Welcome to PDBbind-CN database

Browse entries in the PDBbind-CN Database

HEADER    RNA BINDING PROTEIN/DNA                 16-MAR-16   5ITH              
TITLE     TIA-1 RRM2 RECOGNITION OF TARGET OLIGONUCLEOTIDE                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NUCLEOLYSIN TIA-1 ISOFORM P40;                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 93-183;                                       
COMPND   5 SYNONYM: RNA-BINDING PROTEIN TIA-1,T-CELL-RESTRICTED INTRACELLULAR   
COMPND   6 ANTIGEN-1,TIA-1,P40-TIA-1;                                           
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: DNA (5'-D(*AP*CP*TP*CP*C*TP*TP*TP*TP*T)-3');               
COMPND  10 CHAIN: B;                                                            
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: TIA1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_TAXID: 9606                                                 
KEYWDS    RRM, RNA/DNA BINDING DOMAIN, POLY U BINDING PREFERENCE, AROMATIC BASE 
KEYWDS   2 STACKING INTERACTIONS, DNA BINDING PROTEIN-DNA COMPLEX, RNA BINDING  
KEYWDS   3 PROTEIN-DNA COMPLEX                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.WARIS,J.A.WILCE,M.C.WILCE                                           
REVDAT   2   17-MAY-17 5ITH    1       JRNL                                     
REVDAT   1   22-FEB-17 5ITH    0                                                
JRNL        AUTH   S.WARIS,S.M.GARCIA-MAURINO,A.SIVAKUMARAN,S.A.BECKHAM,        
JRNL        AUTH 2 F.E.LOUGHLIN,M.GOROSPE,I.DIAZ-MORENO,M.C.J.WILCE,J.A.WILCE   
JRNL        TITL   TIA-1 RRM23 BINDING AND RECOGNITION OF TARGET                
JRNL        TITL 2 OLIGONUCLEOTIDES.                                            
JRNL        REF    NUCLEIC ACIDS RES.            V.  45  4944 2017              
JRNL        REFN                   ESSN 1362-4962                               
JRNL        PMID   28184449                                                     
JRNL        DOI    10.1093/NAR/GKX102                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.31 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.4_1496                                    
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) : 2.31                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 22.97                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.380                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 4374                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.229                           
REMARK   3   R VALUE            (WORKING SET) : 0.228                           
REMARK   3   FREE R VALUE                     : 0.261                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.980                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 218                             
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  2.9095 -  2.3101    1.00     2066   108  0.3179 0.3509        
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)     : 0.270            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.210           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005            698                                  
REMARK   3   ANGLE     :  0.908            951                                  
REMARK   3   CHIRALITY :  0.034             96                                  
REMARK   3   PLANARITY :  0.004            115                                  
REMARK   3   DIHEDRAL  : 18.019            242                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 93 THROUGH 126 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.6848 -19.1692  -1.7093              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6130 T22:   0.8431                                     
REMARK   3      T33:   0.4372 T12:   0.3841                                     
REMARK   3      T13:  -0.0167 T23:  -0.1064                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1843 L22:   6.7778                                     
REMARK   3      L33:   5.2864 L12:   0.4585                                     
REMARK   3      L13:  -1.0697 L23:   0.1516                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2981 S12:  -0.1318 S13:  -0.0923                       
REMARK   3      S21:  -0.0719 S22:   0.0762 S23:  -0.4044                       
REMARK   3      S31:   2.1679 S32:   1.9811 S33:  -0.2119                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 127 THROUGH 138 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   5.4776  -6.2783   2.8541              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4511 T22:   1.3833                                     
REMARK   3      T33:   0.9179 T12:  -0.1710                                     
REMARK   3      T13:   0.0004 T23:  -0.2215                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.2248 L22:   5.4657                                     
REMARK   3      L33:   6.0507 L12:   4.8347                                     
REMARK   3      L13:   1.0940 L23:   2.0461                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4508 S12:  -1.0862 S13:   2.0217                       
REMARK   3      S21:  -0.2886 S22:  -0.2517 S23:  -1.3442                       
REMARK   3      S31:  -1.8571 S32:   0.8532 S33:  -0.2874                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 139 THROUGH 171 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.0912 -20.8911   0.6705              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6285 T22:   0.4517                                     
REMARK   3      T33:   0.5376 T12:   0.0805                                     
REMARK   3      T13:  -0.0597 T23:  -0.0020                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4809 L22:   7.8012                                     
REMARK   3      L33:   3.4986 L12:  -0.0574                                     
REMARK   3      L13:  -0.2629 L23:  -0.7484                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2163 S12:   0.0539 S13:  -0.4458                       
REMARK   3      S21:  -0.2610 S22:   0.1174 S23:   1.1102                       
REMARK   3      S31:   1.2554 S32:   0.0954 S33:  -0.2371                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 3 )                     
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.2889  -7.3255  -0.4834              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8976 T22:   0.5604                                     
REMARK   3      T33:   1.0878 T12:   0.1471                                     
REMARK   3      T13:   0.1732 T23:  -0.0184                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2503 L22:   7.0471                                     
REMARK   3      L33:   4.7131 L12:   0.4317                                     
REMARK   3      L13:   0.9249 L23:  -0.9115                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5387 S12:  -0.7099 S13:   2.2680                       
REMARK   3      S21:  -1.3995 S22:   0.0222 S23:  -0.4501                       
REMARK   3      S31:   0.3131 S32:   0.8454 S33:  -0.3272                       
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 5ITH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000218938.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-MAR-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.71080                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 4381                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.310                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 22.974                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 12.60                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 35.0700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.31                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.39                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.170                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 3BS9                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 35.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.91                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 1500, MALONATE-IMIDAZOLE-BORATE,     
REMARK 280  PH 8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       56.60000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       28.30000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       42.45000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       14.15000            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       70.75000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 850 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 5030 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     THR A   172                                                      
REMARK 465     ARG A   173                                                      
REMARK 465     LYS A   174                                                      
REMARK 465     PRO A   175                                                      
REMARK 465     PRO A   176                                                      
REMARK 465     ALA A   177                                                      
REMARK 465     PRO A   178                                                      
REMARK 465     LYS A   179                                                      
REMARK 465     SER A   180                                                      
REMARK 465     THR A   181                                                      
REMARK 465     TYR A   182                                                      
REMARK 465     GLU A   183                                                      
REMARK 465      DA B    -4                                                      
REMARK 465      DC B    -3                                                      
REMARK 465      DT B    -2                                                      
REMARK 465      DC B    -1                                                      
REMARK 465      DC B     0                                                      
REMARK 465      DT B     4                                                      
REMARK 465      DT B     5                                                      
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     ASN A  93    CG   OD1  ND2                                       
REMARK 470     GLU A 109    CG   CD   OE1  OE2                                  
REMARK 470      DT B   1    P    OP1  OP2  O5'  C5'                             
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   OD2  ASP A   101     O    HOH A   201              1.91            
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    HIS A  94     -168.41    -79.95                                   
REMARK 500    MET A 130      -73.81    -59.51                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5ITH A   93   183  UNP    P31483   TIA1_HUMAN      93    183             
DBREF  5ITH B   -4     5  PDB    5ITH     5ITH            -4      5             
SEQADV 5ITH GLY A   92  UNP  P31483              EXPRESSION TAG                 
SEQRES   1 A   92  GLY ASN HIS PHE HIS VAL PHE VAL GLY ASP LEU SER PRO          
SEQRES   2 A   92  GLU ILE THR THR GLU ASP ILE LYS ALA ALA PHE ALA PRO          
SEQRES   3 A   92  PHE GLY ARG ILE SER ASP ALA ARG VAL VAL LYS ASP MET          
SEQRES   4 A   92  ALA THR GLY LYS SER LYS GLY TYR GLY PHE VAL SER PHE          
SEQRES   5 A   92  PHE ASN LYS TRP ASP ALA GLU ASN ALA ILE GLN GLN MET          
SEQRES   6 A   92  GLY GLY GLN TRP LEU GLY GLY ARG GLN ILE ARG THR ASN          
SEQRES   7 A   92  TRP ALA THR ARG LYS PRO PRO ALA PRO LYS SER THR TYR          
SEQRES   8 A   92  GLU                                                          
SEQRES   1 B   10   DA  DC  DT  DC  DC  DT  DT  DT  DT  DT                      
FORMUL   3  HOH   *5(H2 O)                                                      
HELIX    1 AA1 THR A  107  ALA A  116  1                                  10    
HELIX    2 AA2 PRO A  117  GLY A  119  5                                   3    
HELIX    3 AA3 ASN A  145  GLY A  157  1                                  13    
SHEET    1 AA1 4 ILE A 121  LYS A 128  0                                        
SHEET    2 AA1 4 SER A 135  PHE A 143 -1  O  LYS A 136   N  VAL A 127           
SHEET    3 AA1 4 PHE A  95  GLY A 100 -1  N  VAL A  99   O  GLY A 139           
SHEET    4 AA1 4 ARG A 167  TRP A 170 -1  O  ASN A 169   N  PHE A  98           
SHEET    1 AA2 2 TRP A 160  LEU A 161  0                                        
SHEET    2 AA2 2 ARG A 164  GLN A 165 -1  O  ARG A 164   N  LEU A 161           
CRYST1   45.430   45.430   84.900  90.00  90.00 120.00 P 65          6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.022012  0.012709  0.000000        0.00000                         
SCALE2      0.000000  0.025417  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011779        0.00000                         
ATOM      1  N   GLY A  92      -7.674 -18.462 -20.072  1.00 92.50           N  
ATOM      2  CA  GLY A  92      -7.363 -17.073 -19.794  1.00 89.96           C  
ATOM      3  C   GLY A  92      -7.431 -16.740 -18.316  1.00 88.55           C  
ATOM      4  O   GLY A  92      -6.592 -17.189 -17.535  1.00 87.32           O  
ATOM      5  N   ASN A  93      -8.435 -15.950 -17.942  1.00132.82           N  
ANISOU    5  N   ASN A  93    19298  17012  14157    686  -1389    105       N  
ATOM      6  CA  ASN A  93      -8.617 -15.508 -16.562  1.00120.76           C  
ANISOU    6  CA  ASN A  93    17150  15451  13282    540  -1267    159       C  
ATOM      7  C   ASN A  93      -8.565 -16.657 -15.560  1.00108.50           C  
ANISOU    7  C   ASN A  93    15823  13653  11748    741  -1284    -94       C  
ATOM      8  O   ASN A  93      -9.415 -17.546 -15.576  1.00109.56           O  
ANISOU    8  O   ASN A  93    16413  13353  11864    602  -1636   -171       O  
ATOM      9  CB  ASN A  93      -9.946 -14.762 -16.422  1.00120.53           C  
ANISOU    9  CB  ASN A  93    16791  15164  13840     12  -1587    436       C  
ATOM     10  N   HIS A  94      -7.554 -16.634 -14.697  1.00 97.21           N  
ANISOU   10  N   HIS A  94    14081  12502  10353   1061   -914   -212       N  
ATOM     11  CA  HIS A  94      -7.373 -17.677 -13.691  1.00 86.97           C  
ANISOU   11  CA  HIS A  94    12998  11007   9039   1314   -907   -414       C  
ATOM     12  C   HIS A  94      -8.288 -17.462 -12.493  1.00 79.10           C  
ANISOU   12  C   HIS A  94    11689   9740   8626    936  -1016   -315       C  
ATOM     13  O   HIS A  94      -9.199 -16.635 -12.544  1.00 77.63           O  
ANISOU   13  O   HIS A  94    11178   9451   8868    478  -1144   -112       O  
ATOM     14  CB  HIS A  94      -5.916 -17.733 -13.236  1.00 83.01           C  
ANISOU   14  CB  HIS A  94    12260  10946   8335   1829   -515   -565       C  
ATOM     15  CG  HIS A  94      -5.016 -18.444 -14.195  1.00 84.22           C  
ANISOU   15  CG  HIS A  94    12872  11245   7882   2322   -384   -749       C  
ATOM     16  ND1 HIS A  94      -3.641 -18.379 -14.117  1.00 84.61           N  
ANISOU   16  ND1 HIS A  94    12650  11767   7733   2801     -5   -870       N  
