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Browse entries in the PDBbind-CN Database

HEADER    RNA BINDING PROTEIN/RNA                 22-JUN-10   3NMR              
TITLE     CRYSTAL STRUCTURE OF CUGBP1 RRM1/2-RNA COMPLEX                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CUGBP ELAV-LIKE FAMILY MEMBER 1;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RRM1-RRM2 DOMAIN (UNP RESIDUES 14-187);                    
COMPND   5 SYNONYM: CELF-1, CUG-BP- AND ETR-3-LIKE FACTOR 1, BRUNO-LIKE PROTEIN 
COMPND   6 2, RNA-BINDING PROTEIN BRUNOL-2, CUG TRIPLET REPEAT RNA-BINDING      
COMPND   7 PROTEIN 1, CUG-BP1, DEADENYLATION FACTOR CUG-BP, 50 KDA NUCLEAR      
COMPND   8 POLYADENYLATED RNA-BINDING PROTEIN, EMBRYO DEADENYLATION ELEMENT-    
COMPND   9 BINDING PROTEIN HOMOLOG, EDEN-BP HOMOLOG;                            
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: RNA (5'-R(*GP*UP*UP*GP*UP*UP*UP*UP*GP*UP*UP*U)-3');        
COMPND  13 CHAIN: B;                                                            
COMPND  14 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: BRUNOL2, CELF1, CUGBP, CUGBP1, NAB50;                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL;                              
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 SYNTHETIC: YES;                                                      
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS              
KEYWDS    RRM, PRE-MRNA SPLICING, RNA BINDING PROTEIN-RNA COMPLEX               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.TEPLOVA,J.SONG,H.GAW,A.TEPLOV,D.J.PATEL                             
REVDAT   2   08-OCT-14 3NMR    1       AUTHOR VERSN                             
REVDAT   1   27-OCT-10 3NMR    0                                                
JRNL        AUTH   M.TEPLOVA,J.SONG,H.Y.GAW,A.TEPLOV,D.J.PATEL                  
JRNL        TITL   STRUCTURAL INSIGHTS INTO RNA RECOGNITION BY THE              
JRNL        TITL 2 ALTERNATE-SPLICING REGULATOR CUG-BINDING PROTEIN 1.          
JRNL        REF    STRUCTURE                     V.  18  1364 2010              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   20947024                                                     
JRNL        DOI    10.1016/J.STR.2010.06.018                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0066                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 18187                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 986                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.85                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.90                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1306                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.20                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2410                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 58                           
REMARK   3   BIN FREE R VALUE                    : 0.3460                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1375                                    
REMARK   3   NUCLEIC ACID ATOMS       : 107                                     
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 96                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.47000                                             
REMARK   3    B22 (A**2) : -0.20000                                             
REMARK   3    B33 (A**2) : 0.67000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.136         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.088         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.480         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1520 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1313 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2066 ; 1.257 ; 2.044       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3079 ; 1.121 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   174 ; 5.256 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    65 ;37.787 ;23.846       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   260 ;16.078 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    11 ;20.108 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   229 ; 0.072 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1601 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   299 ; 0.000 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   872 ; 0.977 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   354 ; 0.322 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1406 ; 1.719 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   648 ; 2.660 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   660 ; 4.102 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2833 ; 1.299 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   101 ; 5.715 ; 3.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2797 ; 2.046 ; 3.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3NMR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUN-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB060022.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-SEP-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97930, 0.97890, 0.96360          
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18231                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 66.082                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.03600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 36.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.92                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHELXS                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 45% MPD, PH      
REMARK 280  8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
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        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       23.77400            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       35.00600            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       66.10450            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       23.77400            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       35.00600            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       66.10450            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       23.77400            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       35.00600            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       66.10450            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       23.77400            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       35.00600            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       66.10450            
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: 1100 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B  12  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B  28  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 200  LIES ON A SPECIAL POSITION.                          
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       G B     0                                                      
REMARK 465       U B     7                                                      
REMARK 465       G B     8                                                      
REMARK 465       U B     9                                                      
REMARK 465       U B    10                                                      
REMARK 465       U B    11                                                      
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       U B   6    C5'  C4'  O4'  C3'  O3'  C2'  O2'                   
REMARK 470       U B   6    C1'  N1   C2   O2   N3   C4   O4                    
REMARK 470       U B   6    C5   C6                                             
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    MSE A  82      -51.28   -123.92                                   
REMARK 500    ASN A 102      -80.20   -105.67                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3NNA   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN RRM1-RRM2 DOMAIN COMPLEXED WITH                     
REMARK 900 GUUGUUUUUGUU.                                                        
REMARK 900 RELATED ID: 3NNC   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN RRM1-RRM2 DOMAIN COMPLEXED WITH                     
REMARK 900 UGUGUGUUGUGUG.                                                       
REMARK 900 RELATED ID: 3NNH   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN RRM1 DOMAIN COMPLEXED WITH GUUGUUUUGUUU.            
DBREF  3NMR A   14   187  UNP    Q92879   CELF1_HUMAN     14    187             
DBREF  3NMR B    0    11  PDB    3NMR     3NMR             0     11             
SEQADV 3NMR SER A   13  UNP  Q92879              EXPRESSION TAG                 
SEQRES   1 A  175  SER ASP ALA ILE LYS MSE PHE VAL GLY GLN VAL PRO ARG          
SEQRES   2 A  175  THR TRP SER GLU LYS ASP LEU ARG GLU LEU PHE GLU GLN          
SEQRES   3 A  175  TYR GLY ALA VAL TYR GLU ILE ASN VAL LEU ARG ASP ARG          
SEQRES   4 A  175  SER GLN ASN PRO PRO GLN SER LYS GLY CYS CYS PHE VAL          
SEQRES   5 A  175  THR PHE TYR THR ARG LYS ALA ALA LEU GLU ALA GLN ASN          
SEQRES   6 A  175  ALA LEU HIS ASN MSE LYS VAL LEU PRO GLY MSE HIS HIS          
SEQRES   7 A  175  PRO ILE GLN MSE LYS PRO ALA ASP SER GLU LYS ASN ASN          
SEQRES   8 A  175  ALA VAL GLU ASP ARG LYS LEU PHE ILE GLY MSE ILE SER          
SEQRES   9 A  175  LYS LYS CYS THR GLU ASN ASP ILE ARG VAL MSE PHE SER          
SEQRES  10 A  175  SER PHE GLY GLN ILE GLU GLU CYS ARG ILE LEU ARG GLY          
SEQRES  11 A  175  PRO ASP GLY LEU SER ARG GLY CYS ALA PHE VAL THR PHE          
SEQRES  12 A  175  THR THR ARG ALA MSE ALA GLN THR ALA ILE LYS ALA MSE          
SEQRES  13 A  175  HIS GLN ALA GLN THR MSE GLU GLY CYS SER SER PRO MSE          
SEQRES  14 A  175  VAL VAL LYS PHE ALA ASP                                      
SEQRES   1 B   12    G   U   U   G   U   U   U   U   G   U   U   U              
MODRES 3NMR MSE A   18  MET  SELENOMETHIONINE                                   
MODRES 3NMR MSE A   82  MET  SELENOMETHIONINE                                   
MODRES 3NMR MSE A   88  MET  SELENOMETHIONINE                                   
MODRES 3NMR MSE A   94  MET  SELENOMETHIONINE                                   
MODRES 3NMR MSE A  114  MET  SELENOMETHIONINE                                   
MODRES 3NMR MSE A  127  MET  SELENOMETHIONINE                                   
MODRES 3NMR MSE A  160  MET  SELENOMETHIONINE                                   
MODRES 3NMR MSE A  168  MET  SELENOMETHIONINE                                   
MODRES 3NMR MSE A  174  MET  SELENOMETHIONINE                                   
MODRES 3NMR MSE A  181  MET  SELENOMETHIONINE                                   
HET    MSE  A  18       8                                                       
HET    MSE  A  82       8                                                       
HET    MSE  A  88       8                                                       
HET    MSE  A  94       8                                                       
HET    MSE  A 114       8                                                       
HET    MSE  A 127       8                                                       
HET    MSE  A 160       8                                                       
HET    MSE  A 168       8                                                       
HET    MSE  A 174       8                                                       
HET    MSE  A 181       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    10(C5 H11 N O2 SE)                                           
FORMUL   3  HOH   *96(H2 O)                                                     
HELIX    1   1 SER A   28  GLN A   38  1                                  11    
HELIX    2   2 THR A   68  HIS A   80  1                                  13    
HELIX    3   3 ASP A   98  LYS A  101  5                                   4    
HELIX    4   4 ALA A  104  ASP A  107  5                                   4    
HELIX    5   5 THR A  120  SER A  129  1                                  10    
HELIX    6   6 SER A  130  GLY A  132  5                                   3    
HELIX    7   7 THR A  157  HIS A  169  1                                  13    
SHEET    1   A 4 VAL A  42  ASP A  50  0                                        
SHEET    2   A 4 GLN A  57  PHE A  66 -1  O  THR A  65   N  GLU A  44           
SHEET    3   A 4 ILE A  16  GLY A  21 -1  N  MSE A  18   O  VAL A  64           
SHEET    4   A 4 GLN A  93  PRO A  96 -1  O  LYS A  95   N  PHE A  19           
SHEET    1   B 4 ILE A 134  ARG A 141  0                                        
SHEET    2   B 4 SER A 147  PHE A 155 -1  O  ARG A 148   N  LEU A 140           
SHEET    3   B 4 LYS A 109  GLY A 113 -1  N  LEU A 110   O  VAL A 153           
SHEET    4   B 4 VAL A 182  PHE A 185 -1  O  LYS A 184   N  PHE A 111           
LINK         C   LYS A  17                 N   MSE A  18     1555   1555  1.33  
LINK         C   MSE A  18                 N   PHE A  19     1555   1555  1.33  
LINK         C   ASN A  81                 N   MSE A  82     1555   1555  1.33  
LINK         C   MSE A  82                 N   LYS A  83     1555   1555  1.33  
LINK         C   GLY A  87                 N   MSE A  88     1555   1555  1.33  
LINK         C   MSE A  88                 N   HIS A  89     1555   1555  1.33  
LINK         C   GLN A  93                 N   MSE A  94     1555   1555  1.32  
LINK         C   MSE A  94                 N   LYS A  95     1555   1555  1.33  
LINK         C   GLY A 113                 N   MSE A 114     1555   1555  1.33  
LINK         C   MSE A 114                 N   ILE A 115     1555   1555  1.33  
LINK         C   VAL A 126                 N   MSE A 127     1555   1555  1.33  
LINK         C   MSE A 127                 N   PHE A 128     1555   1555  1.33  
LINK         C   ALA A 159                 N   MSE A 160     1555   1555  1.33  
LINK         C   MSE A 160                 N   ALA A 161     1555   1555  1.33  
LINK         C   ALA A 167                 N   MSE A 168     1555   1555  1.33  
LINK         C   MSE A 168                 N   HIS A 169     1555   1555  1.33  
LINK         C   THR A 173                 N   MSE A 174     1555   1555  1.32  
LINK         C   MSE A 174                 N   GLU A 175     1555   1555  1.33  
LINK         C   PRO A 180                 N   MSE A 181     1555   1555  1.34  
LINK         C   MSE A 181                 N   VAL A 182     1555   1555  1.33  
CISPEP   1 ASN A   54    PRO A   55          0         0.72                     
CRYST1   47.548   70.012  132.209  90.00  90.00  90.00 I 2 2 2       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.021031  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014283  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007564        0.00000                         
ATOM      1  N   SER A  13      10.336   5.265  86.529  1.00 46.45           N  
ANISOU    1  N   SER A  13     5992   5823   5832    -34    -39     10       N  
ATOM      2  CA  SER A  13      11.075   5.118  85.229  1.00 46.62           C  
ANISOU    2  CA  SER A  13     5993   5848   5874    -19    -20    -11       C  
ATOM      3  C   SER A  13      12.594   5.111  85.381  1.00 45.51           C  
ANISOU    3  C   SER A  13     5866   5678   5748    -61    -31    -26       C  
ATOM      4  O   SER A  13      13.102   4.659  86.394  1.00 46.68           O  
ANISOU    4  O   SER A  13     6016   5827   5895    -95    -86    -31       O  
ATOM      5  CB  SER A  13      10.664   6.222  84.249  1.00 47.03           C  
ANISOU    5  CB  SER A  13     6049   5907   5914    -40      1     17       C  
ATOM      6  OG  SER A  13      11.261   6.006  82.982  1.00 48.20           O  
ANISOU    6  OG  SER A  13     6260   6084   5969     -2     58    -49       O  
ATOM      7  N   ASP A  14      13.311   5.579  84.359  1.00 44.30           N  
ANISOU    7  N   ASP A  14     5690   5501   5642    -51    -41    -82       N  
ATOM      8  CA  ASP A  14      14.784   5.659  84.373  1.00 42.85           C  
ANISOU    8  CA  ASP A  14     5512   5316   5454    -56    -37    -80       C  
ATOM      9  C   ASP A  14      15.228   6.942  85.100  1.00 40.00           C  
ANISOU    9  C   ASP A  14     5163   4932   5105    -32    -19    -53       C  
ATOM     10  O   ASP A  14      14.385   7.771  85.412  1.00 39.97           O  
ANISOU   10  O   ASP A  14     5213   4846   5126    -76    -27    -85       O  
ATOM     11  CB  ASP A  14      15.298   5.649  82.934  1.00 43.62           C  
ANISOU   11  CB  ASP A  14     5606   5429   5537    -52    -27    -67       C  
ATOM     12  CG  ASP A  14      16.809   5.567  82.837  1.00 46.57           C  
ANISOU   12  CG  ASP A  14     5908   5825   5960    -27    -26    -30       C  
ATOM     13  OD1 ASP A  14      17.404   4.601  83.366  1.00 51.00           O  
ANISOU   13  OD1 ASP A  14     6528   6216   6635     40   -103    143       O  
ATOM     14  OD2 ASP A  14      17.407   6.460  82.196  1.00 49.96           O  
ANISOU   14  OD2 ASP A  14     6484   6149   6348    -75    104     82       O  
ATOM     15  N   ALA A  15      16.524   7.108  85.369  1.00 36.61           N  
ANISOU   15  N   ALA A  15     4847   4413   4650    -78     22    -83       N  
ATOM     16  CA  ALA A  15      16.988   8.162  86.283  1.00 34.47           C  
ANISOU   16  CA  ALA A  15     4545   4172   4380    -49     28    -22       C  
ATOM     17  C   ALA A  15      16.762   9.543  85.700  1.00 32.34           C  
ANISOU   17  C   ALA A  15     4358   3846   4083    -93     48    -79       C  
ATOM     18  O   ALA A  15      16.849   9.735  84.490  1.00 31.04           O  
ANISOU   18  O   ALA A  15     4421   3437   3937   -158     60   -151       O  
ATOM     19  CB  ALA A  15      18.454   7.981  86.621  1.00 34.63           C  
ANISOU   19  CB  ALA A  15     4579   4178   4399    -49     17    -40       C  
ATOM     20  N   ILE A  16      16.470  10.520  86.552  1.00 30.20           N  
ANISOU   20  N   ILE A  16     4064   3624   3787    -98     75    -32       N  
ATOM     21  CA  ILE A  16      16.246  11.860  86.032  1.00 29.06           C  
ANISOU   21  CA  ILE A  16     3876   3498   3668    -66     22    -91       C  
ATOM     22  C   ILE A  16      16.608  12.929  87.054  1.00 28.12           C  
ANISOU   22  C   ILE A  16     3779   3365   3542    -84     50    -64       C  
ATOM     23  O   ILE A  16      16.352  12.780  88.252  1.00 26.53           O  
ANISOU   23  O   ILE A  16     3636   3087   3356   -103    104    -86       O  
ATOM     24  CB  ILE A  16      14.815  12.065  85.515  1.00 29.27           C  
ANISOU   24  CB  ILE A  16     3871   3575   3677    -79     38    -70       C  
ATOM     25  CG1 ILE A  16      14.713  13.438  84.840  1.00 30.37           C  
ANISOU   25  CG1 ILE A  16     3929   3707   3903    -11    -27    -13       C  
ATOM     26  CG2 ILE A  16      13.807  11.931  86.634  1.00 29.16           C  
ANISOU   26  CG2 ILE A  16     3799   3588   3694    -47     13    -62       C  
ATOM     27  CD1 ILE A  16      13.314  13.841  84.456  1.00 31.13           C  
ANISOU   27  CD1 ILE A  16     3993   3884   3951    -53    -56    -10       C  
ATOM     28  N   LYS A  17      17.252  13.981  86.550  1.00 26.55           N  
ANISOU   28  N   LYS A  17     3567   3149   3370   -128     33    -59       N  
ATOM     29  CA  LYS A  17      17.723  15.076  87.390  1.00 25.79           C  
ANISOU   29  CA  LYS A  17     3410   3095   3294    -74     -4    -38       C  
ATOM     30  C   LYS A  17      16.741  16.239  87.301  1.00 24.54           C  
ANISOU   30  C   LYS A  17     3264   2890   3169   -113     -2    -29       C  
ATOM     31  O   LYS A  17      16.399  16.709  86.210  1.00 24.50           O  
ANISOU   31  O   LYS A  17     3378   2779   3153    -71     59    -20       O  
ATOM     32  CB  LYS A  17      19.126  15.523  86.970  1.00 25.66           C  
ANISOU   32  CB  LYS A  17     3367   3093   3291    -33    -25    -19       C  
ATOM     33  CG  LYS A  17      19.748  16.497  87.978  1.00 27.08           C  
ANISOU   33  CG  LYS A  17     3552   3261   3475    -43    -88     -2       C  
ATOM     34  CD  LYS A  17      20.963  17.218  87.433  1.00 30.05           C  
ANISOU   34  CD  LYS A  17     3778   3847   3792     31     -3     19       C  
ATOM     35  CE  LYS A  17      22.118  16.289  87.184  1.00 32.34           C  
ANISOU   35  CE  LYS A  17     4052   4124   4112     10     11    -65       C  
ATOM     36  NZ  LYS A  17      23.332  17.085  86.824  1.00 32.24           N  
ANISOU   36  NZ  LYS A  17     4062   3913   4274   -172    192    111       N  
HETATM   37  N   MSE A  18      16.257  16.659  88.463  1.00 23.64           N  
ANISOU   37  N   MSE A  18     3138   2761   3085   -152    -24    -17       N  
HETATM   38  CA  MSE A  18      15.292  17.737  88.573  1.00 23.43           C  
ANISOU   38  CA  MSE A  18     3064   2769   3069   -177    -33    -15       C  
HETATM   39  C   MSE A  18      15.976  18.985  89.129  1.00 21.98           C  
ANISOU   39  C   MSE A  18     2908   2561   2883   -155    -35      8       C  
HETATM   40  O   MSE A  18      16.805  18.895  90.035  1.00 20.89           O  
ANISOU   40  O   MSE A  18     2822   2388   2727   -323   -103     -6       O  
HETATM   41  CB  MSE A  18      14.187  17.355  89.556  1.00 24.45           C  
ANISOU   41  CB  MSE A  18     3201   2963   3125   -169     -3      0       C  
HETATM   42  CG  MSE A  18      13.462  16.053  89.225  1.00 28.28           C  
ANISOU   42  CG  MSE A  18     3714   3312   3721   -271     23     83       C  
HETATM   43 SE   MSE A  18      12.557  16.158  87.509  1.00 36.84          SE  
ANISOU   43 SE   MSE A  18     4950   4499   4548   -807     -6    138      SE  
HETATM   44  CE  MSE A  18      11.063  17.322  87.958  1.00 35.33           C  
ANISOU   44  CE  MSE A  18     4638   4343   4443   -280    -50     38       C  
ATOM     45  N   PHE A  19      15.619  20.132  88.571  1.00 20.74           N  
ANISOU   45  N   PHE A  19     2714   2423   2745   -112     -6      3       N  
ATOM     46  CA  PHE A  19      16.007  21.428  89.139  1.00 20.18           C  
ANISOU   46  CA  PHE A  19     2671   2371   2624    -84    -12     12       C  
ATOM     47  C   PHE A  19      14.938  21.905  90.102  1.00 20.00           C  
ANISOU   47  C   PHE A  19     2601   2354   2643   -107    -17     62       C  
ATOM     48  O   PHE A  19      13.742  21.865  89.783  1.00 20.51           O  
ANISOU   48  O   PHE A  19     2570   2443   2781   -117    -13    115       O  
ATOM     49  CB  PHE A  19      16.194  22.463  88.023  1.00 19.84           C  
ANISOU   49  CB  PHE A  19     2670   2280   2589    -44     20     -5       C  
ATOM     50  CG  PHE A  19      16.448  23.849  88.523  1.00 20.23           C  
ANISOU   50  CG  PHE A  19     2722   2374   2592    -26     43     58       C  
ATOM     51  CD1 PHE A  19      17.718  24.253  88.884  1.00 19.65           C  
ANISOU   51  CD1 PHE A  19     2702   2203   2560     -3     28     -9       C  
ATOM     52  CD2 PHE A  19      15.404  24.754  88.626  1.00 21.47           C  
ANISOU   52  CD2 PHE A  19     2815   2509   2834     56     -2     -8       C  
ATOM     53  CE1 PHE A  19      17.950  25.554  89.337  1.00 21.01           C  
ANISOU   53  CE1 PHE A  19     2764   2559   2659    -72     15   -143       C  
ATOM     54  CE2 PHE A  19      15.641  26.059  89.063  1.00 21.88           C  
ANISOU   54  CE2 PHE A  19     2843   2562   2910      0   -113    -88       C  
ATOM     55  CZ  PHE A  19      16.916  26.442  89.429  1.00 20.75           C  
ANISOU   55  CZ  PHE A  19     2733   2338   2812    -60    -74     60       C  
ATOM     56  N   VAL A  20      15.373  22.375  91.269  1.00 20.06           N  
ANISOU   56  N   VAL A  20     2587   2338   2696   -111     10     29       N  
ATOM     57  CA  VAL A  20      14.464  22.792  92.326  1.00 20.15           C  
ANISOU   57  CA  VAL A  20     2614   2387   2656    -99      0     15       C  
ATOM     58  C   VAL A  20      14.796  24.184  92.839  1.00 20.44           C  
ANISOU   58  C   VAL A  20     2663   2424   2679    -69    -10      9       C  
ATOM     59  O   VAL A  20      15.912  24.417  93.312  1.00 20.79           O  
ANISOU   59  O   VAL A  20     2727   2290   2882   -156      1    -10       O  
ATOM     60  CB  VAL A  20      14.544  21.834  93.525  1.00 20.26           C  
ANISOU   60  CB  VAL A  20     2640   2391   2668    -69    -11     12       C  
ATOM     61  CG1 VAL A  20      13.473  22.192  94.536  1.00 20.58           C  
