223      55.670  49.053  13.176  1.00 25.08           O  
ANISOU 1857  OD2 ASP A 223     3428   3181   2918   -415     17   -232       O  
ATOM   1858  N   LYS A 224      59.335  46.800  13.753  1.00 19.11           N  
ANISOU 1858  N   LYS A 224     2998   2015   2247   -609    -74     19       N  
ATOM   1859  CA  LYS A 224      59.456  45.374  14.007  1.00 19.62           C  
ANISOU 1859  CA  LYS A 224     2972   2096   2386   -763    114   -182       C  
ATOM   1860  C   LYS A 224      60.756  45.025  14.719  1.00 19.00           C  
ANISOU 1860  C   LYS A 224     2837   1974   2409   -796     50    117       C  
ATOM   1861  O   LYS A 224      60.765  44.176  15.608  1.00 19.01           O  
ANISOU 1861  O   LYS A 224     3254   1796   2173   -777     81    236       O  
ATOM   1862  CB  LYS A 224      59.330  44.602  12.698  1.00 20.77           C  
ANISOU 1862  CB  LYS A 224     2945   2278   2667   -749    418   -388       C  
ATOM   1863  CG  LYS A 224      57.893  44.484  12.233  1.00 22.94           C  
ANISOU 1863  CG  LYS A 224     3003   2742   2972   -808    583   -345       C  
ATOM   1864  CD  LYS A 224      57.797  44.421  10.748  1.00 25.87           C  
ANISOU 1864  CD  LYS A 224     3211   3344   3275   -675    618   -163       C  
ATOM   1865  CE  LYS A 224      57.987  45.788  10.147  1.00 24.56           C  
ANISOU 1865  CE  LYS A 224     3060   3215   3058   -591    819    -38       C  
ATOM   1866  NZ  LYS A 224      56.715  46.552  10.088  1.00 24.34           N  
ANISOU 1866  NZ  LYS A 224     3019   3197   3030   -608   1096   -206       N  
ATOM   1867  N  AARG A 225      61.857  45.670  14.345  0.74 19.15           N  
ANISOU 1867  N  AARG A 225     2714   2157   2404   -742    -22     57       N  
ATOM   1868  N  BARG A 225      61.846  45.681  14.334  0.26 19.29           N  
ANISOU 1868  N  BARG A 225     2724   2148   2457   -696     29     45       N  
ATOM   1869  CA AARG A 225      63.113  45.410  15.035  0.74 18.95           C  
ANISOU 1869  CA AARG A 225     2492   2312   2396   -733    -97     81       C  
ATOM   1870  CA BARG A 225      63.120  45.460  15.000  0.26 19.56           C  
ANISOU 1870  CA BARG A 225     2583   2345   2504   -627     -8     27       C  
ATOM   1871  C  AARG A 225      63.016  45.899  16.478  0.74 19.78           C  
ANISOU 1871  C  AARG A 225     2532   2561   2421   -634     -4    -48       C  
ATOM   1872  C  BARG A 225      63.037  45.918  16.452  0.26 20.24           C  
ANISOU 1872  C  BARG A 225     2677   2514   2497   -652      3    -49       C  
ATOM   1873  O  AARG A 225      63.574  45.287  17.388  0.74 20.23           O  
ANISOU 1873  O  AARG A 225     2444   2824   2417   -581    -92    210       O  
ATOM   1874  O  BARG A 225      63.626  45.306  17.342  0.26 20.56           O  
ANISOU 1874  O  BARG A 225     2658   2644   2511   -610    -47     69       O  
ATOM   1875  CB AARG A 225      64.296  46.073  14.331  0.74 19.20           C  
ANISOU 1875  CB AARG A 225     2450   2357   2488   -713   -126    108       C  
ATOM   1876  CB BARG A 225      64.254  46.187  14.279  0.26 19.63           C  
ANISOU 1876  CB BARG A 225     2447   2416   2597   -525    -28     48       C  
ATOM   1877  CG AARG A 225      65.630  45.775  15.007  0.74 19.99           C  
ANISOU 1877  CG AARG A 225     2566   2439   2592   -640     27    452       C  
ATOM   1878  CG BARG A 225      65.620  45.840  14.838  0.26 19.93           C  
ANISOU 1878  CG BARG A 225     2397   2477   2700   -418     32    115       C  
ATOM   1879  CD AARG A 225      66.808  46.329  14.227  0.74 20.95           C  
ANISOU 1879  CD AARG A 225     2819   2646   2494   -558    101    440       C  
ATOM   1880  CD BARG A 225      66.755  46.432  14.025  0.26 20.18           C  
ANISOU 1880  CD BARG A 225     2395   2573   2701   -315     91     58       C  
ATOM   1881  NE AARG A 225      66.973  45.661  12.942  0.74 20.94           N  
ANISOU 1881  NE AARG A 225     2855   2658   2444   -577    -23    331       N  
ATOM   1882  NE BARG A 225      67.976  45.661  14.225  0.26 20.15           N  
ANISOU 1882  NE BARG A 225     2346   2590   2720   -224     53     -3       N  
ATOM   1883  CZ AARG A 225      67.773  44.619  12.736  0.74 20.41           C  
ANISOU 1883  CZ AARG A 225     2681   2750   2323   -507    107    338       C  
ATOM   1884  CZ BARG A 225      68.407  44.723  13.388  0.26 20.61           C  
ANISOU 1884  CZ BARG A 225     2344   2680   2805   -227     42    -69       C  
ATOM   1885  NH1AARG A 225      68.485  44.109  13.737  0.74 20.10           N  
ANISOU 1885  NH1AARG A 225     2501   2869   2267   -717    143    223       N  
ATOM   1886  NH1BARG A 225      67.727  44.457  12.280  0.26 20.81           N  
ANISOU 1886  NH1BARG A 225     2384   2709   2814   -101     51      8       N  
ATOM   1887  NH2AARG A 225      67.851  44.078  11.530  0.74 19.94           N  
ANISOU 1887  NH2AARG A 225     2607   2745   2224   -395    298    415       N  
ATOM   1888  NH2BARG A 225      69.523  44.058  13.653  0.26 20.73           N  
ANISOU 1888  NH2BARG A 225     2310   2716   2851   -227     62   -136       N  
ATOM   1889  N   ASN A 226      62.288  46.993  16.679  1.00 20.78           N  
ANISOU 1889  N   ASN A 226     2848   2565   2483   -811     32   -115       N  
ATOM   1890  CA  ASN A 226      62.065  47.523  18.020  1.00 22.55           C  
ANISOU 1890  CA  ASN A 226     3242   2818   2510   -884    284   -136       C  
ATOM   1891  C   ASN A 226      61.271  46.547  18.895  1.00 21.50           C  
ANISOU 1891  C   ASN A 226     3047   2702   2419  -1013     84   -175       C  
ATOM   1892  O   ASN A 226      61.522  46.453  20.089  1.00 21.42           O  
ANISOU 1892  O   ASN A 226     3036   2735   2368   -408    -28   -135       O  
ATOM   1893  CB  ASN A 226      61.345  48.880  17.955  1.00 25.39           C  
ANISOU 1893  CB  ASN A 226     3777   3102   2768   -960    366   -352       C  
ATOM   1894  CG  ASN A 226      62.237  49.999  17.436  1.00 30.48           C  
ANISOU 1894  CG  ASN A 226     4456   3801   3324   -627    273   -393       C  
ATOM   1895  OD1 ASN A 226      63.459  49.949  17.576  1.00 32.77           O  
ANISOU 1895  OD1 ASN A 226     4632   4146   3675   -765    398   -335       O  
ATOM   1896  ND2 ASN A 226      61.626  51.019  16.845  1.00 32.50           N  
ANISOU 1896  ND2 ASN A 226     4886   4080   3383   -474    117   -553       N  
ATOM   1897  N   TYR A 227      60.323  45.822  18.300  1.00 21.94           N  
ANISOU 1897  N   TYR A 227     3061   2737   2538  -1042     78    -78       N  
ATOM   1898  CA  TYR A 227      59.568  44.803  19.036  1.00 22.01           C  
ANISOU 1898  CA  TYR A 227     3089   2723   2552  -1122    -41     10       C  
ATOM   1899  C   TYR A 227      60.514  43.798  19.681  1.00 21.07           C  
ANISOU 1899  C   TYR A 227     2966   2669   2372  -1069    -61    -20       C  
ATOM   1900  O   TYR A 227      60.330  43.388  20.830  1.00 20.59           O  
ANISOU 1900  O   TYR A 227     3071   2503   2250   -980    151     73       O  
ATOM   1901  CB  TYR A 227      58.600  44.041  18.117  1.00 22.83           C  
ANISOU 1901  CB  TYR A 227     3085   2938   2652   -969   -213    -39       C  
ATOM   1902  CG  TYR A 227      57.494  44.848  17.465  1.00 25.19           C  
ANISOU 1902  CG  TYR A 227     3392   3171   3008   -628    -95    211       C  
ATOM   1903  CD1 TYR A 227      56.992  46.003  18.049  1.00 26.69           C  
ANISOU 1903  CD1 TYR A 227     3582   3367   3192   -255   -150    309       C  
ATOM   1904  CD2 TYR A 227      56.943  44.434  16.256  1.00 25.76           C  
ANISOU 1904  CD2 TYR A 227     3465   3189   3134   -494   -145    287       C  
ATOM   1905  CE1 TYR A 227      55.976  46.728  17.443  1.00 28.15           C  
ANISOU 1905  CE1 TYR A 227     3771   3557   3367   -168   -136    309       C  
ATOM   1906  CE2 TYR A 227      55.932  45.152  15.643  1.00 26.33           C  
ANISOU 1906  CE2 TYR A 227     3510   3236   3259   -300    -90    435       C  
ATOM   1907  CZ  TYR A 227      55.451  46.297  16.241  1.00 27.59           C  
ANISOU 1907  CZ  TYR A 227     3649   3449   3386   -126   -197    383       C  
ATOM   1908  OH  TYR A 227      54.444  47.015  15.632  1.00 29.17           O  
ANISOU 1908  OH  TYR A 227     3863   3657   3563     -8   -261    392       O  
ATOM   1909  N   ILE A 228      61.520  43.390  18.913  1.00 20.24           N  
ANISOU 1909  N   ILE A 228     2837   2553   2300  -1103    -89   -233       N  
ATOM   1910  CA  ILE A 228      62.462  42.366  19.328  1.00 20.38           C  
ANISOU 1910  CA  ILE A 228     2976   2437   2332   -888    -15   -275       C  
ATOM   1911  C   ILE A 228      63.589  42.903  20.203  1.00 19.88           C  
ANISOU 1911  C   ILE A 228     2914   2351   2287   -865     42   -134       C  
ATOM   1912  O   ILE A 228      63.769  42.469  21.347  1.00 19.94           O  
ANISOU 1912  O   ILE A 228     2874   2463   2239   -731    -33    163       O  
ATOM   1913  CB  ILE A 228      63.077  41.676  18.097  1.00 20.74           C  
ANISOU 1913  CB  ILE A 228     3211   2472   2197   -682     31   -389       C  
ATOM   1914  CG1 ILE A 228      61.978  41.001  17.274  1.00 20.00           C  
ANISOU 1914  CG1 ILE A 228     3327   2422   1850   -715    112   -971       C  
ATOM   1915  CG2 ILE A 228      64.139  40.667  18.508  1.00 20.80           C  
ANISOU 1915  CG2 ILE A 228     3146   2364   2395   -703    188   -278       C  
ATOM   1916  CD1 ILE A 228      62.317  40.849  15.794  1.00 20.39           C  
ANISOU 1916  CD1 ILE A 228     3378   2486   1884   -615     55   -961       C  
ATOM   1917  N   GLU A 229      64.345  43.851  19.662  1.00 20.07           N  
ANISOU 1917  N   GLU A 229     2959   2399   2268  -1326     -6   -220       N  
ATOM   1918  CA  GLU A 229      65.544  44.343  20.326  1.00 22.21           C  
ANISOU 1918  CA  GLU A 229     3275   2824   2338  -1201    -62   -280       C  
ATOM   1919  C   GLU A 229      65.229  45.322  21.450  1.00 23.20           C  
ANISOU 1919  C   GLU A 229     3523   2920   2370  -1052   -137   -467       C  
ATOM   1920  O   GLU A 229      65.988  45.436  22.408  1.00 24.62           O  
ANISOU 1920  O   GLU A 229     3755   3353   2245   -716   -299   -636       O  
ATOM   1921  CB  GLU A 229      66.477  45.002  19.303  1.00 21.96           C  
ANISOU 1921  CB  GLU A 229     3256   2746   2342  -1487    125   -242       C  
ATOM   1922  CG  GLU A 229      66.963  44.041  18.220  1.00 23.17           C  
ANISOU 1922  CG  GLU A 229     3431   3016   2358  -1584    133   -371       C  
ATOM   1923  CD  GLU A 229      67.964  44.677  17.278  1.00 25.48           C  
ANISOU 1923  CD  GLU A 229     3669   3386   2626  -1426    140   -192       C  
ATOM   1924  OE1 GLU A 229      68.129  45.915  17.328  1.00 27.70           O  
ANISOU 1924  OE1 GLU A 229     3959   3656   2911  -1292    211     35       O  
ATOM   1925  OE2 GLU A 229      68.589  43.939  16.493  1.00 26.49           O  
ANISOU 1925  OE2 GLU A 229     3661   3761   2644  -1380     69   -204       O  
ATOM   1926  N   GLY A 230      64.109  46.026  21.335  1.00 22.49           N  
ANISOU 1926  N   GLY A 230     3347   2814   2386  -1254   -216   -670       N  
ATOM   1927  CA  GLY A 230      63.759  47.026  22.329  1.00 22.88           C  
ANISOU 1927  CA  GLY A 230     3422   2776   2495   -905   -172   -654       C  
ATOM   1928  C   GLY A 230      62.819  46.490  23.388  1.00 22.97           C  
ANISOU 1928  C   GLY A 230     3547   2538   2642   -826   -348   -660       C  
ATOM   1929  O   GLY A 230      63.129  46.517  24.578  1.00 25.00           O  
ANISOU 1929  O   GLY A 230     3648   2932   2919   -755   -497   -610       O  
ATOM   1930  N   HIS A 231      61.669  45.987  22.948  1.00 22.03           N  
ANISOU 1930  N   HIS A 231     3545   2137   2689   -818   -358   -626       N  
ATOM   1931  CA  HIS A 231      60.627  45.527  23.859  1.00 23.28           C  
ANISOU 1931  CA  HIS A 231     3677   2328   2841   -797    -55   -563       C  
ATOM   1932  C   HIS A 231      60.827  44.084  24.335  1.00 23.35           C  
ANISOU 1932  C   HIS A 231     3739   2545   2588   -908    134   -529       C  
ATOM   1933  O   HIS A 231      60.252  43.676  25.345  1.00 24.39           O  
ANISOU 1933  O   HIS A 231     3938   2793   2534  -1028    377   -452       O  
ATOM   1934  CB  HIS A 231      59.255  45.657  23.196  1.00 26.50           C  
ANISOU 1934  CB  HIS A 231     4003   2690   3374   -653    -60   -419       C  
ATOM   1935  CG  HIS A 231      58.864  47.068  22.883  1.00 31.80           C  
ANISOU 1935  CG  HIS A 231     4535   3493   4053   -768   -378   -253       C  
ATOM   1936  ND1 HIS A 231      57.834  47.382  22.022  1.00 34.29           N  
ANISOU 1936  ND1 HIS A 231     4874   3814   4342   -774   -477    -94       N  
ATOM   1937  CD2 HIS A 231      59.363  48.249  23.319  1.00 33.91           C  
ANISOU 1937  CD2 HIS A 231     4786   3807   4293   -658   -520   -219       C  
ATOM   1938  CE1 HIS A 231      57.717  48.695  21.939  1.00 35.39           C  
ANISOU 1938  CE1 HIS A 231     5018   3946   4481   -701   -584    -93       C  
ATOM   1939  NE2 HIS A 231      58.633  49.245  22.717  1.00 35.18           N  
ANISOU 1939  NE2 HIS A 231     4957   3923   4488   -698   -601   -118       N  
ATOM   1940  N   GLY A 232      61.634  43.315  23.608  1.00 20.80           N  
ANISOU 1940  N   GLY A 232     3344   2300   2259   -718     40   -567       N  
ATOM   1941  CA  GLY A 232      61.878  41.922  23.954  1.00 19.18           C  
ANISOU 1941  CA  GLY A 232     3006   2107   2176   -908   -163   -489       C  
ATOM   1942  C   GLY A 232      60.651  41.039  23.829  1.00 18.52           C  
ANISOU 1942  C   GLY A 232     2784   2105   2149   -577     69   -201       C  
ATOM   1943  O   GLY A 232      60.402  40.180  24.680  1.00 19.16           O  
ANISOU 1943  O   GLY A 232     2969   2295   2017   -273    -18      4       O  
ATOM   1944  N   ASP A 233      59.892  41.237  22.755  1.00 17.67           N  
ANISOU 1944  N   ASP A 233     2586   1959   2168   -436     20   -674       N  
ATOM   1945  CA  ASP A 233      58.609  40.557  22.586  1.00 17.10           C  
ANISOU 1945  CA  ASP A 233     2488   1752   2256   -564    -42   -510       C  
ATOM   1946  C   ASP A 233      58.736  39.077  22.201  1.00 16.72           C  
ANISOU 1946  C   ASP A 233     2378   1812   2164   -571     78   -333       C  
ATOM   1947  O   ASP A 233      57.738  38.364  22.204  1.00 17.83           O  
ANISOU 1947  O   ASP A 233     2254   2038   2482   -301    152   -229       O  
ATOM   1948  CB  ASP A 233      57.764  41.280  21.534  1.00 18.76           C  
ANISOU 1948  CB  ASP A 233     2650   2013   2464   -472   -109   -329       C  
ATOM   1949  CG  ASP A 233      57.214  42.604  22.031  1.00 20.92           C  
ANISOU 1949  CG  ASP A 233     2933   2247   2768   -518     94   -144       C  
ATOM   1950  OD1 ASP A 233      57.052  42.756  23.261  1.00 21.53           O  
ANISOU 1950  OD1 ASP A 233     3083   2258   2840   -430    270   -261       O  
ATOM   1951  OD2 ASP A 233      56.935  43.485  21.188  1.00 22.12           O  
ANISOU 1951  OD2 ASP A 233     2912   2499   2994   -507    268    173       O  
ATOM   1952  N   PHE A 234      59.947  38.630  21.866  1.00 15.32           N  
ANISOU 1952  N   PHE A 234     2214   1652   1955   -412     19   -208       N  
ATOM   1953  CA  PHE A 234      60.216  37.229  21.505  1.00 15.34           C  
ANISOU 1953  CA  PHE A 234     2201   1904   1721   -276   -134   -216       C  
ATOM   1954  C   PHE A 234      61.513  36.760  22.154  1.00 15.69           C  
ANISOU 1954  C   PHE A 234     2087   2138   1738   -398   -170   -212       C  
ATOM   1955  O   PHE A 234      62.392  37.569  22.447  1.00 16.91           O  
ANISOU 1955  O   PHE A 234     2309   2323   1794   -599    -64   -153       O  
ATOM   1956  CB  PHE A 234      60.311  37.047  19.975  1.00 13.89           C  
ANISOU 1956  CB  PHE A 234     1981   1806   1492   -520    -21   -123       C  
ATOM   1957  CG  PHE A 234      59.064  37.425  19.247  1.00 14.28           C  
ANISOU 1957  CG  PHE A 234     2031   1911   1486   -475   -154   -133       C  
ATOM   1958  CD1 PHE A 234      58.054  36.499  19.046  1.00 14.76           C  
ANISOU 1958  CD1 PHE A 234     2197   1880   1532   -370    -18   -181       C  
ATOM   1959  CD2 PHE A 234      58.886  38.718  18.781  1.00 14.38           C  
ANISOU 1959  CD2 PHE A 234     2014   2005   1443   -380   -238     83       C  
ATOM   1960  CE1 PHE A 234      56.889  36.855  18.391  1.00 14.89           C  
ANISOU 1960  CE1 PHE A 234     2235   1944   1480   -514    -53    -31       C  
ATOM   1961  CE2 PHE A 234      57.729  39.082  18.123  1.00 15.26           C  
ANISOU 1961  CE2 PHE A 234     2081   2092   1624   -533   -287     56       C  
ATOM   1962  CZ  PHE A 234      56.727  38.148  17.921  1.00 15.00           C  
ANISOU 1962  CZ  PHE A 234     2117   1966   1615   -606    -92     99       C  
ATOM   1963  N   SER A 235      61.633  35.453  22.374  1.00 14.70           N  
ANISOU 1963  N   SER A 235     1829   2090   1665   -155   -211    -79       N  
ATOM   1964  CA  SER A 235      62.837  34.892  22.983  1.00 15.20           C  
ANISOU 1964  CA  SER A 235     1769   2288   1720   -437   -163   -139       C  
ATOM   1965  C   SER A 235      64.042  35.132  22.090  1.00 15.19           C  
ANISOU 1965  C   SER A 235     1786   2355   1630   -760   -172   -117       C  
ATOM   1966  O   SER A 235      65.149  35.398  22.563  1.00 17.53           O  
ANISOU 1966  O   SER A 235     2161   2635   1865   -698   -309    -94       O  
ATOM   1967  CB  SER A 235      62.674  33.393  23.241  1.00 15.75           C  
ANISOU 1967  CB  SER A 235     1799   2286   1899   -410    -13   -173       C  
ATOM   1968  OG  SER A 235      61.588  33.140  24.108  1.00 16.08           O  
ANISOU 1968  OG  SER A 235     1682   2306   2122   -536     70   -134       O  
ATOM   1969  N   ALA A 236      63.802  35.015  20.788  1.00 14.57           N  
ANISOU 1969  N   ALA A 236     1882   2264   1391   -445    102    -17       N  
ATOM   1970  CA  ALA A 236      64.825  35.188  19.767  1.00 15.77           C  
ANISOU 1970  CA  ALA A 236     2005   2494   1493   -211    -33    164       C  
ATOM   1971  C   ALA A 236      64.141  35.231  18.418  1.00 14.91           C  
ANISOU 1971  C   ALA A 236     1937   2313   1417   -248     17     -4       C  
ATOM   1972  O   ALA A 236      63.012  34.777  18.282  1.00 15.45           O  
ANISOU 1972  O   ALA A 236     1804   2460   1605   -180    142      2       O  
ATOM   1973  CB  ALA A 236      65.836  34.068  19.805  1.00 15.84           C  
ANISOU 1973  CB  ALA A 236     1987   2426   1606   -212     96     33       C  
ATOM   1974  N   CYS A 237      64.824  35.804  17.434  1.00 14.07           N  
ANISOU 1974  N   CYS A 237     1927   2060   1358   -334    101    136       N  
ATOM   1975  CA  CYS A 237      64.312  35.850  16.075  1.00 14.57           C  
ANISOU 1975  CA  CYS A 237     1940   1969   1627   -287     68     49       C  
ATOM   1976  C   CYS A 237      65.347  35.269  15.131  1.00 14.93           C  
ANISOU 1976  C   CYS A 237     1988   2017   1669   -119     -1    -31       C  
ATOM   1977  O   CYS A 237      66.538  35.598  15.212  1.00 16.39           O  
ANISOU 1977  O   CYS A 237     2082   2239   1908   -172   -180   -116       O  
ATOM   1978  CB  CYS A 237      63.963  37.290  15.679  1.00 15.00           C  
ANISOU 1978  CB  CYS A 237     1986   2022   1693   -181    -57    152       C  
ATOM   1979  SG  CYS A 237      63.511  37.521  13.926  1.00 16.59           S  
ANISOU 1979  SG  CYS A 237     2163   2237   1904   -226    -55    158       S  
ATOM   1980  N   PHE A 238      64.888  34.387  14.252  1.00 14.08           N  
ANISOU 1980  N   PHE A 238     2054   1875   1420   -113    240     17       N  
ATOM   1981  CA  PHE A 238      65.748  33.787  13.245  1.00 14.74           C  
ANISOU 1981  CA  PHE A 238     2140   1898   1563   -219     91     96       C  
ATOM   1982  C   PHE A 238      65.203  34.132  11.883  1.00 14.67           C  
ANISOU 1982  C   PHE A 238     2027   1926   1620   -213     11    148       C  
ATOM   1983  O   PHE A 238      64.063  33.814  11.579  1.00 14.18           O  
ANISOU 1983  O   PHE A 238     1722   2188   1478   -253     41    199       O  
ATOM   1984  CB  PHE A 238      65.835  32.275  13.445  1.00 16.12           C  
ANISOU 1984  CB  PHE A 238     2383   2082   1660     20     66    289       C  
ATOM   1985  CG  PHE A 238      66.487  31.897  14.734  1.00 17.00           C  
ANISOU 1985  CG  PHE A 238     2490   2202   1769     82     -1    429       C  
ATOM   1986  CD1 PHE A 238      65.749  31.849  15.909  1.00 17.57           C  
ANISOU 1986  CD1 PHE A 238     2772   2120   1784     77    123    331       C  
ATOM   1987  CD2 PHE A 238      67.848  31.640  14.788  1.00 17.06           C  
ANISOU 1987  CD2 PHE A 238     2540   2018   1924    -25     76    424       C  
ATOM   1988  CE1 PHE A 238      66.354  31.522  17.106  1.00 18.09           C  
ANISOU 1988  CE1 PHE A 238     2826   2066   1981    115    105    157       C  
ATOM   1989  CE2 PHE A 238      68.454  31.326  15.983  1.00 18.47           C  
ANISOU 1989  CE2 PHE A 238     2762   2172   2083      2     34    332       C  
ATOM   1990  CZ  PHE A 238      67.706  31.266  17.142  1.00 18.87           C  
ANISOU 1990  CZ  PHE A 238     2778   2189   2204    -18     80    231       C  
ATOM   1991  N   SER A 239      66.010  34.828  11.088  1.00 14.98           N  
ANISOU 1991  N   SER A 239     2211   1972   1510   -291     88    330       N  
ATOM   1992  CA  SER A 239      65.612  35.198   9.743  1.00 14.40           C  
ANISOU 1992  CA  SER A 239     2114   1828   1527   -418    258    345       C  
ATOM   1993  C   SER A 239      66.412  34.410   8.730  1.00 14.50           C  
ANISOU 1993  C   SER A 239     1953   1865   1690   -331    203    152       C  
ATOM   1994  O   SER A 239      67.605  34.163   8.921  1.00 15.12           O  
ANISOU 1994  O   SER A 239     1980   2017   1747    -96    150     -7       O  
ATOM   1995  CB  SER A 239      65.805  36.695   9.509  1.00 14.68           C  
ANISOU 1995  CB  SER A 239     2130   1872   1576   -499     27    387       C  
ATOM   1996  OG  SER A 239      65.579  36.998   8.138  1.00 15.18           O  
ANISOU 1996  OG  SER A 239     2116   2071   1581   -264    -31    257       O  
ATOM   1997  N   TYR A 240      65.750  34.028   7.645  1.00 14.88           N  
ANISOU 1997  N   TYR A 240     1964   1972   1718   -287    210    100       N  
ATOM   1998  CA  TYR A 240      66.416  33.299   6.575  1.00 15.31           C  
ANISOU 1998  CA  TYR A 240     1996   2123   1697    -39    238    151       C  
ATOM   1999  C   TYR A 240      66.482  34.151   5.321  1.00 14.88           C  
ANISOU 1999  C   TYR A 240     1778   2032   1844     10     95    326       C  
ATOM   2000  O   TYR A 240      66.628  33.646   4.209  1.00 15.11           O  
ANISOU 2000  O   TYR A 240     1729   2227   1784    163     35    201       O  
ATOM   2001  CB  TYR A 240      65.709  31.967   6.322  1.00 15.26           C  
ANISOU 2001  CB  TYR A 240     1961   2101   1738    121    185    186       C  
ATOM   2002  CG  TYR A 240      65.692  31.129   7.576  1.00 15.43           C  
ANISOU 2002  CG  TYR A 240     2018   2071   1773    124    306    275       C  
ATOM   2003  CD1 TYR A 240      64.574  31.106   8.408  1.00 15.48           C  
ANISOU 2003  CD1 TYR A 240     1994   2199   1687     57    457    385       C  
ATOM   2004  CD2 TYR A 240      66.819  30.416   7.966  1.00 15.91           C  
ANISOU 2004  CD2 TYR A 240     1945   2194   1907    267    133    187       C  
ATOM   2005  CE1 TYR A 240      64.571  30.355   9.583  1.00 16.28           C  
ANISOU 2005  CE1 TYR A 240     2173   2169   1842     67    250    357       C  
ATOM   2006  CE2 TYR A 240      66.824  29.671   9.137  1.00 16.92           C  
ANISOU 2006  CE2 TYR A 240     2128   2302   2001    142    134    260       C  
ATOM   2007  CZ  TYR A 240      65.694  29.646   9.936  1.00 17.47           C  
ANISOU 2007  CZ  TYR A 240     2384   2299   1956    113    219    507       C  
ATOM   2008  OH  TYR A 240      65.696  28.916  11.107  1.00 18.18           O  
ANISOU 2008  OH  TYR A 240     2668   2151   2089    347    142    579       O  
ATOM   2009  N   ASN A 241      66.367  35.458   5.521  1.00 13.86           N  
ANISOU 2009  N   ASN A 241     1586   1896   1784   -205     56    450       N  
ATOM   2010  CA  ASN A 241      66.716  36.406   4.476  1.00 13.92           C  
ANISOU 2010  CA  ASN A 241     1590   2004   1695   -138    183    432       C  
ATOM   2011  C   ASN A 241      68.149  36.835   4.718  1.00 14.30           C  
ANISOU 2011  C   ASN A 241     1347   2294   1793   -197     76    238       C  
ATOM   2012  O   ASN A 241      68.424  37.504   5.710  1.00 15.23           O  
ANISOU 2012  O   ASN A 241     1705   2177   1906   -400    -47    -35       O  
ATOM   2013  CB  ASN A 241      65.776  37.613   4.497  1.00 13.75           C  
ANISOU 2013  CB  ASN A 241     1767   1728   1728     78    138    230       C  
ATOM   2014  CG  ASN A 241      65.965  38.528   3.301  1.00 14.57           C  
ANISOU 2014  CG  ASN A 241     1736   1939   1863   -175    244    258       C  
ATOM   2015  OD1 ASN A 241      67.046  38.590   2.718  1.00 14.43           O  
ANISOU 2015  OD1 ASN A 241     1547   2163   1772    -46    177    347       O  
ATOM   2016  ND2 ASN A 241      64.906  39.242   2.926  1.00 15.76           N  
ANISOU 2016  ND2 ASN A 241     2064   1916   2010   -235    389    260       N  
ATOM   2017  N   LEU A 242      69.063  36.458   3.823  1.00 15.57           N  
ANISOU 2017  N   LEU A 242     1288   2585   2044   -171    290    260       N  
ATOM   2018  CA  LEU A 242      70.470  36.811   4.009  1.00 17.61           C  
ANISOU 2018  CA  LEU A 242     1498   2968   2226   -288    344     74       C  
ATOM   2019  C   LEU A 242      70.710  38.329   4.067  1.00 17.85           C  
ANISOU 2019  C   LEU A 242     1634   2774   2375   -184    192    246       C  
ATOM   2020  O   LEU A 242      71.766  38.765   4.521  1.00 19.85           O  
ANISOU 2020  O   LEU A 242     1689   3203   2649      7    340    195       O  
ATOM   2021  CB  LEU A 242      71.324  36.195   2.902  1.00 18.92           C  
ANISOU 2021  CB  LEU A 242     1544   3302   2341   -180    492    104       C  
ATOM   2022  CG  LEU A 242      71.259  34.670   2.802  1.00 19.99           C  
ANISOU 2022  CG  LEU A 242     1641   3524   2432   -150    494    300       C  
ATOM   2023  CD1 LEU A 242      72.218  34.152   1.722  1.00 20.67           C  
ANISOU 2023  CD1 LEU A 242     1704   3617   2532     13    449     14       C  
ATOM   2024  CD2 LEU A 242      71.550  34.033   4.157  1.00 21.29           C  
ANISOU 2024  CD2 LEU A 242     1775   3753   2562   -199    401    452       C  
ATOM   2025  N   ARG A 243      69.737  39.127   3.619  1.00 17.19           N  
ANISOU 2025  N   ARG A 243     1786   2465   2280   -184    178    459       N  
ATOM   2026  CA  ARG A 243      69.841  40.591   3.696  1.00 16.89           C  
ANISOU 2026  CA  ARG A 243     1870   2497   2051   -319     29    283       C  
ATOM   2027  C   ARG A 243      69.406  41.190   5.029  1.00 16.49           C  
ANISOU 2027  C   ARG A 243     1928   2275   2062   -608    153    412       C  
ATOM   2028  O   ARG A 243      69.655  42.368   5.289  1.00 18.16           O  
ANISOU 2028  O   ARG A 243     2239   2322   2339   -712     98    241       O  
ATOM   2029  CB  ARG A 243      69.024  41.243   2.581  1.00 16.10           C  
ANISOU 2029  CB  ARG A 243     1836   2462   1818   -329    284    470       C  
ATOM   2030  CG  ARG A 243      69.562  40.942   1.205  1.00 16.47           C  
ANISOU 2030  CG  ARG A 243     1925   2559   1774   -315    182    402       C  
ATOM   2031  CD  ARG A 243      68.914  41.821   0.152  1.00 17.70           C  
ANISOU 2031  CD  ARG A 243     2004   2860   1860   -225    140    524       C  
ATOM   2032  NE  ARG A 243      69.173  41.258  -1.162  1.00 18.51           N  
ANISOU 2032  NE  ARG A 243     2045   2952   2035    -88     68    329       N  
ATOM   2033  CZ  ARG A 243      68.506  40.220  -1.662  1.00 18.62           C  
ANISOU 2033  CZ  ARG A 243     1853   2999   2223   -439    108    297       C  
ATOM   2034  NH1 ARG A 243      67.525  39.653  -0.961  1.00 17.21           N  
ANISOU 2034  NH1 ARG A 243     1775   2660   2105   -546    356    431       N  
ATOM   2035  NH2 ARG A 243      68.813  39.742  -2.857  1.00 20.79           N  
ANISOU 2035  NH2 ARG A 243     1908   3426   2564   -224    172    319       N  
ATOM   2036  N   THR A 244      68.756  40.391   5.874  1.00 15.62           N  
ANISOU 2036  N   THR A 244     1828   2253   1852   -499    289    435       N  
ATOM   2037  CA  THR A 244      68.380  40.856   7.197  1.00 16.51           C  
ANISOU 2037  CA  THR A 244     1975   2356   1944   -547    290    129       C  
ATOM   2038  C   THR A 244      69.640  41.215   7.971  1.00 18.61           C  
ANISOU 2038  C   THR A 244     2163   2735   2171   -746    231     -4       C  
ATOM   2039  O   THR A 244      70.606  40.453   7.970  1.00 19.50           O  
ANISOU 2039  O   THR A 244     2338   2795   2278   -844    275   -190       O  
ATOM   2040  CB  THR A 244      67.590  39.783   7.985  1.00 15.09           C  
ANISOU 2040  CB  THR A 244     1729   2142   1861   -528    487    294       C  
ATOM   2041  OG1 THR A 244      66.423  39.394   7.245  1.00 15.65           O  
ANISOU 2041  OG1 THR A 244     1787   2119   2041   -434    293    244       O  
ATOM   2042  CG2 THR A 244      67.183  40.314   9.353  1.00 16.16           C  
ANISOU 2042  CG2 THR A 244     1876   2244   2020   -420    345    127       C  
ATOM   2043  N   SER A 245      69.638  42.381   8.610  1.00 18.60           N  
ANISOU 2043  N   SER A 245     2283   2707   2078   -942    273    -40       N  
ATOM   2044  CA  SER A 245      70.762  42.760   9.453  1.00 21.29           C  
ANISOU 2044  CA  SER A 245     2710   3108   2273   -829    155    127       C  
ATOM   2045  C   SER A 245      70.627  42.093  10.811  1.00 21.31           C  
ANISOU 2045  C   SER A 245     2582   3222   2291   -619    122    105       C  
ATOM   2046  O   SER A 245      69.605  42.242  11.474  1.00 20.26           O  
ANISOU 2046  O   SER A 245     2230   3145   2322   -623     83    -44       O  
ATOM   2047  CB  SER A 245      70.843  44.276   9.616  1.00 24.08           C  
ANISOU 2047  CB  SER A 245     3324   3283   2540   -975     31    376       C  
ATOM   2048  OG  SER A 245      71.098  44.898   8.370  1.00 27.50           O  
ANISOU 2048  OG  SER A 245     3995   3471   2984  -1126    105    473       O  
ATOM   2049  N   PRO A 246      71.659  41.349  11.223  1.00 21.85           N  
ANISOU 2049  N   PRO A 246     2734   3288   2279   -493     64    292       N  
ATOM   2050  CA  PRO A 246      71.615  40.744  12.555  1.00 23.01           C  
ANISOU 2050  CA  PRO A 246     2935   3451   2358   -767      0    158       C  
ATOM   2051  C   PRO A 246      71.721  41.794  13.647  1.00 22.86           C  
ANISOU 2051  C   PRO A 246     2945   3408   2334  -1078    -99    185       C  
ATOM   2052  O   PRO A 246      72.155  42.921  13.406  1.00 22.80           O  
ANISOU 2052  O   PRO A 246     2817   3364   2482  -1014   -195    202       O  
ATOM   2053  CB  PRO A 246      72.833  39.817  12.564  1.00 23.58           C  
ANISOU 2053  CB  PRO A 246     3070   3443   2447   -532    132    200       C  
ATOM   2054  CG  PRO A 246      73.745  40.375  11.524  1.00 24.51           C  
ANISOU 2054  CG  PRO A 246     3160   3586   2569   -252    235    254       C  
ATOM   2055  CD  PRO A 246      72.851  40.935  10.465  1.00 23.33           C  
ANISOU 2055  CD  PRO A 246     2978   3460   2427   -322    181    361       C  
ATOM   2056  N   SER A 247      71.305  41.416  14.847  1.00 23.48           N  
ANISOU 2056  N   SER A 247     3091   3538   2292  -1211   -207    207       N  
ATOM   2057  CA  SER A 247      71.465  42.272  16.007  1.00 23.61           C  
ANISOU 2057  CA  SER A 247     2977   3640   2355  -1476   -345     98       C  
ATOM   2058  C   SER A 247      72.940  42.505  16.307  1.00 26.03           C  
ANISOU 2058  C   SER A 247     3171   4002   2715  -1432   -372    179       C  
ATOM   2059  O   SER A 247      73.778  41.652  16.018  1.00 26.08           O  
ANISOU 2059  O   SER A 247     3120   4116   2671  -1202   -339    334       O  
ATOM   2060  CB  SER A 247      70.782  41.644  17.220  1.00 23.31           C  
ANISOU 2060  CB  SER A 247     3037   3608   2212  -1403   -254    159       C  
ATOM   2061  OG  SER A 247      69.380  41.600  17.044  1.00 23.89           O  
ANISOU 2061  OG  SER A 247     3135   3633   2307  -1466   -181     65       O  
ATOM   2062  N   ASN A 248      73.249  43.659  16.892  1.00 27.43           N  
ANISOU 2062  N   ASN A 248     3218   4149   3057  -1754   -524    344       N  
ATOM   2063  CA  ASN A 248      74.567  43.877  17.474  1.00 29.95           C  
ANISOU 2063  CA  ASN A 248     3346   4523   3510  -1575   -617    342       C  
ATOM   2064  C   ASN A 248      74.780  42.921  18.648  1.00 30.40           C  
ANISOU 2064  C   ASN A 248     3255   4708   3589  -1600   -719    373       C  
ATOM   2065  O   ASN A 248      73.859  42.205  19.049  1.00 30.25           O  
ANISOU 2065  O   ASN A 248     3249   4801   3444  -1703   -687    352       O  
ATOM   2066  CB  ASN A 248      74.727  45.330  17.930  1.00 31.57           C  
ANISOU 2066  CB  ASN A 248     3450   4643   3903  -1597   -656    361       C  
ATOM   2067  CG  ASN A 248      74.699  46.311  16.774  1.00 33.76           C  
ANISOU 2067  CG  ASN A 248     3703   4860   4262  -1408   -604    251       C  
ATOM   2068  OD1 ASN A 248      75.139  46.000  15.669  1.00 33.98           O  
ANISOU 2068  OD1 ASN A 248     3631   5005   4273  -1461   -448    307       O  
ATOM   2069  ND2 ASN A 248      74.180  47.506  17.027  1.00 35.01           N  
ANISOU 2069  ND2 ASN A 248     3907   4886   4508  -1332   -636    206       N  
ATOM   2070  N   ALA A 249      75.987  42.920  19.208  1.00 31.55           N  
ANISOU 2070  N   ALA A 249     3275   4875   3837  -1352   -714    337       N  
ATOM   2071  CA  ALA A 249      76.329  42.004  20.294  1.00 32.34           C  
ANISOU 2071  CA  ALA A 249     3379   4874   4036  -1252   -755    202       C  
ATOM   2072  C   ALA A 249      75.415  42.187  21.505  1.00 31.93           C  
ANISOU 2072  C   ALA A 249     3337   4809   3984  -1241   -866    113       C  
ATOM   2073  O   ALA A 249      75.110  41.230  22.216  1.00 31.77           O  
ANISOU 2073  O   ALA A 249     3245   4915   3911  -1222   -892    275       O  
ATOM   2074  CB  ALA A 249      77.782  42.188  20.699  1.00 33.75           C  
ANISOU 2074  CB  ALA A 249     3579   4993   4253  -1232   -521    282       C  
ATOM   2075  N   THR A 250      74.981  43.420  21.737  1.00 31.46           N  
ANISOU 2075  N   THR A 250     3344   4726   3884  -1372   -897   -213       N  
ATOM   2076  CA  THR A 250      74.059  43.700  22.825  1.00 31.33           C  
ANISOU 2076  CA  THR A 250     3467   4566   3869  -1579   -769   -140       C  
ATOM   2077  C   THR A 250      72.828  44.434  22.315  1.00 29.23           C  
ANISOU 2077  C   THR A 250     3257   4290   3558  -1772   -440    -24       C  
ATOM   2078  O   THR A 250      72.912  45.272  21.416  1.00 30.25           O  
ANISOU 2078  O   THR A 250     3329   4541   3624  -1586   -170     51       O  
ATOM   2079  CB  THR A 250      74.718  44.546  23.936  1.00 33.84           C  
ANISOU 2079  CB  THR A 250     3945   4691   4222  -1593   -875   -188       C  
ATOM   2080  OG1 THR A 250      74.951  45.875  23.452  1.00 36.21           O  
ANISOU 2080  OG1 THR A 250     4363   4961   4436  -1599   -841   -188       O  
ATOM   2081  CG2 THR A 250      76.037  43.924  24.380  1.00 33.73           C  
ANISOU 2081  CG2 THR A 250     3908   4615   4292  -1577   -968   -321       C  
ATOM   2082  N   THR A 251      71.679  44.099  22.888  1.00 27.13           N  
ANISOU 2082  N   THR A 251     3263   3869   3175  -1893   -464    -85       N  
ATOM   2083  CA  THR A 251      70.446  44.816  22.618  1.00 25.26           C  
ANISOU 2083  CA  THR A 251     3167   3536   2894  -1771   -440    -71       C  
ATOM   2084  C   THR A 251      69.845  45.222  23.958  1.00 25.91           C  
ANISOU 2084  C   THR A 251     3422   3411   3012  -1564   -513   -372       C  
ATOM   2085  O   THR A 251      70.127  44.587  24.972  1.00 26.38           O  
ANISOU 2085  O   THR A 251     3646   3466   2912   -854   -512   -247       O  
ATOM   2086  CB  THR A 251      69.442  43.959  21.812  1.00 24.20           C  
ANISOU 2086  CB  THR A 251     3057   3454   2684  -1650   -596    123       C  
ATOM   2087  OG1 THR A 251      69.008  42.855  22.610  1.00 23.73           O  
ANISOU 2087  OG1 THR A 251     3041   3366   2612  -1684   -892    212       O  
ATOM   2088  CG2 THR A 251      70.075  43.438  20.526  1.00 24.90           C  
ANISOU 2088  CG2 THR A 251     3165   3532   2763  -1356   -316    265       C  
ATOM   2089  N   PRO A 252      69.034  46.290  23.971  1.00 27.56           N  
ANISOU 2089  N   PRO A 252     3744   3580   3150  -1428   -480   -547       N  
ATOM   2090  CA  PRO A 252      68.413  46.751  25.218  1.00 28.02           C  
ANISOU 2090  CA  PRO A 252     3859   3707   3080  -1303   -416   -632       C  
ATOM   2091  C   PRO A 252      67.600  45.661  25.913  1.00 26.92           C  
ANISOU 2091  C   PRO A 252     3643   3738   2849  -1271   -513   -779       C  
ATOM   2092  O   PRO A 252      67.626  45.556  27.138  1.00 28.00           O  
ANISOU 2092  O   PRO A 252     3717   4014   2907  -1027   -439   -785       O  
ATOM   2093  CB  PRO A 252      67.510  47.896  24.753  1.00 28.47           C  
ANISOU 2093  CB  PRO A 252     3943   3654   3221  -1315   -491   -647       C  
ATOM   2094  CG  PRO A 252      68.182  48.421  23.532  1.00 28.56           C  
ANISOU 2094  CG  PRO A 252     4010   3605   3236  -1420   -490   -796       C  
ATOM   2095  CD  PRO A 252      68.773  47.214  22.851  1.00 28.64           C  
ANISOU 2095  CD  PRO A 252     3972   3652   3258  -1333   -484   -672       C  
ATOM   2096  N   SER A 253      66.905  44.839  25.133  1.00 24.94           N  
ANISOU 2096  N   SER A 253     3389   3468   2617  -1293   -518   -879       N  
ATOM   2097  CA  SER A 253      66.078  43.782  25.702  1.00 24.21           C  
ANISOU 2097  CA  SER A 253     3332   3372   2495   -951   -583   -725       C  
ATOM   2098  C   SER A 253      66.855  42.503  25.999  1.00 23.22           C  
ANISOU 2098  C   SER A 253     3091   3499   2234   -648   -482   -500       C  
ATOM   2099  O   SER A 253      66.387  41.652  26.749  1.00 22.34           O  
ANISOU 2099  O   SER A 253     2983   3450   2055   -458   -139   -452       O  
ATOM   2100  CB  SER A 253      64.923  43.455  24.758  1.00 23.25           C  
ANISOU 2100  CB  SER A 253     3354   3202   2276   -856   -702   -715       C  
ATOM   2101  OG  SER A 253      65.406  42.801  23.602  1.00 22.43           O  
ANISOU 2101  OG  SER A 253     3368   2907   2248   -996   -712   -429       O  
ATOM   2102  N   GLY A 254      68.026  42.356  25.386  1.00 22.67           N  
ANISOU 2102  N   GLY A 254     2889   3595   2132   -699   -528   -455       N  
ATOM   2103  CA  GLY A 254      68.802  41.136  25.507  1.00 22.50           C  
ANISOU 2103  CA  GLY A 254     2798   3657   2093   -763   -867   -351       C  
ATOM   2104  C   GLY A 254      68.377  40.069  24.505  1.00 21.60           C  
ANISOU 2104  C   GLY A 254     2680   3445   2084   -863   -673   -305       C  
ATOM   2105  O   GLY A 254      68.939  38.980  24.468  1.00 23.04           O  
ANISOU 2105  O   GLY A 254     2757   3725   2271   -730   -632   -132       O  
ATOM   2106  N   ARG A 255      67.376  40.399  23.692  1.00 20.93           N  
ANISOU 2106  N   ARG A 255     2746   3282   1926  -1098   -396   -412       N  
ATOM   2107  CA  ARG A 255      66.862  39.490  22.672  1.00 20.24           C  
ANISOU 2107  CA  ARG A 255     2830   3083   1776  -1075   -260   -252       C  
ATOM   2108  C   ARG A 255      67.466  39.846  21.326  1.00 19.94           C  
ANISOU 2108  C   ARG A 255     2882   2893   1801  -1247   -343   -313       C  
ATOM   2109  O   ARG A 255      67.653  41.022  21.018  1.00 20.66           O  
ANISOU 2109  O   ARG A 255     3080   3006   1763  -1212   -446   -378       O  
ATOM   2110  CB  ARG A 255      65.338  39.563  22.604  1.00 19.45           C  
ANISOU 2110  CB  ARG A 255     2842   2959   1589   -965   -182   -179       C  
ATOM   2111  CG  ARG A 255      64.652  39.390  23.955  1.00 18.97           C  
ANISOU 2111  CG  ARG A 255     2854   2776   1577   -922      1   -207       C  
ATOM   2112  CD  ARG A 255      64.974  38.041  24.566  1.00 20.22           C  
ANISOU 2112  CD  ARG A 255     2902   3035   1745   -792    -53   -227       C  
ATOM   2113  NE  ARG A 255      64.269  37.852  25.832  1.00 21.91           N  
ANISOU 2113  NE  ARG A 255     3008   3305   2010   -798     38    143       N  
ATOM   2114  CZ  ARG A 255      64.297  36.732  26.547  1.00 24.65           C  
ANISOU 2114  CZ  ARG A 255     3235   3835   2298   -670     10    269       C  
ATOM   2115  NH1 ARG A 255      64.996  35.688  26.126  1.00 26.05           N  
ANISOU 2115  NH1 ARG A 255     3318   4008   2571   -581    -26    408       N  
ATOM   2116  NH2 ARG A 255      63.621  36.658  27.686  1.00 25.96           N  
ANISOU 2116  NH2 ARG A 255     3321   4190   2351   -578   -156    206       N  
ATOM   2117  N   HIS A 256      67.736  38.831  20.510  1.00 20.34           N  
ANISOU 2117  N   HIS A 256     2722   3013   1991  -1074   -448   -160       N  
ATOM   2118  CA  HIS A 256      68.502  39.042  19.292  1.00 20.93           C  
ANISOU 2118  CA  HIS A 256     2571   3131   2251   -997   -676    -49       C  
ATOM   2119  C   HIS A 256      67.813  38.556  18.028  1.00 18.52           C  
ANISOU 2119  C   HIS A 256     2113   2772   2151   -776   -374   -103       C  
ATOM   2120  O   HIS A 256      66.985  37.651  18.067  1.00 17.28           O  
ANISOU 2120  O   HIS A 256     1873   2565   2128   -511   -266     -3       O  
ATOM   2121  CB  HIS A 256      69.857  38.354  19.419  1.00 24.58           C  
ANISOU 2121  CB  HIS A 256     2990   3612   2739  -1031   -800     79       C  
ATOM   2122  CG  HIS A 256      70.766  39.002  20.413  1.00 28.26           C  
ANISOU 2122  CG  HIS A 256     3513   4092   3132  -1127   -880    -39       C  
ATOM   2123  ND1 HIS A 256      70.562  38.920  21.774  1.00 30.50           N  
ANISOU 2123  ND1 HIS A 256     3800   4373   3415  -1094   -913     25       N  
ATOM   2124  CD2 HIS A 256      71.880  39.751  20.242  1.00 30.31           C  
ANISOU 2124  CD2 HIS A 256     3812   4281   3424  -1139   -666     66       C  
ATOM   2125  CE1 HIS A 256      71.516  39.589  22.399  1.00 31.25           C  
ANISOU 2125  CE1 HIS A 256     3907   4429   3537  -1162   -793     55       C  
ATOM   2126  NE2 HIS A 256      72.329  40.101  21.492  1.00 31.08           N  
ANISOU 2126  NE2 HIS A 256     3891   4379   3538  -1184   -851     65       N  
ATOM   2127  N   ILE A 257      68.160  39.202  16.919  1.00 18.09           N  
ANISOU 2127  N   ILE A 257     2024   2745   2104   -532    -90    -52       N  
ATOM   2128  CA  ILE A 257      67.843  38.727  15.578  1.00 18.26           C  
ANISOU 2128  CA  ILE A 257     2043   2734   2160   -661     30   -119       C  
ATOM   2129  C   ILE A 257      69.073  38.017  15.014  1.00 18.31           C  
ANISOU 2129  C   ILE A 257     1842   2926   2190   -576     -4     -6       C  
ATOM   2130  O   ILE A 257      70.164  38.604  14.948  1.00 20.36           O  
ANISOU 2130  O   ILE A 257     2124   3143   2471   -300    116     91       O  
ATOM   2131  CB  ILE A 257      67.429  39.884  14.648  1.00 17.81           C  
ANISOU 2131  CB  ILE A 257     2281   2458   2028   -424    110    -87       C  
ATOM   2132  CG1 ILE A 257      66.093  40.481  15.089  1.00 18.16           C  
ANISOU 2132  CG1 ILE A 257     2379   2282   2239   -399    241    151       C  
ATOM   2133  CG2 ILE A 257      67.333  39.412  13.203  1.00 18.61           C  
ANISOU 2133  CG2 ILE A 257     2564   2481   2027   -509    -77   -474       C  
ATOM   2134  CD1 ILE A 257      65.873  41.906  14.614  1.00 19.08           C  
ANISOU 2134  CD1 ILE A 257     2654   2241   2355   -363    184    103       C  
ATOM   2135  N   TYR A 258      68.894  36.750  14.644  1.00 16.87           N  
ANISOU 2135  N   TYR A 258     1807   2852   1750   -304   -152    -10       N  
ATOM   2136  CA  TYR A 258      69.931  35.935  14.010  1.00 16.71           C  
ANISOU 2136  CA  TYR A 258     1665   2931   1753   -568     -3    313       C  
ATOM   2137  C   TYR A 258      69.586  35.700  12.544  1.00 16.10           C  
ANISOU 2137  C   TYR A 258     1605   2677   1836   -618    -42    294       C  
ATOM   2138  O   TYR A 258      68.416  35.662  12.175  1.00 16.53           O  
ANISOU 2138  O   TYR A 258     1418   2937   1927   -431   -196    190       O  
ATOM   2139  CB  TYR A 258      70.094  34.593  14.733  1.00 18.89           C  
ANISOU 2139  CB  TYR A 258     2027   3326   1822   -542    -43    372       C  
ATOM   2140  CG  TYR A 258      70.458  34.737  16.192  1.00 21.91           C  
ANISOU 2140  CG  TYR A 258     2345   3980   1998   -471   -199    371       C  
ATOM   2141  CD1 TYR A 258      71.770  34.990  16.579  1.00 24.34           C  
ANISOU 2141  CD1 TYR A 258     2523   4599   2127   -356   -201    319       C  
ATOM   2142  CD2 TYR A 258      69.489  34.636  17.183  1.00 22.18           C  
ANISOU 2142  CD2 TYR A 258     2441   3994   1993   -350    -65    262       C  
ATOM   2143  CE1 TYR A 258      72.107  35.134  17.915  1.00 25.44           C  
ANISOU 2143  CE1 TYR A 258     2685   4855   2124   -272   -335    406       C  
ATOM   2144  CE2 TYR A 258      69.816  34.779  18.515  1.00 23.47           C  
ANISOU 2144  CE2 TYR A 258     2565   4372   1982   -307   -172    441       C  
ATOM   2145  CZ  TYR A 258      71.124  35.028  18.876  1.00 25.58           C  
ANISOU 2145  CZ  TYR A 258     2798   4874   2048   -261   -381    424       C  
ATOM   2146  OH  TYR A 258      71.445  35.167  20.209  1.00 27.68           O  
ANISOU 2146  OH  TYR A 258     2992   5236   2291   -384   -686    379       O  
ATOM   2147  N   VAL A 259      70.611  35.540  11.716  1.00 16.51           N  
ANISOU 2147  N   VAL A 259     2090   2366   1816   -513     71    124       N  
ATOM   2148  CA  VAL A 259      70.420  35.436  10.273  1.00 17.82           C  
ANISOU 2148  CA  VAL A 259     2162   2616   1991   -469     28     23       C  
ATOM   2149  C   VAL A 259      71.228  34.266   9.731  1.00 18.95           C  
ANISOU 2149  C   VAL A 259     2324   2746   2131   -304   -132    -32       C  
ATOM   2150  O   VAL A 259      72.410  34.125  10.048  1.00 19.90           O  
ANISOU 2150  O   VAL A 259     2414   3025   2120   -261   -244    111       O  
ATOM   2151  CB  VAL A 259      70.845  36.738   9.546  1.00 18.67           C  
ANISOU 2151  CB  VAL A 259     2376   2658   2061   -284   -104    -32       C  
ATOM   2152  CG1 VAL A 259      70.605  36.628   8.046  1.00 18.61           C  
ANISOU 2152  CG1 VAL A 259     2512   2636   1924   -194    -18     69       C  
ATOM   2153  CG2 VAL A 259      70.103  37.943  10.109  1.00 19.17           C  
ANISOU 2153  CG2 VAL A 259     2341   2775   2167   -341   -100   -174       C  
ATOM   2154  N   SER A 260      70.606  33.428   8.906  1.00 19.24           N  
ANISOU 2154  N   SER A 260     2411   2664   2235    -56   -182     81       N  
ATOM   2155  CA  SER A 260      71.322  32.291   8.331  1.00 19.69           C  
ANISOU 2155  CA  SER A 260     2439   2829   2213     34   -145    -31       C  
ATOM   2156  C   SER A 260      70.690  31.803   7.048  1.00 19.59           C  
ANISOU 2156  C   SER A 260     2386   2852   2206    286    -38    -10       C  
ATOM   2157  O   SER A 260      69.582  32.207   6.696  1.00 19.73           O  
ANISOU 2157  O   SER A 260     2337   2916   2242    260    -31     69       O  
ATOM   2158  CB  SER A 260      71.390  31.128   9.326  1.00 21.38           C  
ANISOU 2158  CB  SER A 260     2711   2914   2497    -51   -235    -17       C  
ATOM   2159  OG  SER A 260      70.163  30.417   9.383  1.00 22.54           O  
ANISOU 2159  OG  SER A 260     2829   3185   2552    -54   -335     45       O  
ATOM   2160  N   GLY A 261      71.413  30.929   6.353  1.00 19.76           N  
ANISOU 2160  N   GLY A 261     2506   2844   2157    552    159   -163       N  
ATOM   2161  CA  GLY A 261      70.841  30.167   5.263  1.00 20.05           C  
ANISOU 2161  CA  GLY A 261     2371   2980   2267    671    393   -210       C  
ATOM   2162  C   GLY A 261      69.899  29.128   5.844  1.00 19.94           C  
ANISOU 2162  C   GLY A 261     2538   3039   2001    438    324     63       C  
ATOM   2163  O   GLY A 261      69.812  28.970   7.066  1.00 20.50           O  
ANISOU 2163  O   GLY A 261     2764   3070   1956    282    178    -27       O  
ATOM   2164  N   PHE A 262      69.191  28.408   4.986  1.00 20.21           N  
ANISOU 2164  N   PHE A 262     2378   3219   2080    348    293     68       N  
ATOM   2165  CA  PHE A 262      68.162  27.492   5.458  1.00 20.37           C  
ANISOU 2165  CA  PHE A 262     2489   3185   2068    276    494    326       C  
ATOM   2166  C   PHE A 262      68.628  26.043   5.440  1.00 23.95           C  
ANISOU 2166  C   PHE A 262     2991   3634   2475    645    552    235       C  
ATOM   2167  O   PHE A 262      68.476  25.324   6.424  1.00 26.25           O  
ANISOU 2167  O   PHE A 262     3306   3875   2793    836    425    418       O  
ATOM   2168  CB  PHE A 262      66.892  27.654   4.623  1.00 17.83           C  
ANISOU 2168  CB  PHE A 262     2122   2732   1920    111    271    202       C  
ATOM   2169  CG  PHE A 262      65.707  26.921   5.173  1.00 17.48           C  
ANISOU 2169  CG  PHE A 262     2173   2588   1882    241    164    550       C  
ATOM   2170  CD1 PHE A 262      65.028  27.407   6.279  1.00 18.41           C  
ANISOU 2170  CD1 PHE A 262     2208   2660   2125    157    210    602       C  
ATOM   2171  CD2 PHE A 262      65.252  25.759   4.568  1.00 17.73           C  
ANISOU 2171  CD2 PHE A 262     2258   2550   1929    498    199    390       C  
ATOM   2172  CE1 PHE A 262      63.923  26.742   6.781  1.00 19.20           C  
ANISOU 2172  CE1 PHE A 262     2340   2802   2152    111    260    662       C  
ATOM   2173  CE2 PHE A 262      64.148  25.082   5.067  1.00 18.42           C  
ANISOU 2173  CE2 PHE A 262     2389   2714   1898    424    131    549       C  
ATOM   2174  CZ  PHE A 262      63.485  25.578   6.180  1.00 19.67           C  
ANISOU 2174  CZ  PHE A 262     2421   2922   2130    173     89    631       C  
ATOM   2175  N   SER A 263      69.197  25.616   4.324  1.00 25.65           N  
ANISOU 2175  N   SER A 263     3247   3686   2813    850    525    -62       N  
ATOM   2176  CA  SER A 263      69.690  24.253   4.207  1.00 27.36           C  
ANISOU 2176  CA  SER A 263     3392   3974   3030    864    462     31       C  
ATOM   2177  C   SER A 263      70.951  24.052   5.040  1.00 28.21           C  
ANISOU 2177  C   SER A 263     3243   4236   3239    769    397    -60       C  
ATOM   2178  O   SER A 263      71.687  25.005   5.309  1.00 29.81           O  
ANISOU 2178  O   SER A 263     3428   4442   3458    634    226   -389       O  
ATOM   2179  CB  SER A 263      69.969  23.916   2.745  1.00 27.86           C  
ANISOU 2179  CB  SER A 263     3582   4065   2939    869    707     95       C  
ATOM   2180  OG  SER A 263      71.055  24.683   2.265  1.00 30.09           O  
ANISOU 2180  OG  SER A 263     3889   4278   3267    826    899     57       O  
ATOM   2181  N   GLY A 264      71.192  22.808   5.441  1.00 27.11           N  
ANISOU 2181  N   GLY A 264     2943   4178   3179    898    216    311       N  
ATOM   2182  CA  GLY A 264      72.357  22.472   6.240  1.00 27.29           C  
ANISOU 2182  CA  GLY A 264     2799   4275   3293    715     80    476       C  
ATOM   2183  C   GLY A 264      72.034  21.455   7.322  1.00 27.59           C  
ANISOU 2183  C   GLY A 264     2834   4294   3353    798   -137    428       C  
ATOM   2184  O   GLY A 264      70.988  20.804   7.286  1.00 26.65           O  
ANISOU 2184  O   GLY A 264     2643   4121   3362    954   -264    266       O  
ATOM   2185  N   GLN A 265      72.947  21.313   8.280  1.00 27.95           N  
ANISOU 2185  N   GLN A 265     2823   4332   3464    863   -396    616       N  
ATOM   2186  CA  GLN A 265      72.723  20.479   9.460  1.00 29.39           C  
ANISOU 2186  CA  GLN A 265     3135   4372   3660    719   -232    405       C  
ATOM   2187  C   GLN A 265      72.476  21.356  10.682  1.00 28.82           C  
ANISOU 2187  C   GLN A 265     3116   4272   3564    646   -210    551       C  
ATOM   2188  O   GLN A 265      71.414  21.962  10.810  1.00 28.62           O  
ANISOU 2188  O   GLN A 265     3373   4014   3486    951   -289    719       O  
ATOM   2189  CB  GLN A 265      73.913  19.551   9.701  1.00 32.15           C  
ANISOU 2189  CB  GLN A 265     3594   4574   4047    606   -293     95       C  
ATOM   2190  CG  GLN A 265      74.002  18.397   8.715  1.00 34.88           C  
ANISOU 2190  CG  GLN A 265     4102   4704   4447    361   -234   -213       C  
ATOM   2191  CD  GLN A 265      72.858  17.415   8.868  1.00 37.08           C  
ANISOU 2191  CD  GLN A 265     4534   4768   4787    250   -243   -471       C  
ATOM   2192  OE1 GLN A 265      72.736  16.744   9.890  1.00 37.86           O  
ANISOU 2192  OE1 GLN A 265     4694   4707   4985    115   -171   -434       O  
ATOM   2193  NE2 GLN A 265      72.008  17.333   7.853  1.00 38.24           N  
ANISOU 2193  NE2 GLN A 265     4703   4883   4941    263   -278   -674       N  
ATOM   2194  N   ASP A 266      73.454  21.420  11.582  1.00 28.26           N  
ANISOU 2194  N   ASP A 266     2885   4361   3490    476   -198    471       N  
ATOM   2195  CA  ASP A 266      73.372  22.315  12.731  1.00 28.93           C  
ANISOU 2195  CA  ASP A 266     2826   4521   3645    383    -99    384       C  
ATOM   2196  C   ASP A 266      73.538  23.768  12.299  1.00 26.39           C  
ANISOU 2196  C   ASP A 266     2306   4172   3551    135    176    407       C  
ATOM   2197  O   ASP A 266      74.318  24.064  11.389  1.00 27.50           O  
ANISOU 2197  O   ASP A 266     2514   4314   3622     67    390    333       O  
ATOM   2198  CB  ASP A 266      74.440  21.958  13.770  1.00 32.09           C  
ANISOU 2198  CB  ASP A 266     3389   4932   3873    372   -110     63       C  
ATOM   2199  CG  ASP A 266      74.232  20.587  14.370  1.00 35.87           C  
ANISOU 2199  CG  ASP A 266     4101   5412   4117    485    -48   -315       C  
ATOM   2200  OD1 ASP A 266      73.898  20.509  15.570  1.00 37.45           O  
ANISOU 2200  OD1 ASP A 266     4370   5659   4201    500    123   -358       O  
ATOM   2201  OD2 ASP A 266      74.393  19.585  13.641  1.00 37.55           O  
ANISOU 2201  OD2 ASP A 266     4403   5607   4256    356   -166   -597       O  
ATOM   2202  N   ASP A 267      72.800  24.673  12.939  1.00 24.15           N  
ANISOU 2202  N   ASP A 267     1831   3970   3373      5    127    558       N  
ATOM   2203  CA  ASP A 267      72.983  26.102  12.703  1.00 22.70           C  
ANISOU 2203  CA  ASP A 267     1553   3752   3319   -120    213    454       C  
ATOM   2204  C   ASP A 267      72.704  26.897  13.976  1.00 22.30           C  
ANISOU 2204  C   ASP A 267     1613   3577   3281   -422    282    362       C  
ATOM   2205  O   ASP A 267      72.570  26.318  15.054  1.00 22.60           O  
ANISOU 2205  O   ASP A 267     1872   3553   3163   -513    429    586       O  
ATOM   2206  CB  ASP A 267      72.098  26.592  11.543  1.00 22.00           C  
ANISOU 2206  CB  ASP A 267     1517   3630   3212   -181    239    687       C  
ATOM   2207  CG  ASP A 267      70.607  26.386  11.789  1.00 22.01           C  
ANISOU 2207  CG  ASP A 267     1721   3407   3234   -415    -48    915       C  
ATOM   2208  OD1 ASP A 267      70.205  25.990  12.899  1.00 21.59           O  
ANISOU 2208  OD1 ASP A 267     1569   3489   3144   -243    125    999       O  
ATOM   2209  OD2 ASP A 267      69.818  26.639  10.855  1.00 22.69           O  
ANISOU 2209  OD2 ASP A 267     2031   3376   3213   -427   -230    988       O  
ATOM   2210  N   GLU A 268      72.633  28.218  13.859  1.00 23.35           N  
ANISOU 2210  N   GLU A 268     1895   3651   3326   -716    207    186       N  
ATOM   2211  CA  GLU A 268      72.398  29.054  15.031  1.00 24.71           C  
ANISOU 2211  CA  GLU A 268     2404   3560   3426   -519     -8    119       C  
ATOM   2212  C   GLU A 268      71.077  28.722  15.721  1.00 22.44           C  
ANISOU 2212  C   GLU A 268     2215   3169   3143   -371     75    204       C  
ATOM   2213  O   GLU A 268      70.981  28.804  16.945  1.00 22.98           O  
ANISOU 2213  O   GLU A 268     2306   3254   3171   -278    -48    329       O  
ATOM   2214  CB  GLU A 268      72.438  30.531  14.653  1.00 28.07           C  
ANISOU 2214  CB  GLU A 268     3015   3848   3800   -760   -140     -2       C  
ATOM   2215  CG  GLU A 268      73.839  31.036  14.366  1.00 31.00           C  
ANISOU 2215  CG  GLU A 268     3487   4166   4127   -771   -337   -112       C  
ATOM   2216  CD  GLU A 268      73.923  32.544  14.390  1.00 34.56           C  
ANISOU 2216  CD  GLU A 268     4121   4575   4434   -635   -464   -163       C  
ATOM   2217  OE1 GLU A 268      73.279  33.190  13.538  1.00 35.41           O  
ANISOU 2217  OE1 GLU A 268     4261   4679   4514   -560   -507   -155       O  
ATOM   2218  OE2 GLU A 268      74.625  33.083  15.271  1.00 36.62           O  
ANISOU 2218  OE2 GLU A 268     4534   4804   4575   -641   -518   -238       O  
ATOM   2219  N   PHE A 269      70.068  28.338  14.944  1.00 20.62           N  
ANISOU 2219  N   PHE A 269     1880   2971   2982   -223     54    206       N  
ATOM   2220  CA  PHE A 269      68.768  27.991  15.515  1.00 19.30           C  
ANISOU 2220  CA  PHE A 269     1733   2800   2799   -316     -2    474       C  
ATOM   2221  C   PHE A 269      68.843  26.712  16.350  1.00 18.72           C  
ANISOU 2221  C   PHE A 269     1767   2713   2633    -64     -8    298       C  
ATOM   2222  O   PHE A 269      68.381  26.686  17.496  1.00 18.14           O  
ANISOU 2222  O   PHE A 269     1557   2845   2488    -45     -4    273       O  
ATOM   2223  CB  PHE A 269      67.711  27.848  14.414  1.00 18.52           C  
ANISOU 2223  CB  PHE A 269     1637   2699   2699   -223     15    538       C  
ATOM   2224  CG  PHE A 269      66.370  27.377  14.917  1.00 18.29           C  
ANISOU 2224  CG  PHE A 269     1560   2784   2605    245    135    593       C  
ATOM   2225  CD1 PHE A 269      65.617  28.172  15.766  1.00 19.59           C  
ANISOU 2225  CD1 PHE A 269     1810   2888   2748    451     84    583       C  
ATOM   2226  CD2 PHE A 269      65.867  26.137  14.547  1.00 18.85           C  
ANISOU 2226  CD2 PHE A 269     1617   2976   2568    195    190    390       C  
ATOM   2227  CE1 PHE A 269      64.382  27.744  16.232  1.00 19.72           C  
ANISOU 2227  CE1 PHE A 269     1861   2964   2667    411    114    579       C  
ATOM   2228  CE2 PHE A 269      64.633  25.703  15.015  1.00 19.02           C  
ANISOU 2228  CE2 PHE A 269     1679   2977   2570    185    105    410       C  
ATOM   2229  CZ  PHE A 269      63.888  26.514  15.853  1.00 19.01           C  
ANISOU 2229  CZ  PHE A 269     1743   2965   2514    339    -51    558       C  
ATOM   2230  N   THR A 270      69.436  25.659  15.791  1.00 18.56           N  
ANISOU 2230  N   THR A 270     1670   2662   2719    -62    -75    281       N  
ATOM   2231  CA  THR A 270      69.539  24.398  16.523  1.00 19.45           C  
ANISOU 2231  CA  THR A 270     1940   2673   2777     53   -305    226       C  
ATOM   2232  C   THR A 270      70.477  24.552  17.725  1.00 20.47           C  
ANISOU 2232  C   THR A 270     1920   2957   2901     67   -253    310       C  
ATOM   2233  O   THR A 270      70.184  24.048  18.807  1.00 20.38           O  
ANISOU 2233  O   THR A 270     2041   2828   2874    220     -8    376       O  
ATOM   2234  CB  THR A 270      70.009  23.238  15.623  1.00 20.61           C  
ANISOU 2234  CB  THR A 270     2170   2754   2907    -69   -187    191       C  
ATOM   2235  OG1 THR A 270      71.346  23.474  15.159  1.00 22.27           O  
ANISOU 2235  OG1 THR A 270     2498   2923   3043    -97   -134    367       O  
ATOM   2236  CG2 THR A 270      69.077  23.089  14.435  1.00 20.34           C  
ANISOU 2236  CG2 THR A 270     2222   2646   2859    -97   -118     53       C  
ATOM   2237  N   ASP A 271      71.579  25.276  17.544  1.00 21.91           N  
ANISOU 2237  N   ASP A 271     1901   3333   3090     32   -326    235       N  
ATOM   2238  CA  ASP A 271      72.482  25.562  18.659  1.00 24.48           C  
ANISOU 2238  CA  ASP A 271     2352   3662   3289   -111   -308    211       C  
ATOM   2239  C   ASP A 271      71.733  26.276  19.779  1.00 23.75           C  
ANISOU 2239  C   ASP A 271     2308   3578   3136     58   -480    232       C  
ATOM   2240  O   ASP A 271      71.936  25.992  20.965  1.00 25.02           O  
ANISOU 2240  O   ASP A 271     2468   3881   3157    176   -562    286       O  
ATOM   2241  CB  ASP A 271      73.669  26.412  18.201  1.00 28.15           C  
ANISOU 2241  CB  ASP A 271     2751   4138   3806   -183   -187    168       C  
ATOM   2242  CG  ASP A 271      74.654  25.634  17.351  1.00 32.07           C  
ANISOU 2242  CG  ASP A 271     3312   4526   4347   -122      4    202       C  
ATOM   2243  OD1 ASP A 271      74.606  24.385  17.359  1.00 33.13           O  
ANISOU 2243  OD1 ASP A 271     3465   4615   4507    269    -73    211       O  
ATOM   2244  OD2 ASP A 271      75.486  26.277  16.678  1.00 34.61           O  
ANISOU 2244  OD2 ASP A 271     3573   4908   4668   -169    118    195       O  
ATOM   2245  N   TYR A 272      70.861  27.201  19.392  1.00 22.52           N  
ANISOU 2245  N   TYR A 272     2250   3327   2978    -35   -370    196       N  
ATOM   2246  CA  TYR A 272      70.062  27.964  20.340  1.00 21.61           C  
ANISOU 2246  CA  TYR A 272     2168   3149   2896    -35   -417    181       C  
ATOM   2247  C   TYR A 272      69.114  27.068  21.130  1.00 19.92           C  
ANISOU 2247  C   TYR A 272     1945   2977   2648    -74   -315    182       C  
ATOM   2248  O   TYR A 272      69.074  27.130  22.355  1.00 20.52           O  
ANISOU 2248  O   TYR A 272     1939   3185   2672    119   -349    315       O  
ATOM   2249  CB  TYR A 272      69.274  29.055  19.610  1.00 22.05           C  
ANISOU 2249  CB  TYR A 272     2320   3037   3022      8   -530    307       C  
ATOM   2250  CG  TYR A 272      68.273  29.777  20.475  1.00 23.77           C  
ANISOU 2250  CG  TYR A 272     2498   3209   3326    -22   -638    298       C  
ATOM   2251  CD1 TYR A 272      68.679  30.758  21.374  1.00 23.84           C  
ANISOU 2251  CD1 TYR A 272     2458   3081   3521    -76   -573    254       C  
ATOM   2252  CD2 TYR A 272      66.917  29.486  20.390  1.00 24.60           C  
ANISOU 2252  CD2 TYR A 272     2629   3274   3444    127   -564    479       C  
ATOM   2253  CE1 TYR A 272      67.765  31.419  22.168  1.00 23.95           C  
ANISOU 2253  CE1 TYR A 272     2486   3097   3516    -60   -482    360       C  
ATOM   2254  CE2 TYR A 272      65.997  30.142  21.178  1.00 24.34           C  
ANISOU 2254  CE2 TYR A 272     2622   3115   3513    354   -394    523       C  
ATOM   2255  CZ  TYR A 272      66.424  31.110  22.062  1.00 24.69           C  
ANISOU 2255  CZ  TYR A 272     2652   3110   3618    239   -450    461       C  
ATOM   2256  OH  TYR A 272      65.510  31.766  22.851  1.00 26.82           O  
ANISOU 2256  OH  TYR A 272     3015   3262   3913    367   -271    353       O  
ATOM   2257  N   LEU A 273      68.355  26.233  20.428  1.00 19.70           N  
ANISOU 2257  N   LEU A 273     2028   2858   2602   -150   -312    201       N  
ATOM   2258  CA  LEU A 273      67.442  25.313  21.097  1.00 19.45           C  
ANISOU 2258  CA  LEU A 273     2050   2793   2547   -186   -321    232       C  
ATOM   2259  C   LEU A 273      68.186  24.349  22.016  1.00 20.50           C  
ANISOU 2259  C   LEU A 273     2089   2946   2755    140   -310    163       C  
ATOM   2260  O   LEU A 273      67.751  24.102  23.139  1.00 21.61           O  
ANISOU 2260  O   LEU A 273     2137   3125   2950    165   -100    114       O  
ATOM   2261  CB  LEU A 273      66.623  24.523  20.077  1.00 18.96           C  
ANISOU 2261  CB  LEU A 273     1981   2645   2576    -84   -419    218       C  
ATOM   2262  CG  LEU A 273      65.578  25.334  19.312  1.00 19.26           C  
ANISOU 2262  CG  LEU A 273     2026   2634   2657    218   -595    -44       C  
ATOM   2263  CD1 LEU A 273      64.700  24.400  18.497  1.00 18.06           C  
ANISOU 2263  CD1 LEU A 273     1892   2404   2565    248   -802    -29       C  
ATOM   2264  CD2 LEU A 273      64.737  26.189  20.257  1.00 19.51           C  
ANISOU 2264  CD2 LEU A 273     2248   2493   2672    161   -582   -234       C  
ATOM   2265  N   VAL A 274      69.306  23.812  21.541  1.00 21.17           N  
ANISOU 2265  N   VAL A 274     2071   3165   2810    401   -418    280       N  
ATOM   2266  CA  VAL A 274      70.064  22.844  22.330  1.00 23.27           C  
ANISOU 2266  CA  VAL A 274     2343   3548   2949    573   -546    359       C  
ATOM   2267  C   VAL A 274      70.585  23.486  23.613  1.00 24.62           C  
ANISOU 2267  C   VAL A 274     2467   3898   2990    330   -717    590       C  
ATOM   2268  O   VAL A 274      70.484  22.905  24.694  1.00 25.89           O  
ANISOU 2268  O   VAL A 274     2722   4239   2874    321   -705    833       O  
ATOM   2269  CB  VAL A 274      71.236  22.250  21.520  1.00 23.42           C  
ANISOU 2269  CB  VAL A 274     2350   3526   3021    686   -601    542       C  
ATOM   2270  CG1 VAL A 274      72.179  21.469  22.429  1.00 24.07           C  
ANISOU 2270  CG1 VAL A 274     2395   3641   3109    873   -577    761       C  
ATOM   2271  CG2 VAL A 274      70.707  21.357  20.413  1.00 23.60           C  
ANISOU 2271  CG2 VAL A 274     2376   3393   3198    410   -601    488       C  
ATOM   2272  N   ALA A 275      71.113  24.700  23.491  1.00 24.48           N  
ANISOU 2272  N   ALA A 275     2450   3789   3061     43   -748    370       N  
ATOM   2273  CA  ALA A 275      71.635  25.431  24.641  1.00 25.20           C  
ANISOU 2273  CA  ALA A 275     2565   3895   3113     12   -790    259       C  
ATOM   2274  C   ALA A 275      70.528  25.803  25.625  1.00 26.50           C  
ANISOU 2274  C   ALA A 275     2824   4109   3135    277   -823    221       C  
ATOM   2275  O   ALA A 275      70.691  25.671  26.838  1.00 27.65           O  
ANISOU 2275  O   ALA A 275     3198   4216   3093    632   -859    226       O  
ATOM   2276  CB  ALA A 275      72.371  26.675  24.180  1.00 24.28           C  