ATOM     17  CD2 HIS A  94      -5.294 -19.238 -15.256  1.00 86.44           C  
ANISOU   17  CD2 HIS A  94    13865  11263   7716   2410   -564   -854       C  
ATOM     18  CE1 HIS A  94      -3.112 -19.102 -15.087  1.00 88.43           C  
ANISOU   18  CE1 HIS A  94    13649  12262   7687   3188     83  -1036       C  
ATOM     19  NE2 HIS A  94      -4.094 -19.635 -15.793  1.00 89.67           N  
ANISOU   19  NE2 HIS A  94    14443  11968   7658   2955   -251  -1039       N  
ATOM     20  N   PHE A  95      -8.050 -18.204 -11.413  1.00 73.64           N  
ANISOU   20  N   PHE A  95    11106   8926   7948   1143   -950   -446       N  
ATOM     21  CA  PHE A  95      -8.934 -18.106 -10.254  1.00 67.18           C  
ANISOU   21  CA  PHE A  95    10079   7824   7622    784  -1011   -366       C  
ATOM     22  C   PHE A  95      -8.161 -17.859  -8.961  1.00 62.15           C  
ANISOU   22  C   PHE A  95     9058   7466   7092    980   -727   -420       C  
ATOM     23  O   PHE A  95      -7.404 -18.709  -8.500  1.00 63.66           O  
ANISOU   23  O   PHE A  95     9524   7697   6965   1419   -665   -563       O  
ATOM     24  CB  PHE A  95      -9.789 -19.367 -10.158  1.00 67.09           C  
ANISOU   24  CB  PHE A  95    10710   7237   7545    693  -1293   -438       C  
ATOM     25  CG  PHE A  95     -10.598 -19.628 -11.400  1.00 68.99           C  
ANISOU   25  CG  PHE A  95    11329   7206   7677    449  -1636   -413       C  
ATOM     26  CD1 PHE A  95     -11.839 -19.039 -11.570  1.00 67.25           C  
ANISOU   26  CD1 PHE A  95    10846   6781   7924   -100  -1869   -232       C  
ATOM     27  CD2 PHE A  95     -10.102 -20.435 -12.412  1.00 72.08           C  
ANISOU   27  CD2 PHE A  95    12329   7565   7495    780  -1730   -579       C  
ATOM     28  CE1 PHE A  95     -12.580 -19.265 -12.717  1.00 70.20           C  
ANISOU   28  CE1 PHE A  95    11548   6943   8182   -331  -2252   -204       C  
ATOM     29  CE2 PHE A  95     -10.838 -20.666 -13.562  1.00 75.10           C  
ANISOU   29  CE2 PHE A  95    13099   7717   7719    533  -2079   -578       C  
ATOM     30  CZ  PHE A  95     -12.079 -20.081 -13.714  1.00 73.98           C  
ANISOU   30  CZ  PHE A  95    12679   7397   8034    -31  -2371   -383       C  
ATOM     31  N   HIS A  96      -8.374 -16.686  -8.375  1.00 58.24           N  
ANISOU   31  N   HIS A  96     7937   7145   7045    654   -572   -307       N  
ATOM     32  CA  HIS A  96      -7.492 -16.184  -7.329  1.00 55.60           C  
ANISOU   32  CA  HIS A  96     7156   7195   6774    806   -299   -376       C  
ATOM     33  C   HIS A  96      -8.092 -16.220  -5.926  1.00 53.36           C  
ANISOU   33  C   HIS A  96     6786   6692   6799    564   -260   -370       C  
ATOM     34  O   HIS A  96      -9.275 -15.938  -5.727  1.00 52.27           O  
ANISOU   34  O   HIS A  96     6581   6207   7071    112   -321   -258       O  
ATOM     35  CB  HIS A  96      -7.067 -14.759  -7.674  1.00 55.16           C  
ANISOU   35  CB  HIS A  96     6463   7549   6945    639    -81   -299       C  
ATOM     36  CG  HIS A  96      -6.568 -14.609  -9.077  1.00 58.50           C  
ANISOU   36  CG  HIS A  96     6974   8179   7073    809    -72   -265       C  
ATOM     37  ND1 HIS A  96      -5.248 -14.807  -9.421  1.00 60.29           N  
ANISOU   37  ND1 HIS A  96     7174   8830   6902   1268    111   -397       N  
ATOM     38  CD2 HIS A  96      -7.214 -14.297 -10.225  1.00 59.59           C  
ANISOU   38  CD2 HIS A  96     7243   8166   7233    587   -219   -110       C  
ATOM     39  CE1 HIS A  96      -5.102 -14.616 -10.722  1.00 62.89           C  
ANISOU   39  CE1 HIS A  96     7640   9252   7005   1307    127   -332       C  
ATOM     40  NE2 HIS A  96      -6.279 -14.304 -11.231  1.00 62.37           N  
ANISOU   40  NE2 HIS A  96     7694   8842   7160    898    -94   -151       N  
ATOM     41  N   VAL A  97      -7.240 -16.553  -4.959  1.00 51.69           N  
ANISOU   41  N   VAL A  97     6559   6705   6376    881   -150   -487       N  
ATOM     42  CA  VAL A  97      -7.622 -16.700  -3.562  1.00 48.98           C  
ANISOU   42  CA  VAL A  97     6230   6199   6180    726    -93   -496       C  
ATOM     43  C   VAL A  97      -6.811 -15.778  -2.653  1.00 47.47           C  
ANISOU   43  C   VAL A  97     5482   6491   6064    733    125   -576       C  
ATOM     44  O   VAL A  97      -5.579 -15.746  -2.714  1.00 49.02           O  
ANISOU   44  O   VAL A  97     5496   7149   5980   1126    168   -680       O  
ATOM     45  CB  VAL A  97      -7.433 -18.155  -3.079  1.00 51.13           C  
ANISOU   45  CB  VAL A  97     7152   6217   6057   1106   -229   -547       C  
ATOM     46  CG1 VAL A  97      -7.776 -18.282  -1.595  1.00 50.00           C  
ANISOU   46  CG1 VAL A  97     7064   5932   6003    947   -143   -530       C  
ATOM     47  CG2 VAL A  97      -8.273 -19.105  -3.910  1.00 52.29           C  
ANISOU   47  CG2 VAL A  97     7891   5834   6143   1042   -445   -504       C  
ATOM     48  N   PHE A  98      -7.525 -15.034  -1.814  1.00 44.60           N  
ANISOU   48  N   PHE A  98     4838   6013   6094    284    267   -546       N  
ATOM     49  CA  PHE A  98      -6.939 -14.192  -0.778  1.00 43.77           C  
ANISOU   49  CA  PHE A  98     4281   6281   6067    200    466   -656       C  
ATOM     50  C   PHE A  98      -6.741 -14.967   0.518  1.00 43.76           C  
ANISOU   50  C   PHE A  98     4608   6247   5770    377    430   -721       C  
ATOM     51  O   PHE A  98      -7.682 -15.574   1.042  1.00 43.98           O  
ANISOU   51  O   PHE A  98     5036   5818   5854    197    415   -646       O  
ATOM     52  CB  PHE A  98      -7.827 -12.970  -0.519  1.00 42.17           C  
ANISOU   52  CB  PHE A  98     3654   5935   6434   -368    678   -611       C  
ATOM     53  CG  PHE A  98      -7.497 -12.229   0.751  1.00 43.31           C  
ANISOU   53  CG  PHE A  98     3481   6318   6658   -540    890   -754       C  
ATOM     54  CD1 PHE A  98      -8.142 -12.537   1.942  1.00 44.45           C  
ANISOU   54  CD1 PHE A  98     3856   6205   6828   -729    977   -783       C  
ATOM     55  CD2 PHE A  98      -6.551 -11.218   0.753  1.00 43.37           C  
ANISOU   55  CD2 PHE A  98     3414   6573   6490   -434    835   -646       C  
ATOM     56  CE1 PHE A  98      -7.840 -11.859   3.109  1.00 45.16           C  
ANISOU   56  CE1 PHE A  98     3878   6453   6827   -823   1071   -858       C  
ATOM     57  CE2 PHE A  98      -6.250 -10.534   1.918  1.00 44.67           C  
ANISOU   57  CE2 PHE A  98     3595   6779   6597   -523    871   -672       C  
ATOM     58  CZ  PHE A  98      -6.897 -10.855   3.097  1.00 44.90           C  
ANISOU   58  CZ  PHE A  98     3726   6681   6654   -699    974   -803       C  
ATOM     59  N   VAL A  99      -5.518 -14.922   1.035  1.00 44.18           N  
ANISOU   59  N   VAL A  99     4477   6795   5516    713    417   -849       N  
ATOM     60  CA  VAL A  99      -5.177 -15.579   2.289  1.00 45.89           C  
ANISOU   60  CA  VAL A  99     4981   7063   5391    928    341   -894       C  
ATOM     61  C   VAL A  99      -4.678 -14.566   3.317  1.00 45.15           C  
ANISOU   61  C   VAL A  99     4407   7394   5355    720    476  -1046       C  
ATOM     62  O   VAL A  99      -3.576 -14.043   3.193  1.00 46.12           O  
ANISOU   62  O   VAL A  99     4073   8055   5396    901    459  -1172       O  
ATOM     63  CB  VAL A  99      -4.100 -16.653   2.084  1.00 48.29           C  
ANISOU   63  CB  VAL A  99     5569   7578   5202   1613    115   -910       C  
ATOM     64  CG1 VAL A  99      -3.972 -17.509   3.328  1.00 51.38           C  
ANISOU   64  CG1 VAL A  99     6410   7882   5230   1846     -9   -880       C  
ATOM     65  CG2 VAL A  99      -4.435 -17.513   0.875  1.00 48.58           C  
ANISOU   65  CG2 VAL A  99     6033   7249   5175   1822     10   -820       C  
ATOM     66  N   GLY A 100      -5.490 -14.296   4.332  1.00 44.37           N  
ANISOU   66  N   GLY A 100     4414   7048   5396    321    625  -1051       N  
ATOM     67  CA  GLY A 100      -5.146 -13.318   5.346  1.00 44.92           C  
ANISOU   67  CA  GLY A 100     4102   7457   5510     59    773  -1229       C  
ATOM     68  C   GLY A 100      -4.729 -13.927   6.670  1.00 47.57           C  
ANISOU   68  C   GLY A 100     4783   7936   5357    258    647  -1278       C  
ATOM     69  O   GLY A 100      -4.841 -15.142   6.872  1.00 49.87           O  
ANISOU   69  O   GLY A 100     5661   7980   5309    581    478  -1136       O  
ATOM     70  N   ASP A 101      -4.258 -13.061   7.569  1.00 48.85           N  
ANISOU   70  N   ASP A 101     4606   8478   5475     49    725  -1478       N  
ATOM     71  CA  ASP A 101      -3.785 -13.438   8.900  1.00 52.07           C  
ANISOU   71  CA  ASP A 101     5288   9115   5381    191    581  -1549       C  
ATOM     72  C   ASP A 101      -2.588 -14.388   8.844  1.00 55.17           C  
ANISOU   72  C   ASP A 101     5803   9883   5276    876    181  -1498       C  
ATOM     73  O   ASP A 101      -2.538 -15.380   9.572  1.00 57.53           O  
ANISOU   73  O   ASP A 101     6662  10073   5125   1179     -7  -1377       O  
ATOM     74  CB  ASP A 101      -4.915 -14.067   9.727  1.00 53.32           C  
ANISOU   74  CB  ASP A 101     6104   8728   5427    -14    727  -1414       C  
ATOM     75  CG  ASP A 101      -6.027 -13.079  10.055  1.00 52.58           C  
ANISOU   75  CG  ASP A 101     5847   8324   5806   -674   1154  -1503       C  
ATOM     76  OD1 ASP A 101      -5.816 -11.860   9.886  1.00 51.22           O  
ANISOU   76  OD1 ASP A 101     5095   8395   5970   -964   1312  -1695       O  
ATOM     77  OD2 ASP A 101      -7.109 -13.521  10.505  1.00 53.13           O  
ANISOU   77  OD2 ASP A 101     6366   7891   5929   -901   1357  -1382       O  
ATOM     78  N   LEU A 102      -1.619 -14.071   7.990  1.00 54.97           N  
ANISOU   78  N   LEU A 102     5249  10291   5344   1129     74  -1580       N  
ATOM     79  CA  LEU A 102      -0.412 -14.882   7.872  1.00 58.72           C  
ANISOU   79  CA  LEU A 102     5718  11168   5424   1811   -273  -1554       C  
ATOM     80  C   LEU A 102       0.634 -14.482   8.905  1.00 63.29           C  
ANISOU   80  C   LEU A 102     5952  12387   5707   1896   -495  -1740       C  
ATOM     81  O   LEU A 102       0.800 -13.299   9.199  1.00 62.74           O  
ANISOU   81  O   LEU A 102     5368  12618   5854   1443   -358  -1963       O  
ATOM     82  CB  LEU A 102       0.185 -14.763   6.467  1.00 56.83           C  
ANISOU   82  CB  LEU A 102     5056  11126   5411   2061   -248  -1564       C  
ATOM     83  CG  LEU A 102      -0.629 -15.308   5.294  1.00 54.31           C  
ANISOU   83  CG  LEU A 102     5097  10256   5281   2096   -129  -1390       C  
ATOM     84  CD1 LEU A 102       0.159 -15.173   3.999  1.00 54.73           C  
ANISOU   84  CD1 LEU A 102     4744  10608   5443   2386   -104  -1426       C  
ATOM     85  CD2 LEU A 102      -1.018 -16.756   5.537  1.00 55.68           C  
ANISOU   85  CD2 LEU A 102     6069   9975   5111   2481   -307  -1201       C  
ATOM     86  N   SER A 103       1.335 -15.474   9.449  1.00 68.47           N  
ANISOU   86  N   SER A 103     6904  13238   5873   2478   -855  -1649       N  
ATOM     87  CA  SER A 103       2.449 -15.228  10.361  1.00 74.05           C  
ANISOU   87  CA  SER A 103     7261  14618   6256   2657  -1175  -1805       C  
ATOM     88  C   SER A 103       3.537 -14.399   9.679  1.00 74.73           C  
ANISOU   88  C   SER A 103     6435  15335   6623   2688  -1191  -2022       C  
ATOM     89  O   SER A 103       3.708 -14.486   8.463  1.00 72.79           O  
ANISOU   89  O   SER A 103     5980  15026   6650   2870  -1047  -1971       O  
ATOM     90  CB  SER A 103       3.030 -16.551  10.870  1.00 79.35           C  
ANISOU   90  CB  SER A 103     8410  15352   6387   3391  -1593  -1607       C  
ATOM     91  OG  SER A 103       2.402 -16.955  12.075  1.00 81.50           O  
ANISOU   91  OG  SER A 103     9367  15337   6261   3254  -1658  -1492       O  
ATOM     92  N   PRO A 104       4.272 -13.589  10.464  1.00 79.33           N  
ANISOU   92  N   PRO A 104     6548  16450   7143   2452  -1314  -2258       N  
ATOM     93  CA  PRO A 104       5.301 -12.672   9.954  1.00 81.01           C  
ANISOU   93  CA  PRO A 104     6268  16829   7685   2212  -1109  -2397       C  
ATOM     94  C   PRO A 104       6.327 -13.324   9.035  1.00 84.67           C  
ANISOU   94  C   PRO A 104     6695  17318   8158   2712  -1159  -2269       C  
ATOM     95  O   PRO A 104       6.798 -12.683   8.094  1.00 82.78           O  
ANISOU   95  O   PRO A 104     6260  16962   8231   2461   -938  -2275       O  
ATOM     96  CB  PRO A 104       5.986 -12.177  11.228  1.00 86.09           C  
ANISOU   96  CB  PRO A 104     6690  17916   8104   2052  -1329  -2597       C  
ATOM     97  CG  PRO A 104       4.936 -12.257  12.260  1.00 85.19           C  
ANISOU   97  CG  PRO A 104     6933  17734   7701   1818  -1437  -2634       C  
ATOM     98  CD  PRO A 104       4.110 -13.465  11.923  1.00 82.48           C  
ANISOU   98  CD  PRO A 104     7214  16993   7132   2232  -1522  -2353       C  
ATOM     99  N   GLU A 105       6.678 -14.576   9.302  1.00 90.85           N  
ANISOU   99  N   GLU A 105     7742  18175   8601   3388  -1453  -2127       N  
ATOM    100  CA  GLU A 105       7.729 -15.211   8.522  1.00 97.15           C  
ANISOU  100  CA  GLU A 105     8475  19033   9406   3852  -1483  -2048       C  
ATOM    101  C   GLU A 105       7.217 -16.359   7.658  1.00 93.09           C  
ANISOU  101  C   GLU A 105     8450  18099   8822   4315  -1436  -1842       C  
ATOM    102  O   GLU A 105       7.991 -17.203   7.203  1.00 96.49           O  
ANISOU  102  O   GLU A 105     8966  18543   9154   4819  -1509  -1765       O  
ATOM    103  CB  GLU A 105       8.850 -15.688   9.446  1.00109.46           C  
ANISOU  103  CB  GLU A 105     9903  20993  10695   4264  -1839  -2065       C  
ATOM    104  CG  GLU A 105       9.490 -14.557  10.251  1.00115.54           C  
ANISOU  104  CG  GLU A 105    10172  22195  11532   3812  -1915  -2289       C  
ATOM    105  CD  GLU A 105      10.120 -13.473   9.386  1.00117.37           C  
ANISOU  105  CD  GLU A 105     9943  22494  12160   3369  -1631  -2420       C  
ATOM    106  OE1 GLU A 105      10.406 -13.729   8.197  1.00117.14           O  
ANISOU  106  OE1 GLU A 105     9916  22285  12306   3515  -1453  -2320       O  
ATOM    107  OE2 GLU A 105      10.322 -12.352   9.901  1.00119.90           O  
ANISOU  107  OE2 GLU A 105     9957  22993  12607   2856  -1590  -2608       O  
ATOM    108  N   ILE A 106       5.910 -16.378   7.426  1.00 85.13           N  
ANISOU  108  N   ILE A 106     7758  16705   7884   4129  -1308  -1766       N  
ATOM    109  CA  ILE A 106       5.345 -17.248   6.405  1.00 81.11           C  
ANISOU  109  CA  ILE A 106     7691  15735   7390   4433  -1208  -1600       C  
ATOM    110  C   ILE A 106       5.786 -16.727   5.045  1.00 77.74           C  
ANISOU  110  C   ILE A 106     6999  15270   7270   4175   -940  -1629       C  
ATOM    111  O   ILE A 106       5.559 -15.564   4.716  1.00 74.63           O  
ANISOU  111  O   ILE A 106     6311  14846   7197   3557   -731  -1692       O  
ATOM    112  CB  ILE A 106       3.805 -17.310   6.474  1.00 74.77           C  