ANISOU   61  CG1 VAL A  20     2707   2447   2667    -62     17     79       C  
ATOM     62  CG2 VAL A  20      14.444  20.373  93.065  1.00 21.02           C  
ANISOU   62  CG2 VAL A  20     2695   2527   2766   -111    -57    -20       C  
ATOM     63  N   GLY A  21      13.825  25.092  92.759  1.00 21.02           N  
ANISOU   63  N   GLY A  21     2713   2537   2738    -68     -3      6       N  
ATOM     64  CA  GLY A  21      13.996  26.474  93.231  1.00 21.24           C  
ANISOU   64  CA  GLY A  21     2718   2588   2766    -94      4    -15       C  
ATOM     65  C   GLY A  21      13.163  26.748  94.475  1.00 21.80           C  
ANISOU   65  C   GLY A  21     2766   2691   2826   -106     19      0       C  
ATOM     66  O   GLY A  21      12.300  25.932  94.847  1.00 21.79           O  
ANISOU   66  O   GLY A  21     2902   2623   2755   -149     -5    163       O  
ATOM     67  N   GLN A  22      13.371  27.923  95.075  1.00 21.86           N  
ANISOU   67  N   GLN A  22     2734   2682   2890   -129     60     -2       N  
ATOM     68  CA  GLN A  22      12.764  28.310  96.354  1.00 22.22           C  
ANISOU   68  CA  GLN A  22     2787   2727   2928    -80     28    -13       C  
ATOM     69  C   GLN A  22      13.164  27.372  97.497  1.00 22.28           C  
ANISOU   69  C   GLN A  22     2830   2695   2940    -68     80    -19       C  
ATOM     70  O   GLN A  22      12.352  27.041  98.372  1.00 22.59           O  
ANISOU   70  O   GLN A  22     2884   2720   2979   -146    147    -59       O  
ATOM     71  CB  GLN A  22      11.236  28.454  96.246  1.00 22.47           C  
ANISOU   71  CB  GLN A  22     2815   2707   3015    -68     29      3       C  
ATOM     72  CG  GLN A  22      10.791  29.435  95.168  1.00 23.41           C  
ANISOU   72  CG  GLN A  22     2779   2917   3197    -77     35     40       C  
ATOM     73  CD  GLN A  22      11.320  30.837  95.425  1.00 24.68           C  
ANISOU   73  CD  GLN A  22     3093   2952   3333    -47     88      2       C  
ATOM     74  OE1 GLN A  22      11.249  31.349  96.543  1.00 26.41           O  
ANISOU   74  OE1 GLN A  22     3338   3120   3577    -92    -40     19       O  
ATOM     75  NE2 GLN A  22      11.885  31.445  94.398  1.00 24.92           N  
ANISOU   75  NE2 GLN A  22     3369   2971   3127     33   -108    251       N  
ATOM     76  N   VAL A  23      14.433  26.969  97.465  1.00 21.84           N  
ANISOU   76  N   VAL A  23     2760   2641   2898    -72     36      3       N  
ATOM     77  CA  VAL A  23      15.101  26.261  98.544  1.00 21.69           C  
ANISOU   77  CA  VAL A  23     2748   2634   2860    -22     57      0       C  
ATOM     78  C   VAL A  23      15.873  27.265  99.380  1.00 21.48           C  
ANISOU   78  C   VAL A  23     2670   2635   2856     34     45     62       C  
ATOM     79  O   VAL A  23      16.692  28.027  98.858  1.00 20.48           O  
ANISOU   79  O   VAL A  23     2507   2490   2786    -33    160     97       O  
ATOM     80  CB  VAL A  23      16.089  25.217  97.988  1.00 22.06           C  
ANISOU   80  CB  VAL A  23     2846   2667   2869     -7      2     14       C  
ATOM     81  CG1 VAL A  23      16.934  24.605  99.106  1.00 21.82           C  
ANISOU   81  CG1 VAL A  23     2742   2687   2860     30     75    -70       C  
ATOM     82  CG2 VAL A  23      15.308  24.167  97.214  1.00 22.93           C  
ANISOU   82  CG2 VAL A  23     2997   2698   3016      8    -51      4       C  
ATOM     83  N   PRO A  24      15.608  27.278 100.688  1.00 21.27           N  
ANISOU   83  N   PRO A  24     2677   2619   2785     39     49     71       N  
ATOM     84  CA  PRO A  24      16.326  28.224 101.517  1.00 21.38           C  
ANISOU   84  CA  PRO A  24     2718   2588   2817     16     12     62       C  
ATOM     85  C   PRO A  24      17.847  28.124 101.377  1.00 21.52           C  
ANISOU   85  C   PRO A  24     2741   2599   2837      3     29     46       C  
ATOM     86  O   PRO A  24      18.409  27.023 101.319  1.00 21.15           O  
ANISOU   86  O   PRO A  24     2803   2435   2797    -24     14     68       O  
ATOM     87  CB  PRO A  24      15.863  27.872 102.933  1.00 21.32           C  
ANISOU   87  CB  PRO A  24     2717   2596   2787     38      2     67       C  
ATOM     88  CG  PRO A  24      14.548  27.171 102.757  1.00 21.24           C  
ANISOU   88  CG  PRO A  24     2658   2651   2761     51    -31    112       C  
ATOM     89  CD  PRO A  24      14.692  26.419 101.469  1.00 21.33           C  
ANISOU   89  CD  PRO A  24     2650   2631   2822     43     41     63       C  
ATOM     90  N   ARG A  25      18.506  29.278 101.285  1.00 21.90           N  
ANISOU   90  N   ARG A  25     2811   2619   2891    -47    -18     -8       N  
ATOM     91  CA  ARG A  25      19.961  29.312 101.150  1.00 22.58           C  
ANISOU   91  CA  ARG A  25     2876   2703   2999    -76     -5    -13       C  
ATOM     92  C   ARG A  25      20.680  28.630 102.314  1.00 22.85           C  
ANISOU   92  C   ARG A  25     2911   2777   2994    -82    -47    -60       C  
ATOM     93  O   ARG A  25      21.832  28.221 102.186  1.00 23.06           O  
ANISOU   93  O   ARG A  25     2992   2809   2961    -96    -82   -146       O  
ATOM     94  CB  ARG A  25      20.461  30.757 101.062  1.00 23.03           C  
ANISOU   94  CB  ARG A  25     2947   2744   3059    -87    -27    -36       C  
ATOM     95  CG  ARG A  25      20.038  31.502  99.839  1.00 22.88           C  
ANISOU   95  CG  ARG A  25     2982   2728   2982   -184     -3    -43       C  
ATOM     96  CD  ARG A  25      20.675  32.913  99.812  1.00 23.36           C  
ANISOU   96  CD  ARG A  25     3058   2786   3032   -120    -44    -83       C  
ATOM     97  NE  ARG A  25      19.960  33.741  98.867  1.00 23.49           N  
ANISOU   97  NE  ARG A  25     3218   2728   2980   -187    118    -51       N  
ATOM     98  CZ  ARG A  25      20.197  33.740  97.561  1.00 24.66           C  
ANISOU   98  CZ  ARG A  25     3197   3017   3157    -66      0    -18       C  
ATOM     99  NH1 ARG A  25      21.149  32.969  97.053  1.00 24.72           N  
ANISOU   99  NH1 ARG A  25     3238   2895   3261     30     91     -8       N  
ATOM    100  NH2 ARG A  25      19.485  34.516  96.770  1.00 23.63           N  
ANISOU  100  NH2 ARG A  25     3206   2753   3019    -32    -58    121       N  
ATOM    101  N   THR A  26      20.020  28.511 103.454  1.00 23.42           N  
ANISOU  101  N   THR A  26     2996   2864   3038    -54    -43    -32       N  
ATOM    102  CA  THR A  26      20.628  27.863 104.607  1.00 24.96           C  
ANISOU  102  CA  THR A  26     3203   3108   3171     -5    -16     24       C  
ATOM    103  C   THR A  26      20.582  26.331 104.545  1.00 24.92           C  
ANISOU  103  C   THR A  26     3219   3087   3161    -10    -36     57       C  
ATOM    104  O   THR A  26      21.211  25.647 105.355  1.00 25.31           O  
ANISOU  104  O   THR A  26     3278   3079   3259     16   -138    102       O  
ATOM    105  CB  THR A  26      19.936  28.305 105.900  1.00 25.16           C  
ANISOU  105  CB  THR A  26     3268   3126   3165     -7      7     21       C  
ATOM    106  OG1 THR A  26      18.538  28.037 105.780  1.00 26.11           O  
ANISOU  106  OG1 THR A  26     3345   3391   3186    238    105     44       O  
ATOM    107  CG2 THR A  26      20.163  29.794 106.164  1.00 27.55           C  
ANISOU  107  CG2 THR A  26     3598   3424   3447     15    -39      9       C  
ATOM    108  N   TRP A  27      19.841  25.778 103.601  1.00 24.74           N  
ANISOU  108  N   TRP A  27     3162   3104   3133    -13    -22    110       N  
ATOM    109  CA  TRP A  27      19.707  24.332 103.526  1.00 25.03           C  
ANISOU  109  CA  TRP A  27     3191   3142   3178     38      5     76       C  
ATOM    110  C   TRP A  27      20.922  23.698 102.851  1.00 25.56           C  
ANISOU  110  C   TRP A  27     3241   3201   3269     38      3    116       C  
ATOM    111  O   TRP A  27      21.461  24.234 101.889  1.00 25.34           O  
ANISOU  111  O   TRP A  27     3050   3172   3406     89    126    152       O  
ATOM    112  CB  TRP A  27      18.412  23.956 102.802  1.00 25.37           C  
ANISOU  112  CB  TRP A  27     3260   3114   3267      9     -9     65       C  
ATOM    113  CG  TRP A  27      17.194  23.949 103.687  1.00 24.92           C  
ANISOU  113  CG  TRP A  27     3249   3084   3137      0      5     79       C  
ATOM    114  CD1 TRP A  27      16.942  24.773 104.740  1.00 25.23           C  
ANISOU  114  CD1 TRP A  27     3322   2990   3273      0    -24     99       C  
ATOM    115  CD2 TRP A  27      16.051  23.076 103.580  1.00 25.37           C  
ANISOU  115  CD2 TRP A  27     3270   3087   3284     28    -33     58       C  
ATOM    116  NE1 TRP A  27      15.727  24.462 105.308  1.00 25.61           N  
ANISOU  116  NE1 TRP A  27     3313   3216   3201    -21    -43    -30       N  
ATOM    117  CE2 TRP A  27      15.159  23.427 104.611  1.00 26.40           C  
ANISOU  117  CE2 TRP A  27     3432   3274   3325    -65     39     20       C  
ATOM    118  CE3 TRP A  27      15.699  22.044 102.711  1.00 25.22           C  
ANISOU  118  CE3 TRP A  27     3292   3145   3144     64     49     21       C  
ATOM    119  CZ2 TRP A  27      13.939  22.777 104.802  1.00 27.05           C  
ANISOU  119  CZ2 TRP A  27     3445   3434   3400    -48     33    -65       C  
ATOM    120  CZ3 TRP A  27      14.488  21.387 102.904  1.00 26.24           C  
ANISOU  120  CZ3 TRP A  27     3383   3165   3423     86     50    -31       C  
ATOM    121  CH2 TRP A  27      13.619  21.758 103.943  1.00 27.24           C  
ANISOU  121  CH2 TRP A  27     3599   3340   3411     -6    102     28       C  
ATOM    122  N   SER A  28      21.363  22.552 103.355  1.00 25.23           N  
ANISOU  122  N   SER A  28     3184   3152   3250     32    -48    134       N  
ATOM    123  CA  SER A  28      22.414  21.831 102.679  1.00 25.50           C  
ANISOU  123  CA  SER A  28     3235   3188   3265     26    -88    115       C  
ATOM    124  C   SER A  28      21.847  20.578 102.057  1.00 24.98           C  
ANISOU  124  C   SER A  28     3132   3125   3234     13    -51    144       C  
ATOM    125  O   SER A  28      20.655  20.283 102.163  1.00 24.32           O  
ANISOU  125  O   SER A  28     2985   3034   3220    -22    -66    220       O  
ATOM    126  CB  SER A  28      23.496  21.414 103.666  1.00 26.58           C  
ANISOU  126  CB  SER A  28     3363   3332   3405     41    -72    111       C  
ATOM    127  OG  SER A  28      22.970  20.404 104.505  1.00 28.25           O  
ANISOU  127  OG  SER A  28     3887   3387   3458     60   -152    269       O  
ATOM    128  N   GLU A  29      22.736  19.846 101.404  1.00 24.46           N  
ANISOU  128  N   GLU A  29     3059   3061   3174    -24    -41    131       N  
ATOM    129  CA  GLU A  29      22.404  18.595 100.767  1.00 24.26           C  
ANISOU  129  CA  GLU A  29     3042   3056   3119    -18    -60     93       C  
ATOM    130  C   GLU A  29      21.705  17.646 101.749  1.00 24.77           C  
ANISOU  130  C   GLU A  29     3093   3083   3237      1    -24     71       C  
ATOM    131  O   GLU A  29      20.755  16.926 101.383  1.00 23.74           O  
ANISOU  131  O   GLU A  29     2855   2855   3309   -102    -26    193       O  
ATOM    132  CB  GLU A  29      23.687  17.972 100.215  1.00 24.06           C  
ANISOU  132  CB  GLU A  29     3029   3080   3031     17    -58     75       C  
ATOM    133  CG  GLU A  29      24.173  18.520  98.854  1.00 24.53           C  
ANISOU  133  CG  GLU A  29     3072   3040   3209    -26      0     88       C  
ATOM    134  CD  GLU A  29      25.013  19.796  98.893  1.00 25.06           C  
ANISOU  134  CD  GLU A  29     3127   3210   3186    -83     40     89       C  
ATOM    135  OE1 GLU A  29      25.238  20.392  99.967  1.00 23.06           O  
ANISOU  135  OE1 GLU A  29     2676   2776   3309   -308     45    110       O  
ATOM    136  OE2 GLU A  29      25.446  20.212  97.790  1.00 25.82           O  
ANISOU  136  OE2 GLU A  29     3016   3154   3640     76     63    405       O  
ATOM    137  N   LYS A  30      22.165  17.637 102.997  1.00 25.03           N  
ANISOU  137  N   LYS A  30     3106   3116   3290     15    -25     71       N  
ATOM    138  CA  LYS A  30      21.589  16.711 103.969  1.00 26.41           C  
ANISOU  138  CA  LYS A  30     3303   3287   3446     12     -6     61       C  
ATOM    139  C   LYS A  30      20.100  16.974 104.176  1.00 25.95           C  
ANISOU  139  C   LYS A  30     3245   3155   3461     25     10     55       C  
ATOM    140  O   LYS A  30      19.281  16.052 104.093  1.00 25.27           O  
ANISOU  140  O   LYS A  30     3292   2867   3443     60    100    223       O  
ATOM    141  CB  LYS A  30      22.324  16.779 105.305  1.00 27.50           C  
ANISOU  141  CB  LYS A  30     3411   3483   3556     49    -12     40       C  
ATOM    142  CG  LYS A  30      21.853  15.707 106.274  1.00 30.12           C  
ANISOU  142  CG  LYS A  30     3749   3778   3918     37     21    119       C  
ATOM    143  CD  LYS A  30      22.224  16.068 107.690  1.00 34.26           C  
ANISOU  143  CD  LYS A  30     4374   4412   4233     49      0    -61       C  
ATOM    144  CE  LYS A  30      23.499  16.877 107.726  1.00 36.64           C  
ANISOU  144  CE  LYS A  30     4619   4699   4605    -29     -8    -10       C  
ATOM    145  NZ  LYS A  30      23.782  17.426 109.094  1.00 39.60           N  
ANISOU  145  NZ  LYS A  30     5072   5151   4824    -31      1   -131       N  
ATOM    146  N   ASP A  31      19.754  18.242 104.393  1.00 25.87           N  
ANISOU  146  N   ASP A  31     3280   3086   3462    -28     22      0       N  
ATOM    147  CA  ASP A  31      18.358  18.678 104.550  1.00 25.46           C  
ANISOU  147  CA  ASP A  31     3197   3089   3388    -11     -5     43       C  
ATOM    148  C   ASP A  31      17.522  18.339 103.310  1.00 24.79           C  
ANISOU  148  C   ASP A  31     3122   2980   3318      6     17     25       C  
ATOM    149  O   ASP A  31      16.371  17.889 103.403  1.00 24.96           O  
ANISOU  149  O   ASP A  31     3111   3037   3335     -1     -4     70       O  
ATOM    150  CB  ASP A  31      18.289  20.196 104.771  1.00 25.97           C  
ANISOU  150  CB  ASP A  31     3286   3183   3400    -13     12      6       C  
ATOM    151  CG  ASP A  31      19.104  20.658 105.951  1.00 28.63           C  
ANISOU  151  CG  ASP A  31     3667   3553   3658    -56    -46     45       C  
ATOM    152  OD1 ASP A  31      18.972  20.078 107.044  1.00 34.25           O  
ANISOU  152  OD1 ASP A  31     4565   4545   3904   -186      9     56       O  
ATOM    153  OD2 ASP A  31      19.897  21.596 105.790  1.00 29.86           O  
ANISOU  153  OD2 ASP A  31     3983   3576   3787   -134   -188     62       O  
ATOM    154  N   LEU A  32      18.091  18.565 102.137  1.00 23.64           N  
ANISOU  154  N   LEU A  32     2939   2803   3242    -14    -10     57       N  
ATOM    155  CA  LEU A  32      17.381  18.264 100.906  1.00 23.11           C  
ANISOU  155  CA  LEU A  32     2926   2687   3166     -4      5     22       C  
ATOM    156  C   LEU A  32      17.150  16.759 100.678  1.00 23.42           C  
ANISOU  156  C   LEU A  32     2978   2674   3245    -27    -21     49       C  
ATOM    157  O   LEU A  32      16.068  16.359 100.250  1.00 22.05           O  
ANISOU  157  O   LEU A  32     2870   2314   3194    -79     45    108       O  
ATOM    158  CB  LEU A  32      18.102  18.888  99.732  1.00 22.82           C  
ANISOU  158  CB  LEU A  32     2903   2672   3094    -20     -8     23       C  
ATOM    159  CG  LEU A  32      17.988  20.417  99.765  1.00 21.97           C  
ANISOU  159  CG  LEU A  32     2752   2606   2991     -7      6     88       C  
ATOM    160  CD1 LEU A  32      19.135  21.041  99.012  1.00 22.19           C  
ANISOU  160  CD1 LEU A  32     2802   2680   2949     -1      2     38       C  
ATOM    161  CD2 LEU A  32      16.650  20.872  99.220  1.00 22.46           C  
ANISOU  161  CD2 LEU A  32     2946   2556   3031   -158    -78    224       C  
ATOM    162  N   ARG A  33      18.171  15.943 100.926  1.00 24.08           N  
ANISOU  162  N   ARG A  33     3075   2797   3278    -30    -55     68       N  
ATOM    163  CA  ARG A  33      18.022  14.491 100.786  1.00 25.04           C  
ANISOU  163  CA  ARG A  33     3223   2957   3333      2    -58     35       C  
ATOM    164  C   ARG A  33      16.838  14.008 101.617  1.00 25.80           C  
ANISOU  164  C   ARG A  33     3317   3044   3441     10    -61     70       C  
ATOM    165  O   ARG A  33      15.984  13.265 101.123  1.00 26.39           O  
ANISOU  165  O   ARG A  33     3384   3187   3456    -32    -71    105       O  
ATOM    166  CB  ARG A  33      19.295  13.770 101.214  1.00 25.48           C  
ANISOU  166  CB  ARG A  33     3230   3053   3399    -13    -37     19       C  
ATOM    167  CG  ARG A  33      19.178  12.247 101.144  1.00 27.28           C  
ANISOU  167  CG  ARG A  33     3436   3252   3677    -15    -42     34       C  
ATOM    168  CD  ARG A  33      20.519  11.547 101.270  1.00 30.53           C  
ANISOU  168  CD  ARG A  33     3737   3883   3981     35     27     56       C  
ATOM    169  NE  ARG A  33      21.333  11.650 100.058  1.00 31.75           N  
ANISOU  169  NE  ARG A  33     4006   3986   4070      3     16     56       N  
ATOM    170  CZ  ARG A  33      21.158  10.892  98.989  1.00 33.63           C  
ANISOU  170  CZ  ARG A  33     4236   4301   4239     -7     12     10       C  
ATOM    171  NH1 ARG A  33      20.180   9.998  98.971  1.00 34.11           N  
ANISOU  171  NH1 ARG A  33     4276   4295   4388   -143    106      7       N  
ATOM    172  NH2 ARG A  33      21.942  11.041  97.932  1.00 34.77           N  
ANISOU  172  NH2 ARG A  33     4203   4512   4495    -49     86     97       N  
ATOM    173  N   GLU A  34      16.784  14.449 102.870  1.00 26.61           N  
ANISOU  173  N   GLU A  34     3447   3190   3475     -7    -81     74       N  
ATOM    174  CA  GLU A  34      15.690  14.140 103.787  1.00 28.11           C  
ANISOU  174  CA  GLU A  34     3622   3401   3657    -13    -24     79       C  
ATOM    175  C   GLU A  34      14.317  14.523 103.229  1.00 27.28           C  
ANISOU  175  C   GLU A  34     3542   3289   3533    -68    -53    118       C  
ATOM    176  O   GLU A  34      13.347  13.774 103.354  1.00 26.97           O  
ANISOU  176  O   GLU A  34     3637   3141   3470   -160     99    330       O  
ATOM    177  CB  GLU A  34      15.875  14.908 105.092  1.00 29.54           C  
ANISOU  177  CB  GLU A  34     3802   3634   3786    -20    -39     42       C  
ATOM    178  CG  GLU A  34      16.402  14.138 106.280  1.00 34.85           C  
ANISOU  178  CG  GLU A  34     4585   4333   4325     21    -39     78       C  
ATOM    179  CD  GLU A  34      17.805  13.650 106.083  1.00 39.90           C  
ANISOU  179  CD  GLU A  34     4980   5132   5050    118     26    -25       C  
ATOM    180  OE1 GLU A  34      18.634  13.793 107.015  1.00 43.81           O  
ANISOU  180  OE1 GLU A  34     5688   5555   5402    -27    -64   -106       O  
ATOM    181  OE2 GLU A  34      18.077  13.124 104.983  1.00 45.59           O  
ANISOU  181  OE2 GLU A  34     5985   5866   5471     87    -42    -93       O  
ATOM    182  N   LEU A  35      14.215  15.712 102.648  1.00 25.51           N  
ANISOU  182  N   LEU A  35     3371   2986   3336   -111     -6    136       N  
ATOM    183  CA  LEU A  35      12.939  16.162 102.087  1.00 25.25           C  
ANISOU  183  CA  LEU A  35     3302   2976   3316    -92      3     88       C  
ATOM    184  C   LEU A  35      12.494  15.271 100.926  1.00 24.27           C  
ANISOU  184  C   LEU A  35     3195   2798   3227    -64     15     88       C  
ATOM    185  O   LEU A  35      11.334  14.815 100.872  1.00 24.72           O  
ANISOU  185  O   LEU A  35     3192   2882   3319    -25     76    -50       O  
ATOM    186  CB  LEU A  35      13.051  17.613 101.597  1.00 25.28           C  
ANISOU  186  CB  LEU A  35     3308   2985   3313    -88    -12     92       C  
ATOM    187  CG  LEU A  35      11.869  18.128 100.774  1.00 27.16           C  
ANISOU  187  CG  LEU A  35     3492   3342   3486    -64    -14     52       C  
ATOM    188  CD1 LEU A  35      10.644  18.300 101.667  1.00 29.47           C  
ANISOU  188  CD1 LEU A  35     3701   3728   3767     -3    -28    -14       C  
ATOM    189  CD2 LEU A  35      12.213  19.436 100.070  1.00 28.45           C  
ANISOU  189  CD2 LEU A  35     3774   3500   3534     -8   -142     82       C  
ATOM    190  N   PHE A  36      13.414  15.011 100.001  1.00 23.18           N  
ANISOU  190  N   PHE A  36     3093   2553   3162   -126     -7    151       N  
ATOM    191  CA  PHE A  36      13.063  14.335  98.765  1.00 22.76           C  
ANISOU  191  CA  PHE A  36     3072   2550   3024    -54     22    143       C  
ATOM    192  C   PHE A  36      12.853  12.844  98.953  1.00 23.16           C  
ANISOU  192  C   PHE A  36     3084   2605   3111    -91      0    139       C  
ATOM    193  O   PHE A  36      12.054  12.243  98.222  1.00 22.84           O  
ANISOU  193  O   PHE A  36     3174   2415   3089    -98     19    245       O  
ATOM    194  CB  PHE A  36      14.115  14.587  97.695  1.00 22.88           C  
ANISOU  194  CB  PHE A  36     3028   2543   3122    -31     25    115       C  
ATOM    195  CG  PHE A  36      14.131  16.009  97.218  1.00 22.42           C  
ANISOU  195  CG  PHE A  36     3083   2536   2899    -85     24     93       C  
ATOM    196  CD1 PHE A  36      12.960  16.605  96.799  1.00 24.11           C  
ANISOU  196  CD1 PHE A  36     3383   2583   3196    -54    101     99       C  
ATOM    197  CD2 PHE A  36      15.301  16.743  97.219  1.00 24.71           C  
ANISOU  197  CD2 PHE A  36     3423   2838   3127     23     35     81       C  
ATOM    198  CE1 PHE A  36      12.950  17.924  96.370  1.00 25.36           C  
ANISOU  198  CE1 PHE A  36     3513   2904   3219     28     58    155       C  
ATOM    199  CE2 PHE A  36      15.294  18.061  96.790  1.00 24.97           C  
ANISOU  199  CE2 PHE A  36     3514   2846   3128    -30     15     54       C  
ATOM    200  CZ  PHE A  36      14.110  18.637  96.376  1.00 24.16           C  
ANISOU  200  CZ  PHE A  36     3346   2752   3080     -7    -14    118       C  
ATOM    201  N   GLU A  37      13.567  12.271  99.925  1.00 23.33           N  
ANISOU  201  N   GLU A  37     3063   2663   3139    -81     14    141       N  
ATOM    202  CA  GLU A  37      13.500  10.834 100.172  1.00 24.23           C  
ANISOU  202  CA  GLU A  37     3131   2853   3221    -33      5    121       C  
ATOM    203  C   GLU A  37      12.127  10.412 100.684  1.00 24.84           C  
ANISOU  203  C   GLU A  37     3169   2969   3300    -41      3    151       C  
ATOM    204  O   GLU A  37      11.776   9.237 100.620  1.00 24.11           O  
ANISOU  204  O   GLU A  37     3138   2918   3106    -22    -97    168       O  
ATOM    205  CB  GLU A  37      14.631  10.387 101.111  1.00 24.55           C  
ANISOU  205  CB  GLU A  37     3172   2884   3271    -66     40    122       C  
ATOM    206  CG  GLU A  37      15.905  10.088 100.322  1.00 25.07           C  
ANISOU  206  CG  GLU A  37     3227   2929   3369    -31     33      7       C  
ATOM    207  CD  GLU A  37      17.057   9.666 101.188  1.00 26.81           C  
ANISOU  207  CD  GLU A  37     3370   3262   3554    -82     84    -11       C  
ATOM    208  OE1 GLU A  37      16.987   9.855 102.413  1.00 28.01           O  
ANISOU  208  OE1 GLU A  37     3448   3767   3427   -161     93    229       O  
ATOM    209  OE2 GLU A  37      18.060   9.183 100.634  1.00 28.55           O  
ANISOU  209  OE2 GLU A  37     3698   3114   4036    117    265     19       O  
ATOM    210  N   GLN A  38      11.339  11.372 101.158  1.00 25.98           N  
ANISOU  210  N   GLN A  38     3314   3095   3464    -54     76    151       N  
ATOM    211  CA  GLN A  38       9.927  11.110 101.468  1.00 27.79           C  
ANISOU  211  CA  GLN A  38     3487   3368   3704     12     17    139       C  
ATOM    212  C   GLN A  38       9.151  10.560 100.289  1.00 27.31           C  
ANISOU  212  C   GLN A  38     3437   3289   3652     13    -21    167       C  
ATOM    213  O   GLN A  38       8.143   9.864 100.476  1.00 27.95           O  
ANISOU  213  O   GLN A  38     3505   3294   3822     52    -89    319       O  
ATOM    214  CB  GLN A  38       9.222  12.389 101.896  1.00 28.66           C  
ANISOU  214  CB  GLN A  38     3580   3503   3807      0     79     87       C  
ATOM    215  CG  GLN A  38       9.990  13.207 102.854  1.00 32.33           C  
ANISOU  215  CG  GLN A  38     4057   3996   4230    -34     13    -14       C  
ATOM    216  CD  GLN A  38       9.447  13.130 104.231  1.00 35.10           C  