ANISOU 2276  CB  ALA A 275     2339   3778   3108   -320   -790    196       C  
ATOM   2277  N   GLN A 276      69.400  26.273  25.101  1.00 26.23           N  
ANISOU 2277  N   GLN A 276     2631   4102   3231    130   -783    280       N  
ATOM   2278  CA  GLN A 276      68.277  26.673  25.945  1.00 27.21           C  
ANISOU 2278  CA  GLN A 276     2788   4184   3366    102   -641    373       C  
ATOM   2279  C   GLN A 276      67.622  25.503  26.675  1.00 27.87           C  
ANISOU 2279  C   GLN A 276     2926   4254   3408    154   -359    622       C  
ATOM   2280  O   GLN A 276      67.043  25.686  27.750  1.00 27.79           O  
ANISOU 2280  O   GLN A 276     2909   4290   3359    210   -165    501       O  
ATOM   2281  CB  GLN A 276      67.217  27.395  25.108  1.00 27.02           C  
ANISOU 2281  CB  GLN A 276     2794   4089   3383     57   -622    476       C  
ATOM   2282  CG  GLN A 276      67.646  28.753  24.598  1.00 28.67           C  
ANISOU 2282  CG  GLN A 276     3110   4207   3577   -122   -490    287       C  
ATOM   2283  CD  GLN A 276      67.863  29.744  25.715  1.00 31.19           C  
ANISOU 2283  CD  GLN A 276     3613   4475   3762   -250   -195     66       C  
ATOM   2284  OE1 GLN A 276      67.089  29.798  26.672  1.00 33.10           O  
ANISOU 2284  OE1 GLN A 276     3937   4688   3951    -51     57   -149       O  
ATOM   2285  NE2 GLN A 276      68.924  30.533  25.607  1.00 30.96           N  
ANISOU 2285  NE2 GLN A 276     3708   4309   3748   -582   -351     47       N  
ATOM   2286  N   LEU A 277      67.711  24.308  26.097  1.00 29.17           N  
ANISOU 2286  N   LEU A 277     3123   4293   3666    244   -159    933       N  
ATOM   2287  CA  LEU A 277      66.940  23.168  26.595  1.00 31.78           C  
ANISOU 2287  CA  LEU A 277     3502   4511   4062    260    -24   1071       C  
ATOM   2288  C   LEU A 277      67.783  22.088  27.254  1.00 36.21           C  
ANISOU 2288  C   LEU A 277     4118   4965   4675    531    -80   1462       C  
ATOM   2289  O   LEU A 277      67.270  21.044  27.635  1.00 37.20           O  
ANISOU 2289  O   LEU A 277     4234   5089   4811    627    -33   1459       O  
ATOM   2290  CB  LEU A 277      66.132  22.550  25.455  1.00 30.38           C  
ANISOU 2290  CB  LEU A 277     3293   4340   3911    -15    225    659       C  
ATOM   2291  CG  LEU A 277      65.089  23.466  24.812  1.00 28.33           C  
ANISOU 2291  CG  LEU A 277     2962   4131   3673   -147    328    298       C  
ATOM   2292  CD1 LEU A 277      64.397  22.779  23.638  1.00 27.55           C  
ANISOU 2292  CD1 LEU A 277     2976   3934   3559   -145    144    252       C  
ATOM   2293  CD2 LEU A 277      64.078  23.923  25.855  1.00 27.54           C  
ANISOU 2293  CD2 LEU A 277     2766   4088   3609   -179    511    148       C  
ATOM   2294  N   ALA A 278      69.075  22.339  27.398  1.00 39.60           N  
ANISOU 2294  N   ALA A 278     4566   5385   5095    702   -288   1645       N  
ATOM   2295  CA  ALA A 278      69.974  21.344  27.979  1.00 43.33           C  
ANISOU 2295  CA  ALA A 278     5127   5818   5517    660   -232   1631       C  
ATOM   2296  C   ALA A 278      69.893  21.347  29.509  1.00 46.23           C  
ANISOU 2296  C   ALA A 278     5560   6186   5818    563   -236   1532       C  
ATOM   2297  O   ALA A 278      69.249  22.225  30.096  1.00 46.69           O  
ANISOU 2297  O   ALA A 278     5594   6282   5866    502   -216   1444       O  
ATOM   2298  CB  ALA A 278      71.400  21.593  27.529  1.00 43.85           C  
ANISOU 2298  CB  ALA A 278     5135   5909   5616    655   -207   1602       C  
ATOM   2299  OXT ALA A 278      70.463  20.466  30.157  1.00 47.89           O  
ANISOU 2299  OXT ALA A 278     5829   6324   6042    481   -213   1595       O  
TER    2300      ALA A 278                                                      
ATOM   2301  N   MET B   1      17.153  43.921  -6.858  1.00 39.86           N  
ANISOU 2301  N   MET B   1     4158   5790   5196   -229   -801    -97       N  
ATOM   2302  CA  MET B   1      17.497  43.434  -8.190  1.00 40.01           C  
ANISOU 2302  CA  MET B   1     4203   5768   5233    -62   -894    -54       C  
ATOM   2303  C   MET B   1      18.313  42.155  -8.129  1.00 40.85           C  
ANISOU 2303  C   MET B   1     4409   5881   5230    -71   -877   -129       C  
ATOM   2304  O   MET B   1      18.940  41.846  -7.113  1.00 41.27           O  
ANISOU 2304  O   MET B   1     4403   6014   5265    159   -888     38       O  
ATOM   2305  CB  MET B   1      18.284  44.491  -8.965  1.00 39.68           C  
ANISOU 2305  CB  MET B   1     4104   5690   5283      3   -897    -27       C  
ATOM   2306  CG  MET B   1      19.645  44.790  -8.352  1.00 39.91           C  
ANISOU 2306  CG  MET B   1     4148   5691   5327     13   -918      8       C  
ATOM   2307  SD  MET B   1      20.550  46.092  -9.200  1.00 40.89           S  
ANISOU 2307  SD  MET B   1     4365   5777   5396    137   -887     86       S  
ATOM   2308  CE  MET B   1      21.103  45.222 -10.662  1.00 40.94           C  
ANISOU 2308  CE  MET B   1     4441   5718   5397     62   -815      0       C  
ATOM   2309  N   ARG B   2      18.304  41.415  -9.230  1.00 40.98           N  
ANISOU 2309  N   ARG B   2     4528   5823   5220   -230   -836   -248       N  
ATOM   2310  CA  ARG B   2      19.197  40.282  -9.388  1.00 40.85           C  
ANISOU 2310  CA  ARG B   2     4612   5771   5139   -290   -857   -315       C  
ATOM   2311  C   ARG B   2      20.513  40.765  -9.980  1.00 38.81           C  
ANISOU 2311  C   ARG B   2     4447   5525   4773   -536   -916   -348       C  
ATOM   2312  O   ARG B   2      20.548  41.304 -11.086  1.00 38.34           O  
ANISOU 2312  O   ARG B   2     4383   5442   4742   -619   -864   -378       O  
ATOM   2313  CB  ARG B   2      18.570  39.209 -10.277  1.00 42.97           C  
ANISOU 2313  CB  ARG B   2     4933   5955   5439   -165   -817   -381       C  
ATOM   2314  CG  ARG B   2      19.523  38.089 -10.650  1.00 45.40           C  
ANISOU 2314  CG  ARG B   2     5323   6214   5713    -45   -744   -388       C  
ATOM   2315  CD  ARG B   2      18.873  37.107 -11.608  1.00 47.59           C  
ANISOU 2315  CD  ARG B   2     5682   6426   5973    114   -632   -333       C  
ATOM   2316  NE  ARG B   2      19.866  36.298 -12.309  1.00 49.54           N  
ANISOU 2316  NE  ARG B   2     6056   6588   6179    240   -590   -238       N  
ATOM   2317  CZ  ARG B   2      19.776  34.983 -12.480  1.00 51.13           C  
ANISOU 2317  CZ  ARG B   2     6347   6767   6311    353   -480   -177       C  
ATOM   2318  NH1 ARG B   2      18.736  34.317 -11.997  1.00 51.60           N  
ANISOU 2318  NH1 ARG B   2     6432   6825   6347    311   -482   -138       N  
ATOM   2319  NH2 ARG B   2      20.730  34.333 -13.133  1.00 51.47           N  
ANISOU 2319  NH2 ARG B   2     6410   6808   6337    505   -381   -156       N  
ATOM   2320  N   LEU B   3      21.593  40.584  -9.232  1.00 37.51           N  
ANISOU 2320  N   LEU B   3     4325   5455   4470   -655   -982   -302       N  
ATOM   2321  CA  LEU B   3      22.915  40.968  -9.705  1.00 36.31           C  
ANISOU 2321  CA  LEU B   3     4301   5332   4162   -562   -947   -257       C  
ATOM   2322  C   LEU B   3      23.602  39.753 -10.312  1.00 37.42           C  
ANISOU 2322  C   LEU B   3     4631   5437   4149   -382   -686     -3       C  
ATOM   2323  O   LEU B   3      23.781  38.738  -9.644  1.00 37.24           O  
ANISOU 2323  O   LEU B   3     4612   5456   4082   -270   -358    144       O  
ATOM   2324  CB  LEU B   3      23.751  41.555  -8.561  1.00 34.91           C  
ANISOU 2324  CB  LEU B   3     4114   5118   4032   -572  -1216   -365       C  
ATOM   2325  CG  LEU B   3      25.107  42.168  -8.914  1.00 34.49           C  
ANISOU 2325  CG  LEU B   3     4208   4903   3993   -413  -1304   -281       C  
ATOM   2326  CD1 LEU B   3      24.933  43.334  -9.867  1.00 34.51           C  
ANISOU 2326  CD1 LEU B   3     4238   4891   3984   -358  -1220   -237       C  
ATOM   2327  CD2 LEU B   3      25.843  42.607  -7.649  1.00 34.05           C  
ANISOU 2327  CD2 LEU B   3     4158   4783   3996   -368  -1411   -317       C  
ATOM   2328  N   ASP B   4      23.972  39.855 -11.585  1.00 38.37           N  
ANISOU 2328  N   ASP B   4     4907   5499   4173   -375   -794     13       N  
ATOM   2329  CA  ASP B   4      24.643  38.758 -12.270  1.00 38.83           C  
ANISOU 2329  CA  ASP B   4     4965   5574   4215   -367   -947    100       C  
ATOM   2330  C   ASP B   4      26.146  38.990 -12.284  1.00 38.01           C  
ANISOU 2330  C   ASP B   4     4898   5418   4126   -397   -958    136       C  
ATOM   2331  O   ASP B   4      26.609  40.079 -12.613  1.00 38.95           O  
ANISOU 2331  O   ASP B   4     5132   5556   4113   -405  -1046    170       O  
ATOM   2332  CB  ASP B   4      24.105  38.604 -13.695  1.00 40.24           C  
ANISOU 2332  CB  ASP B   4     5127   5789   4375   -468  -1021    186       C  
ATOM   2333  CG  ASP B   4      22.626  38.260 -13.724  1.00 42.01           C  
ANISOU 2333  CG  ASP B   4     5294   6057   4611   -515   -982    338       C  
ATOM   2334  OD1 ASP B   4      22.190  37.423 -12.907  1.00 42.12           O  
ANISOU 2334  OD1 ASP B   4     5294   6088   4621   -662   -950    380       O  
ATOM   2335  OD2 ASP B   4      21.896  38.829 -14.563  1.00 43.44           O  
ANISOU 2335  OD2 ASP B   4     5390   6219   4898   -486   -992    375       O  
ATOM   2336  N   LEU B   5      26.905  37.963 -11.918  1.00 37.09           N  
ANISOU 2336  N   LEU B   5     4671   5278   4143   -338   -875    164       N  
ATOM   2337  CA  LEU B   5      28.347  38.107 -11.768  1.00 36.65           C  
ANISOU 2337  CA  LEU B   5     4601   5119   4205   -103   -757    186       C  
ATOM   2338  C   LEU B   5      29.123  37.060 -12.562  1.00 37.66           C  
ANISOU 2338  C   LEU B   5     4784   5248   4278   -265   -451     24       C  
ATOM   2339  O   LEU B   5      28.735  35.894 -12.618  1.00 37.34           O  
ANISOU 2339  O   LEU B   5     4775   5164   4250   -385   -283     52       O  
ATOM   2340  CB  LEU B   5      28.729  38.026 -10.286  1.00 35.20           C  
ANISOU 2340  CB  LEU B   5     4366   4899   4111     84   -975    321       C  
ATOM   2341  CG  LEU B   5      28.023  38.996  -9.333  1.00 34.26           C  
ANISOU 2341  CG  LEU B   5     4320   4654   4044    372  -1024    447       C  
ATOM   2342  CD1 LEU B   5      28.451  38.746  -7.892  1.00 33.64           C  
ANISOU 2342  CD1 LEU B   5     4280   4437   4064    597  -1002    567       C  
ATOM   2343  CD2 LEU B   5      28.292  40.441  -9.728  1.00 34.55           C  
ANISOU 2343  CD2 LEU B   5     4377   4730   4021    252   -998    373       C  
ATOM   2344  N   ASP B   6      30.224  37.487 -13.172  1.00 38.92           N  
ANISOU 2344  N   ASP B   6     5002   5443   4343   -288   -279    -80       N  
ATOM   2345  CA  ASP B   6      31.120  36.577 -13.876  1.00 40.08           C  
ANISOU 2345  CA  ASP B   6     5130   5597   4500   -347   -161   -197       C  
ATOM   2346  C   ASP B   6      32.469  36.553 -13.167  1.00 37.98           C  
ANISOU 2346  C   ASP B   6     4806   5172   4455   -335    -60   -312       C  
ATOM   2347  O   ASP B   6      33.070  37.598 -12.929  1.00 37.86           O  
ANISOU 2347  O   ASP B   6     4797   5034   4554   -256    120   -285       O  
ATOM   2348  CB  ASP B   6      31.279  36.996 -15.339  1.00 42.91           C  
ANISOU 2348  CB  ASP B   6     5502   6097   4706   -356   -179   -378       C  
ATOM   2349  CG  ASP B   6      31.936  35.922 -16.188  1.00 45.54           C  
ANISOU 2349  CG  ASP B   6     5789   6505   5009   -388   -106   -488       C  
ATOM   2350  OD1 ASP B   6      33.056  35.483 -15.850  1.00 45.62           O  
ANISOU 2350  OD1 ASP B   6     5826   6565   4941   -521    -36   -537       O  
ATOM   2351  OD2 ASP B   6      31.324  35.507 -17.196  1.00 47.71           O  
ANISOU 2351  OD2 ASP B   6     5976   6717   5434   -296   -110   -484       O  
ATOM   2352  N   PHE B   7      32.946  35.359 -12.835  1.00 36.36           N  
ANISOU 2352  N   PHE B   7     4632   4859   4325   -408    -79   -426       N  
ATOM   2353  CA  PHE B   7      34.138  35.212 -12.000  1.00 35.97           C  
ANISOU 2353  CA  PHE B   7     4631   4685   4353   -270     85   -369       C  
ATOM   2354  C   PHE B   7      35.378  34.750 -12.751  1.00 38.91           C  
ANISOU 2354  C   PHE B   7     5105   5011   4668   -331    103   -519       C  
ATOM   2355  O   PHE B   7      36.365  34.352 -12.133  1.00 39.28           O  
ANISOU 2355  O   PHE B   7     5067   5142   4714   -311    108   -563       O  
ATOM   2356  CB  PHE B   7      33.852  34.224 -10.868  1.00 32.88           C  
ANISOU 2356  CB  PHE B   7     4146   4302   4045   -212     78   -262       C  
ATOM   2357  CG  PHE B   7      32.936  34.767  -9.815  1.00 30.05           C  
ANISOU 2357  CG  PHE B   7     3615   4022   3780   -139     73   -351       C  
ATOM   2358  CD1 PHE B   7      33.453  35.411  -8.704  1.00 29.26           C  
ANISOU 2358  CD1 PHE B   7     3386   4016   3715   -155    -47   -291       C  
ATOM   2359  CD2 PHE B   7      31.560  34.653  -9.941  1.00 29.18           C  
ANISOU 2359  CD2 PHE B   7     3449   3958   3681   -147      9   -255       C  
ATOM   2360  CE1 PHE B   7      32.621  35.919  -7.738  1.00 28.55           C  
ANISOU 2360  CE1 PHE B   7     3296   3981   3572   -138    125   -309       C  
ATOM   2361  CE2 PHE B   7      30.721  35.162  -8.974  1.00 28.78           C  
ANISOU 2361  CE2 PHE B   7     3344   3912   3679    -40      9   -182       C  
ATOM   2362  CZ  PHE B   7      31.251  35.798  -7.874  1.00 28.79           C  
ANISOU 2362  CZ  PHE B   7     3390   3967   3581      9    164   -227       C  
ATOM   2363  N   GLY B   8      35.332  34.810 -14.076  1.00 41.40           N  
ANISOU 2363  N   GLY B   8     5536   5229   4965   -403    159   -679       N  
ATOM   2364  CA  GLY B   8      36.351  34.174 -14.888  1.00 43.95           C  
ANISOU 2364  CA  GLY B   8     5924   5510   5266   -525    114   -748       C  
ATOM   2365  C   GLY B   8      35.728  32.916 -15.455  1.00 46.31           C  
ANISOU 2365  C   GLY B   8     6274   5798   5524   -631    132   -790       C  
ATOM   2366  O   GLY B   8      35.675  31.875 -14.781  1.00 45.70           O  
ANISOU 2366  O   GLY B   8     6173   5715   5477   -616    101   -763       O  
ATOM   2367  N   ARG B   9      35.260  33.036 -16.697  1.00 48.71           N  
ANISOU 2367  N   ARG B   9     6609   6102   5795   -685    276   -838       N  
ATOM   2368  CA  ARG B   9      34.431  32.037 -17.377  1.00 50.16           C  
ANISOU 2368  CA  ARG B   9     6758   6388   5912   -577    418   -957       C  
ATOM   2369  C   ARG B   9      34.948  30.604 -17.241  1.00 50.18           C  
ANISOU 2369  C   ARG B   9     6750   6404   5914   -569    567  -1071       C  
ATOM   2370  O   ARG B   9      36.149  30.376 -17.106  1.00 51.20           O  
ANISOU 2370  O   ARG B   9     6884   6568   6000   -521    455  -1198       O  
ATOM   2371  CB  ARG B   9      34.303  32.412 -18.854  1.00 51.04           C  
ANISOU 2371  CB  ARG B   9     6858   6511   6024   -482    364   -867       C  
ATOM   2372  N   GLY B  10      34.038  29.634 -17.259  1.00 49.17           N  
ANISOU 2372  N   GLY B  10     6595   6247   5841   -660    804   -922       N  
ATOM   2373  CA  GLY B  10      32.616  29.892 -17.399  1.00 48.11           C  
ANISOU 2373  CA  GLY B  10     6462   6047   5770   -468    839   -858       C  
ATOM   2374  C   GLY B  10      31.911  29.932 -16.063  1.00 46.83           C  
ANISOU 2374  C   GLY B  10     6238   5876   5678   -339    914   -758       C  
ATOM   2375  O   GLY B  10      30.698  29.750 -15.987  1.00 46.97           O  
ANISOU 2375  O   GLY B  10     6338   5763   5744   -366    765   -733       O  
ATOM   2376  N   LEU B  11      32.685  30.174 -15.010  1.00 46.10           N  
ANISOU 2376  N   LEU B  11     6019   5935   5561   -304   1014   -651       N  
ATOM   2377  CA  LEU B  11      32.154  30.280 -13.654  1.00 45.58           C  
ANISOU 2377  CA  LEU B  11     5798   6047   5474   -360    923   -522       C  
ATOM   2378  C   LEU B  11      31.272  31.520 -13.484  1.00 44.07           C  
ANISOU 2378  C   LEU B  11     5547   5959   5237   -288    927   -499       C  
ATOM   2379  O   LEU B  11      31.774  32.624 -13.258  1.00 43.21           O  
ANISOU 2379  O   LEU B  11     5412   5895   5110   -327   1134   -404       O  
ATOM   2380  CB  LEU B  11      33.303  30.309 -12.643  1.00 46.42           C  
ANISOU 2380  CB  LEU B  11     5823   6210   5604   -498    764   -523       C  
ATOM   2381  CG  LEU B  11      32.937  30.301 -11.157  1.00 47.28           C  
ANISOU 2381  CG  LEU B  11     5889   6332   5743   -548    596   -546       C  
ATOM   2382  CD1 LEU B  11      32.358  28.952 -10.756  1.00 47.68           C  
ANISOU 2382  CD1 LEU B  11     5889   6420   5807   -628    533   -524       C  
ATOM   2383  CD2 LEU B  11      34.147  30.651 -10.303  1.00 47.50           C  
ANISOU 2383  CD2 LEU B  11     5886   6373   5788   -498    558   -591       C  
ATOM   2384  N   VAL B  12      29.960  31.330 -13.594  1.00 43.21           N  
ANISOU 2384  N   VAL B  12     5369   5916   5133   -259    581   -577       N  
ATOM   2385  CA  VAL B  12      29.002  32.424 -13.466  1.00 42.92           C  
ANISOU 2385  CA  VAL B  12     5307   5941   5059   -294    284   -575       C  
ATOM   2386  C   VAL B  12      28.025  32.154 -12.317  1.00 41.20           C  
ANISOU 2386  C   VAL B  12     5053   5781   4820   -484     35   -664       C  
ATOM   2387  O   VAL B  12      27.659  31.004 -12.056  1.00 40.15           O  
ANISOU 2387  O   VAL B  12     4916   5624   4715   -625    -84   -675       O  
ATOM   2388  CB  VAL B  12      28.226  32.639 -14.787  1.00 44.29           C  
ANISOU 2388  CB  VAL B  12     5515   6116   5199    -76    199   -489       C  
ATOM   2389  CG1 VAL B  12      27.205  33.765 -14.656  1.00 44.79           C  
ANISOU 2389  CG1 VAL B  12     5594   6173   5252    -64    176   -557       C  
ATOM   2390  CG2 VAL B  12      29.194  32.931 -15.924  1.00 44.55           C  
ANISOU 2390  CG2 VAL B  12     5564   6163   5198    -53    209   -414       C  
ATOM   2391  N   ALA B  13      27.625  33.217 -11.625  1.00 39.98           N  
ANISOU 2391  N   ALA B  13     4815   5603   4774   -527    -29   -730       N  
ATOM   2392  CA  ALA B  13      26.687  33.119 -10.511  1.00 39.13           C  
ANISOU 2392  CA  ALA B  13     4572   5562   4732   -563   -273   -683       C  
ATOM   2393  C   ALA B  13      25.863  34.396 -10.407  1.00 38.45           C  
ANISOU 2393  C   ALA B  13     4409   5507   4693   -745   -499   -614       C  
ATOM   2394  O   ALA B  13      26.111  35.362 -11.126  1.00 37.60           O  
ANISOU 2394  O   ALA B  13     4264   5479   4545   -874   -683   -831       O  
ATOM   2395  CB  ALA B  13      27.427  32.857  -9.208  1.00 38.61           C  
ANISOU 2395  CB  ALA B  13     4441   5539   4690   -461   -407   -727       C  
ATOM   2396  N   HIS B  14      24.876  34.395  -9.520  1.00 39.32           N  
ANISOU 2396  N   HIS B  14     4506   5581   4853   -812   -424   -251       N  
ATOM   2397  CA  HIS B  14      24.073  35.585  -9.281  1.00 41.20           C  
ANISOU 2397  CA  HIS B  14     4831   5671   5150   -825   -306     49       C  
ATOM   2398  C   HIS B  14      23.710  35.690  -7.807  1.00 40.36           C  
ANISOU 2398  C   HIS B  14     4625   5613   5099   -753   -347    184       C  
ATOM   2399  O   HIS B  14      23.732  34.694  -7.082  1.00 39.59           O  
ANISOU 2399  O   HIS B  14     4479   5571   4991   -698   -299    296       O  
ATOM   2400  CB  HIS B  14      22.807  35.577 -10.142  1.00 44.54           C  
ANISOU 2400  CB  HIS B  14     5414   5940   5569   -747    -93    195       C  
ATOM   2401  CG  HIS B  14      21.809  34.533  -9.744  1.00 47.52           C  
ANISOU 2401  CG  HIS B  14     5931   6190   5933   -665     68    290       C  
ATOM   2402  ND1 HIS B  14      21.842  33.246 -10.235  1.00 48.64           N  
ANISOU 2402  ND1 HIS B  14     6146   6246   6088   -657    134    368       N  
ATOM   2403  CD2 HIS B  14      20.744  34.592  -8.910  1.00 48.76           C  
ANISOU 2403  CD2 HIS B  14     6145   6292   6088   -625    169    304       C  
ATOM   2404  CE1 HIS B  14      20.843  32.554  -9.716  1.00 49.22           C  
ANISOU 2404  CE1 HIS B  14     6220   6299   6182   -690    227    376       C  
ATOM   2405  NE2 HIS B  14      20.161  33.348  -8.909  1.00 49.10           N  
ANISOU 2405  NE2 HIS B  14     6197   6278   6180   -688    241    370       N  
ATOM   2406  N   VAL B  15      23.389  36.901  -7.364  1.00 39.83           N  
ANISOU 2406  N   VAL B  15     4532   5513   5088   -596   -459    253       N  
ATOM   2407  CA  VAL B  15      23.033  37.132  -5.970  1.00 40.20           C  
ANISOU 2407  CA  VAL B  15     4583   5554   5135   -527   -511    218       C  
ATOM   2408  C   VAL B  15      21.998  38.253  -5.884  1.00 40.92           C  
ANISOU 2408  C   VAL B  15     4598   5667   5283   -640   -588    272       C  
ATOM   2409  O   VAL B  15      22.022  39.199  -6.676  1.00 40.17           O  
ANISOU 2409  O   VAL B  15     4339   5688   5236   -841   -678    293       O  
ATOM   2410  CB  VAL B  15      24.287  37.469  -5.115  1.00 39.22           C  
ANISOU 2410  CB  VAL B  15     4576   5355   4969   -361   -599    140       C  
ATOM   2411  CG1 VAL B  15      24.875  38.819  -5.507  1.00 38.75           C  
ANISOU 2411  CG1 VAL B  15     4503   5316   4904   -441   -689    107       C  
ATOM   2412  CG2 VAL B  15      23.967  37.429  -3.625  1.00 38.71           C  
ANISOU 2412  CG2 VAL B  15     4588   5203   4918   -128   -573    101       C  
ATOM   2413  N  AMET B  16      21.067  38.120  -4.941  0.47 41.62           N  
ANISOU 2413  N  AMET B  16     4741   5726   5347   -615   -564    240       N  
ATOM   2414  N  BMET B  16      21.085  38.144  -4.927  0.53 41.39           N  
ANISOU 2414  N  BMET B  16     4704   5674   5347   -646   -579    308       N  
ATOM   2415  CA AMET B  16      20.024  39.120  -4.744  0.47 42.38           C  
ANISOU 2415  CA AMET B  16     4887   5792   5421   -565   -605    224       C  
ATOM   2416  CA BMET B  16      20.036  39.142  -4.786  0.53 41.92           C  
ANISOU 2416  CA BMET B  16     4811   5688   5430   -625   -638    361       C  
ATOM   2417  C  AMET B  16      20.567  40.350  -4.027  0.47 41.60           C  
ANISOU 2417  C  AMET B  16     4784   5640   5384   -567   -557    310       C  
ATOM   2418  C  BMET B  16      20.528  40.391  -4.052  0.53 41.20           C  
ANISOU 2418  C  BMET B  16     4711   5548   5393   -637   -561    427       C  
ATOM   2419  O  AMET B  16      21.298  40.241  -3.040  0.47 41.42           O  
ANISOU 2419  O  AMET B  16     4720   5630   5386   -588   -563    259       O  
ATOM   2420  O  BMET B  16      21.171  40.302  -3.004  0.53 40.99           O  
ANISOU 2420  O  BMET B  16     4636   5541   5395   -677   -554    355       O  
ATOM   2421  CB AMET B  16      18.847  38.535  -3.953  0.47 43.86           C  
ANISOU 2421  CB AMET B  16     5129   6012   5526   -527   -701    160       C  
ATOM   2422  CB BMET B  16      18.823  38.543  -4.069  0.53 43.17           C  
ANISOU 2422  CB BMET B  16     5013   5839   5550   -599   -777    381       C  
ATOM   2423  CG AMET B  16      18.025  37.502  -4.707  0.47 45.33           C  
ANISOU 2423  CG AMET B  16     5353   6236   5637   -480   -812     77       C  
ATOM   2424  CG BMET B  16      18.097  37.477  -4.877  0.53 44.44           C  
ANISOU 2424  CG BMET B  16     5199   6004   5681   -568   -926    359       C  
ATOM   2425  SD AMET B  16      17.544  38.043  -6.358  0.47 46.76           S  
ANISOU 2425  SD AMET B  16     5546   6453   5768   -430   -915      7       S  
ATOM   2426  SD BMET B  16      17.833  37.931  -6.604  0.53 45.69           S  
ANISOU 2426  SD BMET B  16     5359   6164   5836   -518  -1070    332       S  
ATOM   2427  CE AMET B  16      18.552  36.955  -7.363  0.47 46.83           C  
ANISOU 2427  CE AMET B  16     5600   6462   5732   -424   -928    -39       C  
ATOM   2428  CE BMET B  16      16.804  39.388  -6.432  0.53 45.50           C  
ANISOU 2428  CE BMET B  16     5371   6100   5817   -507  -1122    325       C  
ATOM   2429  N  ALEU B  17      20.201  41.519  -4.539  0.47 41.27           N  
ANISOU 2429  N  ALEU B  17     4798   5537   5345   -496   -523    439       N  
ATOM   2430  N  BLEU B  17      20.240  41.552  -4.634  0.53 40.97           N  
ANISOU 2430  N  BLEU B  17     4748   5460   5361   -546   -507    547       N  
ATOM   2431  CA ALEU B  17      20.583  42.790  -3.939  0.47 41.00           C  
ANISOU 2431  CA ALEU B  17     4819   5461   5298   -452   -505    555       C  
ATOM   2432  CA BLEU B  17      20.532  42.845  -4.017  0.53 40.77           C  
ANISOU 2432  CA BLEU B  17     4786   5385   5319   -501   -481    654       C  
ATOM   2433  C  ALEU B  17      19.316  43.530  -3.514  0.47 41.26           C  
ANISOU 2433  C  ALEU B  17     4914   5450   5314   -383   -481    637       C  
ATOM   2434  C  BLEU B  17      19.234  43.486  -3.547  0.53 41.07           C  
ANISOU 2434  C  BLEU B  17     4886   5398   5319   -420   -467    686       C  
ATOM   2435  O  ALEU B  17      18.737  44.294  -4.288  0.47 41.46           O  
ANISOU 2435  O  ALEU B  17     4940   5459   5353   -343   -465    628       O  
ATOM   2436  O  BLEU B  17      18.557  44.161  -4.325  0.53 41.08           O  
ANISOU 2436  O  BLEU B  17     4884   5375   5348   -403   -458    677       O  
ATOM   2437  CB ALEU B  17      21.409  43.618  -4.928  0.47 40.91           C  
ANISOU 2437  CB ALEU B  17     4826   5448   5270   -482   -476    553       C  
ATOM   2438  CB BLEU B  17      21.243  43.778  -5.002  0.53 40.70           C  
ANISOU 2438  CB BLEU B  17     4802   5348   5314   -531   -437    687       C  
ATOM   2439  CG ALEU B  17      22.150  44.870  -4.455  0.47 40.74           C  
ANISOU 2439  CG ALEU B  17     4814   5445   5218   -525   -441    544       C  
ATOM   2440  CG BLEU B  17      22.736  44.073  -4.855  0.53 40.31           C  
ANISOU 2440  CG BLEU B  17     4752   5302   5262   -547   -449    725       C  
ATOM   2441  CD1ALEU B  17      23.138  44.537  -3.350  0.47 40.57           C  
ANISOU 2441  CD1ALEU B  17     4801   5453   5163   -481   -457    548       C  
ATOM   2442  CD1BLEU B  17      23.145  45.236  -5.753  0.53 40.12           C  
ANISOU 2442  CD1BLEU B  17     4739   5265   5241   -605   -401    758       C  
ATOM   2443  CD2ALEU B  17      22.866  45.513  -5.636  0.47 40.64           C  
ANISOU 2443  CD2ALEU B  17     4827   5411   5205   -622   -406    584       C  
ATOM   2444  CD2BLEU B  17      23.098  44.358  -3.407  0.53 40.15           C  
ANISOU 2444  CD2BLEU B  17     4735   5322   5196   -514   -468    721       C  
ATOM   2445  N   ASP B  18      18.885  43.276  -2.282  1.00 41.32           N  
ANISOU 2445  N   ASP B  18     4927   5451   5320   -338   -521    736       N  
ATOM   2446  CA  ASP B  18      17.613  43.775  -1.771  1.00 41.82           C  
ANISOU 2446  CA  ASP B  18     4999   5516   5374   -296   -611    815       C  
ATOM   2447  C   ASP B  18      17.533  45.295  -1.734  1.00 40.24           C  
ANISOU 2447  C   ASP B  18     4628   5444   5216    -54   -788    871       C  
ATOM   2448  O   ASP B  18      18.487  45.970  -1.348  1.00 39.76           O  
ANISOU 2448  O   ASP B  18     4578   5385   5144     68   -872    988       O  
ATOM   2449  CB  ASP B  18      17.354  43.209  -0.378  1.00 43.88           C  
ANISOU 2449  CB  ASP B  18     5370   5667   5637   -449   -550    784       C  
ATOM   2450  CG  ASP B  18      17.331  41.697  -0.366  1.00 45.21           C  
ANISOU 2450  CG  ASP B  18     5642   5723   5815   -647   -593    732       C  
ATOM   2451  OD1 ASP B  18      16.707  41.101  -1.271  1.00 46.17           O  
ANISOU 2451  OD1 ASP B  18     5732   5871   5940   -735   -615    786       O  
ATOM   2452  OD2 ASP B  18      17.948  41.104   0.542  1.00 45.72           O  
ANISOU 2452  OD2 ASP B  18     5750   5714   5906   -700   -591    668       O  
ATOM   2453  N   ASN B  19      16.380  45.813  -2.151  1.00 39.21           N  
ANISOU 2453  N   ASN B  19     4333   5453   5112    -86   -806    837       N  
ATOM   2454  CA  ASN B  19      16.088  47.244  -2.126  1.00 38.33           C  
ANISOU 2454  CA  ASN B  19     4133   5450   4981    -20   -820    812       C  
ATOM   2455  C   ASN B  19      17.059  48.076  -2.958  1.00 36.44           C  
ANISOU 2455  C   ASN B  19     3736   5306   4806    -38   -778    811       C  
ATOM   2456  O   ASN B  19      17.369  49.215  -2.619  1.00 35.81           O  
ANISOU 2456  O   ASN B  19     3576   5289   4743    -41   -790    847       O  
ATOM   2457  CB  ASN B  19      16.060  47.744  -0.684  1.00 39.08           C  
ANISOU 2457  CB  ASN B  19     4287   5544   5018     20   -844    744       C  
ATOM   2458  CG  ASN B  19      14.850  47.244   0.071  1.00 39.89           C  
ANISOU 2458  CG  ASN B  19     4437   5591   5130      7   -871    661       C  
ATOM   2459  OD1 ASN B  19      13.721  47.373  -0.398  1.00 40.09           O  
ANISOU 2459  OD1 ASN B  19     4465   5589   5178    -48   -929    498       O  
ATOM   2460  ND2 ASN B  19      15.077  46.655   1.237  1.00 40.79           N  
ANISOU 2460  ND2 ASN B  19     4603   5695   5201    -11   -733    742       N  
ATOM   2461  N   VAL B  20      17.535  47.485  -4.049  1.00 35.68           N  
ANISOU 2461  N   VAL B  20     3611   5207   4737     -9   -811    726       N  
ATOM   2462  CA  VAL B  20      18.302  48.206  -5.054  1.00 35.38           C  
ANISOU 2462  CA  VAL B  20     3582   5224   4638    158   -761    652       C  
ATOM   2463  C   VAL B  20      17.712  47.907  -6.421  1.00 36.46           C  
ANISOU 2463  C   VAL B  20     3831   5302   4722    230   -834    567       C  
ATOM   2464  O   VAL B  20      17.722  46.763  -6.863  1.00 36.51           O  
ANISOU 2464  O   VAL B  20     3815   5334   4725    410   -911    526       O  
ATOM   2465  CB  VAL B  20      19.793  47.820  -5.047  1.00 34.15           C  
ANISOU 2465  CB  VAL B  20     3345   5116   4513    127   -653    727       C  
ATOM   2466  CG1 VAL B  20      20.549  48.621  -6.095  1.00 33.45           C  
ANISOU 2466  CG1 VAL B  20     3153   5098   4459    176   -555    761       C  
ATOM   2467  CG2 VAL B  20      20.396  48.044  -3.672  1.00 33.96           C  
ANISOU 2467  CG2 VAL B  20     3412   5072   4418     51   -651    700       C  
ATOM   2468  N   SER B  21      17.178  48.926  -7.084  1.00 37.52           N  
ANISOU 2468  N   SER B  21     4093   5351   4814    197   -741    572       N  
ATOM   2469  CA  SER B  21      16.644  48.741  -8.430  1.00 38.74           C  
ANISOU 2469  CA  SER B  21     4407   5468   4844    287   -857    592       C  
ATOM   2470  C   SER B  21      17.770  48.824  -9.456  1.00 38.38           C  
ANISOU 2470  C   SER B  21     4453   5493   4637    464   -928    631       C  
ATOM   2471  O   SER B  21      18.861  49.296  -9.141  1.00 37.86           O  
ANISOU 2471  O   SER B  21     4366   5482   4538    585   -919    784       O  
ATOM   2472  CB  SER B  21      15.568  49.786  -8.735  1.00 39.77           C  
ANISOU 2472  CB  SER B  21     4536   5540   5035    287   -949    611       C  
ATOM   2473  OG  SER B  21      16.132  51.085  -8.802  1.00 40.75           O  
ANISOU 2473  OG  SER B  21     4641   5622   5219    325   -962    635       O  
ATOM   2474  N   GLU B  22      17.501  48.368 -10.678  1.00 38.94           N  
ANISOU 2474  N   GLU B  22     4625   5616   4555    651  -1002    650       N  
ATOM   2475  CA  GLU B  22      18.469  48.451 -11.768  1.00 38.74           C  
ANISOU 2475  CA  GLU B  22     4632   5671   4416    750  -1048    486       C  
ATOM   2476  C   GLU B  22      18.876  49.894 -12.034  1.00 38.72           C  
ANISOU 2476  C   GLU B  22     4540   5792   4380    941  -1125    409       C  
ATOM   2477  O   GLU B  22      20.053  50.180 -12.262  1.00 38.57           O  
ANISOU 2477  O   GLU B  22     4397   5949   4310    976  -1532    351       O  
ATOM   2478  CB  GLU B  22      17.896  47.822 -13.045  1.00 39.10           C  
ANISOU 2478  CB  GLU B  22     4703   5727   4425    622  -1017    375       C  
ATOM   2479  CG  GLU B  22      18.037  46.312 -13.144  1.00 39.25           C  
ANISOU 2479  CG  GLU B  22     4722   5712   4477    585   -923    371       C  
ATOM   2480  CD  GLU B  22      19.428  45.875 -13.575  0.39 39.47           C  
ANISOU 2480  CD  GLU B  22     4792   5673   4530    451   -730    310       C  
ATOM   2481  OE1 GLU B  22      20.311  46.745 -13.727  0.58 39.29           O  
ANISOU 2481  OE1 GLU B  22     4762   5643   4524    332   -733    266       O  
ATOM   2482  OE2 GLU B  22      19.640  44.657 -13.761  0.47 39.59           O  
ANISOU 2482  OE2 GLU B  22     4817   5660   4567    480   -640    284       O  
ATOM   2483  N   GLU B  23      17.899  50.795 -12.013  1.00 38.27           N  
ANISOU 2483  N   GLU B  23     4535   5661   4343   1176   -889    459       N  
ATOM   2484  CA  GLU B  23      18.164  52.211 -12.232  1.00 37.62           C  
ANISOU 2484  CA  GLU B  23     4560   5488   4247   1308   -783    554       C  
ATOM   2485  C   GLU B  23      19.015  52.806 -11.106  1.00 36.40           C  
ANISOU 2485  C   GLU B  23     4381   5353   4098   1466   -812    637       C  
ATOM   2486  O   GLU B  23      19.870  53.654 -11.348  1.00 37.52           O  
ANISOU 2486  O   GLU B  23     4498   5633   4126   1471   -832    722       O  
ATOM   2487  CB  GLU B  23      16.850  52.980 -12.369  1.00 37.93           C  
ANISOU 2487  CB  GLU B  23     4671   5461   4281   1301   -668    622       C  
ATOM   2488  N   GLN B  24      18.775  52.357  -9.875  1.00 34.45           N  
ANISOU 2488  N   GLN B  24     4063   5076   3950   1660   -850    569       N  
ATOM   2489  CA  GLN B  24      19.529  52.828  -8.712  1.00 33.13           C  
ANISOU 2489  CA  GLN B  24     3997   4836   3755   1555   -624    650       C  
ATOM   2490  C   GLN B  24      20.974  52.351  -8.758  1.00 32.15           C  
ANISOU 2490  C   GLN B  24     3990   4804   3422   1369   -607    686       C  
ATOM   2491  O   GLN B  24      21.891  53.108  -8.442  1.00 32.44           O  
ANISOU 2491  O   GLN B  24     4086   4820   3420   1140   -348    831       O  
ATOM   2492  CB  GLN B  24      18.862  52.364  -7.410  1.00 33.11           C  
ANISOU 2492  CB  GLN B  24     3911   4705   3964   1449   -560    563       C  
ATOM   2493  CG  GLN B  24      17.647  53.186  -7.005  1.00 33.09           C  
ANISOU 2493  CG  GLN B  24     3868   4557   4146   1294   -499    523       C  
ATOM   2494  CD  GLN B  24      16.892  52.569  -5.846  1.00 33.25           C  
ANISOU 2494  CD  GLN B  24     3868   4425   4342   1134   -556    546       C  
ATOM   2495  OE1 GLN B  24      16.857  51.347  -5.693  1.00 33.03           O  
ANISOU 2495  OE1 GLN B  24     3740   4324   4486    960   -711    462       O  
ATOM   2496  NE2 GLN B  24      16.283  53.410  -5.022  1.00 33.74           N  
ANISOU 2496  NE2 GLN B  24     4064   4468   4288    990   -410    589       N  
ATOM   2497  N   TYR B  25      21.165  51.089  -9.131  1.00 30.83           N  
ANISOU 2497  N   TYR B  25     3781   4629   3304   1506   -759    629       N  
ATOM   2498  CA  TYR B  25      22.498  50.549  -9.371  1.00 30.40           C  
ANISOU 2498  CA  TYR B  25     3748   4505   3298   1465   -874    512       C  
ATOM   2499  C   TYR B  25      23.228  51.369 -10.426  1.00 30.97           C  
ANISOU 2499  C   TYR B  25     3850   4604   3312   1508  -1022    564       C  
ATOM   2500  O   TYR B  25      24.384  51.744 -10.243  1.00 30.75           O  
ANISOU 2500  O   TYR B  25     3963   4370   3351   1648   -948    520       O  
ATOM   2501  CB  TYR B  25      22.410  49.083  -9.810  1.00 29.18           C  
ANISOU 2501  CB  TYR B  25     3581   4280   3225   1405   -885    322       C  
ATOM   2502  CG  TYR B  25      23.750  48.416 -10.036  1.00 27.97           C  
ANISOU 2502  CG  TYR B  25     3394   4099   3136   1322   -881    304       C  
ATOM   2503  CD1 TYR B  25      24.351  47.671  -9.031  1.00 28.09           C  
ANISOU 2503  CD1 TYR B  25     3425   4091   3157   1228   -776    314       C  
ATOM   2504  CD2 TYR B  25      24.418  48.533 -11.253  1.00 27.64           C  
ANISOU 2504  CD2 TYR B  25     3467   4021   3016   1360   -654    309       C  
ATOM   2505  CE1 TYR B  25      25.579  47.057  -9.229  1.00 27.60           C  
ANISOU 2505  CE1 TYR B  25     3434   3979   3075   1270   -656    362       C  
ATOM   2506  CE2 TYR B  25      25.648  47.923 -11.457  1.00 27.74           C  
ANISOU 2506  CE2 TYR B  25     3513   4044   2983   1367   -590    385       C  
ATOM   2507  CZ  TYR B  25      26.222  47.189 -10.437  1.00 27.32           C  
ANISOU 2507  CZ  TYR B  25     3466   3931   2981   1211   -514    349       C  
ATOM   2508  OH  TYR B  25      27.437  46.578 -10.622  1.00 27.53           O  
ANISOU 2508  OH  TYR B  25     3564   3895   3002    997   -335    270       O  
ATOM   2509  N   GLN B  26      22.542  51.645 -11.532  1.00 31.89           N  
ANISOU 2509  N   GLN B  26     3992   4747   3378   1386  -1013    689       N  
ATOM   2510  CA  GLN B  26      23.121  52.432 -12.613  1.00 33.02           C  
ANISOU 2510  CA  GLN B  26     4137   4894   3515   1208  -1067    695       C  
ATOM   2511  C   GLN B  26      23.511  53.821 -12.113  1.00 31.45           C  
ANISOU 2511  C   GLN B  26     4002   4693   3255   1347   -871    867       C  
ATOM   2512  O   GLN B  26      24.562  54.352 -12.472  1.00 30.71           O  
ANISOU 2512  O   GLN B  26     3913   4699   3056   1175   -755    932       O  
ATOM   2513  CB  GLN B  26      22.137  52.535 -13.785  1.00 35.46           C  
ANISOU 2513  CB  GLN B  26     4397   5166   3911    930  -1193    620       C  
ATOM   2514  CG  GLN B  26      22.742  53.111 -15.055  1.00 38.44           C  
ANISOU 2514  CG  GLN B  26     4857   5365   4383    703  -1084    554       C  
ATOM   2515  CD  GLN B  26      23.819  52.216 -15.636  1.00 41.65           C  
ANISOU 2515  CD  GLN B  26     5371   5554   4901    288   -807    516       C  
ATOM   2516  OE1 GLN B  26      23.676  50.994 -15.668  1.00 42.65           O  
ANISOU 2516  OE1 GLN B  26     5526   5546   5132    150   -753    350       O  
ATOM   2517  NE2 GLN B  26      24.907  52.820 -16.093  1.00 42.60           N  
ANISOU 2517  NE2 GLN B  26     5544   5608   5032     68   -637    604       N  
ATOM   2518  N   GLN B  27      22.661  54.391 -11.264  1.00 30.05           N  
ANISOU 2518  N   GLN B  27     3740   4504   3175   1605   -658    887       N  
ATOM   2519  CA  GLN B  27      22.911  55.699 -10.678  1.00 30.76           C  
ANISOU 2519  CA  GLN B  27     3740   4603   3345   1495   -375    617       C  
ATOM   2520  C   GLN B  27      24.198  55.700  -9.858  1.00 29.09           C  
ANISOU 2520  C   GLN B  27     3562   4332   3158   1271   -250    610       C  
ATOM   2521  O   GLN B  27      25.032  56.594  -9.985  1.00 29.36           O  
ANISOU 2521  O   GLN B  27     3492   4445   3218   1215   -253    590       O  
ATOM   2522  CB  GLN B  27      21.722  56.116  -9.809  1.00 33.05           C  
ANISOU 2522  CB  GLN B  27     4049   4823   3685   1497   -257    348       C  
ATOM   2523  CG  GLN B  27      21.736  57.566  -9.369  1.00 34.82           C  
ANISOU 2523  CG  GLN B  27     4251   5009   3969   1442   -291    219       C  
ATOM   2524  CD  GLN B  27      20.519  57.934  -8.545  1.00 35.94           C  
ANISOU 2524  CD  GLN B  27     4373   5057   4226   1575   -471    227       C  
ATOM   2525  OE1 GLN B  27      19.612  57.122  -8.362  1.00 36.30           O  
ANISOU 2525  OE1 GLN B  27     4333   5116   4343   1588   -549    338       O  
ATOM   2526  NE2 GLN B  27      20.495  59.162  -8.036  1.00 36.11           N  
ANISOU 2526  NE2 GLN B  27     4472   5002   4245   1654   -582     73       N  
ATOM   2527  N   ILE B  28      24.357  54.676  -9.027  1.00 27.55           N  
ANISOU 2527  N   ILE B  28     3284   4292   2892   1010   -217    636       N  
ATOM   2528  CA  ILE B  28      25.546  54.533  -8.199  1.00 25.53           C  
ANISOU 2528  CA  ILE B  28     2940   3972   2787   1035   -181    657       C  
ATOM   2529  C   ILE B  28      26.789  54.299  -9.057  1.00 24.23           C  
ANISOU 2529  C   ILE B  28     2851   3922   2433    944   -220    535       C  
ATOM   2530  O   ILE B  28      27.836  54.902  -8.828  1.00 23.21           O  
ANISOU 2530  O   ILE B  28     2673   3872   2274    935   -201    539       O  
ATOM   2531  CB  ILE B  28      25.371  53.381  -7.192  1.00 25.64           C  
ANISOU 2531  CB  ILE B  28     2837   3962   2942   1020   -149    709       C  
ATOM   2532  CG1 ILE B  28      24.246  53.718  -6.207  1.00 25.83           C  
ANISOU 2532  CG1 ILE B  28     2748   3934   3132   1313    119    552       C  
ATOM   2533  CG2 ILE B  28      26.674  53.107  -6.452  1.00 25.92           C  
ANISOU 2533  CG2 ILE B  28     2743   4078   3027    799   -415    639       C  
ATOM   2534  CD1 ILE B  28      23.689  52.522  -5.468  1.00 26.25           C  
ANISOU 2534  CD1 ILE B  28     2724   4027   3222   1179    348    472       C  
ATOM   2535  N   SER B  29      26.661  53.437 -10.059  1.00 24.59           N  
ANISOU 2535  N   SER B  29     2995   3931   2417    938   -298    552       N  
ATOM   2536  CA  SER B  29      27.766  53.164 -10.969  1.00 24.36           C  
ANISOU 2536  CA  SER B  29     2933   3870   2451   1059   -211    417       C  
ATOM   2537  C   SER B  29      28.197  54.429 -11.726  1.00 25.12           C  
ANISOU 2537  C   SER B  29     3064   3935   2544   1295   -165    715       C  
ATOM   2538  O   SER B  29      29.390  54.719 -11.837  1.00 24.43           O  
ANISOU 2538  O   SER B  29     3082   3813   2387   1229    -12    688       O  
ATOM   2539  CB  SER B  29      27.380  52.061 -11.957  1.00 25.81           C  
ANISOU 2539  CB  SER B  29     3092   4058   2659    756   -259    -51       C  
ATOM   2540  OG  SER B  29      28.458  51.766 -12.827  1.00 26.61           O  
ANISOU 2540  OG  SER B  29     3190   4143   2778    609   -466   -139       O  
ATOM   2541  N   ASP B  30      27.224  55.191 -12.225  1.00 26.67           N  
ANISOU 2541  N   ASP B  30     3227   4163   2742   1451   -181    740       N  
ATOM   2542  CA  ASP B  30      27.522  56.426 -12.952  1.00 26.94           C  
ANISOU 2542  CA  ASP B  30     3379   4088   2769   1525   -273    846       C  
ATOM   2543  C   ASP B  30      28.299  57.429 -12.110  1.00 25.92           C  
ANISOU 2543  C   ASP B  30     3335   3745   2770   1277    -39    843       C  
ATOM   2544  O   ASP B  30      29.123  58.172 -12.633  1.00 25.73           O  
ANISOU 2544  O   ASP B  30     3292   3577   2906   1023    175    863       O  
ATOM   2545  CB  ASP B  30      26.236  57.085 -13.458  1.00 29.92           C  
ANISOU 2545  CB  ASP B  30     3703   4636   3028   1597   -459    824       C  
ATOM   2546  CG  ASP B  30      25.604  56.325 -14.603  1.00 33.06           C  
ANISOU 2546  CG  ASP B  30     4042   5139   3380   1631   -478    806       C  
ATOM   2547  OD1 ASP B  30      26.284  55.458 -15.194  1.00 34.32           O  
ANISOU 2547  OD1 ASP B  30     4137   5478   3424   1582   -302    832       O  
ATOM   2548  OD2 ASP B  30      24.427  56.604 -14.918  1.00 34.34           O  
ANISOU 2548  OD2 ASP B  30     4201   5226   3620   1669   -537    882       O  
ATOM   2549  N   TYR B  31      28.031  57.452 -10.808  1.00 24.73           N  
ANISOU 2549  N   TYR B  31     3292   3475   2629   1419   -174    587       N  
ATOM   2550  CA  TYR B  31      28.742  58.347  -9.905  1.00 23.64           C  
ANISOU 2550  CA  TYR B  31     3208   3299   2476   1290   -141    548       C  
ATOM   2551  C   TYR B  31      30.154  57.842  -9.606  1.00 21.92           C  
ANISOU 2551  C   TYR B  31     2981   3024   2323   1365   -219    579       C  
ATOM   2552  O   TYR B  31      31.117  58.610  -9.591  1.00 22.64           O  
ANISOU 2552  O   TYR B  31     3165   3205   2233   1295     60    528       O  
ATOM   2553  CB  TYR B  31      27.963  58.517  -8.597  1.00 23.75           C  
ANISOU 2553  CB  TYR B  31     3269   3199   2557   1204    -79    601       C  
ATOM   2554  CG  TYR B  31      28.610  59.488  -7.644  1.00 24.68           C  
ANISOU 2554  CG  TYR B  31     3378   3316   2683   1376    -40    536       C  
ATOM   2555  CD1 TYR B  31      28.446  60.854  -7.810  1.00 24.99           C  
ANISOU 2555  CD1 TYR B  31     3356   3286   2853   1683   -129    405       C  
ATOM   2556  CD2 TYR B  31      29.391  59.043  -6.580  1.00 24.36           C  
ANISOU 2556  CD2 TYR B  31     3220   3297   2740   1407     72    482       C  
ATOM   2557  CE1 TYR B  31      29.040  61.754  -6.955  1.00 25.87           C  
ANISOU 2557  CE1 TYR B  31     3437   3452   2938   1731     12    296       C  
ATOM   2558  CE2 TYR B  31      29.987  59.936  -5.715  1.00 25.75           C  
ANISOU 2558  CE2 TYR B  31     3325   3606   2854   1510    298    459       C  
ATOM   2559  CZ  TYR B  31      29.805  61.293  -5.905  1.00 26.44           C  
ANISOU 2559  CZ  TYR B  31     3491   3606   2949   1553    154    307       C  
ATOM   2560  OH  TYR B  31      30.393  62.198  -5.058  1.00 28.99           O  
ANISOU 2560  OH  TYR B  31     3767   4006   3241   1327     74    285       O  
ATOM   2561  N   PHE B  32      30.260  56.537  -9.373  1.00 21.33           N  
ANISOU 2561  N   PHE B  32     2927   2845   2331   1288   -237    769       N  
ATOM   2562  CA  PHE B  32      31.477  55.925  -8.837  1.00 20.30           C  
ANISOU 2562  CA  PHE B  32     2694   2844   2175   1249    -69    721       C  
ATOM   2563  C   PHE B  32      32.547  55.631  -9.888  1.00 20.13           C  
ANISOU 2563  C   PHE B  32     2682   2867   2100   1187    -94    697       C  
ATOM   2564  O   PHE B  32      33.724  55.928  -9.672  1.00 20.18           O  
ANISOU 2564  O   PHE B  32     2641   2846   2180   1187     29    557       O  
ATOM   2565  CB  PHE B  32      31.098  54.637  -8.101  1.00 18.41           C  
ANISOU 2565  CB  PHE B  32     2441   2520   2033   1213     91    819       C  
ATOM   2566  CG  PHE B  32      32.261  53.912  -7.466  1.00 17.56           C  
ANISOU 2566  CG  PHE B  32     2230   2450   1994   1103    131    717       C  
ATOM   2567  CD1 PHE B  32      33.205  54.589  -6.716  1.00 18.24           C  
ANISOU 2567  CD1 PHE B  32     2437   2557   1936   1020    142    703       C  
ATOM   2568  CD2 PHE B  32      32.383  52.542  -7.602  1.00 18.40           C  
ANISOU 2568  CD2 PHE B  32     2250   2611   2132    890    311    583       C  
ATOM   2569  CE1 PHE B  32      34.259  53.917  -6.125  1.00 17.92           C  
ANISOU 2569  CE1 PHE B  32     2436   2472   1900    966    109    566       C  
ATOM   2570  CE2 PHE B  32      33.427  51.863  -7.009  1.00 17.66           C  
ANISOU 2570  CE2 PHE B  32     2143   2470   2096   1006    228    625       C  
ATOM   2571  CZ  PHE B  32      34.368  52.552  -6.269  1.00 17.95           C  
ANISOU 2571  CZ  PHE B  32     2392   2487   1942    870     91    525       C  
ATOM   2572  N   VAL B  33      32.134  55.063 -11.017  1.00 21.57           N  
ANISOU 2572  N   VAL B  33     2827   3238   2132   1172    101    719       N  
ATOM   2573  CA  VAL B  33      33.086  54.620 -12.038  1.00 22.76           C  
ANISOU 2573  CA  VAL B  33     3000   3555   2093    838      3    693       C  
ATOM   2574  C   VAL B  33      34.054  55.721 -12.504  1.00 23.26           C  
ANISOU 2574  C   VAL B  33     2997   3607   2233   1054    139    857       C  
ATOM   2575  O   VAL B  33      35.253  55.469 -12.600  1.00 23.94           O  
ANISOU 2575  O   VAL B  33     2957   3839   2300    954    104    979       O  
ATOM   2576  CB  VAL B  33      32.354  54.016 -13.255  1.00 22.71           C  
ANISOU 2576  CB  VAL B  33     3079   3577   1974    341    211    572       C  
ATOM   2577  CG1 VAL B  33      33.337  53.712 -14.380  1.00 22.15           C  
ANISOU 2577  CG1 VAL B  33     3140   3498   1778    186    443    586       C  
ATOM   2578  CG2 VAL B  33      31.624  52.749 -12.845  1.00 22.74           C  
ANISOU 2578  CG2 VAL B  33     3023   3569   2046    315     37    550       C  
ATOM   2579  N   PRO B  34      33.562  56.956 -12.759  1.00 23.96           N  
ANISOU 2579  N   PRO B  34     3089   3535   2479   1198    211    982       N  
ATOM   2580  CA  PRO B  34      34.526  57.992 -13.159  1.00 23.81           C  
ANISOU 2580  CA  PRO B  34     3190   3253   2603   1181    129    953       C  
ATOM   2581  C   PRO B  34      35.539  58.362 -12.077  1.00 23.69           C  
ANISOU 2581  C   PRO B  34     3184   3108   2709    785    261    719       C  
ATOM   2582  O   PRO B  34      36.588  58.927 -12.383  1.00 24.59           O  
ANISOU 2582  O   PRO B  34     3296   3325   2722    309    237    664       O  
ATOM   2583  CB  PRO B  34      33.635  59.205 -13.470  1.00 24.60           C  
ANISOU 2583  CB  PRO B  34     3275   3345   2726   1213    -64   1177       C  
ATOM   2584  CG  PRO B  34      32.293  58.653 -13.712  1.00 25.47           C  
ANISOU 2584  CG  PRO B  34     3295   3549   2834   1347    -37   1117       C  
ATOM   2585  CD  PRO B  34      32.179  57.458 -12.816  1.00 24.81           C  
ANISOU 2585  CD  PRO B  34     3217   3563   2646   1352    -55   1090       C  
ATOM   2586  N   LEU B  35      35.230  58.045 -10.824  1.00 21.80           N  
ANISOU 2586  N   LEU B  35     3104   2651   2529    939    267    683       N  
ATOM   2587  CA  LEU B  35      36.094  58.429  -9.724  1.00 21.33           C  
ANISOU 2587  CA  LEU B  35     3102   2465   2536   1083    497    673       C  
ATOM   2588  C   LEU B  35      37.203  57.406  -9.499  1.00 20.09           C  
ANISOU 2588  C   LEU B  35     2991   2240   2404    990    541    619       C  
ATOM   2589  O   LEU B  35      38.248  57.734  -8.942  1.00 21.09           O  
ANISOU 2589  O   LEU B  35     3076   2340   2598    791    532    664       O  
ATOM   2590  CB  LEU B  35      35.281  58.597  -8.442  1.00 22.45           C  
ANISOU 2590  CB  LEU B  35     3205   2717   2607   1056    662    457       C  
ATOM   2591  CG  LEU B  35      34.112  59.579  -8.480  1.00 24.00           C  
ANISOU 2591  CG  LEU B  35     3254   3012   2854   1229    610    476       C  
ATOM   2592  CD1 LEU B  35      33.486  59.674  -7.094  1.00 24.83           C  
ANISOU 2592  CD1 LEU B  35     3282   3254   2898   1223    643    520       C  
ATOM   2593  CD2 LEU B  35      34.571  60.945  -8.955  1.00 24.36           C  
ANISOU 2593  CD2 LEU B  35     3381   2818   3057   1335    548    586       C  
ATOM   2594  N   VAL B  36      36.967  56.176  -9.945  1.00 19.16           N  
ANISOU 2594  N   VAL B  36     3031   2108   2141    657    250    620       N  
ATOM   2595  CA  VAL B  36      37.882  55.066  -9.669  1.00 19.00           C  
ANISOU 2595  CA  VAL B  36     2750   2354   2114    730    210    367       C  
ATOM   2596  C   VAL B  36      39.291  55.320 -10.200  1.00 19.28           C  
ANISOU 2596  C   VAL B  36     2856   2513   1957    665    262    334       C  
ATOM   2597  O   VAL B  36      40.279  54.997  -9.545  1.00 19.24           O  
ANISOU 2597  O   VAL B  36     3003   2352   1954    650     39    329       O  
ATOM   2598  CB  VAL B  36      37.336  53.753 -10.260  1.00 16.87           C  
ANISOU 2598  CB  VAL B  36     2511   1902   1995    791    313    259       C  
ATOM   2599  CG1 VAL B  36      38.388  52.647 -10.216  1.00 16.79           C  
ANISOU 2599  CG1 VAL B  36     2373   2073   1932    535    179    329       C  
ATOM   2600  CG2 VAL B  36      36.077  53.329  -9.519  1.00 17.35           C  
ANISOU 2600  CG2 VAL B  36     2520   2029   2044    962    256    344       C  
ATOM   2601  N   ASN B  37      39.386  55.930 -11.378  1.00 19.89           N  
ANISOU 2601  N   ASN B  37     3040   2522   1996    494    437    277       N  
ATOM   2602  CA  ASN B  37      40.690  56.177 -11.985  1.00 19.86           C  
ANISOU 2602  CA  ASN B  37     3196   2490   1861    599    473    321       C  
ATOM   2603  C   ASN B  37      40.976  57.663 -12.189  1.00 21.08           C  
ANISOU 2603  C   ASN B  37     3511   2558   1940    432    492    205       C  
ATOM   2604  O   ASN B  37      41.837  58.040 -12.984  1.00 22.43           O  
ANISOU 2604  O   ASN B  37     3834   2592   2097    337    339     65       O  
ATOM   2605  CB  ASN B  37      40.796  55.436 -13.317  1.00 19.91           C  
ANISOU 2605  CB  ASN B  37     3194   2579   1793    505    358    409       C  
ATOM   2606  CG  ASN B  37      40.616  53.940 -13.165  1.00 19.96           C  
ANISOU 2606  CG  ASN B  37     3174   2657   1751    312    370    439       C  
ATOM   2607  OD1 ASN B  37      41.440  53.270 -12.538  1.00 20.31           O  
ANISOU 2607  OD1 ASN B  37     3322   2623   1772    370    232    347       O  
ATOM   2608  ND2 ASN B  37      39.539  53.404 -13.739  1.00 20.42           N  
ANISOU 2608  ND2 ASN B  37     3293   2736   1730    135    440    358       N  
ATOM   2609  N   LYS B  38      40.268  58.510 -11.450  1.00 21.93           N  
ANISOU 2609  N   LYS B  38     3652   2587   2093    409    320    235       N  
ATOM   2610  CA  LYS B  38      40.449  59.947 -11.589  1.00 24.15           C  
ANISOU 2610  CA  LYS B  38     3901   2940   2334    388    550    350       C  
ATOM   2611  C   LYS B  38      41.791  60.387 -11.025  1.00 24.61           C  
ANISOU 2611  C   LYS B  38     4020   3004   2328    156    690    308       C  
ATOM   2612  O   LYS B  38      42.067  60.191  -9.844  1.00 25.35           O  
ANISOU 2612  O   LYS B  38     4041   3171   2418    300    543    240       O  
ATOM   2613  CB  LYS B  38      39.315  60.700 -10.897  1.00 26.09           C  
ANISOU 2613  CB  LYS B  38     4058   3172   2682    379    574    628       C  
ATOM   2614  CG  LYS B  38      39.431  62.210 -10.974  1.00 28.67           C  
ANISOU 2614  CG  LYS B  38     4306   3487   3099    135    381    720       C  
ATOM   2615  CD  LYS B  38      38.113  62.866 -10.608  1.00 31.43           C  
ANISOU 2615  CD  LYS B  38     4565   3979   3397    166    195    681       C  
ATOM   2616  CE  LYS B  38      37.010  62.454 -11.577  1.00 33.41           C  
ANISOU 2616  CE  LYS B  38     4718   4371   3604     40     -4    649       C  
ATOM   2617  NZ  LYS B  38      37.285  62.918 -12.974  1.00 34.92           N  
ANISOU 2617  NZ  LYS B  38     4877   4609   3780     21    132    562       N  
ATOM   2618  N   PRO B  39      42.642  60.982 -11.872  1.00 25.28           N  
ANISOU 2618  N   PRO B  39     4289   3087   2228   -100    908    373       N  
ATOM   2619  CA  PRO B  39      43.942  61.474 -11.406  1.00 26.19           C  
ANISOU 2619  CA  PRO B  39     4487   3125   2341   -201   1101    432       C  
ATOM   2620  C   PRO B  39      43.804  62.446 -10.233  1.00 27.78           C  
ANISOU 2620  C   PRO B  39     4722   3227   2604     92   1123    199       C  
ATOM   2621  O   PRO B  39      42.882  63.261 -10.219  1.00 28.21           O  
ANISOU 2621  O   PRO B  39     4807   3213   2697    190   1155      1       O  
ATOM   2622  CB  PRO B  39      44.513  62.188 -12.640  1.00 26.79           C  
ANISOU 2622  CB  PRO B  39     4511   3327   2341   -253   1088    459       C  
ATOM   2623  CG  PRO B  39      43.833  61.545 -13.791  1.00 26.64           C  
ANISOU 2623  CG  PRO B  39     4505   3396   2221   -429   1048    298       C  
ATOM   2624  CD  PRO B  39      42.446  61.221 -13.312  1.00 25.48           C  
ANISOU 2624  CD  PRO B  39     4344   3232   2103   -442   1178    474       C  
ATOM   2625  N   LYS B  40      44.706  62.326  -9.263  1.00 28.43           N  
ANISOU 2625  N   LYS B  40     4780   3271   2750    130   1177    313       N  
ATOM   2626  CA  LYS B  40      44.773  63.208  -8.092  1.00 28.96           C  
ANISOU 2626  CA  LYS B  40     4861   3197   2943    -67   1295    342       C  
ATOM   2627  C   LYS B  40      43.548  63.132  -7.168  1.00 26.54           C  
ANISOU 2627  C   LYS B  40     4647   2777   2659   -174   1027    194       C  
ATOM   2628  O   LYS B  40      43.410  63.939  -6.244  1.00 28.34           O  
ANISOU 2628  O   LYS B  40     4899   2968   2900   -675   1027    -88       O  
ATOM   2629  CB  LYS B  40      45.013  64.655  -8.544  1.00 32.39           C  
ANISOU 2629  CB  LYS B  40     5184   3698   3426      9   1488    499       C  
ATOM   2630  CG  LYS B  40      46.341  64.809  -9.301  1.00 35.75           C  
ANISOU 2630  CG  LYS B  40     5474   4174   3933   -131   1568    595       C  
ATOM   2631  CD  LYS B  40      46.707  66.261  -9.554  1.00 38.68           C  
ANISOU 2631  CD  LYS B  40     5708   4667   4322     60   1496    642       C  
ATOM   2632  CE  LYS B  40      48.158  66.384 -10.022  1.00 40.99           C  
ANISOU 2632  CE  LYS B  40     5902   5034   4636    263   1315    586       C  
ATOM   2633  NZ  LYS B  40      48.451  65.539 -11.215  1.00 42.20           N  
ANISOU 2633  NZ  LYS B  40     6073   5175   4785    394   1134    545       N  
ATOM   2634  N   LEU B  41      42.667  62.165  -7.407  1.00 22.27           N  
ANISOU 2634  N   LEU B  41     4089   2207   2167    214    809    531       N  
ATOM   2635  CA  LEU B  41      41.649  61.813  -6.420  1.00 20.58           C  
ANISOU 2635  CA  LEU B  41     3763   1935   2121    503    523    578       C  
ATOM   2636  C   LEU B  41      42.028  60.497  -5.756  1.00 19.32           C  
ANISOU 2636  C   LEU B  41     3624   1648   2069    614    464    465       C  
ATOM   2637  O   LEU B  41      41.983  59.451  -6.404  1.00 20.47           O  
ANISOU 2637  O   LEU B  41     3968   1535   2273    381    688    328       O  
ATOM   2638  CB  LEU B  41      40.269  61.682  -7.054  1.00 21.82           C  
ANISOU 2638  CB  LEU B  41     3923   2283   2083    679    536    559       C  
ATOM   2639  CG  LEU B  41      39.144  61.256  -6.105  1.00 22.21           C  
ANISOU 2639  CG  LEU B  41     3915   2488   2034    891    276    199       C  
ATOM   2640  CD1 LEU B  41      38.943  62.297  -5.012  1.00 22.41           C  
ANISOU 2640  CD1 LEU B  41     4170   2429   1917    766    377    164       C  
ATOM   2641  CD2 LEU B  41      37.855  61.013  -6.862  1.00 22.54           C  
ANISOU 2641  CD2 LEU B  41     3647   2680   2237   1023   -108    190       C  
ATOM   2642  N  ALYS B  42      42.411  60.552  -4.485  0.55 19.06           N  
ANISOU 2642  N  ALYS B  42     3439   1706   2095    424    567    386       N  
ATOM   2643  N  BLYS B  42      42.409  60.547  -4.483  0.45 19.30           N  
ANISOU 2643  N  BLYS B  42     3453   1810   2071    397    501    390       N  
ATOM   2644  CA ALYS B  42      42.717  59.340  -3.733  0.55 17.45           C  
ANISOU 2644  CA ALYS B  42     3178   1463   1990    492    473    331       C  
ATOM   2645  CA BLYS B  42      42.728  59.327  -3.742  0.45 18.27           C  
ANISOU 2645  CA BLYS B  42     3232   1730   1979    366    373    330       C  
ATOM   2646  C  ALYS B  42      41.507  58.415  -3.740  0.55 17.10           C  
ANISOU 2646  C  ALYS B  42     3191   1360   1948    584    504    296       C  
ATOM   2647  C  BLYS B  42      41.510  58.414  -3.734  0.45 17.44           C  
ANISOU 2647  C  BLYS B  42     3207   1468   1951    491    449    317       C  
ATOM   2648  O  ALYS B  42      40.379  58.859  -3.547  0.55 19.01           O  
ANISOU 2648  O  ALYS B  42     3422   1717   2083    573    439    537       O  
ATOM   2649  O  BLYS B  42      40.387  58.865  -3.523  0.45 19.06           O  
ANISOU 2649  O  BLYS B  42     3368   1804   2068    489    404    536       O  
ATOM   2650  CB ALYS B  42      43.124  59.685  -2.300  0.55 17.44           C  
ANISOU 2650  CB ALYS B  42     3139   1480   2008    336    270    425       C  
ATOM   2651  CB BLYS B  42      43.165  59.644  -2.310  0.45 18.81           C  
ANISOU 2651  CB BLYS B  42     3209   1949   1989    157    135    388       C  
ATOM   2652  CG ALYS B  42      44.422  60.475  -2.200  0.55 18.90           C  
ANISOU 2652  CG ALYS B  42     3263   1718   2201    213    137    451       C  
ATOM   2653  CG BLYS B  42      44.443  60.468  -2.195  0.45 20.24           C  
ANISOU 2653  CG BLYS B  42     3304   2240   2145      3    -50    458       C  
ATOM   2654  CD ALYS B  42      44.774  60.800  -0.753  0.55 20.30           C  
ANISOU 2654  CD ALYS B  42     3366   1953   2394    211     66    383       C  
ATOM   2655  CD BLYS B  42      44.792  60.744  -0.733  0.45 21.46           C  
ANISOU 2655  CD BLYS B  42     3384   2457   2312    -11   -150    506       C  
ATOM   2656  CE ALYS B  42      43.836  61.841  -0.171  0.55 22.60           C  
ANISOU 2656  CE ALYS B  42     3376   2660   2552     67    203    321       C  
ATOM   2657  CE BLYS B  42      45.977  61.692  -0.588  0.45 22.95           C  
ANISOU 2657  CE BLYS B  42     3418   2834   2466    -38    -90    627       C  
ATOM   2658  NZ ALYS B  42      43.963  63.134  -0.894  0.55 23.93           N  
ANISOU 2658  NZ ALYS B  42     3444   2982   2667    -18    182    215       N  
ATOM   2659  NZ BLYS B  42      46.420  61.795   0.832  0.45 24.50           N  
ANISOU 2659  NZ BLYS B  42     3516   3090   2704    -31     27    568       N  
ATOM   2660  N   SER B  43      41.731  57.125  -3.976  1.00 16.68           N  
ANISOU 2660  N   SER B  43     3222   1252   1863    569    504    219       N  
ATOM   2661  CA  SER B  43      40.619  56.190  -4.053  1.00 17.62           C  
ANISOU 2661  CA  SER B  43     3229   1636   1828    380    493     91       C  
ATOM   2662  C   SER B  43      39.917  55.988  -2.703  1.00 17.28           C  
ANISOU 2662  C   SER B  43     3181   1552   1833    624    378    203       C  
ATOM   2663  O   SER B  43      38.752  55.607  -2.672  1.00 17.75           O  
ANISOU 2663  O   SER B  43     3124   1744   1876    673    509    303       O  
ATOM   2664  CB  SER B  43      41.088  54.853  -4.615  1.00 17.46           C  
ANISOU 2664  CB  SER B  43     3312   1613   1706    391    708     42       C  
ATOM   2665  OG  SER B  43      41.267  54.954  -6.020  1.00 19.97           O  
ANISOU 2665  OG  SER B  43     3644   1919   2024    617    936   -104       O  
ATOM   2666  N   ARG B  44      40.600  56.273  -1.599  1.00 17.11           N  
ANISOU 2666  N   ARG B  44     3267   1408   1828    493    604    397       N  
ATOM   2667  CA  ARG B  44      39.909  56.252  -0.309  1.00 17.39           C  
ANISOU 2667  CA  ARG B  44     3398   1468   1740    487    569    307       C  
ATOM   2668  C   ARG B  44      38.805  57.300  -0.316  1.00 18.94           C  
ANISOU 2668  C   ARG B  44     3495   1801   1901    817    743    427       C  
ATOM   2669  O   ARG B  44      37.749  57.101   0.279  1.00 19.62           O  
ANISOU 2669  O   ARG B  44     3356   1968   2130   1139    744    464       O  
ATOM   2670  CB  ARG B  44      40.868  56.485   0.865  1.00 16.94           C  
ANISOU 2670  CB  ARG B  44     3386   1268   1781    352    440    232       C  
ATOM   2671  CG  ARG B  44      41.379  57.918   1.002  1.00 19.15           C  
ANISOU 2671  CG  ARG B  44     3751   1589   1937    -46    268    -27       C  
ATOM   2672  CD  ARG B  44      42.343  58.021   2.162  1.00 22.48           C  
ANISOU 2672  CD  ARG B  44     4318   1905   2320   -457    130   -182       C  
ATOM   2673  NE  ARG B  44      42.762  59.397   2.416  1.00 23.57           N  
ANISOU 2673  NE  ARG B  44     4563   1919   2475   -529    154   -277       N  
ATOM   2674  CZ  ARG B  44      43.929  59.728   2.956  1.00 25.15           C  
ANISOU 2674  CZ  ARG B  44     4892   1909   2754   -732    308   -631       C  
ATOM   2675  NH1 ARG B  44      44.795  58.784   3.302  1.00 26.20           N  
ANISOU 2675  NH1 ARG B  44     5011   2134   2810   -626    492   -866       N  
ATOM   2676  NH2 ARG B  44      44.226  61.009   3.156  1.00 25.12           N  
ANISOU 2676  NH2 ARG B  44     4985   1835   2723  -1093    337   -552       N  
ATOM   2677  N   ASP B  45      39.036  58.405  -1.023  1.00 18.76           N  
ANISOU 2677  N   ASP B  45     3512   1637   1978    953    724    649       N  
ATOM   2678  CA  ASP B  45      38.016  59.441  -1.125  1.00 20.09           C  
ANISOU 2678  CA  ASP B  45     3821   1644   2167   1079    898    489       C  
ATOM   2679  C   ASP B  45      36.955  59.060  -2.146  1.00 20.38           C  
ANISOU 2679  C   ASP B  45     3624   1826   2293   1268    860    467       C  
ATOM   2680  O   ASP B  45      35.770  59.258  -1.909  1.00 22.25           O  
ANISOU 2680  O   ASP B  45     3913   2046   2493   1287    867    547       O  
ATOM   2681  CB  ASP B  45      38.647  60.787  -1.477  1.00 21.84           C  
ANISOU 2681  CB  ASP B  45     4211   1753   2335    825    979    276       C  
ATOM   2682  CG  ASP B  45      39.505  61.327  -0.353  1.00 24.90           C  
ANISOU 2682  CG  ASP B  45     4593   2232   2636    659   1250     84       C  
ATOM   2683  OD1 ASP B  45      39.073  61.233   0.819  1.00 26.20           O  
ANISOU 2683  OD1 ASP B  45     4776   2479   2699    951   1353    210       O  
ATOM   2684  OD2 ASP B  45      40.614  61.822  -0.626  1.00 26.85           O  
ANISOU 2684  OD2 ASP B  45     4899   2460   2842    119   1300     -8       O  
ATOM   2685  N   ALA B  46      37.374  58.485  -3.271  1.00 20.16           N  
ANISOU 2685  N   ALA B  46     3498   1942   2220   1199    687    578       N  
ATOM   2686  CA  ALA B  46      36.431  58.039  -4.281  1.00 20.05           C  
ANISOU 2686  CA  ALA B  46     3389   2060   2169   1143    692    442       C  
ATOM   2687  C   ALA B  46      35.451  57.022  -3.713  1.00 19.60           C  
ANISOU 2687  C   ALA B  46     3354   1967   2124   1328    392    551       C  
ATOM   2688  O   ALA B  46      34.246  57.132  -3.893  1.00 21.29           O  
ANISOU 2688  O   ALA B  46     3795   2164   2129   1395    256    524       O  
ATOM   2689  CB  ALA B  46      37.172  57.442  -5.474  1.00 20.14           C  
ANISOU 2689  CB  ALA B  46     3265   2133   2252   1125    849    118       C  
ATOM   2690  N   ILE B  47      35.984  56.022  -3.016  1.00 19.33           N  
ANISOU 2690  N   ILE B  47     3381   1768   2195   1246    484    448       N  
ATOM   2691  CA  ILE B  47      35.159  54.970  -2.445  1.00 17.42           C  
ANISOU 2691  CA  ILE B  47     3000   1652   1967   1129    615    493       C  
ATOM   2692  C   ILE B  47      34.308  55.475  -1.273  1.00 18.07           C  
ANISOU 2692  C   ILE B  47     3103   1807   1956    986    626    465       C  
ATOM   2693  O   ILE B  47      33.125  55.167  -1.190  1.00 18.66           O  
ANISOU 2693  O   ILE B  47     3128   1906   2057    880    632    463       O  
ATOM   2694  CB  ILE B  47      36.034  53.789  -1.970  1.00 15.30           C  
ANISOU 2694  CB  ILE B  47     2562   1504   1749    825    637    365       C  
ATOM   2695  CG1 ILE B  47      36.807  53.187  -3.143  1.00 15.02           C  
ANISOU 2695  CG1 ILE B  47     2407   1521   1777    876    469    178       C  
ATOM   2696  CG2 ILE B  47      35.190  52.722  -1.302  1.00 15.84           C  