ANISOU  112  CB  ILE A 106     7252  14516   6642   4254  -1157  -1503       C  
ATOM    113  CG1 ILE A 106       3.364 -18.238   7.606  1.00 76.94           C  
ANISOU  113  CG1 ILE A 106     8228  14514   6491   4498  -1426  -1332       C  
ATOM    114  CG2 ILE A 106       3.230 -17.801   5.152  1.00 71.67           C  
ANISOU  114  CG2 ILE A 106     7173  13643   6418   4356   -956  -1394       C  
ATOM    115  CD1 ILE A 106       3.807 -19.678   7.420  1.00 80.91           C  
ANISOU  115  CD1 ILE A 106     9265  14766   6713   5241  -1608  -1152       C  
ATOM    116  N   THR A 107       6.429 -17.580   4.259  1.00 79.92           N  
ANISOU  116  N   THR A 107     7434  15488   7445   4631   -951  -1557       N  
ATOM    117  CA  THR A 107       6.986 -17.145   2.984  1.00 79.71           C  
ANISOU  117  CA  THR A 107     7165  15464   7658   4437   -734  -1561       C  
ATOM    118  C   THR A 107       6.116 -17.563   1.807  1.00 75.85           C  
ANISOU  118  C   THR A 107     7066  14513   7240   4445   -575  -1445       C  
ATOM    119  O   THR A 107       5.142 -18.299   1.969  1.00 74.20           O  
ANISOU  119  O   THR A 107     7340  13956   6896   4649   -641  -1368       O  
ATOM    120  CB  THR A 107       8.405 -17.702   2.769  1.00 84.78           C  
ANISOU  120  CB  THR A 107     7614  16416   8181   4905   -814  -1587       C  
ATOM    121  OG1 THR A 107       8.329 -19.084   2.396  1.00 87.08           O  
ANISOU  121  OG1 THR A 107     8402  16461   8225   5519   -885  -1487       O  
ATOM    122  CG2 THR A 107       9.232 -17.557   4.040  1.00 89.26           C  
ANISOU  122  CG2 THR A 107     7863  17428   8625   5027  -1050  -1687       C  
ATOM    123  N   THR A 108       6.470 -17.069   0.625  1.00 76.27           N  
ANISOU  123  N   THR A 108     6927  14541   7509   4221   -368  -1432       N  
ATOM    124  CA  THR A 108       5.819 -17.472  -0.614  1.00 73.61           C  
ANISOU  124  CA  THR A 108     6925  13838   7205   4267   -227  -1341       C  
ATOM    125  C   THR A 108       5.925 -18.985  -0.781  1.00 75.62           C  
ANISOU  125  C   THR A 108     7677  13933   7122   4954   -354  -1301       C  
ATOM    126  O   THR A 108       4.933 -19.669  -1.059  1.00 73.27           O  
ANISOU  126  O   THR A 108     7905  13204   6729   5086   -374  -1235       O  
ATOM    127  CB  THR A 108       6.446 -16.750  -1.826  1.00 75.86           C  
ANISOU  127  CB  THR A 108     6907  14202   7715   4019      9  -1338       C  
ATOM    128  OG1 THR A 108       6.016 -15.382  -1.844  1.00 71.53           O  
ANISOU  128  OG1 THR A 108     6106  13566   7509   3355    153  -1324       O  
ATOM    129  CG2 THR A 108       6.047 -17.422  -3.132  1.00 76.49           C  
ANISOU  129  CG2 THR A 108     7351  14008   7702   4246    124  -1275       C  
ATOM    130  N   GLU A 109       7.135 -19.499  -0.587  1.00 80.02           N  
ANISOU  130  N   GLU A 109     8091  14791   7524   5381   -437  -1343       N  
ATOM    131  CA  GLU A 109       7.391 -20.933  -0.642  1.00 83.84           C  
ANISOU  131  CA  GLU A 109     9052  15101   7704   6048   -553  -1302       C  
ATOM    132  C   GLU A 109       6.487 -21.693   0.327  1.00 82.83           C  
ANISOU  132  C   GLU A 109     9487  14624   7361   6255   -751  -1233       C  
ATOM    133  O   GLU A 109       5.876 -22.700  -0.038  1.00 83.68           O  
ANISOU  133  O   GLU A 109    10239  14248   7308   6530   -770  -1161       O  
ATOM    134  CB  GLU A 109       8.860 -21.226  -0.330  1.00 89.63           C  
ANISOU  134  CB  GLU A 109     9433  16258   8364   6446   -630  -1359       C  
ATOM    135  N   ASP A 110       6.401 -21.198   1.558  1.00 82.38           N  
ANISOU  135  N   ASP A 110     9221  14774   7304   6098   -887  -1257       N  
ATOM    136  CA  ASP A 110       5.549 -21.811   2.572  1.00 82.23           C  
ANISOU  136  CA  ASP A 110     9728  14418   7099   6261  -1060  -1171       C  
ATOM    137  C   ASP A 110       4.084 -21.848   2.147  1.00 77.68           C  
ANISOU  137  C   ASP A 110     9605  13283   6628   6001   -965  -1095       C  
ATOM    138  O   ASP A 110       3.446 -22.897   2.211  1.00 77.99           O  
ANISOU  138  O   ASP A 110    10366  12771   6495   6266  -1037   -987       O  
ATOM    139  CB  ASP A 110       5.676 -21.070   3.906  1.00 83.90           C  
ANISOU  139  CB  ASP A 110     9568  14999   7311   6056  -1204  -1220       C  
ATOM    140  CG  ASP A 110       6.959 -21.402   4.640  1.00 91.03           C  
ANISOU  140  CG  ASP A 110    10239  16310   8038   6441  -1401  -1253       C  
ATOM    141  OD1 ASP A 110       7.443 -22.547   4.506  1.00 96.74           O  
ANISOU  141  OD1 ASP A 110    11323  16866   8569   6988  -1485  -1179       O  
ATOM    142  OD2 ASP A 110       7.476 -20.522   5.360  1.00 92.37           O  
ANISOU  142  OD2 ASP A 110     9872  16949   8276   6185  -1477  -1358       O  
ATOM    143  N   ILE A 111       3.555 -20.707   1.709  1.00 72.21           N  
ANISOU  143  N   ILE A 111     8511  12679   6247   5444   -794  -1148       N  
ATOM    144  CA  ILE A 111       2.137 -20.613   1.367  1.00 68.25           C  
ANISOU  144  CA  ILE A 111     8343  11670   5917   5163   -694  -1094       C  
ATOM    145  C   ILE A 111       1.810 -21.493   0.158  1.00 68.99           C  
ANISOU  145  C   ILE A 111     8983  11289   5939   5355   -636  -1049       C  
ATOM    146  O   ILE A 111       0.706 -22.051   0.063  1.00 67.78           O  
ANISOU  146  O   ILE A 111     9442  10526   5787   5329   -648   -989       O  
ATOM    147  CB  ILE A 111       1.702 -19.138   1.101  1.00 80.66           C  
ANISOU  147  CB  ILE A 111     9318  13443   7885   4474   -480  -1169       C  
ATOM    148  CG1 ILE A 111       0.191 -18.977   1.275  1.00 76.90           C  
ANISOU  148  CG1 ILE A 111     9194  12417   7605   3975   -397  -1094       C  
ATOM    149  CG2 ILE A 111       2.131 -18.650  -0.277  1.00 80.06           C  
ANISOU  149  CG2 ILE A 111     8980  13467   7974   4254   -304  -1179       C  
ATOM    150  CD1 ILE A 111      -0.306 -17.574   0.983  1.00 73.03           C  
ANISOU  150  CD1 ILE A 111     8169  12045   7534   3295   -172  -1143       C  
ATOM    151  N   LYS A 112       2.773 -21.647  -0.748  1.00 71.00           N  
ANISOU  151  N   LYS A 112     9062  11785   6128   5532   -571  -1087       N  
ATOM    152  CA  LYS A 112       2.561 -22.519  -1.893  1.00 72.88           C  
ANISOU  152  CA  LYS A 112     9822  11623   6248   5748   -524  -1067       C  
ATOM    153  C   LYS A 112       2.610 -23.977  -1.453  1.00 76.28           C  
ANISOU  153  C   LYS A 112    10960  11662   6361   6250   -687  -1006       C  
ATOM    154  O   LYS A 112       1.892 -24.814  -1.990  1.00 76.89           O  
ANISOU  154  O   LYS A 112    11702  11165   6348   6300   -700   -971       O  
ATOM    155  CB  LYS A 112       3.589 -22.255  -2.997  1.00 75.28           C  
ANISOU  155  CB  LYS A 112     9742  12290   6570   5816   -371  -1125       C  
ATOM    156  CG  LYS A 112       3.317 -23.055  -4.261  1.00 77.78           C  
ANISOU  156  CG  LYS A 112    10585  12216   6753   6009   -299  -1129       C  
ATOM    157  CD  LYS A 112       3.671 -22.282  -5.523  1.00 78.40           C  
ANISOU  157  CD  LYS A 112    10283  12544   6961   5796    -70  -1177       C  
ATOM    158  CE  LYS A 112       5.161 -22.019  -5.619  1.00 82.49           C  
ANISOU  158  CE  LYS A 112    10253  13596   7493   5978     31  -1220       C  
ATOM    159  NZ  LYS A 112       5.531 -21.455  -6.945  1.00 82.94           N  
ANISOU  159  NZ  LYS A 112    10076  13805   7633   5831    292  -1255       N  
ATOM    160  N   ALA A 113       3.455 -24.273  -0.471  1.00 79.16           N  
ANISOU  160  N   ALA A 113    11200  12316   6563   6577   -814   -996       N  
ATOM    161  CA  ALA A 113       3.528 -25.620   0.085  1.00 83.69           C  
ANISOU  161  CA  ALA A 113    12438  12512   6847   7030   -955   -920       C  
ATOM    162  C   ALA A 113       2.240 -25.979   0.823  1.00 80.21           C  
ANISOU  162  C   ALA A 113    12623  11461   6392   6826  -1036   -807       C  
ATOM    163  O   ALA A 113       1.829 -27.138   0.854  1.00 82.57           O  
ANISOU  163  O   ALA A 113    13666  11188   6519   6987  -1082   -731       O  
ATOM    164  CB  ALA A 113       4.725 -25.747   1.016  1.00 88.14           C  
ANISOU  164  CB  ALA A 113    12668  13547   7275   7405  -1080   -932       C  
ATOM    165  N   ALA A 114       1.605 -24.972   1.411  1.00 75.77           N  
ANISOU  165  N   ALA A 114    11754  11003   6032   6430  -1034   -789       N  
ATOM    166  CA  ALA A 114       0.375 -25.176   2.161  1.00 72.52           C  
ANISOU  166  CA  ALA A 114    11890  10017   5648   6174  -1095   -643       C  
ATOM    167  C   ALA A 114      -0.831 -25.330   1.240  1.00 70.54           C  
ANISOU  167  C   ALA A 114    12077   9135   5588   5812   -989   -636       C  
ATOM    168  O   ALA A 114      -1.726 -26.131   1.510  1.00 71.14           O  
ANISOU  168  O   ALA A 114    12873   8541   5616   5651  -1021   -515       O  
ATOM    169  CB  ALA A 114       0.155 -24.027   3.127  1.00 68.22           C  
ANISOU  169  CB  ALA A 114    10839   9839   5242   5763  -1110   -623       C  
ATOM    170  N   PHE A 115      -0.864 -24.566   0.152  1.00 67.42           N  
ANISOU  170  N   PHE A 115    11243   8961   5415   5580   -846   -772       N  
ATOM    171  CA  PHE A 115      -2.014 -24.633  -0.747  1.00 65.10           C  
ANISOU  171  CA  PHE A 115    11294   8137   5305   5088   -773   -778       C  
ATOM    172  C   PHE A 115      -1.829 -25.622  -1.899  1.00 67.84           C  
ANISOU  172  C   PHE A 115    12125   8197   5454   5388   -794   -832       C  
ATOM    173  O   PHE A 115      -2.759 -25.863  -2.667  1.00 66.72           O  
ANISOU  173  O   PHE A 115    12376   7572   5401   5062   -796   -854       O  
ATOM    174  CB  PHE A 115      -2.332 -23.243  -1.300  1.00 59.84           C  
ANISOU  174  CB  PHE A 115     9938   7815   4982   4507   -626   -837       C  
ATOM    175  CG  PHE A 115      -3.238 -22.438  -0.412  1.00 55.51           C  
ANISOU  175  CG  PHE A 115     9153   7202   4736   3830   -573   -748       C  
ATOM    176  CD1 PHE A 115      -2.738 -21.779   0.699  1.00 55.33           C  
ANISOU  176  CD1 PHE A 115     8676   7627   4720   3797   -551   -750       C  
ATOM    177  CD2 PHE A 115      -4.591 -22.349  -0.685  1.00 53.46           C  
ANISOU  177  CD2 PHE A 115     9122   6434   4756   3230   -545   -679       C  
ATOM    178  CE1 PHE A 115      -3.573 -21.044   1.520  1.00 52.07           C  
ANISOU  178  CE1 PHE A 115     8087   7130   4568   3185   -453   -699       C  
ATOM    179  CE2 PHE A 115      -5.431 -21.615   0.125  1.00 50.42           C  
ANISOU  179  CE2 PHE A 115     8499   5976   4683   2639   -445   -608       C  
ATOM    180  CZ  PHE A 115      -4.923 -20.961   1.231  1.00 49.89           C  
ANISOU  180  CZ  PHE A 115     8025   6331   4599   2620   -374   -626       C  
ATOM    181  N   ALA A 116      -0.638 -26.203  -2.003  1.00 71.61           N  
ANISOU  181  N   ALA A 116    12543   8995   5668   5895   -819   -844       N  
ATOM    182  CA  ALA A 116      -0.326 -27.162  -3.066  1.00 75.90           C  
ANISOU  182  CA  ALA A 116    13495   9333   6012   6150   -808   -887       C  
ATOM    183  C   ALA A 116      -1.286 -28.362  -3.176  1.00 79.48           C  
ANISOU  183  C   ALA A 116    14828   9009   6362   6012   -892   -833       C  
ATOM    184  O   ALA A 116      -1.627 -28.761  -4.287  1.00 80.96           O  
ANISOU  184  O   ALA A 116    15331   8915   6517   5917   -878   -897       O  
ATOM    185  CB  ALA A 116       1.108 -27.671  -2.903  1.00 79.93           C  
ANISOU  185  CB  ALA A 116    13821  10261   6286   6740   -810   -902       C  
ATOM    186  N   PRO A 117      -1.714 -28.954  -2.041  1.00 81.32           N  
ANISOU  186  N   PRO A 117    15461   8899   6536   5965   -970   -717       N  
ATOM    187  CA  PRO A 117      -2.551 -30.153  -2.202  1.00 85.43           C  
ANISOU  187  CA  PRO A 117    16766   8721   6971   5778  -1018   -671       C  
ATOM    188  C   PRO A 117      -3.969 -29.903  -2.724  1.00 84.67           C  
ANISOU  188  C   PRO A 117    16855   8174   7143   5092  -1031   -677       C  
ATOM    189  O   PRO A 117      -4.693 -30.869  -2.956  1.00 86.50           O  
ANISOU  189  O   PRO A 117    17654   7878   7335   4863  -1074   -656       O  
ATOM    190  CB  PRO A 117      -2.620 -30.724  -0.777  1.00 86.95           C  
ANISOU  190  CB  PRO A 117    17263   8719   7054   5856  -1057   -531       C  
ATOM    191  CG  PRO A 117      -1.451 -30.140  -0.063  1.00 86.58           C  
ANISOU  191  CG  PRO A 117    16668   9311   6916   6306  -1072   -534       C  
ATOM    192  CD  PRO A 117      -1.313 -28.768  -0.633  1.00 81.79           C  
ANISOU  192  CD  PRO A 117    15339   9195   6541   6138  -1015   -628       C  
ATOM    193  N   PHE A 118      -4.360 -28.647  -2.909  1.00 83.80           N  
ANISOU  193  N   PHE A 118    16246   8276   7317   4756   -995   -714       N  
ATOM    194  CA  PHE A 118      -5.737 -28.334  -3.290  1.00 85.64           C  
ANISOU  194  CA  PHE A 118    16585   8098   7855   4067  -1028   -713       C  
ATOM    195  C   PHE A 118      -5.972 -28.275  -4.786  1.00 82.88           C  
ANISOU  195  C   PHE A 118    16297   7689   7504   3940  -1078   -847       C  
ATOM    196  O   PHE A 118      -7.072 -27.955  -5.236  1.00 80.69           O  
ANISOU  196  O   PHE A 118    16049   7132   7477   3372  -1154   -858       O  
ATOM    197  CB  PHE A 118      -6.157 -27.008  -2.674  1.00 86.78           C  
ANISOU  197  CB  PHE A 118    16210   8418   8343   3727   -961   -685       C  
ATOM    198  CG  PHE A 118      -6.345 -27.085  -1.207  1.00 93.17           C  
ANISOU  198  CG  PHE A 118    17095   9118   9186   3658   -920   -532       C  
ATOM    199  CD1 PHE A 118      -7.516 -27.593  -0.682  1.00 96.51           C  
ANISOU  199  CD1 PHE A 118    17875   9024   9771   3113   -907   -406       C  
ATOM    200  CD2 PHE A 118      -5.342 -26.685  -0.349  1.00 94.69           C  
ANISOU  200  CD2 PHE A 118    16943   9807   9228   4089   -887   -506       C  
ATOM    201  CE1 PHE A 118      -7.689 -27.688   0.672  1.00 97.70           C  
ANISOU  201  CE1 PHE A 118    18154   9067   9901   3038   -828   -256       C  
ATOM    202  CE2 PHE A 118      -5.510 -26.779   1.007  1.00 98.41           C  
ANISOU  202  CE2 PHE A 118    17529  10207   9657   4001   -865   -351       C  
ATOM    203  CZ  PHE A 118      -6.691 -27.276   1.523  1.00 99.16           C  
ANISOU  203  CZ  PHE A 118    18132   9664   9881   3524   -821   -222       C  
ATOM    204  N   GLY A 119      -4.939 -28.591  -5.553  1.00 84.42           N  
ANISOU  204  N   GLY A 119    16503   8157   7417   4455  -1040   -938       N  
ATOM    205  CA  GLY A 119      -4.994 -28.447  -6.991  1.00 82.70           C  
ANISOU  205  CA  GLY A 119    16338   7954   7132   4402  -1054  -1070       C  
ATOM    206  C   GLY A 119      -3.788 -27.651  -7.428  1.00 80.10           C  
ANISOU  206  C   GLY A 119    15432   8286   6716   4818   -889  -1144       C  
ATOM    207  O   GLY A 119      -3.054 -27.115  -6.595  1.00 78.19           O  
ANISOU  207  O   GLY A 119    14691   8491   6528   5052   -800  -1097       O  