ANISOU  216  CD  GLN A  38     4548   4307   4481     15     72    116       C  
ATOM    217  OE1 GLN A  38       9.819  12.243 104.997  1.00 39.74           O  
ANISOU  217  OE1 GLN A  38     5238   4392   5470    228   -115     98       O  
ATOM    218  NE2 GLN A  38       8.567  14.073 104.583  1.00 34.36           N  
ANISOU  218  NE2 GLN A  38     4630   3776   4650     42     26    200       N  
ATOM    219  N   TYR A  39       9.586  10.891  99.077  1.00 27.09           N  
ANISOU  219  N   TYR A  39     3408   3240   3644    -42    -19    197       N  
ATOM    220  CA  TYR A  39       8.791  10.604  97.889  1.00 27.38           C  
ANISOU  220  CA  TYR A  39     3537   3314   3553    -66     -7    166       C  
ATOM    221  C   TYR A  39       9.389   9.501  97.032  1.00 26.81           C  
ANISOU  221  C   TYR A  39     3475   3292   3420   -108      8    229       C  
ATOM    222  O   TYR A  39       8.681   8.803  96.309  1.00 27.58           O  
ANISOU  222  O   TYR A  39     3557   3349   3575   -266    -34    266       O  
ATOM    223  CB  TYR A  39       8.526  11.896  97.084  1.00 27.41           C  
ANISOU  223  CB  TYR A  39     3532   3320   3561    -85     -8    133       C  
ATOM    224  CG  TYR A  39       7.949  12.966  97.986  1.00 28.59           C  
ANISOU  224  CG  TYR A  39     3629   3460   3775    -66      9     37       C  
ATOM    225  CD1 TYR A  39       6.620  12.925  98.391  1.00 28.51           C  
ANISOU  225  CD1 TYR A  39     3622   3482   3728    -52    -64      0       C  
ATOM    226  CD2 TYR A  39       8.749  13.991  98.473  1.00 29.40           C  
ANISOU  226  CD2 TYR A  39     3708   3633   3831   -105    -44    -21       C  
ATOM    227  CE1 TYR A  39       6.098  13.875  99.236  1.00 28.94           C  
ANISOU  227  CE1 TYR A  39     3554   3620   3821    -14    -62     24       C  
ATOM    228  CE2 TYR A  39       8.240  14.942  99.323  1.00 29.76           C  
ANISOU  228  CE2 TYR A  39     3730   3532   4044    -60     46    -23       C  
ATOM    229  CZ  TYR A  39       6.912  14.884  99.695  1.00 30.20           C  
ANISOU  229  CZ  TYR A  39     3776   3634   4065    -53     31    -32       C  
ATOM    230  OH  TYR A  39       6.406  15.827 100.548  1.00 32.00           O  
ANISOU  230  OH  TYR A  39     3850   3808   4502    -66     53    -96       O  
ATOM    231  N   GLY A  40      10.694   9.323  97.123  1.00 26.25           N  
ANISOU  231  N   GLY A  40     3376   3240   3357   -147      2    220       N  
ATOM    232  CA  GLY A  40      11.357   8.287  96.356  1.00 25.80           C  
ANISOU  232  CA  GLY A  40     3345   3215   3242   -157     32    113       C  
ATOM    233  C   GLY A  40      12.851   8.298  96.621  1.00 25.56           C  
ANISOU  233  C   GLY A  40     3316   3189   3208   -138     21    109       C  
ATOM    234  O   GLY A  40      13.374   9.265  97.192  1.00 25.87           O  
ANISOU  234  O   GLY A  40     3330   3229   3270   -176     29     67       O  
ATOM    235  N   ALA A  41      13.534   7.248  96.176  1.00 24.70           N  
ANISOU  235  N   ALA A  41     3205   3000   3179   -156     45    139       N  
ATOM    236  CA  ALA A  41      14.967   7.089  96.406  1.00 24.88           C  
ANISOU  236  CA  ALA A  41     3229   3029   3197   -148     24    107       C  
ATOM    237  C   ALA A  41      15.756   8.149  95.645  1.00 24.46           C  
ANISOU  237  C   ALA A  41     3194   2951   3149   -157     16    144       C  
ATOM    238  O   ALA A  41      15.474   8.429  94.476  1.00 24.28           O  
ANISOU  238  O   ALA A  41     3304   2794   3128   -251     60    147       O  
ATOM    239  CB  ALA A  41      15.432   5.727  95.967  1.00 24.65           C  
ANISOU  239  CB  ALA A  41     3188   2982   3196   -153     51    116       C  
ATOM    240  N   VAL A  42      16.762   8.700  96.308  1.00 24.48           N  
ANISOU  240  N   VAL A  42     3208   2934   3159   -114     -7    138       N  
ATOM    241  CA  VAL A  42      17.575   9.763  95.721  1.00 24.30           C  
ANISOU  241  CA  VAL A  42     3137   2962   3135   -105      8     95       C  
ATOM    242  C   VAL A  42      18.988   9.283  95.434  1.00 25.03           C  
ANISOU  242  C   VAL A  42     3255   2989   3265    -60    -16     79       C  
ATOM    243  O   VAL A  42      19.688   8.779  96.319  1.00 25.00           O  
ANISOU  243  O   VAL A  42     3333   2862   3303    -57    -18     29       O  
ATOM    244  CB  VAL A  42      17.568  10.977  96.639  1.00 24.28           C  
ANISOU  244  CB  VAL A  42     3089   2963   3174   -114      5    115       C  
ATOM    245  CG1 VAL A  42      18.628  12.007  96.227  1.00 24.52           C  
ANISOU  245  CG1 VAL A  42     3133   3040   3145   -167     48    115       C  
ATOM    246  CG2 VAL A  42      16.177  11.594  96.652  1.00 23.77           C  
ANISOU  246  CG2 VAL A  42     3040   2889   3103    -83     46     39       C  
ATOM    247  N   TYR A  43      19.405   9.431  94.181  1.00 26.16           N  
ANISOU  247  N   TYR A  43     3415   3087   3439     21      6     37       N  
ATOM    248  CA  TYR A  43      20.773   9.094  93.792  1.00 27.11           C  
ANISOU  248  CA  TYR A  43     3480   3224   3597      6     29     64       C  
ATOM    249  C   TYR A  43      21.754  10.170  94.229  1.00 26.93           C  
ANISOU  249  C   TYR A  43     3452   3202   3579     35     27     82       C  
ATOM    250  O   TYR A  43      22.792   9.876  94.808  1.00 26.04           O  
ANISOU  250  O   TYR A  43     3366   2897   3630     34     21    226       O  
ATOM    251  CB  TYR A  43      20.884   8.855  92.282  1.00 27.83           C  
ANISOU  251  CB  TYR A  43     3575   3328   3672     -9     -5     29       C  
ATOM    252  CG  TYR A  43      22.328   8.796  91.821  1.00 31.71           C  
ANISOU  252  CG  TYR A  43     3969   3906   4172     19     85    -17       C  
ATOM    253  CD1 TYR A  43      23.183   7.801  92.296  1.00 34.85           C  
ANISOU  253  CD1 TYR A  43     4305   4339   4596    110     -6     76       C  
ATOM    254  CD2 TYR A  43      22.848   9.746  90.951  1.00 34.62           C  
ANISOU  254  CD2 TYR A  43     4408   4316   4429     14     87     98       C  
ATOM    255  CE1 TYR A  43      24.504   7.746  91.911  1.00 36.65           C  
ANISOU  255  CE1 TYR A  43     4552   4559   4813     77    107     46       C  
ATOM    256  CE2 TYR A  43      24.177   9.696  90.555  1.00 37.02           C  
ANISOU  256  CE2 TYR A  43     4570   4661   4836     68    113     97       C  
ATOM    257  CZ  TYR A  43      24.999   8.690  91.042  1.00 38.54           C  
ANISOU  257  CZ  TYR A  43     4785   4869   4988     85    104     96       C  
ATOM    258  OH  TYR A  43      26.326   8.616  90.667  1.00 41.46           O  
ANISOU  258  OH  TYR A  43     4874   5343   5537     87    150     90       O  
ATOM    259  N   GLU A  44      21.418  11.433  93.975  1.00 26.98           N  
ANISOU  259  N   GLU A  44     3484   3133   3634     21     49     56       N  
ATOM    260  CA  GLU A  44      22.352  12.499  94.264  1.00 27.46           C  
ANISOU  260  CA  GLU A  44     3557   3202   3674     33     51     31       C  
ATOM    261  C   GLU A  44      21.627  13.828  94.455  1.00 26.08           C  
ANISOU  261  C   GLU A  44     3398   2965   3547      6     36     70       C  
ATOM    262  O   GLU A  44      20.598  14.064  93.840  1.00 23.70           O  
ANISOU  262  O   GLU A  44     3205   2375   3424    -19     87    143       O  
ATOM    263  CB  GLU A  44      23.347  12.583  93.112  1.00 28.80           C  
ANISOU  263  CB  GLU A  44     3722   3386   3835     28     79      5       C  
ATOM    264  CG  GLU A  44      24.208  13.804  93.068  1.00 32.11           C  
ANISOU  264  CG  GLU A  44     4018   3968   4214    -81      0    -23       C  
ATOM    265  CD  GLU A  44      25.264  13.686  91.985  1.00 35.94           C  
ANISOU  265  CD  GLU A  44     4458   4713   4483     -9     90    -45       C  
ATOM    266  OE1 GLU A  44      24.906  13.593  90.788  1.00 39.28           O  
ANISOU  266  OE1 GLU A  44     4931   5260   4732    -33     -3     46       O  
ATOM    267  OE2 GLU A  44      26.455  13.667  92.337  1.00 38.01           O  
ANISOU  267  OE2 GLU A  44     4558   5098   4787     18     23    -11       O  
ATOM    268  N   ILE A  45      22.175  14.656  95.336  1.00 25.60           N  
ANISOU  268  N   ILE A  45     3302   2932   3492      3     19     80       N  
ATOM    269  CA  ILE A  45      21.711  16.023  95.545  1.00 25.59           C  
ANISOU  269  CA  ILE A  45     3253   2969   3500      0     13     42       C  
ATOM    270  C   ILE A  45      22.924  16.944  95.392  1.00 25.38           C  
ANISOU  270  C   ILE A  45     3228   2907   3509     -2    -12     38       C  
ATOM    271  O   ILE A  45      24.029  16.619  95.844  1.00 24.83           O  
ANISOU  271  O   ILE A  45     3189   2634   3610    -76    -50     35       O  
ATOM    272  CB  ILE A  45      21.148  16.257  96.961  1.00 26.16           C  
ANISOU  272  CB  ILE A  45     3332   3106   3502    -20    -17     40       C  
ATOM    273  CG1 ILE A  45      19.956  15.358  97.281  1.00 28.22           C  
ANISOU  273  CG1 ILE A  45     3488   3427   3806    -22    -20     49       C  
ATOM    274  CG2 ILE A  45      20.735  17.706  97.122  1.00 25.44           C  
ANISOU  274  CG2 ILE A  45     3177   3130   3360    -14     83      2       C  
ATOM    275  CD1 ILE A  45      18.671  15.793  96.619  1.00 31.18           C  
ANISOU  275  CD1 ILE A  45     3909   3846   4091     -3    -34     79       C  
ATOM    276  N   ASN A  46      22.712  18.083  94.744  1.00 25.11           N  
ANISOU  276  N   ASN A  46     3189   2887   3464      6     39     28       N  
ATOM    277  CA  ASN A  46      23.776  19.042  94.481  1.00 25.40           C  
ANISOU  277  CA  ASN A  46     3249   2933   3470     62     51     36       C  
ATOM    278  C   ASN A  46      23.180  20.436  94.596  1.00 23.56           C  
ANISOU  278  C   ASN A  46     3017   2689   3247     38     49     43       C  
ATOM    279  O   ASN A  46      22.374  20.824  93.754  1.00 23.13           O  
ANISOU  279  O   ASN A  46     2913   2474   3401     84     99    115       O  
ATOM    280  CB  ASN A  46      24.318  18.818  93.066  1.00 26.63           C  
ANISOU  280  CB  ASN A  46     3459   3096   3563     87     56     39       C  
ATOM    281  CG  ASN A  46      25.316  19.864  92.636  1.00 30.42           C  
ANISOU  281  CG  ASN A  46     3817   3674   4069      2    115     43       C  
ATOM    282  OD1 ASN A  46      25.244  21.023  93.037  1.00 35.91           O  
ANISOU  282  OD1 ASN A  46     4695   4175   4774   -108     67      0       O  
ATOM    283  ND2 ASN A  46      26.253  19.459  91.796  1.00 37.31           N  
ANISOU  283  ND2 ASN A  46     4661   4794   4721     90    271     39       N  
ATOM    284  N   VAL A  47      23.540  21.154  95.652  1.00 22.39           N  
ANISOU  284  N   VAL A  47     2780   2564   3162     72     67    103       N  
ATOM    285  CA  VAL A  47      23.096  22.540  95.813  1.00 21.13           C  
ANISOU  285  CA  VAL A  47     2641   2445   2942     11     55     36       C  
ATOM    286  C   VAL A  47      23.923  23.392  94.865  1.00 20.53           C  
ANISOU  286  C   VAL A  47     2558   2385   2859     26     24     52       C  
ATOM    287  O   VAL A  47      25.144  23.258  94.820  1.00 20.70           O  
ANISOU  287  O   VAL A  47     2565   2303   2997     78    127    149       O  
ATOM    288  CB  VAL A  47      23.264  23.004  97.265  1.00 21.14           C  
ANISOU  288  CB  VAL A  47     2613   2482   2937      0     57     61       C  
ATOM    289  CG1 VAL A  47      23.070  24.516  97.370  1.00 20.29           C  
ANISOU  289  CG1 VAL A  47     2599   2367   2744     56      6     60       C  
ATOM    290  CG2 VAL A  47      22.286  22.268  98.195  1.00 21.80           C  
ANISOU  290  CG2 VAL A  47     2848   2500   2934     87     33     43       C  
ATOM    291  N   LEU A  48      23.277  24.257  94.092  1.00 20.35           N  
ANISOU  291  N   LEU A  48     2525   2469   2738    -37     53     62       N  
ATOM    292  CA  LEU A  48      24.004  25.137  93.189  1.00 19.81           C  
ANISOU  292  CA  LEU A  48     2462   2417   2647      0     38     66       C  
ATOM    293  C   LEU A  48      24.677  26.211  94.024  1.00 19.22           C  
ANISOU  293  C   LEU A  48     2451   2308   2543      6     38    126       C  
ATOM    294  O   LEU A  48      24.020  26.865  94.845  1.00 18.83           O  
ANISOU  294  O   LEU A  48     2306   2203   2644     37     76     98       O  
ATOM    295  CB  LEU A  48      23.069  25.781  92.172  1.00 20.33           C  
ANISOU  295  CB  LEU A  48     2542   2493   2691    -49     84     90       C  
ATOM    296  CG  LEU A  48      22.585  24.938  91.005  1.00 21.25           C  
ANISOU  296  CG  LEU A  48     2644   2673   2757     23     83    -33       C  
ATOM    297  CD1 LEU A  48      21.437  24.063  91.433  1.00 22.81           C  
ANISOU  297  CD1 LEU A  48     3000   2807   2858    -61    135    -98       C  
ATOM    298  CD2 LEU A  48      22.177  25.841  89.847  1.00 23.46           C  
ANISOU  298  CD2 LEU A  48     2847   3016   3050    104     87    -15       C  
ATOM    299  N   ARG A  49      25.980  26.398  93.817  1.00 18.07           N  
ANISOU  299  N   ARG A  49     2279   2209   2377     89      9    161       N  
ATOM    300  CA  ARG A  49      26.723  27.356  94.628  1.00 18.44           C  
ANISOU  300  CA  ARG A  49     2373   2234   2399     24     18    134       C  
ATOM    301  C   ARG A  49      27.324  28.521  93.841  1.00 18.03           C  
ANISOU  301  C   ARG A  49     2318   2206   2328     35     28    103       C  
ATOM    302  O   ARG A  49      27.568  28.412  92.644  1.00 17.65           O  
ANISOU  302  O   ARG A  49     2306   2058   2344     46     21    171       O  
ATOM    303  CB  ARG A  49      27.813  26.641  95.437  1.00 19.22           C  
ANISOU  303  CB  ARG A  49     2430   2373   2500     10      8    120       C  
ATOM    304  CG  ARG A  49      27.239  25.897  96.668  1.00 21.23           C  
ANISOU  304  CG  ARG A  49     2764   2605   2696      4     25    182       C  
ATOM    305  CD  ARG A  49      28.318  25.172  97.457  1.00 24.32           C  
ANISOU  305  CD  ARG A  49     2944   3229   3069    -65    -67    107       C  
ATOM    306  NE  ARG A  49      27.782  24.553  98.668  1.00 25.77           N  
ANISOU  306  NE  ARG A  49     3287   3222   3283    -52    -94    176       N  
ATOM    307  CZ  ARG A  49      27.153  23.385  98.674  1.00 27.48           C  
ANISOU  307  CZ  ARG A  49     3498   3419   3523    -74    -17     71       C  
ATOM    308  NH1 ARG A  49      26.995  22.719  97.537  1.00 26.66           N  
ANISOU  308  NH1 ARG A  49     3298   3416   3415    -94    -28    133       N  
ATOM    309  NH2 ARG A  49      26.687  22.885  99.814  1.00 28.10           N  
ANISOU  309  NH2 ARG A  49     3747   3462   3466    -65    -27     18       N  
ATOM    310  N   ASP A  50      27.519  29.620  94.570  1.00 17.59           N  
ANISOU  310  N   ASP A  50     2236   2130   2316     15     17    106       N  
ATOM    311  CA  ASP A  50      28.147  30.852  94.118  1.00 18.16           C  
ANISOU  311  CA  ASP A  50     2317   2205   2377     46     -3     23       C  
ATOM    312  C   ASP A  50      29.487  30.983  94.850  1.00 17.81           C  
ANISOU  312  C   ASP A  50     2310   2123   2335     23    -69     11       C  
ATOM    313  O   ASP A  50      29.531  31.097  96.095  1.00 17.13           O  
ANISOU  313  O   ASP A  50     2251   1921   2335    111   -105     24       O  
ATOM    314  CB  ASP A  50      27.198  32.016  94.433  1.00 18.18           C  
ANISOU  314  CB  ASP A  50     2382   2162   2362     12    -20    -10       C  
ATOM    315  CG  ASP A  50      27.772  33.384  94.130  1.00 18.99           C  
ANISOU  315  CG  ASP A  50     2406   2315   2496     59     20     35       C  
ATOM    316  OD1 ASP A  50      28.991  33.548  93.922  1.00 19.85           O  
ANISOU  316  OD1 ASP A  50     2331   2397   2813    -62   -146     62       O  
ATOM    317  OD2 ASP A  50      26.952  34.328  94.136  1.00 19.34           O  
ANISOU  317  OD2 ASP A  50     2504   1936   2909     52   -234     82       O  
ATOM    318  N   ARG A  51      30.571  30.920  94.080  1.00 18.00           N  
ANISOU  318  N   ARG A  51     2343   2139   2357    -12    -84      8       N  
ATOM    319  CA  ARG A  51      31.935  31.062  94.620  1.00 18.94           C  
ANISOU  319  CA  ARG A  51     2399   2312   2484     28    -53     61       C  
ATOM    320  C   ARG A  51      32.599  32.393  94.250  1.00 19.40           C  
ANISOU  320  C   ARG A  51     2442   2352   2576     11    -83     19       C  
ATOM    321  O   ARG A  51      33.826  32.511  94.213  1.00 20.28           O  
ANISOU  321  O   ARG A  51     2520   2376   2809     50    -84    129       O  
ATOM    322  CB  ARG A  51      32.800  29.877  94.171  1.00 19.10           C  
ANISOU  322  CB  ARG A  51     2428   2373   2457     20    -56     70       C  
ATOM    323  CG  ARG A  51      32.415  28.588  94.887  1.00 19.75           C  
ANISOU  323  CG  ARG A  51     2458   2353   2693    -42      6     35       C  
ATOM    324  CD  ARG A  51      33.192  27.371  94.378  1.00 21.36           C  
ANISOU  324  CD  ARG A  51     2691   2533   2890     24     -9    101       C  
ATOM    325  NE  ARG A  51      34.608  27.501  94.668  1.00 22.30           N  
ANISOU  325  NE  ARG A  51     2782   2569   3123    158   -200    130       N  
ATOM    326  CZ  ARG A  51      35.534  26.601  94.354  1.00 23.14           C  
ANISOU  326  CZ  ARG A  51     2800   2909   3083     86     -4    -65       C  
ATOM    327  NH1 ARG A  51      35.210  25.474  93.734  1.00 22.61           N  
ANISOU  327  NH1 ARG A  51     2732   2703   3154    319   -106     36       N  
ATOM    328  NH2 ARG A  51      36.788  26.835  94.691  1.00 23.55           N  
ANISOU  328  NH2 ARG A  51     2772   2958   3218    155    -70     48       N  
ATOM    329  N   SER A  52      31.797  33.418  93.990  1.00 20.12           N  
ANISOU  329  N   SER A  52     2559   2446   2639      3   -114     56       N  
ATOM    330  CA  SER A  52      32.361  34.693  93.550  1.00 20.14           C  
ANISOU  330  CA  SER A  52     2588   2409   2654    -33    -86     18       C  
ATOM    331  C   SER A  52      33.184  35.377  94.625  1.00 21.31           C  
ANISOU  331  C   SER A  52     2690   2588   2818    -18    -69     33       C  
ATOM    332  O   SER A  52      34.094  36.140  94.300  1.00 21.84           O  
ANISOU  332  O   SER A  52     2777   2662   2859   -117   -120    103       O  
ATOM    333  CB  SER A  52      31.266  35.631  93.071  1.00 20.34           C  
ANISOU  333  CB  SER A  52     2620   2381   2728    -43    -61     25       C  
ATOM    334  OG  SER A  52      30.359  35.875  94.118  1.00 19.48           O  
ANISOU  334  OG  SER A  52     2744   1962   2694    -58     40     63       O  
ATOM    335  N   GLN A  53      32.860  35.127  95.888  1.00 21.21           N  
ANISOU  335  N   GLN A  53     2646   2656   2756      4    -38      4       N  
ATOM    336  CA  GLN A  53      33.656  35.645  96.996  1.00 22.40           C  
ANISOU  336  CA  GLN A  53     2817   2767   2926     21    -57     -2       C  
ATOM    337  C   GLN A  53      33.604  34.643  98.131  1.00 23.00           C  
ANISOU  337  C   GLN A  53     2884   2848   3006     29   -109      6       C  
ATOM    338  O   GLN A  53      32.944  33.621  98.023  1.00 22.99           O  
ANISOU  338  O   GLN A  53     2742   2878   3114     -7   -207    150       O  
ATOM    339  CB  GLN A  53      33.182  37.041  97.454  1.00 22.49           C  
ANISOU  339  CB  GLN A  53     2823   2820   2903     37    -49    -17       C  
ATOM    340  CG  GLN A  53      31.752  37.112  97.965  1.00 22.41           C  
ANISOU  340  CG  GLN A  53     2921   2749   2846     36    -56    -18       C  
ATOM    341  CD  GLN A  53      31.414  38.494  98.476  1.00 21.09           C  
ANISOU  341  CD  GLN A  53     2677   2621   2716     43    -44     55       C  
ATOM    342  OE1 GLN A  53      31.542  39.481  97.757  1.00 23.53           O  
ANISOU  342  OE1 GLN A  53     3230   2721   2989     76   -176     79       O  
ATOM    343  NE2 GLN A  53      31.007  38.577  99.719  1.00 19.78           N  
ANISOU  343  NE2 GLN A  53     2815   2181   2520     47    -36     18       N  
ATOM    344  N   ASN A  54      34.334  34.922  99.202  1.00 24.01           N  
ANISOU  344  N   ASN A  54     3002   2991   3129     13   -155    -12       N  
ATOM    345  CA  ASN A  54      34.387  34.051 100.363  1.00 24.93           C  
ANISOU  345  CA  ASN A  54     3149   3086   3237    -11   -135     19       C  
ATOM    346  C   ASN A  54      33.318  34.395 101.394  1.00 24.58           C  
ANISOU  346  C   ASN A  54     3143   3038   3160    -23   -144      3       C  
ATOM    347  O   ASN A  54      33.170  35.559 101.773  1.00 25.47           O  
ANISOU  347  O   ASN A  54     3232   3150   3297    -27   -266     11       O  
ATOM    348  CB  ASN A  54      35.772  34.204 100.987  1.00 25.89           C  
ANISOU  348  CB  ASN A  54     3251   3306   3279     -8   -145     54       C  
ATOM    349  CG  ASN A  54      35.954  33.349 102.202  1.00 27.83           C  
ANISOU  349  CG  ASN A  54     3487   3505   3581    -21   -101     68       C  
ATOM    350  OD1 ASN A  54      35.928  32.129 102.108  1.00 31.15           O  
ANISOU  350  OD1 ASN A  54     3602   3809   4424    162    -55     72       O  
ATOM    351  ND2 ASN A  54      36.143  33.984 103.354  1.00 28.77           N  
ANISOU  351  ND2 ASN A  54     3583   4043   3304     40   -154    -42       N  
ATOM    352  N   PRO A  55      32.540  33.398 101.847  1.00 24.38           N  
ANISOU  352  N   PRO A  55     3161   3008   3096     45   -144      1       N  
ATOM    353  CA  PRO A  55      32.595  31.989 101.482  1.00 23.92           C  
ANISOU  353  CA  PRO A  55     3087   2885   3116      0   -148     14       C  
ATOM    354  C   PRO A  55      31.663  31.618 100.331  1.00 23.59           C  
ANISOU  354  C   PRO A  55     3054   2811   3100     58   -119     31       C  
ATOM    355  O   PRO A  55      30.802  32.412  99.983  1.00 22.70           O  
ANISOU  355  O   PRO A  55     2917   2627   3081     44   -200     98       O  
ATOM    356  CB  PRO A  55      32.089  31.314 102.749  1.00 24.15           C  
ANISOU  356  CB  PRO A  55     3116   2947   3114     40    -99    -34       C  
ATOM    357  CG  PRO A  55      31.069  32.241 103.268  1.00 25.43           C  
ANISOU  357  CG  PRO A  55     3296   3109   3256     33    -86      6       C  
ATOM    358  CD  PRO A  55      31.596  33.628 102.957  1.00 24.56           C  
ANISOU  358  CD  PRO A  55     3141   2984   3205    -29    -94     32       C  
ATOM    359  N   PRO A  56      31.797  30.392  99.785  1.00 23.00           N  
ANISOU  359  N   PRO A  56     2969   2745   3026     56    -93     -2       N  
ATOM    360  CA  PRO A  56      30.833  29.915  98.818  1.00 22.64           C  
ANISOU  360  CA  PRO A  56     2926   2676   3000     47    -53     10       C  
ATOM    361  C   PRO A  56      29.449  29.930  99.440  1.00 22.46           C  
ANISOU  361  C   PRO A  56     2967   2674   2893     33    -11    -27       C  
ATOM    362  O   PRO A  56      29.299  29.722 100.648  1.00 23.05           O  
ANISOU  362  O   PRO A  56     3075   2726   2957     40    -60     14       O  
ATOM    363  CB  PRO A  56      31.288  28.478  98.531  1.00 22.57           C  
ANISOU  363  CB  PRO A  56     2886   2678   3012     60    -17     16       C  
ATOM    364  CG  PRO A  56      32.723  28.464  98.925  1.00 22.90           C  
ANISOU  364  CG  PRO A  56     2901   2745   3054     61    -53      3       C  
ATOM    365  CD  PRO A  56      32.807  29.364 100.099  1.00 22.98           C  
ANISOU  365  CD  PRO A  56     2945   2722   3064     40    -44      5       C  
ATOM    366  N   GLN A  57      28.444  30.188  98.618  1.00 21.70           N  
ANISOU  366  N   GLN A  57     2791   2627   2828     22     10    -58       N  
ATOM    367  CA  GLN A  57      27.102  30.368  99.108  1.00 22.09           C  
ANISOU  367  CA  GLN A  57     2842   2688   2864    -36     -9    -27       C  
ATOM    368  C   GLN A  57      26.128  29.610  98.233  1.00 20.42           C  
ANISOU  368  C   GLN A  57     2573   2501   2683    -55      6    -28       C  
ATOM    369  O   GLN A  57      26.284  29.572  97.012  1.00 20.37           O  
ANISOU  369  O   GLN A  57     2508   2491   2741   -191    116    -48       O  
ATOM    370  CB  GLN A  57      26.736  31.846  99.043  1.00 22.66           C  
ANISOU  370  CB  GLN A  57     2825   2792   2991    -19      8   -132       C  