ANISOU 2696  CG2 ILE B  47     2372   1767   1878    357    546    373       C  
ATOM   2697  CD1 ILE B  47      37.995  52.352  -2.705  1.00 15.55           C  
ANISOU 2697  CD1 ILE B  47     2497   1587   1823    694    403   -120       C  
ATOM   2698  N   GLY B  48      34.917  56.261  -0.394  1.00 18.17           N  
ANISOU 2698  N   GLY B  48     3097   1876   1932   1042    798    410       N  
ATOM   2699  CA  GLY B  48      34.214  56.809   0.752  1.00 18.41           C  
ANISOU 2699  CA  GLY B  48     3310   1733   1951   1108    861    442       C  
ATOM   2700  C   GLY B  48      33.067  57.703   0.325  1.00 19.48           C  
ANISOU 2700  C   GLY B  48     3436   1820   2146   1182    820    457       C  
ATOM   2701  O   GLY B  48      31.949  57.578   0.823  1.00 20.72           O  
ANISOU 2701  O   GLY B  48     3670   1883   2318   1262    712    241       O  
ATOM   2702  N   GLN B  49      33.344  58.590  -0.628  1.00 19.77           N  
ANISOU 2702  N   GLN B  49     3463   1801   2249   1134    623    579       N  
ATOM   2703  CA  GLN B  49      32.318  59.490  -1.141  1.00 21.35           C  
ANISOU 2703  CA  GLN B  49     3407   2235   2470   1202    650    683       C  
ATOM   2704  C   GLN B  49      31.211  58.724  -1.846  1.00 21.04           C  
ANISOU 2704  C   GLN B  49     3340   2247   2408   1200    689    535       C  
ATOM   2705  O   GLN B  49      30.036  59.042  -1.693  1.00 23.07           O  
ANISOU 2705  O   GLN B  49     3576   2657   2533   1043    617    681       O  
ATOM   2706  CB  GLN B  49      32.927  60.524  -2.093  1.00 21.18           C  
ANISOU 2706  CB  GLN B  49     3360   2093   2593   1247    655    857       C  
ATOM   2707  CG  GLN B  49      33.808  61.556  -1.418  1.00 22.33           C  
ANISOU 2707  CG  GLN B  49     3486   2297   2702   1195    638    802       C  
ATOM   2708  CD  GLN B  49      34.628  62.355  -2.409  1.00 24.83           C  
ANISOU 2708  CD  GLN B  49     3818   2717   2897    913    572    812       C  
ATOM   2709  OE1 GLN B  49      34.333  62.366  -3.606  1.00 27.46           O  
ANISOU 2709  OE1 GLN B  49     4176   3189   3070    674    555   1114       O  
ATOM   2710  NE2 GLN B  49      35.669  63.017  -1.922  1.00 24.45           N  
ANISOU 2710  NE2 GLN B  49     3852   2496   2942    888    546    523       N  
ATOM   2711  N   ALA B  50      31.581  57.717  -2.632  1.00 21.08           N  
ANISOU 2711  N   ALA B  50     3351   2365   2293   1195    483    586       N  
ATOM   2712  CA  ALA B  50      30.588  56.917  -3.333  1.00 19.97           C  
ANISOU 2712  CA  ALA B  50     3199   2269   2121   1436    599    572       C  
ATOM   2713  C   ALA B  50      29.710  56.117  -2.371  1.00 20.25           C  
ANISOU 2713  C   ALA B  50     3211   2377   2106   1368    423    714       C  
ATOM   2714  O   ALA B  50      28.551  55.854  -2.661  1.00 20.38           O  
ANISOU 2714  O   ALA B  50     3279   2377   2087   1429    518    568       O  
ATOM   2715  CB  ALA B  50      31.261  55.985  -4.316  1.00 20.85           C  
ANISOU 2715  CB  ALA B  50     3245   2414   2263   1450    637    402       C  
ATOM   2716  N   PHE B  51      30.266  55.718  -1.230  1.00 21.06           N  
ANISOU 2716  N   PHE B  51     3185   2493   2324   1424    311    533       N  
ATOM   2717  CA  PHE B  51      29.491  54.946  -0.266  1.00 20.29           C  
ANISOU 2717  CA  PHE B  51     3081   2298   2330   1375    338    773       C  
ATOM   2718  C   PHE B  51      28.448  55.817   0.424  1.00 21.68           C  
ANISOU 2718  C   PHE B  51     3078   2581   2579   1420    516    754       C  
ATOM   2719  O   PHE B  51      27.325  55.381   0.655  1.00 22.54           O  
ANISOU 2719  O   PHE B  51     3031   2887   2645   1474    584    651       O  
ATOM   2720  CB  PHE B  51      30.411  54.299   0.776  1.00 19.52           C  
ANISOU 2720  CB  PHE B  51     3011   2253   2154   1238    303    802       C  
ATOM   2721  CG  PHE B  51      29.688  53.437   1.777  1.00 18.07           C  
ANISOU 2721  CG  PHE B  51     2654   2152   2060   1063    464    575       C  
ATOM   2722  CD1 PHE B  51      28.948  52.339   1.371  1.00 18.26           C  
ANISOU 2722  CD1 PHE B  51     2570   2287   2080    787    240    671       C  
ATOM   2723  CD2 PHE B  51      29.766  53.724   3.129  1.00 18.20           C  
ANISOU 2723  CD2 PHE B  51     2672   2238   2005    699    563    593       C  
ATOM   2724  CE1 PHE B  51      28.286  51.539   2.299  1.00 18.46           C  
ANISOU 2724  CE1 PHE B  51     2483   2454   2077    648    364    430       C  
ATOM   2725  CE2 PHE B  51      29.113  52.925   4.066  1.00 18.07           C  
ANISOU 2725  CE2 PHE B  51     2534   2317   2013    644    554    461       C  
ATOM   2726  CZ  PHE B  51      28.371  51.835   3.645  1.00 18.10           C  
ANISOU 2726  CZ  PHE B  51     2471   2331   2075    572    585    519       C  
ATOM   2727  N   VAL B  52      28.825  57.048   0.743  1.00 21.84           N  
ANISOU 2727  N   VAL B  52     3137   2585   2577   1439    736    781       N  
ATOM   2728  CA  VAL B  52      27.880  58.005   1.315  1.00 23.05           C  
ANISOU 2728  CA  VAL B  52     3221   2757   2779   1702    548    634       C  
ATOM   2729  C   VAL B  52      26.766  58.286   0.309  1.00 23.59           C  
ANISOU 2729  C   VAL B  52     3152   3043   2768   1496    701    681       C  
ATOM   2730  O   VAL B  52      25.584  58.332   0.658  1.00 24.09           O  
ANISOU 2730  O   VAL B  52     3109   3227   2818   1508    493    796       O  
ATOM   2731  CB  VAL B  52      28.584  59.308   1.713  1.00 23.55           C  
ANISOU 2731  CB  VAL B  52     3215   2761   2973   1713    643    342       C  
ATOM   2732  CG1 VAL B  52      27.561  60.382   2.095  1.00 24.75           C  
ANISOU 2732  CG1 VAL B  52     3256   2889   3260   1697    551    310       C  
ATOM   2733  CG2 VAL B  52      29.553  59.049   2.856  1.00 23.25           C  
ANISOU 2733  CG2 VAL B  52     3328   2593   2914   1646    711    204       C  
ATOM   2734  N   MET B  53      27.154  58.448  -0.950  1.00 23.62           N  
ANISOU 2734  N   MET B  53     3165   3118   2692   1344    631    668       N  
ATOM   2735  CA  MET B  53      26.201  58.666  -2.026  1.00 24.27           C  
ANISOU 2735  CA  MET B  53     3252   3176   2793   1376    479    676       C  
ATOM   2736  C   MET B  53      25.254  57.474  -2.183  1.00 24.91           C  
ANISOU 2736  C   MET B  53     3083   3520   2860   1525    332    727       C  
ATOM   2737  O   MET B  53      24.035  57.640  -2.228  1.00 25.74           O  
ANISOU 2737  O   MET B  53     2997   3776   3007   1567    359    812       O  
ATOM   2738  CB  MET B  53      26.955  58.951  -3.334  1.00 25.26           C  
ANISOU 2738  CB  MET B  53     3554   3165   2877   1334    312    630       C  
ATOM   2739  CG  MET B  53      26.076  59.130  -4.565  1.00 26.91           C  
ANISOU 2739  CG  MET B  53     3800   3394   3031   1574    320    650       C  
ATOM   2740  SD  MET B  53      25.733  57.590  -5.440  1.00 27.30           S  
ANISOU 2740  SD  MET B  53     3934   3380   3058   2005    356    752       S  
ATOM   2741  CE  MET B  53      24.822  58.212  -6.854  1.00 28.71           C  
ANISOU 2741  CE  MET B  53     3905   3765   3238   1923    161    847       C  
ATOM   2742  N   ALA B  54      25.816  56.269  -2.237  1.00 23.78           N  
ANISOU 2742  N   ALA B  54     2988   3326   2721   1683    442    622       N  
ATOM   2743  CA  ALA B  54      25.041  55.069  -2.531  1.00 24.06           C  
ANISOU 2743  CA  ALA B  54     2861   3494   2789   1466    621    701       C  
ATOM   2744  C   ALA B  54      24.015  54.747  -1.446  1.00 25.57           C  
ANISOU 2744  C   ALA B  54     3100   3618   2997   1457    468    644       C  
ATOM   2745  O   ALA B  54      22.928  54.233  -1.734  1.00 25.20           O  
ANISOU 2745  O   ALA B  54     2865   3597   3114   1866    223    506       O  
ATOM   2746  CB  ALA B  54      25.973  53.886  -2.734  1.00 23.78           C  
ANISOU 2746  CB  ALA B  54     2672   3575   2789   1456    730    561       C  
ATOM   2747  N   THR B  55      24.367  55.033  -0.199  1.00 25.46           N  
ANISOU 2747  N   THR B  55     3176   3590   2909   1440    578    898       N  
ATOM   2748  CA  THR B  55      23.470  54.739   0.911  1.00 25.46           C  
ANISOU 2748  CA  THR B  55     3136   3515   3022   1534    557    914       C  
ATOM   2749  C   THR B  55      22.345  55.769   0.982  1.00 26.98           C  
ANISOU 2749  C   THR B  55     3273   3756   3222   1542    463   1086       C  
ATOM   2750  O   THR B  55      21.300  55.514   1.579  1.00 27.40           O  
ANISOU 2750  O   THR B  55     3155   3925   3331   1521    592   1166       O  
ATOM   2751  CB  THR B  55      24.226  54.676   2.259  1.00 23.76           C  
ANISOU 2751  CB  THR B  55     2974   3086   2966   1720    483    769       C  
ATOM   2752  OG1 THR B  55      25.063  55.827   2.418  1.00 24.58           O  
ANISOU 2752  OG1 THR B  55     3161   3240   2937   1359    506    685       O  
ATOM   2753  CG2 THR B  55      25.099  53.420   2.306  1.00 23.84           C  
ANISOU 2753  CG2 THR B  55     3032   3032   2995   1714    380    753       C  
ATOM   2754  N   GLU B  56      22.555  56.921   0.352  1.00 27.73           N  
ANISOU 2754  N   GLU B  56     3535   3753   3249   1651    141   1055       N  
ATOM   2755  CA  GLU B  56      21.504  57.930   0.239  1.00 28.91           C  
ANISOU 2755  CA  GLU B  56     3793   3792   3399   1654    233    817       C  
ATOM   2756  C   GLU B  56      20.536  57.573  -0.885  1.00 28.77           C  
ANISOU 2756  C   GLU B  56     3776   3793   3361   1804    392    755       C  
ATOM   2757  O   GLU B  56      19.324  57.760  -0.763  1.00 28.49           O  
ANISOU 2757  O   GLU B  56     3909   3654   3260   1889    632    622       O  
ATOM   2758  CB  GLU B  56      22.104  59.310  -0.011  1.00 30.50           C  
ANISOU 2758  CB  GLU B  56     4125   3927   3537   1469    237    669       C  
ATOM   2759  CG  GLU B  56      22.792  59.930   1.189  1.00 32.16           C  
ANISOU 2759  CG  GLU B  56     4395   4166   3659   1361    308    597       C  
ATOM   2760  CD  GLU B  56      23.515  61.211   0.831  1.00 33.58           C  
ANISOU 2760  CD  GLU B  56     4584   4352   3823   1381    328    497       C  
ATOM   2761  OE1 GLU B  56      23.393  61.647  -0.333  1.00 34.17           O  
ANISOU 2761  OE1 GLU B  56     4761   4392   3830   1334    460    613       O  
ATOM   2762  OE2 GLU B  56      24.208  61.775   1.702  1.00 33.99           O  
ANISOU 2762  OE2 GLU B  56     4571   4408   3937   1357    346    377       O  
ATOM   2763  N   VAL B  57      21.082  57.058  -1.984  1.00 28.66           N  
ANISOU 2763  N   VAL B  57     3627   3820   3443   1849    417    862       N  
ATOM   2764  CA  VAL B  57      20.266  56.605  -3.104  1.00 30.06           C  
ANISOU 2764  CA  VAL B  57     3629   4055   3736   1560    279    795       C  
ATOM   2765  C   VAL B  57      19.412  55.415  -2.688  1.00 30.08           C  
ANISOU 2765  C   VAL B  57     3577   4069   3785   1645    130    821       C  
ATOM   2766  O   VAL B  57      18.221  55.358  -2.987  1.00 31.29           O  
ANISOU 2766  O   VAL B  57     3740   4285   3866   1340    112    805       O  
ATOM   2767  CB  VAL B  57      21.133  56.218  -4.321  1.00 30.74           C  
ANISOU 2767  CB  VAL B  57     3653   4150   3875   1309    216    831       C  
ATOM   2768  CG1 VAL B  57      20.276  55.607  -5.420  1.00 30.57           C  
ANISOU 2768  CG1 VAL B  57     3503   4220   3891   1315    204    853       C  
ATOM   2769  CG2 VAL B  57      21.886  57.430  -4.840  1.00 31.50           C  
ANISOU 2769  CG2 VAL B  57     3749   4242   3978   1245    157    869       C  
ATOM   2770  N   CYS B  58      20.029  54.469  -1.984  1.00 29.42           N  
ANISOU 2770  N   CYS B  58     3537   3966   3675   1843     65   1004       N  
ATOM   2771  CA  CYS B  58      19.333  53.271  -1.532  1.00 30.22           C  
ANISOU 2771  CA  CYS B  58     3526   4216   3742   1873    182    820       C  
ATOM   2772  C   CYS B  58      19.334  53.154  -0.013  1.00 31.37           C  
ANISOU 2772  C   CYS B  58     3633   4404   3883   1951    126    688       C  
ATOM   2773  O   CYS B  58      20.047  52.320   0.552  1.00 30.82           O  
ANISOU 2773  O   CYS B  58     3501   4397   3811   2062    335    587       O  
ATOM   2774  CB  CYS B  58      19.971  52.030  -2.145  1.00 30.98           C  
ANISOU 2774  CB  CYS B  58     3581   4337   3854   1942     87    787       C  
ATOM   2775  SG  CYS B  58      20.097  52.097  -3.935  1.00 32.58           S  
ANISOU 2775  SG  CYS B  58     3783   4599   3999   1577    236    867       S  
ATOM   2776  N   PRO B  59      18.518  53.980   0.658  1.00 31.98           N  
ANISOU 2776  N   PRO B  59     3688   4447   4016   2103     68    680       N  
ATOM   2777  CA  PRO B  59      18.513  54.002   2.125  1.00 32.51           C  
ANISOU 2777  CA  PRO B  59     3771   4540   4043   2044    -40    654       C  
ATOM   2778  C   PRO B  59      17.955  52.724   2.746  1.00 32.58           C  
ANISOU 2778  C   PRO B  59     3769   4615   3996   1960     -3    759       C  
ATOM   2779  O   PRO B  59      18.138  52.508   3.940  1.00 32.62           O  
ANISOU 2779  O   PRO B  59     3895   4628   3869   2188    112    876       O  
ATOM   2780  CB  PRO B  59      17.617  55.202   2.450  1.00 33.04           C  
ANISOU 2780  CB  PRO B  59     3816   4563   4174   2050   -109    554       C  
ATOM   2781  CG  PRO B  59      16.700  55.306   1.279  1.00 33.54           C  
ANISOU 2781  CG  PRO B  59     3944   4574   4225   2031    -12    580       C  
ATOM   2782  CD  PRO B  59      17.522  54.904   0.086  1.00 32.93           C  
ANISOU 2782  CD  PRO B  59     3852   4524   4135   2068     93    645       C  
ATOM   2783  N   ASP B  60      17.296  51.887   1.952  1.00 33.72           N  
ANISOU 2783  N   ASP B  60     3879   4800   4132   1560    -43    855       N  
ATOM   2784  CA  ASP B  60      16.698  50.665   2.478  1.00 34.46           C  
ANISOU 2784  CA  ASP B  60     3881   4885   4328   1149    -58    729       C  
ATOM   2785  C   ASP B  60      17.544  49.437   2.157  1.00 31.75           C  
ANISOU 2785  C   ASP B  60     3366   4550   4148   1003   -111    887       C  
ATOM   2786  O   ASP B  60      17.261  48.336   2.630  1.00 31.63           O  
ANISOU 2786  O   ASP B  60     3280   4608   4128    728    -81   1064       O  
ATOM   2787  CB  ASP B  60      15.283  50.487   1.928  1.00 37.25           C  
ANISOU 2787  CB  ASP B  60     4271   5288   4594    966   -164    523       C  
ATOM   2788  CG  ASP B  60      14.337  51.571   2.403  1.00 39.71           C  
ANISOU 2788  CG  ASP B  60     4640   5601   4848    859   -180    326       C  
ATOM   2789  OD1 ASP B  60      14.520  52.068   3.534  1.00 40.28           O  
ANISOU 2789  OD1 ASP B  60     4738   5730   4838    806   -147    335       O  
ATOM   2790  OD2 ASP B  60      13.414  51.930   1.642  1.00 41.30           O  
ANISOU 2790  OD2 ASP B  60     4798   5832   5063    852   -183    197       O  
ATOM   2791  N   ALA B  61      18.577  49.631   1.346  1.00 28.65           N  
ANISOU 2791  N   ALA B  61     2838   4157   3892   1108    -13    739       N  
ATOM   2792  CA  ALA B  61      19.494  48.553   1.014  1.00 27.12           C  
ANISOU 2792  CA  ALA B  61     2471   4159   3674    926    -50    744       C  
ATOM   2793  C   ALA B  61      20.414  48.251   2.192  1.00 25.32           C  
ANISOU 2793  C   ALA B  61     2200   3920   3500    950     69    724       C  
ATOM   2794  O   ALA B  61      20.628  49.099   3.057  1.00 25.04           O  
ANISOU 2794  O   ALA B  61     2077   3897   3539   1081    234    653       O  
ATOM   2795  CB  ALA B  61      20.311  48.912  -0.220  1.00 26.57           C  
ANISOU 2795  CB  ALA B  61     2486   4100   3511    871   -130    783       C  
ATOM   2796  N   ASN B  62      20.940  47.032   2.222  1.00 23.47           N  
ANISOU 2796  N   ASN B  62     1901   3741   3275    904    120    636       N  
ATOM   2797  CA  ASN B  62      21.983  46.663   3.173  1.00 21.33           C  
ANISOU 2797  CA  ASN B  62     1838   3284   2982    735    162    587       C  
ATOM   2798  C   ASN B  62      23.273  47.404   2.811  1.00 20.75           C  
ANISOU 2798  C   ASN B  62     2182   2938   2766    616    218    373       C  
ATOM   2799  O   ASN B  62      23.845  47.161   1.751  1.00 20.36           O  
ANISOU 2799  O   ASN B  62     2418   2817   2502    852    385    295       O  
ATOM   2800  CB  ASN B  62      22.189  45.143   3.158  1.00 20.92           C  
ANISOU 2800  CB  ASN B  62     1813   3185   2952    633     33    479       C  
ATOM   2801  CG  ASN B  62      23.187  44.662   4.197  1.00 20.33           C  
ANISOU 2801  CG  ASN B  62     1913   2971   2841    465    133    337       C  
ATOM   2802  OD1 ASN B  62      23.905  45.450   4.813  1.00 19.18           O  
ANISOU 2802  OD1 ASN B  62     1733   2889   2667    266    293    275       O  
ATOM   2803  ND2 ASN B  62      23.247  43.347   4.380  1.00 20.23           N  
ANISOU 2803  ND2 ASN B  62     2068   2807   2810    698    -41    320       N  
ATOM   2804  N   PRO B  63      23.726  48.315   3.685  1.00 19.95           N  
ANISOU 2804  N   PRO B  63     2046   2794   2740    455    357    313       N  
ATOM   2805  CA  PRO B  63      24.921  49.116   3.380  1.00 18.53           C  
ANISOU 2805  CA  PRO B  63     1985   2403   2652    482    343    240       C  
ATOM   2806  C   PRO B  63      26.136  48.242   3.085  1.00 17.77           C  
ANISOU 2806  C   PRO B  63     2047   2180   2526    449    240    353       C  
ATOM   2807  O   PRO B  63      26.922  48.548   2.184  1.00 18.25           O  
ANISOU 2807  O   PRO B  63     2095   2243   2597    444    541    287       O  
ATOM   2808  CB  PRO B  63      25.131  49.935   4.655  1.00 18.69           C  
ANISOU 2808  CB  PRO B  63     1906   2534   2663    588    404    298       C  
ATOM   2809  CG  PRO B  63      23.776  49.997   5.294  1.00 18.91           C  
ANISOU 2809  CG  PRO B  63     1780   2658   2748    641    320    289       C  
ATOM   2810  CD  PRO B  63      23.120  48.689   4.976  1.00 19.87           C  
ANISOU 2810  CD  PRO B  63     2039   2719   2792    585    290    295       C  
ATOM   2811  N   SER B  64      26.267  47.150   3.831  1.00 16.04           N  
ANISOU 2811  N   SER B  64     1880   1951   2262    676    192    425       N  
ATOM   2812  CA  SER B  64      27.373  46.223   3.623  1.00 15.71           C  
ANISOU 2812  CA  SER B  64     1685   1977   2307    767     76    356       C  
ATOM   2813  C   SER B  64      27.326  45.618   2.229  1.00 16.38           C  
ANISOU 2813  C   SER B  64     1641   2237   2343    609     48    304       C  
ATOM   2814  O   SER B  64      28.368  45.411   1.601  1.00 16.43           O  
ANISOU 2814  O   SER B  64     1637   2294   2313    644     96    121       O  
ATOM   2815  CB  SER B  64      27.352  45.112   4.672  1.00 15.61           C  
ANISOU 2815  CB  SER B  64     1735   1837   2360    579     82    328       C  
ATOM   2816  OG  SER B  64      28.574  44.392   4.670  1.00 14.76           O  
ANISOU 2816  OG  SER B  64     1676   1553   2379    384    195    160       O  
ATOM   2817  N   ASP B  65      26.120  45.325   1.744  1.00 17.60           N  
ANISOU 2817  N   ASP B  65     1565   2606   2517    314    -14    224       N  
ATOM   2818  CA  ASP B  65      25.947  44.820   0.380  1.00 17.78           C  
ANISOU 2818  CA  ASP B  65     1649   2510   2596    174    144     10       C  
ATOM   2819  C   ASP B  65      26.324  45.873  -0.657  1.00 18.36           C  
ANISOU 2819  C   ASP B  65     1797   2640   2539    404    -30    -28       C  
ATOM   2820  O   ASP B  65      26.896  45.548  -1.700  1.00 18.86           O  
ANISOU 2820  O   ASP B  65     1788   2887   2490    234    -15   -117       O  
ATOM   2821  CB  ASP B  65      24.509  44.354   0.145  1.00 20.08           C  
ANISOU 2821  CB  ASP B  65     1942   2671   3014   -157     53     85       C  
ATOM   2822  CG  ASP B  65      24.257  42.952   0.667  1.00 23.10           C  
ANISOU 2822  CG  ASP B  65     2450   2928   3399   -428    -24    232       C  
ATOM   2823  OD1 ASP B  65      25.123  42.424   1.392  1.00 23.26           O  
ANISOU 2823  OD1 ASP B  65     2631   2670   3536   -125    214    247       O  
ATOM   2824  OD2 ASP B  65      23.188  42.392   0.362  1.00 25.56           O  
ANISOU 2824  OD2 ASP B  65     2865   3271   3578   -670   -321    182       O  
ATOM   2825  N   LEU B  66      26.009  47.136  -0.381  1.00 18.18           N  
ANISOU 2825  N   LEU B  66     1894   2484   2530    585    -33     94       N  
ATOM   2826  CA  LEU B  66      26.412  48.193  -1.296  1.00 18.55           C  
ANISOU 2826  CA  LEU B  66     2083   2468   2498    719     60    234       C  
ATOM   2827  C   LEU B  66      27.934  48.284  -1.336  1.00 17.58           C  
ANISOU 2827  C   LEU B  66     2108   2191   2379    986    -23    521       C  
ATOM   2828  O   LEU B  66      28.523  48.450  -2.394  1.00 19.24           O  
ANISOU 2828  O   LEU B  66     2425   2554   2333    874    107    652       O  
ATOM   2829  CB  LEU B  66      25.801  49.536  -0.897  1.00 18.61           C  
ANISOU 2829  CB  LEU B  66     1953   2680   2437    958    253     98       C  
ATOM   2830  CG  LEU B  66      24.278  49.632  -1.004  1.00 18.83           C  
ANISOU 2830  CG  LEU B  66     1921   2847   2388   1046     42     54       C  
ATOM   2831  CD1 LEU B  66      23.803  50.970  -0.457  1.00 18.90           C  
ANISOU 2831  CD1 LEU B  66     2108   2590   2484    991    -21      8       C  
ATOM   2832  CD2 LEU B  66      23.809  49.441  -2.447  1.00 20.06           C  
ANISOU 2832  CD2 LEU B  66     2096   3184   2342    765     51    245       C  
ATOM   2833  N   TRP B  67      28.580  48.141  -0.187  1.00 16.09           N  
ANISOU 2833  N   TRP B  67     2065   1827   2222    700     56    256       N  
ATOM   2834  CA  TRP B  67      30.041  48.154  -0.152  1.00 15.70           C  
ANISOU 2834  CA  TRP B  67     2054   1833   2077    450     90     98       C  
ATOM   2835  C   TRP B  67      30.644  46.972  -0.907  1.00 16.19           C  
ANISOU 2835  C   TRP B  67     2224   1979   1949    614    138     97       C  
ATOM   2836  O   TRP B  67      31.549  47.127  -1.727  1.00 17.10           O  
ANISOU 2836  O   TRP B  67     2343   2225   1928    849     33    278       O  
ATOM   2837  CB  TRP B  67      30.529  48.124   1.292  1.00 16.06           C  
ANISOU 2837  CB  TRP B  67     2119   1857   2126     83    330    192       C  
ATOM   2838  CG  TRP B  67      31.991  48.366   1.483  1.00 14.82           C  
ANISOU 2838  CG  TRP B  67     2187   1488   1955    406    477    310       C  
ATOM   2839  CD1 TRP B  67      32.993  47.434   1.491  1.00 15.87           C  
ANISOU 2839  CD1 TRP B  67     2409   1729   1893    225    551    269       C  
ATOM   2840  CD2 TRP B  67      32.617  49.632   1.734  1.00 14.10           C  
ANISOU 2840  CD2 TRP B  67     2206   1302   1848    413    523    248       C  
ATOM   2841  NE1 TRP B  67      34.202  48.046   1.730  1.00 14.39           N  
ANISOU 2841  NE1 TRP B  67     2420   1334   1714     81    437     82       N  
ATOM   2842  CE2 TRP B  67      33.998  49.391   1.879  1.00 14.06           C  
ANISOU 2842  CE2 TRP B  67     2245   1364   1732    289    619    318       C  
ATOM   2843  CE3 TRP B  67      32.140  50.945   1.864  1.00 13.91           C  
ANISOU 2843  CE3 TRP B  67     2028   1386   1871    461    546    434       C  
ATOM   2844  CZ2 TRP B  67      34.908  50.411   2.139  1.00 14.18           C  
ANISOU 2844  CZ2 TRP B  67     2203   1491   1692    306    670    316       C  
ATOM   2845  CZ3 TRP B  67      33.047  51.958   2.121  1.00 14.46           C  
ANISOU 2845  CZ3 TRP B  67     2136   1503   1854    623    509    246       C  
ATOM   2846  CH2 TRP B  67      34.416  51.689   2.257  1.00 14.75           C  
ANISOU 2846  CH2 TRP B  67     2137   1624   1843    343    537    328       C  
ATOM   2847  N   HIS B  68      30.126  45.788  -0.600  1.00 15.21           N  
ANISOU 2847  N   HIS B  68     2055   1857   1866    330   -102    -97       N  
ATOM   2848  CA  HIS B  68      30.713  44.525  -1.022  1.00 15.01           C  
ANISOU 2848  CA  HIS B  68     1984   1897   1823     89     -5     65       C  
ATOM   2849  C   HIS B  68      30.332  44.099  -2.438  1.00 16.12           C  
ANISOU 2849  C   HIS B  68     1942   2217   1965    295     54   -136       C  
ATOM   2850  O   HIS B  68      31.185  43.670  -3.218  1.00 17.05           O  
ANISOU 2850  O   HIS B  68     1974   2622   1881    247     24   -229       O  
ATOM   2851  CB  HIS B  68      30.293  43.443  -0.038  1.00 14.72           C  
ANISOU 2851  CB  HIS B  68     2143   1574   1875     40     76    -22       C  
ATOM   2852  CG  HIS B  68      30.794  42.080  -0.376  1.00 15.17           C  
ANISOU 2852  CG  HIS B  68     2284   1604   1877    302    260   -235       C  
ATOM   2853  ND1 HIS B  68      32.141  41.785  -0.498  1.00 16.08           N  
ANISOU 2853  ND1 HIS B  68     2504   1712   1894    210    120   -103       N  
ATOM   2854  CD2 HIS B  68      30.138  40.919  -0.589  1.00 17.42           C  
ANISOU 2854  CD2 HIS B  68     2414   2043   2161    114    455   -112       C  
ATOM   2855  CE1 HIS B  68      32.281  40.507  -0.782  1.00 17.76           C  
ANISOU 2855  CE1 HIS B  68     2552   2074   2122    -15    102   -150       C  
ATOM   2856  NE2 HIS B  68      31.077  39.954  -0.839  1.00 17.39           N  
ANISOU 2856  NE2 HIS B  68     2529   1920   2157    221    252    -89       N  
ATOM   2857  N   HIS B  69      29.046  44.195  -2.762  1.00 16.34           N  
ANISOU 2857  N   HIS B  69     1757   2458   1994    492    -51     -5       N  
ATOM   2858  CA  HIS B  69      28.559  43.676  -4.034  1.00 17.86           C  
ANISOU 2858  CA  HIS B  69     1937   2577   2272    327    -94     83       C  
ATOM   2859  C   HIS B  69      28.515  44.760  -5.102  1.00 18.15           C  
ANISOU 2859  C   HIS B  69     1988   2618   2292    384     49    185       C  
ATOM   2860  O   HIS B  69      28.483  44.459  -6.297  1.00 18.96           O  
ANISOU 2860  O   HIS B  69     2119   2657   2427    513    275    178       O  
ATOM   2861  CB  HIS B  69      27.175  43.043  -3.856  1.00 18.49           C  
ANISOU 2861  CB  HIS B  69     1961   2609   2456    168   -152    300       C  
ATOM   2862  CG  HIS B  69      27.212  41.684  -3.230  1.00 18.83           C  
ANISOU 2862  CG  HIS B  69     1997   2594   2562    245    -95    193       C  
ATOM   2863  ND1 HIS B  69      28.092  40.704  -3.632  1.00 17.81           N  
ANISOU 2863  ND1 HIS B  69     1894   2356   2518    282   -272    224       N  
ATOM   2864  CD2 HIS B  69      26.476  41.144  -2.231  1.00 20.02           C  
ANISOU 2864  CD2 HIS B  69     2084   2780   2743    249   -161    147       C  
ATOM   2865  CE1 HIS B  69      27.893  39.615  -2.913  1.00 19.41           C  
ANISOU 2865  CE1 HIS B  69     2057   2642   2677    108   -256    -56       C  
ATOM   2866  NE2 HIS B  69      26.918  39.855  -2.053  1.00 20.27           N  
ANISOU 2866  NE2 HIS B  69     2127   2830   2746    113   -250    -57       N  
ATOM   2867  N   VAL B  70      28.520  46.021  -4.676  1.00 18.41           N  
ANISOU 2867  N   VAL B  70     2100   2620   2273    340     74    352       N  
ATOM   2868  CA  VAL B  70      28.483  47.115  -5.642  1.00 17.56           C  
ANISOU 2868  CA  VAL B  70     1813   2618   2240    543    112    427       C  
ATOM   2869  C   VAL B  70      29.842  47.810  -5.761  1.00 16.90           C  
ANISOU 2869  C   VAL B  70     1835   2510   2077    522     53    330       C  
ATOM   2870  O   VAL B  70      30.501  47.676  -6.792  1.00 16.58           O  
ANISOU 2870  O   VAL B  70     1884   2576   1841    203    124    299       O  
ATOM   2871  CB  VAL B  70      27.379  48.141  -5.298  1.00 18.20           C  
ANISOU 2871  CB  VAL B  70     1632   2879   2403    505     91    394       C  
ATOM   2872  CG1 VAL B  70      27.309  49.238  -6.358  1.00 19.29           C  
ANISOU 2872  CG1 VAL B  70     1897   3079   2355    403      7    501       C  
ATOM   2873  CG2 VAL B  70      26.040  47.425  -5.183  1.00 19.45           C  
ANISOU 2873  CG2 VAL B  70     1608   3126   2653    344    161    205       C  
ATOM   2874  N   LEU B  71      30.284  48.518  -4.724  1.00 17.10           N  
ANISOU 2874  N   LEU B  71     1933   2447   2116    556      2    126       N  
ATOM   2875  CA  LEU B  71      31.518  49.303  -4.845  1.00 16.59           C  
ANISOU 2875  CA  LEU B  71     1999   2355   1950    629     97    120       C  
ATOM   2876  C   LEU B  71      32.751  48.414  -5.070  1.00 15.77           C  
ANISOU 2876  C   LEU B  71     1956   2213   1824    593     77    355       C  
ATOM   2877  O   LEU B  71      33.555  48.676  -5.971  1.00 15.79           O  
ANISOU 2877  O   LEU B  71     2106   2259   1634    442    151     94       O  
ATOM   2878  CB  LEU B  71      31.725  50.197  -3.613  1.00 16.27           C  
ANISOU 2878  CB  LEU B  71     2148   2182   1853    844    -53    -15       C  
ATOM   2879  CG  LEU B  71      30.607  51.201  -3.303  1.00 17.57           C  
ANISOU 2879  CG  LEU B  71     2617   2096   1963    818   -192    259       C  
ATOM   2880  CD1 LEU B  71      30.964  52.117  -2.138  1.00 19.02           C  
ANISOU 2880  CD1 LEU B  71     2852   2312   2064    697    -30    199       C  
ATOM   2881  CD2 LEU B  71      30.246  52.034  -4.543  1.00 18.76           C  
ANISOU 2881  CD2 LEU B  71     2744   2149   2234    951    -56    270       C  
ATOM   2882  N   TYR B  72      32.897  47.371  -4.249  1.00 14.46           N  
ANISOU 2882  N   TYR B  72     1903   1853   1739    584     53    381       N  
ATOM   2883  CA  TYR B  72      34.007  46.419  -4.388  1.00 13.98           C  
ANISOU 2883  CA  TYR B  72     1787   1797   1729    585      1    127       C  
ATOM   2884  C   TYR B  72      34.090  45.802  -5.775  1.00 14.78           C  
ANISOU 2884  C   TYR B  72     1997   1898   1722    375   -162     63       C  
ATOM   2885  O   TYR B  72      35.143  45.819  -6.404  1.00 14.55           O  
ANISOU 2885  O   TYR B  72     1833   1821   1876    246    144     82       O  
ATOM   2886  CB  TYR B  72      33.872  45.307  -3.348  1.00 13.54           C  
ANISOU 2886  CB  TYR B  72     1889   1564   1693    470   -120    161       C  
ATOM   2887  CG  TYR B  72      34.805  44.111  -3.482  1.00 13.41           C  
ANISOU 2887  CG  TYR B  72     1848   1505   1742    285   -197    168       C  
ATOM   2888  CD1 TYR B  72      36.187  44.271  -3.574  1.00 13.68           C  
ANISOU 2888  CD1 TYR B  72     2132   1287   1778    127    -18    190       C  
ATOM   2889  CD2 TYR B  72      34.295  42.819  -3.465  1.00 13.74           C  
ANISOU 2889  CD2 TYR B  72     2005   1392   1822     12    -48    138       C  
ATOM   2890  CE1 TYR B  72      37.034  43.163  -3.669  1.00 14.16           C  
ANISOU 2890  CE1 TYR B  72     2296   1129   1957    256    -19    195       C  
ATOM   2891  CE2 TYR B  72      35.125  41.717  -3.549  1.00 14.46           C  
ANISOU 2891  CE2 TYR B  72     2108   1396   1988    -67     58    -85       C  
ATOM   2892  CZ  TYR B  72      36.491  41.896  -3.650  1.00 14.41           C  
ANISOU 2892  CZ  TYR B  72     2078   1274   2123   -135    -29    -47       C  
ATOM   2893  OH  TYR B  72      37.310  40.793  -3.731  1.00 15.53           O  
ANISOU 2893  OH  TYR B  72     2239   1426   2235     23      6    -58       O  
ATOM   2894  N   ARG B  73      32.985  45.235  -6.232  1.00 15.29           N  
ANISOU 2894  N   ARG B  73     2121   1851   1837    451   -223    -74       N  
ATOM   2895  CA  ARG B  73      33.022  44.489  -7.480  1.00 16.37           C  
ANISOU 2895  CA  ARG B  73     2242   2167   1811    348     24   -115       C  
ATOM   2896  C   ARG B  73      33.202  45.419  -8.670  1.00 17.51           C  
ANISOU 2896  C   ARG B  73     2568   2210   1875    570      8    -29       C  
ATOM   2897  O   ARG B  73      33.866  45.051  -9.641  1.00 18.12           O  
ANISOU 2897  O   ARG B  73     2730   2427   1729    395    -13     61       O  
ATOM   2898  CB  ARG B  73      31.766  43.630  -7.617  1.00 16.49           C  
ANISOU 2898  CB  ARG B  73     2144   2185   1937    124   -114     52       C  
ATOM   2899  CG  ARG B  73      31.691  42.617  -6.482  1.00 16.60           C  
ANISOU 2899  CG  ARG B  73     2223   2147   1938    -71     48     30       C  
ATOM   2900  CD  ARG B  73      30.636  41.531  -6.650  1.00 17.65           C  
ANISOU 2900  CD  ARG B  73     2308   2186   2213    -67    -27     23       C  
ATOM   2901  NE  ARG B  73      30.563  40.762  -5.415  1.00 19.30           N  
ANISOU 2901  NE  ARG B  73     2458   2430   2444    135     81     74       N  
ATOM   2902  CZ  ARG B  73      31.402  39.787  -5.080  1.00 18.66           C  
ANISOU 2902  CZ  ARG B  73     2318   2398   2372    -53    239    -88       C  
ATOM   2903  NH1 ARG B  73      32.376  39.416  -5.907  1.00 18.30           N  
ANISOU 2903  NH1 ARG B  73     2128   2452   2375   -361    271   -184       N  
ATOM   2904  NH2 ARG B  73      31.259  39.178  -3.911  1.00 19.36           N  
ANISOU 2904  NH2 ARG B  73     2449   2531   2374    -24    151    286       N  
ATOM   2905  N   ILE B  74      32.648  46.627  -8.587  1.00 17.53           N  
ANISOU 2905  N   ILE B  74     2467   2357   1836    412     26     25       N  
ATOM   2906  CA  ILE B  74      32.861  47.616  -9.643  1.00 17.06           C  
ANISOU 2906  CA  ILE B  74     2369   2315   1797    471      7    133       C  
ATOM   2907  C   ILE B  74      34.315  48.096  -9.633  1.00 17.42           C  
ANISOU 2907  C   ILE B  74     2585   2344   1688    562   -142     52       C  
ATOM   2908  O   ILE B  74      34.938  48.226 -10.685  1.00 18.14           O  
ANISOU 2908  O   ILE B  74     2973   2303   1614    358   -189    172       O  
ATOM   2909  CB  ILE B  74      31.905  48.822  -9.506  1.00 18.24           C  
ANISOU 2909  CB  ILE B  74     2280   2680   1970    394    138    313       C  
ATOM   2910  CG1 ILE B  74      30.478  48.417  -9.886  1.00 19.53           C  
ANISOU 2910  CG1 ILE B  74     2316   2934   2172    768     97    259       C  
ATOM   2911  CG2 ILE B  74      32.381  49.999 -10.363  1.00 18.35           C  
ANISOU 2911  CG2 ILE B  74     2132   2866   1974    260    153    507       C  
ATOM   2912  CD1 ILE B  74      29.441  49.500  -9.627  1.00 20.86           C  
ANISOU 2912  CD1 ILE B  74     2561   3003   2362    732    258    399       C  
ATOM   2913  N   TYR B  75      34.869  48.332  -8.444  1.00 15.90           N  
ANISOU 2913  N   TYR B  75     2326   2214   1502    540   -193    139       N  
ATOM   2914  CA  TYR B  75      36.260  48.783  -8.334  1.00 15.23           C  
ANISOU 2914  CA  TYR B  75     2109   2045   1634    625     12     10       C  
ATOM   2915  C   TYR B  75      37.223  47.758  -8.945  1.00 15.93           C  
ANISOU 2915  C   TYR B  75     2211   2077   1764    438    204    242       C  
ATOM   2916  O   TYR B  75      38.141  48.121  -9.693  1.00 17.44           O  
ANISOU 2916  O   TYR B  75     2365   2490   1770    351    140    340       O  
ATOM   2917  CB  TYR B  75      36.623  49.043  -6.871  1.00 13.94           C  
ANISOU 2917  CB  TYR B  75     1937   1964   1395    580     91     14       C  
ATOM   2918  CG  TYR B  75      37.965  49.712  -6.637  1.00 14.05           C  
ANISOU 2918  CG  TYR B  75     2058   1880   1399    416     63     29       C  
ATOM   2919  CD1 TYR B  75      38.061  51.097  -6.509  1.00 13.86           C  
ANISOU 2919  CD1 TYR B  75     2193   1733   1340    362    -45     -8       C  
ATOM   2920  CD2 TYR B  75      39.135  48.958  -6.503  1.00 13.59           C  
ANISOU 2920  CD2 TYR B  75     2050   1796   1316    325    -35    100       C  
ATOM   2921  CE1 TYR B  75      39.276  51.713  -6.284  1.00 14.02           C  
ANISOU 2921  CE1 TYR B  75     2135   1815   1376    371    219    103       C  
ATOM   2922  CE2 TYR B  75      40.364  49.571  -6.280  1.00 13.46           C  
ANISOU 2922  CE2 TYR B  75     2172   1667   1274    231    -92    231       C  
ATOM   2923  CZ  TYR B  75      40.421  50.956  -6.153  1.00 13.32           C  
ANISOU 2923  CZ  TYR B  75     2057   1630   1373    483    169     34       C  
ATOM   2924  OH  TYR B  75      41.616  51.582  -5.934  1.00 15.22           O  
ANISOU 2924  OH  TYR B  75     2263   1721   1798    550    109    -94       O  
ATOM   2925  N   ILE B  76      37.007  46.481  -8.641  1.00 15.90           N  
ANISOU 2925  N   ILE B  76     2223   2117   1699     96    150    187       N  
ATOM   2926  CA  ILE B  76      37.850  45.413  -9.182  1.00 16.64           C  
ANISOU 2926  CA  ILE B  76     2283   2311   1727    133    276   -164       C  
ATOM   2927  C   ILE B  76      37.785  45.378 -10.702  1.00 18.58           C  
ANISOU 2927  C   ILE B  76     2420   2736   1903     15    162   -209       C  
ATOM   2928  O   ILE B  76      38.799  45.188 -11.381  1.00 19.65           O  
ANISOU 2928  O   ILE B  76     2540   2899   2026   -186    156   -167       O  
ATOM   2929  CB  ILE B  76      37.435  44.032  -8.622  1.00 17.40           C  
ANISOU 2929  CB  ILE B  76     2313   2343   1954    224    119   -262       C  
ATOM   2930  CG1 ILE B  76      37.646  43.981  -7.107  1.00 18.46           C  
ANISOU 2930  CG1 ILE B  76     2236   2581   2195    266     21   -108       C  
ATOM   2931  CG2 ILE B  76      38.218  42.920  -9.304  1.00 17.94           C  
ANISOU 2931  CG2 ILE B  76     2484   2290   2044    241      4   -351       C  
ATOM   2932  CD1 ILE B  76      39.086  44.151  -6.676  1.00 17.20           C  
ANISOU 2932  CD1 ILE B  76     2031   2352   2154    -69    127   -142       C  
ATOM   2933  N   ARG B  77      36.584  45.586 -11.224  1.00 19.13           N  
ANISOU 2933  N   ARG B  77     2385   2992   1894    -33     54   -348       N  
ATOM   2934  CA  ARG B  77      36.343  45.536 -12.658  1.00 20.92           C  
ANISOU 2934  CA  ARG B  77     2503   3419   2026      3    -15   -324       C  
ATOM   2935  C   ARG B  77      36.945  46.739 -13.382  1.00 19.28           C  
ANISOU 2935  C   ARG B  77     2421   3040   1863    276     89   -160       C  
ATOM   2936  O   ARG B  77      37.416  46.617 -14.516  1.00 20.64           O  
ANISOU 2936  O   ARG B  77     2687   3139   2017    291    164   -111       O  
ATOM   2937  CB  ARG B  77      34.835  45.464 -12.921  1.00 26.36           C  
ANISOU 2937  CB  ARG B  77     3223   4144   2650   -269    -57   -390       C  
ATOM   2938  CG  ARG B  77      34.436  45.223 -14.362  1.00 31.34           C  
ANISOU 2938  CG  ARG B  77     3914   4647   3347   -389   -113   -399       C  
ATOM   2939  CD  ARG B  77      32.928  45.059 -14.466  1.00 35.89           C  
ANISOU 2939  CD  ARG B  77     4541   5182   3913   -580   -314   -447       C  
ATOM   2940  NE  ARG B  77      32.403  44.202 -13.403  1.00 40.00           N  
ANISOU 2940  NE  ARG B  77     5177   5600   4423   -617   -441   -582       N  
ATOM   2941  CZ  ARG B  77      31.551  44.606 -12.465  1.00 42.80           C  
ANISOU 2941  CZ  ARG B  77     5750   5703   4808   -710   -647   -800       C  
ATOM   2942  NH1 ARG B  77      31.111  45.858 -12.460  1.00 43.56           N  
ANISOU 2942  NH1 ARG B  77     5905   5604   5041   -836   -684   -883       N  
ATOM   2943  NH2 ARG B  77      31.129  43.754 -11.536  1.00 43.70           N  
ANISOU 2943  NH2 ARG B  77     5972   5786   4846   -729   -849   -808       N  
ATOM   2944  N   GLU B  78      36.929  47.900 -12.731  1.00 18.20           N  
ANISOU 2944  N   GLU B  78     2220   2885   1810    452    122   -136       N  
ATOM   2945  CA  GLU B  78      37.252  49.153 -13.405  1.00 17.99           C  
ANISOU 2945  CA  GLU B  78     2178   2870   1787    480    139    231       C  
ATOM   2946  C   GLU B  78      38.641  49.728 -13.123  1.00 16.71           C  
ANISOU 2946  C   GLU B  78     2114   2700   1535    199    105    307       C  
ATOM   2947  O   GLU B  78      39.124  50.548 -13.899  1.00 18.07           O  
ANISOU 2947  O   GLU B  78     2299   2931   1636    -18    122    434       O  
ATOM   2948  CB  GLU B  78      36.204  50.213 -13.043  1.00 19.86           C  
ANISOU 2948  CB  GLU B  78     2455   2963   2126    537    -33    388       C  
ATOM   2949  CG  GLU B  78      34.793  49.838 -13.441  1.00 22.68           C  
ANISOU 2949  CG  GLU B  78     2766   3480   2371    320   -353    455       C  
ATOM   2950  CD  GLU B  78      34.572  49.952 -14.929  1.00 26.82           C  
ANISOU 2950  CD  GLU B  78     3372   4131   2687     83   -349    443       C  
ATOM   2951  OE1 GLU B  78      35.358  50.666 -15.581  1.00 27.72           O  
ANISOU 2951  OE1 GLU B  78     3684   4172   2676    121   -298    684       O  
ATOM   2952  OE2 GLU B  78      33.621  49.324 -15.439  1.00 29.63           O  
ANISOU 2952  OE2 GLU B  78     3604   4725   2930     20   -399    276       O  
ATOM   2953  N   LYS B  79      39.290  49.319 -12.033  1.00 15.19           N  
ANISOU 2953  N   LYS B  79     1917   2409   1445    322    -19    197       N  
ATOM   2954  CA  LYS B  79      40.557  49.947 -11.653  1.00 15.35           C  
ANISOU 2954  CA  LYS B  79     2042   2423   1365    372    168    218       C  
ATOM   2955  C   LYS B  79      41.667  49.625 -12.656  1.00 17.65           C  
ANISOU 2955  C   LYS B  79     2294   2617   1795    411    197    161       C  
ATOM   2956  O   LYS B  79      41.876  48.465 -13.024  1.00 18.31           O  
ANISOU 2956  O   LYS B  79     2224   2828   1904    720    142     81       O  
ATOM   2957  CB  LYS B  79      40.976  49.509 -10.243  1.00 15.73           C  
ANISOU 2957  CB  LYS B  79     2307   2241   1430    417     51    105       C  
ATOM   2958  CG  LYS B  79      42.179  50.249  -9.687  1.00 14.86           C  
ANISOU 2958  CG  LYS B  79     2447   1924   1275    444    -31     17       C  
ATOM   2959  CD  LYS B  79      41.851  51.712  -9.378  1.00 14.00           C  
ANISOU 2959  CD  LYS B  79     2246   1699   1373    462     82   -106       C  
ATOM   2960  CE  LYS B  79      43.026  52.422  -8.742  1.00 14.54           C  
ANISOU 2960  CE  LYS B  79     2238   1822   1463    370   -215   -268       C  
ATOM   2961  NZ  LYS B  79      42.606  53.738  -8.152  1.00 16.82           N  
ANISOU 2961  NZ  LYS B  79     2282   2436   1673    596   -200   -478       N  
ATOM   2962  N   ILE B  80      42.377  50.669 -13.074  1.00 18.57           N  
ANISOU 2962  N   ILE B  80     2589   2618   1848    329    134    371       N  
ATOM   2963  CA  ILE B  80      43.406  50.570 -14.103  1.00 19.22           C  
ANISOU 2963  CA  ILE B  80     2764   2847   1691    291    203    263       C  
ATOM   2964  C   ILE B  80      44.777  50.957 -13.558  1.00 19.12           C  
ANISOU 2964  C   ILE B  80     2861   2565   1839    232    276    255       C  
ATOM   2965  O   ILE B  80      44.878  51.796 -12.659  1.00 19.56           O  
ANISOU 2965  O   ILE B  80     3071   2556   1805   -116    660      1       O  
ATOM   2966  CB  ILE B  80      43.059  51.485 -15.312  1.00 21.10           C  
ANISOU 2966  CB  ILE B  80     2986   3267   1765    227    114    444       C  
ATOM   2967  CG1 ILE B  80      41.709  51.084 -15.895  1.00 22.08           C  
ANISOU 2967  CG1 ILE B  80     3050   3405   1936    255   -131    350       C  
ATOM   2968  CG2 ILE B  80      44.137  51.442 -16.386  1.00 22.91           C  
ANISOU 2968  CG2 ILE B  80     3268   3355   2081    218    -83    445       C  
ATOM   2969  CD1 ILE B  80      41.612  49.627 -16.239  1.00 24.95           C  
ANISOU 2969  CD1 ILE B  80     3466   3771   2243    168   -174    284       C  
ATOM   2970  N   GLY B  81      45.825  50.327 -14.084  1.00 17.90           N  
ANISOU 2970  N   GLY B  81     2608   2288   1905    312    126    435       N  
ATOM   2971  CA  GLY B  81      47.185  50.797 -13.888  1.00 18.22           C  
ANISOU 2971  CA  GLY B  81     2567   2437   1918    214    -21    505       C  
ATOM   2972  C   GLY B  81      47.803  50.330 -12.586  1.00 17.90           C  
ANISOU 2972  C   GLY B  81     2551   2402   1848    289    -40    467       C  
ATOM   2973  O   GLY B  81      48.878  50.786 -12.192  1.00 20.09           O  
ANISOU 2973  O   GLY B  81     2845   2702   2087    223     50    557       O  
ATOM   2974  N   THR B  82      47.113  49.414 -11.922  1.00 16.43           N  
ANISOU 2974  N   THR B  82     2356   2189   1699     90    160    461       N  
ATOM   2975  CA  THR B  82      47.531  48.922 -10.618  1.00 15.57           C  
ANISOU 2975  CA  THR B  82     2263   2004   1648    -10    340    325       C  
ATOM   2976  C   THR B  82      46.689  47.689 -10.340  1.00 16.34           C  
ANISOU 2976  C   THR B  82     2469   1923   1817    -10    326    433       C  
ATOM   2977  O   THR B  82      45.611  47.550 -10.912  1.00 17.92           O  
ANISOU 2977  O   THR B  82     2645   2068   2097     16    350    672       O  
ATOM   2978  CB  THR B  82      47.356  50.000  -9.513  1.00 16.00           C  
ANISOU 2978  CB  THR B  82     2042   2199   1840     -9    309    381       C  
ATOM   2979  OG1 THR B  82      48.052  49.607  -8.325  1.00 16.50           O  
ANISOU 2979  OG1 THR B  82     2178   2308   1781    172     60    412       O  
ATOM   2980  CG2 THR B  82      45.897  50.231  -9.191  1.00 16.56           C  
ANISOU 2980  CG2 THR B  82     2110   2357   1825     97    408    531       C  
ATOM   2981  N   ASP B  83      47.178  46.784  -9.492  1.00 14.59           N  
ANISOU 2981  N   ASP B  83     2351   1632   1559     29    494    321       N  
ATOM   2982  CA  ASP B  83      46.441  45.554  -9.223  1.00 13.22           C  
ANISOU 2982  CA  ASP B  83     2056   1605   1364     94    249    336       C  
ATOM   2983  C   ASP B  83      45.143  45.858  -8.509  1.00 13.44           C  
ANISOU 2983  C   ASP B  83     1906   1883   1317    -12    101    383       C  
ATOM   2984  O   ASP B  83      45.164  46.413  -7.423  1.00 13.84           O  
ANISOU 2984  O   ASP B  83     1971   1877   1409     29    176     10       O  
ATOM   2985  CB  ASP B  83      47.254  44.593  -8.375  1.00 13.78           C  
ANISOU 2985  CB  ASP B  83     2105   1504   1626     19      6    213       C  
ATOM   2986  CG  ASP B  83      46.513  43.306  -8.130  1.00 15.47           C  
ANISOU 2986  CG  ASP B  83     2209   1809   1861     78    158     10       C  
ATOM   2987  OD1 ASP B  83      46.322  42.549  -9.102  1.00 17.48           O  
ANISOU 2987  OD1 ASP B  83     2442   2093   2107    175    253    -22       O  
ATOM   2988  OD2 ASP B  83      46.111  43.049  -6.977  1.00 15.16           O  
ANISOU 2988  OD2 ASP B  83     2435   1536   1788    265    367   -170       O  
ATOM   2989  N   PRO B  84      44.009  45.487  -9.106  1.00 12.99           N  
ANISOU 2989  N   PRO B  84     1797   1871   1268   -150    119     40       N  
ATOM   2990  CA  PRO B  84      42.731  45.882  -8.507  1.00 14.29           C  
ANISOU 2990  CA  PRO B  84     2133   1912   1386   -116    232    179       C  
ATOM   2991  C   PRO B  84      42.510  45.357  -7.089  1.00 13.54           C  
ANISOU 2991  C   PRO B  84     2210   1455   1479   -136     71    237       C  
ATOM   2992  O   PRO B  84      42.128  46.146  -6.221  1.00 14.01           O  
ANISOU 2992  O   PRO B  84     2377   1445   1503    180     65    109       O  
ATOM   2993  CB  PRO B  84      41.711  45.290  -9.476  1.00 13.47           C  
ANISOU 2993  CB  PRO B  84     2058   1955   1107   -292    137     18       C  
ATOM   2994  CG  PRO B  84      42.424  45.372 -10.807  1.00 13.30           C  
ANISOU 2994  CG  PRO B  84     1917   2000   1137   -276   -234     29       C  
ATOM   2995  CD  PRO B  84      43.834  44.952 -10.472  1.00 12.19           C  
ANISOU 2995  CD  PRO B  84     1524   1989   1121   -365   -356    -67       C  
ATOM   2996  N   SER B  85      42.752  44.073  -6.847  1.00 12.14           N  
ANISOU 2996  N   SER B  85     1847   1312   1454   -123    -39    240       N  
ATOM   2997  CA  SER B  85      42.484  43.518  -5.523  1.00 12.70           C  
ANISOU 2997  CA  SER B  85     1949   1338   1537   -275     82     55       C  
ATOM   2998  C   SER B  85      43.357  44.149  -4.435  1.00 10.95           C  
ANISOU 2998  C   SER B  85     1612   1244   1303   -294    203     53       C  
ATOM   2999  O   SER B  85      42.861  44.485  -3.345  1.00 11.52           O  
ANISOU 2999  O   SER B  85     1756   1364   1255    101    112   -147       O  
ATOM   3000  CB  SER B  85      42.676  41.999  -5.533  1.00 13.45           C  
ANISOU 3000  CB  SER B  85     1897   1257   1955   -447    -39    -84       C  
ATOM   3001  OG  SER B  85      41.638  41.360  -6.258  1.00 13.54           O  
ANISOU 3001  OG  SER B  85     2025   1253   1865   -347    -63     33       O  
ATOM   3002  N   GLN B  86      44.648  44.313  -4.709  1.00 10.52           N  
ANISOU 3002  N   GLN B  86     1633   1117   1248   -125     58     56       N  
ATOM   3003  CA  GLN B  86      45.545  44.870  -3.701  1.00 11.06           C  
ANISOU 3003  CA  GLN B  86     1638   1220   1343    133     39    -66       C  
ATOM   3004  C   GLN B  86      45.353  46.377  -3.551  1.00 10.31           C  
ANISOU 3004  C   GLN B  86     1530   1110   1276    167    -58    160       C  
ATOM   3005  O   GLN B  86      45.514  46.929  -2.455  1.00 10.75           O  
ANISOU 3005  O   GLN B  86     1564   1254   1268    204     35      8       O  
ATOM   3006  CB  GLN B  86      46.999  44.535  -4.020  1.00 10.13           C  
ANISOU 3006  CB  GLN B  86     1530    870   1448    177    321     46       C  
ATOM   3007  CG  GLN B  86      47.278  43.033  -3.932  1.00 10.41           C  
ANISOU 3007  CG  GLN B  86     1563    976   1416    153    181    -31       C  
ATOM   3008  CD  GLN B  86      47.394  42.570  -2.487  1.00 10.51           C  
ANISOU 3008  CD  GLN B  86     1431   1118   1443   -142     78     -7       C  
ATOM   3009  OE1 GLN B  86      46.383  42.403  -1.791  1.00 12.02           O  
ANISOU 3009  OE1 GLN B  86     1814   1353   1401     89    122    156       O  
ATOM   3010  NE2 GLN B  86      48.621  42.368  -2.024  1.00 10.60           N  
ANISOU 3010  NE2 GLN B  86     1397   1115   1515   -174   -161    111       N  
ATOM   3011  N   SER B  87      45.004  47.039  -4.649  1.00 11.19           N  
ANISOU 3011  N   SER B  87     1735    997   1520    449    149    325       N  
ATOM   3012  CA  SER B  87      44.596  48.438  -4.560  1.00 11.46           C  
ANISOU 3012  CA  SER B  87     1822   1055   1477    369    225    296       C  
ATOM   3013  C   SER B  87      43.377  48.577  -3.663  1.00 11.71           C  
ANISOU 3013  C   SER B  87     1982   1025   1444    188    191    -68       C  
ATOM   3014  O   SER B  87      43.324  49.470  -2.806  1.00 12.23           O  
ANISOU 3014  O   SER B  87     2209   1056   1381    156    212    -89       O  
ATOM   3015  CB  SER B  87      44.299  49.002  -5.948  1.00 12.90           C  
ANISOU 3015  CB  SER B  87     2050   1332   1518    555     18    255       C  
ATOM   3016  OG  SER B  87      43.853  50.351  -5.843  1.00 13.76           O  
ANISOU 3016  OG  SER B  87     2229   1452   1547    486     46    119       O  
ATOM   3017  N   TRP B  88      42.405  47.689  -3.846  1.00 12.17           N  
ANISOU 3017  N   TRP B  88     1983   1194   1449    238    250     68       N  
ATOM   3018  CA  TRP B  88      41.196  47.699  -3.045  1.00 11.69           C  
ANISOU 3018  CA  TRP B  88     1882   1140   1420    172     98     70       C  
ATOM   3019  C   TRP B  88      41.535  47.545  -1.569  1.00 12.17           C  
ANISOU 3019  C   TRP B  88     1992   1139   1491    392     97     66       C  
ATOM   3020  O   TRP B  88      40.984  48.241  -0.719  1.00 13.43           O  
ANISOU 3020  O   TRP B  88     2083   1331   1689    434    125   -120       O  
ATOM   3021  CB  TRP B  88      40.243  46.588  -3.487  1.00 11.27           C  
ANISOU 3021  CB  TRP B  88     1690   1190   1402    298     11   -141       C  
ATOM   3022  CG  TRP B  88      39.066  46.432  -2.571  1.00 11.60           C  
ANISOU 3022  CG  TRP B  88     1557   1440   1409    409    211     19       C  
ATOM   3023  CD1 TRP B  88      38.876  45.446  -1.646  1.00 11.93           C  
ANISOU 3023  CD1 TRP B  88     1432   1596   1505    325    171    145       C  
ATOM   3024  CD2 TRP B  88      37.919  47.290  -2.481  1.00 12.12           C  
ANISOU 3024  CD2 TRP B  88     1623   1395   1586    467    140    -52       C  
ATOM   3025  NE1 TRP B  88      37.685  45.635  -0.985  1.00 12.55           N  
ANISOU 3025  NE1 TRP B  88     1371   1609   1787    347    186     88       N  
ATOM   3026  CE2 TRP B  88      37.075  46.759  -1.483  1.00 12.51           C  
ANISOU 3026  CE2 TRP B  88     1610   1476   1668    332    136   -131       C  
ATOM   3027  CE3 TRP B  88      37.515  48.448  -3.151  1.00 12.77           C  
ANISOU 3027  CE3 TRP B  88     1554   1533   1765    479    101      2       C  
ATOM   3028  CZ2 TRP B  88      35.860  47.342  -1.142  1.00 13.82           C  
ANISOU 3028  CZ2 TRP B  88     1904   1576   1771    449     67   -149       C  
ATOM   3029  CZ3 TRP B  88      36.308  49.035  -2.801  1.00 14.06           C  
ANISOU 3029  CZ3 TRP B  88     1801   1660   1881    203     26      0       C  
ATOM   3030  CH2 TRP B  88      35.495  48.481  -1.810  1.00 14.26           C  
ANISOU 3030  CH2 TRP B  88     1872   1719   1827    431    149    -36       C  
ATOM   3031  N   VAL B  89      42.440  46.623  -1.247  1.00 10.95           N  
ANISOU 3031  N   VAL B  89     1625   1195   1339    290    116    194       N  
ATOM   3032  CA  VAL B  89      42.843  46.449   0.149  1.00 10.99           C  
ANISOU 3032  CA  VAL B  89     1654   1271   1251    175     53     -8       C  
ATOM   3033  C   VAL B  89      43.360  47.767   0.736  1.00 11.34           C  
ANISOU 3033  C   VAL B  89     1890   1185   1234    117     26    -16       C  
ATOM   3034  O   VAL B  89      42.948  48.200   1.826  1.00 12.63           O  
ANISOU 3034  O   VAL B  89     2202   1342   1256    263    280     11       O  
ATOM   3035  CB  VAL B  89      43.930  45.356   0.292  1.00 10.85           C  
ANISOU 3035  CB  VAL B  89     1436   1477   1211    111     26   -108       C  
ATOM   3036  CG1 VAL B  89      44.461  45.292   1.708  1.00 11.40           C  
ANISOU 3036  CG1 VAL B  89     1461   1510   1360     29    -46   -138       C  
ATOM   3037  CG2 VAL B  89      43.357  44.017  -0.097  1.00 10.72           C  
ANISOU 3037  CG2 VAL B  89     1443   1474   1154   -228     32   -249       C  
ATOM   3038  N   ARG B  90      44.249  48.417  -0.005  1.00 11.88           N  
ANISOU 3038  N   ARG B  90     1926   1073   1516    -89    -58    -37       N  
ATOM   3039  CA  ARG B  90      44.943  49.598   0.500  1.00 11.99           C  
ANISOU 3039  CA  ARG B  90     1849   1066   1640    -26    215    -14       C  
ATOM   3040  C   ARG B  90      44.017  50.803   0.604  1.00 12.62           C  
ANISOU 3040  C   ARG B  90     2226    987   1581    161    451   -118       C  
ATOM   3041  O   ARG B  90      44.205  51.653   1.471  1.00 13.67           O  
ANISOU 3041  O   ARG B  90     2535   1045   1612    253    489   -172       O  
ATOM   3042  CB  ARG B  90      46.137  49.932  -0.402  1.00 11.25           C  
ANISOU 3042  CB  ARG B  90     1562   1127   1583     50    226     17       C  
ATOM   3043  CG  ARG B  90      46.843  51.230  -0.045  1.00 12.95           C  
ANISOU 3043  CG  ARG B  90     1849   1261   1813    -52     91    216       C  
ATOM   3044  CD  ARG B  90      47.474  51.198   1.344  1.00 14.63           C  
ANISOU 3044  CD  ARG B  90     2224   1221   2115   -110   -305     83       C  
ATOM   3045  NE  ARG B  90      48.174  52.459   1.581  1.00 18.43           N  
ANISOU 3045  NE  ARG B  90     2779   1784   2440   -380   -256   -156       N  
ATOM   3046  CZ  ARG B  90      47.904  53.306   2.568  1.00 20.58           C  
ANISOU 3046  CZ  ARG B  90     3130   2086   2603   -387     58   -185       C  
ATOM   3047  NH1 ARG B  90      46.971  53.025   3.468  1.00 20.94           N  
ANISOU 3047  NH1 ARG B  90     3303   2053   2602   -410     30   -120       N  
ATOM   3048  NH2 ARG B  90      48.594  54.434   2.661  1.00 21.11           N  
ANISOU 3048  NH2 ARG B  90     3204   2096   2722   -374    140    -94       N  
ATOM   3049  N   THR B  91      43.015  50.872  -0.263  1.00 12.99           N  
ANISOU 3049  N   THR B  91     2142   1127   1667    393    337    -98       N  
ATOM   3050  CA  THR B  91      42.203  52.080  -0.338  1.00 12.77           C  
ANISOU 3050  CA  THR B  91     2060   1188   1604    468    359    -38       C  
ATOM   3051  C   THR B  91      40.878  51.946   0.386  1.00 12.81           C  
ANISOU 3051  C   THR B  91     2083   1145   1639    356    438    -12       C  
ATOM   3052  O   THR B  91      40.347  52.941   0.884  1.00 14.17           O  
ANISOU 3052  O   THR B  91     2344   1349   1690    664    641   -133       O  
ATOM   3053  CB  THR B  91      41.938  52.488  -1.803  1.00 13.91           C  
ANISOU 3053  CB  THR B  91     2180   1465   1641    393    325   -129       C  
ATOM   3054  OG1 THR B  91      41.278  51.419  -2.498  1.00 14.94           O  
ANISOU 3054  OG1 THR B  91     2334   1545   1798    442     81    -46       O  
ATOM   3055  CG2 THR B  91      43.253  52.811  -2.489  1.00 13.69           C  
ANISOU 3055  CG2 THR B  91     2121   1386   1697    214    355     25       C  
ATOM   3056  N   SER B  92      40.345  50.734   0.481  1.00 13.24           N  
ANISOU 3056  N   SER B  92     2032   1251   1746    294    223    180       N  
ATOM   3057  CA  SER B  92      38.995  50.577   1.018  1.00 14.67           C  
ANISOU 3057  CA  SER B  92     2304   1435   1834    362    157     59       C  
ATOM   3058  C   SER B  92      38.945  50.644   2.538  1.00 14.82           C  
ANISOU 3058  C   SER B  92     2609   1384   1637    420     69    267       C  
ATOM   3059  O   SER B  92      37.940  51.060   3.093  1.00 14.79           O  
ANISOU 3059  O   SER B  92     2726   1372   1523    596    204     28       O  
ATOM   3060  CB  SER B  92      38.364  49.269   0.533  1.00 14.53           C  
ANISOU 3060  CB  SER B  92     2185   1343   1993    345     47     43       C  
ATOM   3061  OG  SER B  92      39.037  48.136   1.054  1.00 13.92           O  
ANISOU 3061  OG  SER B  92     2127   1313   1849    152    172    124       O  
ATOM   3062  N   GLY B  93      40.012  50.229   3.215  1.00 15.31           N  
ANISOU 3062  N   GLY B  93     2829   1409   1581    407   -181    278       N  
ATOM   3063  CA  GLY B  93      40.030  50.316   4.667  1.00 16.29           C  
ANISOU 3063  CA  GLY B  93     3006   1403   1779    561     24    183       C  
ATOM   3064  C   GLY B  93      39.933  51.772   5.089  1.00 16.01           C  
ANISOU 3064  C   GLY B  93     2817   1497   1770    551    351    270       C  
ATOM   3065  O   GLY B  93      39.095  52.158   5.911  1.00 16.47           O  
ANISOU 3065  O   GLY B  93     2651   1891   1717    418    415    284       O  
ATOM   3066  N   GLU B  94      40.793  52.591   4.501  1.00 16.15           N  
ANISOU 3066  N   GLU B  94     2983   1414   1741    522    344    318       N  
ATOM   3067  CA  GLU B  94      40.792  54.021   4.796  1.00 15.77           C  
ANISOU 3067  CA  GLU B  94     2807   1417   1767    358    405    170       C  
ATOM   3068  C   GLU B  94      39.524  54.700   4.273  1.00 14.78           C  
ANISOU 3068  C   GLU B  94     2523   1490   1604    204    293    120       C  
ATOM   3069  O   GLU B  94      39.065  55.689   4.847  1.00 13.98           O  
ANISOU 3069  O   GLU B  94     2530   1344   1437    492    301    -30       O  
ATOM   3070  CB  GLU B  94      42.040  54.695   4.216  1.00 16.39           C  
ANISOU 3070  CB  GLU B  94     2916   1603   1710    415    511    -23       C  
ATOM   3071  CG  GLU B  94      43.301  54.409   5.009  1.00 18.20           C  
ANISOU 3071  CG  GLU B  94     3094   1817   2002    277    370     46       C  
ATOM   3072  CD  GLU B  94      44.511  55.203   4.548  1.00 19.51           C  
ANISOU 3072  CD  GLU B  94     3402   1871   2139    -13    522     27       C  
ATOM   3073  OE1 GLU B  94      44.471  55.809   3.447  1.00 19.17           O  
ANISOU 3073  OE1 GLU B  94     3371   1759   2155    -34    779   -214       O  
ATOM   3074  OE2 GLU B  94      45.510  55.223   5.297  1.00 22.05           O  
ANISOU 3074  OE2 GLU B  94     3839   2161   2378   -114    418    117       O  
ATOM   3075  N   ALA B  95      38.963  54.168   3.191  1.00 13.05           N  
ANISOU 3075  N   ALA B  95     2075   1433   1452    338    283    265       N  
ATOM   3076  CA  ALA B  95      37.700  54.665   2.646  1.00 13.61           C  
ANISOU 3076  CA  ALA B  95     2226   1461   1485    443    549    315       C  
ATOM   3077  C   ALA B  95      36.563  54.585   3.659  1.00 13.76           C  
ANISOU 3077  C   ALA B  95     2342   1364   1524    587    508    336       C  
ATOM   3078  O   ALA B  95      35.715  55.470   3.727  1.00 14.71           O  
ANISOU 3078  O   ALA B  95     2432   1417   1739    783    379    -42       O  
ATOM   3079  CB  ALA B  95      37.333  53.901   1.389  1.00 14.49           C  
ANISOU 3079  CB  ALA B  95     2356   1408   1742    350    330    142       C  
ATOM   3080  N   PHE B  96      36.537  53.503   4.425  1.00 13.78           N  
ANISOU 3080  N   PHE B  96     2500   1297   1438    190    423    509       N  
ATOM   3081  CA  PHE B  96      35.490  53.323   5.418  1.00 13.99           C  
ANISOU 3081  CA  PHE B  96     2532   1342   1442    155    557    469       C  
ATOM   3082  C   PHE B  96      35.623  54.404   6.483  1.00 14.93           C  
ANISOU 3082  C   PHE B  96     2511   1527   1636    391    522    245       C  
ATOM   3083  O   PHE B  96      34.625  54.962   6.930  1.00 15.75           O  
ANISOU 3083  O   PHE B  96     2639   1537   1806    894    537    386       O  
ATOM   3084  CB  PHE B  96      35.565  51.913   6.029  1.00 14.35           C  
ANISOU 3084  CB  PHE B  96     2488   1389   1573    343    490    401       C  
ATOM   3085  CG  PHE B  96      34.509  51.637   7.059  1.00 15.19           C  
ANISOU 3085  CG  PHE B  96     2513   1509   1749    360    530    328       C  
ATOM   3086  CD1 PHE B  96      33.210  52.066   6.877  1.00 16.25           C  
ANISOU 3086  CD1 PHE B  96     2658   1622   1896    323    763    117       C  
ATOM   3087  CD2 PHE B  96      34.818  50.924   8.208  1.00 14.78           C  
ANISOU 3087  CD2 PHE B  96     2345   1621   1652    118    712    218       C  
ATOM   3088  CE1 PHE B  96      32.240  51.808   7.829  1.00 17.64           C  
ANISOU 3088  CE1 PHE B  96     2978   1884   1841    210    512    136       C  
ATOM   3089  CE2 PHE B  96      33.848  50.665   9.166  1.00 15.77           C  
ANISOU 3089  CE2 PHE B  96     2452   1782   1759     19    512     96       C  
ATOM   3090  CZ  PHE B  96      32.566  51.103   8.977  1.00 17.33           C  
ANISOU 3090  CZ  PHE B  96     2677   2000   1907     89    500    -28       C  
ATOM   3091  N   GLU B  97      36.855  54.703   6.877  1.00 14.70           N  
ANISOU 3091  N   GLU B  97     2457   1361   1769    328    251    176       N  
ATOM   3092  CA  GLU B  97      37.108  55.810   7.800  1.00 15.98           C  
ANISOU 3092  CA  GLU B  97     2799   1388   1885    558    309     80       C  
ATOM   3093  C   GLU B  97      36.609  57.125   7.210  1.00 16.22           C  
ANISOU 3093  C   GLU B  97     2871   1447   1845    421    530    166       C  
ATOM   3094  O   GLU B  97      35.994  57.937   7.914  1.00 16.42           O  
ANISOU 3094  O   GLU B  97     2920   1443   1875    429    514     17       O  
ATOM   3095  CB  GLU B  97      38.596  55.939   8.122  1.00 18.72           C  
ANISOU 3095  CB  GLU B  97     3151   1782   2182    731    143     48       C  
ATOM   3096  CG  GLU B  97      39.234  54.733   8.796  1.00 22.37           C  
ANISOU 3096  CG  GLU B  97     3664   2376   2460    941      7    -46       C  
ATOM   3097  CD  GLU B  97      40.724  54.926   8.959  1.00 28.47           C  
ANISOU 3097  CD  GLU B  97     4532   3183   3102    957   -248   -216       C  
ATOM   3098  OE1 GLU B  97      41.127  55.842   9.703  1.00 31.80           O  
ANISOU 3098  OE1 GLU B  97     4933   3619   3531    912   -253   -161       O  
ATOM   3099  OE2 GLU B  97      41.498  54.189   8.318  1.00 32.24           O  
ANISOU 3099  OE2 GLU B  97     4971   3692   3587    790   -352    -72       O  
ATOM   3100  N   VAL B  98      36.893  57.345   5.927  1.00 16.00           N  
ANISOU 3100  N   VAL B  98     2904   1248   1928    315    834    319       N  
ATOM   3101  CA  VAL B  98      36.480  58.581   5.257  1.00 15.22           C  
ANISOU 3101  CA  VAL B  98     2741   1159   1884    467   1084    268       C  
ATOM   3102  C   VAL B  98      34.967  58.729   5.288  1.00 15.27           C  
ANISOU 3102  C   VAL B  98     2786   1193   1825    489    784     87       C  
ATOM   3103  O   VAL B  98      34.441  59.807   5.596  1.00 17.24           O  
ANISOU 3103  O   VAL B  98     2982   1486   2082    676    336    -81       O  
ATOM   3104  CB  VAL B  98      36.980  58.610   3.785  1.00 17.90           C  
ANISOU 3104  CB  VAL B  98     2921   1579   2302    581   1002    560       C  
ATOM   3105  CG1 VAL B  98      36.272  59.705   2.977  1.00 19.41           C  
ANISOU 3105  CG1 VAL B  98     3126   1747   2503    592    902    600       C  
ATOM   3106  CG2 VAL B  98      38.480  58.809   3.754  1.00 19.08           C  
ANISOU 3106  CG2 VAL B  98     2860   1751   2637    633    856    404       C  
ATOM   3107  N   ALA B  99      34.268  57.636   5.002  1.00 15.15           N  
ANISOU 3107  N   ALA B  99     2454   1544   1758    487    855    124       N  
ATOM   3108  CA  ALA B  99      32.817  57.629   4.973  1.00 15.83           C  
ANISOU 3108  CA  ALA B  99     2592   1623   1799    293    679    224       C  
ATOM   3109  C   ALA B  99      32.236  57.917   6.357  1.00 15.63           C  
ANISOU 3109  C   ALA B  99     2744   1526   1670    460    633    283       C  
ATOM   3110  O   ALA B  99      31.265  58.647   6.485  1.00 16.59           O  
ANISOU 3110  O   ALA B  99     2958   1533   1813    480    550     53       O  
ATOM   3111  CB  ALA B  99      32.310  56.291   4.442  1.00 16.70           C  
ANISOU 3111  CB  ALA B  99     2592   1732   2023    377    400    -41       C  
ATOM   3112  N   LEU B 100      32.822  57.314   7.385  1.00 15.27           N  
ANISOU 3112  N   LEU B 100     2723   1490   1588    577    672    274       N  
ATOM   3113  CA  LEU B 100      32.368  57.531   8.756  1.00 14.63           C  
ANISOU 3113  CA  LEU B 100     2513   1339   1706    472    466    257       C  
ATOM   3114  C   LEU B 100      32.464  59.002   9.130  1.00 15.32           C  
ANISOU 3114  C   LEU B 100     2468   1579   1773    376    512    285       C  
ATOM   3115  O   LEU B 100      31.526  59.579   9.689  1.00 15.24           O  
ANISOU 3115  O   LEU B 100     2157   1702   1930    379    556    301       O  