ATOM    208  N   ARG A 120      -3.581 -27.558  -8.733  1.00 79.82           N  
ANISOU  208  N   ARG A 120    15436   8344   6546   4869   -840  -1256       N  
ATOM    209  CA  ARG A 120      -2.355 -26.960  -9.229  1.00 80.54           C  
ANISOU  209  CA  ARG A 120    14992   9065   6546   5244   -632  -1308       C  
ATOM    210  C   ARG A 120      -2.352 -25.440  -9.178  1.00 74.37           C  
ANISOU  210  C   ARG A 120    13502   8777   5979   4987   -514  -1317       C  
ATOM    211  O   ARG A 120      -3.330 -24.769  -9.514  1.00 71.62           O  
ANISOU  211  O   ARG A 120    13176   8284   5752   4519   -581  -1349       O  
ATOM    212  CB  ARG A 120      -2.076 -27.455 -10.639  1.00 86.29           C  
ANISOU  212  CB  ARG A 120    16053   9710   7023   5396   -567  -1421       C  
ATOM    213  CG  ARG A 120      -2.219 -28.957 -10.703  1.00 93.24           C  
ANISOU  213  CG  ARG A 120    17669  10050   7707   5584   -676  -1432       C  
ATOM    214  CD  ARG A 120      -0.989 -29.591 -11.293  1.00100.30           C  
ANISOU  214  CD  ARG A 120    18609  11144   8356   6155   -495  -1504       C  
ATOM    215  NE  ARG A 120      -0.452 -28.813 -12.403  1.00101.88           N  
ANISOU  215  NE  ARG A 120    18457  11758   8494   6183   -290  -1604       N  
ATOM    216  CZ  ARG A 120       0.842 -28.594 -12.611  1.00105.11           C  
ANISOU  216  CZ  ARG A 120    18412  12674   8849   6593    -48  -1631       C  
ATOM    217  NH1 ARG A 120       1.749 -29.125 -11.800  1.00108.38           N  
ANISOU  217  NH1 ARG A 120    18674  13250   9257   7043    -22  -1577       N  
ATOM    218  NH2 ARG A 120       1.229 -27.870 -13.655  1.00105.62           N  
ANISOU  218  NH2 ARG A 120    18198  13081   8852   6534    169  -1712       N  
ATOM    219  N   ILE A 121      -1.211 -24.919  -8.747  1.00 73.58           N  
ANISOU  219  N   ILE A 121    12762   9276   5920   5278   -353  -1286       N  
ATOM    220  CA  ILE A 121      -1.036 -23.504  -8.486  1.00 68.97           C  
ANISOU  220  CA  ILE A 121    11417   9222   5568   5041   -214  -1273       C  
ATOM    221  C   ILE A 121      -0.366 -22.802  -9.659  1.00 70.22           C  
ANISOU  221  C   ILE A 121    11200   9816   5665   5051     10  -1316       C  
ATOM    222  O   ILE A 121       0.738 -23.168 -10.064  1.00 74.19           O  
ANISOU  222  O   ILE A 121    11587  10570   6032   5411    132  -1333       O  
ATOM    223  CB  ILE A 121      -0.207 -23.299  -7.206  1.00 69.88           C  
ANISOU  223  CB  ILE A 121    11018   9740   5794   5234   -207  -1204       C  
ATOM    224  CG1 ILE A 121      -1.013 -23.755  -5.986  1.00 67.83           C  
ANISOU  224  CG1 ILE A 121    11112   9061   5597   5141   -387  -1146       C  
ATOM    225  CG2 ILE A 121       0.209 -21.853  -7.062  1.00 67.08           C  
ANISOU  225  CG2 ILE A 121     9813   9985   5689   4962    -39  -1194       C  
ATOM    226  CD1 ILE A 121      -0.224 -23.780  -4.701  1.00 68.75           C  
ANISOU  226  CD1 ILE A 121    10902   9516   5705   5390   -434  -1083       C  
ATOM    227  N   SER A 122      -1.042 -21.802 -10.213  1.00 66.07           N  
ANISOU  227  N   SER A 122    10514   9366   5224   4648     76  -1327       N  
ATOM    228  CA  SER A 122      -0.478 -21.039 -11.318  1.00 67.29           C  
ANISOU  228  CA  SER A 122    10338   9927   5303   4602    315  -1330       C  
ATOM    229  C   SER A 122       0.499 -20.001 -10.780  1.00 66.51           C  
ANISOU  229  C   SER A 122     9347  10443   5481   4540    518  -1255       C  
ATOM    230  O   SER A 122       1.499 -19.679 -11.423  1.00 68.89           O  
ANISOU  230  O   SER A 122     9326  11101   5748   4631    733  -1249       O  
ATOM    231  CB  SER A 122      -1.581 -20.368 -12.145  1.00 64.24           C  
ANISOU  231  CB  SER A 122    10139   9373   4896   4115    247  -1285       C  
ATOM    232  OG  SER A 122      -2.230 -19.339 -11.418  1.00 60.01           O  
ANISOU  232  OG  SER A 122     9079   8885   4839   3557    172  -1097       O  
ATOM    233  N   ASP A 123       0.207 -19.493  -9.588  1.00 62.96           N  
ANISOU  233  N   ASP A 123     8532  10071   5317   4328    442  -1207       N  
ATOM    234  CA  ASP A 123       1.051 -18.494  -8.948  1.00 63.33           C  
ANISOU  234  CA  ASP A 123     7790  10615   5659   4125    560  -1142       C  
ATOM    235  C   ASP A 123       0.695 -18.393  -7.470  1.00 60.70           C  
ANISOU  235  C   ASP A 123     7291  10238   5535   3986    404  -1122       C  
ATOM    236  O   ASP A 123      -0.401 -18.759  -7.067  1.00 58.55           O  
ANISOU  236  O   ASP A 123     7406   9576   5266   3945    280  -1141       O  
ATOM    237  CB  ASP A 123       0.891 -17.132  -9.630  1.00 61.80           C  
ANISOU  237  CB  ASP A 123     7153  10658   5671   3677    774  -1069       C  
ATOM    238  CG  ASP A 123       1.891 -16.107  -9.130  1.00 62.63           C  
ANISOU  238  CG  ASP A 123     6574  11134   6087   3379    887  -1014       C  
ATOM    239  OD1 ASP A 123       3.042 -16.493  -8.831  1.00 66.01           O  
ANISOU  239  OD1 ASP A 123     6872  11761   6450   3633    879  -1065       O  
ATOM    240  OD2 ASP A 123       1.518 -14.918  -9.021  1.00 59.60           O  
ANISOU  240  OD2 ASP A 123     5835  10786   6024   2878    973   -927       O  
ATOM    241  N   ALA A 124       1.625 -17.905  -6.662  1.00 61.24           N  
ANISOU  241  N   ALA A 124     6845  10669   5752   3898    412  -1105       N  
ATOM    242  CA  ALA A 124       1.365 -17.694  -5.246  1.00 59.60           C  
ANISOU  242  CA  ALA A 124     6471  10476   5697   3734    285  -1100       C  
ATOM    243  C   ALA A 124       2.403 -16.741  -4.693  1.00 60.06           C  
ANISOU  243  C   ALA A 124     5933  10943   5944   3465    341  -1105       C  
ATOM    244  O   ALA A 124       3.583 -16.842  -5.030  1.00 62.77           O  
ANISOU  244  O   ALA A 124     6104  11551   6195   3673    388  -1135       O  
ATOM    245  CB  ALA A 124       1.384 -19.011  -4.485  1.00 61.69           C  
ANISOU  245  CB  ALA A 124     7220  10536   5685   4230     75  -1124       C  
ATOM    246  N   ARG A 125       1.969 -15.805  -3.860  1.00 56.92           N  
ANISOU  246  N   ARG A 125     5256  10547   5824   2992    350  -1091       N  
ATOM    247  CA  ARG A 125       2.916 -14.877  -3.263  1.00 59.87           C  
ANISOU  247  CA  ARG A 125     5189  11193   6366   2713    385  -1121       C  
ATOM    248  C   ARG A 125       2.414 -14.333  -1.939  1.00 56.55           C  
ANISOU  248  C   ARG A 125     4653  10733   6100   2386    316  -1149       C  
ATOM    249  O   ARG A 125       1.216 -14.170  -1.734  1.00 53.51           O  
ANISOU  249  O   ARG A 125     4393  10070   5868   2140    344  -1110       O  
ATOM    250  CB  ARG A 125       3.216 -13.719  -4.222  1.00 59.93           C  
ANISOU  250  CB  ARG A 125     4948  11175   6648   2316    608  -1059       C  
ATOM    251  CG  ARG A 125       2.163 -12.615  -4.259  1.00 58.17           C  
ANISOU  251  CG  ARG A 125     4691  10623   6786   1755    715   -960       C  
ATOM    252  CD  ARG A 125       2.446 -11.650  -5.403  1.00 60.63           C  
ANISOU  252  CD  ARG A 125     4872  10858   7304   1509    930   -864       C  
ATOM    253  NE  ARG A 125       1.684 -10.407  -5.316  1.00 59.72           N  
ANISOU  253  NE  ARG A 125     4723  10379   7587   1014   1025   -731       N  
ATOM    254  CZ  ARG A 125       2.134  -9.295  -4.741  1.00 62.43           C  
ANISOU  254  CZ  ARG A 125     4880  10694   8147    745   1073   -718       C  
ATOM    255  NH1 ARG A 125       3.344  -9.270  -4.196  1.00 66.77           N  
ANISOU  255  NH1 ARG A 125     5205  11584   8579    859   1037   -851       N  
ATOM    256  NH2 ARG A 125       1.374  -8.206  -4.708  1.00 60.48           N  
ANISOU  256  NH2 ARG A 125     4632  10191   8158    405   1130   -611       N  
ATOM    257  N   VAL A 126       3.346 -14.074  -1.033  1.00 58.79           N  
ANISOU  257  N   VAL A 126     4686  11318   6333   2400    233  -1236       N  
ATOM    258  CA  VAL A 126       3.035 -13.335   0.174  1.00 57.03           C  
ANISOU  258  CA  VAL A 126     4319  11102   6246   2037    204  -1293       C  
ATOM    259  C   VAL A 126       3.395 -11.880  -0.087  1.00 56.67           C  
ANISOU  259  C   VAL A 126     4033  10945   6555   1528    377  -1260       C  
ATOM    260  O   VAL A 126       4.498 -11.581  -0.542  1.00 58.93           O  
ANISOU  260  O   VAL A 126     4106  11424   6860   1587    426  -1278       O  
ATOM    261  CB  VAL A 126       3.801 -13.875   1.388  1.00 60.44           C  
ANISOU  261  CB  VAL A 126     4648  11950   6366   2387    -14  -1424       C  
ATOM    262  CG1 VAL A 126       3.388 -13.132   2.647  1.00 59.67           C  
ANISOU  262  CG1 VAL A 126     4420  11897   6353   2011    -33  -1520       C  
ATOM    263  CG2 VAL A 126       3.556 -15.369   1.536  1.00 61.00           C  
ANISOU  263  CG2 VAL A 126     5084  12018   6075   3028   -192  -1398       C  
ATOM    264  N   VAL A 127       2.458 -10.979   0.173  1.00 58.43           N  
ANISOU  264  N   VAL A 127     3924  12498   5778     19      9   -550       N  
ATOM    265  CA  VAL A 127       2.676  -9.567  -0.111  1.00 62.57           C  
ANISOU  265  CA  VAL A 127     4051  13045   6677   -159    202   -696       C  
ATOM    266  C   VAL A 127       3.588  -8.929   0.931  1.00 67.72           C  
ANISOU  266  C   VAL A 127     4376  13705   7650   -560     80  -1111       C  
ATOM    267  O   VAL A 127       3.340  -9.022   2.132  1.00 66.90           O  
ANISOU  267  O   VAL A 127     4356  13694   7369   -571   -197  -1415       O  
ATOM    268  CB  VAL A 127       1.349  -8.795  -0.170  1.00 62.19           C  
ANISOU  268  CB  VAL A 127     4275  12835   6519    151    168   -787       C  
ATOM    269  CG1 VAL A 127       1.606  -7.325  -0.458  1.00 66.24           C  
ANISOU  269  CG1 VAL A 127     5049  12613   7505    -38    327   -861       C  
ATOM    270  CG2 VAL A 127       0.432  -9.401  -1.227  1.00 58.42           C  
ANISOU  270  CG2 VAL A 127     4081  12418   5698    526    264   -352       C  
ATOM    271  N   LYS A 128       4.649  -8.287   0.457  1.00 72.62           N  
ANISOU  271  N   LYS A 128     4818  14079   8695   -935    332  -1086       N  
ATOM    272  CA  LYS A 128       5.617  -7.634   1.328  1.00 78.45           C  
ANISOU  272  CA  LYS A 128     5259  14783   9766  -1391    242  -1474       C  
ATOM    273  C   LYS A 128       5.675  -6.144   1.033  1.00 83.30           C  
ANISOU  273  C   LYS A 128     6224  14673  10751  -1623    459  -1596       C  
ATOM    274  O   LYS A 128       5.430  -5.723  -0.097  1.00 83.80           O  
ANISOU  274  O   LYS A 128     6681  14260  10899  -1548    730  -1236       O  
ATOM    275  CB  LYS A 128       7.002  -8.248   1.140  1.00 81.67           C  
ANISOU  275  CB  LYS A 128     5461  15177  10393  -1600    304  -1300       C  
ATOM    276  CG  LYS A 128       7.197  -9.607   1.780  1.00 79.95           C  
ANISOU  276  CG  LYS A 128     5425  15000   9950  -1303    -14  -1148       C  
ATOM    277  CD  LYS A 128       8.635 -10.062   1.589  1.00 83.42           C  
ANISOU  277  CD  LYS A 128     5619  15307  10769  -1460     37  -1041       C  
ATOM    278  CE  LYS A 128       8.927 -11.347   2.339  1.00 81.99           C  
ANISOU  278  CE  LYS A 128     5531  15108  10514  -1231   -293   -919       C  
ATOM    279  NZ  LYS A 128       9.882 -11.099   3.457  1.00 86.51           N  
ANISOU  279  NZ  LYS A 128     5839  15720  11311  -1493   -554  -1084       N  
ATOM    280  N   ASP A 129       6.001  -5.341   2.040  1.00 86.51           N  
ANISOU  280  N   ASP A 129     6514  14982  11375  -1943    324  -2088       N  
ATOM    281  CA  ASP A 129       6.229  -3.925   1.793  1.00 92.33           C  
ANISOU  281  CA  ASP A 129     7561  14965  12555  -2236    527  -2227       C  
ATOM    282  C   ASP A 129       7.553  -3.741   1.055  1.00 94.76           C  
ANISOU  282  C   ASP A 129     7721  15109  13176  -2723    825  -1992       C  
ATOM    283  O   ASP A 129       8.545  -4.395   1.367  1.00 95.17           O  
ANISOU  283  O   ASP A 129     7244  15668  13248  -2979    780  -2056       O  
ATOM    284  CB  ASP A 129       6.231  -3.126   3.092  1.00 95.97           C  
ANISOU  284  CB  ASP A 129     7923  15377  13164  -2494    334  -2902       C  
ATOM    285  CG  ASP A 129       6.689  -1.696   2.889  1.00103.15           C  
ANISOU  285  CG  ASP A 129     9105  15476  14611  -2891    543  -3079       C  
ATOM    286  OD1 ASP A 129       5.839  -0.814   2.646  1.00105.93           O  
ANISOU  286  OD1 ASP A 129     9921  15148  15179  -2656    588  -3141       O  
ATOM    287  OD2 ASP A 129       7.914  -1.461   2.928  1.00106.24           O  
ANISOU  287  OD2 ASP A 129     9238  15884  15245  -3440    654  -3136       O  
ATOM    288  N   MET A 130       7.550  -2.846   0.074  1.00 97.89           N  
ANISOU  288  N   MET A 130     8572  14799  13823  -2865   1111  -1715       N  
ATOM    289  CA  MET A 130       8.712  -2.592  -0.771  1.00100.86           C  
ANISOU  289  CA  MET A 130     8881  15002  14441  -3394   1463  -1468       C  
ATOM    290  C   MET A 130       9.926  -2.133   0.012  1.00104.61           C  
ANISOU  290  C   MET A 130     8924  15573  15250  -3997   1460  -1910       C  
ATOM    291  O   MET A 130      10.883  -2.889   0.192  1.00104.00           O  
ANISOU  291  O   MET A 130     8254  16082  15178  -4202   1468  -1976       O  
ATOM    292  CB  MET A 130       8.376  -1.536  -1.819  1.00105.79           C  
ANISOU  292  CB  MET A 130    10172  14779  15246  -3516   1695  -1089       C  
ATOM    293  CG  MET A 130       8.941  -1.809  -3.189  1.00107.14           C  
ANISOU  293  CG  MET A 130    10438  14958  15311  -3801   2084   -553       C  
ATOM    294  SD  MET A 130       7.934  -3.067  -3.963  1.00112.52           S  
ANISOU  294  SD  MET A 130    11231  16083  15439  -3156   2063   -106       S  
ATOM    295  CE  MET A 130       6.302  -2.408  -3.608  1.00105.29           C  
ANISOU  295  CE  MET A 130    10866  14636  14503  -2552   1691   -107       C  
ATOM    296  N   ALA A 131       9.864  -0.884   0.458  1.00108.92           N  
ANISOU  296  N   ALA A 131     9758  15515  16113  -4271   1435  -2224       N  
ATOM    297  CA  ALA A 131      10.937  -0.237   1.186  1.00113.95           C  
ANISOU  297  CA  ALA A 131    10075  16142  17078  -4914   1443  -2679       C  
ATOM    298  C   ALA A 131      11.506  -1.106   2.303  1.00110.79           C  
ANISOU  298  C   ALA A 131     8956  16622  16518  -4976   1142  -3046       C  
ATOM    299  O   ALA A 131      12.705  -1.121   2.580  1.00114.26           O  
ANISOU  299  O   ALA A 131     8896  17365  17153  -5492   1173  -3225       O  
ATOM    300  CB  ALA A 131      10.425   1.080   1.737  1.00119.14           C  
ANISOU  300  CB  ALA A 131    11169  16057  18040  -5023   1368  -3077       C  
ATOM    301  N   THR A 132      10.632  -1.870   2.925  1.00105.07           N  
ANISOU  301  N   THR A 132     8167  16334  15420  -4461    823  -3121       N  
ATOM    302  CA  THR A 132      11.013  -2.639   4.096  1.00103.43           C  
ANISOU  302  CA  THR A 132     7378  16918  15003  -4529    438  -3424       C  
ATOM    303  C   THR A 132      11.232  -4.146   3.829  1.00 98.56           C  