ATOM    371  CG  GLN A  57      25.381  32.099  99.581  1.00 27.13           C  
ANISOU  371  CG  GLN A  57     3458   3376   3476     22     20    -99       C  
ATOM    372  CD  GLN A  57      24.963  33.528  99.413  1.00 28.16           C  
ANISOU  372  CD  GLN A  57     3722   3262   3715     63     -4     29       C  
ATOM    373  OE1 GLN A  57      24.833  34.018  98.302  1.00 29.80           O  
ANISOU  373  OE1 GLN A  57     3926   3390   4007    -37    197     92       O  
ATOM    374  NE2 GLN A  57      24.670  34.175 100.515  1.00 32.12           N  
ANISOU  374  NE2 GLN A  57     4462   3709   4032    -11   -182   -119       N  
ATOM    375  N   SER A  58      25.100  29.047  98.856  1.00 19.23           N  
ANISOU  375  N   SER A  58     2559   2314   2434     -5      3     29       N  
ATOM    376  CA  SER A  58      23.963  28.501  98.119  1.00 17.65           C  
ANISOU  376  CA  SER A  58     2304   2079   2325      0      1      8       C  
ATOM    377  C   SER A  58      23.226  29.548  97.295  1.00 17.60           C  
ANISOU  377  C   SER A  58     2299   2078   2310    -12     -7    -27       C  
ATOM    378  O   SER A  58      22.944  30.654  97.774  1.00 17.06           O  
ANISOU  378  O   SER A  58     2407   1903   2172    103    -72    -49       O  
ATOM    379  CB  SER A  58      22.965  27.896  99.087  1.00 18.10           C  
ANISOU  379  CB  SER A  58     2392   2097   2388     26    -14    -13       C  
ATOM    380  OG  SER A  58      21.798  27.519  98.394  1.00 18.16           O  
ANISOU  380  OG  SER A  58     2227   2070   2604   -142     72    189       O  
ATOM    381  N   LYS A  59      22.852  29.164  96.078  1.00 17.01           N  
ANISOU  381  N   LYS A  59     2243   2000   2220     14     25     -2       N  
ATOM    382  CA  LYS A  59      22.065  30.010  95.194  1.00 17.60           C  
ANISOU  382  CA  LYS A  59     2217   2146   2323      8      1     -3       C  
ATOM    383  C   LYS A  59      20.569  29.799  95.388  1.00 17.79           C  
ANISOU  383  C   LYS A  59     2270   2152   2338     46    -10      1       C  
ATOM    384  O   LYS A  59      19.764  30.341  94.650  1.00 17.95           O  
ANISOU  384  O   LYS A  59     2132   2230   2460     70    -95    -21       O  
ATOM    385  CB  LYS A  59      22.478  29.757  93.744  1.00 18.20           C  
ANISOU  385  CB  LYS A  59     2331   2231   2352     35    -57      4       C  
ATOM    386  CG  LYS A  59      23.938  30.174  93.494  1.00 19.04           C  
ANISOU  386  CG  LYS A  59     2316   2346   2572     20     13     58       C  
ATOM    387  CD  LYS A  59      24.371  30.180  92.052  1.00 20.98           C  
ANISOU  387  CD  LYS A  59     2597   2567   2808     48   -130    -67       C  
ATOM    388  CE  LYS A  59      23.662  31.239  91.241  1.00 23.22           C  
ANISOU  388  CE  LYS A  59     2669   2824   3328     23    -57     47       C  
ATOM    389  NZ  LYS A  59      24.358  32.501  91.106  1.00 23.59           N  
ANISOU  389  NZ  LYS A  59     2600   2606   3759    174     37     43       N  
ATOM    390  N   GLY A  60      20.195  28.996  96.375  1.00 17.77           N  
ANISOU  390  N   GLY A  60     2245   2184   2324      6     85     20       N  
ATOM    391  CA  GLY A  60      18.782  28.897  96.756  1.00 18.33           C  
ANISOU  391  CA  GLY A  60     2264   2256   2445     69      1    107       C  
ATOM    392  C   GLY A  60      18.049  27.936  95.859  1.00 18.72           C  
ANISOU  392  C   GLY A  60     2300   2313   2501     20     34     97       C  
ATOM    393  O   GLY A  60      16.834  28.027  95.683  1.00 19.95           O  
ANISOU  393  O   GLY A  60     2358   2533   2689    111    -16    112       O  
ATOM    394  N   CYS A  61      18.808  27.015  95.279  1.00 19.37           N  
ANISOU  394  N   CYS A  61     2363   2402   2596     13     47     25       N  
ATOM    395  CA  CYS A  61      18.273  25.992  94.393  1.00 19.13           C  
ANISOU  395  CA  CYS A  61     2344   2312   2614    -52     19     11       C  
ATOM    396  C   CYS A  61      19.216  24.796  94.383  1.00 19.15           C  
ANISOU  396  C   CYS A  61     2359   2321   2596    -36      9     -5       C  
ATOM    397  O   CYS A  61      20.382  24.877  94.800  1.00 19.59           O  
ANISOU  397  O   CYS A  61     2416   2280   2749   -110     33    -37       O  
ATOM    398  CB  CYS A  61      18.080  26.528  92.963  1.00 19.35           C  
ANISOU  398  CB  CYS A  61     2352   2366   2633    -55     76      9       C  
ATOM    399  SG  CYS A  61      19.518  27.437  92.312  1.00 20.92           S  
ANISOU  399  SG  CYS A  61     2415   2344   3188   -150    129     73       S  
ATOM    400  N   CYS A  62      18.707  23.668  93.913  1.00 19.07           N  
ANISOU  400  N   CYS A  62     2391   2204   2649     -4     67    -10       N  
ATOM    401  CA  CYS A  62      19.505  22.443  93.914  1.00 19.34           C  
ANISOU  401  CA  CYS A  62     2483   2222   2644    -26    -22     68       C  
ATOM    402  C   CYS A  62      19.100  21.553  92.751  1.00 19.27           C  
ANISOU  402  C   CYS A  62     2502   2153   2665    -15    -12     35       C  
ATOM    403  O   CYS A  62      18.078  21.791  92.104  1.00 18.75           O  
ANISOU  403  O   CYS A  62     2547   1904   2674     12     58     -8       O  
ATOM    404  CB  CYS A  62      19.319  21.704  95.240  1.00 19.15           C  
ANISOU  404  CB  CYS A  62     2424   2250   2601    -61      6     77       C  
ATOM    405  SG  CYS A  62      17.701  20.916  95.413  1.00 21.29           S  
ANISOU  405  SG  CYS A  62     2778   2310   3003   -336    -95    364       S  
ATOM    406  N   PHE A  63      19.928  20.545  92.480  1.00 19.66           N  
ANISOU  406  N   PHE A  63     2561   2242   2668    -58     35     45       N  
ATOM    407  CA  PHE A  63      19.571  19.474  91.590  1.00 20.26           C  
ANISOU  407  CA  PHE A  63     2708   2290   2701    -78     48    117       C  
ATOM    408  C   PHE A  63      19.366  18.238  92.448  1.00 20.32           C  
ANISOU  408  C   PHE A  63     2749   2262   2710    -93     37    177       C  
ATOM    409  O   PHE A  63      20.163  17.956  93.343  1.00 20.84           O  
ANISOU  409  O   PHE A  63     2849   2131   2939   -135     82    200       O  
ATOM    410  CB  PHE A  63      20.684  19.170  90.585  1.00 20.23           C  
ANISOU  410  CB  PHE A  63     2690   2253   2742   -112     91    129       C  
ATOM    411  CG  PHE A  63      20.971  20.298  89.628  1.00 20.54           C  
ANISOU  411  CG  PHE A  63     2763   2451   2589   -165     69    167       C  
ATOM    412  CD1 PHE A  63      20.022  20.701  88.710  1.00 20.16           C  
ANISOU  412  CD1 PHE A  63     2800   2285   2573   -215    135    185       C  
ATOM    413  CD2 PHE A  63      22.204  20.932  89.649  1.00 22.69           C  
ANISOU  413  CD2 PHE A  63     3027   2779   2814   -174     79    204       C  
ATOM    414  CE1 PHE A  63      20.290  21.739  87.817  1.00 21.49           C  
ANISOU  414  CE1 PHE A  63     3027   2535   2604   -167     13    141       C  
ATOM    415  CE2 PHE A  63      22.472  21.963  88.758  1.00 22.40           C  
ANISOU  415  CE2 PHE A  63     2999   2679   2832   -163    107    196       C  
ATOM    416  CZ  PHE A  63      21.515  22.351  87.848  1.00 20.65           C  
ANISOU  416  CZ  PHE A  63     2725   2517   2603   -136     97    178       C  
ATOM    417  N   VAL A  64      18.296  17.515  92.176  1.00 21.01           N  
ANISOU  417  N   VAL A  64     2863   2327   2791    -50     29    145       N  
ATOM    418  CA  VAL A  64      18.098  16.205  92.817  1.00 20.79           C  
ANISOU  418  CA  VAL A  64     2839   2321   2739    -82     58    108       C  
ATOM    419  C   VAL A  64      17.884  15.185  91.715  1.00 21.57           C  
ANISOU  419  C   VAL A  64     2921   2471   2803    -84     30     88       C  
ATOM    420  O   VAL A  64      17.046  15.366  90.831  1.00 21.61           O  
ANISOU  420  O   VAL A  64     3068   2449   2694    -87     13     26       O  
ATOM    421  CB  VAL A  64      16.944  16.194  93.836  1.00 21.27           C  
ANISOU  421  CB  VAL A  64     2888   2417   2778    -55      5    120       C  
ATOM    422  CG1 VAL A  64      15.644  16.732  93.242  1.00 20.82           C  
ANISOU  422  CG1 VAL A  64     2691   2476   2744    -97     98     69       C  
ATOM    423  CG2 VAL A  64      16.747  14.778  94.402  1.00 21.48           C  
ANISOU  423  CG2 VAL A  64     2905   2460   2798   -144    115    132       C  
ATOM    424  N   THR A  65      18.661  14.111  91.774  1.00 21.90           N  
ANISOU  424  N   THR A  65     2953   2495   2874    -61     96    -30       N  
ATOM    425  CA  THR A  65      18.567  13.063  90.770  1.00 22.87           C  
ANISOU  425  CA  THR A  65     3104   2590   2996    -88     87     -6       C  
ATOM    426  C   THR A  65      17.893  11.883  91.448  1.00 23.21           C  
ANISOU  426  C   THR A  65     3206   2558   3054    -58     44    -23       C  
ATOM    427  O   THR A  65      18.407  11.378  92.443  1.00 22.76           O  
ANISOU  427  O   THR A  65     3260   2247   3139   -109     11      1       O  
ATOM    428  CB  THR A  65      19.948  12.643  90.263  1.00 23.12           C  
ANISOU  428  CB  THR A  65     3130   2649   3006    -73    119    -47       C  
ATOM    429  OG1 THR A  65      20.597  13.770  89.641  1.00 24.30           O  
ANISOU  429  OG1 THR A  65     3347   2573   3314    -50    357    -98       O  
ATOM    430  CG2 THR A  65      19.811  11.522  89.246  1.00 24.44           C  
ANISOU  430  CG2 THR A  65     3294   2789   3203    -57    134    -76       C  
ATOM    431  N   PHE A  66      16.717  11.518  90.949  1.00 23.89           N  
ANISOU  431  N   PHE A  66     3259   2698   3121    -25     34    -14       N  
ATOM    432  CA  PHE A  66      15.988  10.359  91.436  1.00 25.06           C  
ANISOU  432  CA  PHE A  66     3373   2922   3228    -43     35    -32       C  
ATOM    433  C   PHE A  66      16.354   9.155  90.585  1.00 26.06           C  
ANISOU  433  C   PHE A  66     3551   3011   3340    -35     62    -29       C  
ATOM    434  O   PHE A  66      16.637   9.298  89.401  1.00 26.27           O  
ANISOU  434  O   PHE A  66     3691   2976   3315    -56     45    -82       O  
ATOM    435  CB  PHE A  66      14.487  10.590  91.319  1.00 25.08           C  
ANISOU  435  CB  PHE A  66     3374   2924   3232      0    -14    -17       C  
ATOM    436  CG  PHE A  66      13.950  11.614  92.272  1.00 25.30           C  
ANISOU  436  CG  PHE A  66     3304   3132   3176     12    -30    -34       C  
ATOM    437  CD1 PHE A  66      13.562  11.254  93.545  1.00 25.65           C  
ANISOU  437  CD1 PHE A  66     3359   3146   3242      9     35     49       C  
ATOM    438  CD2 PHE A  66      13.816  12.934  91.883  1.00 25.96           C  
ANISOU  438  CD2 PHE A  66     3427   3147   3290    -46     -4    -98       C  
ATOM    439  CE1 PHE A  66      13.060  12.198  94.428  1.00 25.87           C  
ANISOU  439  CE1 PHE A  66     3375   3109   3347    -14     33     22       C  
ATOM    440  CE2 PHE A  66      13.309  13.872  92.752  1.00 26.03           C  
ANISOU  440  CE2 PHE A  66     3383   3179   3327    -38    -18    -70       C  
ATOM    441  CZ  PHE A  66      12.930  13.506  94.026  1.00 25.44           C  
ANISOU  441  CZ  PHE A  66     3275   3100   3290    -38      6    -29       C  
ATOM    442  N   TYR A  67      16.314   7.966  91.177  1.00 27.01           N  
ANISOU  442  N   TYR A  67     3659   3119   3484    -42     32     -2       N  
ATOM    443  CA  TYR A  67      16.575   6.744  90.413  1.00 27.90           C  
ANISOU  443  CA  TYR A  67     3737   3268   3594    -41     38      1       C  
ATOM    444  C   TYR A  67      15.516   6.481  89.339  1.00 27.95           C  
ANISOU  444  C   TYR A  67     3759   3245   3617   -112     64     27       C  
ATOM    445  O   TYR A  67      15.808   5.906  88.291  1.00 27.97           O  
ANISOU  445  O   TYR A  67     3846   3146   3634   -166     92     82       O  
ATOM    446  CB  TYR A  67      16.675   5.555  91.363  1.00 27.96           C  
ANISOU  446  CB  TYR A  67     3768   3201   3653    -33     42    -16       C  
ATOM    447  CG  TYR A  67      17.970   5.522  92.143  1.00 29.65           C  
ANISOU  447  CG  TYR A  67     3968   3448   3851     -4      3    -16       C  
ATOM    448  CD1 TYR A  67      19.152   5.120  91.537  1.00 30.77           C  
ANISOU  448  CD1 TYR A  67     4000   3655   4036    -37     20     -4       C  
ATOM    449  CD2 TYR A  67      18.009   5.884  93.485  1.00 30.87           C  
ANISOU  449  CD2 TYR A  67     4169   3632   3928      5    -24      2       C  
ATOM    450  CE1 TYR A  67      20.330   5.082  92.234  1.00 31.36           C  
ANISOU  450  CE1 TYR A  67     4149   3603   4165     34    -32    -19       C  
ATOM    451  CE2 TYR A  67      19.195   5.848  94.195  1.00 32.05           C  
ANISOU  451  CE2 TYR A  67     4234   3765   4178    -15      7    -44       C  
ATOM    452  CZ  TYR A  67      20.345   5.442  93.560  1.00 32.16           C  
ANISOU  452  CZ  TYR A  67     4237   3725   4257    -55      0    108       C  
ATOM    453  OH  TYR A  67      21.528   5.404  94.246  1.00 34.22           O  
ANISOU  453  OH  TYR A  67     4510   3877   4615    -76   -145    101       O  
ATOM    454  N   THR A  68      14.285   6.908  89.579  1.00 28.35           N  
ANISOU  454  N   THR A  68     3808   3301   3661    -84     47     50       N  
ATOM    455  CA  THR A  68      13.215   6.604  88.654  1.00 29.24           C  
ANISOU  455  CA  THR A  68     3855   3488   3767   -104     32     69       C  
ATOM    456  C   THR A  68      12.401   7.840  88.319  1.00 29.80           C  
ANISOU  456  C   THR A  68     3944   3549   3829   -107     28     85       C  
ATOM    457  O   THR A  68      12.259   8.740  89.135  1.00 28.95           O  
ANISOU  457  O   THR A  68     3937   3404   3657   -266     34    114       O  
ATOM    458  CB  THR A  68      12.257   5.554  89.242  1.00 29.25           C  
ANISOU  458  CB  THR A  68     3817   3488   3808    -95     36     87       C  
ATOM    459  OG1 THR A  68      11.440   6.162  90.248  1.00 28.60           O  
ANISOU  459  OG1 THR A  68     3885   3211   3769   -262    105    191       O  
ATOM    460  CG2 THR A  68      13.041   4.408  89.858  1.00 29.74           C  
ANISOU  460  CG2 THR A  68     3801   3594   3905   -112    -13     69       C  
ATOM    461  N   ARG A  69      11.823   7.861  87.125  1.00 31.34           N  
ANISOU  461  N   ARG A  69     4126   3762   4021   -116     -6     43       N  
ATOM    462  CA  ARG A  69      10.947   8.964  86.759  1.00 32.24           C  
ANISOU  462  CA  ARG A  69     4180   3923   4148    -82    -12     52       C  
ATOM    463  C   ARG A  69       9.719   8.980  87.634  1.00 31.69           C  
ANISOU  463  C   ARG A  69     4135   3832   4074    -89     -6     44       C  
ATOM    464  O   ARG A  69       9.182  10.039  87.943  1.00 30.71           O  
ANISOU  464  O   ARG A  69     4105   3501   4062   -118    -36    160       O  
ATOM    465  CB  ARG A  69      10.534   8.865  85.299  1.00 33.53           C  
ANISOU  465  CB  ARG A  69     4356   4120   4265    -78    -19      5       C  
ATOM    466  CG  ARG A  69      11.727   8.836  84.391  1.00 37.62           C  
ANISOU  466  CG  ARG A  69     4730   4767   4797      3     55      9       C  
ATOM    467  CD  ARG A  69      11.384   9.275  82.998  1.00 42.09           C  
ANISOU  467  CD  ARG A  69     5426   5353   5215     52    -24     43       C  
ATOM    468  NE  ARG A  69      12.603   9.706  82.332  1.00 45.25           N  
ANISOU  468  NE  ARG A  69     5714   5778   5701    -36     64    -16       N  
ATOM    469  CZ  ARG A  69      12.653  10.701  81.466  1.00 47.98           C  
ANISOU  469  CZ  ARG A  69     6183   6045   6002     -9     12     46       C  
ATOM    470  NH1 ARG A  69      11.545  11.363  81.166  1.00 49.19           N  
ANISOU  470  NH1 ARG A  69     6259   6243   6189     20     -2     18       N  
ATOM    471  NH2 ARG A  69      13.811  11.027  80.912  1.00 49.56           N  
ANISOU  471  NH2 ARG A  69     6279   6335   6217    -52      3      0       N  
ATOM    472  N   LYS A  70       9.258   7.797  88.030  1.00 31.17           N  
ANISOU  472  N   LYS A  70     4094   3709   4042    -82     -3     60       N  
ATOM    473  CA  LYS A  70       8.069   7.718  88.866  1.00 31.27           C  
ANISOU  473  CA  LYS A  70     4037   3818   4028    -98     11     66       C  
ATOM    474  C   LYS A  70       8.295   8.499  90.155  1.00 30.17           C  
ANISOU  474  C   LYS A  70     3883   3657   3924   -128     22     78       C  
ATOM    475  O   LYS A  70       7.428   9.241  90.611  1.00 30.20           O  
ANISOU  475  O   LYS A  70     3766   3690   4017   -193    -27    144       O  
ATOM    476  CB  LYS A  70       7.718   6.257  89.198  1.00 31.52           C  
ANISOU  476  CB  LYS A  70     4079   3802   4097   -106      6     26       C  
ATOM    477  CG  LYS A  70       6.609   6.143  90.241  1.00 34.19           C  
ANISOU  477  CG  LYS A  70     4396   4250   4344    -82     36     16       C  
ATOM    478  CD  LYS A  70       6.263   4.683  90.584  1.00 37.15           C  
ANISOU  478  CD  LYS A  70     4768   4566   4782    -31     29     45       C  
ATOM    479  CE  LYS A  70       4.993   4.578  91.437  1.00 38.76           C  
ANISOU  479  CE  LYS A  70     4900   4892   4934    -49     -3     16       C  
ATOM    480  NZ  LYS A  70       5.100   5.237  92.769  1.00 40.39           N  
ANISOU  480  NZ  LYS A  70     5178   5051   5119     40     15     73       N  
ATOM    481  N   ALA A  71       9.464   8.315  90.756  1.00 29.66           N  
ANISOU  481  N   ALA A  71     3850   3634   3785   -126     32    106       N  
ATOM    482  CA  ALA A  71       9.805   9.022  91.990  1.00 29.47           C  
ANISOU  482  CA  ALA A  71     3810   3614   3772    -88     10     78       C  
ATOM    483  C   ALA A  71       9.829  10.535  91.782  1.00 28.98           C  
ANISOU  483  C   ALA A  71     3738   3576   3698   -107     45     54       C  
ATOM    484  O   ALA A  71       9.273  11.309  92.569  1.00 28.65           O  
ANISOU  484  O   ALA A  71     3701   3576   3609   -203    107    120       O  
ATOM    485  CB  ALA A  71      11.153   8.559  92.474  1.00 29.76           C  
ANISOU  485  CB  ALA A  71     3806   3668   3832   -125    -23     74       C  
ATOM    486  N   ALA A  72      10.505  10.953  90.721  1.00 28.22           N  
ANISOU  486  N   ALA A  72     3673   3498   3550    -96     35     82       N  
ATOM    487  CA  ALA A  72      10.575  12.366  90.380  1.00 28.13           C  
ANISOU  487  CA  ALA A  72     3599   3512   3576    -84     -1     42       C  
ATOM    488  C   ALA A  72       9.182  12.973  90.239  1.00 28.55           C  
ANISOU  488  C   ALA A  72     3664   3571   3611    -77    -35     60       C  
ATOM    489  O   ALA A  72       8.924  14.070  90.725  1.00 27.87           O  
ANISOU  489  O   ALA A  72     3521   3594   3474    -93    -48     68       O  
ATOM    490  CB  ALA A  72      11.354  12.528  89.095  1.00 27.73           C  
ANISOU  490  CB  ALA A  72     3651   3405   3481    -93     35     99       C  
ATOM    491  N   LEU A  73       8.277  12.256  89.576  1.00 29.50           N  
ANISOU  491  N   LEU A  73     3736   3681   3790   -110    -62     51       N  
ATOM    492  CA  LEU A  73       6.941  12.795  89.335  1.00 30.36           C  
ANISOU  492  CA  LEU A  73     3809   3789   3936    -99    -69     -1       C  
ATOM    493  C   LEU A  73       6.148  12.862  90.630  1.00 30.30           C  
ANISOU  493  C   LEU A  73     3763   3800   3950    -94    -89    -22       C  
ATOM    494  O   LEU A  73       5.434  13.825  90.902  1.00 30.87           O  
ANISOU  494  O   LEU A  73     3831   3809   4091   -140   -105    -16       O  
ATOM    495  CB  LEU A  73       6.204  11.951  88.296  1.00 31.37           C  
ANISOU  495  CB  LEU A  73     3945   3917   4057    -89    -76      0       C  
ATOM    496  CG  LEU A  73       4.710  12.249  88.178  1.00 33.16           C  
ANISOU  496  CG  LEU A  73     4122   4186   4293    -16    -84    -33       C  
ATOM    497  CD1 LEU A  73       4.486  13.667  87.711  1.00 34.31           C  
ANISOU  497  CD1 LEU A  73     4273   4315   4450    -50    -54    -23       C  
ATOM    498  CD2 LEU A  73       4.047  11.245  87.228  1.00 35.33           C  
ANISOU  498  CD2 LEU A  73     4479   4465   4478    -43   -131    -95       C  
ATOM    499  N   GLU A  74       6.270  11.836  91.454  1.00 30.39           N  
ANISOU  499  N   GLU A  74     3766   3858   3921    -81    -37    -27       N  
ATOM    500  CA  GLU A  74       5.576  11.859  92.728  1.00 30.69           C  
ANISOU  500  CA  GLU A  74     3816   3912   3932    -66    -22    -28       C  
ATOM    501  C   GLU A  74       6.062  13.008  93.613  1.00 29.70           C  
ANISOU  501  C   GLU A  74     3701   3753   3829    -63    -20      0       C  
ATOM    502  O   GLU A  74       5.266  13.680  94.257  1.00 28.88           O  
ANISOU  502  O   GLU A  74     3530   3738   3704   -208    -17     43       O  
ATOM    503  CB  GLU A  74       5.682  10.498  93.392  1.00 31.21           C  
ANISOU  503  CB  GLU A  74     3871   3983   4003    -32     28    -17       C  
ATOM    504  CG  GLU A  74       4.680   9.564  92.719  1.00 34.86           C  
ANISOU  504  CG  GLU A  74     4365   4461   4419    -94    -34    -81       C  
ATOM    505  CD  GLU A  74       4.848   8.116  93.064  1.00 38.92           C  
ANISOU  505  CD  GLU A  74     4933   4848   5006    -13    -12      3       C  
ATOM    506  OE1 GLU A  74       5.809   7.780  93.785  1.00 42.13           O  
ANISOU  506  OE1 GLU A  74     5241   5575   5190    -96   -197    -65       O  
ATOM    507  OE2 GLU A  74       4.012   7.310  92.585  1.00 41.52           O  
ANISOU  507  OE2 GLU A  74     4994   5368   5415   -161     19    -77       O  
ATOM    508  N   ALA A  75       7.362  13.263  93.609  1.00 29.51           N  
ANISOU  508  N   ALA A  75     3682   3719   3810    -49    -32      4       N  
ATOM    509  CA  ALA A  75       7.903  14.383  94.367  1.00 29.29           C  
ANISOU  509  CA  ALA A  75     3661   3691   3775    -39    -33      8       C  
ATOM    510  C   ALA A  75       7.355  15.695  93.814  1.00 29.44           C  
ANISOU  510  C   ALA A  75     3670   3711   3806    -50    -47     36       C  
ATOM    511  O   ALA A  75       6.953  16.589  94.563  1.00 28.62           O  
ANISOU  511  O   ALA A  75     3554   3598   3722   -136   -114     74       O  
ATOM    512  CB  ALA A  75       9.414  14.373  94.298  1.00 29.27           C  
ANISOU  512  CB  ALA A  75     3672   3711   3739     -3    -19     13       C  
ATOM    513  N   GLN A  76       7.340  15.800  92.492  1.00 30.23           N  
ANISOU  513  N   GLN A  76     3800   3776   3910    -63    -80     16       N  
ATOM    514  CA  GLN A  76       6.870  17.019  91.832  1.00 31.27           C  
ANISOU  514  CA  GLN A  76     3937   3911   4033    -73    -70     -1       C  
ATOM    515  C   GLN A  76       5.408  17.272  92.186  1.00 31.79           C  
ANISOU  515  C   GLN A  76     3971   3992   4115    -65    -79    -18       C  
ATOM    516  O   GLN A  76       5.019  18.374  92.587  1.00 31.16           O  
ANISOU  516  O   GLN A  76     3880   3870   4088   -163   -152    -81       O  
ATOM    517  CB  GLN A  76       7.055  16.898  90.319  1.00 31.39           C  
ANISOU  517  CB  GLN A  76     4007   3902   4018    -75    -72     21       C  
ATOM    518  CG  GLN A  76       6.821  18.185  89.560  1.00 32.36           C  
ANISOU  518  CG  GLN A  76     4102   4023   4170    -55    -59     18       C  
ATOM    519  CD  GLN A  76       6.882  17.989  88.066  1.00 32.56           C  
ANISOU  519  CD  GLN A  76     4190   4016   4167    -59    -41     25       C  
ATOM    520  OE1 GLN A  76       6.167  17.156  87.513  1.00 33.13           O  
ANISOU  520  OE1 GLN A  76     4373   3928   4287    -89     -7     -5       O  
ATOM    521  NE2 GLN A  76       7.711  18.781  87.393  1.00 33.10           N  
ANISOU  521  NE2 GLN A  76     3990   4285   4302   -143    -39    -46       N  
ATOM    522  N   ASN A  77       4.585  16.237  92.051  1.00 32.37           N  
ANISOU  522  N   ASN A  77     4024   4074   4201    -82    -65    -31       N  
ATOM    523  CA  ASN A  77       3.171  16.390  92.368  1.00 32.72           C  
ANISOU  523  CA  ASN A  77     4049   4141   4244    -33    -35    -32       C  
ATOM    524  C   ASN A  77       2.970  16.807  93.825  1.00 32.41           C  
ANISOU  524  C   ASN A  77     3982   4110   4223      2    -49    -27       C  
ATOM    525  O   ASN A  77       2.132  17.663  94.120  1.00 33.16           O  