ATOM   3116  CB  LEU B 100      33.186  56.687   9.741  1.00 15.07           C  
ANISOU 3116  CB  LEU B 100     2470   1544   1711    671    342    233       C  
ATOM   3117  CG  LEU B 100      32.917  55.185   9.827  1.00 16.41           C  
ANISOU 3117  CG  LEU B 100     2373   1879   1985    516    282    372       C  
ATOM   3118  CD1 LEU B 100      33.964  54.515  10.718  1.00 16.90           C  
ANISOU 3118  CD1 LEU B 100     2431   1990   2000    705      8    601       C  
ATOM   3119  CD2 LEU B 100      31.514  54.901  10.351  1.00 16.39           C  
ANISOU 3119  CD2 LEU B 100     2164   1833   2231    309    595    374       C  
ATOM   3120  N   VAL B 101      33.610  59.596   8.834  1.00 15.64           N  
ANISOU 3120  N   VAL B 101     2626   1596   1721    401    409    238       N  
ATOM   3121  CA  VAL B 101      33.838  60.997   9.166  1.00 15.94           C  
ANISOU 3121  CA  VAL B 101     2798   1316   1941    423    590    353       C  
ATOM   3122  C   VAL B 101      32.882  61.897   8.367  1.00 15.73           C  
ANISOU 3122  C   VAL B 101     2889   1259   1828    749    705    127       C  
ATOM   3123  O   VAL B 101      32.240  62.786   8.935  1.00 16.71           O  
ANISOU 3123  O   VAL B 101     2846   1635   1867    634    696    184       O  
ATOM   3124  CB  VAL B 101      35.312  61.398   8.915  1.00 17.35           C  
ANISOU 3124  CB  VAL B 101     3024   1378   2192    568    653    345       C  
ATOM   3125  CG1 VAL B 101      35.490  62.912   9.033  1.00 18.00           C  
ANISOU 3125  CG1 VAL B 101     3113   1361   2365    478    464    304       C  
ATOM   3126  CG2 VAL B 101      36.230  60.686   9.885  1.00 18.47           C  
ANISOU 3126  CG2 VAL B 101     3182   1599   2236    671    835    179       C  
ATOM   3127  N   GLU B 102      32.760  61.648   7.066  1.00 16.30           N  
ANISOU 3127  N   GLU B 102     3011   1491   1693    690    653    233       N  
ATOM   3128  CA  GLU B 102      31.873  62.437   6.212  1.00 17.18           C  
ANISOU 3128  CA  GLU B 102     3144   1622   1760   1058    598    110       C  
ATOM   3129  C   GLU B 102      30.416  62.318   6.626  1.00 17.56           C  
ANISOU 3129  C   GLU B 102     3101   1740   1832   1000    466    148       C  
ATOM   3130  O   GLU B 102      29.713  63.317   6.715  1.00 18.40           O  
ANISOU 3130  O   GLU B 102     3079   1807   2107   1212    572    147       O  
ATOM   3131  CB  GLU B 102      32.012  62.025   4.741  1.00 19.72           C  
ANISOU 3131  CB  GLU B 102     3645   2019   1828   1052    402    226       C  
ATOM   3132  CG  GLU B 102      30.996  62.717   3.824  1.00 22.20           C  
ANISOU 3132  CG  GLU B 102     4013   2261   2161   1079    222    406       C  
ATOM   3133  CD  GLU B 102      31.140  62.338   2.360  1.00 24.54           C  
ANISOU 3133  CD  GLU B 102     4308   2443   2574   1152    182    288       C  
ATOM   3134  OE1 GLU B 102      32.174  61.741   1.988  1.00 25.50           O  
ANISOU 3134  OE1 GLU B 102     4511   2429   2751   1060    308    279       O  
ATOM   3135  OE2 GLU B 102      30.209  62.640   1.578  1.00 25.88           O  
ANISOU 3135  OE2 GLU B 102     4549   2689   2595   1073    258     79       O  
ATOM   3136  N   ARG B 103      29.964  61.098   6.888  1.00 17.19           N  
ANISOU 3136  N   ARG B 103     2913   1841   1779    906    319    109       N  
ATOM   3137  CA  ARG B 103      28.564  60.851   7.190  1.00 16.84           C  
ANISOU 3137  CA  ARG B 103     2592   1974   1833   1065    341     46       C  
ATOM   3138  C   ARG B 103      28.162  61.414   8.548  1.00 17.40           C  
ANISOU 3138  C   ARG B 103     2645   2199   1766   1014    463    140       C  
ATOM   3139  O   ARG B 103      27.076  61.969   8.688  1.00 18.64           O  
ANISOU 3139  O   ARG B 103     2952   2262   1868   1023    739    158       O  
ATOM   3140  CB  ARG B 103      28.280  59.343   7.136  1.00 18.79           C  
ANISOU 3140  CB  ARG B 103     2740   2175   2223    683    317   -200       C  
ATOM   3141  CG  ARG B 103      27.035  58.860   7.868  1.00 21.82           C  
ANISOU 3141  CG  ARG B 103     3027   2653   2611    610    341   -262       C  
ATOM   3142  CD  ARG B 103      25.741  59.376   7.254  1.00 23.98           C  
ANISOU 3142  CD  ARG B 103     3308   2970   2831    376    444    -19       C  
ATOM   3143  NE  ARG B 103      24.581  58.796   7.931  1.00 25.67           N  
ANISOU 3143  NE  ARG B 103     3424   3191   3141    585    737    -98       N  
ATOM   3144  CZ  ARG B 103      24.023  59.290   9.034  1.00 24.70           C  
ANISOU 3144  CZ  ARG B 103     3283   2974   3129    662    856   -138       C  
ATOM   3145  NH1 ARG B 103      22.979  58.682   9.576  1.00 23.79           N  
ANISOU 3145  NH1 ARG B 103     3037   2878   3125    901   1057    204       N  
ATOM   3146  NH2 ARG B 103      24.499  60.397   9.590  1.00 24.59           N  
ANISOU 3146  NH2 ARG B 103     3168   2992   3185    313    680   -246       N  
ATOM   3147  N   TYR B 104      29.031  61.276   9.544  1.00 15.40           N  
ANISOU 3147  N   TYR B 104     2403   1894   1553    881    425    119       N  
ATOM   3148  CA  TYR B 104      28.624  61.617  10.897  1.00 14.44           C  
ANISOU 3148  CA  TYR B 104     2256   1582   1648    888    251    388       C  
ATOM   3149  C   TYR B 104      29.032  62.994  11.395  1.00 14.99           C  
ANISOU 3149  C   TYR B 104     2239   1688   1770    605    192    363       C  
ATOM   3150  O   TYR B 104      28.348  63.541  12.250  1.00 14.53           O  
ANISOU 3150  O   TYR B 104     2083   1692   1747    633    263     87       O  
ATOM   3151  CB  TYR B 104      29.144  60.551  11.867  1.00 15.07           C  
ANISOU 3151  CB  TYR B 104     2387   1442   1896    798    421    356       C  
ATOM   3152  CG  TYR B 104      28.396  59.249  11.719  1.00 15.90           C  
ANISOU 3152  CG  TYR B 104     2316   1591   2134    427    511    317       C  
ATOM   3153  CD1 TYR B 104      27.036  59.190  11.948  1.00 17.05           C  
ANISOU 3153  CD1 TYR B 104     2414   1674   2389    544    427    136       C  
ATOM   3154  CD2 TYR B 104      29.044  58.081  11.321  1.00 16.11           C  
ANISOU 3154  CD2 TYR B 104     2485   1552   2084    500    554    127       C  
ATOM   3155  CE1 TYR B 104      26.332  58.010  11.813  1.00 16.84           C  
ANISOU 3155  CE1 TYR B 104     2520   1494   2385    244    534    146       C  
ATOM   3156  CE2 TYR B 104      28.350  56.893  11.181  1.00 16.55           C  
ANISOU 3156  CE2 TYR B 104     2298   1747   2244    494    454    175       C  
ATOM   3157  CZ  TYR B 104      26.997  56.858  11.428  1.00 17.19           C  
ANISOU 3157  CZ  TYR B 104     2485   1696   2349    496    408     69       C  
ATOM   3158  OH  TYR B 104      26.293  55.687  11.291  1.00 17.87           O  
ANISOU 3158  OH  TYR B 104     2428   1909   2454    548    307    165       O  
ATOM   3159  N   ASN B 105      30.119  63.578  10.892  1.00 13.60           N  
ANISOU 3159  N   ASN B 105     2120   1284   1763    580    250    354       N  
ATOM   3160  CA  ASN B 105      30.545  64.858  11.464  1.00 14.17           C  
ANISOU 3160  CA  ASN B 105     2121   1404   1859    769    504    166       C  
ATOM   3161  C   ASN B 105      29.516  66.003  11.387  1.00 13.91           C  
ANISOU 3161  C   ASN B 105     2158   1385   1742    840    433    325       C  
ATOM   3162  O   ASN B 105      29.392  66.738  12.359  1.00 15.16           O  
ANISOU 3162  O   ASN B 105     2685   1410   1665    632    566     56       O  
ATOM   3163  CB  ASN B 105      31.877  65.299  10.852  1.00 14.48           C  
ANISOU 3163  CB  ASN B 105     2068   1544   1889    544    470    249       C  
ATOM   3164  CG  ASN B 105      33.064  64.867  11.699  1.00 14.66           C  
ANISOU 3164  CG  ASN B 105     2057   1669   1844    504    424    314       C  
ATOM   3165  OD1 ASN B 105      32.887  64.218  12.732  1.00 15.53           O  
ANISOU 3165  OD1 ASN B 105     1874   2088   1940    772    503    409       O  
ATOM   3166  ND2 ASN B 105      34.267  65.243  11.288  1.00 15.74           N  
ANISOU 3166  ND2 ASN B 105     2107   1959   1914    499    521    -45       N  
ATOM   3167  N   PRO B 106      28.762  66.145  10.276  1.00 14.27           N  
ANISOU 3167  N   PRO B 106     2047   1690   1686   1062    184    253       N  
ATOM   3168  CA  PRO B 106      27.793  67.255  10.281  1.00 14.84           C  
ANISOU 3168  CA  PRO B 106     2024   1826   1787   1121    212    330       C  
ATOM   3169  C   PRO B 106      26.659  67.109  11.304  1.00 15.99           C  
ANISOU 3169  C   PRO B 106     2156   1852   2069    733    346    377       C  
ATOM   3170  O   PRO B 106      26.165  68.116  11.816  1.00 16.82           O  
ANISOU 3170  O   PRO B 106     2274   1925   2192    988    413    420       O  
ATOM   3171  CB  PRO B 106      27.232  67.238   8.851  1.00 15.27           C  
ANISOU 3171  CB  PRO B 106     2019   2110   1672    916    164    174       C  
ATOM   3172  CG  PRO B 106      28.280  66.558   8.027  1.00 16.73           C  
ANISOU 3172  CG  PRO B 106     2216   2288   1852    855     66    347       C  
ATOM   3173  CD  PRO B 106      28.858  65.514   8.948  1.00 15.98           C  
ANISOU 3173  CD  PRO B 106     2317   2098   1657    941    179    310       C  
ATOM   3174  N  AVAL B 107      26.261  65.873  11.593  0.54 15.11           N  
ANISOU 3174  N  AVAL B 107     1925   1735   2081    722    418    419       N  
ATOM   3175  N  BVAL B 107      26.258  65.880  11.616  0.46 15.80           N  
ANISOU 3175  N  BVAL B 107     2066   1876   2061    692    301    434       N  
ATOM   3176  CA AVAL B 107      25.234  65.605  12.595  0.54 16.22           C  
ANISOU 3176  CA AVAL B 107     1996   1999   2168    454    488    320       C  
ATOM   3177  CA BVAL B 107      25.212  65.691  12.614  0.46 17.09           C  
ANISOU 3177  CA BVAL B 107     2183   2191   2118    444    275    391       C  
ATOM   3178  C  AVAL B 107      25.803  65.777  14.007  0.54 16.64           C  
ANISOU 3178  C  AVAL B 107     1998   2214   2108    574    524    107       C  
ATOM   3179  C  BVAL B 107      25.790  65.756  14.029  0.46 17.08           C  
ANISOU 3179  C  BVAL B 107     2093   2337   2061    570    424    148       C  
ATOM   3180  O  AVAL B 107      25.113  66.233  14.925  0.54 18.04           O  
ANISOU 3180  O  AVAL B 107     2237   2340   2279    870    549    -95       O  
ATOM   3181  O  BVAL B 107      25.084  66.114  14.977  0.46 18.39           O  
ANISOU 3181  O  BVAL B 107     2283   2529   2174    824    491     16       O  
ATOM   3182  CB AVAL B 107      24.651  64.175  12.437  0.54 17.79           C  
ANISOU 3182  CB AVAL B 107     2153   2221   2385    319    329    296       C  
ATOM   3183  CB BVAL B 107      24.454  64.348  12.423  0.46 18.70           C  
ANISOU 3183  CB BVAL B 107     2386   2449   2270    260    -24    430       C  
ATOM   3184  CG1AVAL B 107      23.707  63.843  13.586  0.54 18.06           C  
ANISOU 3184  CG1AVAL B 107     2104   2298   2459    178    436    156       C  
ATOM   3185  CG1BVAL B 107      23.835  64.275  11.040  0.46 19.39           C  
ANISOU 3185  CG1BVAL B 107     2396   2619   2351    149   -179    344       C  
ATOM   3186  CG2AVAL B 107      23.938  64.033  11.099  0.54 18.48           C  
ANISOU 3186  CG2AVAL B 107     2298   2251   2474    114    278    299       C  
ATOM   3187  CG2BVAL B 107      25.368  63.180  12.625  0.46 18.86           C  
ANISOU 3187  CG2BVAL B 107     2423   2407   2335    127     -6    475       C  
ATOM   3188  N   LEU B 108      27.073  65.430  14.176  1.00 15.92           N  
ANISOU 3188  N   LEU B 108     1965   2174   1909    535    419    -23       N  
ATOM   3189  CA  LEU B 108      27.714  65.482  15.488  1.00 15.05           C  
ANISOU 3189  CA  LEU B 108     2086   1880   1752    544    224     99       C  
ATOM   3190  C   LEU B 108      28.198  66.894  15.830  1.00 16.27           C  
ANISOU 3190  C   LEU B 108     2583   1850   1748    476    200    247       C  
ATOM   3191  O   LEU B 108      28.410  67.215  17.005  1.00 16.38           O  
ANISOU 3191  O   LEU B 108     2572   1891   1762    604    398    -39       O  
ATOM   3192  CB  LEU B 108      28.877  64.486  15.560  1.00 14.04           C  
ANISOU 3192  CB  LEU B 108     1866   1721   1749    589    328    204       C  
ATOM   3193  CG  LEU B 108      28.519  62.999  15.528  1.00 15.18           C  
ANISOU 3193  CG  LEU B 108     2010   1855   1901    437    529    131       C  
ATOM   3194  CD1 LEU B 108      29.777  62.150  15.377  1.00 15.89           C  
ANISOU 3194  CD1 LEU B 108     2058   1932   2049    471    331    188       C  
ATOM   3195  CD2 LEU B 108      27.752  62.608  16.783  1.00 15.95           C  
ANISOU 3195  CD2 LEU B 108     2224   1890   1947    407    463     64       C  
ATOM   3196  N   ALA B 109      28.354  67.741  14.811  1.00 17.72           N  
ANISOU 3196  N   ALA B 109     2912   1774   2045    438    388    255       N  
ATOM   3197  CA  ALA B 109      28.855  69.102  14.994  1.00 18.62           C  
ANISOU 3197  CA  ALA B 109     3084   1939   2050    770    584    224       C  
ATOM   3198  C   ALA B 109      27.981  69.942  15.918  1.00 20.87           C  
ANISOU 3198  C   ALA B 109     3367   2259   2303    961    592    412       C  
ATOM   3199  O   ALA B 109      28.496  70.749  16.683  1.00 21.87           O  
ANISOU 3199  O   ALA B 109     3685   2147   2478    677    770    281       O  
ATOM   3200  CB  ALA B 109      28.986  69.795  13.641  1.00 20.49           C  
ANISOU 3200  CB  ALA B 109     3472   2218   2094    635    568    250       C  
ATOM   3201  N   ARG B 110      26.672  69.723  15.847  1.00 22.88           N  
ANISOU 3201  N   ARG B 110     3383   2856   2456   1193    511    657       N  
ATOM   3202  CA  ARG B 110      25.702  70.406  16.703  1.00 25.92           C  
ANISOU 3202  CA  ARG B 110     3716   3309   2824   1461    289    620       C  
ATOM   3203  C   ARG B 110      25.947  70.137  18.185  1.00 24.19           C  
ANISOU 3203  C   ARG B 110     3537   3143   2513   1440    657    252       C  
ATOM   3204  O   ARG B 110      25.495  70.887  19.050  1.00 26.84           O  
ANISOU 3204  O   ARG B 110     3913   3478   2806   1640    681    320       O  
ATOM   3205  CB  ARG B 110      24.279  69.970  16.345  1.00 30.58           C  
ANISOU 3205  CB  ARG B 110     4197   3992   3428   1426     13    641       C  
ATOM   3206  CG  ARG B 110      24.009  69.826  14.862  1.00 35.86           C  
ANISOU 3206  CG  ARG B 110     4818   4682   4126   1358   -210    549       C  
ATOM   3207  CD  ARG B 110      22.517  69.837  14.589  1.00 39.53           C  
ANISOU 3207  CD  ARG B 110     5196   5313   4510   1504   -265    383       C  
ATOM   3208  NE  ARG B 110      22.113  71.026  13.848  1.00 43.20           N  
ANISOU 3208  NE  ARG B 110     5632   6031   4749   1483   -147    204       N  
ATOM   3209  CZ  ARG B 110      20.851  71.336  13.575  1.00 45.55           C  
ANISOU 3209  CZ  ARG B 110     5937   6441   4928   1274     13    144       C  
ATOM   3210  NH1 ARG B 110      19.871  70.540  13.984  1.00 46.47           N  
ANISOU 3210  NH1 ARG B 110     6050   6620   4985   1022     26    228       N  
ATOM   3211  NH2 ARG B 110      20.568  72.438  12.894  1.00 45.87           N  
ANISOU 3211  NH2 ARG B 110     6043   6389   4995   1322    154    107       N  
ATOM   3212  N   HIS B 111      26.656  69.053  18.467  1.00 19.99           N  
ANISOU 3212  N   HIS B 111     2825   2550   2221   1290    626    238       N  
ATOM   3213  CA  HIS B 111      26.883  68.613  19.838  1.00 17.93           C  
ANISOU 3213  CA  HIS B 111     2440   2140   2234    990    471    154       C  
ATOM   3214  C   HIS B 111      28.318  68.856  20.269  1.00 17.82           C  
ANISOU 3214  C   HIS B 111     2306   2311   2154    822    673     -3       C  
ATOM   3215  O   HIS B 111      28.720  68.480  21.373  1.00 19.94           O  
ANISOU 3215  O   HIS B 111     2387   2942   2249    912    506    323       O  
ATOM   3216  CB  HIS B 111      26.538  67.128  19.969  1.00 17.23           C  
ANISOU 3216  CB  HIS B 111     2308   1886   2353    987    471     27       C  
ATOM   3217  CG  HIS B 111      25.124  66.811  19.616  1.00 17.61           C  
ANISOU 3217  CG  HIS B 111     2416   1932   2342    683    438    106       C  
ATOM   3218  ND1 HIS B 111      24.097  66.877  20.539  1.00 18.14           N  
ANISOU 3218  ND1 HIS B 111     2534   2049   2312    332    628    216       N  
ATOM   3219  CD2 HIS B 111      24.550  66.462  18.445  1.00 17.85           C  
ANISOU 3219  CD2 HIS B 111     2326   2067   2388    353    570     86       C  
ATOM   3220  CE1 HIS B 111      22.960  66.573  19.947  1.00 19.10           C  
ANISOU 3220  CE1 HIS B 111     2601   2287   2370    190    638     87       C  
ATOM   3221  NE2 HIS B 111      23.207  66.313  18.672  1.00 18.77           N  
ANISOU 3221  NE2 HIS B 111     2397   2293   2443    124    718    130       N  
ATOM   3222  N   GLY B 112      29.093  69.476  19.388  1.00 17.08           N  
ANISOU 3222  N   GLY B 112     2412   1824   2252    660    667   -121       N  
ATOM   3223  CA  GLY B 112      30.491  69.731  19.668  1.00 16.50           C  
ANISOU 3223  CA  GLY B 112     2355   1562   2352    479    652   -174       C  
ATOM   3224  C   GLY B 112      31.330  68.470  19.589  1.00 16.09           C  
ANISOU 3224  C   GLY B 112     2263   1536   2313    339    618    -59       C  
ATOM   3225  O   GLY B 112      32.445  68.427  20.092  1.00 17.14           O  
ANISOU 3225  O   GLY B 112     2430   1640   2444    326    295    -84       O  
ATOM   3226  N   ILE B 113      30.793  67.436  18.958  1.00 14.16           N  
ANISOU 3226  N   ILE B 113     2043   1266   2072    344    754    192       N  
ATOM   3227  CA  ILE B 113      31.535  66.190  18.830  1.00 13.21           C  
ANISOU 3227  CA  ILE B 113     1858   1307   1855    420    701    176       C  
ATOM   3228  C   ILE B 113      32.150  66.110  17.433  1.00 13.66           C  
ANISOU 3228  C   ILE B 113     1778   1546   1865    561    621    -64       C  
ATOM   3229  O   ILE B 113      31.518  66.479  16.452  1.00 14.75           O  
ANISOU 3229  O   ILE B 113     1904   1747   1951    605    561     82       O  
ATOM   3230  CB  ILE B 113      30.630  64.970  19.088  1.00 12.85           C  
ANISOU 3230  CB  ILE B 113     1926   1261   1695    260    632    372       C  
ATOM   3231  CG1 ILE B 113      30.074  64.998  20.519  1.00 13.90           C  
ANISOU 3231  CG1 ILE B 113     2028   1496   1757    129    812    471       C  
ATOM   3232  CG2 ILE B 113      31.390  63.673  18.847  1.00 13.52           C  
ANISOU 3232  CG2 ILE B 113     2031   1317   1787    392    259    317       C  
ATOM   3233  CD1 ILE B 113      28.899  64.065  20.704  1.00 14.86           C  
ANISOU 3233  CD1 ILE B 113     2044   1684   1918    199    917    500       C  
ATOM   3234  N   ARG B 114      33.387  65.627  17.349  1.00 12.99           N  
ANISOU 3234  N   ARG B 114     1632   1602   1701    496    762   -243       N  
ATOM   3235  CA  ARG B 114      34.081  65.601  16.062  1.00 14.55           C  
ANISOU 3235  CA  ARG B 114     1877   1584   2066    511    650    118       C  
ATOM   3236  C   ARG B 114      34.857  64.303  15.892  1.00 14.04           C  
ANISOU 3236  C   ARG B 114     1986   1484   1865    651    442     26       C  
ATOM   3237  O   ARG B 114      35.563  63.878  16.807  1.00 15.53           O  
ANISOU 3237  O   ARG B 114     2280   1694   1928    651    195     69       O  
ATOM   3238  CB  ARG B 114      35.019  66.801  15.951  1.00 16.40           C  
ANISOU 3238  CB  ARG B 114     2069   1766   2396    112    928    358       C  
ATOM   3239  CG  ARG B 114      35.780  66.883  14.642  1.00 18.95           C  
ANISOU 3239  CG  ARG B 114     2477   1914   2808   -107    830    572       C  
ATOM   3240  CD  ARG B 114      36.695  68.100  14.643  1.00 21.20           C  
ANISOU 3240  CD  ARG B 114     2606   2208   3240    -26    636    367       C  
ATOM   3241  NE  ARG B 114      37.821  67.937  15.558  1.00 22.91           N  
ANISOU 3241  NE  ARG B 114     2983   2319   3404    -10    693    338       N  
ATOM   3242  CZ  ARG B 114      38.645  68.921  15.907  1.00 23.40           C  
ANISOU 3242  CZ  ARG B 114     3419   1974   3496     22    726    411       C  
ATOM   3243  NH1 ARG B 114      38.453  70.150  15.429  1.00 24.15           N  
ANISOU 3243  NH1 ARG B 114     3684   1717   3775   -104    763    289       N  
ATOM   3244  NH2 ARG B 114      39.654  68.684  16.734  1.00 23.21           N  
ANISOU 3244  NH2 ARG B 114     3336   2114   3371    422    812    482       N  
ATOM   3245  N   LEU B 115      34.709  63.678  14.726  1.00 13.62           N  
ANISOU 3245  N   LEU B 115     1915   1410   1849    563    486    -18       N  
ATOM   3246  CA  LEU B 115      35.504  62.509  14.372  1.00 13.27           C  
ANISOU 3246  CA  LEU B 115     1701   1554   1785    437    206    -83       C  
ATOM   3247  C   LEU B 115      36.664  62.934  13.485  1.00 14.01           C  
ANISOU 3247  C   LEU B 115     1574   1955   1795    549    329    -90       C  
ATOM   3248  O   LEU B 115      36.511  63.807  12.635  1.00 15.08           O  
ANISOU 3248  O   LEU B 115     1767   2077   1886    488    244     38       O  
ATOM   3249  CB  LEU B 115      34.661  61.465  13.640  1.00 14.73           C  
ANISOU 3249  CB  LEU B 115     1874   1784   1939    414     87    -51       C  
ATOM   3250  CG  LEU B 115      33.354  60.983  14.264  1.00 14.81           C  
ANISOU 3250  CG  LEU B 115     1929   1899   1797    349     83    174       C  
ATOM   3251  CD1 LEU B 115      32.713  59.922  13.381  1.00 16.23           C  
ANISOU 3251  CD1 LEU B 115     2010   2221   1934    392     42     43       C  
ATOM   3252  CD2 LEU B 115      33.597  60.433  15.667  1.00 15.70           C  
ANISOU 3252  CD2 LEU B 115     2219   2047   1698    535     12    277       C  
ATOM   3253  N   THR B 116      37.818  62.305  13.671  1.00 14.62           N  
ANISOU 3253  N   THR B 116     1721   1926   1907    573    363     18       N  
ATOM   3254  CA  THR B 116      38.964  62.562  12.805  1.00 15.57           C  
ANISOU 3254  CA  THR B 116     2074   1840   2001    654    464   -112       C  
ATOM   3255  C   THR B 116      39.643  61.256  12.420  1.00 15.64           C  
ANISOU 3255  C   THR B 116     2465   1765   1712    764    459    -29       C  
ATOM   3256  O   THR B 116      40.061  60.491  13.289  1.00 16.01           O  
ANISOU 3256  O   THR B 116     2431   2012   1642    684    325    131       O  
ATOM   3257  CB  THR B 116      39.997  63.472  13.477  1.00 17.16           C  
ANISOU 3257  CB  THR B 116     2082   2074   2364    217    689   -361       C  
ATOM   3258  OG1 THR B 116      39.370  64.695  13.886  1.00 19.24           O  
ANISOU 3258  OG1 THR B 116     2296   2339   2674     31    579   -441       O  
ATOM   3259  CG2 THR B 116      41.121  63.801  12.504  1.00 17.91           C  
ANISOU 3259  CG2 THR B 116     2005   2260   2540    129   1035   -398       C  
ATOM   3260  N   ALA B 117      39.763  60.997  11.122  1.00 16.32           N  
ANISOU 3260  N   ALA B 117     2768   1554   1878    888    553   -119       N  
ATOM   3261  CA  ALA B 117      40.446  59.788  10.678  1.00 17.01           C  
ANISOU 3261  CA  ALA B 117     2906   1744   1814    930    685    163       C  
ATOM   3262  C   ALA B 117      41.934  59.962  10.923  1.00 18.70           C  
ANISOU 3262  C   ALA B 117     2729   2199   2176    995    720    475       C  
ATOM   3263  O   ALA B 117      42.528  60.975  10.552  1.00 20.35           O  
ANISOU 3263  O   ALA B 117     2706   2500   2527    892    837    599       O  
ATOM   3264  CB  ALA B 117      40.162  59.493   9.204  1.00 17.85           C  
ANISOU 3264  CB  ALA B 117     3102   2041   1638    892    688      9       C  
ATOM   3265  N   LEU B 118      42.523  58.975  11.585  1.00 20.74           N  
ANISOU 3265  N   LEU B 118     2812   2720   2349   1123    714    231       N  
ATOM   3266  CA  LEU B 118      43.929  59.010  11.934  1.00 22.38           C  
ANISOU 3266  CA  LEU B 118     2880   3206   2415    919   1191    160       C  
ATOM   3267  C   LEU B 118      44.719  58.360  10.818  1.00 27.04           C  
ANISOU 3267  C   LEU B 118     3376   3881   3019   1087   1123     46       C  
ATOM   3268  O   LEU B 118      45.189  57.230  10.948  1.00 28.67           O  
ANISOU 3268  O   LEU B 118     3623   4056   3213   1312   1043    106       O  
ATOM   3269  CB  LEU B 118      44.179  58.293  13.259  1.00 20.90           C  
ANISOU 3269  CB  LEU B 118     2728   3043   2171    726    979     29       C  
ATOM   3270  CG  LEU B 118      43.402  58.838  14.460  1.00 20.41           C  
ANISOU 3270  CG  LEU B 118     2768   2828   2160    735    869    -46       C  
ATOM   3271  CD1 LEU B 118      43.684  57.976  15.682  1.00 21.20           C  
ANISOU 3271  CD1 LEU B 118     2985   2885   2185    580    659     -1       C  
ATOM   3272  CD2 LEU B 118      43.731  60.307  14.710  1.00 20.09           C  
ANISOU 3272  CD2 LEU B 118     2498   2925   2211    615    925   -157       C  
ATOM   3273  N   PHE B 119      44.834  59.076   9.707  1.00 28.34           N  
ANISOU 3273  N   PHE B 119     3392   4228   3150    516   1398    -14       N  
ATOM   3274  CA  PHE B 119      45.642  58.614   8.593  1.00 32.27           C  
ANISOU 3274  CA  PHE B 119     3928   4816   3516    211   1372   -165       C  
ATOM   3275  C   PHE B 119      47.101  58.789   8.987  1.00 36.29           C  
ANISOU 3275  C   PHE B 119     4428   5177   4182   -280   1412   -371       C  
ATOM   3276  O   PHE B 119      47.387  59.329  10.059  1.00 37.50           O  
ANISOU 3276  O   PHE B 119     4699   5141   4408   -200   1403   -474       O  
ATOM   3277  CB  PHE B 119      45.293  59.380   7.316  1.00 31.59           C  
ANISOU 3277  CB  PHE B 119     3941   4924   3136    224   1301   -219       C  
ATOM   3278  CG  PHE B 119      43.891  59.127   6.832  1.00 29.90           C  
ANISOU 3278  CG  PHE B 119     3844   4742   2774    219   1197   -295       C  
ATOM   3279  CD1 PHE B 119      43.139  60.143   6.258  1.00 29.26           C  
ANISOU 3279  CD1 PHE B 119     3937   4500   2679    209   1093    -94       C  
ATOM   3280  CD2 PHE B 119      43.321  57.868   6.961  1.00 29.20           C  
ANISOU 3280  CD2 PHE B 119     3832   4776   2485    262   1141   -544       C  
ATOM   3281  CE1 PHE B 119      41.844  59.902   5.820  1.00 29.05           C  
ANISOU 3281  CE1 PHE B 119     3993   4449   2594    302   1182   -120       C  
ATOM   3282  CE2 PHE B 119      42.031  57.624   6.529  1.00 29.06           C  
ANISOU 3282  CE2 PHE B 119     3897   4695   2452    191   1289   -618       C  
ATOM   3283  CZ  PHE B 119      41.293  58.642   5.954  1.00 28.99           C  
ANISOU 3283  CZ  PHE B 119     3864   4611   2541    215   1305   -398       C  
ATOM   3284  N   LYS B 120      48.009  58.307   8.139  1.00 39.37           N  
ANISOU 3284  N   LYS B 120     4740   5584   4634   -679   1375   -463       N  
ATOM   3285  CA  LYS B 120      49.446  58.383   8.401  1.00 42.12           C  
ANISOU 3285  CA  LYS B 120     4969   6047   4988   -856   1336   -515       C  
ATOM   3286  C   LYS B 120      49.850  59.755   8.940  1.00 43.58           C  
ANISOU 3286  C   LYS B 120     5077   6303   5179   -916   1380   -465       C  
ATOM   3287  O   LYS B 120      49.600  60.777   8.295  1.00 44.44           O  
ANISOU 3287  O   LYS B 120     5200   6459   5226   -887   1412   -533       O  
ATOM   3288  CB  LYS B 120      50.231  58.074   7.125  1.00 42.73           C  
ANISOU 3288  CB  LYS B 120     5108   6112   5014   -834   1300   -577       C  
ATOM   3289  N   GLY B 121      50.441  59.777  10.133  1.00 44.15           N  
ANISOU 3289  N   GLY B 121     5106   6402   5265   -898   1324   -252       N  
ATOM   3290  CA  GLY B 121      50.911  61.018  10.726  1.00 44.08           C  
ANISOU 3290  CA  GLY B 121     5082   6319   5348   -953   1209    -31       C  
ATOM   3291  C   GLY B 121      50.037  61.608  11.824  1.00 43.67           C  
ANISOU 3291  C   GLY B 121     4968   6228   5397   -942   1160    378       C  
ATOM   3292  O   GLY B 121      50.468  62.500  12.561  1.00 43.01           O  
ANISOU 3292  O   GLY B 121     4812   6167   5362  -1228   1287    595       O  
ATOM   3293  N   GLN B 122      48.806  61.124  11.947  1.00 43.49           N  
ANISOU 3293  N   GLN B 122     4998   6114   5411   -510    902    512       N  
ATOM   3294  CA  GLN B 122      47.876  61.687  12.925  1.00 42.34           C  
ANISOU 3294  CA  GLN B 122     4970   5800   5318    -69    816    655       C  
ATOM   3295  C   GLN B 122      47.738  60.807  14.163  1.00 39.55           C  
ANISOU 3295  C   GLN B 122     4617   5333   5077     74    982    763       C  
ATOM   3296  O   GLN B 122      47.201  61.236  15.185  1.00 38.57           O  
ANISOU 3296  O   GLN B 122     4571   5076   5008    142   1089    852       O  
ATOM   3297  CB  GLN B 122      46.498  61.900  12.288  1.00 43.87           C  
ANISOU 3297  CB  GLN B 122     5255   5895   5519     91    517    679       C  
ATOM   3298  CG  GLN B 122      46.378  63.163  11.446  1.00 45.33           C  
ANISOU 3298  CG  GLN B 122     5539   5973   5713    214    252    766       C  
ATOM   3299  CD  GLN B 122      45.224  63.105  10.464  1.00 47.12           C  
ANISOU 3299  CD  GLN B 122     5870   6111   5922    298    104    788       C  
ATOM   3300  OE1 GLN B 122      45.219  62.283   9.548  1.00 47.35           O  
ANISOU 3300  OE1 GLN B 122     5955   6141   5896    300    123    769       O  
ATOM   3301  NE2 GLN B 122      44.241  63.979  10.649  1.00 48.03           N  
ANISOU 3301  NE2 GLN B 122     6029   6177   6042    370     21    822       N  
ATOM   3302  N   LYS B 123      48.237  59.581  14.064  1.00 36.79           N  
ANISOU 3302  N   LYS B 123     4194   4982   4802    251   1131    818       N  
ATOM   3303  CA  LYS B 123      47.915  58.541  15.029  1.00 35.16           C  
ANISOU 3303  CA  LYS B 123     3941   4716   4703    527   1005    713       C  
ATOM   3304  C   LYS B 123      48.705  58.677  16.325  1.00 32.31           C  
ANISOU 3304  C   LYS B 123     3479   4381   4416    676    920    721       C  
ATOM   3305  O   LYS B 123      48.142  58.565  17.412  1.00 30.88           O  
ANISOU 3305  O   LYS B 123     3339   4173   4221    641   1180    741       O  
ATOM   3306  CB  LYS B 123      48.159  57.168  14.400  1.00 36.01           C  
ANISOU 3306  CB  LYS B 123     4074   4753   4856    684   1071    568       C  
ATOM   3307  CG  LYS B 123      47.408  56.024  15.064  1.00 37.14           C  
ANISOU 3307  CG  LYS B 123     4315   4795   5002    642   1047    472       C  
ATOM   3308  CD  LYS B 123      47.382  54.783  14.173  1.00 37.77           C  
ANISOU 3308  CD  LYS B 123     4443   4866   5044    373   1066    447       C  
ATOM   3309  CE  LYS B 123      46.057  54.646  13.434  1.00 37.64           C  
ANISOU 3309  CE  LYS B 123     4429   4858   5016     59   1181    475       C  
ATOM   3310  NZ  LYS B 123      45.971  53.393  12.633  1.00 37.36           N  
ANISOU 3310  NZ  LYS B 123     4466   4775   4954   -143   1210    581       N  
ATOM   3311  N   GLY B 124      50.003  58.936  16.200  1.00 30.73           N  
ANISOU 3311  N   GLY B 124     3147   4232   4298    778    648    629       N  
ATOM   3312  CA  GLY B 124      50.896  58.999  17.344  1.00 30.00           C  
ANISOU 3312  CA  GLY B 124     3085   4094   4219    659    539    416       C  
ATOM   3313  C   GLY B 124      50.466  59.978  18.418  1.00 28.29           C  
ANISOU 3313  C   GLY B 124     2816   3817   4116    559    532    317       C  
ATOM   3314  O   GLY B 124      50.413  59.630  19.604  1.00 27.78           O  
ANISOU 3314  O   GLY B 124     2693   3850   4011    586    534    214       O  
ATOM   3315  N   LEU B 125      50.155  61.205  18.010  1.00 27.32           N  
ANISOU 3315  N   LEU B 125     2739   3507   4136    311    533    196       N  
ATOM   3316  CA  LEU B 125      49.703  62.213  18.956  1.00 26.58           C  
ANISOU 3316  CA  LEU B 125     2766   3314   4018     45    519    163       C  
ATOM   3317  C   LEU B 125      48.347  61.827  19.543  1.00 24.37           C  
ANISOU 3317  C   LEU B 125     2631   2922   3706   -208    366    163       C  
ATOM   3318  O   LEU B 125      48.114  61.995  20.738  1.00 24.87           O  
ANISOU 3318  O   LEU B 125     2774   2996   3680   -391    311    191       O  
ATOM   3319  CB  LEU B 125      49.623  63.583  18.285  1.00 28.52           C  
ANISOU 3319  CB  LEU B 125     3161   3423   4252   -208    562    143       C  
ATOM   3320  CG  LEU B 125      49.116  64.738  19.149  1.00 30.63           C  
ANISOU 3320  CG  LEU B 125     3501   3648   4488   -306    496    -28       C  
ATOM   3321  CD1 LEU B 125      49.998  64.927  20.377  1.00 31.34           C  
ANISOU 3321  CD1 LEU B 125     3534   3755   4618   -395    371   -212       C  
ATOM   3322  CD2 LEU B 125      49.040  66.020  18.334  1.00 31.07           C  
ANISOU 3322  CD2 LEU B 125     3597   3681   4525   -312    513     -9       C  
ATOM   3323  N   ALA B 126      47.459  61.310  18.701  1.00 22.19           N  
ANISOU 3323  N   ALA B 126     2455   2586   3391   -233    439    147       N  
ATOM   3324  CA  ALA B 126      46.139  60.885  19.162  1.00 20.76           C  
ANISOU 3324  CA  ALA B 126     2452   2371   3063    -71    233     -3       C  
ATOM   3325  C   ALA B 126      46.233  59.781  20.211  1.00 19.88           C  
ANISOU 3325  C   ALA B 126     2451   2241   2862    474    368   -126       C  
ATOM   3326  O   ALA B 126      45.583  59.858  21.254  1.00 19.68           O  
ANISOU 3326  O   ALA B 126     2333   2341   2804    303    347    -42       O  
ATOM   3327  CB  ALA B 126      45.291  60.422  17.989  1.00 20.74           C  
ANISOU 3327  CB  ALA B 126     2613   2306   2962   -210    239    -80       C  
ATOM   3328  N   LEU B 127      47.031  58.751  19.937  1.00 19.68           N  
ANISOU 3328  N   LEU B 127     2402   2238   2838    639    274    -12       N  
ATOM   3329  CA  LEU B 127      47.161  57.643  20.873  1.00 19.47           C  
ANISOU 3329  CA  LEU B 127     2331   2207   2858    712     77     97       C  
ATOM   3330  C   LEU B 127      47.767  58.118  22.190  1.00 19.61           C  
ANISOU 3330  C   LEU B 127     2163   2386   2904    272     34     50       C  
ATOM   3331  O   LEU B 127      47.420  57.613  23.258  1.00 19.74           O  
ANISOU 3331  O   LEU B 127     2035   2510   2955    147     76     23       O  
ATOM   3332  CB  LEU B 127      48.006  56.507  20.272  1.00 19.76           C  
ANISOU 3332  CB  LEU B 127     2429   2154   2926    943    -28    166       C  
ATOM   3333  CG  LEU B 127      47.473  55.858  18.991  1.00 22.21           C  
ANISOU 3333  CG  LEU B 127     2798   2520   3120    824      8    -68       C  
ATOM   3334  CD1 LEU B 127      48.455  54.831  18.433  1.00 22.93           C  
ANISOU 3334  CD1 LEU B 127     2937   2645   3130   1038   -105    -97       C  
ATOM   3335  CD2 LEU B 127      46.112  55.230  19.214  1.00 22.82           C  
ANISOU 3335  CD2 LEU B 127     2785   2665   3222    605    141   -197       C  
ATOM   3336  N   THR B 128      48.659  59.101  22.117  1.00 20.50           N  
ANISOU 3336  N   THR B 128     2307   2484   2999     82    -20    -69       N  
ATOM   3337  CA  THR B 128      49.247  59.679  23.321  1.00 21.71           C  
ANISOU 3337  CA  THR B 128     2409   2709   3130    -88    220   -291       C  
ATOM   3338  C   THR B 128      48.171  60.349  24.168  1.00 21.72           C  
ANISOU 3338  C   THR B 128     2463   2757   3032     91     10   -312       C  
ATOM   3339  O   THR B 128      48.111  60.157  25.380  1.00 23.38           O  
ANISOU 3339  O   THR B 128     2596   3089   3196   -280   -152    -83       O  
ATOM   3340  CB  THR B 128      50.346  60.705  22.982  1.00 23.64           C  
ANISOU 3340  CB  THR B 128     2713   2957   3312    -97    566   -305       C  
ATOM   3341  OG1 THR B 128      51.459  60.028  22.384  1.00 24.82           O  
ANISOU 3341  OG1 THR B 128     2722   3222   3486   -136    551   -232       O  
ATOM   3342  CG2 THR B 128      50.821  61.415  24.240  1.00 24.69           C  
ANISOU 3342  CG2 THR B 128     2834   3173   3373    -62    595   -498       C  
ATOM   3343  N   ARG B 129      47.320  61.134  23.518  1.00 20.93           N  
ANISOU 3343  N   ARG B 129     2478   2562   2912    199    -67   -463       N  
ATOM   3344  CA  ARG B 129      46.219  61.798  24.209  1.00 21.19           C  
ANISOU 3344  CA  ARG B 129     2624   2573   2855    175    -10   -371       C  
ATOM   3345  C   ARG B 129      45.190  60.788  24.722  1.00 20.85           C  
ANISOU 3345  C   ARG B 129     2737   2450   2736    174    -77   -422       C  
ATOM   3346  O   ARG B 129      44.489  61.051  25.697  1.00 22.38           O  
ANISOU 3346  O   ARG B 129     3016   2643   2843     53    -11   -369       O  
ATOM   3347  CB  ARG B 129      45.556  62.820  23.282  1.00 21.65           C  
ANISOU 3347  CB  ARG B 129     2643   2598   2984    -60    122   -135       C  
ATOM   3348  CG  ARG B 129      46.485  63.957  22.856  1.00 21.45           C  
ANISOU 3348  CG  ARG B 129     2548   2514   3089   -124     79   -149       C  
ATOM   3349  CD  ARG B 129      45.947  64.695  21.642  1.00 21.15           C  
ANISOU 3349  CD  ARG B 129     2374   2480   3181    125    128   -154       C  
ATOM   3350  NE  ARG B 129      44.792  65.522  21.975  1.00 20.07           N  
ANISOU 3350  NE  ARG B 129     2169   2407   3048    281    315   -210       N  
ATOM   3351  CZ  ARG B 129      43.711  65.662  21.213  1.00 19.48           C  
ANISOU 3351  CZ  ARG B 129     2251   2308   2841    347    206   -343       C  
ATOM   3352  NH1 ARG B 129      43.610  65.022  20.052  1.00 20.14           N  
ANISOU 3352  NH1 ARG B 129     2363   2375   2916    212   -151   -398       N  
ATOM   3353  NH2 ARG B 129      42.715  66.445  21.622  1.00 19.22           N  
ANISOU 3353  NH2 ARG B 129     2462   1972   2868    342    324   -346       N  
ATOM   3354  N   MET B 130      45.107  59.627  24.071  1.00 20.50           N  
ANISOU 3354  N   MET B 130     2779   2390   2621    -10    -93   -315       N  
ATOM   3355  CA  MET B 130      44.204  58.556  24.503  1.00 19.53           C  
ANISOU 3355  CA  MET B 130     2640   2399   2381    -44    -71   -215       C  
ATOM   3356  C   MET B 130      44.779  57.732  25.647  1.00 20.73           C  
ANISOU 3356  C   MET B 130     2822   2606   2450    149      4   -114       C  
ATOM   3357  O   MET B 130      44.090  56.870  26.203  1.00 21.54           O  
ANISOU 3357  O   MET B 130     2880   2770   2535    -18    -13   -204       O  
ATOM   3358  CB  MET B 130      43.882  57.615  23.338  1.00 18.88           C  
ANISOU 3358  CB  MET B 130     2518   2353   2302     78     62     -3       C  
ATOM   3359  CG  MET B 130      42.927  58.188  22.331  1.00 18.16           C  
ANISOU 3359  CG  MET B 130     2299   2276   2324    111    123    -52       C  
ATOM   3360  SD  MET B 130      42.872  57.156  20.866  1.00 18.46           S  
ANISOU 3360  SD  MET B 130     2371   2272   2371    307     33      1       S  
ATOM   3361  CE  MET B 130      41.983  58.244  19.750  1.00 17.13           C  
ANISOU 3361  CE  MET B 130     2035   2094   2381    526    -49    229       C  
ATOM   3362  N   GLY B 131      46.052  57.963  25.956  1.00 21.68           N  
ANISOU 3362  N   GLY B 131     3104   2732   2403    247   -302   -216       N  
ATOM   3363  CA  GLY B 131      46.741  57.249  27.019  1.00 21.71           C  
ANISOU 3363  CA  GLY B 131     3150   2705   2392    496   -203    -63       C  
ATOM   3364  C   GLY B 131      47.199  55.847  26.660  1.00 22.82           C  
ANISOU 3364  C   GLY B 131     3195   2909   2566    653   -196    -57       C  
ATOM   3365  O   GLY B 131      47.491  55.048  27.550  1.00 23.94           O  
ANISOU 3365  O   GLY B 131     3317   3106   2672    714   -311    108       O  
ATOM   3366  N   VAL B 132      47.274  55.534  25.370  1.00 22.23           N  
ANISOU 3366  N   VAL B 132     2992   2740   2716    759   -101   -207       N  
ATOM   3367  CA  VAL B 132      47.667  54.181  24.967  1.00 23.36           C  
ANISOU 3367  CA  VAL B 132     2864   3012   3001    552   -276    -42       C  
ATOM   3368  C   VAL B 132      48.855  54.153  24.011  1.00 25.04           C  
ANISOU 3368  C   VAL B 132     3028   3160   3327    527   -319     46       C  
ATOM   3369  O   VAL B 132      49.046  53.181  23.281  1.00 24.95           O  
ANISOU 3369  O   VAL B 132     3101   2995   3384    642   -370     33       O  
ATOM   3370  CB  VAL B 132      46.494  53.428  24.309  1.00 22.77           C  
ANISOU 3370  CB  VAL B 132     2561   3040   3052    330   -327     42       C  
ATOM   3371  CG1 VAL B 132      45.424  53.116  25.343  1.00 23.65           C  
ANISOU 3371  CG1 VAL B 132     2487   3247   3252    613   -306    147       C  
ATOM   3372  CG2 VAL B 132      45.925  54.232  23.139  1.00 22.00           C  
ANISOU 3372  CG2 VAL B 132     2379   2890   3092    206   -591     38       C  
ATOM   3373  N   ALA B 133      49.658  55.211  24.019  1.00 26.58           N  
ANISOU 3373  N   ALA B 133     3044   3437   3619    482   -306    195       N  
ATOM   3374  CA  ALA B 133      50.853  55.246  23.186  1.00 29.02           C  
ANISOU 3374  CA  ALA B 133     3239   3755   4031    551   -297    397       C  
ATOM   3375  C   ALA B 133      51.785  54.092  23.540  1.00 31.08           C  
ANISOU 3375  C   ALA B 133     3516   3914   4380    382   -258    328       C  
ATOM   3376  O   ALA B 133      52.013  53.813  24.715  1.00 31.11           O  
ANISOU 3376  O   ALA B 133     3412   3981   4426    344   -276    294       O  
ATOM   3377  CB  ALA B 133      51.570  56.572  23.339  1.00 29.04           C  
ANISOU 3377  CB  ALA B 133     3237   3726   4070    436   -180    516       C  
ATOM   3378  N   ASP B 134      52.298  53.422  22.510  1.00 33.58           N  
ANISOU 3378  N   ASP B 134     3898   4164   4697    169   -215    157       N  
ATOM   3379  CA  ASP B 134      53.243  52.314  22.653  1.00 36.93           C  
ANISOU 3379  CA  ASP B 134     4485   4476   5071    133   -282      1       C  
ATOM   3380  C   ASP B 134      52.663  51.123  23.417  1.00 36.84           C  
ANISOU 3380  C   ASP B 134     4646   4270   5082    454   -415   -154       C  
ATOM   3381  O   ASP B 134      53.404  50.278  23.916  1.00 37.61           O  
ANISOU 3381  O   ASP B 134     4733   4366   5191    570   -331   -220       O  
ATOM   3382  CB  ASP B 134      54.533  52.789  23.331  1.00 40.66           C  
ANISOU 3382  CB  ASP B 134     4936   5041   5474    -74   -126     59       C  
ATOM   3383  CG  ASP B 134      55.178  53.955  22.604  1.00 43.73           C  
ANISOU 3383  CG  ASP B 134     5260   5587   5769   -201     14    -31       C  
ATOM   3384  OD1 ASP B 134      55.582  53.779  21.434  1.00 45.00           O  
ANISOU 3384  OD1 ASP B 134     5430   5821   5846   -221     40    -45       O  
ATOM   3385  OD2 ASP B 134      55.288  55.046  23.206  1.00 44.66           O  
ANISOU 3385  OD2 ASP B 134     5333   5762   5874   -250     41    -51       O  
ATOM   3386  N   ARG B 135      51.338  51.062  23.509  1.00 36.49           N  
ANISOU 3386  N   ARG B 135     4780   4036   5047    622   -520   -252       N  
ATOM   3387  CA  ARG B 135      50.663  49.868  24.000  1.00 36.20           C  
ANISOU 3387  CA  ARG B 135     4869   3918   4967    796   -716   -260       C  
ATOM   3388  C   ARG B 135      50.415  48.938  22.824  1.00 34.98           C  
ANISOU 3388  C   ARG B 135     4806   3627   4857    922   -879   -250       C  
ATOM   3389  O   ARG B 135      50.061  49.394  21.736  1.00 33.56           O  
ANISOU 3389  O   ARG B 135     4616   3439   4696   1041  -1041   -264       O  
ATOM   3390  CB  ARG B 135      49.343  50.218  24.684  1.00 37.65           C  
ANISOU 3390  CB  ARG B 135     5101   4165   5041    817   -692   -263       C  
ATOM   3391  CG  ARG B 135      49.493  51.011  25.959  1.00 39.45           C  
ANISOU 3391  CG  ARG B 135     5367   4431   5191    776   -666   -311       C  
ATOM   3392  CD  ARG B 135      49.856  50.120  27.131  1.00 41.86           C  
ANISOU 3392  CD  ARG B 135     5645   4877   5382    653   -586   -392       C  
ATOM   3393  NE  ARG B 135      49.760  50.851  28.390  1.00 43.88           N  
ANISOU 3393  NE  ARG B 135     5856   5294   5521    507   -597   -378       N  
ATOM   3394  CZ  ARG B 135      49.637  50.282  29.584  1.00 45.40           C  
ANISOU 3394  CZ  ARG B 135     6007   5576   5667    502   -592   -367       C  
ATOM   3395  NH1 ARG B 135      49.590  48.962  29.696  1.00 46.02           N  
ANISOU 3395  NH1 ARG B 135     6042   5704   5739    456   -610   -385       N  
ATOM   3396  NH2 ARG B 135      49.556  51.039  30.670  1.00 46.03           N  
ANISOU 3396  NH2 ARG B 135     6058   5707   5724    564   -547   -332       N  
ATOM   3397  N   VAL B 136      50.602  47.640  23.035  1.00 35.15           N  
ANISOU 3397  N   VAL B 136     4883   3575   4899    952   -900   -148       N  
ATOM   3398  CA  VAL B 136      50.427  46.682  21.950  1.00 35.71           C  
ANISOU 3398  CA  VAL B 136     4949   3720   4900    868   -906    -24       C  
ATOM   3399  C   VAL B 136      48.986  46.737  21.440  1.00 34.01           C  
ANISOU 3399  C   VAL B 136     4796   3431   4697    711   -746    189       C  
ATOM   3400  O   VAL B 136      48.034  46.718  22.220  1.00 34.17           O  
ANISOU 3400  O   VAL B 136     4972   3285   4726    199   -622    263       O  
ATOM   3401  CB  VAL B 136      50.805  45.238  22.389  1.00 36.90           C  
ANISOU 3401  CB  VAL B 136     5078   3918   5026   1106   -974    -56       C  
ATOM   3402  CG1 VAL B 136      49.905  44.739  23.518  1.00 37.12           C  
ANISOU 3402  CG1 VAL B 136     5083   4008   5014   1207  -1021     24       C  
ATOM   3403  CG2 VAL B 136      50.771  44.288  21.200  1.00 38.01           C  
ANISOU 3403  CG2 VAL B 136     5190   4138   5116   1014  -1010    -85       C  
ATOM   3404  N   GLY B 137      48.838  46.866  20.125  1.00 31.79           N  
ANISOU 3404  N   GLY B 137     4475   3208   4394    938   -565    316       N  
ATOM   3405  CA  GLY B 137      47.527  46.907  19.501  1.00 29.16           C  
ANISOU 3405  CA  GLY B 137     4014   2973   4092    987   -588    325       C  
ATOM   3406  C   GLY B 137      46.868  48.278  19.434  1.00 28.09           C  
ANISOU 3406  C   GLY B 137     3796   2933   3943    757   -515    167       C  
ATOM   3407  O   GLY B 137      45.784  48.413  18.870  1.00 28.12           O  
ANISOU 3407  O   GLY B 137     3636   2986   4062    622   -470     94       O  
ATOM   3408  N   SER B 138      47.508  49.296  20.003  1.00 26.08           N  
ANISOU 3408  N   SER B 138     3455   2875   3579    531   -725    241       N  
ATOM   3409  CA  SER B 138      46.927  50.639  20.011  1.00 24.41           C  
ANISOU 3409  CA  SER B 138     3177   2797   3300    584   -519    166       C  
ATOM   3410  C   SER B 138      46.791  51.219  18.600  1.00 23.42           C  
ANISOU 3410  C   SER B 138     3115   2779   3005    663   -143    124       C  
ATOM   3411  O   SER B 138      45.911  52.044  18.348  1.00 21.70           O  
ANISOU 3411  O   SER B 138     2920   2508   2817    580    128   -122       O  
ATOM   3412  CB  SER B 138      47.756  51.580  20.887  1.00 25.88           C  
ANISOU 3412  CB  SER B 138     3227   3178   3431    481   -513    215       C  
ATOM   3413  OG  SER B 138      49.109  51.622  20.468  1.00 27.37           O  
ANISOU 3413  OG  SER B 138     3255   3561   3584    510   -554    234       O  
ATOM   3414  N   ARG B 139      47.638  50.765  17.679  1.00 24.93           N  
ANISOU 3414  N   ARG B 139     3250   3246   2975    724    -23     51       N  
ATOM   3415  CA  ARG B 139      47.600  51.232  16.290  1.00 25.79           C  
ANISOU 3415  CA  ARG B 139     3284   3447   3066    755    -15    126       C  
ATOM   3416  C   ARG B 139      46.295  50.848  15.581  1.00 23.89           C  
ANISOU 3416  C   ARG B 139     3067   3147   2863    894    305     28       C  
ATOM   3417  O   ARG B 139      46.021  51.317  14.476  1.00 24.40           O  
ANISOU 3417  O   ARG B 139     3182   3406   2683    714    471     50       O  
ATOM   3418  CB  ARG B 139      48.791  50.673  15.501  1.00 28.96           C  
ANISOU 3418  CB  ARG B 139     3544   3994   3468    623   -117    202       C  
ATOM   3419  CG  ARG B 139      50.153  50.973  16.103  1.00 32.84           C  
ANISOU 3419  CG  ARG B 139     4088   4420   3968    415   -248    254       C  
ATOM   3420  CD  ARG B 139      50.473  52.457  16.076  1.00 34.55           C  
ANISOU 3420  CD  ARG B 139     4395   4516   4217    294   -320    310       C  
ATOM   3421  NE  ARG B 139      50.657  52.959  14.716  1.00 36.53           N  
ANISOU 3421  NE  ARG B 139     4574   4798   4506    172   -301    247       N  
ATOM   3422  CZ  ARG B 139      51.040  54.199  14.426  1.00 37.92           C  
ANISOU 3422  CZ  ARG B 139     4703   5052   4654     67   -317    217       C  
ATOM   3423  NH1 ARG B 139      51.284  55.065  15.402  1.00 38.31           N  
ANISOU 3423  NH1 ARG B 139     4714   5106   4736     84   -369    189       N  
ATOM   3424  NH2 ARG B 139      51.182  54.575  13.161  1.00 38.60           N  
ANISOU 3424  NH2 ARG B 139     4769   5195   4703    -17   -214    139       N  
ATOM   3425  N   LYS B 140      45.501  49.993  16.220  1.00 21.34           N  
ANISOU 3425  N   LYS B 140     3001   2380   2725   1011    193    -48       N  
ATOM   3426  CA  LYS B 140      44.214  49.563  15.683  1.00 20.12           C  
ANISOU 3426  CA  LYS B 140     2975   2090   2579    905     89     35       C  
ATOM   3427  C   LYS B 140      43.090  50.584  15.906  1.00 19.63           C  
ANISOU 3427  C   LYS B 140     2644   2330   2485    720    136     39       C  
ATOM   3428  O   LYS B 140      41.999  50.443  15.363  1.00 20.07           O  
ANISOU 3428  O   LYS B 140     2390   2618   2617    656    165     64       O  
ATOM   3429  CB  LYS B 140      43.818  48.221  16.297  1.00 22.33           C  
ANISOU 3429  CB  LYS B 140     3519   2356   2610   1004    102    286       C  
ATOM   3430  CG  LYS B 140      44.783  47.087  15.970  1.00 23.95           C  
ANISOU 3430  CG  LYS B 140     3722   2655   2722   1131    328     87       C  
ATOM   3431  CD  LYS B 140      44.746  46.730  14.485  1.00 25.39           C  
ANISOU 3431  CD  LYS B 140     3894   2927   2826   1302    492    -13       C  
ATOM   3432  CE  LYS B 140      45.559  45.469  14.190  1.00 27.61           C  
ANISOU 3432  CE  LYS B 140     4242   3291   2958   1007    563     -8       C  
ATOM   3433  NZ  LYS B 140      45.527  45.116  12.740  1.00 30.45           N  
ANISOU 3433  NZ  LYS B 140     4588   3817   3166    775    652    132       N  
ATOM   3434  N   VAL B 141      43.349  51.599  16.720  1.00 18.75           N  
ANISOU 3434  N   VAL B 141     2637   2139   2348    509     -8     43       N  
ATOM   3435  CA  VAL B 141      42.440  52.740  16.800  1.00 18.26           C  
ANISOU 3435  CA  VAL B 141     2489   2110   2337    738     40     38       C  
ATOM   3436  C   VAL B 141      42.580  53.577  15.524  1.00 18.45           C  
ANISOU 3436  C   VAL B 141     2589   2066   2356    465     43     45       C  
ATOM   3437  O   VAL B 141      43.672  54.041  15.212  1.00 20.57           O  
ANISOU 3437  O   VAL B 141     2836   2472   2505    443   -174    151       O  
ATOM   3438  CB  VAL B 141      42.734  53.605  18.029  1.00 19.59           C  
ANISOU 3438  CB  VAL B 141     2543   2440   2462    697    123    244       C  
ATOM   3439  CG1 VAL B 141      41.788  54.803  18.082  1.00 18.00           C  
ANISOU 3439  CG1 VAL B 141     2200   2282   2358   1251    176    -35       C  
ATOM   3440  CG2 VAL B 141      42.634  52.765  19.296  1.00 21.41           C  
ANISOU 3440  CG2 VAL B 141     2619   2900   2617    383    145    407       C  
ATOM   3441  N   ASP B 142      41.487  53.768  14.788  1.00 15.85           N  
ANISOU 3441  N   ASP B 142     2228   1753   2042    845   -104    199       N  
ATOM   3442  CA  ASP B 142      41.563  54.378  13.452  1.00 17.01           C  
ANISOU 3442  CA  ASP B 142     2394   2002   2066    900    -68     22       C  
ATOM   3443  C   ASP B 142      40.956  55.765  13.361  1.00 16.68           C  
ANISOU 3443  C   ASP B 142     2297   2074   1966    706     18     83       C  
ATOM   3444  O   ASP B 142      41.375  56.581  12.543  1.00 18.70           O  
ANISOU 3444  O   ASP B 142     2579   2203   2323    809    382     50       O  
ATOM   3445  CB  ASP B 142      40.869  53.475  12.432  1.00 19.88           C  
ANISOU 3445  CB  ASP B 142     2814   2436   2302   1046    -53    -59       C  
ATOM   3446  CG  ASP B 142      41.438  52.084  12.411  1.00 22.95           C  
ANISOU 3446  CG  ASP B 142     3026   2847   2846    957     46    -73       C  
ATOM   3447  OD1 ASP B 142      42.681  51.958  12.418  1.00 24.48           O  
ANISOU 3447  OD1 ASP B 142     3221   3031   3048    901    -93    -94       O  
ATOM   3448  OD2 ASP B 142      40.641  51.126  12.391  1.00 24.78           O  
ANISOU 3448  OD2 ASP B 142     3153   3129   3134    827    307   -113       O  
ATOM   3449  N   VAL B 143      39.946  56.018  14.181  1.00 15.00           N  
ANISOU 3449  N   VAL B 143     2159   1918   1623    685    118    -61       N  
ATOM   3450  CA  VAL B 143      39.247  57.296  14.155  1.00 14.32           C  
ANISOU 3450  CA  VAL B 143     2132   1733   1577    620    402    -18       C  
ATOM   3451  C   VAL B 143      39.137  57.804  15.576  1.00 14.99           C  
ANISOU 3451  C   VAL B 143     2355   1795   1546    377    555   -241       C  
ATOM   3452  O   VAL B 143      38.679  57.092  16.460  1.00 16.18           O  
ANISOU 3452  O   VAL B 143     2630   1881   1637    134    641   -177       O  
ATOM   3453  CB  VAL B 143      37.843  57.178  13.546  1.00 15.44           C  
ANISOU 3453  CB  VAL B 143     2279   1925   1661    635    237     69       C  
ATOM   3454  CG1 VAL B 143      37.127  58.527  13.580  1.00 15.45           C  
ANISOU 3454  CG1 VAL B 143     2111   1854   1907    537    196    273       C  
ATOM   3455  CG2 VAL B 143      37.918  56.619  12.116  1.00 17.19           C  
ANISOU 3455  CG2 VAL B 143     2619   2125   1789    412    118    -88       C  
ATOM   3456  N   MET B 144      39.602  59.022  15.794  1.00 14.46           N  
ANISOU 3456  N   MET B 144     2229   1742   1524    373    563   -196       N  
ATOM   3457  CA  MET B 144      39.531  59.661  17.099  1.00 14.63           C  
ANISOU 3457  CA  MET B 144     2006   1683   1872    151    534   -173       C  
ATOM   3458  C   MET B 144      38.182  60.356  17.262  1.00 13.80           C  
ANISOU 3458  C   MET B 144     1954   1461   1828    396    407     55       C  
ATOM   3459  O   MET B 144      37.652  60.916  16.298  1.00 14.20           O  
ANISOU 3459  O   MET B 144     1898   1766   1731    708    283     33       O  
ATOM   3460  CB  MET B 144      40.696  60.639  17.232  1.00 18.43           C  
ANISOU 3460  CB  MET B 144     2154   2148   2701    -19    364   -599       C  
ATOM   3461  CG  MET B 144      40.625  61.644  18.349  1.00 23.61           C  
ANISOU 3461  CG  MET B 144     2409   2705   3855    130    219   -623       C  
ATOM   3462  SD  MET B 144      42.105  62.674  18.199  1.00 25.97           S  
ANISOU 3462  SD  MET B 144     2269   2903   4695    354   -118  -1202       S  
ATOM   3463  CE  MET B 144      41.817  63.581  16.688  1.00 27.50           C  
ANISOU 3463  CE  MET B 144     2492   3197   4760    246   -156  -1277       C  
ATOM   3464  N   ILE B 145      37.621  60.276  18.466  1.00 13.39           N  
ANISOU 3464  N   ILE B 145     1802   1369   1916    497    563    110       N  
ATOM   3465  CA  ILE B 145      36.402  61.000  18.819  1.00 12.80           C  
ANISOU 3465  CA  ILE B 145     1872   1200   1790    370    450      9       C  
ATOM   3466  C   ILE B 145      36.764  62.096  19.810  1.00 13.84           C  
ANISOU 3466  C   ILE B 145     2077   1424   1757    317    519    -27       C  
ATOM   3467  O   ILE B 145      37.376  61.821  20.847  1.00 14.67           O  
ANISOU 3467  O   ILE B 145     2228   1618   1729    284    427     49       O  
ATOM   3468  CB  ILE B 145      35.330  60.096  19.468  1.00 13.33           C  
ANISOU 3468  CB  ILE B 145     1911   1187   1967    359    464    -62       C  
ATOM   3469  CG1 ILE B 145      35.146  58.791  18.686  1.00 13.54           C  
ANISOU 3469  CG1 ILE B 145     1988   1173   1985     82    380    -80       C  
ATOM   3470  CG2 ILE B 145      34.012  60.862  19.611  1.00 14.03           C  
ANISOU 3470  CG2 ILE B 145     1985   1392   1953    648    629    -85       C  
ATOM   3471  CD1 ILE B 145      34.279  57.778  19.416  1.00 14.08           C  
ANISOU 3471  CD1 ILE B 145     2003   1288   2060     41    377    127       C  
ATOM   3472  N   GLU B 146      36.404  63.333  19.478  1.00 13.77           N  
ANISOU 3472  N   GLU B 146     1945   1434   1854     36    569   -261       N  
ATOM   3473  CA  GLU B 146      36.685  64.472  20.342  1.00 13.97           C  
ANISOU 3473  CA  GLU B 146     1811   1441   2057     90    532   -279       C  
ATOM   3474  C   GLU B 146      35.407  65.235  20.662  1.00 14.03           C  
ANISOU 3474  C   GLU B 146     1920   1426   1985    225    414   -167       C  
ATOM   3475  O   GLU B 146      34.420  65.132  19.945  1.00 14.60           O  
ANISOU 3475  O   GLU B 146     1950   1588   2008    478    343     12       O  
ATOM   3476  CB  GLU B 146      37.698  65.411  19.686  1.00 14.69           C  
ANISOU 3476  CB  GLU B 146     1724   1671   2188     85    477    -98       C  
ATOM   3477  CG  GLU B 146      39.111  64.857  19.581  1.00 16.15           C  
ANISOU 3477  CG  GLU B 146     1748   2001   2388     81    626    139       C  
ATOM   3478  CD  GLU B 146      40.016  65.751  18.750  1.00 18.05           C  
ANISOU 3478  CD  GLU B 146     1956   2293   2609    125    383     59       C  
ATOM   3479  OE1 GLU B 146      39.622  66.105  17.625  1.00 18.72           O  
ANISOU 3479  OE1 GLU B 146     2109   2465   2537    -32    243    245       O  
ATOM   3480  OE2 GLU B 146      41.120  66.091  19.217  1.00 18.77           O  
ANISOU 3480  OE2 GLU B 146     1976   2433   2723    172    220   -193       O  
ATOM   3481  N   LYS B 147      35.429  65.981  21.762  1.00 13.73           N  
ANISOU 3481  N   LYS B 147     2148   1278   1793    276    501   -114       N  
ATOM   3482  CA  LYS B 147      34.315  66.848  22.088  1.00 14.93           C  
ANISOU 3482  CA  LYS B 147     2331   1252   2087    593    312    -54       C  
ATOM   3483  C   LYS B 147      34.858  68.194  22.546  1.00 15.91           C  
ANISOU 3483  C   LYS B 147     2430   1459   2156    579    139   -253       C  
ATOM   3484  O   LYS B 147      35.775  68.259  23.365  1.00 16.51           O  
ANISOU 3484  O   LYS B 147     2403   1597   2272    559    183   -344       O  
ATOM   3485  CB  LYS B 147      33.406  66.242  23.160  1.00 17.03           C  
ANISOU 3485  CB  LYS B 147     2415   1702   2354    811    509   -158       C  
ATOM   3486  CG  LYS B 147      32.187  67.134  23.456  1.00 18.39           C  
ANISOU 3486  CG  LYS B 147     2566   1888   2531    812    595     45       C  
ATOM   3487  CD  LYS B 147      31.046  66.387  24.113  1.00 18.39           C  
ANISOU 3487  CD  LYS B 147     2714   2065   2209    648    752    167       C  
ATOM   3488  CE  LYS B 147      29.839  67.302  24.281  1.00 19.52           C  
ANISOU 3488  CE  LYS B 147     2785   2353   2278    568    770    426       C  
ATOM   3489  NZ  LYS B 147      28.711  66.658  24.998  1.00 22.25           N  
ANISOU 3489  NZ  LYS B 147     2799   2828   2826    501    576    235       N  
ATOM   3490  N   GLN B 148      34.291  69.263  22.003  1.00 16.79           N  
ANISOU 3490  N   GLN B 148     2701   1431   2248    502    173   -294       N  
ATOM   3491  CA  GLN B 148      34.699  70.605  22.381  1.00 19.05           C  
ANISOU 3491  CA  GLN B 148     2962   1779   2499    463     63   -175       C  
ATOM   3492  C   GLN B 148      34.319  70.840  23.843  1.00 18.62           C  
ANISOU 3492  C   GLN B 148     2600   1975   2500    463    251   -159       C  
ATOM   3493  O   GLN B 148      33.194  70.549  24.257  1.00 19.21           O  
ANISOU 3493  O   GLN B 148     2560   2169   2571    450    126   -394       O  
ATOM   3494  CB  GLN B 148      34.055  71.646  21.456  1.00 21.76           C  
ANISOU 3494  CB  GLN B 148     3473   1895   2900    315    117     63       C  
ATOM   3495  CG  GLN B 148      34.785  72.994  21.406  1.00 24.54           C  
ANISOU 3495  CG  GLN B 148     3794   2194   3336    147    126    138       C  
ATOM   3496  CD  GLN B 148      34.680  73.769  22.704  1.00 28.03           C  
ANISOU 3496  CD  GLN B 148     3887   2747   4016    124    184    352       C  
ATOM   3497  OE1 GLN B 148      35.656  74.356  23.179  1.00 29.32           O  
ANISOU 3497  OE1 GLN B 148     4001   2743   4398   -186    228    243       O  
ATOM   3498  NE2 GLN B 148      33.491  73.769  23.290  1.00 28.83           N  
ANISOU 3498  NE2 GLN B 148     3752   3106   4095    180    275    606       N  
ATOM   3499  N   GLY B 149      35.278  71.316  24.627  1.00 17.76           N  
ANISOU 3499  N   GLY B 149     2732   1648   2370    359    340   -126       N  
ATOM   3500  CA  GLY B 149      35.037  71.614  26.028  1.00 18.03           C  
ANISOU 3500  CA  GLY B 149     2987   1582   2283    314    262   -176       C  
ATOM   3501  C   GLY B 149      35.091  70.422  26.966  1.00 19.17           C  
ANISOU 3501  C   GLY B 149     2995   1758   2529    358    585   -223       C  
ATOM   3502  O   GLY B 149      34.801  70.548  28.156  1.00 20.55           O  
ANISOU 3502  O   GLY B 149     3112   2031   2666    393    523   -215       O  
ATOM   3503  N   GLY B 150      35.467  69.262  26.436  1.00 19.77           N  
ANISOU 3503  N   GLY B 150     3144   1717   2651    343    654    -74       N  
ATOM   3504  CA  GLY B 150      35.600  68.070  27.255  1.00 20.03           C  
ANISOU 3504  CA  GLY B 150     3098   1883   2628    586    491   -122       C  
ATOM   3505  C   GLY B 150      36.778  67.231  26.810  1.00 19.29           C  
ANISOU 3505  C   GLY B 150     3116   1785   2428    341    339   -111       C  
ATOM   3506  O   GLY B 150      37.510  67.613  25.900  1.00 18.92           O  
ANISOU 3506  O   GLY B 150     2805   1849   2533    254    422    -56       O  
ATOM   3507  N   GLY B 151      36.978  66.094  27.464  1.00 19.90           N  
ANISOU 3507  N   GLY B 151     3078   2044   2439    558     99    -94       N  
ATOM   3508  CA  GLY B 151      37.972  65.145  27.003  1.00 19.12           C  
ANISOU 3508  CA  GLY B 151     3107   1680   2477    412     61     51       C  
ATOM   3509  C   GLY B 151      39.398  65.413  27.442  1.00 19.67           C  
ANISOU 3509  C   GLY B 151     3125   1994   2354    164   -195     44       C  
ATOM   3510  O   GLY B 151      39.696  66.419  28.098  1.00 22.02           O  
ANISOU 3510  O   GLY B 151     3491   2301   2575    156   -359    -24       O  
ATOM   3511  N   ARG B 152      40.280  64.489  27.075  1.00 19.32           N  
ANISOU 3511  N   ARG B 152     2622   2401   2317   -229     98      2       N  
ATOM   3512  CA  ARG B 152      41.692  64.553  27.436  1.00 21.07           C  
ANISOU 3512  CA  ARG B 152     2869   2601   2537   -284    -82   -123       C  
ATOM   3513  C   ARG B 152      42.462  65.472  26.500  1.00 21.18           C  
ANISOU 3513  C   ARG B 152     2728   2691   2626   -681   -110   -299       C  
ATOM   3514  O   ARG B 152      42.193  65.499  25.298  1.00 21.00           O  
ANISOU 3514  O   ARG B 152     2928   2619   2433   -638   -132   -114       O  
ATOM   3515  CB  ARG B 152      42.319  63.158  27.398  1.00 22.44           C  
ANISOU 3515  CB  ARG B 152     3208   2701   2617   -153   -115   -119       C  
ATOM   3516  CG  ARG B 152      41.647  62.138  28.299  1.00 22.63           C  
ANISOU 3516  CG  ARG B 152     3255   2677   2667     33   -168     62       C  
ATOM   3517  CD  ARG B 152      42.033  60.717  27.904  1.00 24.41           C  
ANISOU 3517  CD  ARG B 152     3413   2961   2902    165   -397     81       C  
ATOM   3518  NE  ARG B 152      43.437  60.418  28.178  1.00 24.58           N  
ANISOU 3518  NE  ARG B 152     3386   2917   3034    152   -486    -76       N  
ATOM   3519  CZ  ARG B 152      43.866  59.862  29.308  1.00 25.07           C  
ANISOU 3519  CZ  ARG B 152     3458   2835   3234    259   -461    -18       C  
ATOM   3520  NH1 ARG B 152      43.000  59.554  30.260  1.00 24.91           N  
ANISOU 3520  NH1 ARG B 152     3649   2666   3150    151   -228     11       N  
ATOM   3521  NH2 ARG B 152      45.156  59.618  29.489  1.00 26.06           N  
ANISOU 3521  NH2 ARG B 152     3527   2971   3402    370   -475   -102       N  
ATOM   3522  N   SER B 153      43.419  66.208  27.066  1.00 21.99           N  
ANISOU 3522  N   SER B 153     2613   2806   2934   -548   -107   -472       N  
ATOM   3523  CA  SER B 153      44.383  67.003  26.304  1.00 22.75           C  
ANISOU 3523  CA  SER B 153     2707   2936   3001   -150   -162   -424       C  
ATOM   3524  C   SER B 153      43.773  67.815  25.165  1.00 22.42           C  
ANISOU 3524  C   SER B 153     2899   2585   3036   -155    -71   -478       C  
ATOM   3525  O   SER B 153      44.102  67.598  23.998  1.00 22.28           O  
ANISOU 3525  O   SER B 153     2945   2380   3141   -346   -203   -581       O  
ATOM   3526  CB  SER B 153      45.477  66.090  25.741  1.00 24.20           C  
ANISOU 3526  CB  SER B 153     2706   3369   3120    117   -190   -295       C  
ATOM   3527  OG  SER B 153      46.177  65.434  26.779  1.00 26.46           O  
ANISOU 3527  OG  SER B 153     2753   3908   3391    154    -42   -300       O  
ATOM   3528  N   PRO B 154      42.889  68.765  25.501  1.00 22.62           N  
ANISOU 3528  N   PRO B 154     3123   2416   3056     42     92   -522       N  
ATOM   3529  CA  PRO B 154      42.201  69.555  24.475  1.00 24.03           C  
ANISOU 3529  CA  PRO B 154     3328   2629   3174    -64    469   -513       C  
ATOM   3530  C   PRO B 154      43.164  70.286  23.545  1.00 24.39           C  
ANISOU 3530  C   PRO B 154     3277   2649   3340   -389    705   -685       C  
ATOM   3531  O   PRO B 154      44.211  70.758  23.998  1.00 24.91           O  
ANISOU 3531  O   PRO B 154     3321   2799   3343   -439    842   -757       O  
ATOM   3532  CB  PRO B 154      41.377  70.552  25.297  1.00 22.77           C  
ANISOU 3532  CB  PRO B 154     3296   2418   2939    121    553   -789       C  
ATOM   3533  CG  PRO B 154      42.072  70.619  26.620  1.00 24.07           C  
ANISOU 3533  CG  PRO B 154     3444   2644   3058      2    310   -560       C  
ATOM   3534  CD  PRO B 154      42.556  69.224  26.859  1.00 24.10           C  
ANISOU 3534  CD  PRO B 154     3370   2694   3093     95    152   -562       C  
ATOM   3535  N   ASP B 155      42.819  70.366  22.264  1.00 23.85           N  