ANISOU  303  C   THR A 132     6669  16719  14061  -3976    286  -2869       C  
ATOM    304  O   THR A 132      12.295  -4.711   4.140  1.00 99.89           O  
ANISOU  304  O   THR A 132     6642  17043  14270  -3962    133  -2699       O  
ATOM    305  CB  THR A 132       9.962  -2.426   5.171  1.00101.77           C  
ANISOU  305  CB  THR A 132     7346  16803  14519  -4324    140  -3860       C  
ATOM    306  OG1 THR A 132       8.704  -2.980   4.780  1.00 96.54           O  
ANISOU  306  OG1 THR A 132     7012  16141  13527  -3674    109  -3588       O  
ATOM    307  CG2 THR A 132       9.793  -0.910   5.420  1.00107.50           C  
ANISOU  307  CG2 THR A 132     8459  16784  15600  -4632    295  -4320       C  
ATOM    308  N   GLY A 133      10.239  -4.803   3.235  1.00 93.92           N  
ANISOU  308  N   GLY A 133     6228  16239  13217  -3523    325  -2603       N  
ATOM    309  CA  GLY A 133      10.372  -6.220   2.928  1.00 90.01           C  
ANISOU  309  CA  GLY A 133     5754  15962  12482  -3019    210  -2127       C  
ATOM    310  C   GLY A 133       9.701  -7.077   3.973  1.00 86.99           C  
ANISOU  310  C   GLY A 133     5564  15825  11662  -2606   -216  -2110       C  
ATOM    311  O   GLY A 133      10.039  -8.247   4.112  1.00 84.31           O  
ANISOU  311  O   GLY A 133     5260  15548  11228  -2313   -395  -1803       O  
ATOM    312  N   LYS A 134       8.754  -6.497   4.708  1.00 87.93           N  
ANISOU  312  N   LYS A 134     5827  16024  11556  -2625   -344  -2470       N  
ATOM    313  CA  LYS A 134       8.035  -7.265   5.720  1.00 86.08           C  
ANISOU  313  CA  LYS A 134     5853  16016  10839  -2308   -656  -2446       C  
ATOM    314  C   LYS A 134       6.719  -7.734   5.188  1.00 80.09           C  
ANISOU  314  C   LYS A 134     5357  15317   9755  -1873   -598  -2290       C  
ATOM    315  O   LYS A 134       6.016  -7.005   4.484  1.00 79.72           O  
ANISOU  315  O   LYS A 134     5264  15209   9818  -1852   -412  -2446       O  
ATOM    316  CB  LYS A 134       7.762  -6.481   7.009  1.00 90.48           C  
ANISOU  316  CB  LYS A 134     6448  16679  11252  -2572   -808  -2961       C  
ATOM    317  CG  LYS A 134       8.654  -5.304   7.255  1.00 97.46           C  
ANISOU  317  CG  LYS A 134     7095  17403  12533  -3119   -730  -3362       C  
ATOM    318  CD  LYS A 134      10.073  -5.795   7.208  1.00100.15           C  
ANISOU  318  CD  LYS A 134     7211  17742  13099  -3250   -807  -3029       C  
ATOM    319  CE  LYS A 134      11.053  -4.692   7.262  1.00107.27           C  
ANISOU  319  CE  LYS A 134     7886  18462  14409  -3803   -678  -3346       C  
ATOM    320  NZ  LYS A 134      12.269  -5.157   6.588  1.00108.92           N  
ANISOU  320  NZ  LYS A 134     7829  18616  14937  -3844   -603  -2976       N  
ATOM    321  N   SER A 135       6.382  -8.951   5.582  1.00 76.25           N  
ANISOU  321  N   SER A 135     5144  14916   8912  -1555   -758  -1988       N  
ATOM    322  CA  SER A 135       5.104  -9.533   5.263  1.00 70.50           C  
ANISOU  322  CA  SER A 135     4741  14240   7804  -1164   -708  -1836       C  
ATOM    323  C   SER A 135       4.015  -8.593   5.744  1.00 70.13           C  
ANISOU  323  C   SER A 135     4727  14328   7592  -1170   -700  -2303       C  
ATOM    324  O   SER A 135       4.035  -8.127   6.886  1.00 73.77           O  
ANISOU  324  O   SER A 135     5155  14894   7982  -1399   -798  -2674       O  
ATOM    325  CB  SER A 135       4.970 -10.910   5.904  1.00 67.41           C  
ANISOU  325  CB  SER A 135     4639  13844   7130   -984   -838  -1535       C  
ATOM    326  OG  SER A 135       3.734 -11.501   5.561  1.00 63.10           O  
ANISOU  326  OG  SER A 135     4423  13308   6244   -667   -713  -1393       O  
ATOM    327  N   LYS A 136       3.086  -8.299   4.846  1.00 67.07           N  
ANISOU  327  N   LYS A 136     4371  13929   7184   -908   -582  -2301       N  
ATOM    328  CA  LYS A 136       1.974  -7.410   5.134  1.00 68.08           C  
ANISOU  328  CA  LYS A 136     4461  14134   7274   -810   -604  -2805       C  
ATOM    329  C   LYS A 136       0.909  -8.141   5.948  1.00 66.04           C  
ANISOU  329  C   LYS A 136     4542  14046   6503   -561   -615  -2808       C  
ATOM    330  O   LYS A 136      -0.044  -7.531   6.436  1.00 68.31           O  
ANISOU  330  O   LYS A 136     4805  14428   6721   -469   -612  -3285       O  
ATOM    331  CB  LYS A 136       1.379  -6.868   3.830  1.00 66.46           C  
ANISOU  331  CB  LYS A 136     4324  13607   7321   -499   -426  -2626       C  
ATOM    332  CG  LYS A 136       2.339  -6.025   2.991  1.00 69.51           C  
ANISOU  332  CG  LYS A 136     4842  13316   8254   -735   -155  -2412       C  
ATOM    333  CD  LYS A 136       2.209  -4.539   3.304  1.00 75.37           C  
ANISOU  333  CD  LYS A 136     5795  13396   9447   -870    -78  -2860       C  
ATOM    334  CE  LYS A 136       3.142  -4.122   4.432  1.00 79.35           C  
ANISOU  334  CE  LYS A 136     5978  14067  10104  -1423   -174  -3393       C  
ATOM    335  NZ  LYS A 136       2.982  -2.695   4.830  1.00 85.65           N  
ANISOU  335  NZ  LYS A 136     6976  14212  11353  -1577    -91  -3933       N  
ATOM    336  N   GLY A 137       1.084  -9.452   6.092  1.00 61.83           N  
ANISOU  336  N   GLY A 137     4269  13495   5728   -483   -573  -2310       N  
ATOM    337  CA  GLY A 137       0.157 -10.272   6.849  1.00 59.52           C  
ANISOU  337  CA  GLY A 137     4203  13281   5132   -354   -467  -2214       C  
ATOM    338  C   GLY A 137      -0.862 -10.975   5.972  1.00 57.66           C  
ANISOU  338  C   GLY A 137     4185  12960   4762      7   -282  -1911       C  
ATOM    339  O   GLY A 137      -1.842 -11.531   6.474  1.00 55.11           O  
ANISOU  339  O   GLY A 137     3930  12662   4346    102   -138  -1869       O  
ATOM    340  N   TYR A 138      -0.637 -10.947   4.660  1.00 56.17           N  
ANISOU  340  N   TYR A 138     4052  12662   4626    162   -277  -1680       N  
ATOM    341  CA  TYR A 138      -1.537 -11.612   3.723  1.00 54.13           C  
ANISOU  341  CA  TYR A 138     4024  12312   4230    464    -82  -1374       C  
ATOM    342  C   TYR A 138      -0.850 -11.977   2.409  1.00 52.61           C  
ANISOU  342  C   TYR A 138     3938  12000   4051    497    -76   -987       C  
ATOM    343  O   TYR A 138       0.271 -11.546   2.135  1.00 56.43           O  
ANISOU  343  O   TYR A 138     4201  12459   4779    317   -208   -961       O  
ATOM    344  CB  TYR A 138      -2.769 -10.739   3.443  1.00 55.51           C  
ANISOU  344  CB  TYR A 138     4178  12499   4414    736   -130  -1607       C  
ATOM    345  CG  TYR A 138      -2.494  -9.452   2.691  1.00 59.58           C  
ANISOU  345  CG  TYR A 138     4462  13110   5064    838   -338  -1793       C  
ATOM    346  CD1 TYR A 138      -2.071  -8.309   3.358  1.00 63.92           C  
ANISOU  346  CD1 TYR A 138     4621  13720   5947    648   -495  -2335       C  
ATOM    347  CD2 TYR A 138      -2.680  -9.375   1.316  1.00 58.83           C  
ANISOU  347  CD2 TYR A 138     4426  12895   5029   1096   -311  -1369       C  
ATOM    348  CE1 TYR A 138      -1.830  -7.130   2.676  1.00 68.05           C  
ANISOU  348  CE1 TYR A 138     5131  13708   7016    701   -402  -2354       C  
ATOM    349  CE2 TYR A 138      -2.439  -8.200   0.624  1.00 62.82           C  
ANISOU  349  CE2 TYR A 138     4818  13023   6027   1186   -237  -1324       C  
ATOM    350  CZ  TYR A 138      -2.013  -7.082   1.309  1.00 67.59           C  
ANISOU  350  CZ  TYR A 138     5380  13232   7068    957   -241  -1777       C  
ATOM    351  OH  TYR A 138      -1.771  -5.911   0.628  1.00 71.79           O  
ANISOU  351  OH  TYR A 138     6202  12949   8127    932    -95  -1644       O  
ATOM    352  N   GLY A 139      -1.534 -12.779   1.600  1.00 40.83           N  
ANISOU  352  N   GLY A 139     4468   6266   4778   1504    446   -459       N  
ATOM    353  CA  GLY A 139      -0.993 -13.224   0.331  1.00 40.87           C  
ANISOU  353  CA  GLY A 139     4583   6304   4640   1666    378   -418       C  
ATOM    354  C   GLY A 139      -2.070 -13.723  -0.613  1.00 41.98           C  
ANISOU  354  C   GLY A 139     4919   6256   4775   1593    245   -323       C  
ATOM    355  O   GLY A 139      -3.256 -13.678  -0.289  1.00 42.84           O  
ANISOU  355  O   GLY A 139     5007   6203   5067   1406    204   -265       O  
ATOM    356  N   PHE A 140      -1.647 -14.198  -1.782  1.00 42.66           N  
ANISOU  356  N   PHE A 140     5189   6363   4655   1739    180   -318       N  
ATOM    357  CA  PHE A 140      -2.556 -14.697  -2.807  1.00 44.12           C  
ANISOU  357  CA  PHE A 140     5608   6386   4770   1673    -10   -262       C  
ATOM    358  C   PHE A 140      -2.104 -16.042  -3.368  1.00 46.98           C  
ANISOU  358  C   PHE A 140     6347   6678   4826   1870   -110   -370       C  
ATOM    359  O   PHE A 140      -0.902 -16.302  -3.492  1.00 48.61           O  
ANISOU  359  O   PHE A 140     6594   7018   4859   2111     21   -451       O  
ATOM    360  CB  PHE A 140      -2.676 -13.692  -3.950  1.00 44.12           C  
ANISOU  360  CB  PHE A 140     5512   6466   4787   1623     -1   -142       C  
ATOM    361  CG  PHE A 140      -3.264 -12.375  -3.544  1.00 42.81           C  
ANISOU  361  CG  PHE A 140     4992   6292   4982   1434     78    -24       C  
ATOM    362  CD1 PHE A 140      -4.636 -12.216  -3.445  1.00 42.55           C  
ANISOU  362  CD1 PHE A 140     4878   6074   5216   1233    -68     71       C  
ATOM    363  CD2 PHE A 140      -2.446 -11.289  -3.279  1.00 41.76           C  
ANISOU  363  CD2 PHE A 140     4583   6309   4975   1457    304    -15       C  
ATOM    364  CE1 PHE A 140      -5.183 -11.002  -3.079  1.00 41.18           C  
ANISOU  364  CE1 PHE A 140     4366   5858   5420   1093     37    170       C  
ATOM    365  CE2 PHE A 140      -2.986 -10.072  -2.912  1.00 40.31           C  
ANISOU  365  CE2 PHE A 140     4094   6065   5155   1292    390     67       C  
ATOM    366  CZ  PHE A 140      -4.355  -9.928  -2.812  1.00 40.37           C  
ANISOU  366  CZ  PHE A 140     4038   5882   5419   1127    270    157       C  
ATOM    367  N   VAL A 141      -3.074 -16.892  -3.698  1.00 47.10           N  
ANISOU  367  N   VAL A 141     6615   6458   4822   1767   -340   -380       N  
ATOM    368  CA  VAL A 141      -2.807 -18.160  -4.371  1.00 49.02           C  
ANISOU  368  CA  VAL A 141     7266   6565   4794   1927   -462   -516       C  
ATOM    369  C   VAL A 141      -3.753 -18.324  -5.556  1.00 50.20           C  
ANISOU  369  C   VAL A 141     7642   6579   4853   1783   -735   -516       C  
ATOM    370  O   VAL A 141      -4.960 -18.205  -5.403  1.00 50.24           O  
ANISOU  370  O   VAL A 141     7547   6432   5108   1525   -932   -422       O  
ATOM    371  CB  VAL A 141      -2.977 -19.371  -3.433  1.00 49.19           C  
ANISOU  371  CB  VAL A 141     7453   6354   4884   1944   -529   -566       C  
ATOM    372  CG1 VAL A 141      -2.459 -20.637  -4.111  1.00 52.31           C  
ANISOU  372  CG1 VAL A 141     8264   6587   5026   2169   -605   -737       C  
ATOM    373  CG2 VAL A 141      -2.263 -19.138  -2.112  1.00 47.50           C  
ANISOU  373  CG2 VAL A 141     7014   6277   4756   2034   -337   -525       C  
ATOM    374  N   SER A 142      -3.208 -18.609  -6.731  1.00 51.84           N  
ANISOU  374  N   SER A 142     8154   6844   4700   1952   -749   -625       N  
ATOM    375  CA  SER A 142      -4.008 -18.692  -7.948  1.00 54.64           C  
ANISOU  375  CA  SER A 142     8776   7115   4871   1825  -1047   -638       C  
ATOM    376  C   SER A 142      -4.037 -20.104  -8.528  1.00 55.94           C  
ANISOU  376  C   SER A 142     9446   7037   4769   1911  -1238   -885       C  
ATOM    377  O   SER A 142      -3.009 -20.779  -8.613  1.00 56.66           O  
ANISOU  377  O   SER A 142     9758   7132   4637   2195  -1033  -1057       O  
ATOM    378  CB  SER A 142      -3.478 -17.710  -8.994  1.00 55.33           C  
ANISOU  378  CB  SER A 142     8867   7476   4682   1916   -914   -547       C  
ATOM    379  OG  SER A 142      -3.552 -16.378  -8.515  1.00 53.46           O  
ANISOU  379  OG  SER A 142     8171   7396   4745   1808   -769   -319       O  
ATOM    380  N   PHE A 143      -5.229 -20.535  -8.926  1.00 57.57           N  
ANISOU  380  N   PHE A 143     9816   7012   5048   1663  -1641   -909       N  
ATOM    381  CA  PHE A 143      -5.436 -21.857  -9.501  1.00 62.11           C  
ANISOU  381  CA  PHE A 143    10886   7294   5418   1678  -1893  -1170       C  
ATOM    382  C   PHE A 143      -5.951 -21.765 -10.931  1.00 66.70           C  
ANISOU  382  C   PHE A 143    11811   7896   5637   1581  -2238  -1252       C  
ATOM    383  O   PHE A 143      -6.473 -20.723 -11.355  1.00 67.71           O  
ANISOU  383  O   PHE A 143    11734   8207   5785   1433  -2375  -1038       O  
ATOM    384  CB  PHE A 143      -6.424 -22.668  -8.659  1.00 60.51           C  
ANISOU  384  CB  PHE A 143    10614   6728   5647   1430  -2123  -1159       C  
ATOM    385  CG  PHE A 143      -6.038 -22.794  -7.213  1.00 58.17           C  
ANISOU  385  CG  PHE A 143    10039   6408   5654   1500  -1820  -1048       C  
ATOM    386  CD1 PHE A 143      -5.325 -23.893  -6.767  1.00 59.31           C  
ANISOU  386  CD1 PHE A 143    10432   6362   5742   1717  -1689  -1190       C  
ATOM    387  CD2 PHE A 143      -6.401 -21.821  -6.297  1.00 54.91           C  
ANISOU  387  CD2 PHE A 143     9143   6150   5571   1358  -1676   -802       C  
ATOM    388  CE1 PHE A 143      -4.974 -24.016  -5.434  1.00 57.43           C  
ANISOU  388  CE1 PHE A 143     9973   6116   5731   1784  -1459  -1055       C  
ATOM    389  CE2 PHE A 143      -6.053 -21.935  -4.965  1.00 52.97           C  
ANISOU  389  CE2 PHE A 143     8704   5902   5520   1416  -1418   -714       C  
ATOM    390  CZ  PHE A 143      -5.338 -23.035  -4.531  1.00 54.07           C  
ANISOU  390  CZ  PHE A 143     9104   5879   5561   1625  -1330   -823       C  
ATOM    391  N   PHE A 144      -5.806 -22.873 -11.656  1.00 72.34           N  
ANISOU  391  N   PHE A 144    13069   8401   6016   1671  -2393  -1565       N  
ATOM    392  CA  PHE A 144      -6.330 -23.019 -13.010  1.00 78.56           C  
ANISOU  392  CA  PHE A 144    14303   9162   6383   1567  -2792  -1715       C  
ATOM    393  C   PHE A 144      -7.806 -23.401 -12.979  1.00 82.84           C  
ANISOU  393  C   PHE A 144    14794   9404   7279   1167  -3376  -1698       C  
ATOM    394  O   PHE A 144      -8.594 -22.963 -13.820  1.00 85.40           O  
ANISOU  394  O   PHE A 144    15185   9792   7471    965  -3804  -1630       O  
ATOM    395  CB  PHE A 144      -5.550 -24.087 -13.782  1.00 81.65           C  
ANISOU  395  CB  PHE A 144    15288   9425   6310   1821  -2670  -2091       C  
ATOM    396  CG  PHE A 144      -4.071 -23.842 -13.843  1.00 79.75           C  
ANISOU  396  CG  PHE A 144    14994   9449   5859   2202  -2045  -2084       C  
ATOM    397  CD1 PHE A 144      -3.512 -23.169 -14.916  1.00 81.28           C  
ANISOU  397  CD1 PHE A 144    15262   9958   5664   2299  -1813  -2007       C  
ATOM    398  CD2 PHE A 144      -3.238 -24.294 -12.832  1.00 76.86           C  
ANISOU  398  CD2 PHE A 144    14478   9004   5723   2449  -1699  -2131       C  