ANISOU  525  O   ASN A  77     3938   4272   4390     77    -87    -70       O  
ATOM    526  CB  ASN A  77       2.412  15.104  92.039  1.00 33.23           C  
ANISOU  526  CB  ASN A  77     4127   4198   4302    -59    -19    -47       C  
ATOM    527  CG  ASN A  77       2.237  14.905  90.546  1.00 34.68           C  
ANISOU  527  CG  ASN A  77     4321   4415   4442    -64    -71     34       C  
ATOM    528  OD1 ASN A  77       2.065  15.869  89.809  1.00 37.56           O  
ANISOU  528  OD1 ASN A  77     4675   4796   4801   -195   -144    199       O  
ATOM    529  ND2 ASN A  77       2.268  13.654  90.094  1.00 36.23           N  
ANISOU  529  ND2 ASN A  77     4510   4697   4560     58      0   -174       N  
ATOM    530  N   ALA A  78       3.774  16.256  94.732  1.00 31.48           N  
ANISOU  530  N   ALA A  78     3875   4001   4086     -2    -34     -5       N  
ATOM    531  CA  ALA A  78       3.648  16.572  96.148  1.00 30.64           C  
ANISOU  531  CA  ALA A  78     3758   3903   3979      5    -25     13       C  
ATOM    532  C   ALA A  78       4.139  17.981  96.505  1.00 30.13           C  
ANISOU  532  C   ALA A  78     3677   3872   3900     40    -36     -3       C  
ATOM    533  O   ALA A  78       3.622  18.601  97.433  1.00 30.10           O  
ANISOU  533  O   ALA A  78     3653   3881   3903    127    -99    -22       O  
ATOM    534  CB  ALA A  78       4.404  15.535  96.976  1.00 30.74           C  
ANISOU  534  CB  ALA A  78     3788   3955   3935    -14      1     36       C  
ATOM    535  N   LEU A  79       5.139  18.474  95.779  1.00 29.08           N  
ANISOU  535  N   LEU A  79     3550   3692   3807    -18    -52     41       N  
ATOM    536  CA  LEU A  79       5.902  19.648  96.215  1.00 28.46           C  
ANISOU  536  CA  LEU A  79     3470   3619   3723     30    -39      9       C  
ATOM    537  C   LEU A  79       5.744  20.881  95.338  1.00 28.23           C  
ANISOU  537  C   LEU A  79     3369   3609   3750     15    -40     23       C  
ATOM    538  O   LEU A  79       5.659  21.990  95.858  1.00 28.20           O  
ANISOU  538  O   LEU A  79     3276   3584   3854     47   -112     52       O  
ATOM    539  CB  LEU A  79       7.395  19.310  96.277  1.00 27.84           C  
ANISOU  539  CB  LEU A  79     3370   3550   3658    -15    -49     41       C  
ATOM    540  CG  LEU A  79       7.748  18.272  97.341  1.00 27.17           C  
ANISOU  540  CG  LEU A  79     3375   3473   3477    -13    -26    -21       C  
ATOM    541  CD1 LEU A  79       9.235  17.908  97.268  1.00 26.56           C  
ANISOU  541  CD1 LEU A  79     3306   3385   3402     -4    -48     -1       C  
ATOM    542  CD2 LEU A  79       7.386  18.837  98.699  1.00 27.03           C  
ANISOU  542  CD2 LEU A  79     3388   3366   3517    -82     31     20       C  
ATOM    543  N   HIS A  80       5.754  20.698  94.022  1.00 28.19           N  
ANISOU  543  N   HIS A  80     3342   3638   3730     16    -48     18       N  
ATOM    544  CA  HIS A  80       5.786  21.837  93.107  1.00 28.15           C  
ANISOU  544  CA  HIS A  80     3339   3587   3770    -19    -27     35       C  
ATOM    545  C   HIS A  80       4.543  22.692  93.305  1.00 28.90           C  
ANISOU  545  C   HIS A  80     3492   3671   3816    -13    -36     43       C  
ATOM    546  O   HIS A  80       3.412  22.206  93.233  1.00 28.30           O  
ANISOU  546  O   HIS A  80     3348   3647   3759      0    -28     82       O  
ATOM    547  CB  HIS A  80       5.944  21.389  91.646  1.00 28.02           C  
ANISOU  547  CB  HIS A  80     3313   3569   3764    -13    -52     53       C  
ATOM    548  CG  HIS A  80       5.868  22.510  90.652  1.00 29.11           C  
ANISOU  548  CG  HIS A  80     3463   3736   3862    -31    -18     75       C  
ATOM    549  ND1 HIS A  80       6.908  23.390  90.426  1.00 29.29           N  
ANISOU  549  ND1 HIS A  80     3422   3811   3894     87    -46    134       N  
ATOM    550  CD2 HIS A  80       4.862  22.906  89.835  1.00 29.79           C  
ANISOU  550  CD2 HIS A  80     3646   3892   3779    -90    -76    112       C  
ATOM    551  CE1 HIS A  80       6.546  24.275  89.514  1.00 30.64           C  
ANISOU  551  CE1 HIS A  80     3735   3968   3937   -107    -34    160       C  
ATOM    552  NE2 HIS A  80       5.306  24.006  89.143  1.00 29.94           N  
ANISOU  552  NE2 HIS A  80     3680   3882   3813    -45   -118    143       N  
ATOM    553  N   ASN A  81       4.770  23.967  93.585  1.00 29.77           N  
ANISOU  553  N   ASN A  81     3614   3754   3943    -31    -28      1       N  
ATOM    554  CA  ASN A  81       3.692  24.918  93.797  1.00 31.01           C  
ANISOU  554  CA  ASN A  81     3830   3896   4058     -1    -29     11       C  
ATOM    555  C   ASN A  81       2.807  24.542  94.965  1.00 31.57           C  
ANISOU  555  C   ASN A  81     3853   3992   4152      6    -12      7       C  
ATOM    556  O   ASN A  81       1.688  25.022  95.062  1.00 32.26           O  
ANISOU  556  O   ASN A  81     3897   4083   4277     86    -89     72       O  
ATOM    557  CB  ASN A  81       2.860  25.071  92.527  1.00 31.57           C  
ANISOU  557  CB  ASN A  81     3875   3968   4151      8    -13    -10       C  
ATOM    558  CG  ASN A  81       3.357  26.189  91.653  1.00 33.56           C  
ANISOU  558  CG  ASN A  81     4278   4199   4273      3    -48     42       C  
ATOM    559  OD1 ASN A  81       3.181  26.169  90.434  1.00 37.36           O  
ANISOU  559  OD1 ASN A  81     4743   4898   4554     91    -32   -100       O  
ATOM    560  ND2 ASN A  81       3.990  27.176  92.270  1.00 33.43           N  
ANISOU  560  ND2 ASN A  81     4165   4174   4364    -13   -143     58       N  
HETATM  561  N   MSE A  82       3.318  23.691  95.850  1.00 31.74           N  
ANISOU  561  N   MSE A  82     3891   4035   4135     13    -27     44       N  
HETATM  562  CA  MSE A  82       2.537  23.210  96.983  1.00 32.67           C  
ANISOU  562  CA  MSE A  82     4025   4174   4215     17      3     11       C  
HETATM  563  C   MSE A  82       3.199  23.474  98.335  1.00 32.05           C  
ANISOU  563  C   MSE A  82     3999   4065   4112     10     55      4       C  
HETATM  564  O   MSE A  82       2.568  24.017  99.242  1.00 33.20           O  
ANISOU  564  O   MSE A  82     4005   4367   4244    -12    147     60       O  
HETATM  565  CB  MSE A  82       2.243  21.715  96.830  1.00 33.44           C  
ANISOU  565  CB  MSE A  82     4129   4251   4327      5     -3     37       C  
HETATM  566  CG  MSE A  82       1.509  21.355  95.549  1.00 36.00           C  
ANISOU  566  CG  MSE A  82     4317   4715   4645      2    -27    -47       C  
HETATM  567 SE   MSE A  82      -0.429  21.372  95.763  1.00 43.68          SE  
ANISOU  567 SE   MSE A  82     4540   5870   6186     81    -58   -192      SE  
HETATM  568  CE  MSE A  82      -0.528  20.937  97.661  1.00 42.74           C  
ANISOU  568  CE  MSE A  82     5017   5454   5768     18    -78    -37       C  
ATOM    569  N   LYS A  83       4.463  23.083  98.474  1.00 31.08           N  
ANISOU  569  N   LYS A  83     3902   3929   3979    -42     81     10       N  
ATOM    570  CA  LYS A  83       5.133  23.186  99.753  1.00 30.87           C  
ANISOU  570  CA  LYS A  83     3884   3836   4009    -68     79      0       C  
ATOM    571  C   LYS A  83       5.992  24.443  99.833  1.00 30.11           C  
ANISOU  571  C   LYS A  83     3794   3723   3922    -69     91     11       C  
ATOM    572  O   LYS A  83       6.824  24.677  98.955  1.00 29.01           O  
ANISOU  572  O   LYS A  83     3688   3490   3846   -109    168     59       O  
ATOM    573  CB  LYS A  83       5.999  21.953  99.988  1.00 31.51           C  
ANISOU  573  CB  LYS A  83     4004   3873   4097    -44     69      5       C  
ATOM    574  CG  LYS A  83       6.832  22.019 101.249  1.00 33.71           C  
ANISOU  574  CG  LYS A  83     4276   4211   4321    -54    -32    -10       C  
ATOM    575  CD  LYS A  83       7.285  20.643 101.715  1.00 36.62           C  
ANISOU  575  CD  LYS A  83     4692   4493   4730     20    -34      7       C  
ATOM    576  CE  LYS A  83       6.360  20.059 102.797  1.00 38.37           C  
ANISOU  576  CE  LYS A  83     4908   4857   4814     11     31      8       C  
ATOM    577  NZ  LYS A  83       6.634  20.642 104.155  1.00 40.31           N  
ANISOU  577  NZ  LYS A  83     5220   5151   4946    -13    -71     -4       N  
ATOM    578  N   VAL A  84       5.783  25.229 100.886  1.00 29.28           N  
ANISOU  578  N   VAL A  84     3674   3621   3830    -98    129     -4       N  
ATOM    579  CA  VAL A  84       6.609  26.404 101.157  1.00 29.56           C  
ANISOU  579  CA  VAL A  84     3741   3672   3819    -42     67    -50       C  
ATOM    580  C   VAL A  84       7.611  26.031 102.237  1.00 29.72           C  
ANISOU  580  C   VAL A  84     3789   3683   3819    -61     85    -34       C  
ATOM    581  O   VAL A  84       7.227  25.716 103.372  1.00 29.69           O  
ANISOU  581  O   VAL A  84     3803   3761   3715    -99    163    -75       O  
ATOM    582  CB  VAL A  84       5.753  27.594 101.638  1.00 29.70           C  
ANISOU  582  CB  VAL A  84     3747   3698   3839    -53     52    -22       C  
ATOM    583  CG1 VAL A  84       6.607  28.833 101.803  1.00 30.35           C  
ANISOU  583  CG1 VAL A  84     3840   3738   3952     48     28    -47       C  
ATOM    584  CG2 VAL A  84       4.589  27.851 100.673  1.00 29.30           C  
ANISOU  584  CG2 VAL A  84     3751   3611   3772    -41     41    -33       C  
ATOM    585  N   LEU A  85       8.895  26.036 101.887  1.00 29.49           N  
ANISOU  585  N   LEU A  85     3733   3687   3785    -40    138    -22       N  
ATOM    586  CA  LEU A  85       9.948  25.709 102.845  1.00 29.96           C  
ANISOU  586  CA  LEU A  85     3784   3759   3840    -26     90     -1       C  
ATOM    587  C   LEU A  85      10.134  26.881 103.812  1.00 30.43           C  
ANISOU  587  C   LEU A  85     3825   3850   3887      5     91    -14       C  
ATOM    588  O   LEU A  85       9.783  28.012 103.494  1.00 30.25           O  
ANISOU  588  O   LEU A  85     3744   3806   3942      0    113     -3       O  
ATOM    589  CB  LEU A  85      11.257  25.398 102.104  1.00 30.13           C  
ANISOU  589  CB  LEU A  85     3824   3747   3876     19     82    -16       C  
ATOM    590  CG  LEU A  85      11.535  23.964 101.623  1.00 31.85           C  
ANISOU  590  CG  LEU A  85     4048   3979   4076      1     89    -11       C  
ATOM    591  CD1 LEU A  85      10.316  23.112 101.575  1.00 33.06           C  
ANISOU  591  CD1 LEU A  85     4042   4240   4278    -75    -12   -183       C  
ATOM    592  CD2 LEU A  85      12.284  23.881 100.292  1.00 29.93           C  
ANISOU  592  CD2 LEU A  85     3997   3638   3737    -42     14    -11       C  
ATOM    593  N   PRO A  86      10.671  26.614 105.010  1.00 31.41           N  
ANISOU  593  N   PRO A  86     3990   3972   3971     25     49    -55       N  
ATOM    594  CA  PRO A  86      10.885  27.641 106.031  1.00 31.79           C  
ANISOU  594  CA  PRO A  86     4030   4039   4009      8     23    -77       C  
ATOM    595  C   PRO A  86      11.549  28.919 105.535  1.00 31.72           C  
ANISOU  595  C   PRO A  86     3950   4027   4077      8     27   -126       C  
ATOM    596  O   PRO A  86      12.630  28.882 104.943  1.00 31.62           O  
ANISOU  596  O   PRO A  86     3828   4076   4110     13     46   -244       O  
ATOM    597  CB  PRO A  86      11.788  26.929 107.033  1.00 32.18           C  
ANISOU  597  CB  PRO A  86     4103   4063   4062     22      3   -101       C  
ATOM    598  CG  PRO A  86      11.334  25.544 106.990  1.00 32.61           C  
ANISOU  598  CG  PRO A  86     4198   4131   4062    -27      7    -32       C  
ATOM    599  CD  PRO A  86      10.973  25.270 105.534  1.00 31.86           C  
ANISOU  599  CD  PRO A  86     4105   4063   3936     -2     42    -20       C  
ATOM    600  N   GLY A  87      10.873  30.044 105.763  1.00 31.57           N  
ANISOU  600  N   GLY A  87     3876   3999   4120      3     85   -113       N  
ATOM    601  CA  GLY A  87      11.381  31.360 105.404  1.00 31.03           C  
ANISOU  601  CA  GLY A  87     3858   3903   4029     41     61   -104       C  
ATOM    602  C   GLY A  87      11.053  31.773 103.989  1.00 30.87           C  
ANISOU  602  C   GLY A  87     3817   3833   4079     35     66    -61       C  
ATOM    603  O   GLY A  87      11.203  32.941 103.641  1.00 31.46           O  
ANISOU  603  O   GLY A  87     3891   3817   4247     14     80   -133       O  
HETATM  604  N   MSE A  88      10.619  30.836 103.148  1.00 29.50           N  
ANISOU  604  N   MSE A  88     3655   3664   3889     10     65    -78       N  
HETATM  605  CA  MSE A  88      10.360  31.196 101.770  1.00 29.32           C  
ANISOU  605  CA  MSE A  88     3628   3655   3856      3     86     -8       C  
HETATM  606  C   MSE A  88       9.015  31.891 101.676  1.00 29.22           C  
ANISOU  606  C   MSE A  88     3643   3638   3823     44    115    -13       C  
HETATM  607  O   MSE A  88       8.139  31.671 102.510  1.00 29.51           O  
ANISOU  607  O   MSE A  88     3711   3669   3833    149    211    -64       O  
HETATM  608  CB  MSE A  88      10.387  29.975 100.852  1.00 28.99           C  
ANISOU  608  CB  MSE A  88     3616   3627   3773    -10     89      9       C  
HETATM  609  CG  MSE A  88      11.691  29.193 100.873  1.00 29.05           C  
ANISOU  609  CG  MSE A  88     3613   3590   3836    -17    139     29       C  
HETATM  610 SE   MSE A  88      13.242  30.238 100.301  1.00 32.18          SE  
ANISOU  610 SE   MSE A  88     3859   3654   4713    139    505    281      SE  
HETATM  611  CE  MSE A  88      13.744  31.036 102.012  1.00 31.04           C  
ANISOU  611  CE  MSE A  88     3848   3756   4191     74    166    163       C  
ATOM    612  N   HIS A  89       8.843  32.710 100.649  1.00 29.24           N  
ANISOU  612  N   HIS A  89     3625   3648   3838     50    104     -5       N  
ATOM    613  CA  HIS A  89       7.570  33.384 100.427  1.00 29.56           C  
ANISOU  613  CA  HIS A  89     3678   3704   3848     46     55    -17       C  
ATOM    614  C   HIS A  89       6.882  32.839  99.192  1.00 29.72           C  
ANISOU  614  C   HIS A  89     3656   3678   3960     73      0    -38       C  
ATOM    615  O   HIS A  89       5.822  33.334  98.800  1.00 30.29           O  
ANISOU  615  O   HIS A  89     3614   3688   4207    183    -11   -129       O  
ATOM    616  CB  HIS A  89       7.755  34.892 100.283  1.00 29.45           C  
ANISOU  616  CB  HIS A  89     3683   3675   3832     35     41    -18       C  
ATOM    617  CG  HIS A  89       8.073  35.591 101.568  1.00 30.72           C  
ANISOU  617  CG  HIS A  89     3908   3910   3855      7     45      4       C  
ATOM    618  ND1 HIS A  89       8.471  36.909 101.614  1.00 31.30           N  
ANISOU  618  ND1 HIS A  89     4065   3996   3833   -105     57     18       N  
ATOM    619  CD2 HIS A  89       8.053  35.159 102.851  1.00 32.33           C  
ANISOU  619  CD2 HIS A  89     4159   4086   4039     -5     -6     11       C  
ATOM    620  CE1 HIS A  89       8.686  37.259 102.869  1.00 33.75           C  
ANISOU  620  CE1 HIS A  89     4451   4228   4143    -80     33    -26       C  
ATOM    621  NE2 HIS A  89       8.433  36.217 103.641  1.00 33.57           N  
ANISOU  621  NE2 HIS A  89     4450   4269   4036    -23    -19     31       N  
ATOM    622  N   HIS A  90       7.491  31.830  98.575  1.00 28.77           N  
ANISOU  622  N   HIS A  90     3502   3530   3901    112     46    -42       N  
ATOM    623  CA  HIS A  90       6.899  31.149  97.438  1.00 28.70           C  
ANISOU  623  CA  HIS A  90     3542   3481   3880     75     23     -3       C  
ATOM    624  C   HIS A  90       7.195  29.663  97.573  1.00 27.78           C  
ANISOU  624  C   HIS A  90     3438   3374   3745     35      8     -4       C  
ATOM    625  O   HIS A  90       8.185  29.287  98.201  1.00 26.63           O  
ANISOU  625  O   HIS A  90     3329   3091   3697      9     65    -40       O  
ATOM    626  CB  HIS A  90       7.470  31.653  96.113  1.00 29.24           C  
ANISOU  626  CB  HIS A  90     3571   3589   3949     73     25      4       C  
ATOM    627  CG  HIS A  90       7.206  33.103  95.854  1.00 32.48           C  
ANISOU  627  CG  HIS A  90     4089   3898   4355     42     49     38       C  
ATOM    628  ND1 HIS A  90       5.991  33.565  95.391  1.00 35.46           N  
ANISOU  628  ND1 HIS A  90     4419   4310   4743      5   -124    141       N  
ATOM    629  CD2 HIS A  90       7.993  34.196  96.010  1.00 35.43           C  
ANISOU  629  CD2 HIS A  90     4400   4364   4698      2     -2      1       C  
ATOM    630  CE1 HIS A  90       6.042  34.880  95.273  1.00 37.23           C  
ANISOU  630  CE1 HIS A  90     4710   4468   4967     45    -73     69       C  
ATOM    631  NE2 HIS A  90       7.246  35.288  95.639  1.00 36.89           N  
ANISOU  631  NE2 HIS A  90     4705   4326   4986     -5    -80    104       N  
ATOM    632  N   PRO A  91       6.331  28.822  96.988  1.00 26.82           N  
ANISOU  632  N   PRO A  91     3322   3263   3604     21     -3      0       N  
ATOM    633  CA  PRO A  91       6.489  27.381  97.054  1.00 26.33           C  
ANISOU  633  CA  PRO A  91     3234   3280   3491     -7     20      2       C  
ATOM    634  C   PRO A  91       7.576  26.870  96.130  1.00 25.40           C  
ANISOU  634  C   PRO A  91     3086   3149   3416     13     15     34       C  
ATOM    635  O   PRO A  91       7.922  27.515  95.127  1.00 24.73           O  
ANISOU  635  O   PRO A  91     2958   3039   3400     94     62     94       O  
ATOM    636  CB  PRO A  91       5.131  26.854  96.581  1.00 26.36           C  
ANISOU  636  CB  PRO A  91     3223   3310   3481    -38      0     -6       C  
ATOM    637  CG  PRO A  91       4.595  27.910  95.741  1.00 26.83           C  
ANISOU  637  CG  PRO A  91     3320   3320   3555      0     20      2       C  
ATOM    638  CD  PRO A  91       5.066  29.197  96.340  1.00 27.31           C  
ANISOU  638  CD  PRO A  91     3396   3356   3626      0    -32      5       C  
ATOM    639  N   ILE A  92       8.088  25.703  96.494  1.00 24.25           N  
ANISOU  639  N   ILE A  92     2973   2941   3301    -49     26     66       N  
ATOM    640  CA  ILE A  92       9.041  24.977  95.689  1.00 23.94           C  
ANISOU  640  CA  ILE A  92     2917   2925   3255    -37     25     27       C  
ATOM    641  C   ILE A  92       8.614  24.941  94.232  1.00 24.26           C  
ANISOU  641  C   ILE A  92     2958   2946   3315      1    -22     35       C  
ATOM    642  O   ILE A  92       7.433  24.736  93.896  1.00 23.66           O  
ANISOU  642  O   ILE A  92     2675   2862   3454    -24      4    -29       O  
ATOM    643  CB  ILE A  92       9.172  23.518  96.194  1.00 23.75           C  
ANISOU  643  CB  ILE A  92     2935   2870   3219    -23     30     37       C  
ATOM    644  CG1 ILE A  92       9.849  23.475  97.559  1.00 24.13           C  
ANISOU  644  CG1 ILE A  92     3034   2883   3250    -44     62     94       C  
ATOM    645  CG2 ILE A  92       9.904  22.643  95.171  1.00 23.08           C  
ANISOU  645  CG2 ILE A  92     2710   2910   3151    -23     73     65       C  
ATOM    646  CD1 ILE A  92       9.868  22.069  98.180  1.00 25.65           C  
ANISOU  646  CD1 ILE A  92     3283   3038   3424    -59    -22     86       C  
ATOM    647  N   GLN A  93       9.597  25.130  93.365  1.00 24.31           N  
ANISOU  647  N   GLN A  93     2934   3037   3266     15      2      8       N  
ATOM    648  CA  GLN A  93       9.398  25.016  91.932  1.00 25.85           C  
ANISOU  648  CA  GLN A  93     3176   3242   3405      5    -16      4       C  
ATOM    649  C   GLN A  93      10.287  23.889  91.463  1.00 26.22           C  
ANISOU  649  C   GLN A  93     3255   3302   3407     16    -26      9       C  
ATOM    650  O   GLN A  93      11.476  23.908  91.727  1.00 25.47           O  
ANISOU  650  O   GLN A  93     3075   3228   3374    -42      5    -48       O  
ATOM    651  CB  GLN A  93       9.852  26.295  91.244  1.00 26.38           C  
ANISOU  651  CB  GLN A  93     3264   3306   3453     24      3     38       C  
ATOM    652  CG  GLN A  93       9.153  27.524  91.756  1.00 27.49           C  
ANISOU  652  CG  GLN A  93     3480   3380   3586     25    -41    -28       C  
ATOM    653  CD  GLN A  93       7.680  27.494  91.440  1.00 28.84           C  
ANISOU  653  CD  GLN A  93     3561   3651   3745     53    -53    -49       C  
ATOM    654  OE1 GLN A  93       7.289  27.419  90.280  1.00 31.08           O  
ANISOU  654  OE1 GLN A  93     3723   4160   3925    222   -188    -14       O  
ATOM    655  NE2 GLN A  93       6.855  27.548  92.466  1.00 29.30           N  
ANISOU  655  NE2 GLN A  93     3703   3595   3835    -94    -37     72       N  
HETATM  656  N   MSE A  94       9.727  22.922  90.756  1.00 27.20           N  
ANISOU  656  N   MSE A  94     3377   3437   3520    -61    -75     34       N  
HETATM  657  CA  MSE A  94      10.474  21.734  90.400  1.00 28.78           C  
ANISOU  657  CA  MSE A  94     3587   3649   3699    -70    -48     42       C  
HETATM  658  C   MSE A  94      10.222  21.381  88.942  1.00 29.01           C  
ANISOU  658  C   MSE A  94     3623   3673   3728    -57    -53     32       C  
HETATM  659  O   MSE A  94       9.061  21.327  88.520  1.00 29.54           O  
ANISOU  659  O   MSE A  94     3633   3862   3728   -146   -165    -20       O  
HETATM  660  CB  MSE A  94       9.968  20.597  91.282  1.00 30.14           C  
ANISOU  660  CB  MSE A  94     3774   3812   3866    -79    -16     65       C  
HETATM  661  CG  MSE A  94      11.003  19.655  91.721  1.00 33.70           C  
ANISOU  661  CG  MSE A  94     4309   4167   4329   -151    -53    208       C  
HETATM  662 SE   MSE A  94      10.274  18.502  93.103  1.00 42.63          SE  
ANISOU  662 SE   MSE A  94     5918   4993   5287   -708   -174    822      SE  
HETATM  663  CE  MSE A  94      11.223  16.951  92.432  1.00 42.76           C  
ANISOU  663  CE  MSE A  94     5563   5391   5293   -243     40    165       C  
ATOM    664  N   LYS A  95      11.283  21.125  88.185  1.00 28.50           N  
ANISOU  664  N   LYS A  95     3585   3551   3692    -82    -41     45       N  
ATOM    665  CA  LYS A  95      11.164  20.745  86.782  1.00 29.12           C  
ANISOU  665  CA  LYS A  95     3708   3581   3774    -55    -22     19       C  
ATOM    666  C   LYS A  95      12.438  20.046  86.352  1.00 28.64           C  
ANISOU  666  C   LYS A  95     3682   3522   3679    -60     -9      0       C  
ATOM    667  O   LYS A  95      13.467  20.136  87.032  1.00 27.44           O  
ANISOU  667  O   LYS A  95     3627   3217   3581   -101    -18    -25       O  
ATOM    668  CB  LYS A  95      10.956  21.974  85.898  1.00 29.99           C  
ANISOU  668  CB  LYS A  95     3808   3764   3822    -31    -40     40       C  
ATOM    669  CG  LYS A  95      12.135  22.938  85.932  1.00 32.92           C  
ANISOU  669  CG  LYS A  95     4171   4083   4253    -73    -12     47       C  
ATOM    670  CD  LYS A  95      11.747  24.288  85.345  1.00 36.36           C  
ANISOU  670  CD  LYS A  95     4672   4505   4638      0    -58     63       C  
ATOM    671  CE  LYS A  95      12.957  25.158  85.101  1.00 38.31           C  
ANISOU  671  CE  LYS A  95     4813   4845   4898    -26    -11     30       C  
ATOM    672  NZ  LYS A  95      13.297  25.228  83.661  1.00 39.86           N  
ANISOU  672  NZ  LYS A  95     5102   5129   4914    127    -62      0       N  
ATOM    673  N   PRO A  96      12.382  19.333  85.220  1.00 28.35           N  
ANISOU  673  N   PRO A  96     3636   3512   3623    -42    -27    -33       N  
ATOM    674  CA  PRO A  96      13.583  18.632  84.815  1.00 28.11           C  
ANISOU  674  CA  PRO A  96     3651   3462   3568    -35     -8    -44       C  
ATOM    675  C   PRO A  96      14.705  19.618  84.532  1.00 27.20           C  
ANISOU  675  C   PRO A  96     3584   3332   3417    -49    -19    -51       C  
ATOM    676  O   PRO A  96      14.462  20.696  83.981  1.00 26.11           O  
ANISOU  676  O   PRO A  96     3492   3068   3362     -9    -35    -51       O  
ATOM    677  CB  PRO A  96      13.156  17.911  83.525  1.00 28.38           C  
ANISOU  677  CB  PRO A  96     3673   3523   3586    -20    -21    -40       C  
ATOM    678  CG  PRO A  96      11.702  17.809  83.616  1.00 28.99           C  
ANISOU  678  CG  PRO A  96     3711   3581   3723    -48    -43    -47       C  
ATOM    679  CD  PRO A  96      11.270  19.082  84.291  1.00 29.06           C  
ANISOU  679  CD  PRO A  96     3747   3615   3680    -18      0    -70       C  