ANISOU 3535  N   ASP B 155     3190   2473   3400   -290    898   -603       N  
ATOM   3536  CA  ASP B 155      43.645  71.093  21.307  1.00 24.98           C  
ANISOU 3536  CA  ASP B 155     3251   2589   3653   -368   1025   -631       C  
ATOM   3537  C   ASP B 155      43.349  72.594  21.376  1.00 26.72           C  
ANISOU 3537  C   ASP B 155     3498   2810   3843   -388   1171   -535       C  
ATOM   3538  O   ASP B 155      42.597  73.046  22.245  1.00 26.41           O  
ANISOU 3538  O   ASP B 155     3524   2812   3698   -722   1263   -620       O  
ATOM   3539  CB  ASP B 155      43.446  70.554  19.878  1.00 24.70           C  
ANISOU 3539  CB  ASP B 155     3079   2582   3725   -213    973   -624       C  
ATOM   3540  CG  ASP B 155      42.035  70.770  19.333  1.00 24.65           C  
ANISOU 3540  CG  ASP B 155     3075   2544   3746   -406   1082   -538       C  
ATOM   3541  OD1 ASP B 155      41.252  71.565  19.897  1.00 23.77           O  
ANISOU 3541  OD1 ASP B 155     3116   2260   3654   -352   1172   -144       O  
ATOM   3542  OD2 ASP B 155      41.710  70.142  18.304  1.00 25.80           O  
ANISOU 3542  OD2 ASP B 155     2999   2922   3882     81   1250   -655       O  
ATOM   3543  N   ALA B 156      43.923  73.356  20.449  1.00 26.85           N  
ANISOU 3543  N   ALA B 156     3372   2763   4065   -349   1240   -331       N  
ATOM   3544  CA  ALA B 156      43.777  74.810  20.448  1.00 27.52           C  
ANISOU 3544  CA  ALA B 156     3397   2807   4254   -356   1313   -151       C  
ATOM   3545  C   ALA B 156      42.329  75.263  20.267  1.00 27.98           C  
ANISOU 3545  C   ALA B 156     3455   2758   4417   -404   1440   -165       C  
ATOM   3546  O   ALA B 156      41.962  76.358  20.700  1.00 29.10           O  
ANISOU 3546  O   ALA B 156     3558   2813   4686   -384   1289   -166       O  
ATOM   3547  CB  ALA B 156      44.653  75.421  19.364  1.00 27.99           C  
ANISOU 3547  CB  ALA B 156     3447   2938   4248   -367   1322     61       C  
ATOM   3548  N   GLU B 157      41.512  74.430  19.628  1.00 27.16           N  
ANISOU 3548  N   GLU B 157     3409   2605   4304   -621   1623    181       N  
ATOM   3549  CA  GLU B 157      40.104  74.753  19.407  1.00 27.85           C  
ANISOU 3549  CA  GLU B 157     3634   2636   4313   -412   1467     46       C  
ATOM   3550  C   GLU B 157      39.212  74.244  20.543  1.00 27.56           C  
ANISOU 3550  C   GLU B 157     3725   2455   4293   -252   1396   -311       C  
ATOM   3551  O   GLU B 157      37.990  74.397  20.499  1.00 29.24           O  
ANISOU 3551  O   GLU B 157     3842   2704   4564   -217   1262   -378       O  
ATOM   3552  CB  GLU B 157      39.627  74.178  18.073  1.00 30.37           C  
ANISOU 3552  CB  GLU B 157     3931   3214   4393   -263   1462    126       C  
ATOM   3553  CG  GLU B 157      40.191  74.890  16.854  1.00 32.11           C  
ANISOU 3553  CG  GLU B 157     4229   3552   4420   -199   1323    205       C  
ATOM   3554  CD  GLU B 157      39.729  74.270  15.549  1.00 33.93           C  
ANISOU 3554  CD  GLU B 157     4398   3958   4536   -139   1196    192       C  
ATOM   3555  N   GLY B 158      39.830  73.638  21.550  1.00 25.44           N  
ANISOU 3555  N   GLY B 158     3726   2017   3923   -411   1384   -343       N  
ATOM   3556  CA  GLY B 158      39.109  73.157  22.716  1.00 23.92           C  
ANISOU 3556  CA  GLY B 158     3663   1873   3554   -408   1357   -387       C  
ATOM   3557  C   GLY B 158      38.598  71.728  22.626  1.00 21.66           C  
ANISOU 3557  C   GLY B 158     3459   1600   3173   -262   1320   -453       C  
ATOM   3558  O   GLY B 158      37.910  71.252  23.532  1.00 22.84           O  
ANISOU 3558  O   GLY B 158     3520   1822   3335   -332   1449   -410       O  
ATOM   3559  N   PHE B 159      38.941  71.030  21.550  1.00 19.64           N  
ANISOU 3559  N   PHE B 159     3338   1271   2853    -53   1107   -278       N  
ATOM   3560  CA  PHE B 159      38.505  69.642  21.400  1.00 18.15           C  
ANISOU 3560  CA  PHE B 159     3093   1300   2503    -23    868   -250       C  
ATOM   3561  C   PHE B 159      39.411  68.672  22.151  1.00 17.43           C  
ANISOU 3561  C   PHE B 159     2807   1422   2392   -144    551   -173       C  
ATOM   3562  O   PHE B 159      40.609  68.578  21.880  1.00 18.64           O  
ANISOU 3562  O   PHE B 159     2805   1839   2439    148    558    -24       O  
ATOM   3563  CB  PHE B 159      38.452  69.251  19.925  1.00 18.93           C  
ANISOU 3563  CB  PHE B 159     3231   1508   2455    174    750    -96       C  
ATOM   3564  CG  PHE B 159      37.317  69.874  19.169  1.00 20.02           C  
ANISOU 3564  CG  PHE B 159     3216   1648   2745    339    753    -13       C  
ATOM   3565  CD1 PHE B 159      36.103  69.220  19.047  1.00 20.05           C  
ANISOU 3565  CD1 PHE B 159     3219   1661   2737    476    823   -177       C  
ATOM   3566  CD2 PHE B 159      37.465  71.119  18.578  1.00 22.49           C  
ANISOU 3566  CD2 PHE B 159     3428   2042   3075    100    404    262       C  
ATOM   3567  CE1 PHE B 159      35.056  69.788  18.347  1.00 20.62           C  
ANISOU 3567  CE1 PHE B 159     3232   1725   2879    404    653    102       C  
ATOM   3568  CE2 PHE B 159      36.423  71.699  17.878  1.00 23.71           C  
ANISOU 3568  CE2 PHE B 159     3544   2186   3278    117    331    401       C  
ATOM   3569  CZ  PHE B 159      35.218  71.038  17.761  1.00 22.51           C  
ANISOU 3569  CZ  PHE B 159     3354   2041   3156    132    413    276       C  
ATOM   3570  N   GLY B 160      38.837  67.941  23.098  1.00 16.79           N  
ANISOU 3570  N   GLY B 160     2755   1331   2295    -80    274    -55       N  
ATOM   3571  CA  GLY B 160      39.589  66.936  23.826  1.00 16.91           C  
ANISOU 3571  CA  GLY B 160     2633   1402   2391     75    193   -201       C  
ATOM   3572  C   GLY B 160      39.149  65.538  23.436  1.00 16.27           C  
ANISOU 3572  C   GLY B 160     2453   1491   2239     26    280    -45       C  
ATOM   3573  O   GLY B 160      38.044  65.348  22.939  1.00 16.60           O  
ANISOU 3573  O   GLY B 160     2376   1726   2207    174    347     14       O  
ATOM   3574  N   VAL B 161      40.012  64.559  23.674  1.00 16.72           N  
ANISOU 3574  N   VAL B 161     2393   1717   2242     87    464      1       N  
ATOM   3575  CA  VAL B 161      39.726  63.181  23.277  1.00 16.35           C  
ANISOU 3575  CA  VAL B 161     2208   1655   2349    226    537   -335       C  
ATOM   3576  C   VAL B 161      38.743  62.522  24.225  1.00 17.11           C  
ANISOU 3576  C   VAL B 161     2578   1691   2234    280    294      2       C  
ATOM   3577  O   VAL B 161      38.963  62.502  25.435  1.00 18.45           O  
ANISOU 3577  O   VAL B 161     2940   1863   2206    289    -38   -148       O  
ATOM   3578  CB  VAL B 161      41.005  62.342  23.241  1.00 17.82           C  
ANISOU 3578  CB  VAL B 161     2089   1919   2761    321    462   -524       C  
ATOM   3579  CG1 VAL B 161      40.672  60.876  22.996  1.00 19.71           C  
ANISOU 3579  CG1 VAL B 161     2410   2018   3060    218    492   -691       C  
ATOM   3580  CG2 VAL B 161      41.933  62.878  22.175  1.00 19.08           C  
ANISOU 3580  CG2 VAL B 161     2037   2394   2819    159    384   -246       C  
ATOM   3581  N   VAL B 162      37.662  61.982  23.675  1.00 14.24           N  
ANISOU 3581  N   VAL B 162     2153   1312   1945    234    470    129       N  
ATOM   3582  CA  VAL B 162      36.676  61.280  24.488  1.00 15.16           C  
ANISOU 3582  CA  VAL B 162     2464   1498   1801     98    453     23       C  
ATOM   3583  C   VAL B 162      36.509  59.828  24.063  1.00 14.93           C  
ANISOU 3583  C   VAL B 162     2586   1590   1498    181    456   -200       C  
ATOM   3584  O   VAL B 162      35.775  59.078  24.692  1.00 15.35           O  
ANISOU 3584  O   VAL B 162     2645   1651   1535    159    439    114       O  
ATOM   3585  CB  VAL B 162      35.297  61.973  24.449  1.00 15.26           C  
ANISOU 3585  CB  VAL B 162     2472   1525   1801      4    317   -234       C  
ATOM   3586  CG1 VAL B 162      35.354  63.300  25.188  1.00 17.45           C  
ANISOU 3586  CG1 VAL B 162     2675   1699   2257    -47    410   -181       C  
ATOM   3587  CG2 VAL B 162      34.823  62.170  23.016  1.00 15.10           C  
ANISOU 3587  CG2 VAL B 162     2533   1657   1546     18    350   -336       C  
ATOM   3588  N   GLY B 163      37.174  59.428  22.987  1.00 14.69           N  
ANISOU 3588  N   GLY B 163     2543   1497   1543    345    289   -384       N  
ATOM   3589  CA  GLY B 163      37.105  58.040  22.597  1.00 15.02           C  
ANISOU 3589  CA  GLY B 163     2552   1732   1423    358    306   -601       C  
ATOM   3590  C   GLY B 163      37.856  57.741  21.323  1.00 14.89           C  
ANISOU 3590  C   GLY B 163     2519   1572   1564    416    331   -320       C  
ATOM   3591  O   GLY B 163      38.526  58.609  20.763  1.00 15.16           O  
ANISOU 3591  O   GLY B 163     2534   1422   1803    683    155    -40       O  
ATOM   3592  N   GLY B 164      37.753  56.486  20.879  1.00 14.49           N  
ANISOU 3592  N   GLY B 164     2475   1484   1544    475    388   -536       N  
ATOM   3593  CA  GLY B 164      38.347  56.068  19.621  1.00 14.17           C  
ANISOU 3593  CA  GLY B 164     2285   1501   1599    247      3   -587       C  
ATOM   3594  C   GLY B 164      37.510  54.987  18.971  1.00 14.30           C  
ANISOU 3594  C   GLY B 164     2304   1476   1654    381    177   -391       C  
ATOM   3595  O   GLY B 164      36.786  54.241  19.641  1.00 15.90           O  
ANISOU 3595  O   GLY B 164     2488   1725   1828    227    188   -249       O  
ATOM   3596  N   ILE B 165      37.605  54.920  17.651  1.00 13.47           N  
ANISOU 3596  N   ILE B 165     1989   1614   1517    517    -24   -439       N  
ATOM   3597  CA  ILE B 165      36.879  53.940  16.867  1.00 14.13           C  
ANISOU 3597  CA  ILE B 165     2202   1602   1564    509    195   -377       C  
ATOM   3598  C   ILE B 165      37.866  53.002  16.194  1.00 14.26           C  
ANISOU 3598  C   ILE B 165     2224   1401   1793    520    312   -137       C  
ATOM   3599  O   ILE B 165      38.829  53.454  15.566  1.00 15.69           O  
ANISOU 3599  O   ILE B 165     2555   1372   2036    436    322   -109       O  
ATOM   3600  CB  ILE B 165      36.004  54.610  15.792  1.00 14.86           C  
ANISOU 3600  CB  ILE B 165     2302   1642   1703    498     41   -285       C  
ATOM   3601  CG1 ILE B 165      35.001  55.573  16.429  1.00 16.26           C  
ANISOU 3601  CG1 ILE B 165     2387   1910   1881    455     35    -72       C  
ATOM   3602  CG2 ILE B 165      35.287  53.564  14.964  1.00 16.67           C  
ANISOU 3602  CG2 ILE B 165     2550   2067   1715    378   -268   -420       C  
ATOM   3603  CD1 ILE B 165      34.209  56.358  15.406  1.00 16.72           C  
ANISOU 3603  CD1 ILE B 165     2405   2000   1947    436   -132    314       C  
ATOM   3604  N   HIS B 166      37.638  51.700  16.370  1.00 13.94           N  
ANISOU 3604  N   HIS B 166     2191   1213   1894    717    282   -225       N  
ATOM   3605  CA  HIS B 166      38.320  50.673  15.591  1.00 14.95           C  
ANISOU 3605  CA  HIS B 166     2365   1549   1765    658    202      6       C  
ATOM   3606  C   HIS B 166      37.449  50.382  14.398  1.00 15.60           C  
ANISOU 3606  C   HIS B 166     2499   1607   1821    413    300   -145       C  
ATOM   3607  O   HIS B 166      36.400  49.753  14.541  1.00 16.39           O  
ANISOU 3607  O   HIS B 166     2539   1795   1895    261    260    136       O  
ATOM   3608  CB  HIS B 166      38.532  49.395  16.411  1.00 15.90           C  
ANISOU 3608  CB  HIS B 166     2644   1619   1779    856     22     73       C  
ATOM   3609  CG  HIS B 166      39.276  49.611  17.689  1.00 19.12           C  
ANISOU 3609  CG  HIS B 166     2918   2296   2050    690    184    145       C  
ATOM   3610  ND1 HIS B 166      40.376  48.865  18.045  1.00 20.90           N  
ANISOU 3610  ND1 HIS B 166     3060   2742   2138    558     21    230       N  
ATOM   3611  CD2 HIS B 166      39.074  50.493  18.696  1.00 20.30           C  
ANISOU 3611  CD2 HIS B 166     3134   2428   2152    554   -188    254       C  
ATOM   3612  CE1 HIS B 166      40.825  49.279  19.219  1.00 21.37           C  
ANISOU 3612  CE1 HIS B 166     3153   2729   2238    587    107     28       C  
ATOM   3613  NE2 HIS B 166      40.058  50.271  19.630  1.00 21.95           N  
ANISOU 3613  NE2 HIS B 166     3231   2817   2291    764   -161    205       N  
ATOM   3614  N   ALA B 167      37.863  50.862  13.228  1.00 14.91           N  
ANISOU 3614  N   ALA B 167     2679   1425   1561    331    254   -142       N  
ATOM   3615  CA  ALA B 167      37.074  50.715  12.028  1.00 15.63           C  
ANISOU 3615  CA  ALA B 167     2791   1596   1551     71    172   -107       C  
ATOM   3616  C   ALA B 167      37.637  49.563  11.210  1.00 16.00           C  
ANISOU 3616  C   ALA B 167     2561   1914   1605     26    475   -240       C  
ATOM   3617  O   ALA B 167      38.833  49.524  10.927  1.00 18.75           O  
ANISOU 3617  O   ALA B 167     2711   2408   2007   -275    658   -302       O  
ATOM   3618  CB  ALA B 167      37.077  52.004  11.225  1.00 16.81           C  
ANISOU 3618  CB  ALA B 167     3126   1723   1539   -349   -246    266       C  
ATOM   3619  N   LYS B 168      36.782  48.605  10.885  1.00 13.43           N  
ANISOU 3619  N   LYS B 168     2233   1530   1339    161    220   -123       N  
ATOM   3620  CA  LYS B 168      37.197  47.447  10.103  1.00 14.27           C  
ANISOU 3620  CA  LYS B 168     2263   1698   1461    441     84   -171       C  
ATOM   3621  C   LYS B 168      36.123  47.106   9.096  1.00 13.64           C  
ANISOU 3621  C   LYS B 168     1991   1692   1498    537    219   -130       C  
ATOM   3622  O   LYS B 168      34.965  46.945   9.465  1.00 15.10           O  
ANISOU 3622  O   LYS B 168     2022   1966   1751    491    344   -275       O  
ATOM   3623  CB  LYS B 168      37.450  46.229  11.003  1.00 16.60           C  
ANISOU 3623  CB  LYS B 168     2577   1960   1770    411    -44    145       C  
ATOM   3624  CG  LYS B 168      38.296  46.480  12.240  1.00 18.39           C  
ANISOU 3624  CG  LYS B 168     2725   2076   2186     33   -158     79       C  
ATOM   3625  CD  LYS B 168      38.434  45.197  13.053  1.00 19.99           C  
ANISOU 3625  CD  LYS B 168     2992   2161   2441    133   -295     32       C  
ATOM   3626  CE  LYS B 168      39.097  45.430  14.416  1.00 22.33           C  
ANISOU 3626  CE  LYS B 168     3070   2624   2790    312   -168    126       C  
ATOM   3627  NZ  LYS B 168      40.489  45.953  14.312  1.00 23.59           N  
ANISOU 3627  NZ  LYS B 168     3030   2946   2986    487   -177    153       N  
ATOM   3628  N   VAL B 169      36.487  46.991   7.823  1.00 12.18           N  
ANISOU 3628  N   VAL B 169     1900   1411   1317    457     95     41       N  
ATOM   3629  CA  VAL B 169      35.504  46.584   6.833  1.00 12.68           C  
ANISOU 3629  CA  VAL B 169     1941   1443   1435    249    213    -22       C  
ATOM   3630  C   VAL B 169      35.017  45.175   7.122  1.00 13.64           C  
ANISOU 3630  C   VAL B 169     1869   1564   1749    393    278    -28       C  
ATOM   3631  O   VAL B 169      33.823  44.886   7.066  1.00 14.77           O  
ANISOU 3631  O   VAL B 169     1935   1695   1982    150    406     77       O  
ATOM   3632  CB  VAL B 169      36.077  46.639   5.408  1.00 13.26           C  
ANISOU 3632  CB  VAL B 169     1962   1491   1586    156    254     90       C  
ATOM   3633  CG1 VAL B 169      35.105  46.006   4.426  1.00 13.96           C  
ANISOU 3633  CG1 VAL B 169     1673   1868   1762    122    265     17       C  
ATOM   3634  CG2 VAL B 169      36.391  48.085   5.020  1.00 13.70           C  
ANISOU 3634  CG2 VAL B 169     2074   1233   1899    277    247    376       C  
ATOM   3635  N   SER B 170      35.962  44.304   7.449  1.00 12.59           N  
ANISOU 3635  N   SER B 170     1862   1258   1665    397    376     58       N  
ATOM   3636  CA  SER B 170      35.659  42.905   7.676  1.00 13.40           C  
ANISOU 3636  CA  SER B 170     1926   1341   1824    242    373    268       C  
ATOM   3637  C   SER B 170      36.511  42.394   8.824  1.00 15.14           C  
ANISOU 3637  C   SER B 170     2076   1753   1922    302    370    394       C  
ATOM   3638  O   SER B 170      37.481  43.041   9.212  1.00 15.66           O  
ANISOU 3638  O   SER B 170     2333   1850   1768    357    319    241       O  
ATOM   3639  CB  SER B 170      35.894  42.103   6.395  1.00 14.13           C  
ANISOU 3639  CB  SER B 170     1996   1381   1990    104    532     15       C  
ATOM   3640  OG  SER B 170      37.166  42.382   5.856  1.00 14.48           O  
ANISOU 3640  OG  SER B 170     2063   1357   2083   -102    537     18       O  
ATOM   3641  N   LEU B 171      36.154  41.231   9.360  1.00 16.97           N  
ANISOU 3641  N   LEU B 171     2229   2046   2171    446    233    638       N  
ATOM   3642  CA  LEU B 171      36.680  40.817  10.657  1.00 18.69           C  
ANISOU 3642  CA  LEU B 171     2406   2178   2516    496    291    741       C  
ATOM   3643  C   LEU B 171      37.557  39.564  10.644  1.00 21.66           C  
ANISOU 3643  C   LEU B 171     2899   2360   2970    515     84    849       C  
ATOM   3644  O   LEU B 171      37.658  38.876  11.659  1.00 23.82           O  
ANISOU 3644  O   LEU B 171     3132   2582   3337    435    -88   1084       O  
ATOM   3645  CB  LEU B 171      35.508  40.599  11.616  1.00 18.50           C  
ANISOU 3645  CB  LEU B 171     2313   2108   2609    487    419    539       C  
ATOM   3646  CG  LEU B 171      34.609  41.818  11.839  1.00 18.35           C  
ANISOU 3646  CG  LEU B 171     2298   2050   2625    232    443    348       C  
ATOM   3647  CD1 LEU B 171      33.416  41.444  12.703  1.00 19.40           C  
ANISOU 3647  CD1 LEU B 171     2405   2199   2768     35    658    166       C  
ATOM   3648  CD2 LEU B 171      35.390  42.961  12.468  1.00 17.51           C  
ANISOU 3648  CD2 LEU B 171     2024   2072   2557     27    507    256       C  
ATOM   3649  N   ALA B 172      38.212  39.266   9.531  1.00 22.41           N  
ANISOU 3649  N   ALA B 172     3084   2231   3199    832     25    838       N  
ATOM   3650  CA  ALA B 172      39.052  38.066   9.479  1.00 23.46           C  
ANISOU 3650  CA  ALA B 172     3335   2388   3192    907    125   1037       C  
ATOM   3651  C   ALA B 172      40.310  38.246  10.331  1.00 26.07           C  
ANISOU 3651  C   ALA B 172     3632   2880   3392   1285     91    986       C  
ATOM   3652  O   ALA B 172      40.946  37.266  10.731  1.00 28.13           O  
ANISOU 3652  O   ALA B 172     4055   3113   3520   1224    -28    942       O  
ATOM   3653  CB  ALA B 172      39.422  37.733   8.050  1.00 24.02           C  
ANISOU 3653  CB  ALA B 172     3337   2517   3274    819    367    822       C  
ATOM   3654  N   GLU B 173      40.649  39.495  10.629  1.00 29.00           N  
ANISOU 3654  N   GLU B 173     3903   3495   3621    905    136    397       N  
ATOM   3655  CA  GLU B 173      41.871  39.798  11.362  1.00 30.92           C  
ANISOU 3655  CA  GLU B 173     4031   3810   3907   1128    -18     19       C  
ATOM   3656  C   GLU B 173      41.807  39.381  12.827  1.00 31.23           C  
ANISOU 3656  C   GLU B 173     4231   3778   3858   1335   -307   -399       C  
ATOM   3657  O   GLU B 173      40.741  39.071  13.361  1.00 30.41           O  
ANISOU 3657  O   GLU B 173     4225   3556   3776   1126   -647   -494       O  
ATOM   3658  CB  GLU B 173      42.186  41.290  11.268  1.00 33.30           C  
ANISOU 3658  CB  GLU B 173     4227   4216   4211    746     75     42       C  
ATOM   3659  N   ARG B 174      42.977  39.372  13.455  1.00 33.54           N  
ANISOU 3659  N   ARG B 174     4553   4227   3963   1442     -7   -679       N  
ATOM   3660  CA  ARG B 174      43.141  39.024  14.860  1.00 34.70           C  
ANISOU 3660  CA  ARG B 174     4841   4319   4022   1578    175   -858       C  
ATOM   3661  C   ARG B 174      42.632  40.152  15.765  1.00 35.29           C  
ANISOU 3661  C   ARG B 174     4771   4392   4243   1682    343   -790       C  
ATOM   3662  O   ARG B 174      43.412  40.983  16.225  1.00 35.60           O  
ANISOU 3662  O   ARG B 174     4759   4462   4307   1651    350   -533       O  
ATOM   3663  CB  ARG B 174      44.622  38.734  15.136  1.00 36.17           C  
ANISOU 3663  CB  ARG B 174     5110   4618   4015   1541    229   -888       C  
ATOM   3664  CG  ARG B 174      44.947  38.171  16.509  1.00 37.27           C  
ANISOU 3664  CG  ARG B 174     5210   4899   4051   1430    242   -773       C  
ATOM   3665  CD  ARG B 174      44.579  36.706  16.619  1.00 36.93           C  
ANISOU 3665  CD  ARG B 174     5089   4975   3968   1429    270   -778       C  
ATOM   3666  NE  ARG B 174      45.191  35.876  15.585  1.00 35.62           N  
ANISOU 3666  NE  ARG B 174     4762   4902   3871   1420     57   -591       N  
ATOM   3667  CZ  ARG B 174      45.126  34.548  15.570  1.00 34.91           C  
ANISOU 3667  CZ  ARG B 174     4466   4966   3833   1411    -95   -207       C  
ATOM   3668  NH1 ARG B 174      44.488  33.907  16.540  1.00 34.07           N  
ANISOU 3668  NH1 ARG B 174     4238   4966   3743   1168    -30      8       N  
ATOM   3669  NH2 ARG B 174      45.701  33.861  14.593  1.00 34.39           N  
ANISOU 3669  NH2 ARG B 174     4404   4902   3761   1481   -300   -256       N  
ATOM   3670  N   VAL B 175      41.326  40.176  16.020  1.00 34.29           N  
ANISOU 3670  N   VAL B 175     4424   4292   4313   1685    396  -1059       N  
ATOM   3671  CA  VAL B 175      40.714  41.268  16.781  1.00 33.77           C  
ANISOU 3671  CA  VAL B 175     4233   4150   4448   1387    358  -1248       C  
ATOM   3672  C   VAL B 175      41.161  41.250  18.254  1.00 31.93           C  
ANISOU 3672  C   VAL B 175     4048   3656   4428   1474    343  -1162       C  
ATOM   3673  O   VAL B 175      41.008  42.237  18.974  1.00 31.73           O  
ANISOU 3673  O   VAL B 175     4171   3395   4491   1419    216  -1566       O  
ATOM   3674  CB  VAL B 175      39.163  41.210  16.676  1.00 34.73           C  
ANISOU 3674  CB  VAL B 175     4291   4279   4627    956    279  -1277       C  
ATOM   3675  CG1 VAL B 175      38.508  42.394  17.380  1.00 33.79           C  
ANISOU 3675  CG1 VAL B 175     4115   4039   4685    882    306  -1281       C  
ATOM   3676  CG2 VAL B 175      38.741  41.190  15.217  1.00 35.58           C  
ANISOU 3676  CG2 VAL B 175     4313   4497   4711    690     88  -1206       C  
ATOM   3677  N   SER B 176      41.745  40.142  18.698  1.00 29.77           N  
ANISOU 3677  N   SER B 176     3711   3325   4274   1478    415   -808       N  
ATOM   3678  CA  SER B 176      42.280  40.080  20.055  1.00 27.87           C  
ANISOU 3678  CA  SER B 176     3594   3033   3963   1092    718   -553       C  
ATOM   3679  C   SER B 176      43.426  41.080  20.219  1.00 27.06           C  
ANISOU 3679  C   SER B 176     3512   3122   3646    930    917   -112       C  
ATOM   3680  O   SER B 176      43.725  41.513  21.333  1.00 25.25           O  
ANISOU 3680  O   SER B 176     3336   2659   3597    795    958     35       O  
ATOM   3681  CB  SER B 176      42.744  38.662  20.398  1.00 27.87           C  
ANISOU 3681  CB  SER B 176     3559   3001   4030    973    747   -404       C  
ATOM   3682  OG  SER B 176      43.752  38.224  19.506  1.00 27.45           O  
ANISOU 3682  OG  SER B 176     3454   2962   4015    970    889   -399       O  
ATOM   3683  N   ASP B 177      44.053  41.445  19.100  1.00 26.96           N  
ANISOU 3683  N   ASP B 177     3588   3259   3395   1257   1134     25       N  
ATOM   3684  CA  ASP B 177      45.041  42.523  19.061  1.00 27.45           C  
ANISOU 3684  CA  ASP B 177     3706   3331   3391   1420   1195    283       C  
ATOM   3685  C   ASP B 177      44.503  43.791  19.683  1.00 27.17           C  
ANISOU 3685  C   ASP B 177     3675   3229   3418   1397    868    431       C  
ATOM   3686  O   ASP B 177      45.211  44.509  20.390  1.00 27.88           O  
ANISOU 3686  O   ASP B 177     3612   3283   3698   1171    797    453       O  
ATOM   3687  CB  ASP B 177      45.447  42.844  17.624  1.00 29.73           C  
ANISOU 3687  CB  ASP B 177     3961   3819   3517   1617   1434    249       C  
ATOM   3688  CG  ASP B 177      46.378  41.823  17.035  1.00 32.64           C  
ANISOU 3688  CG  ASP B 177     4182   4485   3735   1681   1381    293       C  
ATOM   3689  OD1 ASP B 177      46.471  40.701  17.577  1.00 34.07           O  
ANISOU 3689  OD1 ASP B 177     4493   4659   3794   1564   1263    280       O  
ATOM   3690  OD2 ASP B 177      47.019  42.162  16.021  1.00 32.68           O  
ANISOU 3690  OD2 ASP B 177     4044   4624   3747   1797   1582    290       O  
ATOM   3691  N   ASP B 178      43.239  44.065  19.389  1.00 25.78           N  
ANISOU 3691  N   ASP B 178     3614   3149   3033   1113    648    312       N  
ATOM   3692  CA  ASP B 178      42.626  45.337  19.757  1.00 24.04           C  
ANISOU 3692  CA  ASP B 178     3506   2965   2663   1296    596    111       C  
ATOM   3693  C   ASP B 178      42.350  45.466  21.237  1.00 22.19           C  
ANISOU 3693  C   ASP B 178     3273   2754   2406   1076    500     53       C  
ATOM   3694  O   ASP B 178      42.231  46.574  21.745  1.00 21.45           O  
ANISOU 3694  O   ASP B 178     3221   2629   2300   1370    376    -88       O  
ATOM   3695  CB  ASP B 178      41.306  45.531  19.016  1.00 25.66           C  
ANISOU 3695  CB  ASP B 178     3801   3300   2647   1332    583    244       C  
ATOM   3696  CG  ASP B 178      41.481  45.614  17.526  1.00 27.30           C  
ANISOU 3696  CG  ASP B 178     4063   3614   2696   1503    521     30       C  
ATOM   3697  OD1 ASP B 178      41.032  46.621  16.945  1.00 27.51           O  
ANISOU 3697  OD1 ASP B 178     3843   3821   2787   1313    424    -40       O  
ATOM   3698  OD2 ASP B 178      42.058  44.674  16.939  1.00 28.84           O  
ANISOU 3698  OD2 ASP B 178     4454   3654   2848   1655    480      6       O  
ATOM   3699  N   ILE B 179      42.235  44.334  21.920  1.00 21.10           N  
ANISOU 3699  N   ILE B 179     2968   2646   2403    892    410      9       N  
ATOM   3700  CA  ILE B 179      41.633  44.299  23.250  1.00 22.72           C  
ANISOU 3700  CA  ILE B 179     3125   2777   2729    615    314     25       C  
ATOM   3701  C   ILE B 179      42.392  45.070  24.343  1.00 21.36           C  
ANISOU 3701  C   ILE B 179     2966   2444   2706    774    268   -183       C  
ATOM   3702  O   ILE B 179      41.768  45.834  25.083  1.00 20.70           O  
ANISOU 3702  O   ILE B 179     3029   2230   2607    486    227     34       O  
ATOM   3703  CB  ILE B 179      41.432  42.836  23.720  1.00 25.41           C  
ANISOU 3703  CB  ILE B 179     3568   3095   2990    461    319    164       C  
ATOM   3704  CG1 ILE B 179      40.519  42.079  22.750  1.00 28.83           C  
ANISOU 3704  CG1 ILE B 179     3967   3740   3248    395    141    219       C  
ATOM   3705  CG2 ILE B 179      40.889  42.793  25.142  1.00 25.15           C  
ANISOU 3705  CG2 ILE B 179     3530   3070   2956    347    360    269       C  
ATOM   3706  CD1 ILE B 179      39.372  42.901  22.191  1.00 31.05           C  
ANISOU 3706  CD1 ILE B 179     4269   4011   3518    264    145    247       C  
ATOM   3707  N   PRO B 180      43.725  44.884  24.461  1.00 21.96           N  
ANISOU 3707  N   PRO B 180     3046   2472   2825   1149    169   -200       N  
ATOM   3708  CA  PRO B 180      44.374  45.536  25.607  1.00 22.77           C  
ANISOU 3708  CA  PRO B 180     3110   2528   3012    954     20    -87       C  
ATOM   3709  C   PRO B 180      44.241  47.060  25.608  1.00 21.79           C  
ANISOU 3709  C   PRO B 180     2970   2461   2849    667     87   -121       C  
ATOM   3710  O   PRO B 180      43.911  47.638  26.648  1.00 21.94           O  
ANISOU 3710  O   PRO B 180     3009   2650   2676    694    257    -53       O  
ATOM   3711  CB  PRO B 180      45.843  45.119  25.462  1.00 24.11           C  
ANISOU 3711  CB  PRO B 180     3145   2846   3169   1094    -59   -101       C  
ATOM   3712  CG  PRO B 180      45.791  43.830  24.714  1.00 24.45           C  
ANISOU 3712  CG  PRO B 180     3141   2945   3204   1375    -83    -40       C  
ATOM   3713  CD  PRO B 180      44.672  44.024  23.726  1.00 23.56           C  
ANISOU 3713  CD  PRO B 180     3027   2941   2985   1300      2   -122       C  
ATOM   3714  N   ALA B 181      44.481  47.696  24.468  1.00 21.48           N  
ANISOU 3714  N   ALA B 181     2825   2420   2918    270     65   -102       N  
ATOM   3715  CA  ALA B 181      44.400  49.153  24.407  1.00 19.89           C  
ANISOU 3715  CA  ALA B 181     2610   2201   2744    281    160   -144       C  
ATOM   3716  C   ALA B 181      42.954  49.608  24.543  1.00 18.58           C  
ANISOU 3716  C   ALA B 181     2407   2048   2602    288    130    -95       C  
ATOM   3717  O   ALA B 181      42.678  50.655  25.132  1.00 17.46           O  
ANISOU 3717  O   ALA B 181     2253   1766   2614    651    138     81       O  
ATOM   3718  CB  ALA B 181      45.004  49.671  23.122  1.00 20.41           C  
ANISOU 3718  CB  ALA B 181     2603   2343   2810     10    567    187       C  
ATOM   3719  N  ASER B 182      42.036  48.821  23.995  0.82 17.43           N  
ANISOU 3719  N  ASER B 182     2261   1965   2398    445    153   -102       N  
ATOM   3720  N  BSER B 182      42.028  48.812  24.017  0.18 18.27           N  
ANISOU 3720  N  BSER B 182     2369   2032   2540    256     92     60       N  
ATOM   3721  CA ASER B 182      40.620  49.124  24.122  0.82 16.08           C  
ANISOU 3721  CA ASER B 182     2227   1639   2243    547    -78     49       C  
ATOM   3722  CA BSER B 182      40.611  49.137  24.128  0.18 18.24           C  
ANISOU 3722  CA BSER B 182     2370   2045   2513    209    -50    251       C  
ATOM   3723  C  ASER B 182      40.204  49.133  25.590  0.82 17.04           C  
ANISOU 3723  C  ASER B 182     2505   1825   2145    492   -156    254       C  
ATOM   3724  C  BSER B 182      40.167  49.116  25.587  0.18 18.52           C  
ANISOU 3724  C  BSER B 182     2542   2045   2449    192   -181    356       C  
ATOM   3725  O  ASER B 182      39.545  50.060  26.043  0.82 17.51           O  
ANISOU 3725  O  ASER B 182     2806   1892   1955    354    111    122       O  
ATOM   3726  O  BSER B 182      39.447  50.008  26.029  0.18 18.79           O  
ANISOU 3726  O  BSER B 182     2622   2084   2432    121   -169    397       O  
ATOM   3727  CB ASER B 182      39.781  48.123  23.333  0.82 15.54           C  
ANISOU 3727  CB ASER B 182     2088   1759   2059    521    -24   -231       C  
ATOM   3728  CB BSER B 182      39.758  48.173  23.301  0.18 18.14           C  
ANISOU 3728  CB BSER B 182     2213   2169   2508    192    -53    295       C  
ATOM   3729  OG ASER B 182      38.400  48.406  23.445  0.82 15.29           O  
ANISOU 3729  OG ASER B 182     2184   1623   2003    419     10   -248       O  
ATOM   3730  OG BSER B 182      39.750  46.877  23.871  0.18 17.77           O  
ANISOU 3730  OG BSER B 182     2070   2199   2484    222    -46    360       O  
ATOM   3731  N   ARG B 183      40.601  48.107  26.338  1.00 18.71           N  
ANISOU 3731  N   ARG B 183     2670   2025   2416    203   -236    401       N  
ATOM   3732  CA  ARG B 183      40.248  48.030  27.755  1.00 21.60           C  
ANISOU 3732  CA  ARG B 183     3011   2594   2601    370   -187    614       C  
ATOM   3733  C   ARG B 183      40.852  49.179  28.557  1.00 20.54           C  
ANISOU 3733  C   ARG B 183     2905   2603   2295    700    115    430       C  
ATOM   3734  O   ARG B 183      40.201  49.739  29.438  1.00 21.54           O  
ANISOU 3734  O   ARG B 183     3046   2931   2206    734    321    548       O  
ATOM   3735  CB  ARG B 183      40.685  46.690  28.364  1.00 26.31           C  
ANISOU 3735  CB  ARG B 183     3480   3367   3150    303   -207    858       C  
ATOM   3736  CG  ARG B 183      39.823  45.500  27.957  1.00 32.85           C  
ANISOU 3736  CG  ARG B 183     4222   4430   3832    -64    -93    899       C  
ATOM   3737  CD  ARG B 183      38.347  45.873  27.857  1.00 38.74           C  
ANISOU 3737  CD  ARG B 183     4941   5222   4558   -553    -70    922       C  
ATOM   3738  NE  ARG B 183      37.707  46.105  29.151  1.00 43.19           N  
ANISOU 3738  NE  ARG B 183     5534   5741   5136   -767    -21    856       N  
ATOM   3739  CZ  ARG B 183      36.932  45.219  29.773  1.00 46.24           C  
ANISOU 3739  CZ  ARG B 183     6038   6072   5458   -771   -113    920       C  
ATOM   3740  NH1 ARG B 183      36.705  44.032  29.226  1.00 47.34           N  
ANISOU 3740  NH1 ARG B 183     6211   6175   5600   -749   -236    987       N  
ATOM   3741  NH2 ARG B 183      36.382  45.518  30.943  1.00 46.38           N  
ANISOU 3741  NH2 ARG B 183     6129   6263   5232   -799    -23    970       N  
ATOM   3742  N   ILE B 184      42.094  49.534  28.246  1.00 19.37           N  
ANISOU 3742  N   ILE B 184     2780   2345   2234    695    -93    190       N  
ATOM   3743  CA  ILE B 184      42.748  50.665  28.896  1.00 18.98           C  
ANISOU 3743  CA  ILE B 184     2755   2280   2176    620   -239    174       C  
ATOM   3744  C   ILE B 184      41.944  51.947  28.692  1.00 18.28           C  
ANISOU 3744  C   ILE B 184     2993   2059   1894    331   -285     52       C  
ATOM   3745  O   ILE B 184      41.701  52.692  29.642  1.00 20.62           O  
ANISOU 3745  O   ILE B 184     3199   2348   2288    280   -158   -346       O  
ATOM   3746  CB  ILE B 184      44.186  50.866  28.375  1.00 20.90           C  
ANISOU 3746  CB  ILE B 184     2869   2635   2438    166   -321    165       C  
ATOM   3747  CG1 ILE B 184      45.073  49.700  28.820  1.00 23.33           C  
ANISOU 3747  CG1 ILE B 184     2976   3110   2779     62   -279     96       C  
ATOM   3748  CG2 ILE B 184      44.762  52.198  28.867  1.00 21.23           C  
ANISOU 3748  CG2 ILE B 184     2908   2684   2474    242   -450     75       C  
ATOM   3749  CD1 ILE B 184      46.448  49.700  28.199  1.00 25.25           C  
ANISOU 3749  CD1 ILE B 184     3142   3424   3027     74   -186     75       C  
ATOM   3750  N  AMET B 185      41.538  52.198  27.446  0.54 17.29           N  
ANISOU 3750  N  AMET B 185     2878   1883   1807    336   -462    123       N  
ATOM   3751  N  BMET B 185      41.514  52.189  27.459  0.46 18.08           N  
ANISOU 3751  N  BMET B 185     3002   2020   1849    202   -442     33       N  
ATOM   3752  CA AMET B 185      40.761  53.390  27.116  0.54 16.14           C  
ANISOU 3752  CA AMET B 185     2617   1978   1538    105   -386    285       C  
ATOM   3753  CA BMET B 185      40.776  53.406  27.163  0.46 17.76           C  
ANISOU 3753  CA BMET B 185     2911   2178   1661    -73   -381     97       C  
ATOM   3754  C  AMET B 185      39.421  53.388  27.845  0.54 17.02           C  
ANISOU 3754  C  AMET B 185     2792   2037   1639    153   -159    199       C  
ATOM   3755  C  BMET B 185      39.414  53.393  27.850  0.46 17.95           C  
ANISOU 3755  C  BMET B 185     2928   2176   1716     13   -170    133       C  
ATOM   3756  O  AMET B 185      39.000  54.411  28.379  0.54 17.47           O  
ANISOU 3756  O  AMET B 185     2810   2166   1662    309    -69   -103       O  
ATOM   3757  O  BMET B 185      38.962  54.422  28.350  0.46 18.71           O  
ANISOU 3757  O  BMET B 185     2962   2343   1804     81   -108    -91       O  
ATOM   3758  CB AMET B 185      40.543  53.498  25.599  0.54 16.30           C  
ANISOU 3758  CB AMET B 185     2500   2117   1576    -76   -277    499       C  
ATOM   3759  CB BMET B 185      40.627  53.594  25.646  0.46 18.96           C  
ANISOU 3759  CB BMET B 185     3066   2399   1741   -347   -354    104       C  
ATOM   3760  CG AMET B 185      41.802  53.832  24.817  0.54 17.20           C  
ANISOU 3760  CG AMET B 185     2282   2486   1768    -10    -96    487       C  
ATOM   3761  CG BMET B 185      41.889  54.144  24.961  0.46 19.96           C  
ANISOU 3761  CG BMET B 185     3119   2631   1834   -458   -317    -45       C  
ATOM   3762  SD AMET B 185      41.510  53.920  23.040  0.54 17.78           S  
ANISOU 3762  SD AMET B 185     2069   2624   2061    221    229    504       S  
ATOM   3763  SD BMET B 185      41.800  54.296  23.165  0.46 20.57           S  
ANISOU 3763  SD BMET B 185     3163   2588   2066   -655   -291   -228       S  
ATOM   3764  CE AMET B 185      40.359  55.286  22.924  0.54 16.33           C  
ANISOU 3764  CE AMET B 185     1882   2350   1974    604    260    641       C  
ATOM   3765  CE BMET B 185      41.681  52.617  22.675  0.46 20.53           C  
ANISOU 3765  CE BMET B 185     3241   2492   2065   -653   -598   -626       C  
ATOM   3766  N   MET B 186      38.766  52.232  27.883  1.00 17.03           N  
ANISOU 3766  N   MET B 186     2818   2080   1571     71    -28    212       N  
ATOM   3767  CA  MET B 186      37.479  52.105  28.576  1.00 18.03           C  
ANISOU 3767  CA  MET B 186     3080   2020   1751    115    189     89       C  
ATOM   3768  C   MET B 186      37.626  52.404  30.067  1.00 18.80           C  
ANISOU 3768  C   MET B 186     3112   2191   1839     69    399    -33       C  
ATOM   3769  O   MET B 186      36.784  53.086  30.658  1.00 19.39           O  
ANISOU 3769  O   MET B 186     3104   2614   1648    264    772    149       O  
ATOM   3770  CB  MET B 186      36.885  50.714  28.370  1.00 18.25           C  
ANISOU 3770  CB  MET B 186     3224   1924   1788     48    246   -193       C  
ATOM   3771  CG  MET B 186      36.485  50.452  26.926  1.00 18.25           C  
ANISOU 3771  CG  MET B 186     3178   1905   1851     71    100   -169       C  
ATOM   3772  SD  MET B 186      35.935  48.752  26.652  1.00 20.15           S  
ANISOU 3772  SD  MET B 186     3169   2205   2284    -94     84   -224       S  
ATOM   3773  CE  MET B 186      34.358  48.795  27.506  1.00 20.47           C  
ANISOU 3773  CE  MET B 186     3039   2583   2157   -224     20    -33       C  
ATOM   3774  N   GLY B 187      38.721  51.925  30.648  1.00 19.98           N  
ANISOU 3774  N   GLY B 187     3403   2274   1915   -140    156   -254       N  
ATOM   3775  CA  GLY B 187      39.047  52.195  32.038  1.00 20.65           C  
ANISOU 3775  CA  GLY B 187     3732   2233   1881   -323     49   -364       C  
ATOM   3776  C   GLY B 187      39.272  53.668  32.329  1.00 21.21           C  
ANISOU 3776  C   GLY B 187     3813   2464   1782   -352   -140   -287       C  
ATOM   3777  O   GLY B 187      39.083  54.119  33.457  1.00 22.43           O  
ANISOU 3777  O   GLY B 187     3948   2829   1745   -207   -160   -251       O  
ATOM   3778  N   GLU B 188      39.676  54.425  31.314  1.00 20.37           N  
ANISOU 3778  N   GLU B 188     3658   2356   1728   -289     -2     25       N  
ATOM   3779  CA  GLU B 188      39.892  55.857  31.475  1.00 19.20           C  
ANISOU 3779  CA  GLU B 188     3283   2312   1701   -350    -96    -41       C  
ATOM   3780  C   GLU B 188      38.599  56.634  31.284  1.00 20.61           C  
ANISOU 3780  C   GLU B 188     3439   2501   1890   -229     51     -2       C  
ATOM   3781  O   GLU B 188      38.588  57.861  31.348  1.00 23.32           O  
ANISOU 3781  O   GLU B 188     3817   2830   2215   -350     20     76       O  
ATOM   3782  CB  GLU B 188      40.933  56.367  30.483  1.00 18.47           C  
ANISOU 3782  CB  GLU B 188     2962   2333   1722   -242   -205   -149       C  
ATOM   3783  CG  GLU B 188      42.314  55.789  30.663  1.00 20.08           C  
ANISOU 3783  CG  GLU B 188     2974   2657   1997   -293   -143    -86       C  
ATOM   3784  CD  GLU B 188      43.217  56.125  29.499  1.00 22.15           C  
ANISOU 3784  CD  GLU B 188     3116   2973   2328   -345   -235    169       C  
ATOM   3785  OE1 GLU B 188      42.690  56.306  28.378  1.00 22.54           O  
ANISOU 3785  OE1 GLU B 188     3084   3154   2325   -326   -328    171       O  
ATOM   3786  OE2 GLU B 188      44.445  56.205  29.699  1.00 24.12           O  
ANISOU 3786  OE2 GLU B 188     3366   3259   2541   -481   -141    116       O  
ATOM   3787  N   GLY B 189      37.511  55.916  31.033  1.00 19.09           N  
ANISOU 3787  N   GLY B 189     3180   2363   1712     60   -163     65       N  
ATOM   3788  CA  GLY B 189      36.234  56.548  30.775  1.00 19.73           C  
ANISOU 3788  CA  GLY B 189     3196   2441   1857     88    -53     58       C  
ATOM   3789  C   GLY B 189      36.090  57.005  29.334  1.00 20.08           C  
ANISOU 3789  C   GLY B 189     3135   2409   2088      7    -49    152       C  
ATOM   3790  O   GLY B 189      35.194  57.780  29.015  1.00 21.04           O  
ANISOU 3790  O   GLY B 189     2987   2585   2422   -103    127    246       O  
ATOM   3791  N   LEU B 190      36.973  56.524  28.465  1.00 18.91           N  
ANISOU 3791  N   LEU B 190     3181   2214   1789     85    -32    -39       N  
ATOM   3792  CA  LEU B 190      36.873  56.830  27.039  1.00 17.73           C  
ANISOU 3792  CA  LEU B 190     2995   1939   1804      5    -18     33       C  
ATOM   3793  C   LEU B 190      36.003  55.801  26.346  1.00 17.27           C  
ANISOU 3793  C   LEU B 190     3167   1692   1705    132   -143     68       C  
ATOM   3794  O   LEU B 190      35.924  54.653  26.779  1.00 19.49           O  
ANISOU 3794  O   LEU B 190     3746   1832   1828    154   -270    301       O  
ATOM   3795  CB  LEU B 190      38.253  56.859  26.375  1.00 17.66           C  
ANISOU 3795  CB  LEU B 190     2740   1928   2042     72    215     -3       C  
ATOM   3796  CG  LEU B 190      39.318  57.812  26.910  1.00 19.30           C  
ANISOU 3796  CG  LEU B 190     2818   2019   2497    300    453    -31       C  
ATOM   3797  CD1 LEU B 190      40.629  57.610  26.172  1.00 20.66           C  
ANISOU 3797  CD1 LEU B 190     2684   2390   2777    175    645     70       C  
ATOM   3798  CD2 LEU B 190      38.845  59.251  26.788  1.00 20.26           C  
ANISOU 3798  CD2 LEU B 190     3110   1835   2753    427    378     -2       C  
ATOM   3799  N   LEU B 191      35.355  56.208  25.262  1.00 15.14           N  
ANISOU 3799  N   LEU B 191     2827   1382   1545    341    -37   -113       N  
ATOM   3800  CA  LEU B 191      34.600  55.275  24.450  1.00 15.69           C  
ANISOU 3800  CA  LEU B 191     2652   1550   1758    358    177    -93       C  
ATOM   3801  C   LEU B 191      35.570  54.515  23.564  1.00 16.40           C  
ANISOU 3801  C   LEU B 191     2624   1732   1874    355    391    -60       C  
ATOM   3802  O   LEU B 191      36.504  55.089  23.005  1.00 18.04           O  
ANISOU 3802  O   LEU B 191     2809   1923   2124    352    532    -12       O  
ATOM   3803  CB  LEU B 191      33.556  55.998  23.598  1.00 16.44           C  
ANISOU 3803  CB  LEU B 191     2630   1717   1900    673    249    209       C  
ATOM   3804  CG  LEU B 191      32.473  56.741  24.378  1.00 18.55           C  
ANISOU 3804  CG  LEU B 191     2854   2062   2132    692    328    591       C  
ATOM   3805  CD1 LEU B 191      31.547  57.478  23.423  1.00 19.79           C  
ANISOU 3805  CD1 LEU B 191     3027   2161   2332    905    288    738       C  
ATOM   3806  CD2 LEU B 191      31.688  55.773  25.244  1.00 21.53           C  
ANISOU 3806  CD2 LEU B 191     3065   2665   2452    421    260    728       C  
ATOM   3807  N   SER B 192      35.359  53.212  23.467  1.00 15.71           N  
ANISOU 3807  N   SER B 192     2600   1560   1811    440    340    -45       N  
ATOM   3808  CA  SER B 192      36.136  52.384  22.573  1.00 15.44           C  
ANISOU 3808  CA  SER B 192     2534   1543   1790    494    163     50       C  
ATOM   3809  C   SER B 192      35.162  51.610  21.708  1.00 14.33           C  
ANISOU 3809  C   SER B 192     2471   1412   1564    219    297    201       C  
ATOM   3810  O   SER B 192      34.555  50.645  22.148  1.00 15.53           O  
ANISOU 3810  O   SER B 192     2700   1476   1725    113    235    238       O  
ATOM   3811  CB  SER B 192      37.042  51.446  23.366  1.00 16.11           C  
ANISOU 3811  CB  SER B 192     2710   1465   1947    870      7    127       C  
ATOM   3812  OG  SER B 192      37.775  50.624  22.473  1.00 17.78           O  
ANISOU 3812  OG  SER B 192     2826   1852   2079    616    134     -6       O  
ATOM   3813  N   VAL B 193      34.998  52.048  20.471  1.00 14.19           N  
ANISOU 3813  N   VAL B 193     2475   1464   1454    254    204     57       N  
ATOM   3814  CA  VAL B 193      33.929  51.541  19.639  1.00 15.06           C  
ANISOU 3814  CA  VAL B 193     2446   1656   1619    468    197      9       C  
ATOM   3815  C   VAL B 193      34.497  50.717  18.505  1.00 14.94           C  
ANISOU 3815  C   VAL B 193     2414   1641   1620    167    281   -100       C  
ATOM   3816  O   VAL B 193      35.475  51.115  17.874  1.00 16.25           O  
ANISOU 3816  O   VAL B 193     2566   1801   1807     13    527     59       O  
ATOM   3817  CB  VAL B 193      33.078  52.695  19.062  1.00 16.00           C  
ANISOU 3817  CB  VAL B 193     2488   1889   1704    713     -6    -71       C  
ATOM   3818  CG1 VAL B 193      32.018  52.168  18.110  1.00 17.65           C  
ANISOU 3818  CG1 VAL B 193     2745   2277   1685    634     77    -90       C  
ATOM   3819  CG2 VAL B 193      32.432  53.468  20.206  1.00 17.02           C  
ANISOU 3819  CG2 VAL B 193     2528   2122   1815    674     17   -218       C  
ATOM   3820  N   LEU B 194      33.900  49.554  18.281  1.00 14.33           N  
ANISOU 3820  N   LEU B 194     2292   1533   1618    202     54   -351       N  
ATOM   3821  CA  LEU B 194      34.183  48.780  17.085  1.00 14.55           C  
ANISOU 3821  CA  LEU B 194     2262   1400   1866    242    106   -274       C  
ATOM   3822  C   LEU B 194      33.122  49.087  16.038  1.00 15.26           C  
ANISOU 3822  C   LEU B 194     2201   1814   1781    229    101     -7       C  
ATOM   3823  O   LEU B 194      31.952  48.774  16.227  1.00 16.98           O  
ANISOU 3823  O   LEU B 194     2465   2129   1859      0     28    297       O  
ATOM   3824  CB  LEU B 194      34.212  47.290  17.412  1.00 14.89           C  
ANISOU 3824  CB  LEU B 194     2364   1043   2252    207    207   -341       C  
ATOM   3825  CG  LEU B 194      34.535  46.343  16.251  1.00 17.42           C  
ANISOU 3825  CG  LEU B 194     2609   1399   2611     42    484   -187       C  
ATOM   3826  CD1 LEU B 194      35.924  46.607  15.727  1.00 20.04           C  
ANISOU 3826  CD1 LEU B 194     2856   2012   2747      3    571   -243       C  
ATOM   3827  CD2 LEU B 194      34.402  44.891  16.696  1.00 19.26           C  
ANISOU 3827  CD2 LEU B 194     2930   1586   2802    -72    370    202       C  
ATOM   3828  N  ASER B 195      33.531  49.723  14.944  0.62 14.66           N  
ANISOU 3828  N  ASER B 195     2140   1763   1669    223    326     34       N  
ATOM   3829  N  BSER B 195      33.542  49.700  14.937  0.38 14.68           N  
ANISOU 3829  N  BSER B 195     2107   1763   1707    186    227     80       N  
ATOM   3830  CA ASER B 195      32.620  50.029  13.845  0.62 14.68           C  
ANISOU 3830  CA ASER B 195     2168   1693   1717    203    415   -107       C  
ATOM   3831  CA BSER B 195      32.641  50.030  13.838  0.38 14.73           C  
ANISOU 3831  CA BSER B 195     2126   1736   1734     48    258     54       C  
ATOM   3832  C  ASER B 195      33.014  49.162  12.661  0.62 14.24           C  
ANISOU 3832  C  ASER B 195     2046   1706   1659    203    199    -67       C  
ATOM   3833  C  BSER B 195      33.017  49.182  12.635  0.38 14.07           C  
ANISOU 3833  C  BSER B 195     2023   1674   1649    130    138     23       C  
ATOM   3834  O  ASER B 195      34.186  49.105  12.298  0.62 14.30           O  
ANISOU 3834  O  ASER B 195     1894   1840   1699    235    113    -24       O  
ATOM   3835  O  BSER B 195      34.180  49.152  12.236  0.38 13.86           O  
ANISOU 3835  O  BSER B 195     1885   1746   1634    123      8     37       O  
ATOM   3836  CB ASER B 195      32.672  51.512  13.457  0.62 16.32           C  
ANISOU 3836  CB ASER B 195     2550   1756   1895    428    472   -152       C  
ATOM   3837  CB BSER B 195      32.722  51.519  13.494  0.38 16.22           C  
ANISOU 3837  CB BSER B 195     2425   1855   1881    -45    249     99       C  
ATOM   3838  OG ASER B 195      32.214  52.361  14.501  0.62 16.94           O  
ANISOU 3838  OG ASER B 195     2770   1743   1924    665    523   -247       O  
ATOM   3839  OG BSER B 195      31.828  51.870  12.452  0.38 17.06           O  
ANISOU 3839  OG BSER B 195     2614   1918   1950   -133    218     75       O  
ATOM   3840  N   THR B 196      32.043  48.490  12.058  1.00 13.85           N  
ANISOU 3840  N   THR B 196     2129   1486   1649    220    323      6       N  
ATOM   3841  CA  THR B 196      32.354  47.551  10.991  1.00 13.76           C  
ANISOU 3841  CA  THR B 196     2162   1419   1645    332    393     28       C  
ATOM   3842  C   THR B 196      31.255  47.435   9.950  1.00 14.02           C  
ANISOU 3842  C   THR B 196     2034   1576   1716    350    319    -38       C  
ATOM   3843  O   THR B 196      30.077  47.642  10.248  1.00 15.02           O  
ANISOU 3843  O   THR B 196     2081   1823   1804    339    450     11       O  
ATOM   3844  CB  THR B 196      32.653  46.147  11.587  1.00 14.32           C  
ANISOU 3844  CB  THR B 196     2243   1516   1681    410    643      5       C  
ATOM   3845  OG1 THR B 196      33.125  45.260  10.562  1.00 14.21           O  
ANISOU 3845  OG1 THR B 196     2101   1552   1746    476    356   -205       O  
ATOM   3846  CG2 THR B 196      31.406  45.534  12.227  1.00 15.37           C  
ANISOU 3846  CG2 THR B 196     2326   1555   1957     61    824     45       C  
ATOM   3847  N   LEU B 197      31.657  47.112   8.719  1.00 13.06           N  
ANISOU 3847  N   LEU B 197     2140   1347   1476    352    196     44       N  
ATOM   3848  CA  LEU B 197      30.716  46.741   7.670  1.00 14.60           C  
ANISOU 3848  CA  LEU B 197     2144   1748   1656    125    266    209       C  
ATOM   3849  C   LEU B 197      30.393  45.239   7.736  1.00 14.62           C  
ANISOU 3849  C   LEU B 197     2010   1712   1834    122    180    105       C  
ATOM   3850  O   LEU B 197      29.482  44.762   7.048  1.00 16.01           O  
ANISOU 3850  O   LEU B 197     2066   2063   1955    213     22     82       O  
ATOM   3851  CB  LEU B 197      31.280  47.125   6.290  1.00 14.78           C  
ANISOU 3851  CB  LEU B 197     2306   1658   1653    390    523    236       C  
ATOM   3852  CG  LEU B 197      31.427  48.642   6.133  1.00 16.77           C  
ANISOU 3852  CG  LEU B 197     2637   1884   1851    602    495    488       C  
ATOM   3853  CD1 LEU B 197      32.303  48.980   4.947  1.00 17.63           C  
ANISOU 3853  CD1 LEU B 197     2893   1864   1942    479    611    539       C  
ATOM   3854  CD2 LEU B 197      30.064  49.286   5.984  1.00 20.11           C  
ANISOU 3854  CD2 LEU B 197     2931   2620   2089    787    447    523       C  
ATOM   3855  N   ASP B 198      31.142  44.514   8.574  1.00 14.15           N  
ANISOU 3855  N   ASP B 198     1922   1582   1873    336    412     92       N  
ATOM   3856  CA  ASP B 198      31.008  43.058   8.745  1.00 14.23           C  
ANISOU 3856  CA  ASP B 198     1763   1730   1914     18    413      7       C  
ATOM   3857  C   ASP B 198      30.805  42.369   7.407  1.00 14.27           C  
ANISOU 3857  C   ASP B 198     1749   1794   1880    153    290    -33       C  
ATOM   3858  O   ASP B 198      29.841  41.627   7.218  1.00 15.16           O  
ANISOU 3858  O   ASP B 198     1756   2001   2004   -233     98   -135       O  
ATOM   3859  CB  ASP B 198      29.855  42.728   9.713  1.00 14.68           C  
ANISOU 3859  CB  ASP B 198     1857   1721   2000    -13    526     92       C  
ATOM   3860  CG  ASP B 198      29.829  41.258  10.136  1.00 16.15           C  
ANISOU 3860  CG  ASP B 198     2079   1932   2126    -43    365     78       C  
ATOM   3861  OD1 ASP B 198      30.862  40.566   9.981  1.00 16.56           O  
ANISOU 3861  OD1 ASP B 198     2137   1822   2334    143     57    174       O  
ATOM   3862  OD2 ASP B 198      28.771  40.808  10.634  1.00 17.93           O  
ANISOU 3862  OD2 ASP B 198     2473   2212   2127      4    199    -52       O  
ATOM   3863  N   VAL B 199      31.702  42.648   6.467  1.00 13.65           N  
ANISOU 3863  N   VAL B 199     1786   1675   1725    402    255    100       N  
ATOM   3864  CA  VAL B 199      31.638  42.033   5.147  1.00 13.71           C  
ANISOU 3864  CA  VAL B 199     1789   1606   1815     66    256     25       C  
ATOM   3865  C   VAL B 199      32.205  40.623   5.141  1.00 13.56           C  
ANISOU 3865  C   VAL B 199     1564   1591   1998   -194    156   -147       C  
ATOM   3866  O   VAL B 199      33.341  40.405   5.555  1.00 14.80           O  
ANISOU 3866  O   VAL B 199     1645   1806   2171    -81    210     21       O  
ATOM   3867  CB  VAL B 199      32.412  42.861   4.091  1.00 13.33           C  
ANISOU 3867  CB  VAL B 199     1796   1417   1851    -51    516    -93       C  
ATOM   3868  CG1 VAL B 199      32.455  42.114   2.755  1.00 13.18           C  
ANISOU 3868  CG1 VAL B 199     1882   1262   1864     61    387   -316       C  
ATOM   3869  CG2 VAL B 199      31.786  44.234   3.929  1.00 13.27           C  
ANISOU 3869  CG2 VAL B 199     1736   1264   2042    275    446    -76       C  
ATOM   3870  N   LYS B 200      31.397  39.669   4.690  1.00 14.70           N  
ANISOU 3870  N   LYS B 200     1747   1777   2061   -128     67   -355       N  
ATOM   3871  CA  LYS B 200      31.906  38.364   4.278  1.00 14.41           C  
ANISOU 3871  CA  LYS B 200     1612   1768   2096    284     74   -183       C  
ATOM   3872  C   LYS B 200      30.843  37.615   3.506  1.00 15.31           C  
ANISOU 3872  C   LYS B 200     1712   1913   2194      8    253   -211       C  
ATOM   3873  O   LYS B 200      29.765  37.324   4.026  1.00 15.70           O  
ANISOU 3873  O   LYS B 200     1817   2192   1955     52    391   -308       O  
ATOM   3874  CB  LYS B 200      32.364  37.513   5.471  1.00 15.27           C  
ANISOU 3874  CB  LYS B 200     1701   1838   2262    132    450     28       C  
ATOM   3875  CG  LYS B 200      32.873  36.128   5.081  1.00 14.96           C  
ANISOU 3875  CG  LYS B 200     1446   1881   2355   -104    701    -60       C  
ATOM   3876  CD  LYS B 200      34.156  36.187   4.254  1.00 15.54           C  
ANISOU 3876  CD  LYS B 200     1640   1823   2443     99    631    -53       C  
ATOM   3877  CE  LYS B 200      34.630  34.780   3.894  1.00 16.15           C  
ANISOU 3877  CE  LYS B 200     1747   2054   2333    422    699   -137       C  
ATOM   3878  NZ  LYS B 200      35.929  34.838   3.170  1.00 15.51           N  
ANISOU 3878  NZ  LYS B 200     1811   1719   2363     10    619     19       N  
ATOM   3879  N   SER B 201      31.150  37.302   2.253  1.00 15.06           N  
ANISOU 3879  N   SER B 201     1620   1903   2198   -191    405   -211       N  
ATOM   3880  CA  SER B 201      30.353  36.353   1.498  1.00 16.18           C  
ANISOU 3880  CA  SER B 201     1912   1840   2394    -90    246   -186       C  
ATOM   3881  C   SER B 201      31.302  35.288   0.974  1.00 16.32           C  
ANISOU 3881  C   SER B 201     1700   2079   2423   -239    372   -273       C  
ATOM   3882  O   SER B 201      32.503  35.515   0.843  1.00 18.67           O  
ANISOU 3882  O   SER B 201     1984   2356   2752   -171    522   -456       O  
ATOM   3883  CB  SER B 201      29.593  37.028   0.353  1.00 19.58           C  
ANISOU 3883  CB  SER B 201     2403   2445   2593   -232    160     50       C  
ATOM   3884  OG  SER B 201      30.442  37.295  -0.753  1.00 19.40           O  
ANISOU 3884  OG  SER B 201     2381   2496   2493   -245    414    189       O  
ATOM   3885  N   PHE B 202      30.768  34.111   0.702  1.00 15.39           N  
ANISOU 3885  N   PHE B 202     1862   1723   2261   -223    197   -256       N  
ATOM   3886  CA  PHE B 202      31.573  33.065   0.102  1.00 15.84           C  
ANISOU 3886  CA  PHE B 202     1846   1715   2456   -128    352   -120       C  
ATOM   3887  C   PHE B 202      31.197  32.973  -1.361  1.00 16.82           C  
ANISOU 3887  C   PHE B 202     1731   2132   2527   -214    226   -307       C  
ATOM   3888  O   PHE B 202      30.028  32.822  -1.689  1.00 18.53           O  
ANISOU 3888  O   PHE B 202     1905   2371   2764    -68    230   -300       O  
ATOM   3889  CB  PHE B 202      31.358  31.735   0.820  1.00 16.81           C  
ANISOU 3889  CB  PHE B 202     1958   1857   2572   -430    236     51       C  
ATOM   3890  CG  PHE B 202      31.899  31.721   2.211  1.00 16.24           C  
ANISOU 3890  CG  PHE B 202     1980   1674   2518   -350    235     62       C  
ATOM   3891  CD1 PHE B 202      33.178  31.249   2.468  1.00 16.37           C  
ANISOU 3891  CD1 PHE B 202     2038   1579   2604   -178    520   -121       C  
ATOM   3892  CD2 PHE B 202      31.150  32.218   3.267  1.00 18.04           C  
ANISOU 3892  CD2 PHE B 202     2224   1948   2681   -494    166    -60       C  
ATOM   3893  CE1 PHE B 202      33.687  31.241   3.749  1.00 16.76           C  
ANISOU 3893  CE1 PHE B 202     2114   1590   2664   -189    432   -210       C  
ATOM   3894  CE2 PHE B 202      31.659  32.218   4.559  1.00 17.88           C  
ANISOU 3894  CE2 PHE B 202     2261   1800   2732   -406    169   -177       C  
ATOM   3895  CZ  PHE B 202      32.928  31.733   4.798  1.00 17.78           C  
ANISOU 3895  CZ  PHE B 202     2248   1756   2752   -471    313   -116       C  
ATOM   3896  N   PRO B 203      32.188  33.105  -2.250  1.00 17.75           N  
ANISOU 3896  N   PRO B 203     1501   2693   2551   -374     65   -608       N  
ATOM   3897  CA  PRO B 203      31.948  33.066  -3.694  1.00 18.95           C  
ANISOU 3897  CA  PRO B 203     1702   2884   2613   -571    108   -691       C  
ATOM   3898  C   PRO B 203      31.849  31.637  -4.221  1.00 21.16           C  
ANISOU 3898  C   PRO B 203     2207   3014   2819   -290    165   -781       C  
ATOM   3899  O   PRO B 203      32.048  30.683  -3.468  1.00 20.81           O  
ANISOU 3899  O   PRO B 203     2332   2714   2861   -365     16   -802       O  
ATOM   3900  CB  PRO B 203      33.178  33.781  -4.259  1.00 18.45           C  
ANISOU 3900  CB  PRO B 203     1454   2939   2618   -657    211   -722       C  
ATOM   3901  CG  PRO B 203      34.265  33.415  -3.297  1.00 17.88           C  
ANISOU 3901  CG  PRO B 203     1361   2860   2574   -540     72   -685       C  
ATOM   3902  CD  PRO B 203      33.609  33.335  -1.935  1.00 17.45           C  
ANISOU 3902  CD  PRO B 203     1328   2724   2577   -496     98   -774       C  
ATOM   3903  N   PRO B 204      31.519  31.484  -5.508  1.00 23.66           N  
ANISOU 3903  N   PRO B 204     2512   3360   3120   -216    183   -889       N  
ATOM   3904  CA  PRO B 204      31.677  30.170  -6.137  1.00 25.45           C  
ANISOU 3904  CA  PRO B 204     2806   3447   3415   -291    104  -1031       C  
ATOM   3905  C   PRO B 204      33.103  29.659  -5.923  1.00 27.82           C  
ANISOU 3905  C   PRO B 204     3070   3628   3871   -331    348  -1100       C  
ATOM   3906  O   PRO B 204      33.996  30.482  -5.739  1.00 28.12           O  
ANISOU 3906  O   PRO B 204     3053   3575   4058   -368    799  -1269       O  
ATOM   3907  CB  PRO B 204      31.387  30.454  -7.612  1.00 25.96           C  
ANISOU 3907  CB  PRO B 204     2913   3648   3303   -101     15   -780       C  
ATOM   3908  CG  PRO B 204      30.446  31.605  -7.583  1.00 25.87           C  
ANISOU 3908  CG  PRO B 204     2953   3625   3249    -68    -71   -754       C  
ATOM   3909  CD  PRO B 204      30.866  32.452  -6.406  1.00 24.07           C  
ANISOU 3909  CD  PRO B 204     2677   3303   3165     -8     91   -708       C  
ATOM   3910  N   PRO B 205      33.334  28.338  -5.977  1.00 29.71           N  
ANISOU 3910  N   PRO B 205     3442   3657   4191   -438     84  -1069       N  
ATOM   3911  CA  PRO B 205      32.473  27.244  -6.445  1.00 31.11           C  
ANISOU 3911  CA  PRO B 205     3608   3881   4330   -543    -91   -931       C  
ATOM   3912  C   PRO B 205      31.274  26.905  -5.560  1.00 31.77           C  
ANISOU 3912  C   PRO B 205     3664   4179   4230   -764   -126   -882       C  
ATOM   3913  O   PRO B 205      30.193  26.689  -6.105  1.00 34.10           O  
ANISOU 3913  O   PRO B 205     3883   4729   4346  -1006   -219   -831       O  
ATOM   3914  CB  PRO B 205      33.439  26.047  -6.503  1.00 31.49           C  
ANISOU 3914  CB  PRO B 205     3690   3791   4483   -392    -32   -990       C  
ATOM   3915  CG  PRO B 205      34.819  26.644  -6.477  1.00 31.82           C  
ANISOU 3915  CG  PRO B 205     3804   3750   4535   -321     58   -959       C  
ATOM   3916  CD  PRO B 205      34.665  27.839  -5.596  1.00 30.46           C  
ANISOU 3916  CD  PRO B 205     3615   3592   4367   -551    -54  -1057       C  
ATOM   3917  N   HIS B 206      31.438  26.863  -4.241  1.00 28.99           N  
ANISOU 3917  N   HIS B 206     3502   3503   4011   -648     -7  -1070       N  
ATOM   3918  CA  HIS B 206      30.380  26.309  -3.397  1.00 28.20           C  
ANISOU 3918  CA  HIS B 206     3431   3244   4038   -427    -12  -1009       C  
ATOM   3919  C   HIS B 206      29.709  27.327  -2.479  1.00 26.91           C  
ANISOU 3919  C   HIS B 206     3185   3090   3948   -278    208  -1068       C  
ATOM   3920  O   HIS B 206      28.778  26.977  -1.752  1.00 28.98           O  
ANISOU 3920  O   HIS B 206     3549   3289   4174   -249    290   -993       O  
ATOM   3921  CB  HIS B 206      30.935  25.140  -2.572  1.00 28.93           C  
ANISOU 3921  CB  HIS B 206     3557   3260   4176   -378    -71   -812       C  
ATOM   3922  CG  HIS B 206      31.597  24.087  -3.404  1.00 30.01           C  
ANISOU 3922  CG  HIS B 206     3669   3323   4411   -426   -264   -651       C  
ATOM   3923  ND1 HIS B 206      31.038  23.596  -4.564  1.00 30.29           N  
ANISOU 3923  ND1 HIS B 206     3709   3323   4478   -426   -391   -559       N  
ATOM   3924  CD2 HIS B 206      32.777  23.442  -3.250  1.00 31.29           C  
ANISOU 3924  CD2 HIS B 206     3824   3498   4568   -483   -351   -517       C  
ATOM   3925  CE1 HIS B 206      31.844  22.692  -5.088  1.00 31.00           C  
ANISOU 3925  CE1 HIS B 206     3794   3449   4537   -455   -363   -494       C  
ATOM   3926  NE2 HIS B 206      32.906  22.577  -4.310  1.00 31.62           N  
ANISOU 3926  NE2 HIS B 206     3841   3553   4620   -478   -282   -525       N  
ATOM   3927  N   GLY B 207      30.166  28.577  -2.509  1.00 23.81           N  
ANISOU 3927  N   GLY B 207     2627   2788   3632   -411    -35  -1046       N  
ATOM   3928  CA  GLY B 207      29.527  29.613  -1.712  1.00 21.48           C  
ANISOU 3928  CA  GLY B 207     2304   2597   3261   -444   -242  -1058       C  
ATOM   3929  C   GLY B 207      28.358  30.236  -2.459  1.00 20.36           C  
ANISOU 3929  C   GLY B 207     2097   2559   3080   -535   -331  -1074       C  
ATOM   3930  O   GLY B 207      28.306  30.179  -3.685  1.00 21.67           O  
ANISOU 3930  O   GLY B 207     2349   2806   3079   -256   -248  -1175       O  
ATOM   3931  N   ASP B 208      27.419  30.837  -1.731  1.00 19.73           N  
ANISOU 3931  N   ASP B 208     1835   2615   3045   -423   -261   -596       N  
ATOM   3932  CA  ASP B 208      26.226  31.397  -2.364  1.00 19.90           C  
ANISOU 3932  CA  ASP B 208     1916   2652   2993   -360   -145   -274       C  
ATOM   3933  C   ASP B 208      26.227  32.929  -2.441  1.00 20.10           C  
ANISOU 3933  C   ASP B 208     1850   2768   3020   -465     20   -161       C  
ATOM   3934  O   ASP B 208      25.202  33.539  -2.756  1.00 21.82           O  
ANISOU 3934  O   ASP B 208     2037   3039   3213   -470     81   -134       O  
ATOM   3935  CB  ASP B 208      24.955  30.913  -1.644  1.00 20.39           C  
ANISOU 3935  CB  ASP B 208     2070   2719   2960   -376   -100   -205       C  
ATOM   3936  CG  ASP B 208      24.868  31.371  -0.191  1.00 21.74           C  
ANISOU 3936  CG  ASP B 208     2251   2924   3085   -459    218    -66       C  
ATOM   3937  OD1 ASP B 208      25.650  32.249   0.242  1.00 21.15           O  
ANISOU 3937  OD1 ASP B 208     2116   2870   3052   -235    235     29       O  
ATOM   3938  OD2 ASP B 208      23.979  30.856   0.524  1.00 22.24           O  
ANISOU 3938  OD2 ASP B 208     2241   3040   3171   -706    490   -178       O  
ATOM   3939  N   LEU B 209      27.371  33.536  -2.134  1.00 18.93           N  
ANISOU 3939  N   LEU B 209     1537   2899   2757   -404      4   -176       N  
ATOM   3940  CA  LEU B 209      27.570  34.986  -2.259  1.00 18.43           C  
ANISOU 3940  CA  LEU B 209     1488   2944   2571   -237     30     -2       C  
ATOM   3941  C   LEU B 209      26.687  35.844  -1.349  1.00 18.16           C  
ANISOU 3941  C   LEU B 209     1610   2670   2619   -167      9   -123       C  
ATOM   3942  O   LEU B 209      26.695  37.075  -1.459  1.00 18.05           O  
ANISOU 3942  O   LEU B 209     1715   2504   2639      7    127     -5       O  
ATOM   3943  CB  LEU B 209      27.367  35.422  -3.715  1.00 19.51           C  
ANISOU 3943  CB  LEU B 209     1615   3287   2512   -288    -58     52       C  
ATOM   3944  CG  LEU B 209      28.500  35.007  -4.652  1.00 20.48           C  
ANISOU 3944  CG  LEU B 209     1892   3534   2356   -334   -141    -19       C  
ATOM   3945  CD1 LEU B 209      28.057  35.155  -6.096  1.00 21.69           C  
ANISOU 3945  CD1 LEU B 209     2092   3822   2326   -352   -361   -151       C  
ATOM   3946  CD2 LEU B 209      29.727  35.850  -4.394  1.00 21.55           C  
ANISOU 3946  CD2 LEU B 209     1885   3842   2461   -271   -206     42       C  
ATOM   3947  N   VAL B 210      25.939  35.219  -0.444  1.00 18.61           N  
ANISOU 3947  N   VAL B 210     1772   2767   2533   -228     60   -405       N  
ATOM   3948  CA  VAL B 210      25.165  36.002   0.514  1.00 17.73           C  
ANISOU 3948  CA  VAL B 210     1659   2721   2357   -258    243   -462       C  
ATOM   3949  C   VAL B 210      26.098  36.544   1.593  1.00 16.11           C  
ANISOU 3949  C   VAL B 210     1619   2211   2291   -248    134   -361       C  
ATOM   3950  O   VAL B 210      26.852  35.807   2.230  1.00 16.48           O  
ANISOU 3950  O   VAL B 210     1720   2259   2282   -218    -16   -112       O  
ATOM   3951  CB  VAL B 210      24.030  35.189   1.160  1.00 17.95           C  
ANISOU 3951  CB  VAL B 210     1597   2917   2307   -443    353   -385       C  
ATOM   3952  CG1 VAL B 210      23.274  36.045   2.157  1.00 18.60           C  
ANISOU 3952  CG1 VAL B 210     1535   2989   2543   -249    442   -252       C  
ATOM   3953  CG2 VAL B 210      23.077  34.656   0.084  1.00 19.32           C  
ANISOU 3953  CG2 VAL B 210     1683   3240   2418   -461    243   -495       C  
ATOM   3954  N   ASN B 211      26.023  37.853   1.788  1.00 15.14           N  