ATOM    399  CE1 PHE A 144      -2.150 -22.945 -14.977  1.00 80.44           C  
ANISOU  399  CE1 PHE A 144    15045  10071   5449   2612  -1240  -1984       C  
ATOM    400  CE2 PHE A 144      -1.875 -24.073 -12.886  1.00 75.99           C  
ANISOU  400  CE2 PHE A 144    14225   9131   5519   2773  -1165  -2096       C  
ATOM    401  CZ  PHE A 144      -1.330 -23.398 -13.961  1.00 77.84           C  
ANISOU  401  CZ  PHE A 144    14501   9664   5411   2842   -930  -2029       C  
ATOM    402  N   ASN A 145      -8.162 -24.242 -12.012  1.00 84.23           N  
ANISOU  402  N   ASN A 145    14847   9242   7915   1054  -3400  -1742       N  
ATOM    403  CA  ASN A 145      -9.536 -24.697 -11.847  1.00 88.55           C  
ANISOU  403  CA  ASN A 145    15276   9459   8909    658  -3892  -1714       C  
ATOM    404  C   ASN A 145     -10.289 -23.804 -10.871  1.00 84.96           C  
ANISOU  404  C   ASN A 145    14136   9091   9054    442  -3829  -1332       C  
ATOM    405  O   ASN A 145      -9.789 -23.489  -9.790  1.00 80.73           O  
ANISOU  405  O   ASN A 145    13285   8656   8734    567  -3382  -1178       O  
ATOM    406  CB  ASN A 145      -9.562 -26.152 -11.362  1.00 92.37           C  
ANISOU  406  CB  ASN A 145    16025   9477   9595    630  -3927  -1951       C  
ATOM    407  CG  ASN A 145     -10.962 -26.752 -11.356  1.00 96.37           C  
ANISOU  407  CG  ASN A 145    16460   9592  10563    192  -4464  -1962       C  
ATOM    408  OD1 ASN A 145     -11.960 -26.046 -11.498  1.00 97.26           O  
ANISOU  408  OD1 ASN A 145    16209   9792  10953    -91  -4780  -1748       O  
ATOM    409  ND2 ASN A 145     -11.036 -28.068 -11.186  1.00 99.33           N  
ANISOU  409  ND2 ASN A 145    17157   9506  11077    136  -4569  -2202       N  
ATOM    410  N   LYS A 146     -11.492 -23.396 -11.267  1.00 86.72           N  
ANISOU  410  N   LYS A 146    14135   9271   9542    126  -4289  -1191       N  
ATOM    411  CA  LYS A 146     -12.386 -22.658 -10.385  1.00 84.37           C  
ANISOU  411  CA  LYS A 146    13179   8981   9895    -99  -4251   -857       C  
ATOM    412  C   LYS A 146     -12.700 -23.482  -9.145  1.00 83.05           C  
ANISOU  412  C   LYS A 146    12832   8495  10227   -226  -4059   -839       C  
ATOM    413  O   LYS A 146     -12.748 -22.958  -8.027  1.00 80.05           O  
ANISOU  413  O   LYS A 146    12018   8195  10203   -227  -3677   -615       O  
ATOM    414  CB  LYS A 146     -13.680 -22.293 -11.111  1.00 88.42           C  
ANISOU  414  CB  LYS A 146    13495   9436  10666   -415  -4853   -732       C  
ATOM    415  CG  LYS A 146     -14.729 -21.657 -10.216  1.00 88.03           C  
ANISOU  415  CG  LYS A 146    12734   9326  11387   -653  -4812   -407       C  
ATOM    416  CD  LYS A 146     -15.273 -20.382 -10.829  1.00 89.64           C  
ANISOU  416  CD  LYS A 146    12608   9763  11688   -700  -5056   -140       C  
ATOM    417  CE  LYS A 146     -16.277 -19.711  -9.911  1.00 89.15           C  
ANISOU  417  CE  LYS A 146    11810   9625  12437   -890  -4940    166       C  
ATOM    418  NZ  LYS A 146     -16.102 -18.232  -9.917  1.00 86.76           N  
ANISOU  418  NZ  LYS A 146    11171   9617  12179   -736  -4714    431       N  
ATOM    419  N   TRP A 147     -12.904 -24.779  -9.351  1.00 86.35           N  
ANISOU  419  N   TRP A 147    13621   8539  10649   -334  -4315  -1078       N  
ATOM    420  CA  TRP A 147     -13.225 -25.663  -8.247  1.00 85.20           C  
ANISOU  420  CA  TRP A 147    13361   8042  10970   -472  -4150  -1032       C  
ATOM    421  C   TRP A 147     -12.101 -25.686  -7.230  1.00 79.61           C  
ANISOU  421  C   TRP A 147    12672   7461  10114   -154  -3556   -981       C  
ATOM    422  O   TRP A 147     -12.357 -25.695  -6.035  1.00 77.59           O  
ANISOU  422  O   TRP A 147    12104   7133  10243   -235  -3265   -769       O  
ATOM    423  CB  TRP A 147     -13.507 -27.089  -8.722  1.00 91.47           C  
ANISOU  423  CB  TRP A 147    14614   8366  11776   -621  -4523  -1323       C  
ATOM    424  CG  TRP A 147     -14.088 -27.905  -7.618  1.00 92.90           C  
ANISOU  424  CG  TRP A 147    14601   8148  12547   -845  -4397  -1190       C  
ATOM    425  CD1 TRP A 147     -15.412 -28.141  -7.386  1.00 96.22           C  
ANISOU  425  CD1 TRP A 147    14668   8277  13614  -1274  -4678  -1044       C  
ATOM    426  CD2 TRP A 147     -13.372 -28.568  -6.572  1.00 91.60           C  
ANISOU  426  CD2 TRP A 147    14562   7837  12404   -654  -3941  -1144       C  
ATOM    427  NE1 TRP A 147     -15.565 -28.909  -6.257  1.00 96.73           N  
ANISOU  427  NE1 TRP A 147    14649   8019  14083  -1372  -4374   -903       N  
ATOM    428  CE2 TRP A 147     -14.324 -29.192  -5.739  1.00 93.87           C  
ANISOU  428  CE2 TRP A 147    14605   7740  13321   -989  -3941   -954       C  
ATOM    429  CE3 TRP A 147     -12.016 -28.687  -6.243  1.00 88.73           C  
ANISOU  429  CE3 TRP A 147    14469   7631  11611   -228  -3539  -1216       C  
ATOM    430  CZ2 TRP A 147     -13.969 -29.924  -4.610  1.00 93.82           C  
ANISOU  430  CZ2 TRP A 147    14676   7506  13464   -911  -3556   -818       C  
ATOM    431  CZ3 TRP A 147     -11.662 -29.421  -5.133  1.00 88.76           C  
ANISOU  431  CZ3 TRP A 147    14525   7411  11789   -141  -3215  -1096       C  
ATOM    432  CH2 TRP A 147     -12.634 -30.037  -4.331  1.00 91.23           C  
ANISOU  432  CH2 TRP A 147    14651   7342  12670   -479  -3227   -891       C  
ATOM    433  N   ASP A 148     -10.861 -25.717  -7.703  1.00 76.99           N  
ANISOU  433  N   ASP A 148    12710   7320   9225    208  -3379  -1171       N  
ATOM    434  CA  ASP A 148      -9.717 -25.789  -6.804  1.00 72.51           C  
ANISOU  434  CA  ASP A 148    12152   6873   8524    527  -2883  -1133       C  
ATOM    435  C   ASP A 148      -9.676 -24.574  -5.884  1.00 68.37           C  
ANISOU  435  C   ASP A 148    11107   6684   8188    535  -2546   -843       C  
ATOM    436  O   ASP A 148      -9.404 -24.697  -4.691  1.00 65.84           O  
ANISOU  436  O   ASP A 148    10638   6350   8028    593  -2231   -711       O  
ATOM    437  CB  ASP A 148      -8.415 -25.898  -7.599  1.00 71.75           C  
ANISOU  437  CB  ASP A 148    12459   6954   7848    916  -2749  -1378       C  
ATOM    438  CG  ASP A 148      -8.276 -27.233  -8.310  1.00 75.75           C  
ANISOU  438  CG  ASP A 148    13539   7081   8160    978  -2974  -1716       C  
ATOM    439  OD1 ASP A 148      -9.081 -28.148  -8.032  1.00 77.71           O  
ANISOU  439  OD1 ASP A 148    13869   6899   8757    726  -3215  -1747       O  
ATOM    440  OD2 ASP A 148      -7.364 -27.365  -9.152  1.00 76.51           O  
ANISOU  440  OD2 ASP A 148    14007   7292   7773   1274  -2885  -1958       O  
ATOM    441  N   ALA A 149      -9.962 -23.404  -6.443  1.00 67.95           N  
ANISOU  441  N   ALA A 149    10804   6911   8102    474  -2626   -746       N  
ATOM    442  CA  ALA A 149      -9.961 -22.171  -5.668  1.00 65.85           C  
ANISOU  442  CA  ALA A 149    10057   6926   8036    474  -2320   -509       C  
ATOM    443  C   ALA A 149     -11.127 -22.137  -4.684  1.00 66.36           C  
ANISOU  443  C   ALA A 149     9732   6804   8678    176  -2287   -305       C  
ATOM    444  O   ALA A 149     -10.940 -21.836  -3.501  1.00 63.96           O  
ANISOU  444  O   ALA A 149     9203   6579   8519    213  -1914   -180       O  
ATOM    445  CB  ALA A 149     -10.009 -20.964  -6.593  1.00 65.24           C  
ANISOU  445  CB  ALA A 149     9835   7133   7819    487  -2430   -438       C  
ATOM    446  N   GLU A 150     -12.324 -22.457  -5.170  1.00 72.20           N  
ANISOU  446  N   GLU A 150    10394   7298   9742   -124  -2674   -277       N  
ATOM    447  CA  GLU A 150     -13.515 -22.423  -4.326  1.00 75.60           C  
ANISOU  447  CA  GLU A 150    10397   7536  10790   -423  -2621    -68       C  
ATOM    448  C   GLU A 150     -13.373 -23.414  -3.173  1.00 72.14           C  
ANISOU  448  C   GLU A 150    10079   6865  10465   -437  -2334    -39       C  
ATOM    449  O   GLU A 150     -13.799 -23.147  -2.052  1.00 71.05           O  
ANISOU  449  O   GLU A 150     9626   6720  10649   -537  -1996    155       O  
ATOM    450  CB  GLU A 150     -14.778 -22.723  -5.145  1.00 86.10           C  
ANISOU  450  CB  GLU A 150    11614   8616  12485   -751  -3155    -56       C  
ATOM    451  CG  GLU A 150     -15.060 -24.201  -5.382  1.00 94.77           C  
ANISOU  451  CG  GLU A 150    13069   9299  13641   -914  -3454   -223       C  
ATOM    452  CD  GLU A 150     -16.135 -24.434  -6.417  1.00103.20           C  
ANISOU  452  CD  GLU A 150    14087  10163  14963  -1221  -4091   -276       C  
ATOM    453  OE1 GLU A 150     -16.672 -23.446  -6.957  1.00105.65           O  
ANISOU  453  OE1 GLU A 150    14073  10669  15399  -1289  -4314   -148       O  
ATOM    454  OE2 GLU A 150     -16.458 -25.607  -6.680  1.00110.65           O  
ANISOU  454  OE2 GLU A 150    15306  10729  16008  -1402  -4395   -439       O  
ATOM    455  N   ASN A 151     -12.747 -24.548  -3.455  1.00 70.84           N  
ANISOU  455  N   ASN A 151    10398   6504  10013   -317  -2446   -228       N  
ATOM    456  CA  ASN A 151     -12.533 -25.570  -2.453  1.00 68.97           C  
ANISOU  456  CA  ASN A 151    10340   6011   9856   -299  -2216   -175       C  
ATOM    457  C   ASN A 151     -11.492 -25.128  -1.451  1.00 64.98           C  
ANISOU  457  C   ASN A 151     9817   5797   9076     -9  -1761    -93       C  
ATOM    458  O   ASN A 151     -11.656 -25.316  -0.247  1.00 64.54           O  
ANISOU  458  O   ASN A 151     9660   5675   9186    -65  -1460     96       O  
ATOM    459  CB  ASN A 151     -12.085 -26.871  -3.091  1.00 70.63           C  
ANISOU  459  CB  ASN A 151    11083   5900   9854   -210  -2468   -415       C  
ATOM    460  CG  ASN A 151     -12.092 -28.023  -2.113  1.00 71.36           C  
ANISOU  460  CG  ASN A 151    11348   5622  10144   -249  -2295   -308       C  
ATOM    461  OD1 ASN A 151     -13.057 -28.215  -1.374  1.00 72.68           O  
ANISOU  461  OD1 ASN A 151    11260   5579  10775   -548  -2206    -81       O  
ATOM    462  ND2 ASN A 151     -11.009 -28.793  -2.095  1.00 71.03           N  
ANISOU  462  ND2 ASN A 151    11730   5486   9773     65  -2222   -445       N  
ATOM    463  N   ALA A 152     -10.411 -24.551  -1.968  1.00 61.98           N  
ANISOU  463  N   ALA A 152     9546   5737   8264    292  -1721   -234       N  
ATOM    464  CA  ALA A 152      -9.308 -24.091  -1.139  1.00 59.11           C  
ANISOU  464  CA  ALA A 152     9150   5669   7638    573  -1364   -192       C  
ATOM    465  C   ALA A 152      -9.785 -23.052  -0.140  1.00 58.02           C  
ANISOU  465  C   ALA A 152     8589   5729   7726    441  -1076      4       C  
ATOM    466  O   ALA A 152      -9.382 -23.074   1.022  1.00 57.02           O  
ANISOU  466  O   ALA A 152     8454   5681   7531    524   -789    103       O  
ATOM    467  CB  ALA A 152      -8.196 -23.524  -2.002  1.00 57.29           C  
ANISOU  467  CB  ALA A 152     9018   5744   7004    864  -1375   -362       C  
ATOM    468  N   ILE A 153     -10.649 -22.149  -0.596  1.00 58.94           N  
ANISOU  468  N   ILE A 153     8373   5916   8105    245  -1163     56       N  
ATOM    469  CA  ILE A 153     -11.209 -21.125   0.281  1.00 58.54           C  
ANISOU  469  CA  ILE A 153     7906   6006   8331    122   -867    213       C  
ATOM    470  C   ILE A 153     -11.932 -21.746   1.473  1.00 63.64           C  
ANISOU  470  C   ILE A 153     8498   6429   9254    -63   -632    380       C  
ATOM    471  O   ILE A 153     -11.812 -21.264   2.599  1.00 62.87           O  
ANISOU  471  O   ILE A 153     8282   6477   9131    -34   -261    464       O  
ATOM    472  CB  ILE A 153     -12.185 -20.207  -0.477  1.00 57.53           C  
ANISOU  472  CB  ILE A 153     7410   5898   8549    -63  -1044    273       C  
ATOM    473  CG1 ILE A 153     -11.436 -19.392  -1.530  1.00 54.52           C  
ANISOU  473  CG1 ILE A 153     7074   5780   7863    125  -1193    170       C  
ATOM    474  CG2 ILE A 153     -12.905 -19.272   0.484  1.00 56.20           C  
ANISOU  474  CG2 ILE A 153     6801   5790   8762   -192   -698    424       C  
ATOM    475  CD1 ILE A 153     -12.341 -18.559  -2.392  1.00 55.25           C  
ANISOU  475  CD1 ILE A 153     6864   5877   8251    -29  -1441    265       C  
ATOM    476  N   GLN A 154     -12.660 -22.830   1.226  1.00 69.87           N  
ANISOU  476  N   GLN A 154     9404   6855  10288   -261   -840    424       N  
ATOM    477  CA  GLN A 154     -13.469 -23.451   2.269  1.00 75.23           C  
ANISOU  477  CA  GLN A 154    10008   7280  11295   -482   -599    629       C  
ATOM    478  C   GLN A 154     -12.675 -24.379   3.183  1.00 74.51           C  
ANISOU  478  C   GLN A 154    10310   7113  10889   -321   -405    687       C  
ATOM    479  O   GLN A 154     -12.976 -24.492   4.372  1.00 75.25           O  
ANISOU  479  O   GLN A 154    10364   7174  11055   -402    -45    885       O  
ATOM    480  CB  GLN A 154     -14.633 -24.223   1.647  1.00 83.34           C  
ANISOU  480  CB  GLN A 154    10950   7910  12807   -805   -914    676       C  
ATOM    481  CG  GLN A 154     -15.986 -23.632   1.991  1.00 87.92           C  
ANISOU  481  CG  GLN A 154    10988   8423  13994  -1106   -759    866       C  
ATOM    482  CD  GLN A 154     -16.187 -23.482   3.489  1.00 90.80           C  
ANISOU  482  CD  GLN A 154    11233   8831  14437  -1139   -167   1071       C  
ATOM    483  OE1 GLN A 154     -15.862 -24.382   4.266  1.00 93.35           O  
ANISOU  483  OE1 GLN A 154    11873   9011  14585  -1115     25   1170       O  
ATOM    484  NE2 GLN A 154     -16.706 -22.331   3.903  1.00 91.04           N  
ANISOU  484  NE2 GLN A 154    10834   9053  14704  -1177    135   1138       N  
ATOM    485  N   GLN A 155     -11.665 -25.046   2.637  1.00 72.65           N  
ANISOU  485  N   GLN A 155    10460   6845  10300    -78   -629    530       N  
ATOM    486  CA  GLN A 155     -10.888 -25.990   3.430  1.00 72.92           C  
ANISOU  486  CA  GLN A 155    10861   6769  10078    108   -505    610       C  
ATOM    487  C   GLN A 155      -9.751 -25.317   4.198  1.00 68.02           C  
ANISOU  487  C   GLN A 155    10264   6551   9031    404   -273    606       C  
ATOM    488  O   GLN A 155      -9.315 -25.825   5.228  1.00 69.14           O  
ANISOU  488  O   GLN A 155    10609   6671   8990    510   -101    760       O  
ATOM    489  CB  GLN A 155     -10.321 -27.097   2.543  1.00 75.15           C  
ANISOU  489  CB  GLN A 155    11539   6777  10237    259   -831    438       C  
ATOM    490  CG  GLN A 155     -11.342 -27.822   1.681  1.00 79.18           C  
ANISOU  490  CG  GLN A 155    12088   6867  11129    -36  -1148    373       C  
ATOM    491  CD  GLN A 155     -12.284 -28.689   2.491  1.00 83.06           C  
ANISOU  491  CD  GLN A 155    12574   6949  12035   -334  -1026    631       C  
ATOM    492  OE1 GLN A 155     -13.285 -28.208   3.023  1.00 83.73           O  
ANISOU  492  OE1 GLN A 155    12293   7052  12468   -614   -830    824       O  
ATOM    493  NE2 GLN A 155     -11.969 -29.976   2.588  1.00 86.28           N  
ANISOU  493  NE2 GLN A 155    13380   6962  12442   -270  -1109    647       N  
ATOM    494  N   MET A 156      -9.268 -24.182   3.703  1.00 63.60           N  
ANISOU  494  N   MET A 156     9500   6344   8320    526   -292    445       N  