ATOM    680  N   ALA A  97      15.919  19.234  84.895  1.00 26.42           N  
ANISOU  680  N   ALA A  97     3499   3212   3327    -12     11    -42       N  
ATOM    681  CA  ALA A  97      17.071  20.107  84.764  1.00 26.62           C  
ANISOU  681  CA  ALA A  97     3537   3266   3311    -63     51      2       C  
ATOM    682  C   ALA A  97      17.391  20.378  83.307  1.00 27.38           C  
ANISOU  682  C   ALA A  97     3702   3342   3358    -97     50     -5       C  
ATOM    683  O   ALA A  97      17.050  19.584  82.437  1.00 27.36           O  
ANISOU  683  O   ALA A  97     3828   3219   3347   -159    131     10       O  
ATOM    684  CB  ALA A  97      18.274  19.486  85.438  1.00 26.57           C  
ANISOU  684  CB  ALA A  97     3508   3299   3288    -63     69     33       C  
ATOM    685  N   ASP A  98      18.054  21.502  83.047  1.00 27.96           N  
ANISOU  685  N   ASP A  98     3786   3403   3433   -114    116    -23       N  
ATOM    686  CA  ASP A  98      18.437  21.850  81.686  1.00 28.74           C  
ANISOU  686  CA  ASP A  98     3861   3527   3533    -95    101     -3       C  
ATOM    687  C   ASP A  98      19.374  20.788  81.096  1.00 29.23           C  
ANISOU  687  C   ASP A  98     3901   3563   3641    -69    102     -5       C  
ATOM    688  O   ASP A  98      19.320  20.497  79.902  1.00 29.68           O  
ANISOU  688  O   ASP A  98     4058   3565   3655    -83    186    -51       O  
ATOM    689  CB  ASP A  98      19.100  23.231  81.645  1.00 28.61           C  
ANISOU  689  CB  ASP A  98     3875   3509   3488    -91    128     22       C  
ATOM    690  CG  ASP A  98      18.105  24.365  81.840  1.00 28.87           C  
ANISOU  690  CG  ASP A  98     3768   3540   3661    -97     83     82       C  
ATOM    691  OD1 ASP A  98      16.890  24.131  81.774  1.00 30.00           O  
ANISOU  691  OD1 ASP A  98     3963   3579   3857   -121    -79    161       O  
ATOM    692  OD2 ASP A  98      18.528  25.513  82.058  1.00 29.71           O  
ANISOU  692  OD2 ASP A  98     4020   3482   3786    -80    102    -66       O  
ATOM    693  N   SER A  99      20.227  20.208  81.926  1.00 30.38           N  
ANISOU  693  N   SER A  99     4029   3707   3808    -84    103    -16       N  
ATOM    694  CA  SER A  99      21.189  19.214  81.451  1.00 31.22           C  
ANISOU  694  CA  SER A  99     4096   3844   3922    -26     95      0       C  
ATOM    695  C   SER A  99      20.511  17.957  80.897  1.00 32.75           C  
ANISOU  695  C   SER A  99     4311   4030   4104    -20     64     -5       C  
ATOM    696  O   SER A  99      21.137  17.171  80.186  1.00 32.95           O  
ANISOU  696  O   SER A  99     4395   4012   4111    -11     81     23       O  
ATOM    697  CB  SER A  99      22.186  18.853  82.558  1.00 31.07           C  
ANISOU  697  CB  SER A  99     4068   3813   3926    -49     92    -26       C  
ATOM    698  OG  SER A  99      21.559  18.272  83.697  1.00 29.99           O  
ANISOU  698  OG  SER A  99     4045   3578   3771    -51    108    -45       O  
ATOM    699  N   GLU A 100      19.235  17.764  81.204  1.00 34.94           N  
ANISOU  699  N   GLU A 100     4544   4356   4377      2     31      4       N  
ATOM    700  CA  GLU A 100      18.526  16.564  80.765  1.00 37.17           C  
ANISOU  700  CA  GLU A 100     4829   4625   4668    -23      0     -2       C  
ATOM    701  C   GLU A 100      17.918  16.778  79.386  1.00 39.39           C  
ANISOU  701  C   GLU A 100     5114   4946   4905    -25    -24     -7       C  
ATOM    702  O   GLU A 100      17.451  15.833  78.750  1.00 38.79           O  
ANISOU  702  O   GLU A 100     5137   4806   4796   -102    -33     84       O  
ATOM    703  CB  GLU A 100      17.407  16.196  81.741  1.00 37.54           C  
ANISOU  703  CB  GLU A 100     4868   4651   4745    -29     -7     -5       C  
ATOM    704  CG  GLU A 100      17.874  15.924  83.162  1.00 38.15           C  
ANISOU  704  CG  GLU A 100     4975   4748   4772    -15     28      4       C  
ATOM    705  CD  GLU A 100      18.808  14.733  83.270  1.00 39.68           C  
ANISOU  705  CD  GLU A 100     5071   4957   5050    -20    111     82       C  
ATOM    706  OE1 GLU A 100      19.965  14.802  82.792  1.00 43.74           O  
ANISOU  706  OE1 GLU A 100     5337   5773   5509    -33    211     61       O  
ATOM    707  OE2 GLU A 100      18.402  13.731  83.874  1.00 36.95           O  
ANISOU  707  OE2 GLU A 100     4703   4338   4997   -139    254     -3       O  
ATOM    708  N   LYS A 101      17.893  18.027  78.940  1.00 41.81           N  
ANISOU  708  N   LYS A 101     5431   5203   5251    -50    -12     37       N  
ATOM    709  CA  LYS A 101      17.285  18.335  77.662  1.00 44.53           C  
ANISOU  709  CA  LYS A 101     5721   5615   5583    -23    -24     28       C  
ATOM    710  C   LYS A 101      18.042  17.559  76.589  1.00 46.21           C  
ANISOU  710  C   LYS A 101     5925   5851   5781     -2      0     51       C  
ATOM    711  O   LYS A 101      19.260  17.633  76.460  1.00 46.81           O  
ANISOU  711  O   LYS A 101     5981   5972   5833     13     26     71       O  
ATOM    712  CB  LYS A 101      17.258  19.840  77.409  1.00 44.87           C  
ANISOU  712  CB  LYS A 101     5770   5644   5636    -13    -34     31       C  
ATOM    713  CG  LYS A 101      16.228  20.559  78.289  1.00 46.97           C  
ANISOU  713  CG  LYS A 101     5969   5960   5919     -2     14     25       C  
ATOM    714  CD  LYS A 101      16.387  22.081  78.275  1.00 49.13           C  
ANISOU  714  CD  LYS A 101     6295   6140   6232     -5    -23     -6       C  
ATOM    715  CE  LYS A 101      15.315  22.754  79.125  1.00 50.64           C  
ANISOU  715  CE  LYS A 101     6429   6405   6408     10      9    -10       C  
ATOM    716  NZ  LYS A 101      15.378  24.246  79.074  1.00 52.10           N  
ANISOU  716  NZ  LYS A 101     6637   6543   6616    -28    -32      1       N  
ATOM    717  N   ASN A 102      17.316  16.795  75.845  1.00 48.31           N  
ANISOU  717  N   ASN A 102     6215   6103   6036    -13    -17     19       N  
ATOM    718  CA  ASN A 102      17.961  15.911  74.943  1.00 50.05           C  
ANISOU  718  CA  ASN A 102     6395   6339   6282      7      6     12       C  
ATOM    719  C   ASN A 102      17.897  16.326  73.464  1.00 50.36           C  
ANISOU  719  C   ASN A 102     6438   6393   6303    -13     -1     23       C  
ATOM    720  O   ASN A 102      18.864  16.829  72.920  1.00 50.80           O  
ANISOU  720  O   ASN A 102     6505   6452   6345     -9     16     28       O  
ATOM    721  CB  ASN A 102      17.361  14.539  75.141  1.00 50.50           C  
ANISOU  721  CB  ASN A 102     6453   6379   6355    -26     -8     12       C  
ATOM    722  CG  ASN A 102      18.371  13.529  75.167  1.00 52.39           C  
ANISOU  722  CG  ASN A 102     6652   6612   6643     24    -17     30       C  
ATOM    723  OD1 ASN A 102      19.357  13.754  75.845  1.00 54.37           O  
ANISOU  723  OD1 ASN A 102     6745   6954   6960    -55    -48     21       O  
ATOM    724  ND2 ASN A 102      18.208  12.539  74.485  1.00 55.70           N  
ANISOU  724  ND2 ASN A 102     7173   6957   7033    -56   -106    -86       N  
ATOM    725  N   ASN A 103      16.780  16.056  72.817  1.00 50.76           N  
ANISOU  725  N   ASN A 103     6453   6479   6356     12    -19     37       N  
ATOM    726  CA  ASN A 103      16.630  16.461  71.426  1.00 50.64           C  
ANISOU  726  CA  ASN A 103     6439   6483   6317      2     23     15       C  
ATOM    727  C   ASN A 103      16.333  17.931  71.301  1.00 49.98           C  
ANISOU  727  C   ASN A 103     6358   6422   6212      0     31     25       C  
ATOM    728  O   ASN A 103      15.237  18.289  70.896  1.00 50.44           O  
ANISOU  728  O   ASN A 103     6380   6509   6275     -7     62      7       O  
ATOM    729  CB  ASN A 103      15.448  15.738  70.788  1.00 50.90           C  
ANISOU  729  CB  ASN A 103     6459   6526   6353      2     15      6       C  
ATOM    730  CG  ASN A 103      15.792  14.348  70.344  1.00 51.91           C  
ANISOU  730  CG  ASN A 103     6607   6578   6540     10      9      1       C  
ATOM    731  OD1 ASN A 103      15.239  13.846  69.368  1.00 53.23           O  
ANISOU  731  OD1 ASN A 103     6740   6826   6660    -20   -111     42       O  
ATOM    732  ND2 ASN A 103      16.719  13.715  71.051  1.00 53.69           N  
ANISOU  732  ND2 ASN A 103     6771   6914   6714     32    -44     53       N  
ATOM    733  N   ALA A 104      17.269  18.803  71.627  1.00 49.46           N  
ANISOU  733  N   ALA A 104     6303   6362   6126     15     16     19       N  
ATOM    734  CA  ALA A 104      16.975  20.206  71.422  1.00 49.47           C  
ANISOU  734  CA  ALA A 104     6287   6333   6175      1     16     21       C  
ATOM    735  C   ALA A 104      16.309  20.327  70.046  1.00 49.60           C  
ANISOU  735  C   ALA A 104     6300   6324   6223     16      9     35       C  
ATOM    736  O   ALA A 104      16.768  19.743  69.064  1.00 48.96           O  
ANISOU  736  O   ALA A 104     6202   6284   6115     60     -4     72       O  
ATOM    737  CB  ALA A 104      18.242  21.037  71.505  1.00 49.68           C  
ANISOU  737  CB  ALA A 104     6326   6340   6210      4     12     25       C  
ATOM    738  N   VAL A 105      15.193  21.040  69.979  1.00 50.00           N  
ANISOU  738  N   VAL A 105     6340   6365   6291     -5     31     28       N  
ATOM    739  CA  VAL A 105      14.575  21.327  68.694  1.00 50.70           C  
ANISOU  739  CA  VAL A 105     6415   6450   6397    -17     23     22       C  
ATOM    740  C   VAL A 105      15.580  22.066  67.814  1.00 51.15           C  
ANISOU  740  C   VAL A 105     6487   6498   6450    -24     32     31       C  
ATOM    741  O   VAL A 105      15.685  21.796  66.619  1.00 50.72           O  
ANISOU  741  O   VAL A 105     6443   6446   6383    -45     73     35       O  
ATOM    742  CB  VAL A 105      13.318  22.201  68.850  1.00 50.78           C  
ANISOU  742  CB  VAL A 105     6417   6450   6426    -15     17     28       C  
ATOM    743  CG1 VAL A 105      12.925  22.813  67.512  1.00 51.09           C  
ANISOU  743  CG1 VAL A 105     6447   6518   6445    -24     31      7       C  
ATOM    744  CG2 VAL A 105      12.168  21.385  69.427  1.00 51.31           C  
ANISOU  744  CG2 VAL A 105     6457   6538   6501      0     25     22       C  
ATOM    745  N   GLU A 106      16.317  22.991  68.425  1.00 51.77           N  
ANISOU  745  N   GLU A 106     6549   6586   6534    -37      9     24       N  
ATOM    746  CA  GLU A 106      17.263  23.842  67.703  1.00 52.39           C  
ANISOU  746  CA  GLU A 106     6636   6651   6617    -12     14     20       C  
ATOM    747  C   GLU A 106      18.301  23.041  66.921  1.00 51.62           C  
ANISOU  747  C   GLU A 106     6532   6546   6534      6      8     34       C  
ATOM    748  O   GLU A 106      18.929  23.572  66.003  1.00 52.09           O  
ANISOU  748  O   GLU A 106     6572   6592   6628     56      0     45       O  
ATOM    749  CB  GLU A 106      18.013  24.757  68.674  1.00 53.05           C  
ANISOU  749  CB  GLU A 106     6703   6727   6727    -24     -1     23       C  
ATOM    750  CG  GLU A 106      17.165  25.389  69.757  1.00 55.29           C  
ANISOU  750  CG  GLU A 106     7020   6992   6997     22     34    -24       C  
ATOM    751  CD  GLU A 106      17.985  25.735  70.985  1.00 57.86           C  
ANISOU  751  CD  GLU A 106     7343   7326   7314     20    -75    -18       C  
ATOM    752  OE1 GLU A 106      18.707  24.839  71.476  1.00 59.69           O  
ANISOU  752  OE1 GLU A 106     7539   7526   7613     83    -21     31       O  
ATOM    753  OE2 GLU A 106      17.911  26.892  71.460  1.00 59.56           O  
ANISOU  753  OE2 GLU A 106     7591   7450   7588    -12    -67    -23       O  
ATOM    754  N   ASP A 107      18.503  21.782  67.294  1.00 50.35           N  
ANISOU  754  N   ASP A 107     6386   6386   6360     -8     14     32       N  
ATOM    755  CA  ASP A 107      19.520  20.956  66.653  1.00 49.34           C  
ANISOU  755  CA  ASP A 107     6268   6244   6235     -7      1     33       C  
ATOM    756  C   ASP A 107      18.886  19.888  65.761  1.00 48.09           C  
ANISOU  756  C   ASP A 107     6100   6106   6067     21     16     58       C  
ATOM    757  O   ASP A 107      19.549  18.942  65.335  1.00 48.34           O  
ANISOU  757  O   ASP A 107     6138   6174   6056     74     57     56       O  
ATOM    758  CB  ASP A 107      20.400  20.284  67.707  1.00 49.55           C  
ANISOU  758  CB  ASP A 107     6289   6269   6269     -1      8     21       C  
ATOM    759  CG  ASP A 107      21.192  21.276  68.544  1.00 49.83           C  
ANISOU  759  CG  ASP A 107     6337   6292   6304      7     18     25       C  
ATOM    760  OD1 ASP A 107      21.520  22.376  68.051  1.00 50.50           O  
ANISOU  760  OD1 ASP A 107     6512   6223   6452    -13     24     30       O  
ATOM    761  OD2 ASP A 107      21.505  20.943  69.705  1.00 49.50           O  
ANISOU  761  OD2 ASP A 107     6220   6314   6274     66     34      9       O  
ATOM    762  N   ARG A 108      17.595  20.047  65.490  1.00 46.05           N  
ANISOU  762  N   ARG A 108     5867   5840   5791     -7     -1     57       N  
ATOM    763  CA  ARG A 108      16.836  19.115  64.669  1.00 44.46           C  
ANISOU  763  CA  ARG A 108     5669   5655   5569     -1      0     65       C  
ATOM    764  C   ARG A 108      16.111  19.905  63.586  1.00 41.97           C  
ANISOU  764  C   ARG A 108     5358   5327   5260    -23     22     57       C  
ATOM    765  O   ARG A 108      15.271  19.368  62.867  1.00 42.03           O  
ANISOU  765  O   ARG A 108     5400   5340   5228      2     39     91       O  
ATOM    766  CB  ARG A 108      15.765  18.422  65.516  1.00 44.98           C  
ANISOU  766  CB  ARG A 108     5742   5703   5645    -13    -23     56       C  
ATOM    767  CG  ARG A 108      16.159  17.093  66.106  1.00 46.42           C  
ANISOU  767  CG  ARG A 108     5936   5841   5861      0    -50     25       C  
ATOM    768  CD  ARG A 108      14.944  16.370  66.662  1.00 46.90           C  
ANISOU  768  CD  ARG A 108     5904   5976   5940    -14     -2     23       C  
ATOM    769  NE  ARG A 108      14.380  17.030  67.837  1.00 48.25           N  
ANISOU  769  NE  ARG A 108     6159   6123   6051     63    -36     10       N  
ATOM    770  CZ  ARG A 108      13.118  17.440  67.943  1.00 48.66           C  
ANISOU  770  CZ  ARG A 108     6141   6218   6128      6     22     -8       C  
ATOM    771  NH1 ARG A 108      12.258  17.272  66.946  1.00 48.23           N  
ANISOU  771  NH1 ARG A 108     6084   6210   6032     -6     64     43       N  
ATOM    772  NH2 ARG A 108      12.714  18.025  69.059  1.00 49.87           N  
ANISOU  772  NH2 ARG A 108     6336   6377   6236      9     14     27       N  
ATOM    773  N   LYS A 109      16.405  21.197  63.514  1.00 38.85           N  
ANISOU  773  N   LYS A 109     4925   5031   4804    -30     47    112       N  
ATOM    774  CA  LYS A 109      15.619  22.106  62.697  1.00 36.66           C  
ANISOU  774  CA  LYS A 109     4630   4748   4551    -59     80     94       C  
ATOM    775  C   LYS A 109      16.449  22.617  61.527  1.00 34.23           C  
ANISOU  775  C   LYS A 109     4318   4465   4222    -70     47    131       C  
ATOM    776  O   LYS A 109      17.582  23.045  61.719  1.00 33.43           O  
ANISOU  776  O   LYS A 109     4291   4375   4034   -123    132    277       O  
ATOM    777  CB  LYS A 109      15.186  23.298  63.536  1.00 36.88           C  
ANISOU  777  CB  LYS A 109     4638   4793   4583    -65     64     62       C  
ATOM    778  CG  LYS A 109      14.195  24.204  62.850  1.00 38.03           C  
ANISOU  778  CG  LYS A 109     4828   4907   4715    -18     16     75       C  
ATOM    779  CD  LYS A 109      14.341  25.622  63.342  1.00 40.50           C  
ANISOU  779  CD  LYS A 109     5145   5157   5087    -21     18      9       C  
ATOM    780  CE  LYS A 109      12.997  26.299  63.503  1.00 42.14           C  
ANISOU  780  CE  LYS A 109     5296   5422   5293      2     55    -28       C  
ATOM    781  NZ  LYS A 109      12.577  26.275  64.940  1.00 42.68           N  
ANISOU  781  NZ  LYS A 109     5442   5519   5254    -32     90     58       N  
ATOM    782  N   LEU A 110      15.863  22.573  60.336  1.00 31.65           N  
ANISOU  782  N   LEU A 110     3961   4144   3919    -94     94    118       N  
ATOM    783  CA  LEU A 110      16.514  23.034  59.113  1.00 29.75           C  
ANISOU  783  CA  LEU A 110     3718   3833   3752    -49     67     88       C  
ATOM    784  C   LEU A 110      15.974  24.368  58.643  1.00 28.20           C  
ANISOU  784  C   LEU A 110     3498   3675   3543    -39     77     83       C  
ATOM    785  O   LEU A 110      14.776  24.612  58.675  1.00 28.30           O  
ANISOU  785  O   LEU A 110     3466   3647   3638    -60     95     79       O  
ATOM    786  CB  LEU A 110      16.306  22.037  57.983  1.00 29.52           C  
ANISOU  786  CB  LEU A 110     3676   3871   3671    -70     83    109       C  
ATOM    787  CG  LEU A 110      16.957  20.664  58.138  1.00 28.59           C  
ANISOU  787  CG  LEU A 110     3643   3661   3557    -39     36    107       C  
ATOM    788  CD1 LEU A 110      16.636  19.794  56.955  1.00 29.82           C  
ANISOU  788  CD1 LEU A 110     3815   3749   3765    -44    -11     87       C  
ATOM    789  CD2 LEU A 110      18.459  20.774  58.300  1.00 28.35           C  
ANISOU  789  CD2 LEU A 110     3576   3612   3583    -23     12    114       C  
ATOM    790  N   PHE A 111      16.885  25.233  58.211  1.00 26.41           N  
ANISOU  790  N   PHE A 111     3316   3404   3315      6     72     25       N  
ATOM    791  CA  PHE A 111      16.539  26.369  57.389  1.00 24.78           C  
ANISOU  791  CA  PHE A 111     3143   3177   3097     11     79     24       C  
ATOM    792  C   PHE A 111      16.568  25.941  55.921  1.00 24.30           C  
ANISOU  792  C   PHE A 111     3082   3081   3069      3     86     72       C  
ATOM    793  O   PHE A 111      17.572  25.404  55.440  1.00 24.08           O  
ANISOU  793  O   PHE A 111     3144   3106   2899     33    240    114       O  
ATOM    794  CB  PHE A 111      17.536  27.508  57.603  1.00 24.85           C  
ANISOU  794  CB  PHE A 111     3179   3219   3043     34     75     24       C  
ATOM    795  CG  PHE A 111      17.348  28.646  56.648  1.00 24.21           C  
ANISOU  795  CG  PHE A 111     3120   3033   3045     18     65     21       C  
ATOM    796  CD1 PHE A 111      16.378  29.604  56.880  1.00 23.62           C  
ANISOU  796  CD1 PHE A 111     2954   3032   2990     -3     25    -24       C  
ATOM    797  CD2 PHE A 111      18.124  28.739  55.504  1.00 22.77           C  
ANISOU  797  CD2 PHE A 111     2872   2875   2906    -11     77    -18       C  
ATOM    798  CE1 PHE A 111      16.177  30.637  55.977  1.00 23.64           C  
ANISOU  798  CE1 PHE A 111     3143   2793   3046      1    144    -40       C  
ATOM    799  CE2 PHE A 111      17.947  29.773  54.611  1.00 22.50           C  
ANISOU  799  CE2 PHE A 111     2863   2958   2727      7     93     19       C  
ATOM    800  CZ  PHE A 111      16.981  30.731  54.844  1.00 23.72           C  
ANISOU  800  CZ  PHE A 111     3171   2900   2943     -2     70    -39       C  
ATOM    801  N   ILE A 112      15.462  26.175  55.227  1.00 23.44           N  
ANISOU  801  N   ILE A 112     2960   2970   2976    -66    103     75       N  
ATOM    802  CA  ILE A 112      15.354  25.919  53.801  1.00 23.18           C  
ANISOU  802  CA  ILE A 112     2927   2890   2992    -41     90     60       C  
ATOM    803  C   ILE A 112      15.257  27.280  53.128  1.00 22.09           C  
ANISOU  803  C   ILE A 112     2749   2744   2901      5    100     66       C  
ATOM    804  O   ILE A 112      14.303  28.013  53.345  1.00 22.22           O  
ANISOU  804  O   ILE A 112     2713   2754   2974    -70    264      0       O  
ATOM    805  CB  ILE A 112      14.073  25.141  53.447  1.00 23.28           C  
ANISOU  805  CB  ILE A 112     2900   2932   3015    -46     65     47       C  
ATOM    806  CG1 ILE A 112      13.825  24.018  54.454  1.00 23.76           C  
ANISOU  806  CG1 ILE A 112     2941   3030   3057    -55     30     66       C  
ATOM    807  CG2 ILE A 112      14.149  24.575  52.033  1.00 24.02           C  
ANISOU  807  CG2 ILE A 112     3047   2938   3140    -54     35     84       C  
ATOM    808  CD1 ILE A 112      14.904  22.954  54.498  1.00 24.62           C  
ANISOU  808  CD1 ILE A 112     3119   3029   3207    -55     81     60       C  
ATOM    809  N   GLY A 113      16.252  27.634  52.331  1.00 21.17           N  
ANISOU  809  N   GLY A 113     2628   2621   2796     40    102     28       N  
ATOM    810  CA  GLY A 113      16.204  28.887  51.597  1.00 20.24           C  
ANISOU  810  CA  GLY A 113     2511   2519   2660     25     99     -5       C  
ATOM    811  C   GLY A 113      16.037  28.641  50.119  1.00 19.89           C  
ANISOU  811  C   GLY A 113     2386   2528   2643     -1     32     -3       C  
ATOM    812  O   GLY A 113      16.133  27.496  49.661  1.00 19.10           O  
ANISOU  812  O   GLY A 113     2380   2309   2568    -25     -4    123       O  
HETATM  813  N   MSE A 114      15.814  29.724  49.381  1.00 19.40           N  
ANISOU  813  N   MSE A 114     2273   2473   2626      5     72    -39       N  
HETATM  814  CA  MSE A 114      15.676  29.679  47.925  1.00 20.16           C  
ANISOU  814  CA  MSE A 114     2373   2571   2716    -43     39    -74       C  
HETATM  815  C   MSE A 114      14.599  28.678  47.519  1.00 21.09           C  
ANISOU  815  C   MSE A 114     2489   2714   2810    -76     55   -123       C  
HETATM  816  O   MSE A 114      14.803  27.861  46.630  1.00 20.41           O  
ANISOU  816  O   MSE A 114     2365   2608   2782   -320      5   -264       O  
HETATM  817  CB  MSE A 114      17.010  29.334  47.254  1.00 20.13           C  
ANISOU  817  CB  MSE A 114     2436   2560   2652    -49     78    -44       C  
HETATM  818  CG  MSE A 114      18.040  30.442  47.327  1.00 21.11           C  
ANISOU  818  CG  MSE A 114     2572   2590   2860    -26     71      3       C  
HETATM  819 SE   MSE A 114      17.575  31.977  46.207  1.00 27.52          SE  
ANISOU  819 SE   MSE A 114     3593   3153   3712    -55     52    226      SE  
HETATM  820  CE  MSE A 114      16.950  33.122  47.644  1.00 24.97           C  
ANISOU  820  CE  MSE A 114     3213   3034   3239   -106     75     87       C  
ATOM    821  N   ILE A 115      13.444  28.760  48.173  1.00 21.95           N  
ANISOU  821  N   ILE A 115     2610   2888   2841   -140     97    -88       N  
ATOM    822  CA  ILE A 115      12.283  28.040  47.693  1.00 23.14           C  
ANISOU  822  CA  ILE A 115     2782   3035   2976   -112     52    -73       C  
ATOM    823  C   ILE A 115      11.382  29.030  46.982  1.00 23.85           C  
ANISOU  823  C   ILE A 115     2899   3133   3031    -92     30    -49       C  
ATOM    824  O   ILE A 115      11.445  30.232  47.210  1.00 23.56           O  
ANISOU  824  O   ILE A 115     2748   3233   2971   -154     38    -78       O  
ATOM    825  CB  ILE A 115      11.525  27.319  48.831  1.00 22.95           C  
ANISOU  825  CB  ILE A 115     2796   2985   2938   -109     13    -36       C  
ATOM    826  CG1 ILE A 115      10.942  28.338  49.809  1.00 23.85           C  
ANISOU  826  CG1 ILE A 115     2837   3141   3084   -101     55    -32       C  
ATOM    827  CG2 ILE A 115      12.452  26.342  49.530  1.00 23.81           C  
ANISOU  827  CG2 ILE A 115     2905   3051   3089   -139    119    -19       C  
ATOM    828  CD1 ILE A 115      10.070  27.727  50.880  1.00 25.57           C  
ANISOU  828  CD1 ILE A 115     3205   3306   3204    -71     18     17       C  
ATOM    829  N   SER A 116      10.575  28.514  46.070  1.00 25.56           N  
ANISOU  829  N   SER A 116     3114   3347   3251   -111    -19    -80       N  
ATOM    830  CA  SER A 116       9.643  29.326  45.319  1.00 27.00           C  
ANISOU  830  CA  SER A 116     3327   3519   3414    -63    -44    -48       C  
ATOM    831  C   SER A 116       8.702  30.033  46.276  1.00 28.21           C  
ANISOU  831  C   SER A 116     3468   3696   3556    -50    -77    -71       C  
ATOM    832  O   SER A 116       8.276  29.457  47.274  1.00 28.31           O  
ANISOU  832  O   SER A 116     3444   3724   3588    -66    -44    -49       O  
ATOM    833  CB  SER A 116       8.817  28.417  44.400  1.00 27.03           C  
ANISOU  833  CB  SER A 116     3371   3546   3353    -16    -83    -69       C  
ATOM    834  OG  SER A 116       7.695  29.115  43.912  1.00 28.64           O  
ANISOU  834  OG  SER A 116     3560   3736   3584     50    -33   -192       O  