ANISOU 3954  N   ASN B 211     1727   1906   2118   -378    190   -570       N  
ATOM   3955  CA  ASN B 211      26.932  38.571   2.663  1.00 15.22           C  
ANISOU 3955  CA  ASN B 211     1963   1652   2168   -470    394   -316       C  
ATOM   3956  C   ASN B 211      26.486  38.496   4.118  1.00 15.89           C  
ANISOU 3956  C   ASN B 211     1974   1795   2268   -274    202   -217       C  
ATOM   3957  O   ASN B 211      25.890  39.428   4.654  1.00 16.11           O  
ANISOU 3957  O   ASN B 211     1948   1953   2221    -56    230   -148       O  
ATOM   3958  CB  ASN B 211      27.018  40.014   2.176  1.00 16.02           C  
ANISOU 3958  CB  ASN B 211     2210   1529   2348   -340    385   -285       C  
ATOM   3959  CG  ASN B 211      27.918  40.878   3.026  1.00 16.52           C  
ANISOU 3959  CG  ASN B 211     2176   1726   2374    -99    327   -274       C  
ATOM   3960  OD1 ASN B 211      28.767  40.386   3.769  1.00 17.54           O  
ANISOU 3960  OD1 ASN B 211     2327   1764   2573     98    129    -94       O  
ATOM   3961  ND2 ASN B 211      27.731  42.188   2.917  1.00 16.90           N  
ANISOU 3961  ND2 ASN B 211     2207   1924   2291   -211    402    -20       N  
ATOM   3962  N   ARG B 212      26.778  37.373   4.758  1.00 15.82           N  
ANISOU 3962  N   ARG B 212     1893   1782   2334   -495    224   -173       N  
ATOM   3963  CA  ARG B 212      26.272  37.135   6.095  1.00 15.83           C  
ANISOU 3963  CA  ARG B 212     1758   1930   2328   -397    257   -247       C  
ATOM   3964  C   ARG B 212      27.182  37.659   7.206  1.00 16.60           C  
ANISOU 3964  C   ARG B 212     1698   2203   2405   -368    272   -252       C  
ATOM   3965  O   ARG B 212      26.757  37.766   8.354  1.00 17.22           O  
ANISOU 3965  O   ARG B 212     1748   2604   2190   -494    184    -86       O  
ATOM   3966  CB  ARG B 212      26.028  35.642   6.286  1.00 16.70           C  
ANISOU 3966  CB  ARG B 212     1861   1958   2526   -482    223   -219       C  
ATOM   3967  CG  ARG B 212      24.972  35.089   5.355  1.00 17.40           C  
ANISOU 3967  CG  ARG B 212     1852   2170   2590   -504    380   -287       C  
ATOM   3968  CD  ARG B 212      24.630  33.646   5.702  1.00 18.54           C  
ANISOU 3968  CD  ARG B 212     1926   2311   2809   -706    307   -361       C  
ATOM   3969  NE  ARG B 212      23.627  33.114   4.786  1.00 21.09           N  
ANISOU 3969  NE  ARG B 212     2112   2667   3233   -745    409   -241       N  
ATOM   3970  CZ  ARG B 212      23.914  32.532   3.626  1.00 22.01           C  
ANISOU 3970  CZ  ARG B 212     2254   2722   3385   -776    370   -192       C  
ATOM   3971  NH1 ARG B 212      25.179  32.380   3.252  1.00 21.20           N  
ANISOU 3971  NH1 ARG B 212     2104   2589   3361   -558    366    -73       N  
ATOM   3972  NH2 ARG B 212      22.937  32.093   2.844  1.00 23.64           N  
ANISOU 3972  NH2 ARG B 212     2502   2966   3514   -959    330   -189       N  
ATOM   3973  N   GLY B 213      28.424  37.994   6.869  1.00 17.12           N  
ANISOU 3973  N   GLY B 213     1872   2120   2513     -1    188    -49       N  
ATOM   3974  CA  GLY B 213      29.353  38.492   7.867  1.00 16.80           C  
ANISOU 3974  CA  GLY B 213     2002   1831   2550    237    135    -63       C  
ATOM   3975  C   GLY B 213      29.968  37.388   8.705  1.00 16.80           C  
ANISOU 3975  C   GLY B 213     2004   1788   2590    153    304    -32       C  
ATOM   3976  O   GLY B 213      29.867  36.213   8.349  1.00 19.37           O  
ANISOU 3976  O   GLY B 213     2281   2077   3001    -81    230    224       O  
ATOM   3977  N   GLU B 214      30.599  37.765   9.814  1.00 15.42           N  
ANISOU 3977  N   GLU B 214     1822   1744   2292    345    341    250       N  
ATOM   3978  CA  GLU B 214      31.424  36.842  10.586  1.00 15.96           C  
ANISOU 3978  CA  GLU B 214     1806   2055   2204    337    432    241       C  
ATOM   3979  C   GLU B 214      31.137  36.877  12.081  1.00 17.06           C  
ANISOU 3979  C   GLU B 214     1806   2294   2383    -76    542    329       C  
ATOM   3980  O   GLU B 214      31.927  36.365  12.869  1.00 18.69           O  
ANISOU 3980  O   GLU B 214     1916   2812   2374    357    469    483       O  
ATOM   3981  CB  GLU B 214      32.909  37.153  10.346  1.00 16.17           C  
ANISOU 3981  CB  GLU B 214     1818   2173   2152    305    355    162       C  
ATOM   3982  CG  GLU B 214      33.317  36.969   8.891  1.00 17.79           C  
ANISOU 3982  CG  GLU B 214     1956   2686   2116    -25    680   -137       C  
ATOM   3983  CD  GLU B 214      34.699  37.511   8.550  1.00 21.27           C  
ANISOU 3983  CD  GLU B 214     2608   3089   2383    -78    617    -89       C  
ATOM   3984  OE1 GLU B 214      35.458  37.859   9.472  1.00 24.41           O  
ANISOU 3984  OE1 GLU B 214     2909   3459   2906    -54    640   -136       O  
ATOM   3985  OE2 GLU B 214      35.018  37.588   7.339  1.00 22.24           O  
ANISOU 3985  OE2 GLU B 214     2809   3131   2508     54    671    115       O  
ATOM   3986  N   LEU B 215      30.016  37.473  12.476  1.00 16.50           N  
ANISOU 3986  N   LEU B 215     1959   2024   2288   -160    482     38       N  
ATOM   3987  CA  LEU B 215      29.752  37.680  13.896  1.00 17.10           C  
ANISOU 3987  CA  LEU B 215     2222   2103   2170   -221    359    117       C  
ATOM   3988  C   LEU B 215      28.871  36.608  14.556  1.00 17.03           C  
ANISOU 3988  C   LEU B 215     2246   2113   2111   -483    415    -77       C  
ATOM   3989  O   LEU B 215      28.648  36.658  15.766  1.00 19.33           O  
ANISOU 3989  O   LEU B 215     2563   2544   2239   -619    427     39       O  
ATOM   3990  CB  LEU B 215      29.143  39.072  14.095  1.00 16.77           C  
ANISOU 3990  CB  LEU B 215     2047   2168   2157   -161    270    163       C  
ATOM   3991  CG  LEU B 215      30.216  40.168  14.108  1.00 16.62           C  
ANISOU 3991  CG  LEU B 215     1967   2236   2113    -83     43    375       C  
ATOM   3992  CD1 LEU B 215      29.617  41.553  13.950  1.00 16.38           C  
ANISOU 3992  CD1 LEU B 215     2041   1989   2192   -174     64    250       C  
ATOM   3993  CD2 LEU B 215      31.037  40.102  15.391  1.00 18.11           C  
ANISOU 3993  CD2 LEU B 215     2162   2502   2217     59    -18    275       C  
ATOM   3994  N   GLY B 216      28.394  35.629  13.792  1.00 16.84           N  
ANISOU 3994  N   GLY B 216     2116   2135   2150   -503    520    290       N  
ATOM   3995  CA  GLY B 216      27.576  34.576  14.380  1.00 17.41           C  
ANISOU 3995  CA  GLY B 216     2298   2051   2267   -424    499    306       C  
ATOM   3996  C   GLY B 216      26.301  35.122  15.007  1.00 17.87           C  
ANISOU 3996  C   GLY B 216     2427   2071   2291   -451    530    275       C  
ATOM   3997  O   GLY B 216      25.789  36.149  14.582  1.00 19.32           O  
ANISOU 3997  O   GLY B 216     2604   2258   2478   -298    386     30       O  
ATOM   3998  N   THR B 217      25.797  34.441  16.036  1.00 18.68           N  
ANISOU 3998  N   THR B 217     2601   2276   2219   -285    461    483       N  
ATOM   3999  CA  THR B 217      24.550  34.829  16.700  1.00 18.58           C  
ANISOU 3999  CA  THR B 217     2578   2250   2231   -447    495    368       C  
ATOM   4000  C   THR B 217      24.730  34.800  18.217  1.00 19.01           C  
ANISOU 4000  C   THR B 217     2613   2303   2305   -404    411     94       C  
ATOM   4001  O   THR B 217      25.669  34.189  18.700  1.00 19.50           O  
ANISOU 4001  O   THR B 217     2761   2339   2308   -302    314     24       O  
ATOM   4002  CB  THR B 217      23.388  33.880  16.326  1.00 20.55           C  
ANISOU 4002  CB  THR B 217     3016   2485   2305   -585    151    327       C  
ATOM   4003  OG1 THR B 217      23.640  32.584  16.881  1.00 22.25           O  
ANISOU 4003  OG1 THR B 217     3329   2748   2376   -415    238    388       O  
ATOM   4004  CG2 THR B 217      23.223  33.763  14.814  1.00 21.11           C  
ANISOU 4004  CG2 THR B 217     3146   2595   2280   -760    149    176       C  
ATOM   4005  N   PRO B 218      23.835  35.457  18.979  1.00 19.61           N  
ANISOU 4005  N   PRO B 218     2626   2474   2352   -266    492    382       N  
ATOM   4006  CA  PRO B 218      23.937  35.314  20.440  1.00 20.61           C  
ANISOU 4006  CA  PRO B 218     2775   2719   2337   -148    628    407       C  
ATOM   4007  C   PRO B 218      23.903  33.845  20.900  1.00 22.08           C  
ANISOU 4007  C   PRO B 218     3046   2922   2422   -255    390    704       C  
ATOM   4008  O   PRO B 218      24.633  33.478  21.822  1.00 22.14           O  
ANISOU 4008  O   PRO B 218     3073   3070   2271   -182    227    662       O  
ATOM   4009  CB  PRO B 218      22.712  36.079  20.948  1.00 21.19           C  
ANISOU 4009  CB  PRO B 218     2879   2797   2374   -219    607    272       C  
ATOM   4010  CG  PRO B 218      22.477  37.123  19.893  1.00 21.48           C  
ANISOU 4010  CG  PRO B 218     2882   2910   2371   -368    539    290       C  
ATOM   4011  CD  PRO B 218      22.782  36.413  18.595  1.00 20.54           C  
ANISOU 4011  CD  PRO B 218     2756   2721   2326   -117    363    268       C  
ATOM   4012  N   ASP B 219      23.085  33.020  20.255  1.00 23.12           N  
ANISOU 4012  N   ASP B 219     3196   2884   2705   -420    297    809       N  
ATOM   4013  CA  ASP B 219      23.005  31.604  20.611  1.00 26.09           C  
ANISOU 4013  CA  ASP B 219     3441   3387   3085   -522    273    596       C  
ATOM   4014  C   ASP B 219      24.240  30.832  20.173  1.00 24.95           C  
ANISOU 4014  C   ASP B 219     3331   3164   2987   -487    151    328       C  
ATOM   4015  O   ASP B 219      24.618  29.838  20.796  1.00 24.94           O  
ANISOU 4015  O   ASP B 219     3230   3194   3052   -228    161    358       O  
ATOM   4016  CB  ASP B 219      21.762  30.962  19.995  1.00 30.35           C  
ANISOU 4016  CB  ASP B 219     3773   4085   3673   -816    346    611       C  
ATOM   4017  CG  ASP B 219      20.522  31.179  20.827  1.00 35.73           C  
ANISOU 4017  CG  ASP B 219     4374   4980   4222   -634    181    363       C  
ATOM   4018  OD1 ASP B 219      20.659  31.510  22.026  1.00 36.87           O  
ANISOU 4018  OD1 ASP B 219     4502   5233   4272   -375    296    412       O  
ATOM   4019  OD2 ASP B 219      19.410  31.014  20.284  1.00 38.86           O  
ANISOU 4019  OD2 ASP B 219     4742   5382   4640   -735     82    188       O  
ATOM   4020  N   ARG B 220      24.861  31.285  19.091  1.00 23.99           N  
ANISOU 4020  N   ARG B 220     3306   3010   2799   -513    217     19       N  
ATOM   4021  CA  ARG B 220      26.049  30.626  18.571  1.00 25.55           C  
ANISOU 4021  CA  ARG B 220     3569   3127   3013   -331    286    -20       C  
ATOM   4022  C   ARG B 220      27.098  31.661  18.201  1.00 21.61           C  
ANISOU 4022  C   ARG B 220     3223   2445   2544   -131    500     93       C  
ATOM   4023  O   ARG B 220      27.311  31.947  17.026  1.00 22.24           O  
ANISOU 4023  O   ARG B 220     3348   2420   2683    -87    634     98       O  
ATOM   4024  CB  ARG B 220      25.691  29.761  17.363  1.00 30.94           C  
ANISOU 4024  CB  ARG B 220     4284   3869   3604   -110    322   -280       C  
ATOM   4025  CG  ARG B 220      26.719  28.702  17.023  1.00 36.68           C  
ANISOU 4025  CG  ARG B 220     5066   4573   4297    112    235   -428       C  
ATOM   4026  CD  ARG B 220      26.108  27.616  16.146  1.00 41.38           C  
ANISOU 4026  CD  ARG B 220     5677   5147   4899    401    251   -629       C  
ATOM   4027  NE  ARG B 220      27.133  26.783  15.526  1.00 44.72           N  
ANISOU 4027  NE  ARG B 220     6083   5550   5359    630    218   -789       N  
ATOM   4028  CZ  ARG B 220      27.729  27.079  14.376  1.00 47.50           C  
ANISOU 4028  CZ  ARG B 220     6424   5857   5766    772    138   -863       C  
ATOM   4029  NH1 ARG B 220      27.400  28.186  13.723  1.00 48.41           N  
ANISOU 4029  NH1 ARG B 220     6521   5996   5875    788     78   -903       N  
ATOM   4030  NH2 ARG B 220      28.654  26.269  13.878  1.00 48.85           N  
ANISOU 4030  NH2 ARG B 220     6561   5965   6033    847     82   -840       N  
ATOM   4031  N   PRO B 221      27.754  32.240  19.212  1.00 20.49           N  
ANISOU 4031  N   PRO B 221     3087   2532   2167   -129    573    330       N  
ATOM   4032  CA  PRO B 221      28.648  33.365  18.920  1.00 20.18           C  
ANISOU 4032  CA  PRO B 221     2973   2650   2046   -233    511    273       C  
ATOM   4033  C   PRO B 221      29.965  32.964  18.274  1.00 20.37           C  
ANISOU 4033  C   PRO B 221     2877   2708   2153     27    463    467       C  
ATOM   4034  O   PRO B 221      30.526  31.918  18.584  1.00 23.74           O  
ANISOU 4034  O   PRO B 221     3265   3208   2546    146    465    530       O  
ATOM   4035  CB  PRO B 221      28.893  33.986  20.299  1.00 20.30           C  
ANISOU 4035  CB  PRO B 221     3123   2713   1876   -435    361    183       C  
ATOM   4036  CG  PRO B 221      28.621  32.893  21.274  1.00 21.56           C  
ANISOU 4036  CG  PRO B 221     3363   2834   1995   -653    598    190       C  
ATOM   4037  CD  PRO B 221      27.566  32.027  20.659  1.00 21.17           C  
ANISOU 4037  CD  PRO B 221     3304   2641   2097   -514    496    287       C  
ATOM   4038  N   SER B 222      30.439  33.793  17.351  1.00 20.06           N  
ANISOU 4038  N   SER B 222     2646   2715   2261     54    450    277       N  
ATOM   4039  CA  SER B 222      31.810  33.671  16.906  1.00 20.96           C  
ANISOU 4039  CA  SER B 222     2619   2903   2441     96    555    460       C  
ATOM   4040  C   SER B 222      32.700  34.207  18.013  1.00 21.37           C  
ANISOU 4040  C   SER B 222     2630   2921   2568     37    420    341       C  
ATOM   4041  O   SER B 222      32.220  34.873  18.935  1.00 19.98           O  
ANISOU 4041  O   SER B 222     2643   2487   2462    155    366    207       O  
ATOM   4042  CB  SER B 222      32.045  34.435  15.604  1.00 22.62           C  
ANISOU 4042  CB  SER B 222     2949   3094   2553    244    372    704       C  
ATOM   4043  OG  SER B 222      31.934  35.826  15.814  1.00 23.35           O  
ANISOU 4043  OG  SER B 222     3063   3170   2637    414     97    688       O  
ATOM   4044  N   ASP B 223      33.995  33.932  17.924  1.00 24.27           N  
ANISOU 4044  N   ASP B 223     3064   3202   2956     14    136    369       N  
ATOM   4045  CA  ASP B 223      34.935  34.432  18.918  1.00 27.68           C  
ANISOU 4045  CA  ASP B 223     3559   3523   3434    -49    299    470       C  
ATOM   4046  C   ASP B 223      34.900  35.956  18.969  1.00 26.11           C  
ANISOU 4046  C   ASP B 223     3265   3325   3330   -242    357    778       C  
ATOM   4047  O   ASP B 223      35.061  36.552  20.031  1.00 25.77           O  
ANISOU 4047  O   ASP B 223     3190   3362   3239   -444    277    809       O  
ATOM   4048  CB  ASP B 223      36.353  33.931  18.628  1.00 33.19           C  
ANISOU 4048  CB  ASP B 223     4400   4157   4055   -140    522    486       C  
ATOM   4049  CG  ASP B 223      36.545  32.469  19.009  1.00 38.89           C  
ANISOU 4049  CG  ASP B 223     5276   4858   4642   -190    730    370       C  
ATOM   4050  OD1 ASP B 223      35.836  31.995  19.921  1.00 41.32           O  
ANISOU 4050  OD1 ASP B 223     5733   5079   4885   -157    721    317       O  
ATOM   4051  OD2 ASP B 223      37.406  31.796  18.401  1.00 41.27           O  
ANISOU 4051  OD2 ASP B 223     5571   5223   4886   -265    762    313       O  
ATOM   4052  N  ALYS B 224      34.676  36.580  17.814  0.54 25.87           N  
ANISOU 4052  N  ALYS B 224     3193   3241   3395    -92    436    800       N  
ATOM   4053  N  BLYS B 224      34.664  36.591  17.826  0.46 25.88           N  
ANISOU 4053  N  BLYS B 224     3225   3251   3359   -143    355    773       N  
ATOM   4054  CA ALYS B 224      34.583  38.033  17.741  0.54 25.67           C  
ANISOU 4054  CA ALYS B 224     3215   3101   3435    -24    331    938       C  
ATOM   4055  CA BLYS B 224      34.610  38.045  17.792  0.46 25.64           C  
ANISOU 4055  CA BLYS B 224     3252   3119   3372   -126    194    858       C  
ATOM   4056  C  ALYS B 224      33.384  38.561  18.511  0.54 23.40           C  
ANISOU 4056  C  ALYS B 224     3014   2574   3302    -16     79    851       C  
ATOM   4057  C  BLYS B 224      33.371  38.588  18.494  0.46 23.54           C  
ANISOU 4057  C  BLYS B 224     3029   2656   3261   -100     28    785       C  
ATOM   4058  O  ALYS B 224      33.490  39.558  19.217  0.54 23.57           O  
ANISOU 4058  O  ALYS B 224     3094   2412   3449    -40    -71    720       O  
ATOM   4059  O  BLYS B 224      33.439  39.625  19.146  0.46 23.92           O  
ANISOU 4059  O  BLYS B 224     3096   2608   3386   -165   -101    630       O  
ATOM   4060  CB ALYS B 224      34.509  38.502  16.287  0.54 28.01           C  
ANISOU 4060  CB ALYS B 224     3481   3481   3680     56    389   1124       C  
ATOM   4061  CB BLYS B 224      34.673  38.548  16.350  0.46 27.69           C  
ANISOU 4061  CB BLYS B 224     3507   3449   3564   -107    135    938       C  
ATOM   4062  CG ALYS B 224      35.865  38.760  15.658  0.54 30.43           C  
ANISOU 4062  CG ALYS B 224     3766   3836   3960    186    346   1047       C  
ATOM   4063  CG BLYS B 224      36.099  38.685  15.834  0.46 29.60           C  
ANISOU 4063  CG BLYS B 224     3700   3762   3784    -23    -19    738       C  
ATOM   4064  CD ALYS B 224      36.314  37.590  14.807  0.54 31.05           C  
ANISOU 4064  CD ALYS B 224     3898   3788   4113    434    187   1115       C  
ATOM   4065  CD BLYS B 224      36.278  38.133  14.422  0.46 30.39           C  
ANISOU 4065  CD BLYS B 224     3833   3771   3945    192   -170    559       C  
ATOM   4066  CE ALYS B 224      37.817  37.619  14.595  0.54 31.12           C  
ANISOU 4066  CE ALYS B 224     3966   3707   4149    714    -42   1256       C  
ATOM   4067  CE BLYS B 224      35.047  37.394  13.922  0.46 30.45           C  
ANISOU 4067  CE BLYS B 224     3863   3688   4019    294   -335    434       C  
ATOM   4068  NZ ALYS B 224      38.220  36.773  13.442  0.54 31.04           N  
ANISOU 4068  NZ ALYS B 224     3987   3592   4216    846   -119   1162       N  
ATOM   4069  NZ BLYS B 224      35.375  36.424  12.841  0.46 30.80           N  
ANISOU 4069  NZ BLYS B 224     3921   3659   4124    347   -399    308       N  
ATOM   4070  N   ARG B 225      32.243  37.892  18.373  1.00 21.00           N  
ANISOU 4070  N   ARG B 225     2657   2271   3051   -111     64    718       N  
ATOM   4071  CA  ARG B 225      31.044  38.319  19.083  1.00 19.71           C  
ANISOU 4071  CA  ARG B 225     2464   2074   2950     93     37    325       C  
ATOM   4072  C   ARG B 225      31.269  38.160  20.578  1.00 20.23           C  
ANISOU 4072  C   ARG B 225     2743   2098   2846    120    134    -10       C  
ATOM   4073  O   ARG B 225      30.828  38.991  21.369  1.00 21.63           O  
ANISOU 4073  O   ARG B 225     3011   2107   3099    -67   -110   -422       O  
ATOM   4074  CB  ARG B 225      29.800  37.537  18.651  1.00 18.80           C  
ANISOU 4074  CB  ARG B 225     2108   2058   2979   -326    218     53       C  
ATOM   4075  CG  ARG B 225      28.558  37.913  19.477  1.00 19.38           C  
ANISOU 4075  CG  ARG B 225     2325   1915   3125   -311     96    -46       C  
ATOM   4076  CD  ARG B 225      27.283  37.222  18.999  1.00 20.37           C  
ANISOU 4076  CD  ARG B 225     2496   2150   3094   -551    -73    264       C  
ATOM   4077  NE  ARG B 225      26.948  37.604  17.632  1.00 22.04           N  
ANISOU 4077  NE  ARG B 225     2632   2517   3223   -251   -127    295       N  
ATOM   4078  CZ  ARG B 225      26.076  38.556  17.304  1.00 20.77           C  
ANISOU 4078  CZ  ARG B 225     2219   2502   3171    -21   -119    345       C  
ATOM   4079  NH1 ARG B 225      25.422  39.234  18.242  1.00 19.60           N  
ANISOU 4079  NH1 ARG B 225     2084   2382   2980   -346    -76    482       N  
ATOM   4080  NH2 ARG B 225      25.859  38.825  16.028  1.00 20.64           N  
ANISOU 4080  NH2 ARG B 225     1916   2751   3178   -116      9    250       N  
ATOM   4081  N   ASN B 226      31.973  37.096  20.953  1.00 19.96           N  
ANISOU 4081  N   ASN B 226     2721   2162   2701    -24     99    272       N  
ATOM   4082  CA  ASN B 226      32.308  36.857  22.355  1.00 21.20           C  
ANISOU 4082  CA  ASN B 226     3069   2186   2799     89    -98    351       C  
ATOM   4083  C   ASN B 226      33.126  37.985  22.959  1.00 21.14           C  
ANISOU 4083  C   ASN B 226     3071   2166   2795    144    -73    141       C  
ATOM   4084  O   ASN B 226      32.982  38.284  24.139  1.00 20.30           O  
ANISOU 4084  O   ASN B 226     2967   2151   2597    159   -116     37       O  
ATOM   4085  CB  ASN B 226      33.073  35.541  22.521  1.00 22.77           C  
ANISOU 4085  CB  ASN B 226     3215   2440   2996   -239    -85    672       C  
ATOM   4086  CG  ASN B 226      32.164  34.331  22.496  1.00 26.17           C  
ANISOU 4086  CG  ASN B 226     3502   3163   3280   -239    119    634       C  
ATOM   4087  OD1 ASN B 226      30.994  34.416  22.862  1.00 27.94           O  
ANISOU 4087  OD1 ASN B 226     3683   3517   3415    -58     82    566       O  
ATOM   4088  ND2 ASN B 226      32.705  33.193  22.076  1.00 26.28           N  
ANISOU 4088  ND2 ASN B 226     3604   3111   3268   -350    264    651       N  
ATOM   4089  N   TYR B 227      33.982  38.607  22.153  1.00 21.97           N  
ANISOU 4089  N   TYR B 227     3190   2219   2939     43     53   -155       N  
ATOM   4090  CA  TYR B 227      34.792  39.731  22.632  1.00 22.58           C  
ANISOU 4090  CA  TYR B 227     3103   2346   3129     35      1   -350       C  
ATOM   4091  C   TYR B 227      33.915  40.863  23.147  1.00 20.97           C  
ANISOU 4091  C   TYR B 227     2917   2211   2841    155     53    -83       C  
ATOM   4092  O   TYR B 227      34.210  41.471  24.173  1.00 21.54           O  
ANISOU 4092  O   TYR B 227     3033   2272   2878    159   -307   -270       O  
ATOM   4093  CB  TYR B 227      35.701  40.271  21.530  1.00 25.07           C  
ANISOU 4093  CB  TYR B 227     3158   2695   3673    225     42   -552       C  
ATOM   4094  CG  TYR B 227      36.839  39.364  21.135  1.00 27.79           C  
ANISOU 4094  CG  TYR B 227     3336   3080   4141    633    -45   -565       C  
ATOM   4095  CD1 TYR B 227      37.412  38.487  22.047  1.00 29.18           C  
ANISOU 4095  CD1 TYR B 227     3396   3327   4365    803    -49   -562       C  
ATOM   4096  CD2 TYR B 227      37.345  39.392  19.842  1.00 29.27           C  
ANISOU 4096  CD2 TYR B 227     3440   3344   4335    713   -157   -571       C  
ATOM   4097  CE1 TYR B 227      38.459  37.658  21.676  1.00 30.27           C  
ANISOU 4097  CE1 TYR B 227     3565   3392   4545    819   -129   -601       C  
ATOM   4098  CE2 TYR B 227      38.385  38.570  19.464  1.00 30.34           C  
ANISOU 4098  CE2 TYR B 227     3621   3390   4518    720   -213   -684       C  
ATOM   4099  CZ  TYR B 227      38.939  37.707  20.384  1.00 31.00           C  
ANISOU 4099  CZ  TYR B 227     3727   3402   4651    797   -124   -574       C  
ATOM   4100  OH  TYR B 227      39.979  36.891  20.000  1.00 32.04           O  
ANISOU 4100  OH  TYR B 227     3859   3453   4860    956    -79   -512       O  
ATOM   4101  N   ILE B 228      32.831  41.132  22.427  1.00 19.46           N  
ANISOU 4101  N   ILE B 228     2825   2029   2539    345     65    196       N  
ATOM   4102  CA  ILE B 228      31.924  42.221  22.780  1.00 19.37           C  
ANISOU 4102  CA  ILE B 228     3078   1823   2460    271    222     54       C  
ATOM   4103  C   ILE B 228      30.895  41.815  23.843  1.00 19.30           C  
ANISOU 4103  C   ILE B 228     3101   1701   2531     75    233   -143       C  
ATOM   4104  O   ILE B 228      30.860  42.383  24.934  1.00 19.36           O  
ANISOU 4104  O   ILE B 228     3231   1518   2609    -67     60   -238       O  
ATOM   4105  CB  ILE B 228      31.171  42.736  21.535  1.00 20.45           C  
ANISOU 4105  CB  ILE B 228     3424   1989   2357    145    435    419       C  
ATOM   4106  CG1 ILE B 228      32.160  43.239  20.473  1.00 22.15           C  
ANISOU 4106  CG1 ILE B 228     3648   2298   2469   -100    424    459       C  
ATOM   4107  CG2 ILE B 228      30.194  43.821  21.931  1.00 21.41           C  
ANISOU 4107  CG2 ILE B 228     3682   2118   2336    249    480    489       C  
ATOM   4108  CD1 ILE B 228      31.722  42.967  19.054  1.00 23.20           C  
ANISOU 4108  CD1 ILE B 228     3818   2237   2759   -174    447    401       C  
ATOM   4109  N   GLU B 229      30.071  40.820  23.524  1.00 19.17           N  
ANISOU 4109  N   GLU B 229     2855   1940   2489    -17    435     44       N  
ATOM   4110  CA  GLU B 229      28.968  40.428  24.395  1.00 19.39           C  
ANISOU 4110  CA  GLU B 229     2814   2065   2487     61    426    -72       C  
ATOM   4111  C   GLU B 229      29.429  39.684  25.640  1.00 20.51           C  
ANISOU 4111  C   GLU B 229     3126   2146   2523    -22    206    -42       C  
ATOM   4112  O   GLU B 229      28.844  39.833  26.708  1.00 22.70           O  
ANISOU 4112  O   GLU B 229     3297   2518   2809    -12    550     49       O  
ATOM   4113  CB  GLU B 229      27.966  39.569  23.626  1.00 18.38           C  
ANISOU 4113  CB  GLU B 229     2473   2083   2425   -143    396   -175       C  
ATOM   4114  CG  GLU B 229      27.384  40.266  22.414  1.00 19.69           C  
ANISOU 4114  CG  GLU B 229     2496   2442   2544     83    531     40       C  
ATOM   4115  CD  GLU B 229      26.316  39.447  21.727  1.00 21.13           C  
ANISOU 4115  CD  GLU B 229     2721   2617   2689    -44    393     -3       C  
ATOM   4116  OE1 GLU B 229      26.172  38.253  22.056  1.00 23.28           O  
ANISOU 4116  OE1 GLU B 229     3098   2843   2906     14    385     81       O  
ATOM   4117  OE2 GLU B 229      25.613  39.997  20.860  1.00 23.27           O  
ANISOU 4117  OE2 GLU B 229     2855   3158   2830   -418    331     64       O  
ATOM   4118  N   GLY B 230      30.479  38.888  25.507  1.00 20.39           N  
ANISOU 4118  N   GLY B 230     3306   2024   2418     58   -165    257       N  
ATOM   4119  CA  GLY B 230      30.948  38.099  26.630  1.00 21.30           C  
ANISOU 4119  CA  GLY B 230     3618   1973   2502     82   -321    320       C  
ATOM   4120  C   GLY B 230      31.975  38.832  27.465  1.00 22.82           C  
ANISOU 4120  C   GLY B 230     3808   2219   2642     23   -277    350       C  
ATOM   4121  O   GLY B 230      31.802  38.997  28.672  1.00 23.83           O  
ANISOU 4121  O   GLY B 230     4045   2441   2570   -528     12    151       O  
ATOM   4122  N   HIS B 231      33.054  39.268  26.823  1.00 22.34           N  
ANISOU 4122  N   HIS B 231     3584   2084   2821     89   -181    662       N  
ATOM   4123  CA  HIS B 231      34.174  39.868  27.539  1.00 25.13           C  
ANISOU 4123  CA  HIS B 231     3869   2419   3260    143   -164    627       C  
ATOM   4124  C   HIS B 231      33.932  41.343  27.853  1.00 24.91           C  
ANISOU 4124  C   HIS B 231     3678   2667   3119     98    -88    623       C  
ATOM   4125  O   HIS B 231      34.426  41.859  28.855  1.00 26.57           O  
ANISOU 4125  O   HIS B 231     3763   3126   3207    163     37    620       O  
ATOM   4126  CB  HIS B 231      35.470  39.728  26.738  1.00 28.22           C  
ANISOU 4126  CB  HIS B 231     4151   2798   3773    231   -270    625       C  
ATOM   4127  CG  HIS B 231      35.898  38.313  26.501  1.00 33.51           C  
ANISOU 4127  CG  HIS B 231     4538   3711   4482    243   -147    457       C  
ATOM   4128  ND1 HIS B 231      35.093  37.231  26.776  1.00 35.71           N  
ANISOU 4128  ND1 HIS B 231     4687   4058   4823    433   -100    387       N  
ATOM   4129  CD2 HIS B 231      37.054  37.808  26.007  1.00 35.35           C  
ANISOU 4129  CD2 HIS B 231     4698   4014   4718    312     -5    373       C  
ATOM   4130  CE1 HIS B 231      35.732  36.118  26.463  1.00 36.89           C  
ANISOU 4130  CE1 HIS B 231     4804   4267   4947    356    -18    301       C  
ATOM   4131  NE2 HIS B 231      36.924  36.441  25.994  1.00 36.59           N  
ANISOU 4131  NE2 HIS B 231     4805   4222   4877    342     58    340       N  
ATOM   4132  N   GLY B 232      33.182  42.022  26.986  1.00 22.49           N  
ANISOU 4132  N   GLY B 232     3276   2408   2863    133   -255    622       N  
ATOM   4133  CA  GLY B 232      32.929  43.444  27.162  1.00 21.64           C  
ANISOU 4133  CA  GLY B 232     3311   2143   2768    132    -36    314       C  
ATOM   4134  C   GLY B 232      34.160  44.256  26.818  1.00 20.91           C  
ANISOU 4134  C   GLY B 232     3341   2061   2545     62    -60    147       C  
ATOM   4135  O   GLY B 232      34.490  45.237  27.495  1.00 21.33           O  
ANISOU 4135  O   GLY B 232     3498   2181   2427    -88     21    149       O  
ATOM   4136  N   ASP B 233      34.842  43.851  25.752  1.00 20.10           N  
ANISOU 4136  N   ASP B 233     3246   1890   2502    364   -103    260       N  
ATOM   4137  CA  ASP B 233      36.139  44.423  25.422  1.00 21.00           C  
ANISOU 4137  CA  ASP B 233     3214   2085   2681    257   -118    413       C  
ATOM   4138  C   ASP B 233      36.055  45.689  24.565  1.00 19.01           C  
ANISOU 4138  C   ASP B 233     3096   1884   2243    178   -131    273       C  
ATOM   4139  O   ASP B 233      37.076  46.283  24.246  1.00 20.15           O  
ANISOU 4139  O   ASP B 233     3145   2281   2230     10     21    536       O  
ATOM   4140  CB  ASP B 233      36.999  43.382  24.713  1.00 23.33           C  
ANISOU 4140  CB  ASP B 233     3168   2374   3324    434   -295    682       C  
ATOM   4141  CG  ASP B 233      37.479  42.278  25.646  1.00 27.53           C  
ANISOU 4141  CG  ASP B 233     3447   2977   4039     88    -97    679       C  
ATOM   4142  OD1 ASP B 233      37.564  42.517  26.871  1.00 27.52           O  
ANISOU 4142  OD1 ASP B 233     3243   3204   4008   -454   -369    848       O  
ATOM   4143  OD2 ASP B 233      37.771  41.170  25.148  1.00 30.04           O  
ANISOU 4143  OD2 ASP B 233     3537   3287   4591    642    195    659       O  
ATOM   4144  N   PHE B 234      34.842  46.075  24.190  1.00 17.36           N  
ANISOU 4144  N   PHE B 234     2971   1625   1999    471    -66    152       N  
ATOM   4145  CA  PHE B 234      34.596  47.368  23.546  1.00 15.97           C  
ANISOU 4145  CA  PHE B 234     2848   1487   1733    539     83     -9       C  
ATOM   4146  C   PHE B 234      33.386  47.995  24.214  1.00 16.91           C  
ANISOU 4146  C   PHE B 234     3083   1639   1703    348    183     94       C  
ATOM   4147  O   PHE B 234      32.556  47.281  24.784  1.00 18.16           O  
ANISOU 4147  O   PHE B 234     3090   2040   1771    152    211    252       O  
ATOM   4148  CB  PHE B 234      34.338  47.205  22.040  1.00 16.42           C  
ANISOU 4148  CB  PHE B 234     2716   1890   1633    371    384    -29       C  
ATOM   4149  CG  PHE B 234      35.527  46.727  21.259  1.00 17.38           C  
ANISOU 4149  CG  PHE B 234     2717   2061   1827    301    651      6       C  
ATOM   4150  CD1 PHE B 234      36.449  47.631  20.750  1.00 19.83           C  
ANISOU 4150  CD1 PHE B 234     2936   2637   1962    260    559    -98       C  
ATOM   4151  CD2 PHE B 234      35.713  45.375  21.010  1.00 19.10           C  
ANISOU 4151  CD2 PHE B 234     2861   2427   1969    159    810   -104       C  
ATOM   4152  CE1 PHE B 234      37.543  47.195  20.023  1.00 20.96           C  
ANISOU 4152  CE1 PHE B 234     3135   2841   1988    152    541   -163       C  
ATOM   4153  CE2 PHE B 234      36.808  44.934  20.275  1.00 20.41           C  
ANISOU 4153  CE2 PHE B 234     2991   2696   2069    132    715   -214       C  
ATOM   4154  CZ  PHE B 234      37.719  45.846  19.787  1.00 21.43           C  
ANISOU 4154  CZ  PHE B 234     3242   2839   2061    145    567    -77       C  
ATOM   4155  N   SER B 235      33.264  49.320  24.117  1.00 15.96           N  
ANISOU 4155  N   SER B 235     3080   1386   1596    610     53     35       N  
ATOM   4156  CA  SER B 235      32.127  50.022  24.705  1.00 16.91           C  
ANISOU 4156  CA  SER B 235     3123   1539   1765    397    236      8       C  
ATOM   4157  C   SER B 235      30.843  49.662  23.986  1.00 17.41           C  
ANISOU 4157  C   SER B 235     3061   1881   1672    199    477     27       C  
ATOM   4158  O   SER B 235      29.770  49.563  24.586  1.00 17.55           O  
ANISOU 4158  O   SER B 235     3196   1900   1573     -8    614    434       O  
ATOM   4159  CB  SER B 235      32.346  51.538  24.651  1.00 17.67           C  
ANISOU 4159  CB  SER B 235     3062   1557   2094    315    271     95       C  
ATOM   4160  OG  SER B 235      33.591  51.895  25.223  1.00 18.35           O  
ANISOU 4160  OG  SER B 235     3037   1737   2197    136    174    -15       O  
ATOM   4161  N   ALA B 236      30.973  49.481  22.675  1.00 16.50           N  
ANISOU 4161  N   ALA B 236     2980   1727   1564    285    332    -60       N  
ATOM   4162  CA  ALA B 236      29.872  49.129  21.808  1.00 16.09           C  
ANISOU 4162  CA  ALA B 236     2593   1695   1825    263    589    -81       C  
ATOM   4163  C   ALA B 236      30.448  48.691  20.477  1.00 15.24           C  
ANISOU 4163  C   ALA B 236     2398   1563   1830    207    365   -183       C  
ATOM   4164  O   ALA B 236      31.588  49.014  20.149  1.00 15.70           O  
ANISOU 4164  O   ALA B 236     2458   1708   1798    206    402   -288       O  
ATOM   4165  CB  ALA B 236      28.928  50.308  21.612  1.00 15.80           C  
ANISOU 4165  CB  ALA B 236     2521   1536   1946    740    556     42       C  
ATOM   4166  N   CYS B 237      29.648  47.952  19.724  1.00 15.14           N  
ANISOU 4166  N   CYS B 237     2321   1705   1726    201    322   -257       N  
ATOM   4167  CA  CYS B 237      29.982  47.622  18.354  1.00 15.83           C  
ANISOU 4167  CA  CYS B 237     2459   1622   1932    280    267   -173       C  
ATOM   4168  C   CYS B 237      28.827  48.035  17.480  1.00 16.59           C  
ANISOU 4168  C   CYS B 237     2581   1803   1920     80    529     76       C  
ATOM   4169  O   CYS B 237      27.664  47.763  17.798  1.00 17.30           O  
ANISOU 4169  O   CYS B 237     2770   1886   1916     79    683     29       O  
ATOM   4170  CB  CYS B 237      30.275  46.126  18.209  1.00 15.42           C  
ANISOU 4170  CB  CYS B 237     2561   1312   1986    184    427   -222       C  
ATOM   4171  SG  CYS B 237      30.391  45.510  16.494  1.00 16.67           S  
ANISOU 4171  SG  CYS B 237     2506   1652   2177    225    294     -5       S  
ATOM   4172  N   PHE B 238      29.148  48.700  16.374  1.00 15.05           N  
ANISOU 4172  N   PHE B 238     2335   1569   1813    207    428    253       N  
ATOM   4173  CA  PHE B 238      28.150  49.045  15.386  1.00 14.79           C  
ANISOU 4173  CA  PHE B 238     2366   1497   1756    187    640    -14       C  
ATOM   4174  C   PHE B 238      28.461  48.350  14.073  1.00 15.14           C  
ANISOU 4174  C   PHE B 238     2270   1713   1770    245    520   -226       C  
ATOM   4175  O   PHE B 238      29.547  48.506  13.521  1.00 16.27           O  
ANISOU 4175  O   PHE B 238     2095   2110   1978    158    549   -320       O  
ATOM   4176  CB  PHE B 238      28.079  50.564  15.217  1.00 16.14           C  
ANISOU 4176  CB  PHE B 238     2486   1628   2020    277    660     12       C  
ATOM   4177  CG  PHE B 238      27.525  51.257  16.423  1.00 17.57           C  
ANISOU 4177  CG  PHE B 238     2931   1559   2184    401    699      1       C  
ATOM   4178  CD1 PHE B 238      26.183  51.573  16.494  1.00 19.02           C  
ANISOU 4178  CD1 PHE B 238     3062   1780   2383    315    538      2       C  
ATOM   4179  CD2 PHE B 238      28.335  51.530  17.509  1.00 18.35           C  
ANISOU 4179  CD2 PHE B 238     3080   1654   2237    508    665   -112       C  
ATOM   4180  CE1 PHE B 238      25.664  52.178  17.628  1.00 19.95           C  
ANISOU 4180  CE1 PHE B 238     3189   1920   2472    446    679    -97       C  
ATOM   4181  CE2 PHE B 238      27.819  52.135  18.643  1.00 19.51           C  
ANISOU 4181  CE2 PHE B 238     3259   1725   2428    769    736     52       C  
ATOM   4182  CZ  PHE B 238      26.481  52.456  18.687  1.00 20.12           C  
ANISOU 4182  CZ  PHE B 238     3233   1960   2450    583    853    163       C  
ATOM   4183  N   SER B 239      27.505  47.566  13.601  1.00 15.00           N  
ANISOU 4183  N   SER B 239     2423   1377   1901    279    480   -257       N  
ATOM   4184  CA  SER B 239      27.638  46.929  12.305  1.00 14.91           C  
ANISOU 4184  CA  SER B 239     2003   1769   1894    330    434   -182       C  
ATOM   4185  C   SER B 239      26.658  47.506  11.308  1.00 15.48           C  
ANISOU 4185  C   SER B 239     1788   1972   2121    376    538      8       C  
ATOM   4186  O   SER B 239      25.483  47.725  11.624  1.00 16.14           O  
ANISOU 4186  O   SER B 239     1787   2078   2268    391    675    270       O  
ATOM   4187  CB  SER B 239      27.428  45.424  12.416  1.00 14.82           C  
ANISOU 4187  CB  SER B 239     1929   1829   1873    270    338   -178       C  
ATOM   4188  OG  SER B 239      27.377  44.844  11.121  1.00 15.14           O  
ANISOU 4188  OG  SER B 239     1953   1945   1853    329    250   -123       O  
ATOM   4189  N   TYR B 240      27.151  47.748  10.096  1.00 15.86           N  
ANISOU 4189  N   TYR B 240     1846   2064   2114    221    384     85       N  
ATOM   4190  CA  TYR B 240      26.326  48.276   9.025  1.00 15.51           C  
ANISOU 4190  CA  TYR B 240     1883   1907   2104    273    519     29       C  
ATOM   4191  C   TYR B 240      25.970  47.188   8.020  1.00 15.64           C  
ANISOU 4191  C   TYR B 240     1735   2015   2193    464    339    -72       C  
ATOM   4192  O   TYR B 240      25.547  47.474   6.898  1.00 17.33           O  
ANISOU 4192  O   TYR B 240     1989   2237   2359    298    415    -71       O  
ATOM   4193  CB  TYR B 240      27.040  49.445   8.356  1.00 16.60           C  
ANISOU 4193  CB  TYR B 240     2283   1773   2253    185    421    -68       C  
ATOM   4194  CG  TYR B 240      27.292  50.566   9.335  1.00 17.09           C  
ANISOU 4194  CG  TYR B 240     2515   1777   2200    342    310   -165       C  
ATOM   4195  CD1 TYR B 240      26.265  51.424   9.701  1.00 17.94           C  
ANISOU 4195  CD1 TYR B 240     2657   1815   2345    352    247    -52       C  
ATOM   4196  CD2 TYR B 240      28.540  50.749   9.912  1.00 16.18           C  
ANISOU 4196  CD2 TYR B 240     2537   1627   1982    283    327   -111       C  
ATOM   4197  CE1 TYR B 240      26.473  52.443  10.603  1.00 18.70           C  
ANISOU 4197  CE1 TYR B 240     2834   1951   2321    305    341    -63       C  
ATOM   4198  CE2 TYR B 240      28.764  51.778  10.828  1.00 17.04           C  
ANISOU 4198  CE2 TYR B 240     2670   1741   2064    240    334    -62       C  
ATOM   4199  CZ  TYR B 240      27.721  52.616  11.163  1.00 17.31           C  
ANISOU 4199  CZ  TYR B 240     2794   1670   2112    437    222   -139       C  
ATOM   4200  OH  TYR B 240      27.920  53.630  12.072  1.00 19.49           O  
ANISOU 4200  OH  TYR B 240     3252   1955   2197    510    431   -111       O  
ATOM   4201  N   ASN B 241      26.148  45.938   8.440  1.00 15.24           N  
ANISOU 4201  N   ASN B 241     1623   2015   2152    440    177    -84       N  
ATOM   4202  CA  ASN B 241      25.595  44.797   7.729  1.00 15.92           C  
ANISOU 4202  CA  ASN B 241     1652   2098   2300    587    162    105       C  
ATOM   4203  C   ASN B 241      24.249  44.457   8.351  1.00 15.85           C  
ANISOU 4203  C   ASN B 241     1504   2307   2210    507    371    185       C  
ATOM   4204  O   ASN B 241      24.192  43.980   9.487  1.00 15.79           O  
ANISOU 4204  O   ASN B 241     1688   2240   2071    395    427    285       O  
ATOM   4205  CB  ASN B 241      26.540  43.585   7.789  1.00 15.18           C  
ANISOU 4205  CB  ASN B 241     1730   1852   2187    646     84    -14       C  
ATOM   4206  CG  ASN B 241      26.107  42.459   6.866  1.00 14.73           C  
ANISOU 4206  CG  ASN B 241     1648   1772   2176    484    -83    131       C  
ATOM   4207  OD1 ASN B 241      24.942  42.375   6.469  1.00 15.15           O  
ANISOU 4207  OD1 ASN B 241     1616   2172   1968    328     31     -3       O  
ATOM   4208  ND2 ASN B 241      27.052  41.570   6.519  1.00 15.36           N  
ANISOU 4208  ND2 ASN B 241     1860   1611   2365    284     37   -102       N  
ATOM   4209  N   LEU B 242      23.167  44.697   7.615  1.00 16.59           N  
ANISOU 4209  N   LEU B 242     1368   2595   2340    464    405    110       N  
ATOM   4210  CA  LEU B 242      21.827  44.423   8.135  1.00 17.77           C  
ANISOU 4210  CA  LEU B 242     1432   2814   2505    387    284    109       C  
ATOM   4211  C   LEU B 242      21.605  42.947   8.471  1.00 17.67           C  
ANISOU 4211  C   LEU B 242     1446   2716   2550    406    363    101       C  
ATOM   4212  O   LEU B 242      20.658  42.610   9.188  1.00 19.67           O  
ANISOU 4212  O   LEU B 242     1597   3102   2775    320    466     72       O  
ATOM   4213  CB  LEU B 242      20.761  44.885   7.140  1.00 18.36           C  
ANISOU 4213  CB  LEU B 242     1411   2954   2612    539    324    213       C  
ATOM   4214  CG  LEU B 242      20.762  46.382   6.837  1.00 19.75           C  
ANISOU 4214  CG  LEU B 242     1619   3186   2701    656    411    302       C  
ATOM   4215  CD1 LEU B 242      19.579  46.748   5.958  1.00 20.91           C  
ANISOU 4215  CD1 LEU B 242     1643   3416   2887    940    165    425       C  
ATOM   4216  CD2 LEU B 242      20.754  47.202   8.118  1.00 20.38           C  
ANISOU 4216  CD2 LEU B 242     1807   3314   2621    580    853    271       C  
ATOM   4217  N   ARG B 243      22.471  42.067   7.965  1.00 17.92           N  
ANISOU 4217  N   ARG B 243     1695   2634   2480    250    191    111       N  
ATOM   4218  CA  ARG B 243      22.373  40.640   8.274  1.00 18.58           C  
ANISOU 4218  CA  ARG B 243     1867   2642   2549   -146    109    -55       C  
ATOM   4219  C   ARG B 243      23.073  40.254   9.574  1.00 17.95           C  
ANISOU 4219  C   ARG B 243     1992   2374   2455   -149    185    110       C  
ATOM   4220  O   ARG B 243      22.884  39.147  10.077  1.00 18.08           O  
ANISOU 4220  O   ARG B 243     2215   2059   2596   -152    263    136       O  
ATOM   4221  CB  ARG B 243      22.941  39.805   7.129  1.00 19.25           C  
ANISOU 4221  CB  ARG B 243     1774   2934   2608     -8    244   -315       C  
ATOM   4222  CG  ARG B 243      22.090  39.858   5.883  1.00 20.76           C  
ANISOU 4222  CG  ARG B 243     1912   3237   2739     94    339   -264       C  
ATOM   4223  CD  ARG B 243      22.441  38.760   4.896  1.00 22.13           C  
ANISOU 4223  CD  ARG B 243     2096   3479   2832    175    223   -429       C  
ATOM   4224  NE  ARG B 243      21.876  39.070   3.590  1.00 22.93           N  
ANISOU 4224  NE  ARG B 243     2290   3571   2852    321    291   -283       N  
ATOM   4225  CZ  ARG B 243      22.427  39.926   2.738  1.00 24.50           C  
ANISOU 4225  CZ  ARG B 243     2599   3720   2991     22    318   -325       C  
ATOM   4226  NH1 ARG B 243      23.561  40.538   3.060  1.00 24.64           N  
ANISOU 4226  NH1 ARG B 243     2744   3580   3038    -43    500   -257       N  
ATOM   4227  NH2 ARG B 243      21.853  40.171   1.566  1.00 25.76           N  
ANISOU 4227  NH2 ARG B 243     2760   3867   3162   -122   -155   -254       N  
ATOM   4228  N   THR B 244      23.882  41.157  10.115  1.00 16.21           N  
ANISOU 4228  N   THR B 244     1783   2200   2175     -6    349    254       N  
ATOM   4229  CA  THR B 244      24.523  40.928  11.406  1.00 16.43           C  
ANISOU 4229  CA  THR B 244     1877   2201   2163     28    382    248       C  
ATOM   4230  C   THR B 244      23.442  40.714  12.453  1.00 17.68           C  
ANISOU 4230  C   THR B 244     1920   2363   2433     56    646    430       C  
ATOM   4231  O   THR B 244      22.491  41.484  12.515  1.00 19.94           O  
ANISOU 4231  O   THR B 244     2319   2450   2807    121    725    265       O  
ATOM   4232  CB  THR B 244      25.419  42.120  11.825  1.00 15.55           C  
ANISOU 4232  CB  THR B 244     1699   2099   2112    -34    318    161       C  
ATOM   4233  OG1 THR B 244      26.514  42.242  10.913  1.00 16.51           O  
ANISOU 4233  OG1 THR B 244     1657   2407   2208    118    374     48       O  
ATOM   4234  CG2 THR B 244      25.970  41.931  13.234  1.00 15.70           C  
ANISOU 4234  CG2 THR B 244     1912   1949   2103     65    153    385       C  
ATOM   4235  N   SER B 245      23.569  39.663  13.257  1.00 18.77           N  
ANISOU 4235  N   SER B 245     2109   2559   2464    -39    576    501       N  
ATOM   4236  CA  SER B 245      22.625  39.453  14.349  1.00 20.00           C  
ANISOU 4236  CA  SER B 245     2132   2882   2584   -159    535    161       C  
ATOM   4237  C   SER B 245      22.888  40.466  15.454  1.00 19.62           C  
ANISOU 4237  C   SER B 245     2165   2847   2442    -46    478    198       C  
ATOM   4238  O   SER B 245      23.996  40.533  15.979  1.00 19.38           O  
ANISOU 4238  O   SER B 245     2092   2864   2409     19    308    256       O  
ATOM   4239  CB  SER B 245      22.725  38.028  14.899  1.00 21.84           C  
ANISOU 4239  CB  SER B 245     2362   3097   2838   -191    384     81       C  
ATOM   4240  OG  SER B 245      22.322  37.078  13.929  1.00 22.43           O  
ANISOU 4240  OG  SER B 245     2399   3079   3043   -366    340    -44       O  
ATOM   4241  N   PRO B 246      21.873  41.267  15.811  1.00 21.44           N  
ANISOU 4241  N   PRO B 246     2369   3218   2561     66    289     56       N  
ATOM   4242  CA  PRO B 246      22.062  42.191  16.931  1.00 21.11           C  
ANISOU 4242  CA  PRO B 246     2331   3165   2524    288    470   -166       C  
ATOM   4243  C   PRO B 246      22.122  41.435  18.245  1.00 21.41           C  
ANISOU 4243  C   PRO B 246     2490   3079   2567     18    599     40       C  
ATOM   4244  O   PRO B 246      21.645  40.301  18.331  1.00 21.91           O  
ANISOU 4244  O   PRO B 246     2603   3205   2518   -452    645    237       O  
ATOM   4245  CB  PRO B 246      20.821  43.085  16.865  1.00 22.41           C  
ANISOU 4245  CB  PRO B 246     2396   3376   2744    535    414   -361       C  
ATOM   4246  CG  PRO B 246      19.783  42.218  16.256  1.00 23.09           C  
ANISOU 4246  CG  PRO B 246     2448   3505   2819    459    318   -241       C  
ATOM   4247  CD  PRO B 246      20.505  41.332  15.266  1.00 22.71           C  
ANISOU 4247  CD  PRO B 246     2420   3471   2737    463    336     36       C  
ATOM   4248  N   SER B 247      22.713  42.055  19.254  1.00 22.68           N  
ANISOU 4248  N   SER B 247     2788   3299   2531    -63    510    189       N  
ATOM   4249  CA  SER B 247      22.724  41.485  20.592  1.00 23.64           C  
ANISOU 4249  CA  SER B 247     3031   3386   2567   -388    599    259       C  
ATOM   4250  C   SER B 247      21.308  41.322  21.118  1.00 25.27           C  
ANISOU 4250  C   SER B 247     3078   3659   2863   -439    741      8       C  
ATOM   4251  O   SER B 247      20.399  42.031  20.690  1.00 26.20           O  
ANISOU 4251  O   SER B 247     3184   3828   2943   -542    833    -10       O  
ATOM   4252  CB  SER B 247      23.528  42.374  21.539  1.00 23.97           C  
ANISOU 4252  CB  SER B 247     3076   3371   2662   -471    367    240       C  
ATOM   4253  OG  SER B 247      24.896  42.389  21.189  1.00 23.20           O  
ANISOU 4253  OG  SER B 247     2801   3249   2767   -514    368    298       O  
ATOM   4254  N   ASN B 248      21.128  40.394  22.053  1.00 25.56           N  
ANISOU 4254  N   ASN B 248     3040   3564   3107   -590   1099    -72       N  
ATOM   4255  CA  ASN B 248      19.883  40.314  22.809  1.00 26.83           C  
ANISOU 4255  CA  ASN B 248     3189   3714   3291   -344   1365    -40       C  
ATOM   4256  C   ASN B 248      19.679  41.604  23.599  1.00 27.35           C  
ANISOU 4256  C   ASN B 248     3352   3841   3198   -116   1420   -106       C  
ATOM   4257  O   ASN B 248      20.575  42.446  23.660  1.00 27.26           O  
ANISOU 4257  O   ASN B 248     3511   3888   2961     74   1412    -59       O  
ATOM   4258  CB  ASN B 248      19.890  39.107  23.748  1.00 28.39           C  
ANISOU 4258  CB  ASN B 248     3351   3793   3642   -445   1321    -70       C  
ATOM   4259  CG  ASN B 248      19.934  37.784  23.000  1.00 30.39           C  
ANISOU 4259  CG  ASN B 248     3562   4036   3948   -447   1272   -171       C  
ATOM   4260  OD1 ASN B 248      19.332  37.637  21.935  1.00 31.76           O  
ANISOU 4260  OD1 ASN B 248     3631   4312   4126   -675   1199   -257       O  
ATOM   4261  ND2 ASN B 248      20.649  36.811  23.560  1.00 30.40           N  
ANISOU 4261  ND2 ASN B 248     3581   3930   4041   -245   1309   -260       N  
ATOM   4262  N   ALA B 249      18.503  41.765  24.200  1.00 29.38           N  
ANISOU 4262  N   ALA B 249     3520   4049   3595   -128   1326   -161       N  
ATOM   4263  CA  ALA B 249      18.226  42.959  24.998  1.00 30.62           C  
ANISOU 4263  CA  ALA B 249     3602   4183   3849     59   1450   -155       C  
ATOM   4264  C   ALA B 249      19.249  43.104  26.123  1.00 29.53           C  
ANISOU 4264  C   ALA B 249     3509   3884   3825    224   1538    123       C  
ATOM   4265  O   ALA B 249      19.621  44.211  26.502  1.00 29.77           O  
ANISOU 4265  O   ALA B 249     3592   3899   3821    438   1597    159       O  
ATOM   4266  CB  ALA B 249      16.813  42.911  25.559  1.00 32.05           C  
ANISOU 4266  CB  ALA B 249     3657   4474   4047    -19   1338   -173       C  
ATOM   4267  N   THR B 250      19.705  41.972  26.648  1.00 28.27           N  
ANISOU 4267  N   THR B 250     3482   3500   3760    193   1565    331       N  
ATOM   4268  CA  THR B 250      20.784  41.959  27.622  1.00 27.79           C  
ANISOU 4268  CA  THR B 250     3633   3261   3664     66   1674    117       C  
ATOM   4269  C   THR B 250      21.930  41.091  27.107  1.00 26.04           C  
ANISOU 4269  C   THR B 250     3576   2856   3461    182   1312   -122       C  
ATOM   4270  O   THR B 250      21.712  40.128  26.372  1.00 27.61           O  
ANISOU 4270  O   THR B 250     3767   3021   3702    149   1058   -495       O  
ATOM   4271  CB  THR B 250      20.323  41.417  28.987  1.00 30.48           C  
ANISOU 4271  CB  THR B 250     4044   3660   3875      5   1928    264       C  
ATOM   4272  OG1 THR B 250      20.096  40.007  28.887  1.00 34.50           O  
ANISOU 4272  OG1 THR B 250     4511   4332   4267    -93   1804    363       O  
ATOM   4273  CG2 THR B 250      19.041  42.102  29.427  1.00 29.56           C  
ANISOU 4273  CG2 THR B 250     4008   3582   3642    186   2259    140       C  
ATOM   4274  N   THR B 251      23.150  41.443  27.489  1.00 23.05           N  
ANISOU 4274  N   THR B 251     3266   2478   3013    161   1194     82       N  
ATOM   4275  CA  THR B 251      24.317  40.636  27.165  1.00 21.90           C  
ANISOU 4275  CA  THR B 251     3376   2324   2621   -254   1017    384       C  
ATOM   4276  C   THR B 251      25.066  40.345  28.457  1.00 22.30           C  
ANISOU 4276  C   THR B 251     3486   2446   2539   -123    867    318       C  
ATOM   4277  O   THR B 251      24.880  41.049  29.446  1.00 24.71           O  
ANISOU 4277  O   THR B 251     3779   3017   2592     23    818    302       O  
ATOM   4278  CB  THR B 251      25.241  41.348  26.155  1.00 21.31           C  
ANISOU 4278  CB  THR B 251     3452   2209   2435   -204    756    451       C  
ATOM   4279  OG1 THR B 251      25.795  42.520  26.759  1.00 21.76           O  
ANISOU 4279  OG1 THR B 251     3577   2374   2317   -223    731    321       O  
ATOM   4280  CG2 THR B 251      24.464  41.734  24.914  1.00 21.37           C  
ANISOU 4280  CG2 THR B 251     3450   2125   2546   -158    461    304       C  
ATOM   4281  N   PRO B 252      25.896  39.293  28.466  1.00 21.81           N  
ANISOU 4281  N   PRO B 252     3649   2323   2314    -72    829    241       N  
ATOM   4282  CA  PRO B 252      26.661  38.972  29.676  1.00 22.79           C  
ANISOU 4282  CA  PRO B 252     3885   2567   2208     29    662     38       C  
ATOM   4283  C   PRO B 252      27.488  40.150  30.199  1.00 22.80           C  
ANISOU 4283  C   PRO B 252     4033   2578   2051   -167    678    133       C  
ATOM   4284  O   PRO B 252      27.605  40.336  31.412  1.00 24.35           O  
ANISOU 4284  O   PRO B 252     4372   2988   1890   -236    761    -61       O  
ATOM   4285  CB  PRO B 252      27.569  37.829  29.218  1.00 23.56           C  
ANISOU 4285  CB  PRO B 252     3999   2667   2285    241    585     70       C  
ATOM   4286  CG  PRO B 252      26.789  37.162  28.132  1.00 22.69           C  
ANISOU 4286  CG  PRO B 252     3940   2367   2313    337    555    185       C  
ATOM   4287  CD  PRO B 252      26.053  38.265  27.420  1.00 21.59           C  
ANISOU 4287  CD  PRO B 252     3733   2228   2243    249    704    264       C  
ATOM   4288  N   SER B 253      28.031  40.952  29.291  1.00 22.10           N  
ANISOU 4288  N   SER B 253     3796   2553   2047   -355    543    155       N  
ATOM   4289  CA  SER B 253      28.923  42.041  29.676  1.00 22.03           C  
ANISOU 4289  CA  SER B 253     3839   2471   2060   -368    313     26       C  
ATOM   4290  C   SER B 253      28.223  43.390  29.802  1.00 23.75           C  
ANISOU 4290  C   SER B 253     4090   2857   2079   -112    362     62       C  
ATOM   4291  O   SER B 253      28.761  44.323  30.398  1.00 25.15           O  
ANISOU 4291  O   SER B 253     4280   3098   2179   -121    242     -5       O  
ATOM   4292  CB  SER B 253      30.050  42.168  28.661  1.00 22.18           C  
ANISOU 4292  CB  SER B 253     3760   2643   2025   -452    197    161       C  
ATOM   4293  OG  SER B 253      29.531  42.600  27.418  1.00 22.16           O  
ANISOU 4293  OG  SER B 253     3810   2464   2146   -462    292    280       O  
ATOM   4294  N   GLY B 254      27.033  43.495  29.227  1.00 22.93           N  
ANISOU 4294  N   GLY B 254     4053   2716   1943     42    569    235       N  
ATOM   4295  CA  GLY B 254      26.338  44.763  29.155  1.00 22.73           C  
ANISOU 4295  CA  GLY B 254     4080   2464   2090    143   1012    310       C  
ATOM   4296  C   GLY B 254      26.721  45.551  27.916  1.00 23.71           C  
ANISOU 4296  C   GLY B 254     4178   2494   2335    101    999    168       C  
ATOM   4297  O   GLY B 254      26.180  46.626  27.671  1.00 25.75           O  
ANISOU 4297  O   GLY B 254     4531   2513   2738    209   1085    223       O  
ATOM   4298  N   ARG B 255      27.654  45.012  27.133  1.00 21.14           N  
ANISOU 4298  N   ARG B 255     3882   2168   1983    -84    859      5       N  
ATOM   4299  CA  ARG B 255      28.083  45.653  25.891  1.00 20.04           C  
ANISOU 4299  CA  ARG B 255     3650   1981   1983    -39    570    103       C  
ATOM   4300  C   ARG B 255      27.374  45.002  24.716  1.00 19.21           C  
ANISOU 4300  C   ARG B 255     3508   1840   1952    -46    581    160       C  
ATOM   4301  O   ARG B 255      27.178  43.783  24.697  1.00 20.02           O  
ANISOU 4301  O   ARG B 255     3647   1777   2181     14    440    100       O  
ATOM   4302  CB  ARG B 255      29.595  45.557  25.717  1.00 19.22           C  
ANISOU 4302  CB  ARG B 255     3615   1683   2005   -153    236    118       C  
ATOM   4303  CG  ARG B 255      30.383  46.042  26.920  1.00 19.25           C  
ANISOU 4303  CG  ARG B 255     3630   1775   1908   -144    101    156       C  
ATOM   4304  CD  ARG B 255      30.082  47.496  27.244  1.00 20.49           C  
ANISOU 4304  CD  ARG B 255     3592   2056   2139     63     47     95       C  
ATOM   4305  NE  ARG B 255      30.874  47.945  28.381  1.00 22.95           N  
ANISOU 4305  NE  ARG B 255     3873   2317   2528     90     92    -26       N  
ATOM   4306  CZ  ARG B 255      30.898  49.193  28.833  1.00 26.47           C  
ANISOU 4306  CZ  ARG B 255     4238   2880   2938     44     24   -113       C  
ATOM   4307  NH1 ARG B 255      30.174  50.133  28.237  1.00 29.34           N  
ANISOU 4307  NH1 ARG B 255     4545   3229   3374    274     25   -170       N  
ATOM   4308  NH2 ARG B 255      31.653  49.498  29.878  1.00 27.72           N  
ANISOU 4308  NH2 ARG B 255     4392   3223   2917    -35    150   -140       N  
ATOM   4309  N   HIS B 256      27.009  45.811  23.728  1.00 18.93           N  
ANISOU 4309  N   HIS B 256     3098   2218   1876    138    532     95       N  
ATOM   4310  CA  HIS B 256      26.144  45.341  22.663  1.00 19.66           C  
ANISOU 4310  CA  HIS B 256     2933   2391   2146     53    855    141       C  
ATOM   4311  C   HIS B 256      26.727  45.484  21.274  1.00 18.48           C  
ANISOU 4311  C   HIS B 256     2693   2160   2167   -133    696     20       C  
ATOM   4312  O   HIS B 256      27.592  46.324  21.010  1.00 19.05           O  
ANISOU 4312  O   HIS B 256     2786   2209   2242    -67    677   -212       O  
ATOM   4313  CB  HIS B 256      24.809  46.087  22.701  1.00 21.81           C  
ANISOU 4313  CB  HIS B 256     2759   2985   2542     92    880     18       C  
ATOM   4314  CG  HIS B 256      23.970  45.761  23.895  1.00 25.06           C  
ANISOU 4314  CG  HIS B 256     2940   3614   2970   -107    997    -74       C  
ATOM   4315  ND1 HIS B 256      22.746  45.136  23.793  1.00 26.73           N  
ANISOU 4315  ND1 HIS B 256     3069   3855   3233   -301    972   -192       N  
ATOM   4316  CD2 HIS B 256      24.177  45.970  25.216  1.00 27.29           C  
ANISOU 4316  CD2 HIS B 256     3154   3980   3235   -189    913    -57       C  
ATOM   4317  CE1 HIS B 256      22.235  44.974  25.001  1.00 27.42           C  
ANISOU 4317  CE1 HIS B 256     3202   3956   3262   -450   1030   -166       C  
ATOM   4318  NE2 HIS B 256      23.086  45.468  25.882  1.00 28.11           N  
ANISOU 4318  NE2 HIS B 256     3289   4109   3281   -215   1016   -137       N  
ATOM   4319  N   ILE B 257      26.225  44.629  20.395  1.00 17.58           N  
ANISOU 4319  N   ILE B 257     2560   2082   2039     60    550     14       N  
ATOM   4320  CA  ILE B 257      26.361  44.804  18.965  1.00 17.87           C  
ANISOU 4320  CA  ILE B 257     2339   2263   2189   -136    397     24       C  
ATOM   4321  C   ILE B 257      25.087  45.431  18.432  1.00 18.52           C  
ANISOU 4321  C   ILE B 257     2434   2170   2433     15    578    -23       C  
ATOM   4322  O   ILE B 257      24.010  44.844  18.539  1.00 20.18           O  
ANISOU 4322  O   ILE B 257     2751   2177   2740     17    336    308       O  
ATOM   4323  CB  ILE B 257      26.617  43.477  18.260  1.00 16.31           C  
ANISOU 4323  CB  ILE B 257     2024   2203   1969    -84    232    -78       C  
ATOM   4324  CG1 ILE B 257      27.951  42.891  18.733  1.00 16.05           C  
ANISOU 4324  CG1 ILE B 257     1926   2162   2010   -331    123   -153       C  
ATOM   4325  CG2 ILE B 257      26.557  43.675  16.747  1.00 16.57           C  
ANISOU 4325  CG2 ILE B 257     2001   2259   2034    153     24   -205       C  
ATOM   4326  CD1 ILE B 257      28.178  41.448  18.318  1.00 17.23           C  
ANISOU 4326  CD1 ILE B 257     2440   2067   2038   -318    123   -231       C  
ATOM   4327  N   TYR B 258      25.213  46.632  17.871  1.00 18.18           N  
ANISOU 4327  N   TYR B 258     2422   2165   2319     32    757    110       N  
ATOM   4328  CA  TYR B 258      24.080  47.345  17.291  1.00 19.09           C  
ANISOU 4328  CA  TYR B 258     2392   2530   2334    224    925    -55       C  
ATOM   4329  C   TYR B 258      24.151  47.279  15.774  1.00 19.39           C  
ANISOU 4329  C   TYR B 258     2597   2513   2256    326    721    231       C  
ATOM   4330  O   TYR B 258      25.237  47.320  15.202  1.00 20.55           O  
ANISOU 4330  O   TYR B 258     2757   2639   2413    525    690    350       O  
ATOM   4331  CB  TYR B 258      24.054  48.806  17.748  1.00 19.63           C  
ANISOU 4331  CB  TYR B 258     2313   2639   2508    446   1172   -161       C  
ATOM   4332  CG  TYR B 258      23.886  48.993  19.244  1.00 22.04           C  
ANISOU 4332  CG  TYR B 258     2904   2959   2510    205   1100   -254       C  
ATOM   4333  CD1 TYR B 258      24.940  49.440  20.032  1.00 22.68           C  
ANISOU 4333  CD1 TYR B 258     3064   2921   2634     85   1255   -108       C  
ATOM   4334  CD2 TYR B 258      22.673  48.720  19.865  1.00 24.30           C  
ANISOU 4334  CD2 TYR B 258     3255   3306   2673    246    949   -425       C  
ATOM   4335  CE1 TYR B 258      24.788  49.621  21.405  1.00 23.15           C  
ANISOU 4335  CE1 TYR B 258     3274   2936   2586    -27   1464    -50       C  
ATOM   4336  CE2 TYR B 258      22.510  48.894  21.233  1.00 25.74           C  
ANISOU 4336  CE2 TYR B 258     3545   3607   2627    194   1165   -179       C  
ATOM   4337  CZ  TYR B 258      23.569  49.342  21.995  1.00 26.19           C  
ANISOU 4337  CZ  TYR B 258     3776   3529   2647    165   1333   -218       C  
ATOM   4338  OH  TYR B 258      23.411  49.512  23.357  1.00 27.14           O  
ANISOU 4338  OH  TYR B 258     4163   3631   2519    508   1389   -423       O  
ATOM   4339  N   VAL B 259      22.996  47.171  15.133  1.00 20.31           N  
ANISOU 4339  N   VAL B 259     2723   2652   2342    429    711    262       N  
ATOM   4340  CA  VAL B 259      22.926  47.006  13.687  1.00 21.21           C  
ANISOU 4340  CA  VAL B 259     2645   2994   2420    663    685    449       C  
ATOM   4341  C   VAL B 259      22.112  48.149  13.104  1.00 22.89           C  
ANISOU 4341  C   VAL B 259     2836   3087   2775   1062    887    689       C  
ATOM   4342  O   VAL B 259      21.036  48.462  13.614  1.00 24.70           O  
ANISOU 4342  O   VAL B 259     2903   3480   3002   1173   1083    742       O  
ATOM   4343  CB  VAL B 259      22.282  45.667  13.299  1.00 20.77           C  
ANISOU 4343  CB  VAL B 259     2581   3095   2217    371    377    278       C  
ATOM   4344  CG1 VAL B 259      22.250  45.501  11.782  1.00 21.42           C  
ANISOU 4344  CG1 VAL B 259     2598   3304   2235      5    383    367       C  
ATOM   4345  CG2 VAL B 259      23.031  44.513  13.940  1.00 21.34           C  
ANISOU 4345  CG2 VAL B 259     2658   3268   2184    269    149    183       C  
ATOM   4346  N   SER B 260      22.616  48.780  12.048  1.00 23.51           N  
ANISOU 4346  N   SER B 260     2965   3043   2927   1171    972    757       N  
ATOM   4347  CA  SER B 260      21.897  49.914  11.481  1.00 25.95           C  
ANISOU 4347  CA  SER B 260     3183   3406   3273   1001   1139    702       C  
ATOM   4348  C   SER B 260      22.252  50.200  10.032  1.00 24.50           C  
ANISOU 4348  C   SER B 260     3030   3038   3243   1055   1161    874       C  
ATOM   4349  O   SER B 260      23.246  49.698   9.500  1.00 23.58           O  
ANISOU 4349  O   SER B 260     2861   2853   3243    918   1240    873       O  
ATOM   4350  CB  SER B 260      22.154  51.174  12.311  1.00 29.74           C  
ANISOU 4350  CB  SER B 260     3553   4193   3554    474   1155    437       C  
ATOM   4351  OG  SER B 260      23.367  51.803  11.931  1.00 31.50           O  
ANISOU 4351  OG  SER B 260     3571   4711   3686    111   1144    401       O  
ATOM   4352  N   GLY B 261      21.419  51.028   9.407  1.00 24.72           N  
ANISOU 4352  N   GLY B 261     3229   2859   3305   1126    765   1042       N  
ATOM   4353  CA  GLY B 261      21.687  51.544   8.080  1.00 24.14           C  
ANISOU 4353  CA  GLY B 261     3260   2754   3160    837    842    713       C  
ATOM   4354  C   GLY B 261      22.708  52.659   8.171  1.00 24.81           C  
ANISOU 4354  C   GLY B 261     3372   2772   3282    862    679    282       C  
ATOM   4355  O   GLY B 261      23.213  52.971   9.255  1.00 24.27           O  
ANISOU 4355  O   GLY B 261     3285   2707   3228   1036    658    148       O  
ATOM   4356  N   PHE B 262      23.012  53.269   7.034  1.00 25.00           N  
ANISOU 4356  N   PHE B 262     3244   2909   3345    545    719    264       N  
ATOM   4357  CA  PHE B 262      24.056  54.286   6.979  1.00 27.03           C  
ANISOU 4357  CA  PHE B 262     3411   3222   3638    520    496    155       C  
ATOM   4358  C   PHE B 262      23.508  55.608   6.466  1.00 30.01           C  
ANISOU 4358  C   PHE B 262     3686   3701   4016    665    136    259       C  
ATOM   4359  O   PHE B 262      24.220  56.605   6.419  1.00 31.57           O  
ANISOU 4359  O   PHE B 262     3841   3996   4158    719      3    408       O  
ATOM   4360  CB  PHE B 262      25.207  53.810   6.092  1.00 25.63           C  
ANISOU 4360  CB  PHE B 262     3220   3069   3449    405    653     98       C  
ATOM   4361  CG  PHE B 262      26.516  54.500   6.354  1.00 23.63           C  
ANISOU 4361  CG  PHE B 262     3251   2542   3188    343    656    -88       C  
ATOM   4362  CD1 PHE B 262      26.993  55.465   5.487  1.00 21.20           C  
ANISOU 4362  CD1 PHE B 262     3185   1860   3010    729    721    -75       C  
ATOM   4363  CD2 PHE B 262      27.291  54.154   7.445  1.00 23.39           C  
ANISOU 4363  CD2 PHE B 262     3316   2479   3090    145    563   -229       C  
ATOM   4364  CE1 PHE B 262      28.208  56.082   5.715  1.00 20.68           C  
ANISOU 4364  CE1 PHE B 262     3217   1782   2859    696    732   -223       C  
ATOM   4365  CE2 PHE B 262      28.507  54.770   7.675  1.00 23.32           C  
ANISOU 4365  CE2 PHE B 262     3449   2347   3066    152    675   -299       C  
ATOM   4366  CZ  PHE B 262      28.962  55.738   6.808  1.00 21.76           C  
ANISOU 4366  CZ  PHE B 262     3324   1966   2977    292    702   -322       C  
ATOM   4367  N   SER B 263      22.240  55.612   6.076  1.00 32.93           N  
ANISOU 4367  N   SER B 263     4179   4064   4269    739   -193    379       N  
ATOM   4368  CA  SER B 263      21.624  56.834   5.575  1.00 36.52           C  
ANISOU 4368  CA  SER B 263     4616   4703   4555    550   -233    343       C  
ATOM   4369  C   SER B 263      20.987  57.642   6.701  1.00 39.04           C  
ANISOU 4369  C   SER B 263     5026   5096   4712    565   -237    189       C  
ATOM   4370  O   SER B 263      20.887  57.180   7.842  1.00 39.98           O  
ANISOU 4370  O   SER B 263     5182   5289   4719    586   -367    304       O  
ATOM   4371  CB  SER B 263      20.574  56.514   4.509  1.00 37.66           C  
ANISOU 4371  CB  SER B 263     4659   4978   4671    227   -374    374       C  
ATOM   4372  OG  SER B 263      19.314  56.240   5.095  1.00 38.73           O  
ANISOU 4372  OG  SER B 263     4729   5231   4755    -89   -429    346       O  
ATOM   4373  N   GLY B 264      20.567  58.858   6.371  1.00 39.93           N  
ANISOU 4373  N   GLY B 264     5230   5154   4786    678    -61    -12       N  