ATOM    495  CA  MET A 156      -8.159 -23.494   4.360  1.00 59.85           C  
ANISOU  495  CA  MET A 156     9010   6241   7490    779   -122    409       C  
ATOM    496  C   MET A 156      -8.634 -22.391   5.299  1.00 58.95           C  
ANISOU  496  C   MET A 156     8602   6349   7446    638    192    486       C  
ATOM    497  O   MET A 156      -7.875 -21.926   6.150  1.00 58.73           O  
ANISOU  497  O   MET A 156     8598   6584   7132    785    350    475       O  
ATOM    498  CB  MET A 156      -7.194 -22.907   3.330  1.00 56.71           C  
ANISOU  498  CB  MET A 156     8572   6086   6888   1009   -282    190       C  
ATOM    499  CG  MET A 156      -6.309 -23.932   2.655  1.00 57.15           C  
ANISOU  499  CG  MET A 156     8962   6004   6747   1267   -486     77       C  
ATOM    500  SD  MET A 156      -5.516 -25.055   3.822  1.00 68.75           S  
ANISOU  500  SD  MET A 156    10742   7352   8029   1492   -421    225       S  
ATOM    501  CE  MET A 156      -3.983 -24.191   4.155  1.00 56.57           C  
ANISOU  501  CE  MET A 156     9052   6280   6163   1823   -350    136       C  
ATOM    502  N   GLY A 157      -9.884 -21.968   5.137  1.00 58.19           N  
ANISOU  502  N   GLY A 157     8226   6139   7746    358    271    546       N  
ATOM    503  CA  GLY A 157     -10.451 -20.951   6.004  1.00 57.46           C  
ANISOU  503  CA  GLY A 157     7849   6202   7783    229    622    601       C  
ATOM    504  C   GLY A 157     -10.413 -21.370   7.461  1.00 59.55           C  
ANISOU  504  C   GLY A 157     8316   6470   7839    222    940    755       C  
ATOM    505  O   GLY A 157     -10.907 -22.437   7.821  1.00 62.32           O  
ANISOU  505  O   GLY A 157     8850   6543   8287    108    985    947       O  
ATOM    506  N   GLY A 158      -9.803 -20.537   8.298  1.00 58.97           N  
ANISOU  506  N   GLY A 158     8238   6705   7463    337   1148    676       N  
ATOM    507  CA  GLY A 158      -9.711 -20.816   9.719  1.00 61.92           C  
ANISOU  507  CA  GLY A 158     8853   7141   7532    341   1438    810       C  
ATOM    508  C   GLY A 158      -8.687 -21.878  10.078  1.00 62.81           C  
ANISOU  508  C   GLY A 158     9384   7244   7238    558   1239    906       C  
ATOM    509  O   GLY A 158      -8.535 -22.219  11.250  1.00 65.59           O  
ANISOU  509  O   GLY A 158    10000   7648   7272    582   1420   1061       O  
ATOM    510  N   GLN A 159      -7.985 -22.403   9.078  1.00 61.79           N  
ANISOU  510  N   GLN A 159     9327   7043   7108    730    875    824       N  
ATOM    511  CA  GLN A 159      -6.977 -23.432   9.313  1.00 62.77           C  
ANISOU  511  CA  GLN A 159     9805   7117   6927    981    671    911       C  
ATOM    512  C   GLN A 159      -5.661 -22.807   9.761  1.00 61.07           C  
ANISOU  512  C   GLN A 159     9602   7287   6315   1240    583    782       C  
ATOM    513  O   GLN A 159      -5.316 -21.702   9.347  1.00 58.62           O  
ANISOU  513  O   GLN A 159     9019   7229   6026   1265    568    562       O  
ATOM    514  CB  GLN A 159      -6.760 -24.280   8.056  1.00 64.05           C  
ANISOU  514  CB  GLN A 159    10051   7017   7270   1081    360    842       C  
ATOM    515  CG  GLN A 159      -6.834 -25.778   8.305  1.00 68.79           C  
ANISOU  515  CG  GLN A 159    11011   7231   7895   1114    282   1059       C  
ATOM    516  CD  GLN A 159      -8.189 -26.215   8.832  1.00 72.73           C  
ANISOU  516  CD  GLN A 159    11523   7433   8679    774    517   1298       C  
ATOM    517  OE1 GLN A 159      -9.228 -25.830   8.294  1.00 72.64           O  
ANISOU  517  OE1 GLN A 159    11239   7321   9041    507    574   1245       O  
ATOM    518  NE2 GLN A 159      -8.185 -27.018   9.892  1.00 76.65           N  
ANISOU  518  NE2 GLN A 159    12319   7785   9020    783    657   1591       N  
ATOM    519  N   TRP A 160      -4.933 -23.518  10.614  1.00 62.95           N  
ANISOU  519  N   TRP A 160    10144   7552   6221   1424    504    941       N  
ATOM    520  CA  TRP A 160      -3.693 -22.998  11.176  1.00 62.58           C  
ANISOU  520  CA  TRP A 160    10100   7868   5810   1653    368    845       C  
ATOM    521  C   TRP A 160      -2.527 -23.116  10.202  1.00 61.63           C  
ANISOU  521  C   TRP A 160     9865   7813   5739   1941     66    688       C  
ATOM    522  O   TRP A 160      -2.308 -24.165   9.592  1.00 63.05           O  
ANISOU  522  O   TRP A 160    10198   7728   6031   2094    -88    758       O  
ATOM    523  CB  TRP A 160      -3.343 -23.722  12.474  1.00 65.89           C  
ANISOU  523  CB  TRP A 160    10891   8306   5839   1755    346   1109       C  
ATOM    524  CG  TRP A 160      -4.295 -23.489  13.614  1.00 67.80           C  
ANISOU  524  CG  TRP A 160    11287   8571   5904   1506    701   1258       C  
ATOM    525  CD1 TRP A 160      -5.390 -24.240  13.934  1.00 69.04           C  
ANISOU  525  CD1 TRP A 160    11625   8413   6192   1305    961   1527       C  
ATOM    526  CD2 TRP A 160      -4.229 -22.442  14.592  1.00 67.02           C  
ANISOU  526  CD2 TRP A 160    11182   8817   5466   1429    870   1135       C  
ATOM    527  NE1 TRP A 160      -6.006 -23.728  15.052  1.00 70.51           N  
ANISOU  527  NE1 TRP A 160    11916   8746   6129   1124   1327   1599       N  
ATOM    528  CE2 TRP A 160      -5.312 -22.622  15.477  1.00 69.85           C  
ANISOU  528  CE2 TRP A 160    11747   9066   5728   1203   1273   1340       C  
ATOM    529  CE3 TRP A 160      -3.355 -21.368  14.810  1.00 66.14           C  
ANISOU  529  CE3 TRP A 160    10915   9079   5138   1518    728    857       C  
ATOM    530  CZ2 TRP A 160      -5.551 -21.771  16.560  1.00 70.72           C  
ANISOU  530  CZ2 TRP A 160    11953   9436   5480   1089   1562   1251       C  
ATOM    531  CZ3 TRP A 160      -3.593 -20.522  15.892  1.00 67.93           C  
ANISOU  531  CZ3 TRP A 160    11239   9543   5028   1384    961    753       C  
ATOM    532  CH2 TRP A 160      -4.682 -20.729  16.750  1.00 69.34           C  
ANISOU  532  CH2 TRP A 160    11664   9615   5066   1184   1385    938       C  
ATOM    533  N   LEU A 161      -1.778 -22.030  10.065  1.00 59.11           N  
ANISOU  533  N   LEU A 161     9274   7827   5357   2010     12    468       N  
ATOM    534  CA  LEU A 161      -0.583 -22.024   9.239  1.00 58.31           C  
ANISOU  534  CA  LEU A 161     9017   7836   5303   2286   -210    332       C  
ATOM    535  C   LEU A 161       0.513 -21.265   9.966  1.00 59.79           C  
ANISOU  535  C   LEU A 161     9050   8397   5270   2406   -332    238       C  
ATOM    536  O   LEU A 161       0.390 -20.066  10.212  1.00 59.79           O  
ANISOU  536  O   LEU A 161     8840   8615   5264   2235   -222     76       O  
ATOM    537  CB  LEU A 161      -0.867 -21.400   7.876  1.00 53.65           C  
ANISOU  537  CB  LEU A 161     8167   7224   4995   2204   -148    142       C  
ATOM    538  CG  LEU A 161       0.196 -21.648   6.809  1.00 53.04           C  
ANISOU  538  CG  LEU A 161     7995   7177   4980   2489   -296     29       C  
ATOM    539  CD1 LEU A 161       0.515 -23.135   6.721  1.00 55.48           C  
ANISOU  539  CD1 LEU A 161     8613   7207   5262   2728   -435    154       C  
ATOM    540  CD2 LEU A 161      -0.275 -21.113   5.465  1.00 49.80           C  
ANISOU  540  CD2 LEU A 161     7427   6721   4774   2376   -219   -112       C  
ATOM    541  N   GLY A 162       1.586 -21.965  10.308  1.00 63.38           N  
ANISOU  541  N   GLY A 162     9597   8903   5581   2700   -581    337       N  
ATOM    542  CA  GLY A 162       2.569 -21.416  11.219  1.00 65.38           C  
ANISOU  542  CA  GLY A 162     9747   9493   5602   2795   -776    293       C  
ATOM    543  C   GLY A 162       1.975 -21.511  12.608  1.00 69.16           C  
ANISOU  543  C   GLY A 162    10556  10009   5714   2638   -724    450       C  
ATOM    544  O   GLY A 162       1.429 -22.550  12.980  1.00 70.92           O  
ANISOU  544  O   GLY A 162    11125   9983   5837   2650   -680    713       O  
ATOM    545  N   GLY A 163       2.060 -20.431  13.375  1.00 69.84           N  
ANISOU  545  N   GLY A 163    10559  10383   5593   2482   -705    285       N  
ATOM    546  CA  GLY A 163       1.473 -20.415  14.701  1.00 74.15           C  
ANISOU  546  CA  GLY A 163    11456  10994   5722   2325   -597    393       C  
ATOM    547  C   GLY A 163       0.208 -19.581  14.759  1.00 73.30           C  
ANISOU  547  C   GLY A 163    11318  10834   5697   1996   -168    255       C  
ATOM    548  O   GLY A 163      -0.236 -19.193  15.838  1.00 75.89           O  
ANISOU  548  O   GLY A 163    11871  11279   5684   1842     -1    237       O  
ATOM    549  N   ARG A 164      -0.377 -19.311  13.595  1.00 71.06           N  
ANISOU  549  N   ARG A 164    10765  10374   5862   1901     12    161       N  
ATOM    550  CA  ARG A 164      -1.529 -18.418  13.514  1.00 70.86           C  
ANISOU  550  CA  ARG A 164    10609  10289   6027   1618    388     27       C  
ATOM    551  C   ARG A 164      -2.619 -18.921  12.568  1.00 66.96           C  
ANISOU  551  C   ARG A 164    10050   9461   5929   1508    574    151       C  
ATOM    552  O   ARG A 164      -2.339 -19.557  11.551  1.00 64.69           O  
ANISOU  552  O   ARG A 164     9701   9026   5852   1640    396    203       O  
ATOM    553  CB  ARG A 164      -1.074 -17.021  13.086  1.00 72.86           C  
ANISOU  553  CB  ARG A 164    10481  10736   6466   1564    372   -296       C  
ATOM    554  CG  ARG A 164      -0.444 -16.213  14.213  1.00 79.41           C  
ANISOU  554  CG  ARG A 164    11373  11858   6943   1533    289   -495       C  
ATOM    555  CD  ARG A 164       0.310 -15.003  13.685  1.00 81.17           C  
ANISOU  555  CD  ARG A 164    11194  12238   7409   1515    176   -790       C  
ATOM    556  NE  ARG A 164      -0.482 -14.229  12.732  1.00 80.33           N  
ANISOU  556  NE  ARG A 164    10795  11968   7757   1365    452   -884       N  
ATOM    557  CZ  ARG A 164      -0.561 -12.901  12.732  1.00 81.30           C  
ANISOU  557  CZ  ARG A 164    10681  12139   8069   1214    589  -1143       C  
ATOM    558  NH1 ARG A 164       0.094 -12.195  13.646  1.00 85.16           N  
ANISOU  558  NH1 ARG A 164    11204  12831   8321   1168    480  -1379       N  
ATOM    559  NH2 ARG A 164      -1.305 -12.279  11.827  1.00 78.24           N  
ANISOU  559  NH2 ARG A 164    10036  11578   8114   1105    811  -1164       N  
ATOM    560  N   GLN A 165      -3.866 -18.626  12.924  1.00 65.29           N  
ANISOU  560  N   GLN A 165     9851   9132   5825   1266    935    183       N  
ATOM    561  CA  GLN A 165      -5.023 -19.014  12.126  1.00 62.26           C  
ANISOU  561  CA  GLN A 165     9357   8435   5864   1112   1094    300       C  
ATOM    562  C   GLN A 165      -5.231 -18.079  10.943  1.00 57.53           C  
ANISOU  562  C   GLN A 165     8354   7829   5674   1050   1079    106       C  
ATOM    563  O   GLN A 165      -5.392 -16.872  11.121  1.00 56.04           O  
ANISOU  563  O   GLN A 165     7949   7774   5570    955   1248    -79       O  
ATOM    564  CB  GLN A 165      -6.284 -19.029  12.992  1.00 64.61           C  
ANISOU  564  CB  GLN A 165     9755   8610   6183    879   1514    432       C  
ATOM    565  CG  GLN A 165      -6.743 -20.411  13.398  1.00 67.77           C  
ANISOU  565  CG  GLN A 165    10480   8759   6512    850   1567    768       C  
ATOM    566  CD  GLN A 165      -8.064 -20.391  14.138  1.00 70.50           C  
ANISOU  566  CD  GLN A 165    10856   8967   6966    595   2052    918       C  
ATOM    567  OE1 GLN A 165      -8.419 -19.394  14.765  1.00 71.31           O  
ANISOU  567  OE1 GLN A 165    10869   9234   6993    499   2372    766       O  
ATOM    568  NE2 GLN A 165      -8.801 -21.495  14.070  1.00 72.95           N  
ANISOU  568  NE2 GLN A 165    11284   8950   7484    483   2136   1211       N  
ATOM    569  N   ILE A 166      -5.240 -18.638   9.738  1.00 53.77           N  
ANISOU  569  N   ILE A 166     7811   7180   5440   1106    878    150       N  
ATOM    570  CA  ILE A 166      -5.446 -17.836   8.539  1.00 50.40           C  
ANISOU  570  CA  ILE A 166     7057   6745   5348   1056    832     18       C  
ATOM    571  C   ILE A 166      -6.921 -17.746   8.181  1.00 50.21           C  
ANISOU  571  C   ILE A 166     6871   6480   5728    811   1000    107       C  
ATOM    572  O   ILE A 166      -7.727 -18.579   8.596  1.00 52.71           O  
ANISOU  572  O   ILE A 166     7331   6582   6116    690   1108    283       O  
ATOM    573  CB  ILE A 166      -4.676 -18.404   7.328  1.00 49.41           C  
ANISOU  573  CB  ILE A 166     6962   6585   5228   1249    530     -8       C  
ATOM    574  CG1 ILE A 166      -5.359 -19.666   6.795  1.00 49.64           C  
ANISOU  574  CG1 ILE A 166     7189   6283   5388   1204    427    140       C  
ATOM    575  CG2 ILE A 166      -3.226 -18.675   7.697  1.00 48.70           C  
ANISOU  575  CG2 ILE A 166     6991   6698   4815   1516    363    -56       C  
ATOM    576  CD1 ILE A 166      -4.675 -20.265   5.582  1.00 49.66           C  
ANISOU  576  CD1 ILE A 166     7282   6220   5367   1399    167     70       C  
ATOM    577  N   ARG A 167      -7.275 -16.721   7.417  1.00 47.83           N  
ANISOU  577  N   ARG A 167     6247   6201   5727    735   1019      8       N  
ATOM    578  CA  ARG A 167      -8.624 -16.627   6.878  1.00 48.54           C  
ANISOU  578  CA  ARG A 167     6117   6060   6265    528   1085    107       C  
ATOM    579  C   ARG A 167      -8.514 -16.659   5.365  1.00 46.10           C  
ANISOU  579  C   ARG A 167     5722   5695   6098    573    762     89       C  
ATOM    580  O   ARG A 167      -7.483 -16.285   4.817  1.00 45.36           O  
ANISOU  580  O   ARG A 167     5638   5781   5815    742    624    -22       O  
ATOM    581  CB  ARG A 167      -9.323 -15.354   7.355  1.00 49.34           C  
ANISOU  581  CB  ARG A 167     5908   6200   6639    397   1403     42       C  
ATOM    582  CG  ARG A 167      -8.669 -14.080   6.863  1.00 48.35           C  
ANISOU  582  CG  ARG A 167     5567   6251   6554    481   1354   -128       C  
ATOM    583  CD  ARG A 167      -8.926 -12.914   7.804  1.00 50.94           C  
ANISOU  583  CD  ARG A 167     5730   6645   6978    414   1711   -266       C  
ATOM    584  NE  ARG A 167      -8.397 -11.675   7.245  1.00 50.58           N  
ANISOU  584  NE  ARG A 167     5450   6696   7074    465   1660   -406       N  
ATOM    585  CZ  ARG A 167      -9.136 -10.770   6.613  1.00 51.68           C  
ANISOU  585  CZ  ARG A 167     5255   6702   7680    390   1722   -372       C  
ATOM    586  NH1 ARG A 167     -10.443 -10.956   6.480  1.00 54.14           N  
ANISOU  586  NH1 ARG A 167     5389   6800   8383    264   1822   -219       N  
ATOM    587  NH2 ARG A 167      -8.570  -9.677   6.124  1.00 50.58           N  
ANISOU  587  NH2 ARG A 167     4935   6628   7655    439   1679   -468       N  
ATOM    588  N   THR A 168      -9.551 -17.127   4.681  1.00 46.95           N  
ANISOU  588  N   THR A 168     5756   5559   6525    416    636    201       N  
ATOM    589  CA  THR A 168      -9.508 -17.162   3.222  1.00 46.27           C  
ANISOU  589  CA  THR A 168     5647   5428   6506    447    299    176       C  
ATOM    590  C   THR A 168     -10.730 -16.501   2.619  1.00 49.94           C  