ATOM    835  N   LYS A 117       8.340  31.269  45.967  1.00 30.17           N  
ANISOU  835  N   LYS A 117     3687   3947   3828    -81    -76    -29       N  
ATOM    836  CA  LYS A 117       7.393  31.982  46.816  1.00 31.88           C  
ANISOU  836  CA  LYS A 117     3890   4166   4057    -30    -45    -30       C  
ATOM    837  C   LYS A 117       5.971  31.398  46.749  1.00 32.73           C  
ANISOU  837  C   LYS A 117     3986   4301   4150     -8    -36     -5       C  
ATOM    838  O   LYS A 117       5.130  31.699  47.594  1.00 32.60           O  
ANISOU  838  O   LYS A 117     3805   4395   4185    -14    -53     57       O  
ATOM    839  CB  LYS A 117       7.424  33.471  46.483  1.00 32.82           C  
ANISOU  839  CB  LYS A 117     4020   4278   4173     -4    -39    -10       C  
ATOM    840  CG  LYS A 117       8.672  34.154  47.039  1.00 34.78           C  
ANISOU  840  CG  LYS A 117     4264   4507   4445    -36    -46    -32       C  
ATOM    841  CD  LYS A 117       8.697  35.643  46.768  1.00 37.83           C  
ANISOU  841  CD  LYS A 117     4748   4758   4867     45    -20    -19       C  
ATOM    842  CE  LYS A 117       9.890  36.314  47.434  1.00 39.45           C  
ANISOU  842  CE  LYS A 117     4882   5016   5093      0      5    -43       C  
ATOM    843  NZ  LYS A 117      11.155  35.575  47.159  1.00 41.06           N  
ANISOU  843  NZ  LYS A 117     5030   5167   5403    -17     22     -4       N  
ATOM    844  N   LYS A 118       5.718  30.535  45.772  1.00 33.70           N  
ANISOU  844  N   LYS A 118     4095   4382   4327    -57    -56      8       N  
ATOM    845  CA  LYS A 118       4.413  29.894  45.641  1.00 34.66           C  
ANISOU  845  CA  LYS A 118     4262   4469   4438    -57    -28     23       C  
ATOM    846  C   LYS A 118       4.334  28.669  46.543  1.00 34.52           C  
ANISOU  846  C   LYS A 118     4235   4465   4416    -77    -19     31       C  
ATOM    847  O   LYS A 118       3.249  28.143  46.800  1.00 34.75           O  
ANISOU  847  O   LYS A 118     4177   4580   4446    -76    -88     62       O  
ATOM    848  CB  LYS A 118       4.174  29.471  44.196  1.00 34.90           C  
ANISOU  848  CB  LYS A 118     4294   4505   4461    -60    -44    -13       C  
ATOM    849  CG  LYS A 118       4.024  30.624  43.221  1.00 36.85           C  
ANISOU  849  CG  LYS A 118     4584   4691   4727    -32    -43     28       C  
ATOM    850  CD  LYS A 118       4.113  30.116  41.797  1.00 40.00           C  
ANISOU  850  CD  LYS A 118     5058   5150   4990     -1    -17     -4       C  
ATOM    851  CE  LYS A 118       3.522  31.101  40.790  1.00 41.70           C  
ANISOU  851  CE  LYS A 118     5277   5331   5236     12    -20     63       C  
ATOM    852  NZ  LYS A 118       3.577  30.515  39.412  1.00 43.29           N  
ANISOU  852  NZ  LYS A 118     5471   5595   5384      6   -102      7       N  
ATOM    853  N   CYS A 119       5.490  28.230  47.025  1.00 33.83           N  
ANISOU  853  N   CYS A 119     4109   4388   4356    -60     12      2       N  
ATOM    854  CA  CYS A 119       5.580  27.051  47.868  1.00 33.96           C  
ANISOU  854  CA  CYS A 119     4133   4412   4360    -76     32    -27       C  
ATOM    855  C   CYS A 119       4.766  27.140  49.140  1.00 34.11           C  
ANISOU  855  C   CYS A 119     4171   4381   4408    -86     46    -20       C  
ATOM    856  O   CYS A 119       4.865  28.082  49.928  1.00 33.00           O  
ANISOU  856  O   CYS A 119     3938   4294   4307   -177    109    -47       O  
ATOM    857  CB  CYS A 119       7.025  26.773  48.260  1.00 34.09           C  
ANISOU  857  CB  CYS A 119     4157   4410   4386    -71     30    -21       C  
ATOM    858  SG  CYS A 119       7.858  25.801  47.041  1.00 35.49           S  
ANISOU  858  SG  CYS A 119     4139   4798   4547   -148     49   -142       S  
ATOM    859  N   THR A 120       3.999  26.081  49.337  1.00 34.55           N  
ANISOU  859  N   THR A 120     4191   4463   4474    -93     24    -40       N  
ATOM    860  CA  THR A 120       3.123  25.947  50.464  1.00 35.08           C  
ANISOU  860  CA  THR A 120     4282   4510   4535   -103      0    -14       C  
ATOM    861  C   THR A 120       3.771  25.132  51.568  1.00 35.42           C  
ANISOU  861  C   THR A 120     4309   4578   4572    -97    -15    -30       C  
ATOM    862  O   THR A 120       4.724  24.400  51.330  1.00 35.54           O  
ANISOU  862  O   THR A 120     4372   4593   4537   -143    -27    -17       O  
ATOM    863  CB  THR A 120       1.858  25.249  49.956  1.00 35.17           C  
ANISOU  863  CB  THR A 120     4252   4573   4539    -92      4      1       C  
ATOM    864  OG1 THR A 120       0.803  26.214  49.892  1.00 36.21           O  
ANISOU  864  OG1 THR A 120     4311   4625   4824    -68     21    -26       O  
ATOM    865  CG2 THR A 120       1.500  24.093  50.827  1.00 35.03           C  
ANISOU  865  CG2 THR A 120     4268   4481   4562    -77    -51    -11       C  
ATOM    866  N   GLU A 121       3.255  25.240  52.786  1.00 36.51           N  
ANISOU  866  N   GLU A 121     4492   4710   4670    -37    -53    -27       N  
ATOM    867  CA  GLU A 121       3.733  24.369  53.838  1.00 37.26           C  
ANISOU  867  CA  GLU A 121     4610   4789   4758    -39    -18      3       C  
ATOM    868  C   GLU A 121       3.612  22.921  53.377  1.00 37.32           C  
ANISOU  868  C   GLU A 121     4622   4788   4770    -35    -18     -8       C  
ATOM    869  O   GLU A 121       4.507  22.117  53.621  1.00 37.10           O  
ANISOU  869  O   GLU A 121     4532   4844   4719   -105    -42      8       O  
ATOM    870  CB  GLU A 121       2.972  24.590  55.141  1.00 37.66           C  
ANISOU  870  CB  GLU A 121     4660   4844   4806    -24    -10     -2       C  
ATOM    871  CG  GLU A 121       3.302  23.534  56.170  1.00 39.43           C  
ANISOU  871  CG  GLU A 121     4902   5049   5030     -6    -11     41       C  
ATOM    872  CD  GLU A 121       2.524  23.693  57.450  1.00 42.06           C  
ANISOU  872  CD  GLU A 121     5205   5458   5317     18     18     -8       C  
ATOM    873  OE1 GLU A 121       2.060  24.821  57.716  1.00 44.29           O  
ANISOU  873  OE1 GLU A 121     5414   5744   5671     83     12    -36       O  
ATOM    874  OE2 GLU A 121       2.396  22.693  58.191  1.00 44.44           O  
ANISOU  874  OE2 GLU A 121     5401   5820   5666   -184    159    138       O  
ATOM    875  N   ASN A 122       2.520  22.582  52.691  1.00 37.79           N  
ANISOU  875  N   ASN A 122     4696   4828   4834     -9    -15    -28       N  
ATOM    876  CA  ASN A 122       2.321  21.201  52.257  1.00 37.97           C  
ANISOU  876  CA  ASN A 122     4724   4831   4870    -27    -10    -26       C  
ATOM    877  C   ASN A 122       3.351  20.778  51.212  1.00 37.62           C  
ANISOU  877  C   ASN A 122     4686   4787   4821    -32     -4    -25       C  
ATOM    878  O   ASN A 122       3.879  19.670  51.266  1.00 37.83           O  
ANISOU  878  O   ASN A 122     4666   4826   4880    -49     27    -33       O  
ATOM    879  CB  ASN A 122       0.923  20.975  51.688  1.00 38.43           C  
ANISOU  879  CB  ASN A 122     4797   4886   4919    -14     -9    -32       C  
ATOM    880  CG  ASN A 122       0.699  19.526  51.299  1.00 39.30           C  
ANISOU  880  CG  ASN A 122     4909   4975   5047    -80    -13     -4       C  
ATOM    881  OD1 ASN A 122       0.807  18.628  52.135  1.00 40.63           O  
ANISOU  881  OD1 ASN A 122     5008   5063   5365    -87      2     30       O  
ATOM    882  ND2 ASN A 122       0.433  19.286  50.021  1.00 40.31           N  
ANISOU  882  ND2 ASN A 122     4949   5145   5221    -95    -63    -81       N  
ATOM    883  N   ASP A 123       3.624  21.667  50.265  1.00 37.16           N  
ANISOU  883  N   ASP A 123     4596   4767   4758    -32    -32    -31       N  
ATOM    884  CA  ASP A 123       4.664  21.443  49.271  1.00 36.98           C  
ANISOU  884  CA  ASP A 123     4637   4714   4701    -55    -35    -23       C  
ATOM    885  C   ASP A 123       5.992  21.055  49.913  1.00 36.30           C  
ANISOU  885  C   ASP A 123     4511   4627   4653    -75      9    -28       C  
ATOM    886  O   ASP A 123       6.651  20.113  49.484  1.00 36.13           O  
ANISOU  886  O   ASP A 123     4441   4667   4619   -144    -14    -17       O  
ATOM    887  CB  ASP A 123       4.858  22.709  48.443  1.00 37.20           C  
ANISOU  887  CB  ASP A 123     4677   4713   4744    -74    -29    -22       C  
ATOM    888  CG  ASP A 123       3.652  23.032  47.598  1.00 38.05           C  
ANISOU  888  CG  ASP A 123     4774   4786   4898    -33    -57    -21       C  
ATOM    889  OD1 ASP A 123       2.942  22.083  47.206  1.00 39.72           O  
ANISOU  889  OD1 ASP A 123     4992   5063   5037   -140   -170    -56       O  
ATOM    890  OD2 ASP A 123       3.400  24.224  47.335  1.00 38.72           O  
ANISOU  890  OD2 ASP A 123     4893   4887   4933   -120    -37    163       O  
ATOM    891  N   ILE A 124       6.397  21.790  50.942  1.00 35.88           N  
ANISOU  891  N   ILE A 124     4446   4629   4557    -60     14      5       N  
ATOM    892  CA  ILE A 124       7.690  21.534  51.553  1.00 35.26           C  
ANISOU  892  CA  ILE A 124     4392   4512   4494    -39     47     17       C  
ATOM    893  C   ILE A 124       7.636  20.205  52.284  1.00 35.38           C  
ANISOU  893  C   ILE A 124     4403   4506   4534    -46     54     33       C  
ATOM    894  O   ILE A 124       8.551  19.402  52.164  1.00 34.38           O  
ANISOU  894  O   ILE A 124     4198   4392   4474   -123    121    106       O  
ATOM    895  CB  ILE A 124       8.114  22.673  52.496  1.00 35.25           C  
ANISOU  895  CB  ILE A 124     4405   4510   4480    -40     31     26       C  
ATOM    896  CG1 ILE A 124       8.259  23.971  51.704  1.00 34.70           C  
ANISOU  896  CG1 ILE A 124     4337   4404   4445     -2     30     12       C  
ATOM    897  CG2 ILE A 124       9.429  22.344  53.175  1.00 34.73           C  
ANISOU  897  CG2 ILE A 124     4350   4419   4428    -26     35     35       C  
ATOM    898  CD1 ILE A 124       9.162  23.831  50.498  1.00 34.83           C  
ANISOU  898  CD1 ILE A 124     4391   4398   4443    -33    -14    -27       C  
ATOM    899  N   ARG A 125       6.546  19.958  53.009  1.00 35.86           N  
ANISOU  899  N   ARG A 125     4464   4566   4595    -53     57     42       N  
ATOM    900  CA  ARG A 125       6.386  18.696  53.730  1.00 36.61           C  
ANISOU  900  CA  ARG A 125     4560   4661   4688    -64     50     39       C  
ATOM    901  C   ARG A 125       6.573  17.512  52.801  1.00 36.88           C  
ANISOU  901  C   ARG A 125     4607   4670   4737   -112     55     33       C  
ATOM    902  O   ARG A 125       7.291  16.565  53.116  1.00 37.05           O  
ANISOU  902  O   ARG A 125     4598   4699   4779   -220     78     83       O  
ATOM    903  CB  ARG A 125       5.018  18.615  54.408  1.00 36.65           C  
ANISOU  903  CB  ARG A 125     4567   4667   4692    -53     58     42       C  
ATOM    904  CG  ARG A 125       4.936  19.402  55.706  1.00 37.11           C  
ANISOU  904  CG  ARG A 125     4644   4712   4745    -55     25     -5       C  
ATOM    905  CD  ARG A 125       3.698  19.029  56.527  1.00 37.82           C  
ANISOU  905  CD  ARG A 125     4673   4817   4880    -48     79     10       C  
ATOM    906  NE  ARG A 125       3.569  19.879  57.704  1.00 39.40           N  
ANISOU  906  NE  ARG A 125     4862   5169   4941   -127    124     16       N  
ATOM    907  CZ  ARG A 125       3.920  19.511  58.931  1.00 40.70           C  
ANISOU  907  CZ  ARG A 125     5004   5244   5218    -45     50     50       C  
ATOM    908  NH1 ARG A 125       4.409  18.298  59.139  1.00 41.14           N  
ANISOU  908  NH1 ARG A 125     5070   5221   5340    -81    175    112       N  
ATOM    909  NH2 ARG A 125       3.773  20.351  59.950  1.00 41.77           N  
ANISOU  909  NH2 ARG A 125     5175   5437   5260    -86     86     19       N  
ATOM    910  N   VAL A 126       5.940  17.586  51.638  1.00 37.96           N  
ANISOU  910  N   VAL A 126     4747   4776   4901   -107     57     25       N  
ATOM    911  CA  VAL A 126       6.049  16.526  50.643  1.00 38.19           C  
ANISOU  911  CA  VAL A 126     4811   4762   4936    -89     63     -3       C  
ATOM    912  C   VAL A 126       7.479  16.377  50.137  1.00 38.18           C  
ANISOU  912  C   VAL A 126     4823   4706   4976    -91     77     10       C  
ATOM    913  O   VAL A 126       7.991  15.262  50.009  1.00 38.05           O  
ANISOU  913  O   VAL A 126     4847   4593   5018   -214    153    -11       O  
ATOM    914  CB  VAL A 126       5.099  16.804  49.475  1.00 38.63           C  
ANISOU  914  CB  VAL A 126     4863   4833   4980    -50     55      4       C  
ATOM    915  CG1 VAL A 126       5.305  15.797  48.340  1.00 39.27           C  
ANISOU  915  CG1 VAL A 126     4932   4955   5033      0     39    -24       C  
ATOM    916  CG2 VAL A 126       3.657  16.769  49.976  1.00 39.43           C  
ANISOU  916  CG2 VAL A 126     4943   4914   5125    -38     47    -14       C  
HETATM  917  N   MSE A 127       8.143  17.499  49.874  1.00 37.93           N  
ANISOU  917  N   MSE A 127     4827   4635   4949   -123     84     -4       N  
HETATM  918  CA  MSE A 127       9.490  17.444  49.324  1.00 38.03           C  
ANISOU  918  CA  MSE A 127     4841   4641   4966   -131     40     -1       C  
HETATM  919  C   MSE A 127      10.439  16.761  50.287  1.00 37.28           C  
ANISOU  919  C   MSE A 127     4757   4528   4879   -165     47     -2       C  
HETATM  920  O   MSE A 127      11.401  16.116  49.869  1.00 37.20           O  
ANISOU  920  O   MSE A 127     4795   4423   4915   -168     11    -35       O  
HETATM  921  CB  MSE A 127      10.012  18.849  49.014  1.00 38.64           C  
ANISOU  921  CB  MSE A 127     4919   4720   5043   -168     74      8       C  
HETATM  922  CG  MSE A 127       9.376  19.504  47.817  1.00 41.39           C  
ANISOU  922  CG  MSE A 127     5327   5029   5369   -206     47     57       C  
HETATM  923 SE   MSE A 127      10.338  21.156  47.393  1.00 51.48          SE  
ANISOU  923 SE   MSE A 127     7018   5703   6838   -782    254    327      SE  
HETATM  924  CE  MSE A 127      12.051  20.658  48.145  1.00 48.68           C  
ANISOU  924  CE  MSE A 127     6497   5801   6197   -236     92     14       C  
ATOM    925  N   PHE A 128      10.188  16.921  51.579  1.00 36.79           N  
ANISOU  925  N   PHE A 128     4688   4469   4822   -175     70     80       N  
ATOM    926  CA  PHE A 128      11.140  16.463  52.578  1.00 36.92           C  
ANISOU  926  CA  PHE A 128     4703   4546   4779   -131     62     77       C  
ATOM    927  C   PHE A 128      10.655  15.268  53.386  1.00 38.14           C  
ANISOU  927  C   PHE A 128     4888   4688   4916   -116     58    107       C  
ATOM    928  O   PHE A 128      11.348  14.817  54.290  1.00 38.10           O  
ANISOU  928  O   PHE A 128     4931   4652   4895   -169    126    102       O  
ATOM    929  CB  PHE A 128      11.465  17.598  53.536  1.00 36.20           C  
ANISOU  929  CB  PHE A 128     4612   4464   4680   -130     68    113       C  
ATOM    930  CG  PHE A 128      12.398  18.613  52.953  1.00 33.66           C  
ANISOU  930  CG  PHE A 128     4246   4184   4359    -84     54     68       C  
ATOM    931  CD1 PHE A 128      13.763  18.408  53.000  1.00 32.29           C  
ANISOU  931  CD1 PHE A 128     4166   3947   4154   -121     53    101       C  
ATOM    932  CD2 PHE A 128      11.910  19.751  52.347  1.00 32.31           C  
ANISOU  932  CD2 PHE A 128     4030   4105   4140    -79     98     86       C  
ATOM    933  CE1 PHE A 128      14.637  19.340  52.461  1.00 31.21           C  
ANISOU  933  CE1 PHE A 128     3960   3954   3944   -117     71     56       C  
ATOM    934  CE2 PHE A 128      12.778  20.685  51.797  1.00 31.04           C  
ANISOU  934  CE2 PHE A 128     3874   3800   4118   -100      9     76       C  
ATOM    935  CZ  PHE A 128      14.138  20.477  51.860  1.00 30.29           C  
ANISOU  935  CZ  PHE A 128     3857   3698   3953    -30     77     69       C  
ATOM    936  N   SER A 129       9.472  14.768  53.059  1.00 39.91           N  
ANISOU  936  N   SER A 129     5104   4938   5121   -110     56     86       N  
ATOM    937  CA  SER A 129       8.866  13.691  53.841  1.00 41.07           C  
ANISOU  937  CA  SER A 129     5229   5125   5250    -82     53     60       C  
ATOM    938  C   SER A 129       9.602  12.357  53.702  1.00 41.88           C  
ANISOU  938  C   SER A 129     5346   5214   5352    -71     53     57       C  
ATOM    939  O   SER A 129       9.543  11.519  54.599  1.00 42.46           O  
ANISOU  939  O   SER A 129     5428   5263   5441   -126     88     81       O  
ATOM    940  CB  SER A 129       7.395  13.550  53.452  1.00 41.25           C  
ANISOU  940  CB  SER A 129     5236   5168   5271    -79     48     41       C  
ATOM    941  OG ASER A 129       7.482  12.748  52.285  0.50 41.19           O  
ANISOU  941  OG ASER A 129     5236   5159   5255    -45     85      8       O  
ATOM    942  OG BSER A 129       6.778  14.361  54.440  0.50 40.79           O  
ANISOU  942  OG BSER A 129     5191   5093   5215    -68     34     26       O  
ATOM    943  N   SER A 130      10.328  12.169  52.606  1.00 42.62           N  
ANISOU  943  N   SER A 130     5460   5309   5426    -73     71     33       N  
ATOM    944  CA  SER A 130      11.037  10.912  52.374  1.00 43.06           C  
ANISOU  944  CA  SER A 130     5479   5387   5493    -49     55     34       C  
ATOM    945  C   SER A 130      12.203  10.708  53.335  1.00 43.53           C  
ANISOU  945  C   SER A 130     5545   5452   5542    -34     56     22       C  
ATOM    946  O   SER A 130      12.731   9.598  53.443  1.00 43.76           O  
ANISOU  946  O   SER A 130     5603   5383   5642    -51     61      8       O  
ATOM    947  CB  SER A 130      11.541  10.832  50.929  1.00 43.16           C  
ANISOU  947  CB  SER A 130     5482   5411   5507    -40     45      3       C  
ATOM    948  OG  SER A 130      12.829  11.421  50.799  1.00 43.38           O  
ANISOU  948  OG  SER A 130     5574   5400   5507    -54    113     66       O  
ATOM    949  N   PHE A 131      12.602  11.762  54.042  1.00 43.59           N  
ANISOU  949  N   PHE A 131     5570   5428   5564    -50     52     21       N  
ATOM    950  CA  PHE A 131      13.775  11.689  54.915  1.00 43.83           C  
ANISOU  950  CA  PHE A 131     5564   5500   5591    -26     33     24       C  
ATOM    951  C   PHE A 131      13.454  11.421  56.384  1.00 44.37           C  
ANISOU  951  C   PHE A 131     5633   5569   5657    -34     22     41       C  
ATOM    952  O   PHE A 131      14.355  11.194  57.194  1.00 44.61           O  
ANISOU  952  O   PHE A 131     5650   5593   5705    -52     29     57       O  
ATOM    953  CB  PHE A 131      14.590  12.980  54.806  1.00 43.80           C  
ANISOU  953  CB  PHE A 131     5574   5500   5567    -16     29     16       C  
ATOM    954  CG  PHE A 131      14.933  13.337  53.400  1.00 43.01           C  
ANISOU  954  CG  PHE A 131     5470   5406   5466     -9     45     37       C  
ATOM    955  CD1 PHE A 131      15.836  12.571  52.685  1.00 42.72           C  
ANISOU  955  CD1 PHE A 131     5456   5329   5446     14     25     62       C  
ATOM    956  CD2 PHE A 131      14.318  14.403  52.774  1.00 42.44           C  
ANISOU  956  CD2 PHE A 131     5417   5288   5419    -35     48     -2       C  
ATOM    957  CE1 PHE A 131      16.138  12.879  51.378  1.00 42.38           C  
ANISOU  957  CE1 PHE A 131     5420   5308   5374      6     56      1       C  
ATOM    958  CE2 PHE A 131      14.621  14.719  51.470  1.00 42.08           C  
ANISOU  958  CE2 PHE A 131     5394   5259   5334    -20     14     22       C  
ATOM    959  CZ  PHE A 131      15.528  13.955  50.769  1.00 42.21           C  
ANISOU  959  CZ  PHE A 131     5360   5300   5376      6     52     54       C  
ATOM    960  N   GLY A 132      12.177  11.452  56.736  1.00 44.84           N  
ANISOU  960  N   GLY A 132     5682   5648   5708     -9     36     37       N  
ATOM    961  CA  GLY A 132      11.785  11.182  58.109  1.00 45.13           C  
ANISOU  961  CA  GLY A 132     5734   5700   5714    -26     21     29       C  
ATOM    962  C   GLY A 132      10.513  11.903  58.485  1.00 45.31           C  
ANISOU  962  C   GLY A 132     5737   5746   5734    -16     27     34       C  
ATOM    963  O   GLY A 132       9.914  12.597  57.666  1.00 45.56           O  
ANISOU  963  O   GLY A 132     5761   5802   5749    -49     50     38       O  
ATOM    964  N   GLN A 133      10.101  11.747  59.736  1.00 45.62           N  
ANISOU  964  N   GLN A 133     5769   5785   5781    -30     34     52       N  
ATOM    965  CA  GLN A 133       8.890  12.399  60.201  1.00 45.93           C  
ANISOU  965  CA  GLN A 133     5821   5818   5811    -33     44     36       C  
ATOM    966  C   GLN A 133       9.151  13.870  60.481  1.00 45.29           C  
ANISOU  966  C   GLN A 133     5728   5763   5717    -59     57     76       C  
ATOM    967  O   GLN A 133      10.100  14.229  61.180  1.00 45.06           O  
ANISOU  967  O   GLN A 133     5661   5732   5729   -110     99    134       O  
ATOM    968  CB  GLN A 133       8.323  11.721  61.457  1.00 46.28           C  
ANISOU  968  CB  GLN A 133     5872   5864   5848    -39     44     56       C  
ATOM    969  CG  GLN A 133       7.210  12.542  62.094  1.00 48.04           C  
ANISOU  969  CG  GLN A 133     6092   6091   6071     -1     48     40       C  
ATOM    970  CD  GLN A 133       6.178  11.703  62.825  1.00 50.25           C  
ANISOU  970  CD  GLN A 133     6286   6361   6444    -48     55     73       C  
ATOM    971  OE1 GLN A 133       6.501  10.678  63.432  1.00 51.03           O  
ANISOU  971  OE1 GLN A 133     6421   6420   6547     28     21    122       O  
ATOM    972  NE2 GLN A 133       4.922  12.146  62.779  1.00 51.45           N  
ANISOU  972  NE2 GLN A 133     6401   6524   6622     22      9     57       N  
ATOM    973  N   ILE A 134       8.280  14.710  59.940  1.00 44.82           N  
ANISOU  973  N   ILE A 134     5632   5719   5680    -51     66     47       N  
ATOM    974  CA  ILE A 134       8.395  16.142  60.106  1.00 44.58           C  
ANISOU  974  CA  ILE A 134     5599   5696   5642    -30     43     15       C  
ATOM    975  C   ILE A 134       7.423  16.592  61.181  1.00 44.53           C  
ANISOU  975  C   ILE A 134     5578   5711   5630    -59     53     42       C  
ATOM    976  O   ILE A 134       6.214  16.499  61.007  1.00 44.54           O  
ANISOU  976  O   ILE A 134     5561   5755   5608   -104     75     48       O  
ATOM    977  CB  ILE A 134       8.098  16.881  58.790  1.00 44.41           C  
ANISOU  977  CB  ILE A 134     5579   5671   5624    -17     42     11       C  
ATOM    978  CG1 ILE A 134       9.149  16.511  57.737  1.00 44.52           C  
ANISOU  978  CG1 ILE A 134     5617   5680   5619     -4     19      8       C  
ATOM    979  CG2 ILE A 134       8.078  18.377  59.026  1.00 44.24           C  
ANISOU  979  CG2 ILE A 134     5570   5648   5592    -29     30     26       C  
ATOM    980  CD1 ILE A 134       8.768  16.877  56.309  1.00 44.23           C  
ANISOU  980  CD1 ILE A 134     5575   5611   5620     24      3     -4       C  
ATOM    981  N   GLU A 135       7.977  17.091  62.279  1.00 44.47           N  
ANISOU  981  N   GLU A 135     5574   5715   5607    -68     54     36       N  
ATOM    982  CA  GLU A 135       7.215  17.518  63.445  1.00 44.78           C  
ANISOU  982  CA  GLU A 135     5620   5718   5678    -45     39     26       C  
ATOM    983  C   GLU A 135       6.691  18.939  63.272  1.00 44.51           C  
ANISOU  983  C   GLU A 135     5571   5715   5625    -48     55     33       C  
ATOM    984  O   GLU A 135       5.690  19.333  63.880  1.00 44.72           O  
ANISOU  984  O   GLU A 135     5594   5768   5630    -72     91     50       O  
ATOM    985  CB  GLU A 135       8.111  17.395  64.680  1.00 45.09           C  
ANISOU  985  CB  GLU A 135     5678   5771   5685    -40     41     25       C  
ATOM    986  CG  GLU A 135       7.996  18.508  65.702  1.00 46.31           C  
ANISOU  986  CG  GLU A 135     5867   5842   5887    -46     57      6       C  
ATOM    987  CD  GLU A 135       9.003  18.351  66.824  1.00 47.68           C  
ANISOU  987  CD  GLU A 135     6040   6048   6029    -37     43      7       C  
ATOM    988  OE1 GLU A 135       9.578  17.252  66.960  1.00 49.23           O  
ANISOU  988  OE1 GLU A 135     6254   6232   6221    -10    112     69       O  
ATOM    989  OE2 GLU A 135       9.231  19.323  67.571  1.00 49.49           O  