ATOM   4374  CA  GLY B 264      19.813  59.678   7.300  1.00 41.28           C  
ANISOU 4374  CA  GLY B 264     5467   5293   4923    719    134    -85       C  
ATOM   4375  C   GLY B 264      20.637  60.624   8.149  1.00 42.09           C  
ANISOU 4375  C   GLY B 264     5611   5337   5045    604    440    -84       C  
ATOM   4376  O   GLY B 264      21.746  61.002   7.784  1.00 42.47           O  
ANISOU 4376  O   GLY B 264     5737   5419   4981    684    654   -211       O  
ATOM   4377  N  AGLN B 265      20.101  60.998   9.304  0.55 41.71           N  
ANISOU 4377  N  AGLN B 265     5526   5261   5061    521    602     -8       N  
ATOM   4378  N  BGLN B 265      20.073  61.004   9.290  0.45 42.29           N  
ANISOU 4378  N  BGLN B 265     5595   5341   5133    516    472     19       N  
ATOM   4379  CA AGLN B 265      20.746  61.974  10.170  0.55 41.23           C  
ANISOU 4379  CA AGLN B 265     5404   5161   5099    347    708     99       C  
ATOM   4380  CA BGLN B 265      20.687  61.980  10.174  0.45 42.37           C  
ANISOU 4380  CA BGLN B 265     5553   5321   5223    359    469    136       C  
ATOM   4381  C  AGLN B 265      21.172  61.360  11.497  0.55 40.89           C  
ANISOU 4381  C  AGLN B 265     5316   5117   5103    355    897     61       C  
ATOM   4382  C  BGLN B 265      21.147  61.358  11.478  0.45 41.71           C  
ANISOU 4382  C  BGLN B 265     5407   5250   5191    363    745     81       C  
ATOM   4383  O  AGLN B 265      22.234  60.739  11.612  0.55 39.38           O  
ANISOU 4383  O  AGLN B 265     5161   4789   5012    349   1099      2       O  
ATOM   4384  O  BGLN B 265      22.232  60.782  11.570  0.45 40.78           O  
ANISOU 4384  O  BGLN B 265     5313   5033   5149    342    877     26       O  
ATOM   4385  CB AGLN B 265      19.793  63.127  10.427  0.55 41.08           C  
ANISOU 4385  CB AGLN B 265     5363   5116   5129    198    638    254       C  
ATOM   4386  CB BGLN B 265      19.698  63.107  10.474  0.45 43.02           C  
ANISOU 4386  CB BGLN B 265     5650   5365   5331    236    221    307       C  
ATOM   4387  CG AGLN B 265      20.225  64.455   9.840  0.55 41.05           C  
ANISOU 4387  CG AGLN B 265     5323   5108   5165     17    603    385       C  
ATOM   4388  CG BGLN B 265      19.227  63.859   9.253  0.45 43.65           C  
ANISOU 4388  CG BGLN B 265     5729   5414   5444    126     21    438       C  
ATOM   4389  CD AGLN B 265      19.293  65.586  10.244  0.55 41.30           C  
ANISOU 4389  CD AGLN B 265     5328   5148   5216   -128    575    421       C  
ATOM   4390  CD BGLN B 265      20.271  64.798   8.747  0.45 44.19           C  
ANISOU 4390  CD BGLN B 265     5801   5449   5540     36   -115    480       C  
ATOM   4391  OE1AGLN B 265      18.731  66.294   9.396  0.55 41.68           O  
ANISOU 4391  OE1AGLN B 265     5375   5221   5242   -255    573    429       O  
ATOM   4392  OE1BGLN B 265      21.155  65.209   9.507  0.45 44.40           O  
ANISOU 4392  OE1BGLN B 265     5807   5427   5636     40   -208    493       O  
ATOM   4393  NE2AGLN B 265      19.126  65.766  11.546  0.55 41.18           N  
ANISOU 4393  NE2AGLN B 265     5293   5109   5243   -142    578    417       N  
ATOM   4394  NE2BGLN B 265      20.191  65.144   7.458  0.45 44.20           N  
ANISOU 4394  NE2BGLN B 265     5837   5457   5499    -45    -36    523       N  
ATOM   4395  N   ASP B 266      20.311  61.524  12.497  1.00 41.61           N  
ANISOU 4395  N   ASP B 266     5278   5357   5176    441    933     48       N  
ATOM   4396  CA  ASP B 266      20.533  60.927  13.799  1.00 41.95           C  
ANISOU 4396  CA  ASP B 266     5074   5602   5262    383   1064   -169       C  
ATOM   4397  C   ASP B 266      20.159  59.465  13.697  1.00 41.55           C  
ANISOU 4397  C   ASP B 266     4744   5671   5370    268   1131   -326       C  
ATOM   4398  O   ASP B 266      19.066  59.127  13.242  1.00 42.62           O  
ANISOU 4398  O   ASP B 266     4841   5860   5492    245   1208   -331       O  
ATOM   4399  CB  ASP B 266      19.704  61.625  14.884  1.00 41.55           C  
ANISOU 4399  CB  ASP B 266     5028   5597   5162    485   1217   -268       C  
ATOM   4400  N   ASP B 267      21.082  58.596  14.084  1.00 39.78           N  
ANISOU 4400  N   ASP B 267     4310   5501   5303    153   1146   -459       N  
ATOM   4401  CA  ASP B 267      20.827  57.165  14.057  1.00 38.04           C  
ANISOU 4401  CA  ASP B 267     3946   5315   5194   -107   1128   -662       C  
ATOM   4402  C   ASP B 267      21.283  56.580  15.376  1.00 35.50           C  
ANISOU 4402  C   ASP B 267     3714   4823   4950   -126   1277   -429       C  
ATOM   4403  O   ASP B 267      21.623  57.325  16.300  1.00 34.29           O  
ANISOU 4403  O   ASP B 267     3504   4571   4953   -244   1212   -471       O  
ATOM   4404  CB  ASP B 267      21.539  56.494  12.877  1.00 38.01           C  
ANISOU 4404  CB  ASP B 267     3861   5393   5187   -175    929  -1250       C  
ATOM   4405  CG  ASP B 267      23.050  56.421  13.055  1.00 37.53           C  
ANISOU 4405  CG  ASP B 267     3708   5499   5053   -318    853  -1586       C  
ATOM   4406  OD1 ASP B 267      23.625  57.250  13.787  1.00 37.74           O  
ANISOU 4406  OD1 ASP B 267     3766   5592   4981   -539    756  -1894       O  
ATOM   4407  OD2 ASP B 267      23.674  55.534  12.445  1.00 36.28           O  
ANISOU 4407  OD2 ASP B 267     3394   5490   4901    -49   1017  -1905       O  
ATOM   4408  N   GLU B 268      21.297  55.257  15.470  1.00 34.69           N  
ANISOU 4408  N   GLU B 268     3813   4566   4801   -152   1278   -282       N  
ATOM   4409  CA  GLU B 268      21.733  54.615  16.695  1.00 33.17           C  
ANISOU 4409  CA  GLU B 268     3831   4194   4577     11   1373   -218       C  
ATOM   4410  C   GLU B 268      23.164  54.995  17.056  1.00 28.43           C  
ANISOU 4410  C   GLU B 268     3363   3447   3990   -101   1481   -306       C  
ATOM   4411  O   GLU B 268      23.480  55.127  18.228  1.00 28.53           O  
ANISOU 4411  O   GLU B 268     3350   3413   4077   -168   1492   -635       O  
ATOM   4412  CB  GLU B 268      21.600  53.096  16.586  1.00 36.03           C  
ANISOU 4412  CB  GLU B 268     4298   4492   4901     93   1295      0       C  
ATOM   4413  CG  GLU B 268      20.251  52.576  17.045  1.00 38.92           C  
ANISOU 4413  CG  GLU B 268     4857   4847   5086    332   1249    243       C  
ATOM   4414  CD  GLU B 268      20.304  51.116  17.445  1.00 41.10           C  
ANISOU 4414  CD  GLU B 268     5212   5173   5230    427   1186    447       C  
ATOM   4415  OE1 GLU B 268      20.759  50.295  16.623  1.00 41.58           O  
ANISOU 4415  OE1 GLU B 268     5231   5375   5194    441   1191    570       O  
ATOM   4416  OE2 GLU B 268      19.912  50.794  18.592  1.00 42.17           O  
ANISOU 4416  OE2 GLU B 268     5354   5309   5358    441   1098    378       O  
ATOM   4417  N   PHE B 269      24.028  55.185  16.061  1.00 24.11           N  
ANISOU 4417  N   PHE B 269     2947   2793   3420     91   1442   -193       N  
ATOM   4418  CA  PHE B 269      25.408  55.523  16.375  1.00 19.53           C  
ANISOU 4418  CA  PHE B 269     2594   2041   2784    435   1280    -85       C  
ATOM   4419  C   PHE B 269      25.544  56.954  16.909  1.00 19.69           C  
ANISOU 4419  C   PHE B 269     2608   2076   2797    476    920   -116       C  
ATOM   4420  O   PHE B 269      26.179  57.172  17.934  1.00 18.66           O  
ANISOU 4420  O   PHE B 269     2447   1944   2698    488    966   -208       O  
ATOM   4421  CB  PHE B 269      26.321  55.338  15.162  1.00 18.66           C  
ANISOU 4421  CB  PHE B 269     2796   1849   2447    638   1027    -15       C  
ATOM   4422  CG  PHE B 269      27.751  55.674  15.446  1.00 18.92           C  
ANISOU 4422  CG  PHE B 269     2763   2108   2318    711    785    -24       C  
ATOM   4423  CD1 PHE B 269      28.383  56.717  14.786  1.00 20.64           C  
ANISOU 4423  CD1 PHE B 269     2841   2697   2305    301    720    -57       C  
ATOM   4424  CD2 PHE B 269      28.462  54.968  16.409  1.00 20.00           C  
ANISOU 4424  CD2 PHE B 269     2842   2284   2473    884    632   -165       C  
ATOM   4425  CE1 PHE B 269      29.702  57.029  15.064  1.00 21.56           C  
ANISOU 4425  CE1 PHE B 269     2943   2867   2383    472    689    -54       C  
ATOM   4426  CE2 PHE B 269      29.780  55.288  16.688  1.00 20.05           C  
ANISOU 4426  CE2 PHE B 269     2824   2395   2397    900    571   -369       C  
ATOM   4427  CZ  PHE B 269      30.396  56.313  16.018  1.00 21.13           C  
ANISOU 4427  CZ  PHE B 269     2870   2682   2477    807    644   -251       C  
ATOM   4428  N   THR B 270      24.959  57.925  16.212  1.00 19.04           N  
ANISOU 4428  N   THR B 270     2405   2268   2561    584    729   -101       N  
ATOM   4429  CA  THR B 270      25.053  59.307  16.671  1.00 19.95           C  
ANISOU 4429  CA  THR B 270     2550   2453   2578    781    728    -10       C  
ATOM   4430  C   THR B 270      24.406  59.474  18.034  1.00 19.96           C  
ANISOU 4430  C   THR B 270     2345   2629   2611    707    691    -13       C  
ATOM   4431  O   THR B 270      24.974  60.100  18.923  1.00 19.57           O  
ANISOU 4431  O   THR B 270     2282   2494   2661    613    321   -166       O  
ATOM   4432  CB  THR B 270      24.392  60.281  15.697  1.00 22.93           C  
ANISOU 4432  CB  THR B 270     3109   2925   2679    916    674     21       C  
ATOM   4433  OG1 THR B 270      22.997  59.981  15.603  1.00 26.65           O  
ANISOU 4433  OG1 THR B 270     3469   3560   3095   1219    199   -194       O  
ATOM   4434  CG2 THR B 270      25.011  60.145  14.336  1.00 21.18           C  
ANISOU 4434  CG2 THR B 270     3312   2503   2231   1035    896    250       C  
ATOM   4435  N   ASP B 271      23.220  58.897  18.201  1.00 21.14           N  
ANISOU 4435  N   ASP B 271     2455   3061   2516    777    978    145       N  
ATOM   4436  CA  ASP B 271      22.512  59.019  19.471  1.00 21.83           C  
ANISOU 4436  CA  ASP B 271     2548   3197   2548    515    916    176       C  
ATOM   4437  C   ASP B 271      23.252  58.301  20.598  1.00 20.37           C  
ANISOU 4437  C   ASP B 271     2568   2652   2520    536    845    -99       C  
ATOM   4438  O   ASP B 271      23.169  58.706  21.756  1.00 20.19           O  
ANISOU 4438  O   ASP B 271     2645   2580   2449    418    543   -226       O  
ATOM   4439  CB  ASP B 271      21.084  58.491  19.339  1.00 24.98           C  
ANISOU 4439  CB  ASP B 271     2777   3864   2850    367    748    281       C  
ATOM   4440  CG  ASP B 271      20.167  59.471  18.627  1.00 28.90           C  
ANISOU 4440  CG  ASP B 271     3205   4448   3327    292    478    136       C  
ATOM   4441  OD1 ASP B 271      20.553  60.655  18.484  1.00 30.20           O  
ANISOU 4441  OD1 ASP B 271     3336   4644   3495    767    353    -15       O  
ATOM   4442  OD2 ASP B 271      19.060  59.067  18.222  1.00 30.79           O  
ANISOU 4442  OD2 ASP B 271     3363   4841   3495     82    340    198       O  
ATOM   4443  N   TYR B 272      23.979  57.237  20.259  1.00 19.43           N  
ANISOU 4443  N   TYR B 272     2636   2048   2699    557    629   -296       N  
ATOM   4444  CA  TYR B 272      24.834  56.567  21.228  1.00 19.06           C  
ANISOU 4444  CA  TYR B 272     2647   1828   2768    421    812   -278       C  
ATOM   4445  C   TYR B 272      25.950  57.503  21.695  1.00 18.10           C  
ANISOU 4445  C   TYR B 272     2585   1704   2588    339    824      8       C  
ATOM   4446  O   TYR B 272      26.176  57.667  22.892  1.00 17.88           O  
ANISOU 4446  O   TYR B 272     2581   1727   2485    403    481    -47       O  
ATOM   4447  CB  TYR B 272      25.431  55.278  20.634  1.00 19.92           C  
ANISOU 4447  CB  TYR B 272     2708   1827   3032    367    940   -379       C  
ATOM   4448  CG  TYR B 272      26.537  54.699  21.476  1.00 21.54           C  
ANISOU 4448  CG  TYR B 272     2890   1873   3421    504    861   -409       C  
ATOM   4449  CD1 TYR B 272      26.252  53.934  22.600  1.00 23.31           C  
ANISOU 4449  CD1 TYR B 272     3066   2174   3618    458    668   -300       C  
ATOM   4450  CD2 TYR B 272      27.870  54.930  21.163  1.00 21.38           C  
ANISOU 4450  CD2 TYR B 272     2654   1921   3550    787   1064   -373       C  
ATOM   4451  CE1 TYR B 272      27.263  53.408  23.381  1.00 24.19           C  
ANISOU 4451  CE1 TYR B 272     3193   2205   3792    619    545   -339       C  
ATOM   4452  CE2 TYR B 272      28.883  54.420  21.942  1.00 23.74           C  
ANISOU 4452  CE2 TYR B 272     2948   2343   3729    594    961   -279       C  
ATOM   4453  CZ  TYR B 272      28.576  53.654  23.045  1.00 24.38           C  
ANISOU 4453  CZ  TYR B 272     3167   2221   3874    778    636   -259       C  
ATOM   4454  OH  TYR B 272      29.587  53.140  23.820  1.00 26.82           O  
ANISOU 4454  OH  TYR B 272     3475   2618   4095    837    496   -165       O  
ATOM   4455  N   LEU B 273      26.644  58.128  20.744  1.00 17.84           N  
ANISOU 4455  N   LEU B 273     2481   1760   2539    557    946    138       N  
ATOM   4456  CA  LEU B 273      27.730  59.035  21.096  1.00 17.92           C  
ANISOU 4456  CA  LEU B 273     2349   2040   2419    601   1087     34       C  
ATOM   4457  C   LEU B 273      27.218  60.222  21.901  1.00 18.05           C  
ANISOU 4457  C   LEU B 273     2259   2122   2478    738   1000     42       C  
ATOM   4458  O   LEU B 273      27.794  60.582  22.923  1.00 19.42           O  
ANISOU 4458  O   LEU B 273     2652   2304   2423    658    869    118       O  
ATOM   4459  CB  LEU B 273      28.451  59.546  19.845  1.00 17.38           C  
ANISOU 4459  CB  LEU B 273     2326   1999   2278    726   1063    302       C  
ATOM   4460  CG  LEU B 273      29.279  58.538  19.054  1.00 18.25           C  
ANISOU 4460  CG  LEU B 273     2375   2197   2363    821    814    482       C  
ATOM   4461  CD1 LEU B 273      29.945  59.268  17.905  1.00 18.54           C  
ANISOU 4461  CD1 LEU B 273     2480   2279   2284    821    908    542       C  
ATOM   4462  CD2 LEU B 273      30.317  57.889  19.946  1.00 18.22           C  
ANISOU 4462  CD2 LEU B 273     2336   2250   2337    835    583    597       C  
ATOM   4463  N   VAL B 274      26.144  60.832  21.413  1.00 16.06           N  
ANISOU 4463  N   VAL B 274     1879   1910   2313    380    955    132       N  
ATOM   4464  CA  VAL B 274      25.589  62.007  22.063  1.00 15.96           C  
ANISOU 4464  CA  VAL B 274     1893   1867   2306    553    764     66       C  
ATOM   4465  C   VAL B 274      25.171  61.689  23.497  1.00 16.12           C  
ANISOU 4465  C   VAL B 274     2042   1816   2266    358    681     29       C  
ATOM   4466  O   VAL B 274      25.450  62.466  24.412  1.00 18.25           O  
ANISOU 4466  O   VAL B 274     2482   2163   2290    238    502    160       O  
ATOM   4467  CB  VAL B 274      24.392  62.555  21.281  1.00 16.15           C  
ANISOU 4467  CB  VAL B 274     1896   1901   2341    386    815    -43       C  
ATOM   4468  CG1 VAL B 274      23.674  63.635  22.086  1.00 16.89           C  
ANISOU 4468  CG1 VAL B 274     1881   2082   2454    437    909   -406       C  
ATOM   4469  CG2 VAL B 274      24.859  63.117  19.945  1.00 18.54           C  
ANISOU 4469  CG2 VAL B 274     2348   2244   2454    195    928    149       C  
ATOM   4470  N   ALA B 275      24.509  60.551  23.692  1.00 15.45           N  
ANISOU 4470  N   ALA B 275     1911   1752   2207    474    795   -105       N  
ATOM   4471  CA  ALA B 275      24.036  60.196  25.032  1.00 17.26           C  
ANISOU 4471  CA  ALA B 275     2124   1928   2504    247    648     89       C  
ATOM   4472  C   ALA B 275      25.197  59.883  25.966  1.00 18.62           C  
ANISOU 4472  C   ALA B 275     2258   2217   2598    424    676     49       C  
ATOM   4473  O   ALA B 275      25.168  60.230  27.148  1.00 19.83           O  
ANISOU 4473  O   ALA B 275     2312   2555   2668    341    737   -145       O  
ATOM   4474  CB  ALA B 275      23.077  59.019  24.969  1.00 17.30           C  
ANISOU 4474  CB  ALA B 275     2084   1967   2521    177    601    193       C  
ATOM   4475  N   GLN B 276      26.218  59.218  25.433  1.00 18.40           N  
ANISOU 4475  N   GLN B 276     2188   2157   2645    560    746    233       N  
ATOM   4476  CA  GLN B 276      27.386  58.863  26.226  1.00 19.74           C  
ANISOU 4476  CA  GLN B 276     2419   2373   2708    587    536    262       C  
ATOM   4477  C   GLN B 276      28.164  60.088  26.666  1.00 20.38           C  
ANISOU 4477  C   GLN B 276     2583   2470   2692    628    318    498       C  
ATOM   4478  O   GLN B 276      28.737  60.109  27.751  1.00 22.88           O  
ANISOU 4478  O   GLN B 276     2877   3015   2800    453    210    566       O  
ATOM   4479  CB  GLN B 276      28.309  57.924  25.443  1.00 21.24           C  
ANISOU 4479  CB  GLN B 276     2707   2447   2917    597    499    197       C  
ATOM   4480  CG  GLN B 276      27.778  56.512  25.306  1.00 24.10           C  
ANISOU 4480  CG  GLN B 276     3120   2865   3172    478    253    260       C  
ATOM   4481  CD  GLN B 276      27.643  55.801  26.642  1.00 27.13           C  
ANISOU 4481  CD  GLN B 276     3439   3421   3448    285    143    329       C  
ATOM   4482  OE1 GLN B 276      28.534  55.871  27.489  1.00 29.27           O  
ANISOU 4482  OE1 GLN B 276     3814   3618   3691    229     44    358       O  
ATOM   4483  NE2 GLN B 276      26.525  55.111  26.834  1.00 27.63           N  
ANISOU 4483  NE2 GLN B 276     3282   3673   3543    384    224    322       N  
ATOM   4484  N   LEU B 277      28.162  61.118  25.825  1.00 21.49           N  
ANISOU 4484  N   LEU B 277     2676   2597   2894    326    386    481       N  
ATOM   4485  CA  LEU B 277      29.025  62.274  26.032  1.00 21.99           C  
ANISOU 4485  CA  LEU B 277     2758   2605   2992    359    344    473       C  
ATOM   4486  C   LEU B 277      28.296  63.507  26.558  1.00 24.94           C  
ANISOU 4486  C   LEU B 277     3149   3025   3300    519    416    308       C  
ATOM   4487  O   LEU B 277      28.926  64.529  26.832  1.00 25.43           O  
ANISOU 4487  O   LEU B 277     3211   3046   3404    177    347    258       O  
ATOM   4488  CB  LEU B 277      29.734  62.618  24.718  1.00 21.24           C  
ANISOU 4488  CB  LEU B 277     2554   2656   2860    217    309    683       C  
ATOM   4489  CG  LEU B 277      30.565  61.468  24.144  1.00 20.97           C  
ANISOU 4489  CG  LEU B 277     2461   2790   2718    266    330    748       C  
ATOM   4490  CD1 LEU B 277      30.996  61.767  22.716  1.00 20.02           C  
ANISOU 4490  CD1 LEU B 277     2321   2581   2706     -5    449    683       C  
ATOM   4491  CD2 LEU B 277      31.774  61.190  25.020  1.00 22.47           C  
ANISOU 4491  CD2 LEU B 277     2541   3268   2727     20    211    715       C  
ATOM   4492  N   ALA B 278      26.979  63.414  26.710  1.00 25.80           N  
ANISOU 4492  N   ALA B 278     3298   3179   3324   1029    558    230       N  
ATOM   4493  CA  ALA B 278      26.196  64.566  27.157  1.00 28.34           C  
ANISOU 4493  CA  ALA B 278     3771   3538   3461   1004    651   -257       C  
ATOM   4494  C   ALA B 278      26.324  64.781  28.656  1.00 31.73           C  
ANISOU 4494  C   ALA B 278     4336   4104   3617    840    742   -181       C  
ATOM   4495  O   ALA B 278      26.426  63.825  29.426  1.00 31.36           O  
ANISOU 4495  O   ALA B 278     4364   4133   3419    687    851     10       O  
ATOM   4496  CB  ALA B 278      24.738  64.402  26.778  1.00 27.54           C  
ANISOU 4496  CB  ALA B 278     3598   3381   3485   1220    826   -442       C  
ATOM   4497  OXT ALA B 278      26.314  65.923  29.119  1.00 34.77           O  
ANISOU 4497  OXT ALA B 278     4803   4520   3889    702    649   -193       O  
TER    4498      ALA B 278                                                      
ATOM   4499  O5'  DT C  -2      31.478  24.290   3.885  1.00 46.37           O  
ANISOU 4499  O5'  DT C  -2     5916   5258   6446   -916    799   1325       O  
ATOM   4500  C5'  DT C  -2      30.239  24.448   4.567  1.00 47.78           C  
ANISOU 4500  C5'  DT C  -2     6079   5526   6551   -711    690   1067       C  
ATOM   4501  C4'  DT C  -2      30.405  24.233   6.063  1.00 48.32           C  
ANISOU 4501  C4'  DT C  -2     6079   5655   6625   -686    700    766       C  
ATOM   4502  O4'  DT C  -2      31.386  23.191   6.300  1.00 48.06           O  
ANISOU 4502  O4'  DT C  -2     5954   5678   6627   -829    645    600       O  
ATOM   4503  C3'  DT C  -2      30.896  25.443   6.848  1.00 47.97           C  
ANISOU 4503  C3'  DT C  -2     6059   5536   6632   -715    805    680       C  
ATOM   4504  O3'  DT C  -2      30.352  25.415   8.159  1.00 48.30           O  
ANISOU 4504  O3'  DT C  -2     6146   5538   6670   -606    871    780       O  
ATOM   4505  C2'  DT C  -2      32.400  25.223   6.875  1.00 47.43           C  
ANISOU 4505  C2'  DT C  -2     5905   5535   6580   -893    797    616       C  
ATOM   4506  C1'  DT C  -2      32.469  23.716   7.041  1.00 47.24           C  
ANISOU 4506  C1'  DT C  -2     5793   5624   6531  -1032    690    454       C  
ATOM   4507  N1   DT C  -2      33.723  23.118   6.524  1.00 45.55           N  
ANISOU 4507  N1   DT C  -2     5449   5518   6341  -1589    748    267       N  
ATOM   4508  C2   DT C  -2      34.770  22.912   7.386  1.00 45.63           C  
ANISOU 4508  C2   DT C  -2     5449   5677   6211  -1525    734    133       C  
ATOM   4509  O2   DT C  -2      34.727  23.202   8.568  1.00 46.34           O  
ANISOU 4509  O2   DT C  -2     5475   5937   6195  -1284    735    -18       O  
ATOM   4510  N3   DT C  -2      35.879  22.349   6.814  1.00 44.63           N  
ANISOU 4510  N3   DT C  -2     5389   5479   6088  -1744    819    179       N  
ATOM   4511  C4   DT C  -2      36.040  21.977   5.492  1.00 44.14           C  
ANISOU 4511  C4   DT C  -2     5355   5351   6064  -1872    903    245       C  
ATOM   4512  O4   DT C  -2      37.079  21.475   5.075  1.00 43.97           O  
ANISOU 4512  O4   DT C  -2     5384   5340   5981  -1831   1011    206       O  
ATOM   4513  C5   DT C  -2      34.899  22.220   4.639  1.00 43.99           C  
ANISOU 4513  C5   DT C  -2     5265   5333   6115  -1908    850    277       C  
ATOM   4514  C7   DT C  -2      34.952  21.859   3.184  1.00 44.19           C  
ANISOU 4514  C7   DT C  -2     5263   5411   6114  -1903    830    180       C  
ATOM   4515  C6   DT C  -2      33.810  22.773   5.191  1.00 44.43           C  
ANISOU 4515  C6   DT C  -2     5276   5400   6205  -1898    795    323       C  
ATOM   4516  P    DC C  -1      29.826  26.767   8.851  1.00 48.09           P  
ANISOU 4516  P    DC C  -1     6081   5491   6698   -537    975    877       P  
ATOM   4517  OP1  DC C  -1      29.263  26.407  10.171  1.00 49.74           O  
ANISOU 4517  OP1  DC C  -1     6323   5869   6707   -301   1088    918       O  
ATOM   4518  OP2  DC C  -1      28.989  27.478   7.857  1.00 49.04           O  
ANISOU 4518  OP2  DC C  -1     6232   5641   6760   -573    827    899       O  
ATOM   4519  O5'  DC C  -1      31.156  27.632   9.080  1.00 45.29           O  
ANISOU 4519  O5'  DC C  -1     5656   5097   6457   -518   1036    959       O  
ATOM   4520  C5'  DC C  -1      31.989  27.379  10.211  1.00 42.08           C  
ANISOU 4520  C5'  DC C  -1     5201   4705   6083   -469   1008   1284       C  
ATOM   4521  C4'  DC C  -1      33.325  28.103  10.094  1.00 38.82           C  
ANISOU 4521  C4'  DC C  -1     4749   4295   5705   -421   1005   1587       C  
ATOM   4522  O4'  DC C  -1      34.120  27.515   9.029  1.00 36.73           O  
ANISOU 4522  O4'  DC C  -1     4340   4038   5577   -562    940   1750       O  
ATOM   4523  C3'  DC C  -1      33.246  29.592   9.762  1.00 37.61           C  
ANISOU 4523  C3'  DC C  -1     4745   4087   5459    -72   1044   1620       C  
ATOM   4524  O3'  DC C  -1      34.342  30.254  10.357  1.00 37.25           O  
ANISOU 4524  O3'  DC C  -1     5084   3898   5171    556   1076   1410       O  
ATOM   4525  C2'  DC C  -1      33.386  29.585   8.244  1.00 36.30           C  
ANISOU 4525  C2'  DC C  -1     4281   4021   5490   -451   1083   1770       C  
ATOM   4526  C1'  DC C  -1      34.459  28.525   8.091  1.00 34.21           C  
ANISOU 4526  C1'  DC C  -1     3963   3616   5421   -802   1001   1959       C  
ATOM   4527  N1   DC C  -1      34.529  27.913   6.747  1.00 32.88           N  
ANISOU 4527  N1   DC C  -1     3659   3528   5308   -977    574   1945       N  
ATOM   4528  C2   DC C  -1      35.572  27.034   6.464  1.00 31.70           C  
ANISOU 4528  C2   DC C  -1     3345   3494   5206   -729    484   1675       C  
ATOM   4529  O2   DC C  -1      36.411  26.798   7.345  1.00 31.12           O  
ANISOU 4529  O2   DC C  -1     3292   3481   5050   -654    486   1669       O  
ATOM   4530  N3   DC C  -1      35.639  26.470   5.235  1.00 31.15           N  
ANISOU 4530  N3   DC C  -1     3181   3494   5162  -1005    321   1576       N  
ATOM   4531  C4   DC C  -1      34.714  26.756   4.316  1.00 31.18           C  
ANISOU 4531  C4   DC C  -1     3238   3419   5190  -1157    268   1663       C  
ATOM   4532  N4   DC C  -1      34.823  26.170   3.117  1.00 31.37           N  
ANISOU 4532  N4   DC C  -1     3207   3456   5254  -1277    -28   1371       N  
ATOM   4533  C5   DC C  -1      33.640  27.654   4.585  1.00 31.61           C  
ANISOU 4533  C5   DC C  -1     3505   3381   5123  -1191    301   1761       C  
ATOM   4534  C6   DC C  -1      33.586  28.208   5.801  1.00 31.70           C  
ANISOU 4534  C6   DC C  -1     3657   3350   5036  -1079    389   1846       C  
ATOM   4535  P    DG C   0      34.191  30.986  11.776  1.00 36.92           P  
ANISOU 4535  P    DG C   0     5525   3679   4825   1073   1214   1545       P  
ATOM   4536  OP1  DG C   0      33.511  30.061  12.709  1.00 38.12           O  
ANISOU 4536  OP1  DG C   0     5605   3886   4994   1118   1267   1663       O  
ATOM   4537  OP2  DG C   0      33.620  32.332  11.522  1.00 37.22           O  
ANISOU 4537  OP2  DG C   0     5433   3760   4947   1566   1245   1572       O  
ATOM   4538  O5'  DG C   0      35.704  31.161  12.275  1.00 32.15           O  
ANISOU 4538  O5'  DG C   0     5056   2971   4191    877   1069   1291       O  
ATOM   4539  C5'  DG C   0      36.344  30.079  12.967  1.00 31.00           C  
ANISOU 4539  C5'  DG C   0     5104   2990   3683    383    952    673       C  
ATOM   4540  C4'  DG C   0      37.849  30.016  12.709  1.00 29.62           C  
ANISOU 4540  C4'  DG C   0     5100   2965   3189   -369    982    123       C  
ATOM   4541  O4'  DG C   0      38.121  29.589  11.351  1.00 28.50           O  
ANISOU 4541  O4'  DG C   0     5121   2688   3020   -703   1013   -141       O  
ATOM   4542  C3'  DG C   0      38.623  31.305  12.886  1.00 29.82           C  
ANISOU 4542  C3'  DG C   0     5131   3174   3024   -637    987     11       C  
ATOM   4543  O3'  DG C   0      39.936  30.972  13.312  1.00 31.34           O  
ANISOU 4543  O3'  DG C   0     5285   3558   3066   -728   1037    290       O  
ATOM   4544  C2'  DG C   0      38.621  31.891  11.468  1.00 28.36           C  
ANISOU 4544  C2'  DG C   0     4987   2886   2904   -595    974   -276       C  
ATOM   4545  C1'  DG C   0      38.751  30.631  10.615  1.00 27.44           C  
ANISOU 4545  C1'  DG C   0     4877   2687   2864   -597    962   -349       C  
ATOM   4546  N9   DG C   0      38.066  30.694   9.330  1.00 25.56           N  
ANISOU 4546  N9   DG C   0     4494   2409   2807   -387    954   -151       N  
ATOM   4547  C8   DG C   0      36.895  31.352   9.055  1.00 24.63           C  
ANISOU 4547  C8   DG C   0     4449   2095   2813   -245    966   -236       C  
ATOM   4548  N7   DG C   0      36.479  31.181   7.834  1.00 24.43           N  
ANISOU 4548  N7   DG C   0     4337   2211   2734   -320    945   -108       N  
ATOM   4549  C5   DG C   0      37.424  30.331   7.266  1.00 22.31           C  
ANISOU 4549  C5   DG C   0     4002   1950   2526   -328   1095    -20       C  
ATOM   4550  C6   DG C   0      37.496  29.796   5.958  1.00 21.27           C  
ANISOU 4550  C6   DG C   0     3936   1806   2340   -333    855    175       C  
ATOM   4551  O6   DG C   0      36.709  29.968   5.022  1.00 21.48           O  
ANISOU 4551  O6   DG C   0     4028   1771   2362   -199    414    140       O  
ATOM   4552  N1   DG C   0      38.615  28.979   5.793  1.00 21.17           N  
ANISOU 4552  N1   DG C   0     3760   1883   2399   -323    833    233       N  
ATOM   4553  C2   DG C   0      39.545  28.715   6.769  1.00 21.97           C  
ANISOU 4553  C2   DG C   0     3688   2125   2534   -563   1032    148       C  
ATOM   4554  N2   DG C   0      40.558  27.908   6.423  1.00 23.31           N  
ANISOU 4554  N2   DG C   0     3689   2452   2717   -710    898    292       N  
ATOM   4555  N3   DG C   0      39.488  29.212   8.001  1.00 22.69           N  
ANISOU 4555  N3   DG C   0     3737   2373   2511   -574   1079    -95       N  
ATOM   4556  C4   DG C   0      38.401  30.009   8.175  1.00 22.74           C  
ANISOU 4556  C4   DG C   0     3938   2124   2579   -405   1108    -96       C  
ATOM   4557  P    DA C   1      40.944  32.098  13.846  1.00 33.43           P  
ANISOU 4557  P    DA C   1     5547   3891   3264   -560    835    155       P  
ATOM   4558  OP1  DA C   1      41.734  31.500  14.939  1.00 33.47           O  
ANISOU 4558  OP1  DA C   1     5482   4090   3145   -590    455    505       O  
ATOM   4559  OP2  DA C   1      40.178  33.348  14.070  1.00 33.99           O  
ANISOU 4559  OP2  DA C   1     5612   3916   3387   -429    811      4       O  
ATOM   4560  O5'  DA C   1      41.953  32.296  12.622  1.00 31.04           O  
ANISOU 4560  O5'  DA C   1     5192   3784   2818   -308    731    298       O  
ATOM   4561  C5'  DA C   1      42.892  31.273  12.298  1.00 27.44           C  
ANISOU 4561  C5'  DA C   1     4693   3167   2567   -532    495    477       C  
ATOM   4562  C4'  DA C   1      43.692  31.635  11.054  1.00 25.37           C  
ANISOU 4562  C4'  DA C   1     4249   2921   2470   -713    207    189       C  
ATOM   4563  O4'  DA C   1      42.824  31.631   9.894  1.00 23.26           O  
ANISOU 4563  O4'  DA C   1     3975   2378   2486   -741    280      4       O  
ATOM   4564  C3'  DA C   1      44.337  33.023  11.069  1.00 24.89           C  
ANISOU 4564  C3'  DA C   1     4142   2933   2383   -664     97     25       C  
ATOM   4565  O3'  DA C   1      45.542  32.969  10.342  1.00 26.77           O  
ANISOU 4565  O3'  DA C   1     4557   3177   2436   -691    -50     44       O  
ATOM   4566  C2'  DA C   1      43.309  33.865  10.327  1.00 22.56           C  
ANISOU 4566  C2'  DA C   1     3759   2687   2127   -617    156     18       C  
ATOM   4567  C1'  DA C   1      42.938  32.879   9.234  1.00 21.73           C  
ANISOU 4567  C1'  DA C   1     3563   2373   2319   -574    215     22       C  
ATOM   4568  N9   DA C   1      41.682  33.150   8.572  1.00 19.21           N  
ANISOU 4568  N9   DA C   1     3164   1856   2279    -98    467    -13       N  
ATOM   4569  C8   DA C   1      40.643  33.918   9.022  1.00 19.81           C  
ANISOU 4569  C8   DA C   1     3083   2008   2433     75    374    -26       C  
ATOM   4570  N7   DA C   1      39.625  33.954   8.201  1.00 20.33           N  
ANISOU 4570  N7   DA C   1     3125   2107   2492    255    516    -46       N  
ATOM   4571  C5   DA C   1      40.028  33.144   7.143  1.00 17.33           C  
ANISOU 4571  C5   DA C   1     2907   1453   2224    173    525     13       C  
ATOM   4572  C6   DA C   1      39.402  32.766   5.942  1.00 16.64           C  
ANISOU 4572  C6   DA C   1     2791   1305   2225     -5    509    120       C  
ATOM   4573  N6   DA C   1      38.181  33.167   5.588  1.00 17.74           N  
ANISOU 4573  N6   DA C   1     2787   1586   2368   -261    415    193       N  
ATOM   4574  N1   DA C   1      40.088  31.951   5.110  1.00 16.24           N  
ANISOU 4574  N1   DA C   1     2591   1390   2189     29    567    151       N  
ATOM   4575  C2   DA C   1      41.308  31.548   5.463  1.00 16.21           C  
ANISOU 4575  C2   DA C   1     2447   1588   2124   -270    454     55       C  
ATOM   4576  N3   DA C   1      41.993  31.823   6.568  1.00 16.20           N  
ANISOU 4576  N3   DA C   1     2495   1551   2109   -252    452    -98       N  
ATOM   4577  C4   DA C   1      41.292  32.650   7.364  1.00 17.00           C  
ANISOU 4577  C4   DA C   1     2736   1610   2111   -231    457     -2       C  
ATOM   4578  P    DC C   2      46.845  33.743  10.861  1.00 26.93           P  
ANISOU 4578  P    DC C   2     4865   2905   2462  -1092     36    133       P  
ATOM   4579  OP1  DC C   2      47.401  32.962  11.994  1.00 27.58           O  
ANISOU 4579  OP1  DC C   2     4592   3493   2393   -888     32    295       O  
ATOM   4580  OP2  DC C   2      46.485  35.164  11.051  1.00 30.66           O  
ANISOU 4580  OP2  DC C   2     5484   3351   2814   -597    155    -88       O  
ATOM   4581  O5'  DC C   2      47.860  33.630   9.636  1.00 23.77           O  
ANISOU 4581  O5'  DC C   2     4513   2426   2092  -1307     18    248       O  
ATOM   4582  C5'  DC C   2      48.324  32.359   9.215  1.00 22.20           C  
ANISOU 4582  C5'  DC C   2     4180   2418   1837  -1207     28    232       C  
ATOM   4583  C4'  DC C   2      48.273  32.254   7.706  1.00 19.26           C  
ANISOU 4583  C4'  DC C   2     3745   2014   1560  -1259      8    297       C  
ATOM   4584  O4'  DC C   2      46.906  32.245   7.282  1.00 17.98           O  
ANISOU 4584  O4'  DC C   2     3458   1985   1387  -1015    105    163       O  
ATOM   4585  C3'  DC C   2      48.909  33.427   6.988  1.00 19.37           C  
ANISOU 4585  C3'  DC C   2     3602   2182   1576  -1350   -143    466       C  
ATOM   4586  O3'  DC C   2      50.270  33.133   6.779  1.00 20.77           O  
ANISOU 4586  O3'  DC C   2     3776   2444   1670  -1676   -264    368       O  
ATOM   4587  C2'  DC C   2      48.129  33.495   5.663  1.00 18.12           C  
ANISOU 4587  C2'  DC C   2     3479   1996   1409  -1199   -309    413       C  
ATOM   4588  C1'  DC C   2      46.794  32.806   5.985  1.00 17.24           C  
ANISOU 4588  C1'  DC C   2     3364   1841   1346  -1107   -189    229       C  
ATOM   4589  N1   DC C   2      45.597  33.713   5.983  1.00 17.17           N  
ANISOU 4589  N1   DC C   2     3325   1635   1565   -855    -74    106       N  
ATOM   4590  C2   DC C   2      44.587  33.532   5.030  1.00 16.41           C  
ANISOU 4590  C2   DC C   2     3088   1525   1622   -993    211    -11       C  
ATOM   4591  O2   DC C   2      44.709  32.631   4.200  1.00 15.82           O  
ANISOU 4591  O2   DC C   2     2928   1569   1514   -708    155    113       O  
ATOM   4592  N3   DC C   2      43.501  34.343   5.049  1.00 17.82           N  
ANISOU 4592  N3   DC C   2     3482   1574   1716   -841    351   -132       N  
ATOM   4593  C4   DC C   2      43.405  35.310   5.975  1.00 18.47           C  
ANISOU 4593  C4   DC C   2     3565   1484   1968   -714    253   -168       C  
ATOM   4594  N4   DC C   2      42.315  36.083   5.960  1.00 20.02           N  
ANISOU 4594  N4   DC C   2     3540   1935   2132   -760    701    105       N  
ATOM   4595  C5   DC C   2      44.415  35.504   6.961  1.00 18.89           C  
ANISOU 4595  C5   DC C   2     3622   1486   2069   -850     43     60       C  
ATOM   4596  C6   DC C   2      45.482  34.700   6.930  1.00 18.69           C  
ANISOU 4596  C6   DC C   2     3524   1751   1828  -1010     -7     44       C  
ATOM   4597  P    DC C   3      51.354  34.314   6.859  1.00 23.56           P  
ANISOU 4597  P    DC C   3     4321   2929   1701  -1937    -28    234       P  
ATOM   4598  OP1  DC C   3      52.659  33.676   6.912  1.00 23.86           O  
ANISOU 4598  OP1  DC C   3     4318   2874   1874  -1805   -232    545       O  
ATOM   4599  OP2  DC C   3      50.914  35.309   7.852  1.00 27.58           O  
ANISOU 4599  OP2  DC C   3     4741   3709   2031  -1916    445    -83       O  
ATOM   4600  O5'  DC C   3      51.253  34.999   5.421  1.00 17.38           O  
ANISOU 4600  O5'  DC C   3     3520   1981   1103  -1116    134    117       O  
ATOM   4601  C5'  DC C   3      51.471  34.227   4.278  1.00 15.04           C  
ANISOU 4601  C5'  DC C   3     2905   1735   1076   -652    189    372       C  
ATOM   4602  C4'  DC C   3      51.173  35.058   3.054  1.00 12.75           C  
ANISOU 4602  C4'  DC C   3     2196   1391   1256   -553    131    238       C  
ATOM   4603  O4'  DC C   3      49.810  35.529   3.102  1.00 13.05           O  
ANISOU 4603  O4'  DC C   3     2099   1254   1605   -479    275    180       O  
ATOM   4604  C3'  DC C   3      52.047  36.286   2.866  1.00 11.36           C  
ANISOU 4604  C3'  DC C   3     1885   1156   1276   -387    113    288       C  
ATOM   4605  O3'  DC C   3      52.336  36.397   1.503  1.00 11.16           O  
ANISOU 4605  O3'  DC C   3     1572   1393   1276   -214    112    149       O  
ATOM   4606  C2'  DC C   3      51.153  37.440   3.342  1.00 11.86           C  
ANISOU 4606  C2'  DC C   3     1898   1183   1427   -280    244    117       C  
ATOM   4607  C1'  DC C   3      49.764  36.939   2.973  1.00 13.01           C  
ANISOU 4607  C1'  DC C   3     1980   1336   1625   -483    383    143       C  
ATOM   4608  N1   DC C   3      48.695  37.404   3.877  1.00 12.67           N  
ANISOU 4608  N1   DC C   3     2004   1263   1549   -315    397    167       N  
ATOM   4609  C2   DC C   3      47.579  38.082   3.374  1.00 13.16           C  
ANISOU 4609  C2   DC C   3     2146   1228   1627   -393    514    -16       C  
ATOM   4610  O2   DC C   3      47.512  38.347   2.168  1.00 13.75           O  
ANISOU 4610  O2   DC C   3     2366   1209   1650   -371    344     81       O  
ATOM   4611  N3   DC C   3      46.603  38.458   4.236  1.00 13.80           N  
ANISOU 4611  N3   DC C   3     2227   1467   1552   -692    420   -188       N  
ATOM   4612  C4   DC C   3      46.698  38.151   5.526  1.00 14.24           C  
ANISOU 4612  C4   DC C   3     2195   1456   1760   -308    285    -85       C  
ATOM   4613  N4   DC C   3      45.715  38.548   6.336  1.00 14.75           N  
ANISOU 4613  N4   DC C   3     2168   1534   1904   -306    349   -267       N  
ATOM   4614  C5   DC C   3      47.806  37.433   6.046  1.00 13.79           C  
ANISOU 4614  C5   DC C   3     2181   1294   1766    -17    461    -67       C  
ATOM   4615  C6   DC C   3      48.767  37.077   5.199  1.00 12.89           C  
ANISOU 4615  C6   DC C   3     2139   1228   1530   -248    706    108       C  
ATOM   4616  P    DG C   4      53.720  37.018   0.988  1.00 11.17           P  
ANISOU 4616  P    DG C   4     1629   1218   1396     -9     -3    113       P  
ATOM   4617  OP1  DG C   4      54.333  36.011   0.096  1.00 11.29           O  
ANISOU 4617  OP1  DG C   4     1583   1268   1438     64    101      5       O  
ATOM   4618  OP2  DG C   4      54.496  37.599   2.093  1.00 12.73           O  
ANISOU 4618  OP2  DG C   4     1865   1406   1564   -134   -329     63       O  
ATOM   4619  O5'  DG C   4      53.248  38.244   0.082  1.00 12.07           O  
ANISOU 4619  O5'  DG C   4     1783   1416   1385    -17   -412    130       O  
ATOM   4620  C5'  DG C   4      52.366  38.050  -0.998  1.00 10.92           C  
ANISOU 4620  C5'  DG C   4     1490   1297   1360    167   -371    355       C  
ATOM   4621  C4'  DG C   4      51.928  39.403  -1.537  1.00 11.08           C  
ANISOU 4621  C4'  DG C   4     1473   1244   1493    -17    -61    210       C  
ATOM   4622  O4'  DG C   4      50.962  39.997  -0.634  1.00 12.00           O  
ANISOU 4622  O4'  DG C   4     1788   1299   1470   -161     28    -92       O  
ATOM   4623  C3'  DG C   4      53.046  40.427  -1.658  1.00 11.27           C  
ANISOU 4623  C3'  DG C   4     1509   1324   1451   -356    -54    156       C  
ATOM   4624  O3'  DG C   4      52.761  41.263  -2.742  1.00 12.38           O  
ANISOU 4624  O3'  DG C   4     1734   1534   1436   -126    129    250       O  
ATOM   4625  C2'  DG C   4      52.953  41.190  -0.331  1.00 11.93           C  
ANISOU 4625  C2'  DG C   4     1526   1439   1568   -149    -36   -192       C  
ATOM   4626  C1'  DG C   4      51.451  41.239  -0.127  1.00 12.14           C  
ANISOU 4626  C1'  DG C   4     1796   1320   1496   -137     46   -176       C  
ATOM   4627  N9   DG C   4      51.041  41.287   1.262  1.00 11.71           N  
ANISOU 4627  N9   DG C   4     1929   1104   1417     80   -156      8       N  
ATOM   4628  C8   DG C   4      51.829  41.125   2.379  1.00 11.87           C  
ANISOU 4628  C8   DG C   4     2100    926   1485    -40    -46    -49       C  
ATOM   4629  N7   DG C   4      51.147  41.145   3.490  1.00 10.99           N  
ANISOU 4629  N7   DG C   4     1766    928   1483    -73   -263    -94       N  
ATOM   4630  C5   DG C   4      49.830  41.292   3.081  1.00 10.61           C  
ANISOU 4630  C5   DG C   4     1638   1035   1357    134   -169    -71       C  
ATOM   4631  C6   DG C   4      48.640  41.371   3.838  1.00 11.73           C  
ANISOU 4631  C6   DG C   4     1773   1128   1556    -90    -60   -140       C  
ATOM   4632  O6   DG C   4      48.507  41.305   5.068  1.00 12.86           O  
ANISOU 4632  O6   DG C   4     1901   1386   1601   -109    -58     -4       O  
ATOM   4633  N1   DG C   4      47.523  41.516   3.031  1.00 11.96           N  
ANISOU 4633  N1   DG C   4     1951   1070   1522     -5     13    -29       N  
ATOM   4634  C2   DG C   4      47.546  41.582   1.660  1.00 11.81           C  
ANISOU 4634  C2   DG C   4     1812   1260   1414     14     86    -35       C  
ATOM   4635  N2   DG C   4      46.364  41.718   1.054  1.00 13.02           N  
ANISOU 4635  N2   DG C   4     2157   1451   1338   -180    136     76       N  
ATOM   4636  N3   DG C   4      48.652  41.515   0.940  1.00 11.65           N  
ANISOU 4636  N3   DG C   4     1698   1334   1394   -151     35    123       N  
ATOM   4637  C4   DG C   4      49.751  41.369   1.712  1.00 11.51           C  
ANISOU 4637  C4   DG C   4     1638   1327   1407    -17    -17    -52       C  
ATOM   4638  P    DG C   5      53.867  41.563  -3.858  1.00 12.56           P  
ANISOU 4638  P    DG C   5     1773   1392   1606   -131    -22     63       P  
ATOM   4639  OP1  DG C   5      54.042  40.363  -4.714  1.00 13.44           O  
ANISOU 4639  OP1  DG C   5     1714   1624   1767    -28     78    -16       O  
ATOM   4640  OP2  DG C   5      55.054  42.154  -3.198  1.00 14.21           O  
ANISOU 4640  OP2  DG C   5     1729   1813   1856    -57   -278   -108       O  
ATOM   4641  O5'  DG C   5      53.138  42.655  -4.742  1.00 12.05           O  
ANISOU 4641  O5'  DG C   5     1842   1297   1440    -48    -47    144       O  
ATOM   4642  C5'  DG C   5      51.928  42.289  -5.401  1.00 11.36           C  
ANISOU 4642  C5'  DG C   5     1484   1313   1518    227    112    146       C  
ATOM   4643  C4'  DG C   5      50.940  43.438  -5.403  1.00 11.02           C  
ANISOU 4643  C4'  DG C   5     1644   1180   1363    132    257    106       C  
ATOM   4644  O4'  DG C   5      50.473  43.702  -4.053  1.00 11.55           O  
ANISOU 4644  O4'  DG C   5     2135    954   1300    -76    216     26       O  
ATOM   4645  C3'  DG C   5      51.486  44.744  -5.928  1.00 11.65           C  
ANISOU 4645  C3'  DG C   5     1654   1357   1413     54     77    -97       C  
ATOM   4646  O3'  DG C   5      50.468  45.342  -6.706  1.00 11.91           O  
ANISOU 4646  O3'  DG C   5     1811   1274   1441     23    161    121       O  
ATOM   4647  C2'  DG C   5      51.820  45.537  -4.643  1.00 11.82           C  
ANISOU 4647  C2'  DG C   5     1791   1523   1177   -158    329   -222       C  
ATOM   4648  C1'  DG C   5      50.757  45.053  -3.679  1.00 11.67           C  
ANISOU 4648  C1'  DG C   5     1944   1227   1263   -284    100     71       C  
ATOM   4649  N9   DG C   5      51.165  45.003  -2.280  1.00 11.61           N  
ANISOU 4649  N9   DG C   5     1869   1289   1253   -184     98    251       N  
ATOM   4650  C8   DG C   5      52.347  44.520  -1.772  1.00 12.02           C  
ANISOU 4650  C8   DG C   5     2018   1151   1398    -17     -5     44       C  
ATOM   4651  N7   DG C   5      52.392  44.536  -0.456  1.00 12.23           N  
ANISOU 4651  N7   DG C   5     2020   1168   1457    -58    146     54       N  
ATOM   4652  C5   DG C   5      51.141  45.009  -0.087  1.00 11.57           C  
ANISOU 4652  C5   DG C   5     1965   1098   1334    -63    128    -67       C  
ATOM   4653  C6   DG C   5      50.602  45.242   1.193  1.00 10.99           C  
ANISOU 4653  C6   DG C   5     1675   1152   1349    -15     47    -77       C  
ATOM   4654  O6   DG C   5      51.130  45.027   2.285  1.00 12.38           O  
ANISOU 4654  O6   DG C   5     1866   1388   1451     65   -103      1       O  
ATOM   4655  N1   DG C   5      49.305  45.746   1.132  1.00 11.53           N  
ANISOU 4655  N1   DG C   5     1732   1417   1233    153    -88     35       N  
ATOM   4656  C2   DG C   5      48.609  45.996  -0.029  1.00 10.52           C  
ANISOU 4656  C2   DG C   5     1316   1297   1386    310    -40     -3       C  
ATOM   4657  N2   DG C   5      47.352  46.481   0.101  1.00 11.22           N  
ANISOU 4657  N2   DG C   5     1282   1296   1687    234     53    302       N  
ATOM   4658  N3   DG C   5      49.111  45.784  -1.235  1.00 11.29           N  
ANISOU 4658  N3   DG C   5     1621   1382   1287     45    150     65       N  
ATOM   4659  C4   DG C   5      50.375  45.300  -1.188  1.00 10.74           C  
ANISOU 4659  C4   DG C   5     1680   1175   1226   -147    276     -6       C  
ATOM   4660  P    DT C   6      50.687  46.764  -7.418  1.00 12.64           P  
ANISOU 4660  P    DT C   6     1787   1451   1564    173    256    127       P  
ATOM   4661  OP1  DT C   6      49.810  46.763  -8.602  1.00 14.74           O  
ANISOU 4661  OP1  DT C   6     2132   1729   1740    426    179    -19       O  
ATOM   4662  OP2  DT C   6      52.140  47.030  -7.555  1.00 13.39           O  
ANISOU 4662  OP2  DT C   6     1682   1763   1643    143     74    100       O  
ATOM   4663  O5'  DT C   6      50.071  47.774  -6.360  1.00 12.57           O  
ANISOU 4663  O5'  DT C   6     1713   1426   1637     82    456     65       O  
ATOM   4664  C5'  DT C   6      48.753  47.588  -5.918  1.00 12.82           C  
ANISOU 4664  C5'  DT C   6     1989   1273   1611    393    467    143       C  
ATOM   4665  C4'  DT C   6      48.490  48.453  -4.714  1.00 12.28           C  
ANISOU 4665  C4'  DT C   6     2116   1054   1497    221    245    320       C  
ATOM   4666  O4'  DT C   6      49.386  48.087  -3.660  1.00 12.21           O  
ANISOU 4666  O4'  DT C   6     2009    990   1638    375     87    121       O  
ATOM   4667  C3'  DT C   6      48.705  49.952  -4.927  1.00 12.61           C  
ANISOU 4667  C3'  DT C   6     2018   1145   1627    151    218   -100       C  
ATOM   4668  O3'  DT C   6      47.447  50.585  -4.851  1.00 14.22           O  
ANISOU 4668  O3'  DT C   6     2193   1406   1803    283    225    103       O  
ATOM   4669  C2'  DT C   6      49.661  50.372  -3.779  1.00 13.27           C  
ANISOU 4669  C2'  DT C   6     2218   1221   1604    287    296    -95       C  
ATOM   4670  C1'  DT C   6      49.551  49.196  -2.829  1.00 12.55           C  
ANISOU 4670  C1'  DT C   6     2064   1110   1596    403    143   -167       C  
ATOM   4671  N1   DT C   6      50.741  48.913  -2.001  1.00 13.82           N  
ANISOU 4671  N1   DT C   6     2078   1308   1865    218    142     67       N  
ATOM   4672  C2   DT C   6      50.625  48.961  -0.639  1.00 14.52           C  
ANISOU 4672  C2   DT C   6     2172   1412   1934    180    190   -123       C  
ATOM   4673  O2   DT C   6      49.605  49.312  -0.072  1.00 15.08           O  
ANISOU 4673  O2   DT C   6     2603   1427   1698    367    101    -91       O  
ATOM   4674  N3   DT C   6      51.754  48.598   0.040  1.00 14.15           N  
ANISOU 4674  N3   DT C   6     1893   1340   2142   -189    102    -44       N  
ATOM   4675  C4   DT C   6      52.954  48.173  -0.500  1.00 13.96           C  
ANISOU 4675  C4   DT C   6     1678   1458   2168   -166     69   -181       C  
ATOM   4676  O4   DT C   6      53.913  47.858   0.195  1.00 15.14           O  
ANISOU 4676  O4   DT C   6     2035   1515   2202    227   -150   -276       O  
ATOM   4677  C5   DT C   6      53.004  48.131  -1.939  1.00 12.95           C  
ANISOU 4677  C5   DT C   6     1434   1385   2100   -155    101    -60       C  
ATOM   4678  C7   DT C   6      54.258  47.698  -2.641  1.00 13.47           C  
ANISOU 4678  C7   DT C   6     1182   1681   2253    -67    288     70       C  
ATOM   4679  C6   DT C   6      51.902  48.481  -2.611  1.00 13.74           C  
ANISOU 4679  C6   DT C   6     1798   1337   2084    -39    292    125       C  
ATOM   4680  P    DC C   7      47.195  52.011  -5.549  1.00 13.66           P  
ANISOU 4680  P    DC C   7     2205   1307   1676     58    112    180       P  
ATOM   4681  OP1  DC C   7      45.737  52.124  -5.702  1.00 13.73           O  
ANISOU 4681  OP1  DC C   7     2007   1438   1773    115    210     97       O  
ATOM   4682  OP2  DC C   7      48.095  52.128  -6.720  1.00 15.05           O  
ANISOU 4682  OP2  DC C   7     2451   1582   1684    -41    279     39       O  
ATOM   4683  O5'  DC C   7      47.721  53.060  -4.482  1.00 15.77           O  
ANISOU 4683  O5'  DC C   7     2702   1427   1861    140    184    125       O  
ATOM   4684  C5'  DC C   7      46.945  53.358  -3.341  1.00 15.80           C  
ANISOU 4684  C5'  DC C   7     2709   1461   1834    120    109    -57       C  
ATOM   4685  C4'  DC C   7      47.743  54.193  -2.373  1.00 16.67           C  
ANISOU 4685  C4'  DC C   7     2921   1521   1893    -31     97    150       C  
ATOM   4686  O4'  DC C   7      48.804  53.388  -1.814  1.00 16.58           O  
ANISOU 4686  O4'  DC C   7     2835   1424   2039   -294    206    261       O  
ATOM   4687  C3'  DC C   7      48.445  55.409  -3.009  1.00 16.58           C  
ANISOU 4687  C3'  DC C   7     3024   1250   2023   -335     67    140       C  
ATOM   4688  O3'  DC C   7      48.305  56.535  -2.160  1.00 18.47           O  
ANISOU 4688  O3'  DC C   7     3422   1522   2072    -18    -83    -47       O  
ATOM   4689  C2'  DC C   7      49.899  54.968  -3.049  1.00 17.08           C  
ANISOU 4689  C2'  DC C   7     3024   1352   2114   -268    -13    386       C  
ATOM   4690  C1'  DC C   7      49.933  54.200  -1.749  1.00 17.35           C  
ANISOU 4690  C1'  DC C   7     2957   1540   2097   -310    -37    307       C  
ATOM   4691  N1   DC C   7      51.133  53.367  -1.519  1.00 17.04           N  
ANISOU 4691  N1   DC C   7     2848   1656   1971   -216      2    102       N  
ATOM   4692  C2   DC C   7      51.384  52.929  -0.218  1.00 16.91           C  
ANISOU 4692  C2   DC C   7     2851   1672   1903   -260     46     57       C  
ATOM   4693  O2   DC C   7      50.592  53.250   0.678  1.00 17.84           O  
ANISOU 4693  O2   DC C   7     3187   1728   1864    -30    311   -136       O  
ATOM   4694  N3   DC C   7      52.478  52.177   0.024  1.00 16.17           N  
ANISOU 4694  N3   DC C   7     2754   1512   1880   -333   -116    217       N  
ATOM   4695  C4   DC C   7      53.301  51.868  -0.970  1.00 16.07           C  
ANISOU 4695  C4   DC C   7     2583   1529   1993   -190   -274    172       C  
ATOM   4696  N4   DC C   7      54.373  51.142  -0.676  1.00 16.64           N  
ANISOU 4696  N4   DC C   7     2396   1659   2269    229   -242    406       N  
ATOM   4697  C5   DC C   7      53.067  52.310  -2.316  1.00 16.11           C  
ANISOU 4697  C5   DC C   7     2697   1580   1845   -179   -131    433       C  
ATOM   4698  C6   DC C   7      51.975  53.049  -2.538  1.00 16.72           C  
ANISOU 4698  C6   DC C   7     2805   1764   1784   -166    -13    140       C  
ATOM   4699  P    DG C   8      47.041  57.507  -2.290  1.00 19.36           P  
ANISOU 4699  P    DG C   8     3553   1497   2306    -16    -79    185       P  
ATOM   4700  OP1  DG C   8      45.804  56.745  -2.554  1.00 18.73           O  
ANISOU 4700  OP1  DG C   8     3465   1534   2117   -214    213    113       O  
ATOM   4701  OP2  DG C   8      47.441  58.571  -3.246  1.00 20.63           O  
ANISOU 4701  OP2  DG C   8     3380   2042   2414    -56   -185    263       O  
ATOM   4702  O5'  DG C   8      46.959  58.205  -0.855  1.00 21.16           O  
ANISOU 4702  O5'  DG C   8     3959   1645   2435     90    -48   -120       O  
ATOM   4703  C5'  DG C   8      46.808  57.422   0.324  1.00 21.82           C  
ANISOU 4703  C5'  DG C   8     4072   1787   2432     17   -243   -188       C  
ATOM   4704  C4'  DG C   8      47.899  57.732   1.343  1.00 23.46           C  
ANISOU 4704  C4'  DG C   8     4234   2066   2612    222   -340   -313       C  
ATOM   4705  O4'  DG C   8      49.070  56.909   1.093  1.00 22.67           O  
ANISOU 4705  O4'  DG C   8     4066   1908   2640     78   -350    -47       O  
ATOM   4706  C3'  DG C   8      48.400  59.180   1.356  1.00 24.40           C  
ANISOU 4706  C3'  DG C   8     4255   2315   2701    324   -409   -398       C  
ATOM   4707  O3'  DG C   8      48.425  59.670   2.701  1.00 27.37           O  
ANISOU 4707  O3'  DG C   8     4646   2812   2942    450   -385   -516       O  
ATOM   4708  C2'  DG C   8      49.815  59.068   0.783  1.00 23.79           C  
ANISOU 4708  C2'  DG C   8     4067   2127   2845    198   -576   -413       C  
ATOM   4709  C1'  DG C   8      50.211  57.693   1.293  1.00 23.28           C  
ANISOU 4709  C1'  DG C   8     3970   2162   2714    271   -591   -360       C  
ATOM   4710  N9   DG C   8      51.333  57.078   0.589  1.00 23.04           N  
ANISOU 4710  N9   DG C   8     3852   2214   2688   -127   -665   -481       N  
ATOM   4711  C8   DG C   8      51.609  57.129  -0.757  1.00 22.36           C  
ANISOU 4711  C8   DG C   8     3761   2094   2639   -222   -669   -359       C  
ATOM   4712  N7   DG C   8      52.685  56.466  -1.092  1.00 21.82           N  
ANISOU 4712  N7   DG C   8     3727   1922   2643   -298   -632   -180       N  
ATOM   4713  C5   DG C   8      53.141  55.934   0.110  1.00 22.23           C  
ANISOU 4713  C5   DG C   8     3754   2072   2620   -411   -674   -137       C  
ATOM   4714  C6   DG C   8      54.267  55.122   0.377  1.00 22.79           C  
ANISOU 4714  C6   DG C   8     3799   2192   2669   -466   -553     13       C  
ATOM   4715  O6   DG C   8      55.115  54.700  -0.423  1.00 24.44           O  
ANISOU 4715  O6   DG C   8     3970   2455   2861   -481   -423   -100       O  
ATOM   4716  N1   DG C   8      54.369  54.810   1.731  1.00 23.15           N  
ANISOU 4716  N1   DG C   8     4012   2157   2629   -371   -470     23       N  
ATOM   4717  C2   DG C   8      53.484  55.227   2.703  1.00 23.36           C  
ANISOU 4717  C2   DG C   8     4097   2109   2671      8   -709    110       C  
ATOM   4718  N2   DG C   8      53.741  54.831   3.958  1.00 25.26           N  
ANISOU 4718  N2   DG C   8     4350   2384   2861     68   -964     93       N  
ATOM   4719  N3   DG C   8      52.423  55.985   2.463  1.00 23.98           N  
ANISOU 4719  N3   DG C   8     4126   2299   2686   -115   -741   -252       N  
ATOM   4720  C4   DG C   8      52.318  56.302   1.150  1.00 22.01           C  
ANISOU 4720  C4   DG C   8     3856   1920   2585   -117   -729   -135       C  
TER    4721       DG C   8                                                      
ATOM   4722  O5'  DT D  -2      58.278  56.152   0.845  1.00 32.97           O  
ANISOU 4722  O5'  DT D  -2     4096   3943   4489  -1325   -430   1249       O  
ATOM   4723  C5'  DT D  -2      59.686  56.281   0.935  1.00 33.81           C  
ANISOU 4723  C5'  DT D  -2     4332   3971   4545  -1063   -203   1138       C  
ATOM   4724  C4'  DT D  -2      60.115  56.501   2.373  1.00 34.40           C  
ANISOU 4724  C4'  DT D  -2     4425   3950   4696  -1223     77    927       C  
ATOM   4725  O4'  DT D  -2      59.200  57.435   3.018  1.00 33.45           O  
ANISOU 4725  O4'  DT D  -2     4389   3609   4713  -1460    207    891       O  
ATOM   4726  C3'  DT D  -2      60.106  55.247   3.253  1.00 34.08           C  
ANISOU 4726  C3'  DT D  -2     4347   3848   4754  -1486    168    865       C  
ATOM   4727  O3'  DT D  -2      61.182  55.309   4.173  1.00 35.20           O  
ANISOU 4727  O3'  DT D  -2     4493   4112   4770  -1560    137    628       O  
ATOM   4728  C2'  DT D  -2      58.780  55.384   3.982  1.00 34.29           C  
ANISOU 4728  C2'  DT D  -2     4319   3923   4785  -1398    222    889       C  
ATOM   4729  C1'  DT D  -2      58.792  56.870   4.241  1.00 33.60           C  
ANISOU 4729  C1'  DT D  -2     4210   3724   4832  -1629    314    861       C  
ATOM   4730  N1   DT D  -2      57.476  57.440   4.655  1.00 34.08           N  
ANISOU 4730  N1   DT D  -2     4212   3720   5017  -1637    443    889       N  
ATOM   4731  C2   DT D  -2      57.247  57.655   5.991  1.00 35.99           C  
ANISOU 4731  C2   DT D  -2     4357   4131   5188  -1526    392    943       C  
ATOM   4732  O2   DT D  -2      58.064  57.392   6.853  1.00 38.23           O  
ANISOU 4732  O2   DT D  -2     4611   4612   5304  -1410    348    725       O  
ATOM   4733  N3   DT D  -2      56.026  58.191   6.288  1.00 35.72           N  
ANISOU 4733  N3   DT D  -2     4266   4073   5233  -1488    375   1012       N  
ATOM   4734  C4   DT D  -2      55.025  58.527   5.400  1.00 35.59           C  
ANISOU 4734  C4   DT D  -2     4386   3880   5257  -1403    328   1085       C  
ATOM   4735  O4   DT D  -2      53.953  59.005   5.768  1.00 36.30           O  
ANISOU 4735  O4   DT D  -2     4539   3975   5278  -1116    251   1019       O  
ATOM   4736  C5   DT D  -2      55.328  58.283   4.009  1.00 34.02           C  
ANISOU 4736  C5   DT D  -2     4293   3457   5178  -1640    377   1148       C  
ATOM   4737  C7   DT D  -2      54.315  58.608   2.954  1.00 34.22           C  
ANISOU 4737  C7   DT D  -2     4473   3224   5304  -1526    232   1119       C  
ATOM   4738  C6   DT D  -2      56.528  57.757   3.705  1.00 33.54           C  
ANISOU 4738  C6   DT D  -2     4134   3521   5087  -1694    432    985       C  
ATOM   4739  P    DC D  -1      61.910  53.972   4.683  1.00 35.82           P  
ANISOU 4739  P    DC D  -1     4462   4487   4661  -1690    438    364       P  
ATOM   4740  OP1  DC D  -1      62.983  54.405   5.611  1.00 36.99           O  
ANISOU 4740  OP1  DC D  -1     4386   4752   4917  -1827    279    297       O  
ATOM   4741  OP2  DC D  -1      62.227  53.139   3.502  1.00 37.78           O  
ANISOU 4741  OP2  DC D  -1     4771   4877   4708  -1529    255     77       O  
ATOM   4742  O5'  DC D  -1      60.796  53.224   5.559  1.00 32.91           O  
ANISOU 4742  O5'  DC D  -1     4308   3941   4256  -1431    452    370       O  
ATOM   4743  C5'  DC D  -1      60.589  53.589   6.915  1.00 29.64           C  
ANISOU 4743  C5'  DC D  -1     4038   3344   3881  -1345    363    537       C  
ATOM   4744  C4'  DC D  -1      59.229  53.126   7.400  1.00 26.08           C  
ANISOU 4744  C4'  DC D  -1     3712   2747   3449  -1002      0    356       C  
ATOM   4745  O4'  DC D  -1      58.225  53.408   6.392  1.00 25.06           O  
ANISOU 4745  O4'  DC D  -1     3817   2339   3367   -987   -287    221       O  
ATOM   4746  C3'  DC D  -1      59.087  51.636   7.667  1.00 24.72           C  
ANISOU 4746  C3'  DC D  -1     3627   2612   3151   -654     49    464       C  
ATOM   4747  O3'  DC D  -1      57.972  51.485   8.488  1.00 24.44           O  
ANISOU 4747  O3'  DC D  -1     3647   2760   2879   -439    196    653       O  
ATOM   4748  C2'  DC D  -1      58.771  51.126   6.267  1.00 23.55           C  
ANISOU 4748  C2'  DC D  -1     3621   2172   3156   -491   -228    375       C  
ATOM   4749  C1'  DC D  -1      57.756  52.183   5.849  1.00 24.52           C  
ANISOU 4749  C1'  DC D  -1     3756   2225   3334   -753   -339    338       C  
ATOM   4750  N1   DC D  -1      57.580  52.359   4.378  1.00 24.93           N  
ANISOU 4750  N1   DC D  -1     3686   2374   3413   -742   -249    363       N  
ATOM   4751  C2   DC D  -1      56.466  53.063   3.922  1.00 25.62           C  
ANISOU 4751  C2   DC D  -1     3734   2482   3517   -876   -373    409       C  
ATOM   4752  O2   DC D  -1      55.668  53.515   4.754  1.00 25.85           O  
ANISOU 4752  O2   DC D  -1     3748   2517   3558   -738   -666    403       O  
ATOM   4753  N3   DC D  -1      56.296  53.240   2.588  1.00 25.87           N  
ANISOU 4753  N3   DC D  -1     3742   2546   3544  -1208   -344    363       N  
ATOM   4754  C4   DC D  -1      57.184  52.738   1.732  1.00 26.21           C  
ANISOU 4754  C4   DC D  -1     3837   2640   3481  -1228   -185    280       C  
ATOM   4755  N4   DC D  -1      56.970  52.936   0.424  1.00 27.52           N  
ANISOU 4755  N4   DC D  -1     4040   2746   3669  -1414   -146    371       N  
ATOM   4756  C5   DC D  -1      58.333  52.013   2.177  1.00 25.40           C  
ANISOU 4756  C5   DC D  -1     3724   2501   3427  -1163   -113    156       C  
ATOM   4757  C6   DC D  -1      58.490  51.847   3.498  1.00 24.70           C  
ANISOU 4757  C6   DC D  -1     3690   2274   3422   -885   -141    491       C  
ATOM   4758  P    DG D   0      57.843  50.296   9.556  1.00 23.97           P  
ANISOU 4758  P    DG D   0     3749   2782   2576   -593    162    481       P  
ATOM   4759  OP1  DG D   0      58.618  50.719  10.746  1.00 24.96           O  
ANISOU 4759  OP1  DG D   0     3867   2889   2729   -928     61    287       O  
ATOM   4760  OP2  DG D   0      58.123  48.999   8.914  1.00 23.97           O  
ANISOU 4760  OP2  DG D   0     3824   2775   2506   -560    241    104       O  
ATOM   4761  O5'  DG D   0      56.280  50.361   9.901  1.00 23.61           O  
ANISOU 4761  O5'  DG D   0     3553   2734   2686   -290    153    139       O  
ATOM   4762  C5'  DG D   0      55.739  51.568  10.411  1.00 23.51           C  
ANISOU 4762  C5'  DG D   0     3460   2799   2674   -120     94     17       C  
ATOM   4763  C4'  DG D   0      54.323  51.825   9.910  1.00 21.08           C  
ANISOU 4763  C4'  DG D   0     3179   2421   2409    -85     31     23       C  
ATOM   4764  O4'  DG D   0      54.303  51.990   8.465  1.00 19.89           O  
ANISOU 4764  O4'  DG D   0     3194   2116   2246   -168     62     44       O  
ATOM   4765  C3'  DG D   0      53.293  50.748  10.218  1.00 20.72           C  
ANISOU 4765  C3'  DG D   0     3096   2356   2421   -277    -61    -78       C  
ATOM   4766  O3'  DG D   0      52.041  51.407  10.456  1.00 21.72           O  
ANISOU 4766  O3'  DG D   0     3074   2683   2497   -255     28   -262       O  
ATOM   4767  C2'  DG D   0      53.268  49.938   8.916  1.00 20.04           C  
ANISOU 4767  C2'  DG D   0     3196   2105   2312   -376    154    160       C  
ATOM   4768  C1'  DG D   0      53.401  51.057   7.891  1.00 18.68           C  
ANISOU 4768  C1'  DG D   0     3052   1943   2101   -215    132    133       C  
ATOM   4769  N9   DG D   0      53.958  50.658   6.598  1.00 18.40           N  
ANISOU 4769  N9   DG D   0     3128   1794   2070   -137    -16    110       N  
ATOM   4770  C8   DG D   0      55.110  49.943   6.374  1.00 16.92           C  
ANISOU 4770  C8   DG D   0     3095   1306   2026   -341     31    173       C  
ATOM   4771  N7   DG D   0      55.385  49.787   5.105  1.00 17.59           N  
ANISOU 4771  N7   DG D   0     3112   1545   2028   -328    -28    197       N  
ATOM   4772  C5   DG D   0      54.369  50.477   4.447  1.00 17.86           C  
ANISOU 4772  C5   DG D   0     3090   1622   2075   -390   -118    -60       C  
ATOM   4773  C6   DG D   0      54.140  50.677   3.060  1.00 16.84           C  
ANISOU 4773  C6   DG D   0     2969   1446   1985   -410   -184   -288       C  
ATOM   4774  O6   DG D   0      54.807  50.273   2.107  1.00 17.78           O  
ANISOU 4774  O6   DG D   0     3215   1463   2077   -426    -26    -87       O  
ATOM   4775  N1   DG D   0      52.997  51.427   2.828  1.00 16.44           N  
ANISOU 4775  N1   DG D   0     3008   1428   1811   -240   -149   -255       N  
ATOM   4776  C2   DG D   0      52.180  51.935   3.803  1.00 18.52           C  
ANISOU 4776  C2   DG D   0     3259   1812   1966    185   -237    -43       C  
ATOM   4777  N2   DG D   0      51.120  52.637   3.381  1.00 20.09           N  
ANISOU 4777  N2   DG D   0     3601   2139   1892    560   -155    -52       N  
ATOM   4778  N3   DG D   0      52.383  51.758   5.106  1.00 18.18           N  
ANISOU 4778  N3   DG D   0     3117   1876   1915    179   -191     96       N  
ATOM   4779  C4   DG D   0      53.495  51.031   5.349  1.00 17.86           C  
ANISOU 4779  C4   DG D   0     3085   1713   1990    -56    -91   -106       C  
ATOM   4780  P    DA D   1      50.960  50.832  11.489  1.00 22.50           P  
ANISOU 4780  P    DA D   1     2893   3192   2465    298   -168   -390       P  
ATOM   4781  OP1  DA D   1      50.228  52.022  11.996  1.00 25.16           O  
ANISOU 4781  OP1  DA D   1     3212   3539   2808    619    336   -242       O  
ATOM   4782  OP2  DA D   1      51.615  49.901  12.434  1.00 23.02           O  
ANISOU 4782  OP2  DA D   1     2871   3514   2363    132   -309    172       O  
ATOM   4783  O5'  DA D   1      49.973  49.983  10.563  1.00 22.04           O  
ANISOU 4783  O5'  DA D   1     2730   3089   2554    219   -485   -301       O  
ATOM   4784  C5'  DA D   1      48.989  50.653   9.808  1.00 21.27           C  
ANISOU 4784  C5'  DA D   1     2668   2970   2443    278   -406   -275       C  
ATOM   4785  C4'  DA D   1      48.354  49.727   8.797  1.00 20.28           C  
ANISOU 4785  C4'  DA D   1     2536   2700   2469    170     80    -96       C  
ATOM   4786  O4'  DA D   1      49.238  49.547   7.671  1.00 19.64           O  
ANISOU 4786  O4'  DA D   1     2530   2533   2400    142    263    164       O  
ATOM   4787  C3'  DA D   1      48.034  48.317   9.301  1.00 20.14           C  
ANISOU 4787  C3'  DA D   1     2363   2831   2459    303    206     58       C  
ATOM   4788  O3'  DA D   1      46.799  47.943   8.789  1.00 21.96           O  
ANISOU 4788  O3'  DA D   1     2462   3273   2610    113    -10    -52       O  
ATOM   4789  C2'  DA D   1      49.127  47.472   8.659  1.00 18.51           C  
ANISOU 4789  C2'  DA D   1     2392   2473   2167    131    465    293       C  
ATOM   4790  C1'  DA D   1      49.220  48.190   7.332  1.00 18.12           C  
ANISOU 4790  C1'  DA D   1     2340   2394   2152    -89    258    224       C  
ATOM   4791  N9   DA D   1      50.398  47.881   6.558  1.00 16.67           N  
ANISOU 4791  N9   DA D   1     2228   2096   2009      7     51    110       N  
ATOM   4792  C8   DA D   1      51.518  47.219   6.969  1.00 15.63           C  
ANISOU 4792  C8   DA D   1     2214   1809   1916     63    -97    294       C  
ATOM   4793  N7   DA D   1      52.425  47.091   6.034  1.00 15.59           N  
ANISOU 4793  N7   DA D   1     2256   1762   1905     23    -86    289       N  
ATOM   4794  C5   DA D   1      51.848  47.718   4.933  1.00 14.85           C  