ANISOU  590  C   THR A 168     5763   5766   7444    249    245    264       C  
ATOM    591  O   THR A 168     -11.788 -16.439   3.246  1.00 51.44           O  
ANISOU  591  O   THR A 168     5745   5810   7990     66    439    368       O  
ATOM    592  CB  THR A 168      -9.416 -18.594   2.681  1.00 45.71           C  
ANISOU  592  CB  THR A 168     5909   5157   6301    477     27    192       C  
ATOM    593  OG1 THR A 168     -10.551 -19.345   3.129  1.00 47.77           O  
ANISOU  593  OG1 THR A 168     6158   5133   6860    250     70    334       O  
ATOM    594  CG2 THR A 168      -8.128 -19.267   3.151  1.00 44.21           C  
ANISOU  594  CG2 THR A 168     6041   5073   5684    726     42    124       C  
ATOM    595  N   ASN A 169     -10.577 -16.011   1.394  1.00 52.46           N  
ANISOU  595  N   ASN A 169     6016   6145   7773    297    -12    243       N  
ATOM    596  CA  ASN A 169     -11.696 -15.408   0.683  1.00 56.56           C  
ANISOU  596  CA  ASN A 169     6212   6545   8734    135   -162    361       C  
ATOM    597  C   ASN A 169     -11.362 -15.278  -0.799  1.00 54.74           C  
ANISOU  597  C   ASN A 169     6093   6378   8328    212   -537    352       C  
ATOM    598  O   ASN A 169     -10.239 -15.552  -1.200  1.00 53.10           O  
ANISOU  598  O   ASN A 169     6178   6315   7681    400   -589    240       O  
ATOM    599  CB  ASN A 169     -12.036 -14.048   1.293  1.00 60.82           C  
ANISOU  599  CB  ASN A 169     6366   7151   9591    106    158    390       C  
ATOM    600  CG  ASN A 169     -13.491 -13.675   1.111  1.00 68.28           C  
ANISOU  600  CG  ASN A 169     6907   7890  11145    -88    122    553       C  
ATOM    601  OD1 ASN A 169     -14.264 -14.417   0.503  1.00 71.42           O  
ANISOU  601  OD1 ASN A 169     7291   8108  11738   -228   -189    651       O  
ATOM    602  ND2 ASN A 169     -13.884 -12.538   1.677  1.00 71.77           N  
ANISOU  602  ND2 ASN A 169     7003   8335  11931    -98    440    569       N  
ATOM    603  N   TRP A 170     -12.328 -14.888  -1.621  1.00 53.47           N  
ANISOU  603  N   TRP A 170     5706   6110   8500     77   -799    481       N  
ATOM    604  CA  TRP A 170     -12.036 -14.673  -3.032  1.00 52.26           C  
ANISOU  604  CA  TRP A 170     5700   6042   8113    150  -1153    498       C  
ATOM    605  C   TRP A 170     -11.152 -13.445  -3.184  1.00 50.39           C  
ANISOU  605  C   TRP A 170     5373   6041   7731    319   -947    508       C  
ATOM    606  O   TRP A 170     -11.249 -12.501  -2.400  1.00 49.08           O  
ANISOU  606  O   TRP A 170     4897   5901   7849    309   -639    541       O  
ATOM    607  CB  TRP A 170     -13.321 -14.516  -3.849  1.00 54.02           C  
ANISOU  607  CB  TRP A 170     5693   6101   8730    -41  -1547    666       C  
ATOM    608  CG  TRP A 170     -14.049 -15.807  -4.079  1.00 56.96           C  
ANISOU  608  CG  TRP A 170     6220   6237   9187   -221  -1879    631       C  
ATOM    609  CD1 TRP A 170     -15.193 -16.223  -3.463  1.00 58.36           C  
ANISOU  609  CD1 TRP A 170     6108   6170   9895   -452  -1874    720       C  
ATOM    610  CD2 TRP A 170     -13.683 -16.853  -4.991  1.00 57.26           C  
ANISOU  610  CD2 TRP A 170     6734   6228   8794   -197  -2244    484       C  
ATOM    611  NE1 TRP A 170     -15.561 -17.461  -3.932  1.00 61.02           N  
ANISOU  611  NE1 TRP A 170     6697   6297  10190   -598  -2246    648       N  
ATOM    612  CE2 TRP A 170     -14.648 -17.870  -4.872  1.00 60.60           C  
ANISOU  612  CE2 TRP A 170     7138   6353   9535   -439  -2487    481       C  
ATOM    613  CE3 TRP A 170     -12.626 -17.028  -5.892  1.00 57.26           C  
ANISOU  613  CE3 TRP A 170     7177   6395   8184      7  -2355    342       C  
ATOM    614  CZ2 TRP A 170     -14.595 -19.046  -5.621  1.00 62.17           C  
ANISOU  614  CZ2 TRP A 170     7769   6391   9463   -491  -2875    313       C  
ATOM    615  CZ3 TRP A 170     -12.575 -18.197  -6.637  1.00 59.17           C  
ANISOU  615  CZ3 TRP A 170     7861   6497   8123    -17  -2700    169       C  
ATOM    616  CH2 TRP A 170     -13.552 -19.190  -6.495  1.00 61.62           C  
ANISOU  616  CH2 TRP A 170     8166   6486   8760   -267  -2975    141       C  
ATOM    617  N   ALA A 171     -10.285 -13.464  -4.191  1.00 50.50           N  
ANISOU  617  N   ALA A 171     5668   6208   7310    467  -1091    470       N  
ATOM    618  CA  ALA A 171      -9.375 -12.352  -4.430  1.00 49.44           C  
ANISOU  618  CA  ALA A 171     5455   6283   7048    611   -888    503       C  
ATOM    619  C   ALA A 171      -9.861 -11.467  -5.575  1.00 50.91           C  
ANISOU  619  C   ALA A 171     5525   6474   7343    575  -1126    724       C  
ATOM    620  O   ALA A 171     -10.993 -11.603  -6.039  1.00 52.86           O  
ANISOU  620  O   ALA A 171     5681   6569   7836    431  -1459    852       O  
ATOM    621  CB  ALA A 171      -7.975 -12.869  -4.718  1.00 49.23           C  
ANISOU  621  CB  ALA A 171     5773   6439   6492    821   -794    349       C  
TER     622      ALA A 171                                                      
ATOM    623  C4'  DT B   1      -4.243  -4.299   5.193  1.00 86.02           C  
ANISOU  623  C4'  DT B   1     8324   9253  15106   1581    845  -2918       C  
ATOM    624  O4'  DT B   1      -3.644  -5.612   5.358  1.00 84.25           O  
ANISOU  624  O4'  DT B   1     8331   9530  14148   1796   1150  -2668       O  
ATOM    625  C3'  DT B   1      -5.652  -4.572   4.692  1.00 83.52           C  
ANISOU  625  C3'  DT B   1     8437   8666  14632   1576    770  -2794       C  
ATOM    626  O3'  DT B   1      -5.633  -4.753   3.282  1.00 82.54           O  
ANISOU  626  O3'  DT B   1     8799   8119  14443   1466    903  -2152       O  
ATOM    627  C2'  DT B   1      -5.982  -5.873   5.407  1.00 80.91           C  
ANISOU  627  C2'  DT B   1     8322   8899  13520   1799    928  -2873       C  
ATOM    628  C1'  DT B   1      -4.651  -6.607   5.292  1.00 80.36           C  
ANISOU  628  C1'  DT B   1     8326   9144  13065   1916   1225  -2550       C  
ATOM    629  N1   DT B   1      -4.411  -7.590   6.382  1.00 79.30           N  
ANISOU  629  N1   DT B   1     8154   9652  12325   2149   1324  -2760       N  
ATOM    630  C2   DT B   1      -5.213  -8.706   6.482  1.00 75.44           C  
ANISOU  630  C2   DT B   1     8114   9352  11197   2269   1428  -2638       C  
ATOM    631  O2   DT B   1      -6.133  -8.943   5.719  1.00 73.15           O  
ANISOU  631  O2   DT B   1     8238   8738  10819   2186   1424  -2382       O  
ATOM    632  N3   DT B   1      -4.899  -9.541   7.520  1.00 75.69           N  
ANISOU  632  N3   DT B   1     8099   9960  10698   2472   1505  -2812       N  
ATOM    633  C4   DT B   1      -3.886  -9.379   8.445  1.00 78.18           C  
ANISOU  633  C4   DT B   1     7975  10687  11044   2574   1454  -3091       C  
ATOM    634  O4   DT B   1      -3.681 -10.185   9.344  1.00 78.90           O  
ANISOU  634  O4   DT B   1     8090  11280  10608   2758   1493  -3202       O  
ATOM    635  C5   DT B   1      -3.085  -8.194   8.281  1.00 81.00           C  
ANISOU  635  C5   DT B   1     7850  10825  12100   2428   1320  -3223       C  
ATOM    636  C7   DT B   1      -1.963  -7.912   9.227  1.00 83.63           C  
ANISOU  636  C7   DT B   1     7663  11559  12553   2488   1193  -3526       C  
ATOM    637  C6   DT B   1      -3.380  -7.367   7.269  1.00 81.25           C  
ANISOU  637  C6   DT B   1     7925  10279  12667   2220   1279  -3049       C  
ATOM    638  P    DT B   2      -6.968  -4.537   2.414  1.00 84.86           P  
ANISOU  638  P    DT B   2     9476   7887  14880   1344    687  -1937       P  
ATOM    639  OP1  DT B   2      -6.983  -3.129   1.959  1.00 87.79           O  
ANISOU  639  OP1  DT B   2     9595   7685  16076   1133    426  -1967       O  
ATOM    640  OP2  DT B   2      -8.108  -5.075   3.190  1.00 82.97           O  
ANISOU  640  OP2  DT B   2     9238   7924  14365   1469    577  -2276       O  
ATOM    641  O5'  DT B   2      -6.748  -5.475   1.137  1.00 73.15           O  
ANISOU  641  O5'  DT B   2     8712   6261  12819   1327    960  -1224       O  
ATOM    642  C5'  DT B   2      -5.566  -5.346   0.357  1.00 74.68           C  
ANISOU  642  C5'  DT B   2     9012   6325  13038   1258   1231   -808       C  
ATOM    643  C4'  DT B   2      -5.646  -6.208  -0.890  1.00 73.17           C  
ANISOU  643  C4'  DT B   2     9605   5935  12261   1250   1465   -186       C  
ATOM    644  O4'  DT B   2      -6.273  -7.475  -0.563  1.00 69.33           O  
ANISOU  644  O4'  DT B   2     9490   5766  11085   1429   1523   -215       O  
ATOM    645  C3'  DT B   2      -6.466  -5.611  -2.038  1.00 74.29           C  
ANISOU  645  C3'  DT B   2    10148   5434  12645   1014   1205    153       C  
ATOM    646  O3'  DT B   2      -5.800  -5.829  -3.275  1.00 76.05           O  
ANISOU  646  O3'  DT B   2    10907   5413  12574    934   1511    747       O  
ATOM    647  C2'  DT B   2      -7.781  -6.385  -1.968  1.00 71.07           C  
ANISOU  647  C2'  DT B   2    10108   5055  11840   1067    989    106       C  
ATOM    648  C1'  DT B   2      -7.299  -7.742  -1.489  1.00 67.89           C  
ANISOU  648  C1'  DT B   2     9910   5192  10691   1306   1351    104       C  
ATOM    649  N1   DT B   2      -8.355  -8.546  -0.812  1.00 64.60           N  
ANISOU  649  N1   DT B   2     9582   5035   9928   1395   1198   -134       N  
ATOM    650  C2   DT B   2      -8.924  -9.603  -1.482  1.00 62.65           C  
ANISOU  650  C2   DT B   2    10049   4694   9062   1386   1229    216       C  
ATOM    651  O2   DT B   2      -8.609  -9.922  -2.613  1.00 63.02           O  
ANISOU  651  O2   DT B   2    10706   4455   8784   1330   1379    688       O  
ATOM    652  N3   DT B   2      -9.883 -10.279  -0.776  1.00 60.50           N  
ANISOU  652  N3   DT B   2     9770   4669   8546   1430   1087    -10       N  
ATOM    653  C4   DT B   2     -10.321 -10.009   0.505  1.00 59.77           C  
ANISOU  653  C4   DT B   2     9056   4929   8725   1499    965   -540       C  
ATOM    654  O4   DT B   2     -11.191 -10.677   1.054  1.00 58.40           O  
ANISOU  654  O4   DT B   2     8925   4976   8289   1517    888   -679       O  
ATOM    655  C5   DT B   2      -9.683  -8.886   1.153  1.00 61.68           C  
ANISOU  655  C5   DT B   2     8614   5254   9569   1532    943   -921       C  
ATOM    656  C7   DT B   2     -10.075  -8.495   2.548  1.00 61.79           C  
ANISOU  656  C7   DT B   2     7983   5635   9858   1616    828  -1545       C  
ATOM    657  C6   DT B   2      -8.742  -8.216   0.470  1.00 63.71           C  
ANISOU  657  C6   DT B   2     8854   5244  10110   1468   1036   -700       C  
ATOM    658  P    DT B   3      -5.484  -4.593  -4.253  1.00 98.32           P  
ANISOU  658  P    DT B   3    13734   7653  15970    646   1428   1086       P  
ATOM    659  OP1  DT B   3      -5.212  -3.411  -3.405  1.00 98.66           O  
ANISOU  659  OP1  DT B   3    12971   7671  16844    564   1205    643       O  
ATOM    660  OP2  DT B   3      -6.558  -4.533  -5.270  1.00 99.56           O  
ANISOU  660  OP2  DT B   3    14513   7304  16009    487   1124   1431       O  
ATOM    661  O5'  DT B   3      -4.113  -5.014  -4.965  1.00105.61           O  
ANISOU  661  O5'  DT B   3    14906   8694  16528    675   2022   1544       O  
ATOM    662  C5'  DT B   3      -2.931  -5.186  -4.188  1.00106.24           C  
ANISOU  662  C5'  DT B   3    14436   9256  16676    833   2355   1342       C  
ATOM    663  C4'  DT B   3      -1.830  -5.828  -5.013  1.00108.07           C  
ANISOU  663  C4'  DT B   3    15025   9593  16445    918   2964   1837       C  
ATOM    664  O4'  DT B   3      -2.015  -7.262  -5.036  1.00105.16           O  
ANISOU  664  O4'  DT B   3    15203   9515  15239   1205   3197   1908       O  
ATOM    665  C3'  DT B   3      -1.771  -5.375  -6.477  1.00110.61           C  
ANISOU  665  C3'  DT B   3    15913   9380  16733    668   3110   2428       C  
ATOM    666  O3'  DT B   3      -0.519  -4.753  -6.747  1.00114.07           O  
ANISOU  666  O3'  DT B   3    15959   9820  17564    548   3483   2656       O  
ATOM    667  C2'  DT B   3      -1.952  -6.668  -7.290  1.00109.45           C  
ANISOU  667  C2'  DT B   3    16682   9267  15639    848   3435   2783       C  
ATOM    668  C1'  DT B   3      -1.593  -7.750  -6.281  1.00107.01           C  
ANISOU  668  C1'  DT B   3    16136   9555  14967   1213   3636   2456       C  
ATOM    669  N1   DT B   3      -2.260  -9.078  -6.539  1.00103.42           N  
ANISOU  669  N1   DT B   3    16467   9159  13669   1411   3684   2541       N  
ATOM    670  C2   DT B   3      -3.626  -9.204  -6.377  1.00100.59           C  
ANISOU  670  C2   DT B   3    16370   8631  13218   1319   3171   2368       C  
ATOM    671  O2   DT B   3      -4.351  -8.287  -6.032  1.00100.17           O  
ANISOU  671  O2   DT B   3    15935   8387  13738   1122   2693   2137       O  
ATOM    672  N3   DT B   3      -4.120 -10.456  -6.640  1.00 97.92           N  
ANISOU  672  N3   DT B   3    16659   8434  12111   1448   3187   2411       N  
ATOM    673  C4   DT B   3      -3.405 -11.572  -7.037  1.00 98.20           C  
ANISOU  673  C4   DT B   3    16981   8824  11506   1659   3573   2459       C  
ATOM    674  O4   DT B   3      -3.942 -12.655  -7.248  1.00 95.91           O  
ANISOU  674  O4   DT B   3    17023   8738  10679   1704   3406   2280       O  
ATOM    675  C5   DT B   3      -1.983 -11.374  -7.185  1.00101.77           C  
ANISOU  675  C5   DT B   3    17236   9342  12089   1824   4176   2694       C  
ATOM    676  C7   DT B   3      -1.105 -12.514  -7.611  1.00103.43           C  
ANISOU  676  C7   DT B   3    17660   9867  11770   2121   4588   2682       C  
ATOM    677  C6   DT B   3      -1.486 -10.153  -6.932  1.00104.09           C  
ANISOU  677  C6   DT B   3    16981   9450  13117   1683   4246   2789       C  
TER     678       DT B   3                                                      
HETATM  679  O   HOH A 201      -8.039 -15.163  10.803  1.00 53.70           O  
HETATM  680  O   HOH A 202      -9.308 -29.658 -11.009  1.00 59.10           O  
HETATM  681  O   HOH A 203      -0.086 -28.418  -6.929  1.00 49.42           O  
HETATM  682  O   HOH A 204     -19.582 -21.817   0.628  1.00 77.41           O  
HETATM  683  O   HOH A 205     -20.284 -23.876   1.101  1.00 66.23           O  
MASTER      324    0    0    3    6    0    0    6  681    2    0    9          
END

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Related entries of code: 5ith

Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code	Check Database	Protein Sequence Similarity
No similar entries are found!
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	5ith
Complex Type	Protein-Nucleic Acid
PDBbind Subset	general set
Protein Name	Nucleolysin TIA-1 RRM2
Ligand Name	ACTCCTTTTT DNA
EC.Number	E.C.-.-.-.-
Resolution	2.31(Å)
Affinity (Kd/Ki/IC50)	Kd=0.03uM
Release Year	2017
Protein/NA Sequence	Check fasta file
Primary Reference	(2017) Nucleic Acids Res. Vol. 45: pp. 4944-4957

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): P31483
Entrez Gene ID	NCBI Entrez Gene ID: 7072
ASD	Information of known allosteric effects of PDB entries

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