ANISOU 4794  C5   DA D   1     2165   1601   1877   -118   -145    229       C  
ATOM   4795  C6   DA D   1      52.287  47.919   3.612  1.00 14.43           C  
ANISOU 4795  C6   DA D   1     2231   1348   1904   -155     55   -152       C  
ATOM   4796  N6   DA D   1      53.470  47.507   3.156  1.00 15.14           N  
ANISOU 4796  N6   DA D   1     2336   1247   2168    -64    333   -247       N  
ATOM   4797  N1   DA D   1      51.462  48.578   2.777  1.00 15.66           N  
ANISOU 4797  N1   DA D   1     2342   1676   1931    208    110    -44       N  
ATOM   4798  C2   DA D   1      50.277  48.994   3.228  1.00 15.41           C  
ANISOU 4798  C2   DA D   1     2303   1777   1773    100    242    -51       C  
ATOM   4799  N3   DA D   1      49.756  48.861   4.442  1.00 15.86           N  
ANISOU 4799  N3   DA D   1     2366   1800   1858    -14    224     70       N  
ATOM   4800  C4   DA D   1      50.602  48.207   5.249  1.00 14.80           C  
ANISOU 4800  C4   DA D   1     2159   1718   1747    -81     -9    217       C  
ATOM   4801  P    DC D   2      45.546  47.737   9.756  1.00 22.14           P  
ANISOU 4801  P    DC D   2     2380   3559   2472    259   -210     14       P  
ATOM   4802  OP1  DC D   2      45.460  48.935  10.628  1.00 24.52           O  
ANISOU 4802  OP1  DC D   2     2657   4019   2639    425   -503   -209       O  
ATOM   4803  OP2  DC D   2      45.660  46.373  10.314  1.00 23.76           O  
ANISOU 4803  OP2  DC D   2     2681   3528   2820    512   -459    779       O  
ATOM   4804  O5'  DC D   2      44.310  47.734   8.744  1.00 19.01           O  
ANISOU 4804  O5'  DC D   2     1933   3276   2016    163    -98   -107       O  
ATOM   4805  C5'  DC D   2      43.918  48.927   8.122  1.00 16.63           C  
ANISOU 4805  C5'  DC D   2     2020   2627   1673    215     43   -130       C  
ATOM   4806  C4'  DC D   2      43.710  48.706   6.634  1.00 14.84           C  
ANISOU 4806  C4'  DC D   2     2028   2086   1525    115    -38   -187       C  
ATOM   4807  O4'  DC D   2      44.986  48.536   6.005  1.00 14.07           O  
ANISOU 4807  O4'  DC D   2     1999   1796   1551     94     41   -441       O  
ATOM   4808  C3'  DC D   2      42.933  47.449   6.292  1.00 13.41           C  
ANISOU 4808  C3'  DC D   2     1902   1754   1439     61     25   -210       C  
ATOM   4809  O3'  DC D   2      41.554  47.766   6.225  1.00 14.17           O  
ANISOU 4809  O3'  DC D   2     2079   1719   1587    106    237    -84       O  
ATOM   4810  C2'  DC D   2      43.486  47.034   4.916  1.00 13.22           C  
ANISOU 4810  C2'  DC D   2     1749   1779   1496    228     55     10       C  
ATOM   4811  C1'  DC D   2      44.832  47.769   4.816  1.00 13.84           C  
ANISOU 4811  C1'  DC D   2     1987   1706   1565    177    -30    -88       C  
ATOM   4812  N1   DC D   2      46.015  46.893   4.750  1.00 12.48           N  
ANISOU 4812  N1   DC D   2     1974   1279   1489    143    163   -155       N  
ATOM   4813  C2   DC D   2      46.882  46.965   3.652  1.00 12.30           C  
ANISOU 4813  C2   DC D   2     1980   1285   1407    253    104     -6       C  
ATOM   4814  O2   DC D   2      46.617  47.735   2.719  1.00 12.54           O  
ANISOU 4814  O2   DC D   2     2141   1293   1331    137    176    -65       O  
ATOM   4815  N3   DC D   2      47.991  46.193   3.641  1.00 11.93           N  
ANISOU 4815  N3   DC D   2     1894   1099   1541    142    -49    153       N  
ATOM   4816  C4   DC D   2      48.254  45.386   4.673  1.00 12.44           C  
ANISOU 4816  C4   DC D   2     1656   1246   1823    -61     40     13       C  
ATOM   4817  N4   DC D   2      49.366  44.639   4.618  1.00 12.70           N  
ANISOU 4817  N4   DC D   2     1249   1345   2232   -200     66   -237       N  
ATOM   4818  C5   DC D   2      47.394  45.315   5.806  1.00 13.12           C  
ANISOU 4818  C5   DC D   2     1877   1364   1744    -28    183   -244       C  
ATOM   4819  C6   DC D   2      46.303  46.082   5.807  1.00 12.74           C  
ANISOU 4819  C6   DC D   2     1997   1365   1479      2    201   -118       C  
ATOM   4820  P    DC D   3      40.431  46.732   6.709  1.00 14.50           P  
ANISOU 4820  P    DC D   3     2259   1794   1457     69    327     45       P  
ATOM   4821  OP1  DC D   3      39.166  47.478   6.847  1.00 15.72           O  
ANISOU 4821  OP1  DC D   3     2195   1975   1802    249    653     50       O  
ATOM   4822  OP2  DC D   3      40.942  45.927   7.847  1.00 16.35           O  
ANISOU 4822  OP2  DC D   3     2490   2170   1553   -106    336    156       O  
ATOM   4823  O5'  DC D   3      40.269  45.744   5.472  1.00 12.55           O  
ANISOU 4823  O5'  DC D   3     1958   1593   1216    129     62     84       O  
ATOM   4824  C5'  DC D   3      39.981  46.263   4.189  1.00 13.04           C  
ANISOU 4824  C5'  DC D   3     1980   1432   1544    149     66   -167       C  
ATOM   4825  C4'  DC D   3      40.133  45.163   3.157  1.00 12.66           C  
ANISOU 4825  C4'  DC D   3     1636   1312   1862    205    131   -268       C  
ATOM   4826  O4'  DC D   3      41.498  44.679   3.173  1.00 12.51           O  
ANISOU 4826  O4'  DC D   3     1637   1166   1950     64    304   -143       O  
ATOM   4827  C3'  DC D   3      39.249  43.940   3.394  1.00 12.68           C  
ANISOU 4827  C3'  DC D   3     1600   1385   1832     60    -69   -103       C  
ATOM   4828  O3'  DC D   3      38.781  43.494   2.155  1.00 13.26           O  
ANISOU 4828  O3'  DC D   3     1600   1686   1754    -62    147    102       O  
ATOM   4829  C2'  DC D   3      40.210  42.920   4.014  1.00 13.14           C  
ANISOU 4829  C2'  DC D   3     1399   1637   1957    -27     -4    134       C  
ATOM   4830  C1'  DC D   3      41.513  43.275   3.316  1.00 12.30           C  
ANISOU 4830  C1'  DC D   3     1492   1391   1789   -135    138    -59       C  
ATOM   4831  N1   DC D   3      42.717  42.955   4.101  1.00 12.63           N  
ANISOU 4831  N1   DC D   3     1730   1538   1530    194    127    -33       N  
ATOM   4832  C2   DC D   3      43.763  42.259   3.510  1.00 11.64           C  
ANISOU 4832  C2   DC D   3     1722   1342   1357    112     75    108       C  
ATOM   4833  O2   DC D   3      43.638  41.873   2.338  1.00 11.54           O  
ANISOU 4833  O2   DC D   3     1501   1432   1452      8     13    116       O  
ATOM   4834  N3   DC D   3      44.870  42.004   4.238  1.00 11.98           N  
ANISOU 4834  N3   DC D   3     1999   1204   1348     47     45      3       N  
ATOM   4835  C4   DC D   3      44.949  42.413   5.510  1.00 12.23           C  
ANISOU 4835  C4   DC D   3     1804   1442   1399    159    -81     25       C  
ATOM   4836  N4   DC D   3      46.063  42.138   6.189  1.00 13.66           N  
ANISOU 4836  N4   DC D   3     1971   1581   1638    -25   -159    -22       N  
ATOM   4837  C5   DC D   3      43.895  43.140   6.123  1.00 12.18           C  
ANISOU 4837  C5   DC D   3     1711   1458   1460     94    -23      3       C  
ATOM   4838  C6   DC D   3      42.814  43.398   5.384  1.00 12.46           C  
ANISOU 4838  C6   DC D   3     1834   1570   1331     36    103    -58       C  
ATOM   4839  P    DG D   4      37.307  42.911   1.984  1.00 13.29           P  
ANISOU 4839  P    DG D   4     1678   1539   1831    332    231    -14       P  
ATOM   4840  OP1  DG D   4      36.570  43.830   1.104  1.00 13.87           O  
ANISOU 4840  OP1  DG D   4     1793   1538   1940    314    168    116       O  
ATOM   4841  OP2  DG D   4      36.739  42.531   3.298  1.00 14.05           O  
ANISOU 4841  OP2  DG D   4     1538   1966   1836    272    204    -18       O  
ATOM   4842  O5'  DG D   4      37.560  41.549   1.209  1.00 14.55           O  
ANISOU 4842  O5'  DG D   4     2191   1611   1726    248    375    -62       O  
ATOM   4843  C5'  DG D   4      38.145  41.572  -0.062  1.00 15.15           C  
ANISOU 4843  C5'  DG D   4     2277   1718   1762    360    438   -195       C  
ATOM   4844  C4'  DG D   4      38.549  40.173  -0.469  1.00 15.66           C  
ANISOU 4844  C4'  DG D   4     2312   1686   1952     89    201   -305       C  
ATOM   4845  O4'  DG D   4      39.693  39.738   0.299  1.00 15.60           O  
ANISOU 4845  O4'  DG D   4     2333   1513   2081   -142    392     60       O  
ATOM   4846  C3'  DG D   4      37.490  39.111  -0.251  1.00 15.37           C  
ANISOU 4846  C3'  DG D   4     2130   1649   2062    -69    384   -171       C  
ATOM   4847  O3'  DG D   4      37.635  38.138  -1.254  1.00 16.01           O  
ANISOU 4847  O3'  DG D   4     2005   1686   2391    -45    336   -206       O  
ATOM   4848  C2'  DG D   4      37.852  38.536   1.118  1.00 15.18           C  
ANISOU 4848  C2'  DG D   4     2167   1530   2071    193    254   -170       C  
ATOM   4849  C1'  DG D   4      39.368  38.572   1.062  1.00 15.14           C  
ANISOU 4849  C1'  DG D   4     2385   1343   2023   -291    256    -17       C  
ATOM   4850  N9   DG D   4      40.009  38.773   2.339  1.00 14.60           N  
ANISOU 4850  N9   DG D   4     2581   1179   1787   -138    404   -168       N  
ATOM   4851  C8   DG D   4      39.426  39.190   3.516  1.00 16.23           C  
ANISOU 4851  C8   DG D   4     2954   1172   2042   -187    207   -152       C  
ATOM   4852  N7   DG D   4      40.284  39.376   4.476  1.00 15.59           N  
ANISOU 4852  N7   DG D   4     2899   1155   1872      6    157     23       N  
ATOM   4853  C5   DG D   4      41.515  39.100   3.886  1.00 14.61           C  
ANISOU 4853  C5   DG D   4     2529   1287   1735     -9    463     71       C  
ATOM   4854  C6   DG D   4      42.821  39.139   4.423  1.00 15.54           C  
ANISOU 4854  C6   DG D   4     2691   1481   1733    -27    680    242       C  
ATOM   4855  O6   DG D   4      43.169  39.437   5.567  1.00 15.69           O  
ANISOU 4855  O6   DG D   4     2667   1457   1837     98    579    312       O  
ATOM   4856  N1   DG D   4      43.789  38.793   3.476  1.00 13.79           N  
ANISOU 4856  N1   DG D   4     2612   1091   1538    -62    624      9       N  
ATOM   4857  C2   DG D   4      43.526  38.448   2.178  1.00 14.17           C  
ANISOU 4857  C2   DG D   4     2358   1308   1718    119    541    -23       C  
ATOM   4858  N2   DG D   4      44.589  38.148   1.414  1.00 12.97           N  
ANISOU 4858  N2   DG D   4     1965   1443   1521     14    616   -187       N  
ATOM   4859  N3   DG D   4      42.309  38.411   1.657  1.00 13.93           N  
ANISOU 4859  N3   DG D   4     2233   1377   1684     82    487   -253       N  
ATOM   4860  C4   DG D   4      41.355  38.753   2.567  1.00 14.58           C  
ANISOU 4860  C4   DG D   4     2456   1350   1735    -70    405    -24       C  
ATOM   4861  P    DG D   5      36.370  37.625  -2.073  1.00 15.74           P  
ANISOU 4861  P    DG D   5     1856   1591   2534     28    363     41       P  
ATOM   4862  OP1  DG D   5      35.999  38.618  -3.107  1.00 16.85           O  
ANISOU 4862  OP1  DG D   5     1815   1782   2807    -34    323     71       O  
ATOM   4863  OP2  DG D   5      35.357  37.193  -1.085  1.00 18.10           O  
ANISOU 4863  OP2  DG D   5     2182   1860   2835    262    446    208       O  
ATOM   4864  O5'  DG D   5      36.968  36.365  -2.834  1.00 15.59           O  
ANISOU 4864  O5'  DG D   5     1818   1696   2409     62    425   -146       O  
ATOM   4865  C5'  DG D   5      38.006  36.591  -3.763  1.00 14.57           C  
ANISOU 4865  C5'  DG D   5     1424   1715   2397    287    281   -245       C  
ATOM   4866  C4'  DG D   5      39.002  35.454  -3.738  1.00 13.95           C  
ANISOU 4866  C4'  DG D   5     1450   1490   2359    217     71   -166       C  
ATOM   4867  O4'  DG D   5      39.706  35.430  -2.474  1.00 13.28           O  
ANISOU 4867  O4'  DG D   5     1689   1136   2220    -13     17   -101       O  
ATOM   4868  C3'  DG D   5      38.406  34.071  -3.918  1.00 13.56           C  
ANISOU 4868  C3'  DG D   5     1281   1480   2393    126    203    -19       C  
ATOM   4869  O3'  DG D   5      39.290  33.340  -4.721  1.00 13.49           O  
ANISOU 4869  O3'  DG D   5     1139   1539   2445      3    -55   -278       O  
ATOM   4870  C2'  DG D   5      38.309  33.535  -2.478  1.00 13.87           C  
ANISOU 4870  C2'  DG D   5     1508   1590   2172   -156    220    186       C  
ATOM   4871  C1'  DG D   5      39.517  34.183  -1.813  1.00 13.99           C  
ANISOU 4871  C1'  DG D   5     1870   1398   2049   -182    176     78       C  
ATOM   4872  N9   DG D   5      39.377  34.494  -0.392  1.00 14.03           N  
ANISOU 4872  N9   DG D   5     2090   1229   2013     51    304   -145       N  
ATOM   4873  C8   DG D   5      38.297  35.079   0.231  1.00 14.61           C  
ANISOU 4873  C8   DG D   5     2288   1361   1903     43    378   -138       C  
ATOM   4874  N7   DG D   5      38.492  35.301   1.501  1.00 13.89           N  
ANISOU 4874  N7   DG D   5     2231   1166   1879   -155    420      9       N  
ATOM   4875  C5   DG D   5      39.788  34.853   1.732  1.00 14.45           C  
ANISOU 4875  C5   DG D   5     2208   1328   1955   -366    409    144       C  
ATOM   4876  C6   DG D   5      40.551  34.837   2.923  1.00 14.67           C  
ANISOU 4876  C6   DG D   5     2293   1418   1861   -430    518     36       C  
ATOM   4877  O6   DG D   5      40.225  35.255   4.045  1.00 16.95           O  
ANISOU 4877  O6   DG D   5     2791   1573   2075   -140    366   -108       O  
ATOM   4878  N1   DG D   5      41.821  34.288   2.731  1.00 14.21           N  
ANISOU 4878  N1   DG D   5     2153   1320   1926   -261    495   -153       N  
ATOM   4879  C2   DG D   5      42.298  33.828   1.521  1.00 13.01           C  
ANISOU 4879  C2   DG D   5     1959   1225   1759   -106    360   -146       C  
ATOM   4880  N2   DG D   5      43.556  33.347   1.519  1.00 12.54           N  
ANISOU 4880  N2   DG D   5     1803   1212   1750     27    276   -264       N  
ATOM   4881  N3   DG D   5      41.592  33.843   0.399  1.00 14.17           N  
ANISOU 4881  N3   DG D   5     2033   1462   1887   -287    160    122       N  
ATOM   4882  C4   DG D   5      40.347  34.361   0.576  1.00 13.71           C  
ANISOU 4882  C4   DG D   5     2049   1241   1921   -242    190    -64       C  
ATOM   4883  P    DT D   6      38.984  31.819  -5.128  1.00 13.33           P  
ANISOU 4883  P    DT D   6     1286   1484   2293     14   -197   -220       P  
ATOM   4884  OP1  DT D   6      39.572  31.640  -6.463  1.00 15.92           O  
ANISOU 4884  OP1  DT D   6     1823   1692   2534    109   -119   -284       O  
ATOM   4885  OP2  DT D   6      37.554  31.515  -4.893  1.00 14.51           O  
ANISOU 4885  OP2  DT D   6     1004   1982   2527     86     -4   -331       O  
ATOM   4886  O5'  DT D   6      39.820  30.990  -4.050  1.00 12.68           O  
ANISOU 4886  O5'  DT D   6     1274   1487   2058    -27   -388   -180       O  
ATOM   4887  C5'  DT D   6      41.217  31.212  -3.933  1.00 11.17           C  
ANISOU 4887  C5'  DT D   6     1175   1350   1717    163   -651     21       C  
ATOM   4888  C4'  DT D   6      41.745  30.581  -2.669  1.00 12.17           C  
ANISOU 4888  C4'  DT D   6     1520   1234   1870     76   -166   -320       C  
ATOM   4889  O4'  DT D   6      41.103  31.175  -1.520  1.00 13.80           O  
ANISOU 4889  O4'  DT D   6     1929   1286   2029    236   -109   -208       O  
ATOM   4890  C3'  DT D   6      41.506  29.077  -2.567  1.00 13.26           C  
ANISOU 4890  C3'  DT D   6     1659   1330   2049     46    -28   -162       C  
ATOM   4891  O3'  DT D   6      42.772  28.417  -2.570  1.00 12.89           O  
ANISOU 4891  O3'  DT D   6     1606   1214   2079     41    -14   -132       O  
ATOM   4892  C2'  DT D   6      40.729  28.897  -1.246  1.00 13.71           C  
ANISOU 4892  C2'  DT D   6     1931   1335   1942    -27    -81   -302       C  
ATOM   4893  C1'  DT D   6      41.028  30.200  -0.513  1.00 13.65           C  
ANISOU 4893  C1'  DT D   6     1875   1372   1937    146     86   -226       C  
ATOM   4894  N1   DT D   6      40.002  30.665   0.449  1.00 13.80           N  
ANISOU 4894  N1   DT D   6     1925   1289   2027    223     52    -12       N  
ATOM   4895  C2   DT D   6      40.358  30.844   1.761  1.00 13.98           C  
ANISOU 4895  C2   DT D   6     1856   1415   2040     62    141   -111       C  
ATOM   4896  O2   DT D   6      41.452  30.549   2.197  1.00 15.04           O  
ANISOU 4896  O2   DT D   6     2049   1612   2052    -26    269    -80       O  
ATOM   4897  N3   DT D   6      39.373  31.364   2.561  1.00 14.67           N  
ANISOU 4897  N3   DT D   6     1833   1334   2408    110    235    167       N  
ATOM   4898  C4   DT D   6      38.103  31.735   2.170  1.00 15.28           C  
ANISOU 4898  C4   DT D   6     1890   1479   2436   -138    289    213       C  
ATOM   4899  O4   DT D   6      37.294  32.202   2.955  1.00 16.19           O  
ANISOU 4899  O4   DT D   6     1951   1520   2679    252    248    220       O  
ATOM   4900  C5   DT D   6      37.796  31.537   0.774  1.00 15.48           C  
ANISOU 4900  C5   DT D   6     1929   1516   2438    -41    176     79       C  
ATOM   4901  C7   DT D   6      36.438  31.898   0.244  1.00 15.89           C  
ANISOU 4901  C7   DT D   6     1783   1583   2671      0     90    -80       C  
ATOM   4902  C6   DT D   6      38.755  31.032  -0.014  1.00 14.26           C  
ANISOU 4902  C6   DT D   6     1867   1300   2250      4     34     85       C  
ATOM   4903  P    DC D   7      42.904  26.863  -2.985  1.00 12.90           P  
ANISOU 4903  P    DC D   7     1545   1209   2146    -88   -226    -95       P  
ATOM   4904  OP1  DC D   7      44.298  26.700  -3.420  1.00 14.16           O  
ANISOU 4904  OP1  DC D   7     1510   1675   2196     18   -149    -74       O  
ATOM   4905  OP2  DC D   7      41.807  26.494  -3.904  1.00 15.71           O  
ANISOU 4905  OP2  DC D   7     1609   1792   2569   -220   -297     91       O  
ATOM   4906  O5'  DC D   7      42.662  26.095  -1.635  1.00 13.29           O  
ANISOU 4906  O5'  DC D   7     1566   1297   2187   -323   -208    -86       O  
ATOM   4907  C5'  DC D   7      43.667  26.099  -0.642  1.00 13.94           C  
ANISOU 4907  C5'  DC D   7     1616   1520   2161   -320   -140     26       C  
ATOM   4908  C4'  DC D   7      43.184  25.416   0.606  1.00 13.93           C  
ANISOU 4908  C4'  DC D   7     1529   1414   2348   -450    194    -27       C  
ATOM   4909  O4'  DC D   7      42.192  26.236   1.256  1.00 15.14           O  
ANISOU 4909  O4'  DC D   7     1982   1449   2320   -562    185     -1       O  
ATOM   4910  C3'  DC D   7      42.505  24.067   0.356  1.00 13.80           C  
ANISOU 4910  C3'  DC D   7     1550   1264   2428   -376      3     68       C  
ATOM   4911  O3'  DC D   7      42.882  23.171   1.370  1.00 14.88           O  
ANISOU 4911  O3'  DC D   7     1638   1607   2411     20   -223    354       O  
ATOM   4912  C2'  DC D   7      41.028  24.412   0.467  1.00 13.92           C  
ANISOU 4912  C2'  DC D   7     1555   1326   2409   -250    104     -2       C  
ATOM   4913  C1'  DC D   7      41.108  25.408   1.600  1.00 14.57           C  
ANISOU 4913  C1'  DC D   7     1709   1390   2438   -398    134    -71       C  
ATOM   4914  N1   DC D   7      39.923  26.263   1.787  1.00 15.43           N  
ANISOU 4914  N1   DC D   7     1842   1601   2420   -117     21     64       N  
ATOM   4915  C2   DC D   7      39.767  26.907   3.009  1.00 15.35           C  
ANISOU 4915  C2   DC D   7     1897   1592   2344   -381    254     90       C  
ATOM   4916  O2   DC D   7      40.613  26.720   3.890  1.00 15.55           O  
ANISOU 4916  O2   DC D   7     1884   1706   2317   -415    240    -34       O  
ATOM   4917  N3   DC D   7      38.699  27.715   3.194  1.00 14.97           N  
ANISOU 4917  N3   DC D   7     1905   1300   2483   -464    247    -36       N  
ATOM   4918  C4   DC D   7      37.825  27.894   2.209  1.00 15.70           C  
ANISOU 4918  C4   DC D   7     1988   1410   2569   -269    238    162       C  
ATOM   4919  N4   DC D   7      36.783  28.692   2.443  1.00 15.88           N  
ANISOU 4919  N4   DC D   7     1951   1211   2873   -197    284    230       N  
ATOM   4920  C5   DC D   7      37.971  27.248   0.942  1.00 14.99           C  
ANISOU 4920  C5   DC D   7     1822   1528   2345   -283    182     96       C  
ATOM   4921  C6   DC D   7      39.032  26.452   0.775  1.00 15.35           C  
ANISOU 4921  C6   DC D   7     1718   1731   2383   -325    186    200       C  
ATOM   4922  P    DG D   8      44.090  22.149   1.131  1.00 15.70           P  
ANISOU 4922  P    DG D   8     1668   1564   2733   -196   -242     89       P  
ATOM   4923  OP1  DG D   8      45.251  22.882   0.572  1.00 16.24           O  
ANISOU 4923  OP1  DG D   8     1577   1679   2915   -258     88     81       O  
ATOM   4924  OP2  DG D   8      43.561  20.971   0.379  1.00 17.92           O  
ANISOU 4924  OP2  DG D   8     1917   2042   2851   -313   -305    -96       O  
ATOM   4925  O5'  DG D   8      44.426  21.651   2.594  1.00 16.52           O  
ANISOU 4925  O5'  DG D   8     1834   1579   2863   -406   -215    118       O  
ATOM   4926  C5'  DG D   8      44.994  22.529   3.547  1.00 17.46           C  
ANISOU 4926  C5'  DG D   8     1979   1774   2882   -352   -160     72       C  
ATOM   4927  C4'  DG D   8      44.314  22.357   4.889  1.00 20.07           C  
ANISOU 4927  C4'  DG D   8     2256   2267   3102   -143    -37    420       C  
ATOM   4928  O4'  DG D   8      43.023  23.020   4.857  1.00 19.87           O  
ANISOU 4928  O4'  DG D   8     2095   2364   3092   -176    -25    306       O  
ATOM   4929  C3'  DG D   8      44.031  20.909   5.290  1.00 22.36           C  
ANISOU 4929  C3'  DG D   8     2785   2467   3246   -165     55    482       C  
ATOM   4930  O3'  DG D   8      44.189  20.757   6.698  1.00 26.17           O  
ANISOU 4930  O3'  DG D   8     3373   3108   3461   -167    136    470       O  
ATOM   4931  C2'  DG D   8      42.574  20.718   4.868  1.00 20.73           C  
ANISOU 4931  C2'  DG D   8     2345   2291   3242   -394     81    605       C  
ATOM   4932  C1'  DG D   8      41.996  22.090   5.168  1.00 20.08           C  
ANISOU 4932  C1'  DG D   8     2135   2384   3110   -303     55    562       C  
ATOM   4933  N9   DG D   8      40.827  22.432   4.361  1.00 21.30           N  
ANISOU 4933  N9   DG D   8     2360   2604   3130   -646     34    614       N  
ATOM   4934  C8   DG D   8      40.521  21.978   3.099  1.00 22.69           C  
ANISOU 4934  C8   DG D   8     2513   2802   3306   -718   -169    561       C  
ATOM   4935  N7   DG D   8      39.415  22.484   2.622  1.00 22.64           N  
ANISOU 4935  N7   DG D   8     2425   2785   3394   -851   -197    580       N  
ATOM   4936  C5   DG D   8      38.967  23.330   3.628  1.00 23.06           C  
ANISOU 4936  C5   DG D   8     2466   2801   3496   -984   -151    618       C  
ATOM   4937  C6   DG D   8      37.816  24.159   3.688  1.00 24.37           C  
ANISOU 4937  C6   DG D   8     2669   2854   3738  -1302   -275    815       C  
ATOM   4938  O6   DG D   8      36.932  24.315   2.835  1.00 26.42           O  
ANISOU 4938  O6   DG D   8     2887   3221   3932  -1260   -347   1228       O  
ATOM   4939  N1   DG D   8      37.744  24.851   4.887  1.00 23.90           N  
ANISOU 4939  N1   DG D   8     2695   2572   3815  -1189   -137    806       N  
ATOM   4940  C2   DG D   8      38.660  24.763   5.901  1.00 23.15           C  
ANISOU 4940  C2   DG D   8     2702   2383   3712   -946    118    695       C  
ATOM   4941  N2   DG D   8      38.411  25.500   6.980  1.00 23.16           N  
ANISOU 4941  N2   DG D   8     2807   2206   3786   -796    248    546       N  
ATOM   4942  N3   DG D   8      39.741  23.995   5.864  1.00 22.27           N  
ANISOU 4942  N3   DG D   8     2590   2433   3437   -942    201    835       N  
ATOM   4943  C4   DG D   8      39.829  23.309   4.701  1.00 22.01           C  
ANISOU 4943  C4   DG D   8     2464   2523   3374   -723     44    777       C  
TER    4944       DG D   8                                                      
HETATM 4945  O   HOH A 301      65.233  48.675  17.963  1.00 44.00           O  
HETATM 4946  O   HOH A 302      40.968  24.445  19.234  1.00 51.80           O  
HETATM 4947  O   HOH A 303      75.697  34.880  16.048  1.00 43.11           O  
HETATM 4948  O   HOH A 304      56.318  54.600  -7.052  1.00 87.47           O  
HETATM 4949  O   HOH A 305      39.302  12.547  -3.612  1.00 33.57           O  
HETATM 4950  O   HOH A 306      65.803  19.922 -14.779  1.00 40.65           O  
HETATM 4951  O   HOH A 307      54.707  45.547   4.786  1.00 18.90           O  
HETATM 4952  O   HOH A 308      59.588  30.295 -14.454  1.00 42.22           O  
HETATM 4953  O   HOH A 309      72.931  22.340  16.868  1.00 32.86           O  
HETATM 4954  O   HOH A 310      54.948  41.146  -7.260  1.00 24.35           O  
HETATM 4955  O   HOH A 311      66.082  28.447 -16.313  1.00 37.14           O  
HETATM 4956  O   HOH A 312      69.317  36.934  -4.782  1.00 28.45           O  
HETATM 4957  O   HOH A 313      68.376  48.731  -7.285  1.00 39.75           O  
HETATM 4958  O   HOH A 314      55.579  44.436  -1.924  1.00 15.70           O  
HETATM 4959  O   HOH A 315      50.466  30.954  22.698  1.00 25.97           O  
HETATM 4960  O   HOH A 316      68.218  12.440  13.792  1.00 33.79           O  
HETATM 4961  O   HOH A 317      49.901  25.582 -15.101  1.00 27.90           O  
HETATM 4962  O   HOH A 318      55.761  45.734  21.435  1.00 28.50           O  
HETATM 4963  O   HOH A 319      47.391  26.414  10.372  1.00 24.92           O  
HETATM 4964  O   HOH A 320      68.064  40.680  -6.046  1.00 21.47           O  
HETATM 4965  O   HOH A 321      72.880  39.954   6.899  1.00 42.59           O  
HETATM 4966  O   HOH A 322      73.481  37.352   5.806  1.00 33.70           O  
HETATM 4967  O   HOH A 323      67.212  43.827   8.364  1.00 21.59           O  
HETATM 4968  O   HOH A 324      60.630  33.032 -11.113  1.00 26.84           O  
HETATM 4969  O   HOH A 325      53.318  14.123  -4.660  1.00 32.46           O  
HETATM 4970  O   HOH A 326      59.450  27.472 -14.982  1.00 28.32           O  
HETATM 4971  O   HOH A 327      48.195  37.906  10.511  1.00 49.64           O  
HETATM 4972  O   HOH A 328      50.297  32.517  24.572  1.00 59.15           O  
HETATM 4973  O   HOH A 329      57.016  18.686  18.868  1.00 22.38           O  
HETATM 4974  O   HOH A 330      62.424  33.154  26.566  1.00 26.86           O  
HETATM 4975  O   HOH A 331      53.798  45.889  -9.318  1.00 16.34           O  
HETATM 4976  O   HOH A 332      41.238   9.683  -6.810  1.00 36.73           O  
HETATM 4977  O   HOH A 333      54.753  53.797  -5.260  1.00 32.50           O  
HETATM 4978  O   HOH A 334      70.689  26.559   8.390  1.00 29.84           O  
HETATM 4979  O   HOH A 335      60.731  32.036  28.219  1.00 37.13           O  
HETATM 4980  O   HOH A 336      43.283  31.273  23.612  1.00 35.48           O  
HETATM 4981  O   HOH A 337      45.734  25.095  13.825  1.00 34.73           O  
HETATM 4982  O   HOH A 338      69.972  35.003  22.378  1.00 33.23           O  
HETATM 4983  O   HOH A 339      57.642  44.871 -20.662  1.00 40.82           O  
HETATM 4984  O   HOH A 340      62.259  49.212 -10.415  1.00 24.03           O  
HETATM 4985  O   HOH A 341      46.700  23.594  31.000  1.00 33.21           O  
HETATM 4986  O   HOH A 342      63.258  28.021 -16.937  1.00 38.09           O  
HETATM 4987  O   HOH A 343      66.484  33.400  24.683  1.00 36.36           O  
HETATM 4988  O   HOH A 344      45.789  20.556  -3.528  1.00 13.99           O  
HETATM 4989  O   HOH A 345      54.542  34.653 -12.028  1.00 23.52           O  
HETATM 4990  O   HOH A 346      49.259  16.671   0.920  1.00 21.05           O  
HETATM 4991  O   HOH A 347      55.062  17.674   3.490  1.00 22.64           O  
HETATM 4992  O   HOH A 348      50.038  38.001  -4.697  1.00 13.72           O  
HETATM 4993  O   HOH A 349      65.130  43.192   6.838  1.00 16.12           O  
HETATM 4994  O   HOH A 350      49.991  31.498 -16.390  1.00 47.29           O  
HETATM 4995  O   HOH A 351      48.376  37.094  20.158  1.00 19.80           O  
HETATM 4996  O   HOH A 352      63.793  28.834  12.974  1.00 22.97           O  
HETATM 4997  O   HOH A 353      75.521  32.984   0.185  1.00 43.87           O  
HETATM 4998  O   HOH A 354      44.428  24.706   7.912  1.00 32.72           O  
HETATM 4999  O   HOH A 355      48.407  19.263  29.943  1.00 28.12           O  
HETATM 5000  O   HOH A 356      72.971  21.277  -0.562  1.00 27.24           O  
HETATM 5001  O   HOH A 357      50.155  29.457   9.191  1.00 40.07           O  
HETATM 5002  O   HOH A 358      57.355  42.006  -5.033  1.00 15.99           O  
HETATM 5003  O   HOH A 359      62.461  46.219  -3.082  1.00 19.58           O  
HETATM 5004  O   HOH A 360      57.734  42.069  25.765  1.00 28.40           O  
HETATM 5005  O   HOH A 361      52.611  33.615  13.199  1.00 28.44           O  
HETATM 5006  O   HOH A 362      61.864  47.009   2.890  1.00 28.85           O  
HETATM 5007  O   HOH A 363      68.267  21.738 -15.059  1.00 51.56           O  
HETATM 5008  O   HOH A 364      49.043  28.578  13.456  1.00 23.71           O  
HETATM 5009  O   HOH A 365      50.712  20.746 -11.284  1.00 32.53           O  
HETATM 5010  O   HOH A 366      67.833  44.616   4.394  1.00 23.73           O  
HETATM 5011  O   HOH A 367      41.990  34.768 -10.570  1.00 27.61           O  
HETATM 5012  O   HOH A 368      49.491  26.191  12.234  1.00 22.57           O  
HETATM 5013  O   HOH A 369      57.947  23.706  29.845  1.00 46.90           O  
HETATM 5014  O   HOH A 370      39.926  28.309  23.633  1.00 32.32           O  
HETATM 5015  O   HOH A 371      43.056  16.740  -5.288  1.00 29.42           O  
HETATM 5016  O   HOH A 372      50.463  16.091   4.493  1.00 32.46           O  
HETATM 5017  O   HOH A 373      45.039  28.629  14.408  1.00 40.95           O  
HETATM 5018  O   HOH A 374      50.064  36.158  10.397  1.00 28.26           O  
HETATM 5019  O   HOH A 375      53.155  15.525  21.516  1.00 26.08           O  
HETATM 5020  O   HOH A 376      74.221  24.774  21.786  1.00 31.48           O  
HETATM 5021  O   HOH A 377      59.328  11.449  17.724  1.00 34.24           O  
HETATM 5022  O   HOH A 378      54.163  30.791   8.156  1.00 19.94           O  
HETATM 5023  O   HOH A 379      42.629  24.449  -8.068  1.00 34.24           O  
HETATM 5024  O   HOH A 380      66.700  50.831   7.968  1.00 33.35           O  
HETATM 5025  O   HOH A 381      60.925  26.226  28.228  1.00 31.75           O  
HETATM 5026  O   HOH A 382      59.244  40.667   6.334  1.00 18.77           O  
HETATM 5027  O   HOH A 383      48.442  18.563  19.614  1.00 21.55           O  
HETATM 5028  O   HOH A 384      48.844  29.610   5.141  1.00 21.24           O  
HETATM 5029  O   HOH A 385      51.092  18.889   5.711  1.00 20.58           O  
HETATM 5030  O   HOH A 386      72.831  30.040  18.547  1.00 33.98           O  
HETATM 5031  O   HOH A 387      74.747  28.793  -8.794  1.00 33.04           O  
HETATM 5032  O   HOH A 388      63.008  15.904  15.896  1.00 19.46           O  
HETATM 5033  O   HOH A 389      49.521  21.177  -4.611  1.00 16.92           O  
HETATM 5034  O   HOH A 390      66.887  35.764 -19.910  1.00 32.01           O  
HETATM 5035  O   HOH A 391      54.296  15.426  17.288  1.00 37.15           O  
HETATM 5036  O   HOH A 392      46.360  37.896  -2.426  1.00 11.66           O  
HETATM 5037  O   HOH A 393      73.240  35.881  12.944  1.00 22.86           O  
HETATM 5038  O   HOH A 394      69.707  34.312  -3.913  1.00 24.19           O  
HETATM 5039  O   HOH A 395      64.374  18.409 -10.487  1.00 31.90           O  
HETATM 5040  O   HOH A 396      62.512  15.593   7.971  1.00 36.56           O  
HETATM 5041  O   HOH A 397      69.445  28.618  -0.017  1.00 17.74           O  
HETATM 5042  O   HOH A 398      62.249  45.712   0.678  1.00 21.38           O  
HETATM 5043  O   HOH A 399      46.055  39.534  25.141  1.00 33.63           O  
HETATM 5044  O   HOH A 400      67.649  36.234  21.715  1.00 20.08           O  
HETATM 5045  O   HOH A 401      50.130  18.307  21.964  1.00 19.39           O  
HETATM 5046  O   HOH A 402      57.802  16.606  -8.756  1.00 32.26           O  
HETATM 5047  O   HOH A 403      48.415  34.229 -12.536  1.00 34.17           O  
HETATM 5048  O   HOH A 404      75.531  34.649  -8.401  1.00 36.23           O  
HETATM 5049  O   HOH A 405      71.653  47.042  19.669  1.00 35.76           O  
HETATM 5050  O   HOH A 406      45.613  36.157  -8.448  1.00 16.94           O  
HETATM 5051  O   HOH A 407      72.085  30.555   1.922  1.00 22.04           O  
HETATM 5052  O   HOH A 408      44.049  30.056 -11.789  1.00 26.33           O  
HETATM 5053  O   HOH A 409      46.380  18.708   8.987  1.00 29.63           O  
HETATM 5054  O   HOH A 410      43.344  38.190  -5.915  1.00 13.68           O  
HETATM 5055  O   HOH A 411      48.248  12.438  -7.455  1.00 34.94           O  
HETATM 5056  O   HOH A 412      54.399  33.418   1.428  1.00 11.60           O  
HETATM 5057  O   HOH A 413      66.670  22.467   3.147  1.00 49.08           O  
HETATM 5058  O   HOH A 414      71.813  51.704   8.811  1.00 41.35           O  
HETATM 5059  O   HOH A 415      56.194  38.332  28.994  1.00 37.56           O  
HETATM 5060  O   HOH A 416      54.943  46.816   7.520  1.00 24.82           O  
HETATM 5061  O   HOH A 417      76.986  27.499  -5.064  1.00 48.29           O  
HETATM 5062  O   HOH A 418      51.671  18.464  12.254  1.00 20.13           O  
HETATM 5063  O   HOH A 419      51.248  16.262 -11.483  1.00 44.58           O  
HETATM 5064  O   HOH A 420      43.794  19.367  20.104  1.00 21.99           O  
HETATM 5065  O   HOH A 421      37.757  28.835  -8.561  1.00 34.23           O  
HETATM 5066  O   HOH A 422      73.229  34.522  -2.470  1.00 25.69           O  
HETATM 5067  O   HOH A 423      62.456   7.525  22.338  1.00 42.74           O  
HETATM 5068  O   HOH A 424      52.178  33.750  10.364  1.00 19.66           O  
HETATM 5069  O   HOH A 425      62.683  20.255 -18.064  1.00 37.99           O  
HETATM 5070  O   HOH A 426      54.187  18.372  33.482  1.00 30.73           O  
HETATM 5071  O   HOH A 427      69.269  45.793   6.391  1.00 36.88           O  
HETATM 5072  O   HOH A 428      45.330  18.750  -5.010  1.00 31.61           O  
HETATM 5073  O   HOH A 429      69.437  20.051  24.353  1.00 34.63           O  
HETATM 5074  O   HOH A 430      62.191  39.616  26.825  1.00 28.55           O  
HETATM 5075  O   HOH A 431      59.445  23.288 -15.299  1.00 34.21           O  
HETATM 5076  O   HOH A 432      42.926  28.718  23.594  1.00 26.59           O  
HETATM 5077  O   HOH A 433      63.530  47.583  -0.567  1.00 25.84           O  
HETATM 5078  O   HOH A 434      47.916  30.858 -12.903  1.00 34.45           O  
HETATM 5079  O   HOH A 435      59.655  15.328  11.285  1.00 34.51           O  
HETATM 5080  O   HOH A 436      56.691  16.080  14.506  1.00 27.16           O  
HETATM 5081  O   HOH A 437      38.536  28.141  -6.006  1.00 32.33           O  
HETATM 5082  O   HOH A 438      45.775  29.024  30.576  1.00 41.97           O  
HETATM 5083  O   HOH A 439      68.832  47.529  19.594  1.00 32.74           O  
HETATM 5084  O   HOH A 440      46.326  18.327  11.671  1.00 33.43           O  
HETATM 5085  O   HOH A 441      69.995  27.699   2.324  1.00 18.88           O  
HETATM 5086  O   HOH A 442      56.373  25.663 -16.522  1.00 33.20           O  
HETATM 5087  O   HOH A 443      73.552  28.142  -4.373  1.00 20.58           O  
HETATM 5088  O   HOH A 444      60.971  51.111  -2.677  1.00 29.88           O  
HETATM 5089  O   HOH A 445      76.130  46.353  20.872  1.00 34.79           O  
HETATM 5090  O   HOH A 446      70.996  35.406 -16.449  1.00 30.55           O  
HETATM 5091  O   HOH A 447      47.213  25.477   3.445  1.00 15.17           O  
HETATM 5092  O   HOH A 448      66.941  44.892  -8.880  1.00 42.98           O  
HETATM 5093  O   HOH A 449      56.894  18.830   7.774  1.00 18.65           O  
HETATM 5094  O   HOH A 450      71.163  45.586  17.444  1.00 27.69           O  
HETATM 5095  O   HOH A 451      50.109  17.507  17.797  1.00 35.85           O  
HETATM 5096  O   HOH A 452      61.873  18.140  -0.150  1.00 32.16           O  
HETATM 5097  O   HOH A 453      66.987  18.590   6.760  1.00 41.13           O  
HETATM 5098  O   HOH A 454      54.427  18.753  11.906  1.00 16.15           O  
HETATM 5099  O   HOH A 455      43.454  30.128  31.091  1.00 31.14           O  
HETATM 5100  O   HOH A 456      50.193  39.211  26.434  1.00 33.23           O  
HETATM 5101  O   HOH A 457      49.394  36.623  -2.373  1.00 12.01           O  
HETATM 5102  O   HOH A 458      76.891  22.824  16.435  1.00 41.50           O  
HETATM 5103  O   HOH A 459      64.640  54.248  12.310  1.00 35.02           O  
HETATM 5104  O   HOH A 460      68.256  42.807  -8.329  1.00 28.90           O  
HETATM 5105  O   HOH A 461      70.756  32.187  12.457  1.00 31.38           O  
HETATM 5106  O   HOH A 462      70.110  29.320  12.190  1.00 26.50           O  
HETATM 5107  O   HOH A 463      59.295  16.188 -11.332  1.00 47.78           O  
HETATM 5108  O   HOH A 464      66.014  40.147  -4.237  1.00 18.30           O  
HETATM 5109  O   HOH A 465      48.693  37.597  -9.343  1.00 33.88           O  
HETATM 5110  O   HOH A 466      64.084  46.847   6.176  1.00 23.67           O  
HETATM 5111  O   HOH A 467      69.890  43.063 -18.061  1.00 37.79           O  
HETATM 5112  O   HOH A 468      54.100  37.366 -11.448  1.00 29.12           O  
HETATM 5113  O   HOH A 469      70.443  53.957   5.854  1.00 35.17           O  
HETATM 5114  O   HOH A 470      64.449  12.639  19.652  1.00 23.11           O  
HETATM 5115  O   HOH A 471      68.517  32.246  11.037  1.00 21.51           O  
HETATM 5116  O   HOH A 472      66.418  14.370  25.357  1.00 33.97           O  
HETATM 5117  O   HOH A 473      74.409  32.128  10.961  1.00 34.99           O  
HETATM 5118  O   HOH A 474      74.758  35.918  10.351  1.00 39.48           O  
HETATM 5119  O   HOH A 475      50.661  22.531  31.460  1.00 43.56           O  
HETATM 5120  O   HOH A 476      72.795  31.129 -15.351  1.00 42.51           O  
HETATM 5121  O   HOH A 477      52.433  30.179  10.309  1.00 30.31           O  
HETATM 5122  O   HOH A 478      73.363  49.239  11.979  1.00 38.17           O  
HETATM 5123  O   HOH A 479      73.712  29.422  11.324  1.00 30.11           O  
HETATM 5124  O   HOH A 480      76.407  29.417  -6.752  1.00 32.93           O  
HETATM 5125  O   HOH A 481      58.650  51.396  17.221  1.00 45.00           O  
HETATM 5126  O   HOH A 482      43.460  23.500  15.876  1.00 25.50           O  
HETATM 5127  O   HOH A 483      46.832  21.654  -5.377  1.00 28.19           O  
HETATM 5128  O   HOH A 484      70.993  38.130  -0.640  1.00 25.31           O  
HETATM 5129  O   HOH A 485      53.138  39.340 -20.793  1.00 36.99           O  
HETATM 5130  O   HOH A 486      58.299  33.793  34.104  1.00 48.28           O  
HETATM 5131  O   HOH A 487      56.979  41.323  -0.906  1.00 13.83           O  
HETATM 5132  O   HOH A 488      75.146  26.184  -5.692  1.00 29.81           O  
HETATM 5133  O   HOH A 489      50.001  44.053   7.893  1.00  8.46           O  
HETATM 5134  O   HOH A 490      68.369  20.888   4.709  1.00 34.55           O  
HETATM 5135  O   HOH A 491      62.720  49.132  -3.386  1.00 19.62           O  
HETATM 5136  O   HOH A 492      65.190  24.697  30.091  1.00 44.94           O  
HETATM 5137  O   HOH A 493      69.934  15.023   8.389  1.00 35.30           O  
HETATM 5138  O   HOH A 494      62.334  45.771 -13.768  1.00 30.90           O  
HETATM 5139  O   HOH A 495      46.042  38.760  -8.303  1.00 21.51           O  
HETATM 5140  O   HOH A 496      57.002  35.381 -13.414  1.00 24.23           O  
HETATM 5141  O   HOH A 497      46.134  25.871  29.863  1.00 23.70           O  
HETATM 5142  O   HOH A 498      43.574  33.562  20.968  1.00 22.74           O  
HETATM 5143  O   HOH A 499      42.901  28.576 -14.505  1.00 27.35           O  
HETATM 5144  O   HOH A 500      73.006  38.462  16.395  1.00 41.16           O  
HETATM 5145  O   HOH A 501      56.816  30.158 -18.151  1.00 44.50           O  
HETATM 5146  O   HOH A 502      65.139  32.556  26.888  1.00 36.60           O  
HETATM 5147  O   HOH A 503      58.451  16.558   8.514  1.00 31.38           O  
HETATM 5148  O   HOH A 504      57.842  39.234  26.480  1.00 29.56           O  
HETATM 5149  O   HOH A 505      45.520  17.148  19.340  1.00 32.04           O  
HETATM 5150  O   HOH A 506      44.132  16.655   3.066  1.00 43.22           O  
HETATM 5151  O   HOH A 507      58.704  14.066  14.109  1.00 43.40           O  
HETATM 5152  O   HOH A 508      50.659  15.477  22.393  1.00 27.67           O  
HETATM 5153  O   HOH A 509      49.417  16.603   7.065  1.00 43.09           O  
HETATM 5154  O   HOH A 510      59.369  34.060 -13.234  1.00 35.63           O  
HETATM 5155  O   HOH A 511      54.840  41.839   3.568  1.00 16.39           O  
HETATM 5156  O   HOH A 512      55.104  15.064  -9.469  1.00 37.33           O  
HETATM 5157  O   HOH A 513      50.092  47.097  15.642  1.00 38.03           O  
HETATM 5158  O   HOH A 514      66.173  48.716  20.345  1.00 42.36           O  
HETATM 5159  O   HOH A 515      69.208  13.006   9.741  1.00 32.90           O  
HETATM 5160  O   HOH A 516      47.963  28.891   9.245  1.00 41.75           O  
HETATM 5161  O   HOH A 517      50.006  14.385  24.965  1.00 30.58           O  
HETATM 5162  O   HOH A 518      49.159  40.462  -5.704  1.00 15.53           O  
HETATM 5163  O   HOH A 519      46.402  26.900  32.556  1.00 47.58           O  
HETATM 5164  O   HOH A 520      68.434  11.956  22.506  1.00 39.38           O  
HETATM 5165  O   HOH A 521      75.089  31.069 -10.585  1.00 48.19           O  
HETATM 5166  O   HOH A 522      65.759  50.703  -0.308  1.00 42.11           O  
HETATM 5167  O   HOH A 523      52.339  34.561 -13.920  1.00 45.56           O  
HETATM 5168  O   HOH A 524      69.805  51.419   6.637  1.00 41.25           O  
HETATM 5169  O   HOH A 525      50.286  14.133   0.398  1.00 35.51           O  
HETATM 5170  O   HOH A 526      62.464  46.596 -11.682  1.00 37.52           O  
HETATM 5171  O   HOH A 527      59.857  48.286   4.317  1.00 33.00           O  
HETATM 5172  O   HOH A 528      61.999  14.257  10.484  1.00 42.24           O  
HETATM 5173  O   HOH A 529      44.970  39.483  -4.185  1.00 12.73           O  
HETATM 5174  O   HOH A 530      74.343  37.088  14.981  1.00 41.60           O  
HETATM 5175  O   HOH A 531      74.396  31.229   2.915  1.00 40.49           O  
HETATM 5176  O   HOH A 532      55.338  16.981   6.224  1.00 30.49           O  
HETATM 5177  O   HOH A 533      69.512  45.019   1.939  1.00 27.21           O  
HETATM 5178  O   HOH A 534      50.703  17.252  10.010  1.00 28.47           O  
HETATM 5179  O   HOH A 535      43.458  16.966  -1.071  1.00 43.58           O  
HETATM 5180  O   HOH A 536      65.430  46.716 -18.906  1.00 35.84           O  
HETATM 5181  O   HOH A 537      71.558  44.056   1.786  1.00 47.89           O  
HETATM 5182  O   HOH A 538      60.561  24.077  29.725  1.00 39.65           O  
HETATM 5183  O   HOH A 539      52.735  18.292   7.818  1.00 23.72           O  
HETATM 5184  O   HOH A 540      50.240  40.494  -8.188  1.00 27.30           O  
HETATM 5185  O   HOH A 541      55.463  16.208  12.204  1.00 30.30           O  
HETATM 5186  O   HOH A 542      52.188  15.539  19.023  1.00 38.32           O  
HETATM 5187  O   HOH A 543      68.596  14.321   2.069  1.00 33.41           O  
HETATM 5188  O   HOH A 544      54.644  19.422   9.213  1.00 20.68           O  
HETATM 5189  O   HOH A 545      44.053  34.747 -12.635  1.00 33.25           O  
HETATM 5190  O   HOH A 546      46.476  36.035 -11.219  1.00 26.82           O  
HETATM 5191  O   HOH A 547      68.250  44.619 -15.908  1.00 40.87           O  
HETATM 5192  O   HOH B 301      39.348  51.312  21.462  1.00 57.77           O  
HETATM 5193  O   HOH B 302      33.077  74.951  25.081  1.00 43.29           O  
HETATM 5194  O   HOH B 303      45.772  46.673  22.225  1.00 27.24           O  
HETATM 5195  O   HOH B 304      16.837  67.513   9.180  1.00 77.53           O  
HETATM 5196  O   HOH B 305      30.049  35.454  24.705  1.00 41.11           O  
HETATM 5197  O   HOH B 306      19.468  74.126  11.732  1.00 31.81           O  
HETATM 5198  O   HOH B 307      33.915  34.560  12.941  1.00 47.55           O  
HETATM 5199  O   HOH B 308      43.262  49.648  12.047  1.00 29.84           O  
HETATM 5200  O   HOH B 309      39.557  35.264  12.061  1.00 37.19           O  
HETATM 5201  O   HOH B 310      28.861  52.190  25.991  1.00 34.43           O  
HETATM 5202  O   HOH B 311      45.709  40.525  22.512  1.00 30.01           O  
HETATM 5203  O   HOH B 312      35.013  35.414   0.679  1.00 22.00           O  
HETATM 5204  O   HOH B 313      42.972  52.141   8.338  1.00 34.59           O  
HETATM 5205  O   HOH B 314      46.199  63.528  15.571  1.00 47.48           O  
HETATM 5206  O   HOH B 315      30.462  29.816  20.000  1.00 42.23           O  
HETATM 5207  O   HOH B 316      25.868  38.069  12.925  1.00 21.96           O  
HETATM 5208  O   HOH B 317      25.746  63.331   7.010  1.00 42.10           O  
HETATM 5209  O   HOH B 318      26.127  61.304  29.376  1.00 41.99           O  
HETATM 5210  O   HOH B 319      20.134  41.831  11.632  1.00 39.25           O  
HETATM 5211  O   HOH B 320      47.803  56.244   4.877  1.00 28.93           O  
HETATM 5212  O   HOH B 321      38.242  64.445  16.245  1.00 21.31           O  
HETATM 5213  O   HOH B 322      41.013  61.433   2.487  1.00 23.32           O  
HETATM 5214  O   HOH B 323      31.825  69.791  26.307  1.00 40.31           O  
HETATM 5215  O   HOH B 324      27.619  38.521  10.964  1.00 16.75           O  
HETATM 5216  O   HOH B 325      30.063  53.567  13.695  1.00 23.31           O  
HETATM 5217  O   HOH B 326      51.213  52.922  19.684  1.00 34.88           O  
HETATM 5218  O   HOH B 327      43.329  78.258  21.851  1.00 37.79           O  
HETATM 5219  O   HOH B 328      27.083  42.244  33.120  1.00 42.81           O  
HETATM 5220  O   HOH B 329      27.540  31.040  14.582  1.00 31.93           O  
HETATM 5221  O   HOH B 330      19.764  38.595  17.679  1.00 36.71           O  
HETATM 5222  O   HOH B 331      42.106  63.060   9.013  1.00 27.36           O  
HETATM 5223  O   HOH B 332      45.903  55.169  31.622  1.00 47.06           O  
HETATM 5224  O   HOH B 333      47.303  60.900  27.767  1.00 29.38           O  
HETATM 5225  O   HOH B 334      42.765  67.575  17.791  1.00 21.86           O  
HETATM 5226  O   HOH B 335      21.639  45.482  19.515  1.00 40.49           O  
HETATM 5227  O   HOH B 336      45.125  54.655   7.849  1.00 33.24           O  
HETATM 5228  O   HOH B 337      37.607  56.049 -13.665  1.00 40.16           O  
HETATM 5229  O   HOH B 338      46.471  53.366 -11.232  1.00 31.37           O  
HETATM 5230  O   HOH B 339      22.147  38.585  -1.149  1.00 29.74           O  
HETATM 5231  O   HOH B 340      43.588  48.814  20.311  1.00 34.58           O  
HETATM 5232  O   HOH B 341      21.151  33.726  23.420  1.00 40.21           O  
HETATM 5233  O   HOH B 342      38.897  40.583   6.795  1.00 21.14           O  
HETATM 5234  O   HOH B 343      28.556  44.808  -8.969  1.00 26.30           O  
HETATM 5235  O   HOH B 344      36.923  38.631   5.774  1.00 17.89           O  
HETATM 5236  O   HOH B 345      36.799  62.646   0.807  1.00 27.87           O  
HETATM 5237  O   HOH B 346      20.716  45.396   0.114  1.00 31.28           O  
HETATM 5238  O   HOH B 347      45.451  31.239  15.106  1.00 38.67           O  
HETATM 5239  O   HOH B 348      28.531  53.300 -15.030  1.00 33.64           O  
HETATM 5240  O   HOH B 349      36.001  40.293  30.366  1.00 29.47           O  
HETATM 5241  O   HOH B 350      46.257  39.116  19.915  1.00 24.20           O  
HETATM 5242  O   HOH B 351      31.591  67.264  13.818  1.00 17.52           O  
HETATM 5243  O   HOH B 352      29.899  61.867  -0.983  1.00 40.64           O  
HETATM 5244  O   HOH B 353      29.403  58.195 -15.317  1.00 33.83           O  
HETATM 5245  O   HOH B 354      40.702  48.763  13.696  1.00 20.75           O  
HETATM 5246  O   HOH B 355      22.671  37.709  25.625  1.00 37.20           O  
HETATM 5247  O   HOH B 356      44.014  41.272  -2.456  1.00 12.37           O  
HETATM 5248  O   HOH B 357      44.407  54.567   1.041  1.00 16.42           O  
HETATM 5249  O   HOH B 358      21.943  30.617  16.095  1.00 34.61           O  
HETATM 5250  O   HOH B 359      43.565  54.414 -11.292  1.00 33.11           O  
HETATM 5251  O   HOH B 360      39.999  40.906  -4.123  1.00 14.74           O  
HETATM 5252  O   HOH B 361      24.411  36.869   9.401  1.00 23.47           O  
HETATM 5253  O   HOH B 362      47.099  64.380   1.346  1.00 38.13           O  
HETATM 5254  O   HOH B 363      46.678  42.633 -11.799  1.00 33.98           O  
HETATM 5255  O   HOH B 364      40.399  57.357  -7.128  1.00 17.07           O  
HETATM 5256  O   HOH B 365      50.347  57.673  11.860  1.00 39.75           O  
HETATM 5257  O   HOH B 366      32.765  52.520  27.743  1.00 27.27           O  
HETATM 5258  O   HOH B 367      21.816  51.489   2.506  1.00 27.46           O  
HETATM 5259  O   HOH B 368      41.821  62.910  -2.822  1.00 20.74           O  
HETATM 5260  O   HOH B 369      18.341  39.348  26.899  1.00 37.91           O  
HETATM 5261  O   HOH B 370      42.500  52.173  32.203  1.00 22.34           O  
HETATM 5262  O   HOH B 371      40.333  59.977  30.680  1.00 31.55           O  
HETATM 5263  O   HOH B 372      38.179  50.683 -16.461  1.00 24.41           O  
HETATM 5264  O   HOH B 373      24.193  58.360  28.890  1.00 33.79           O  
HETATM 5265  O   HOH B 374      41.028  71.575  16.076  1.00 29.79           O  
HETATM 5266  O   HOH B 375      21.334  65.667  16.784  1.00 38.37           O  
HETATM 5267  O   HOH B 376      43.163  50.921   3.894  1.00 19.57           O  
HETATM 5268  O   HOH B 377      46.398  40.395  -6.367  1.00 13.79           O  
HETATM 5269  O   HOH B 378      26.947  64.952  23.780  1.00 18.56           O  
HETATM 5270  O   HOH B 379      22.414  66.684  14.748  1.00 34.23           O  
HETATM 5271  O   HOH B 380      22.556  33.827  -3.409  1.00 55.50           O  
HETATM 5272  O   HOH B 381      39.209  69.118  28.197  1.00 29.69           O  
HETATM 5273  O   HOH B 382      30.649  65.737   5.807  1.00 21.69           O  
HETATM 5274  O   HOH B 383      40.378  46.258 -13.694  1.00 28.25           O  
HETATM 5275  O   HOH B 384      34.394  42.377 -10.014  1.00 22.09           O  
HETATM 5276  O   HOH B 385      28.059  33.454   1.453  1.00 21.43           O  
HETATM 5277  O   HOH B 386      32.741  46.294  29.563  1.00 25.92           O  
HETATM 5278  O   HOH B 387      33.473  27.100  -2.393  1.00 28.59           O  
HETATM 5279  O   HOH B 388      50.724  50.113  -8.797  1.00 20.07           O  
HETATM 5280  O   HOH B 389      48.765  62.573   2.068  1.00 38.21           O  
HETATM 5281  O   HOH B 390      19.752  37.301   3.551  1.00 45.46           O  
HETATM 5282  O   HOH B 391      52.935  57.104  14.523  1.00 46.36           O  
HETATM 5283  O   HOH B 392      40.078  42.945 -12.386  1.00 28.98           O  
HETATM 5284  O   HOH B 393      34.196  29.796  -1.953  1.00 19.52           O  
HETATM 5285  O   HOH B 394      24.439  58.119   3.851  1.00 50.07           O  
HETATM 5286  O   HOH B 395      27.201  48.547  24.284  1.00 19.61           O  
HETATM 5287  O   HOH B 396      29.167  49.178 -13.564  1.00 30.38           O  
HETATM 5288  O   HOH B 397      34.444  59.654  27.067  1.00 23.05           O  
HETATM 5289  O   HOH B 398      45.626  64.314  18.266  1.00 21.90           O  
HETATM 5290  O   HOH B 399      36.900  46.568   1.911  1.00 12.93           O  
HETATM 5291  O   HOH B 400      23.296  38.908  22.976  1.00 28.20           O  
HETATM 5292  O   HOH B 401      44.281  46.224  29.026  1.00 28.98           O  
HETATM 5293  O   HOH B 402      32.668  37.004  -2.412  1.00 20.19           O  
HETATM 5294  O   HOH B 403      42.998  39.600  -7.949  1.00 24.53           O  
HETATM 5295  O   HOH B 404      21.610  30.061  -0.730  1.00 46.07           O  
HETATM 5296  O   HOH B 405      52.028  54.929  18.106  1.00 34.61           O  
HETATM 5297  O   HOH B 406      44.192  46.927 -13.420  1.00 29.10           O  
HETATM 5298  O   HOH B 407      31.326  61.258 -10.508  1.00 27.20           O  
HETATM 5299  O   HOH B 408      24.721  59.326 -10.565  1.00 33.29           O  
HETATM 5300  O   HOH B 409      34.457  54.152  29.125  1.00 36.15           O  
HETATM 5301  O   HOH B 410      20.074  53.582  13.570  1.00 48.46           O  
HETATM 5302  O   HOH B 411      16.830  51.451  -0.788  1.00 37.79           O  
HETATM 5303  O   HOH B 412      19.633  50.331   5.386  1.00 35.98           O  
HETATM 5304  O   HOH B 413      24.603  27.106  20.103  1.00 40.10           O  
HETATM 5305  O   HOH B 414      40.538  67.231  13.499  1.00 32.35           O  
HETATM 5306  O   HOH B 415      29.309  34.849   5.299  1.00 29.73           O  
HETATM 5307  O   HOH B 416      35.764  62.288   5.364  1.00 20.90           O  
HETATM 5308  O   HOH B 417      28.769  47.030  31.195  1.00 37.92           O  
HETATM 5309  O   HOH B 418      24.002  60.457   4.197  1.00 48.11           O  
HETATM 5310  O   HOH B 419      21.021  44.757  21.582  1.00 39.02           O  
HETATM 5311  O   HOH B 420      22.751  60.587  -8.983  1.00 40.50           O  
HETATM 5312  O   HOH B 421      27.376  31.255  -6.139  1.00 31.90           O  
HETATM 5313  O   HOH B 422      36.229  71.437  14.211  1.00 31.38           O  
HETATM 5314  O   HOH B 423      46.164  68.463  22.230  1.00 36.25           O  
HETATM 5315  O   HOH B 424      21.219  53.023   4.819  1.00 30.20           O  
HETATM 5316  O   HOH B 425      43.561  41.866  -8.765  1.00 16.39           O  
HETATM 5317  O   HOH B 426      34.793  31.904  16.057  1.00 36.95           O  
HETATM 5318  O   HOH B 427      38.248  48.348  31.027  1.00 30.61           O  
HETATM 5319  O   HOH B 428      39.242  62.931   9.044  1.00 18.30           O  
HETATM 5320  O   HOH B 429      33.362  40.525   8.536  1.00 17.13           O  
HETATM 5321  O   HOH B 430      37.550  66.258  11.514  1.00 26.63           O  
HETATM 5322  O   HOH B 431      24.531  39.486  -0.091  1.00 21.90           O  
HETATM 5323  O   HOH B 432      30.849  40.319 -13.055  1.00 46.89           O  
HETATM 5324  O   HOH B 433      45.787  63.053  28.403  1.00 32.46           O  
HETATM 5325  O   HOH B 434      43.174  35.421  18.984  1.00 35.34           O  
HETATM 5326  O   HOH B 435      40.571  40.216  -8.713  1.00 34.30           O  
HETATM 5327  O   HOH B 436      28.511  34.764  11.014  1.00 24.87           O  
HETATM 5328  O   HOH B 437      42.654  57.439  -9.064  1.00 29.63           O  
HETATM 5329  O   HOH B 438      40.961  42.620  -2.139  1.00 12.30           O  
HETATM 5330  O   HOH B 439      16.154  42.018 -11.119  1.00 42.53           O  
HETATM 5331  O   HOH B 440      32.991  40.202  -8.659  1.00 28.01           O  
HETATM 5332  O   HOH B 441      20.688  33.853  18.760  1.00 29.71           O  
HETATM 5333  O   HOH B 442      40.877  50.901   9.310  1.00 31.22           O  
HETATM 5334  O   HOH B 443      20.507  47.153  16.724  1.00 30.09           O  
HETATM 5335  O   HOH B 444      27.755  32.847   4.630  1.00 27.58           O  
HETATM 5336  O   HOH B 445      46.009  70.023  26.232  1.00 37.93           O  
HETATM 5337  O   HOH B 446      41.182  47.791  10.397  1.00 35.50           O  
HETATM 5338  O   HOH B 447      48.591  63.971  25.862  1.00 38.15           O  
HETATM 5339  O   HOH B 448      44.633  58.218  -6.951  1.00 28.01           O  
HETATM 5340  O   HOH B 449      23.871  35.630  11.822  1.00 28.67           O  
HETATM 5341  O   HOH B 450      20.490  42.347   3.767  1.00 31.03           O  
HETATM 5342  O   HOH B 451      43.765  66.321  30.047  1.00 31.17           O  
HETATM 5343  O   HOH B 452      49.907  57.388  26.079  1.00 32.09           O  
HETATM 5344  O   HOH B 453      40.869  65.546  -6.353  1.00 41.59           O  
HETATM 5345  O   HOH B 454      27.043  49.496  27.395  1.00 39.99           O  
HETATM 5346  O   HOH B 455      38.377  71.116  26.512  1.00 34.00           O  
HETATM 5347  O   HOH B 456      17.712  45.380   2.149  1.00 35.31           O  
HETATM 5348  O   HOH B 457      19.562  56.186  10.381  1.00 48.50           O  
HETATM 5349  O   HOH B 458      34.407  66.223   8.421  1.00 26.94           O  
HETATM 5350  O   HOH B 459      37.272  65.288  -3.156  1.00 35.14           O  
HETATM 5351  O   HOH B 460      34.909  62.905   2.664  1.00 31.43           O  
HETATM 5352  O   HOH B 461      14.560  49.497  -4.919  1.00 38.86           O  
HETATM 5353  O   HOH B 462      40.686  37.343  16.992  1.00 23.15           O  
HETATM 5354  O   HOH B 463      18.417  59.139   1.838  1.00 42.71           O  
HETATM 5355  O   HOH B 464      51.655  46.828  25.835  1.00 29.17           O  
HETATM 5356  O   HOH B 465      34.868  65.453  29.643  1.00 48.37           O  
HETATM 5357  O   HOH B 466      21.268  56.420  22.649  1.00 36.98           O  
HETATM 5358  O   HOH B 467      43.687  58.200  32.980  1.00 42.11           O  
HETATM 5359  O   HOH B 468      27.890  30.366   1.316  1.00 28.06           O  
HETATM 5360  O   HOH B 469      25.087  32.208  -5.573  1.00 41.73           O  
HETATM 5361  O   HOH B 470      30.340  70.733  23.014  1.00 32.58           O  
HETATM 5362  O   HOH B 471      30.336  53.385  28.127  1.00 31.46           O  
HETATM 5363  O   HOH B 472      31.615  71.184  16.854  1.00 32.85           O  
HETATM 5364  O   HOH B 473      24.100  42.977  31.831  1.00 38.42           O  
HETATM 5365  O   HOH B 474      19.910  59.791   3.405  1.00 39.47           O  
HETATM 5366  O   HOH B 475      33.966  38.585   1.491  1.00 14.58           O  
HETATM 5367  O   HOH B 476      14.791  52.609  -2.313  1.00 32.57           O  
HETATM 5368  O   HOH B 477      22.826  44.449  28.910  1.00 26.03           O  
HETATM 5369  O   HOH B 478      36.007  23.342  -3.950  1.00 43.88           O  
HETATM 5370  O   HOH B 479      29.888  52.342  30.626  1.00 34.67           O  
HETATM 5371  O   HOH B 480      19.443  54.196   7.822  1.00 42.86           O  
HETATM 5372  O   HOH B 481      48.376  45.500 -12.394  1.00 41.62           O  
HETATM 5373  O   HOH B 482      31.074  32.852 -19.299  1.00 48.52           O  
HETATM 5374  O   HOH B 483      41.521  56.458  34.244  1.00 40.99           O  
HETATM 5375  O   HOH B 484      40.712  38.282  -4.827  1.00 17.47           O  
HETATM 5376  O   HOH B 485      35.725  68.488  11.296  1.00 30.14           O  
HETATM 5377  O   HOH B 486      25.952  29.032   4.402  1.00 39.11           O  
HETATM 5378  O   HOH B 487      36.579  39.563  -7.066  1.00 45.78           O  
HETATM 5379  O   HOH B 488      29.751  31.432  14.285  1.00 54.08           O  
HETATM 5380  O   HOH B 489      31.242  69.012  10.055  1.00 26.31           O  
HETATM 5381  O   HOH B 490      29.559  26.712 -17.876  1.00 48.03           O  
HETATM 5382  O   HOH B 491      26.125  33.895  11.254  1.00 45.88           O  
HETATM 5383  O   HOH B 492      50.322  62.309 -10.244  1.00 47.26           O  
HETATM 5384  O   HOH B 493      42.885  67.261  15.135  1.00 34.04           O  
HETATM 5385  O   HOH B 494      33.123  68.774  12.437  1.00 29.86           O  
HETATM 5386  O   HOH B 495      37.842  61.898  29.129  1.00 46.68           O  
HETATM 5387  O   HOH B 496      34.917  64.829   5.933  1.00 29.75           O  
HETATM 5388  O   HOH B 497      22.608  35.578   7.872  1.00 32.56           O  
HETATM 5389  O   HOH B 498      46.160  55.813  -8.316  1.00 27.96           O  
HETATM 5390  O   HOH B 499      41.236  43.986 -14.478  1.00 39.23           O  
HETATM 5391  O   HOH B 500      17.553  49.694   6.910  1.00 39.03           O  
HETATM 5392  O   HOH B 501      31.906  67.547   7.862  1.00 26.47           O  
HETATM 5393  O   HOH B 502      39.305  37.896  -7.094  1.00 31.68           O  
HETATM 5394  O   HOH B 503      38.706  65.563   9.322  1.00 29.03           O  
HETATM 5395  O   HOH B 504      18.942  55.012  19.858  1.00 40.14           O  
HETATM 5396  O   HOH B 505      42.652  63.832   6.155  1.00 39.63           O  
HETATM 5397  O   HOH B 506      35.636  41.322 -11.949  1.00 34.22           O  
HETATM 5398  O   HOH B 507      18.735  56.938  22.161  1.00 34.41           O  
HETATM 5399  O   HOH B 508      40.201  62.773   4.900  1.00 30.34           O  
HETATM 5400  O   HOH B 509      38.442  61.927   6.534  1.00 25.31           O  
HETATM 5401  O   HOH B 510      36.013  68.550   8.553  1.00 30.57           O  
HETATM 5402  O   HOH B 511      42.123  41.639 -11.137  1.00 31.91           O  
HETATM 5403  O   HOH B 512      33.178  65.868   4.702  1.00 31.14           O  
HETATM 5404  O   HOH B 513      33.428  70.572  14.546  1.00 37.87           O  
HETATM 5405  O   HOH C 101      44.434  56.573  -4.854  1.00 17.10           O  
HETATM 5406  O   HOH C 102      50.547  47.208 -11.146  1.00 35.40           O  
HETATM 5407  O   HOH C 103      56.242  35.872  -1.801  1.00 15.80           O  
HETATM 5408  O   HOH C 104      34.983  33.377   7.360  1.00 26.66           O  
HETATM 5409  O   HOH C 105      43.577  56.189  -1.118  1.00 16.38           O  
HETATM 5410  O   HOH C 106      44.747  54.467  -6.631  1.00 15.93           O  
HETATM 5411  O   HOH C 107      56.029  54.538  -2.967  1.00 31.12           O  
HETATM 5412  O   HOH C 108      53.653  44.138   2.707  1.00 11.46           O  
HETATM 5413  O   HOH C 109      46.009  59.714  -5.301  1.00 39.74           O  
HETATM 5414  O   HOH C 110      49.971  44.922 -10.680  1.00 37.03           O  
HETATM 5415  O   HOH C 111      48.530  60.991  -2.382  1.00 32.62           O  
HETATM 5416  O   HOH C 112      48.492  38.615  -0.515  1.00 10.75           O  
HETATM 5417  O   HOH C 113      50.580  53.509  -6.349  1.00 30.23           O  
HETATM 5418  O   HOH C 114      37.172  35.259   7.470  1.00 23.61           O  
HETATM 5419  O   HOH C 115      47.309  53.749  -8.960  1.00 28.14           O  
HETATM 5420  O   HOH C 116      44.467  30.342   6.984  1.00 22.71           O  
HETATM 5421  O   HOH C 117      47.201  30.030  12.157  1.00 37.18           O  
HETATM 5422  O   HOH C 118      55.826  40.198   1.472  1.00 13.49           O  
HETATM 5423  O   HOH C 119      56.627  51.985  -2.448  1.00 20.64           O  
HETATM 5424  O   HOH C 120      45.927  37.756   9.248  1.00 24.19           O  
HETATM 5425  O   HOH C 121      32.844  33.329   8.524  1.00 39.37           O  
HETATM 5426  O   HOH C 122      43.302  28.517   8.767  1.00 39.18           O  
HETATM 5427  O   HOH C 123      31.892  27.990   1.878  1.00 38.57           O  
HETATM 5428  O   HOH C 124      53.489  43.220  -8.513  1.00 18.16           O  
HETATM 5429  O   HOH C 125      47.292  62.738  -3.909  1.00 45.12           O  
HETATM 5430  O   HOH D 101      59.749  47.971   7.357  1.00 26.75           O  
HETATM 5431  O   HOH D 102      42.712  18.736   1.508  1.00 25.10           O  
HETATM 5432  O   HOH D 103      36.759  30.101  -2.801  1.00 18.47           O  
HETATM 5433  O   HOH D 104      53.597  50.654  14.023  1.00 27.51           O  
HETATM 5434  O   HOH D 105      34.789  37.626  -5.260  1.00 24.87           O  
HETATM 5435  O   HOH D 106      46.184  22.520  -1.898  1.00 17.81           O  
HETATM 5436  O   HOH D 107      41.284  24.702  -5.822  1.00 28.05           O  
HETATM 5437  O   HOH D 108      38.529  21.624   0.242  1.00 31.21           O  
HETATM 5438  O   HOH D 109      50.786  53.257   6.682  1.00 33.11           O  
HETATM 5439  O   HOH D 110      36.335  23.822   0.247  1.00 33.75           O  
HETATM 5440  O   HOH D 111      39.545  25.765  -2.575  1.00 19.64           O  
HETATM 5441  O   HOH D 112      34.245  43.591  -0.299  1.00 15.87           O  
HETATM 5442  O   HOH D 113      35.631  32.554  -6.530  1.00 21.46           O  
HETATM 5443  O   HOH D 114      47.160  49.507  12.692  1.00 29.99           O  
HETATM 5444  O   HOH D 115      45.128  24.113  -3.799  1.00 17.09           O  
HETATM 5445  O   HOH D 116      41.700  40.684   7.528  1.00 29.06           O  
HETATM 5446  O   HOH D 117      37.788  36.235   4.875  1.00 15.62           O  
HETATM 5447  O   HOH D 118      38.972  33.126  -8.717  1.00 24.69           O  
HETATM 5448  O   HOH D 119      47.731  23.504   1.638  1.00 13.82           O  
HETATM 5449  O   HOH D 120      41.774  21.340  -1.719  1.00 29.59           O  
HETATM 5450  O   HOH D 121      57.161  47.824   4.250  1.00 26.79           O  
HETATM 5451  O   HOH D 122      35.536  40.033   3.630  1.00 14.15           O  
HETATM 5452  O   HOH D 123      44.919  19.453  -1.533  1.00 25.32           O  
HETATM 5453  O   HOH D 124      42.992  44.692   9.319  1.00 39.21           O  
HETATM 5454  O   HOH D 125      45.176  51.714  10.255  1.00 33.39           O  
HETATM 5455  O   HOH D 126      38.726  50.067   7.895  1.00 19.03           O  
HETATM 5456  O   HOH D 127      47.278  50.231   4.818  1.00 21.38           O  
HETATM 5457  O   HOH D 128      55.874  54.651   7.449  1.00 32.28           O  
HETATM 5458  O   HOH D 129      34.631  28.620   0.556  1.00 23.76           O  
HETATM 5459  O   HOH D 130      42.227  40.999  -0.133  1.00 12.37           O  
HETATM 5460  O   HOH D 131      45.371  22.548   8.796  1.00 31.75           O  
HETATM 5461  O   HOH D 132      49.412  47.891  13.232  1.00 32.51           O  
HETATM 5462  O   HOH D 133      45.112  51.623   6.083  1.00 42.86           O  
HETATM 5463  O   HOH D 134      40.748  42.890   8.398  1.00 37.22           O  
HETATM 5464  O   HOH D 135      35.957  35.290  -6.202  1.00 22.24           O  
HETATM 5465  O   HOH D 136      37.723  27.563  -3.098  1.00 27.53           O  
HETATM 5466  O   HOH D 137      38.037  35.899  -7.827  1.00 30.84           O  
HETATM 5467  O   HOH D 138      43.582  21.665  -3.846  1.00 33.69           O  
HETATM 5468  O   HOH D 139      39.429  22.816  -2.239  1.00 32.30           O  
MASTER      277    0    0   21   16    0    0    6 5239    4    0   46          
END

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Related entries of code: 5dwa

Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code	Check Database	Protein Sequence Similarity
4zsf	RCSB PDB PDBbind	14aa, >4ZSF_2\|Chain... *
Complexes with the same small molecule ligand
PDB Code	Check Database	Ligand Name
No complexes with the same small molecule ligand are found!

Entry Information

PDB ID	5dwa
Complex Type	Protein-Nucleic Acid
PDBbind Subset	general set
Protein Name	Type-2 restriction enzyme AgeI
Ligand Name	11-mer SP11 DNA
EC.Number	E.C.3.1.21.4
Resolution	1.5(Å)
Affinity (Kd/Ki/IC50)	Kd=0.9nM
Release Year	2016
Protein/NA Sequence	Check fasta file
Primary Reference	(2017) Nucleic Acids Res. Vol. 45: pp. 3547-3558

Links to External Databases

RCSB PDB	The mother database
PDBsum	Enhanced annotations on PDB entries
Pubchem	Comprehensive collection of chemical and biological data
UniProtKB AC	UniProt accession number (AC): Q9KHV6
Entrez Gene ID	No matched NCBI Entrez Gene ID found!
ASD	Information of known allosteric effects of PDB entries

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