ANISOU  989  OE2 GLU A 135     6351   6287   6166   -101     88    -97       O  
ATOM    990  N   GLU A 136       7.356  19.716  62.427  1.00 43.63           N  
ANISOU  990  N   GLU A 136     5463   5624   5491    -43     72     61       N  
ATOM    991  CA  GLU A 136       6.874  21.046  62.122  1.00 43.27           C  
ANISOU  991  CA  GLU A 136     5414   5569   5457    -32     70     57       C  
ATOM    992  C   GLU A 136       7.476  21.575  60.825  1.00 42.25           C  
ANISOU  992  C   GLU A 136     5279   5421   5353    -26     62     79       C  
ATOM    993  O   GLU A 136       8.603  21.240  60.459  1.00 41.40           O  
ANISOU  993  O   GLU A 136     5170   5317   5243    -50    138    148       O  
ATOM    994  CB  GLU A 136       7.179  22.004  63.268  1.00 43.91           C  
ANISOU  994  CB  GLU A 136     5496   5648   5539    -41     62     46       C  
ATOM    995  CG  GLU A 136       6.754  23.440  63.000  1.00 46.28           C  
ANISOU  995  CG  GLU A 136     5830   5867   5886      0     55     49       C  
ATOM    996  CD  GLU A 136       6.977  24.328  64.205  1.00 49.38           C  
ANISOU  996  CD  GLU A 136     6322   6248   6194    -26     26    -34       C  
ATOM    997  OE1 GLU A 136       6.345  24.069  65.249  1.00 51.86           O  
ANISOU  997  OE1 GLU A 136     6603   6618   6485    -33    115     59       O  
ATOM    998  OE2 GLU A 136       7.783  25.278  64.118  1.00 51.60           O  
ANISOU  998  OE2 GLU A 136     6592   6461   6553   -120     21     32       O  
ATOM    999  N   CYS A 137       6.692  22.395  60.139  1.00 41.04           N  
ANISOU  999  N   CYS A 137     5109   5296   5187    -34     58     81       N  
ATOM   1000  CA  CYS A 137       7.111  23.008  58.890  1.00 40.44           C  
ANISOU 1000  CA  CYS A 137     5009   5209   5146    -35     49     54       C  
ATOM   1001  C   CYS A 137       6.402  24.344  58.793  1.00 39.94           C  
ANISOU 1001  C   CYS A 137     4963   5141   5072    -30     46     47       C  
ATOM   1002  O   CYS A 137       5.170  24.409  58.800  1.00 40.01           O  
ANISOU 1002  O   CYS A 137     4935   5162   5105    -27     60     51       O  
ATOM   1003  CB  CYS A 137       6.756  22.111  57.699  1.00 40.31           C  
ANISOU 1003  CB  CYS A 137     5000   5204   5112    -21     49     77       C  
ATOM   1004  SG  CYS A 137       7.200  22.786  56.085  1.00 40.34           S  
ANISOU 1004  SG  CYS A 137     4750   5322   5254   -158    167     85       S  
ATOM   1005  N   ARG A 138       7.192  25.407  58.739  1.00 39.22           N  
ANISOU 1005  N   ARG A 138     4866   5041   4994    -27     62     40       N  
ATOM   1006  CA  ARG A 138       6.674  26.762  58.647  1.00 39.00           C  
ANISOU 1006  CA  ARG A 138     4843   5019   4958    -22     75     51       C  
ATOM   1007  C   ARG A 138       7.339  27.510  57.500  1.00 37.42           C  
ANISOU 1007  C   ARG A 138     4670   4808   4740    -12     61     49       C  
ATOM   1008  O   ARG A 138       8.564  27.603  57.447  1.00 36.57           O  
ANISOU 1008  O   ARG A 138     4540   4736   4619    -55    126    147       O  
ATOM   1009  CB  ARG A 138       6.961  27.542  59.931  1.00 39.70           C  
ANISOU 1009  CB  ARG A 138     4938   5130   5015    -17     50     21       C  
ATOM   1010  CG  ARG A 138       6.427  28.975  59.879  1.00 43.15           C  
ANISOU 1010  CG  ARG A 138     5420   5448   5527     15     48     69       C  
ATOM   1011  CD  ARG A 138       7.283  29.970  60.656  1.00 47.68           C  
ANISOU 1011  CD  ARG A 138     6007   6032   6078    -39    -27    -14       C  
ATOM   1012  NE  ARG A 138       6.987  30.002  62.085  1.00 51.13           N  
ANISOU 1012  NE  ARG A 138     6497   6549   6381     -3     50      9       N  
ATOM   1013  CZ  ARG A 138       7.417  29.090  62.949  1.00 53.75           C  
ANISOU 1013  CZ  ARG A 138     6818   6824   6780     30    -18     58       C  
ATOM   1014  NH1 ARG A 138       8.151  28.074  62.521  1.00 54.93           N  
ANISOU 1014  NH1 ARG A 138     6999   6938   6932     36     55     -8       N  
ATOM   1015  NH2 ARG A 138       7.108  29.188  64.237  1.00 54.57           N  
ANISOU 1015  NH2 ARG A 138     6898   6970   6868     -7     37    -18       N  
ATOM   1016  N   ILE A 139       6.524  28.048  56.604  1.00 35.77           N  
ANISOU 1016  N   ILE A 139     4425   4610   4557    -14     74     -3       N  
ATOM   1017  CA  ILE A 139       6.990  29.007  55.613  1.00 35.23           C  
ANISOU 1017  CA  ILE A 139     4376   4524   4487      4     49     -8       C  
ATOM   1018  C   ILE A 139       7.075  30.370  56.283  1.00 34.99           C  
ANISOU 1018  C   ILE A 139     4320   4508   4468      1     69    -15       C  
ATOM   1019  O   ILE A 139       6.117  30.792  56.924  1.00 34.01           O  
ANISOU 1019  O   ILE A 139     4101   4467   4356     -4    159    -42       O  
ATOM   1020  CB  ILE A 139       5.986  29.134  54.456  1.00 35.20           C  
ANISOU 1020  CB  ILE A 139     4374   4501   4500    -10     27     -3       C  
ATOM   1021  CG1 ILE A 139       5.685  27.763  53.852  1.00 35.69           C  
ANISOU 1021  CG1 ILE A 139     4467   4532   4560     43     40     -2       C  
ATOM   1022  CG2 ILE A 139       6.504  30.083  53.393  1.00 34.77           C  
ANISOU 1022  CG2 ILE A 139     4290   4547   4374      8     -2     37       C  
ATOM   1023  CD1 ILE A 139       6.910  26.996  53.459  1.00 35.68           C  
ANISOU 1023  CD1 ILE A 139     4411   4543   4601     -3     46     12       C  
ATOM   1024  N   LEU A 140       8.202  31.062  56.152  1.00 34.59           N  
ANISOU 1024  N   LEU A 140     4211   4501   4430     -4     94    -14       N  
ATOM   1025  CA  LEU A 140       8.288  32.436  56.640  1.00 35.10           C  
ANISOU 1025  CA  LEU A 140     4310   4549   4477     -6     70    -13       C  
ATOM   1026  C   LEU A 140       7.569  33.365  55.680  1.00 35.20           C  
ANISOU 1026  C   LEU A 140     4321   4554   4501      6     67    -22       C  
ATOM   1027  O   LEU A 140       7.809  33.360  54.473  1.00 34.93           O  
ANISOU 1027  O   LEU A 140     4173   4558   4539     36     85    -57       O  
ATOM   1028  CB  LEU A 140       9.737  32.892  56.806  1.00 35.33           C  
ANISOU 1028  CB  LEU A 140     4367   4583   4474    -32     33     -4       C  
ATOM   1029  CG  LEU A 140      10.441  32.325  58.031  1.00 36.87           C  
ANISOU 1029  CG  LEU A 140     4578   4716   4715    -18     -5     24       C  
ATOM   1030  CD1 LEU A 140      10.283  30.817  58.046  1.00 37.99           C  
ANISOU 1030  CD1 LEU A 140     4746   4815   4875    -17    -40    -14       C  
ATOM   1031  CD2 LEU A 140      11.905  32.733  58.046  1.00 37.18           C  
ANISOU 1031  CD2 LEU A 140     4598   4836   4691    -20     -2      2       C  
ATOM   1032  N   ARG A 141       6.664  34.164  56.228  1.00 35.86           N  
ANISOU 1032  N   ARG A 141     4458   4605   4563     -9     80    -48       N  
ATOM   1033  CA  ARG A 141       5.862  35.059  55.421  1.00 36.29           C  
ANISOU 1033  CA  ARG A 141     4527   4663   4600     25     53    -37       C  
ATOM   1034  C   ARG A 141       5.944  36.457  56.006  1.00 37.43           C  
ANISOU 1034  C   ARG A 141     4648   4795   4779     51     59    -59       C  
ATOM   1035  O   ARG A 141       6.202  36.636  57.197  1.00 37.28           O  
ANISOU 1035  O   ARG A 141     4645   4727   4794    173     88   -134       O  
ATOM   1036  CB  ARG A 141       4.411  34.570  55.335  1.00 36.23           C  
ANISOU 1036  CB  ARG A 141     4522   4623   4619     -6     51    -38       C  
ATOM   1037  CG  ARG A 141       4.269  33.169  54.720  1.00 35.81           C  
ANISOU 1037  CG  ARG A 141     4466   4579   4563     34     45    -29       C  
ATOM   1038  CD  ARG A 141       2.810  32.712  54.578  1.00 35.12           C  
ANISOU 1038  CD  ARG A 141     4353   4472   4519     19      5    -29       C  
ATOM   1039  NE  ARG A 141       2.716  31.378  53.989  1.00 34.86           N  
ANISOU 1039  NE  ARG A 141     4186   4517   4541     96     49     22       N  
ATOM   1040  CZ  ARG A 141       2.799  31.132  52.686  1.00 34.86           C  
ANISOU 1040  CZ  ARG A 141     4261   4442   4542     23    -99    -21       C  
ATOM   1041  NH1 ARG A 141       2.956  32.125  51.828  1.00 34.85           N  
ANISOU 1041  NH1 ARG A 141     4311   4434   4496     24     14    -20       N  
ATOM   1042  NH2 ARG A 141       2.736  29.891  52.234  1.00 36.31           N  
ANISOU 1042  NH2 ARG A 141     4469   4519   4809     17   -104     22       N  
ATOM   1043  N   GLY A 142       5.774  37.444  55.143  1.00 38.85           N  
ANISOU 1043  N   GLY A 142     4810   4971   4979     74     57    -39       N  
ATOM   1044  CA  GLY A 142       5.765  38.826  55.568  1.00 40.34           C  
ANISOU 1044  CA  GLY A 142     5025   5135   5169     18     33    -59       C  
ATOM   1045  C   GLY A 142       4.345  39.259  55.886  1.00 41.42           C  
ANISOU 1045  C   GLY A 142     5137   5287   5313     34     48    -61       C  
ATOM   1046  O   GLY A 142       3.431  38.439  55.926  1.00 41.11           O  
ANISOU 1046  O   GLY A 142     5056   5286   5278     59     67    -97       O  
ATOM   1047  N   PRO A 143       4.156  40.561  56.107  1.00 42.96           N  
ANISOU 1047  N   PRO A 143     5370   5437   5516     11     15    -36       N  
ATOM   1048  CA  PRO A 143       2.895  41.121  56.593  1.00 43.61           C  
ANISOU 1048  CA  PRO A 143     5451   5533   5587     11      8    -33       C  
ATOM   1049  C   PRO A 143       1.682  40.836  55.699  1.00 43.75           C  
ANISOU 1049  C   PRO A 143     5465   5565   5594     -7     14    -46       C  
ATOM   1050  O   PRO A 143       0.574  40.674  56.216  1.00 44.34           O  
ANISOU 1050  O   PRO A 143     5531   5653   5662    -27     37    -66       O  
ATOM   1051  CB  PRO A 143       3.181  42.628  56.648  1.00 43.84           C  
ANISOU 1051  CB  PRO A 143     5483   5544   5632      0      8    -26       C  
ATOM   1052  CG  PRO A 143       4.664  42.729  56.801  1.00 43.95           C  
ANISOU 1052  CG  PRO A 143     5530   5514   5654     12      5    -17       C  
ATOM   1053  CD  PRO A 143       5.208  41.585  55.985  1.00 43.43           C  
ANISOU 1053  CD  PRO A 143     5425   5520   5555      5     33    -20       C  
ATOM   1054  N   ASP A 144       1.885  40.791  54.383  1.00 43.09           N  
ANISOU 1054  N   ASP A 144     5405   5494   5473     18     16    -33       N  
ATOM   1055  CA  ASP A 144       0.794  40.535  53.444  1.00 42.76           C  
ANISOU 1055  CA  ASP A 144     5362   5437   5446     19     20    -31       C  
ATOM   1056  C   ASP A 144       0.642  39.055  53.084  1.00 41.53           C  
ANISOU 1056  C   ASP A 144     5185   5327   5266     40     13    -19       C  
ATOM   1057  O   ASP A 144      -0.004  38.717  52.089  1.00 41.05           O  
ANISOU 1057  O   ASP A 144     5116   5302   5181     60     28    -63       O  
ATOM   1058  CB  ASP A 144       1.002  41.335  52.159  1.00 43.36           C  
ANISOU 1058  CB  ASP A 144     5440   5540   5495     24     -1      1       C  
ATOM   1059  CG  ASP A 144       1.135  42.827  52.410  1.00 45.88           C  
ANISOU 1059  CG  ASP A 144     5821   5784   5829      1     17    -26       C  
ATOM   1060  OD1 ASP A 144       0.328  43.387  53.179  1.00 48.33           O  
ANISOU 1060  OD1 ASP A 144     6078   6081   6203    132     82    -27       O  
ATOM   1061  OD2 ASP A 144       2.050  43.450  51.826  1.00 49.78           O  
ANISOU 1061  OD2 ASP A 144     6250   6277   6387   -115     64     41       O  
ATOM   1062  N   GLY A 145       1.224  38.178  53.896  1.00 39.96           N  
ANISOU 1062  N   GLY A 145     4975   5124   5083     38      6    -42       N  
ATOM   1063  CA  GLY A 145       1.117  36.731  53.686  1.00 38.72           C  
ANISOU 1063  CA  GLY A 145     4807   4991   4912     46     23    -39       C  
ATOM   1064  C   GLY A 145       1.985  36.215  52.545  1.00 37.55           C  
ANISOU 1064  C   GLY A 145     4644   4838   4785     62     -8    -29       C  
ATOM   1065  O   GLY A 145       1.970  35.024  52.228  1.00 36.85           O  
ANISOU 1065  O   GLY A 145     4463   4882   4657    115    -50    -90       O  
ATOM   1066  N   LEU A 146       2.740  37.113  51.926  1.00 36.30           N  
ANISOU 1066  N   LEU A 146     4469   4708   4614     90     36    -26       N  
ATOM   1067  CA  LEU A 146       3.666  36.724  50.872  1.00 35.84           C  
ANISOU 1067  CA  LEU A 146     4411   4630   4575     68    -20     10       C  
ATOM   1068  C   LEU A 146       4.861  36.006  51.482  1.00 34.21           C  
ANISOU 1068  C   LEU A 146     4153   4460   4386     58      0    -20       C  
ATOM   1069  O   LEU A 146       5.439  36.455  52.476  1.00 33.77           O  
ANISOU 1069  O   LEU A 146     3966   4521   4343    152     15    -56       O  
ATOM   1070  CB  LEU A 146       4.119  37.941  50.070  1.00 36.11           C  
ANISOU 1070  CB  LEU A 146     4444   4647   4631     28     13     25       C  
ATOM   1071  CG  LEU A 146       2.964  38.617  49.326  1.00 38.00           C  
ANISOU 1071  CG  LEU A 146     4744   4847   4848     20    -35     35       C  
ATOM   1072  CD1 LEU A 146       3.375  39.971  48.767  1.00 39.09           C  
ANISOU 1072  CD1 LEU A 146     4948   4906   4997     -8     -2     61       C  
ATOM   1073  CD2 LEU A 146       2.450  37.703  48.224  1.00 38.62           C  
ANISOU 1073  CD2 LEU A 146     4862   4949   4862      8      0      7       C  
ATOM   1074  N   SER A 147       5.187  34.868  50.888  1.00 32.45           N  
ANISOU 1074  N   SER A 147     3924   4261   4144     47     -6     21       N  
ATOM   1075  CA  SER A 147       6.327  34.067  51.295  1.00 31.56           C  
ANISOU 1075  CA  SER A 147     3863   4115   4012      2     13     52       C  
ATOM   1076  C   SER A 147       7.615  34.890  51.240  1.00 30.89           C  
ANISOU 1076  C   SER A 147     3760   4022   3956     20      8     44       C  
ATOM   1077  O   SER A 147       7.820  35.671  50.318  1.00 30.35           O  
ANISOU 1077  O   SER A 147     3665   3937   3928     45    -35    145       O  
ATOM   1078  CB  SER A 147       6.449  32.880  50.348  1.00 31.12           C  
ANISOU 1078  CB  SER A 147     3813   4011   3999      0     17     54       C  
ATOM   1079  OG  SER A 147       7.552  32.070  50.684  1.00 30.79           O  
ANISOU 1079  OG  SER A 147     3621   4175   3904    -17    124    118       O  
ATOM   1080  N   ARG A 148       8.489  34.703  52.218  1.00 30.46           N  
ANISOU 1080  N   ARG A 148     3749   3944   3882     12      8    -20       N  
ATOM   1081  CA  ARG A 148       9.815  35.304  52.150  1.00 30.55           C  
ANISOU 1081  CA  ARG A 148     3764   3919   3923     29     13    -41       C  
ATOM   1082  C   ARG A 148      10.777  34.348  51.430  1.00 29.11           C  
ANISOU 1082  C   ARG A 148     3600   3712   3750    -16     14    -71       C  
ATOM   1083  O   ARG A 148      11.987  34.565  51.376  1.00 29.02           O  
ANISOU 1083  O   ARG A 148     3580   3645   3801     58     16    -93       O  
ATOM   1084  CB  ARG A 148      10.299  35.674  53.556  1.00 31.61           C  
ANISOU 1084  CB  ARG A 148     3908   4052   4049     -5    -43    -20       C  
ATOM   1085  CG  ARG A 148       9.544  36.858  54.157  1.00 35.57           C  
ANISOU 1085  CG  ARG A 148     4371   4521   4622     75     31    -78       C  
ATOM   1086  CD  ARG A 148       9.832  37.085  55.638  1.00 42.42           C  
ANISOU 1086  CD  ARG A 148     5338   5521   5257     16    -24    -27       C  
ATOM   1087  NE  ARG A 148       9.593  38.481  56.019  1.00 48.30           N  
ANISOU 1087  NE  ARG A 148     6116   6009   6227     10     -2    -51       N  
ATOM   1088  CZ  ARG A 148       9.054  38.876  57.173  1.00 52.88           C  
ANISOU 1088  CZ  ARG A 148     6750   6728   6613     26     35    -72       C  
ATOM   1089  NH1 ARG A 148       8.663  37.986  58.079  1.00 54.42           N  
ANISOU 1089  NH1 ARG A 148     6953   6878   6845      3     15     22       N  
ATOM   1090  NH2 ARG A 148       8.881  40.169  57.415  1.00 54.89           N  
ANISOU 1090  NH2 ARG A 148     7021   6870   6965      5    -20    -37       N  
ATOM   1091  N   GLY A 149      10.231  33.301  50.831  1.00 27.69           N  
ANISOU 1091  N   GLY A 149     3412   3482   3628     10     96    -47       N  
ATOM   1092  CA  GLY A 149      11.043  32.402  50.025  1.00 26.88           C  
ANISOU 1092  CA  GLY A 149     3388   3351   3474    -41     46    -54       C  
ATOM   1093  C   GLY A 149      11.940  31.523  50.869  1.00 25.46           C  
ANISOU 1093  C   GLY A 149     3214   3141   3318    -60     56    -43       C  
ATOM   1094  O   GLY A 149      12.986  31.068  50.413  1.00 25.10           O  
ANISOU 1094  O   GLY A 149     3213   3073   3251   -164    117     61       O  
ATOM   1095  N   CYS A 150      11.528  31.260  52.101  1.00 24.75           N  
ANISOU 1095  N   CYS A 150     3095   3064   3246    -52     69    -92       N  
ATOM   1096  CA  CYS A 150      12.265  30.338  52.952  1.00 24.72           C  
ANISOU 1096  CA  CYS A 150     3031   3149   3211     -6     89    -90       C  
ATOM   1097  C   CYS A 150      11.363  29.658  53.983  1.00 24.87           C  
ANISOU 1097  C   CYS A 150     3092   3202   3156    -15     70    -43       C  
ATOM   1098  O   CYS A 150      10.217  30.073  54.197  1.00 25.05           O  
ANISOU 1098  O   CYS A 150     3058   3354   3106    -31    164    -64       O  
ATOM   1099  CB  CYS A 150      13.439  31.057  53.626  1.00 24.33           C  
ANISOU 1099  CB  CYS A 150     2960   3070   3214    -29     91    -86       C  
ATOM   1100  SG  CYS A 150      12.986  32.504  54.615  1.00 25.89           S  
ANISOU 1100  SG  CYS A 150     2813   3162   3861     85    276   -295       S  
ATOM   1101  N   ALA A 151      11.877  28.612  54.618  1.00 25.39           N  
ANISOU 1101  N   ALA A 151     3153   3292   3202     11    100    -15       N  
ATOM   1102  CA  ALA A 151      11.078  27.812  55.561  1.00 25.85           C  
ANISOU 1102  CA  ALA A 151     3227   3342   3252      0     53     49       C  
ATOM   1103  C   ALA A 151      11.940  27.236  56.668  1.00 26.96           C  
ANISOU 1103  C   ALA A 151     3371   3507   3366      0     54     97       C  
ATOM   1104  O   ALA A 151      13.166  27.157  56.544  1.00 25.59           O  
ANISOU 1104  O   ALA A 151     3179   3378   3167     -7    101    137       O  
ATOM   1105  CB  ALA A 151      10.402  26.686  54.838  1.00 25.80           C  
ANISOU 1105  CB  ALA A 151     3205   3314   3283     16     79     90       C  
ATOM   1106  N   PHE A 152      11.274  26.806  57.740  1.00 28.12           N  
ANISOU 1106  N   PHE A 152     3467   3716   3502     -6     78     44       N  
ATOM   1107  CA  PHE A 152      11.904  25.965  58.742  1.00 29.15           C  
ANISOU 1107  CA  PHE A 152     3629   3829   3618    -11     46     49       C  
ATOM   1108  C   PHE A 152      11.248  24.591  58.746  1.00 29.75           C  
ANISOU 1108  C   PHE A 152     3712   3901   3691     -1     12     23       C  
ATOM   1109  O   PHE A 152      10.018  24.468  58.713  1.00 30.02           O  
ANISOU 1109  O   PHE A 152     3699   4013   3693    -17    -13     83       O  
ATOM   1110  CB  PHE A 152      11.800  26.612  60.126  1.00 29.99           C  
ANISOU 1110  CB  PHE A 152     3717   3919   3760    -23     13     18       C  
ATOM   1111  CG  PHE A 152      12.628  27.848  60.269  1.00 31.60           C  
ANISOU 1111  CG  PHE A 152     4028   3997   3982    -23    -26     36       C  
ATOM   1112  CD1 PHE A 152      14.001  27.761  60.391  1.00 31.87           C  
ANISOU 1112  CD1 PHE A 152     3992   4097   4021     48    129      6       C  
ATOM   1113  CD2 PHE A 152      12.041  29.093  60.279  1.00 34.80           C  
ANISOU 1113  CD2 PHE A 152     4349   4272   4603     50     14    -67       C  
ATOM   1114  CE1 PHE A 152      14.772  28.886  60.517  1.00 33.89           C  
ANISOU 1114  CE1 PHE A 152     4231   4312   4333     50     55    -72       C  
ATOM   1115  CE2 PHE A 152      12.817  30.233  60.401  1.00 36.06           C  
ANISOU 1115  CE2 PHE A 152     4434   4486   4780    -21     16   -105       C  
ATOM   1116  CZ  PHE A 152      14.188  30.126  60.521  1.00 35.15           C  
ANISOU 1116  CZ  PHE A 152     4390   4392   4573     73    -14    -42       C  
ATOM   1117  N   VAL A 153      12.073  23.554  58.785  1.00 30.43           N  
ANISOU 1117  N   VAL A 153     3797   3991   3775    -11    -10     34       N  
ATOM   1118  CA  VAL A 153      11.581  22.188  58.865  1.00 31.21           C  
ANISOU 1118  CA  VAL A 153     3901   4036   3921    -19      4     50       C  
ATOM   1119  C   VAL A 153      12.237  21.492  60.042  1.00 32.39           C  
ANISOU 1119  C   VAL A 153     4054   4194   4057    -16     12     76       C  
ATOM   1120  O   VAL A 153      13.463  21.431  60.122  1.00 31.84           O  
ANISOU 1120  O   VAL A 153     3942   4143   4012    -29     32    184       O  
ATOM   1121  CB  VAL A 153      11.900  21.416  57.573  1.00 31.20           C  
ANISOU 1121  CB  VAL A 153     3914   4030   3912    -24     15     44       C  
ATOM   1122  CG1 VAL A 153      11.557  19.936  57.705  1.00 31.20           C  
ANISOU 1122  CG1 VAL A 153     3930   4009   3917    -11    -13     28       C  
ATOM   1123  CG2 VAL A 153      11.168  22.048  56.400  1.00 31.19           C  
ANISOU 1123  CG2 VAL A 153     3858   4025   3969     18     14     51       C  
ATOM   1124  N   THR A 154      11.417  20.983  60.957  1.00 33.75           N  
ANISOU 1124  N   THR A 154     4215   4367   4241    -35     47     94       N  
ATOM   1125  CA  THR A 154      11.916  20.270  62.120  1.00 35.04           C  
ANISOU 1125  CA  THR A 154     4421   4543   4349    -25     51     80       C  
ATOM   1126  C   THR A 154      11.608  18.789  61.933  1.00 35.77           C  
ANISOU 1126  C   THR A 154     4558   4633   4401    -44     63    114       C  
ATOM   1127  O   THR A 154      10.463  18.399  61.691  1.00 35.98           O  
ANISOU 1127  O   THR A 154     4657   4638   4376   -116    123    183       O  
ATOM   1128  CB  THR A 154      11.261  20.791  63.414  1.00 35.44           C  
ANISOU 1128  CB  THR A 154     4464   4577   4423    -32     33     57       C  
ATOM   1129  OG1 THR A 154      11.444  22.210  63.514  1.00 37.13           O  
ANISOU 1129  OG1 THR A 154     4810   4726   4571    -19    114     87       O  
ATOM   1130  CG2 THR A 154      11.869  20.139  64.630  1.00 35.67           C  
ANISOU 1130  CG2 THR A 154     4507   4580   4467    -23     20     70       C  
ATOM   1131  N   PHE A 155      12.646  17.967  61.982  1.00 37.01           N  
ANISOU 1131  N   PHE A 155     4746   4792   4525    -30     76    121       N  
ATOM   1132  CA  PHE A 155      12.470  16.528  61.934  1.00 38.45           C  
ANISOU 1132  CA  PHE A 155     4918   4930   4762    -27     47     87       C  
ATOM   1133  C   PHE A 155      12.444  16.035  63.373  1.00 39.65           C  
ANISOU 1133  C   PHE A 155     5087   5106   4874    -50     71     87       C  
ATOM   1134  O   PHE A 155      12.729  16.800  64.291  1.00 39.74           O  
ANISOU 1134  O   PHE A 155     5129   5160   4812   -106    123    153       O  
ATOM   1135  CB  PHE A 155      13.619  15.863  61.181  1.00 38.44           C  
ANISOU 1135  CB  PHE A 155     4932   4921   4753      3     47     93       C  
ATOM   1136  CG  PHE A 155      13.526  15.994  59.696  1.00 38.22           C  
ANISOU 1136  CG  PHE A 155     4897   4846   4777     12     21     89       C  
ATOM   1137  CD1 PHE A 155      12.845  15.054  58.952  1.00 38.15           C  
ANISOU 1137  CD1 PHE A 155     4921   4766   4809     -5     26    134       C  
ATOM   1138  CD2 PHE A 155      14.117  17.065  59.044  1.00 38.43           C  
ANISOU 1138  CD2 PHE A 155     4864   4892   4845    -40     83    108       C  
ATOM   1139  CE1 PHE A 155      12.759  15.164  57.577  1.00 38.79           C  
ANISOU 1139  CE1 PHE A 155     4927   4951   4862    -14     20     84       C  
ATOM   1140  CE2 PHE A 155      14.028  17.185  57.671  1.00 38.27           C  
ANISOU 1140  CE2 PHE A 155     4843   4907   4791    -93     10     72       C  
ATOM   1141  CZ  PHE A 155      13.355  16.244  56.936  1.00 38.02           C  
ANISOU 1141  CZ  PHE A 155     4826   4786   4835    -38     38     87       C  
ATOM   1142  N   THR A 156      12.118  14.763  63.569  1.00 41.25           N  
ANISOU 1142  N   THR A 156     5296   5254   5123    -44     60     87       N  
ATOM   1143  CA  THR A 156      12.025  14.230  64.922  1.00 42.76           C  
ANISOU 1143  CA  THR A 156     5468   5433   5346    -38     54     96       C  
ATOM   1144  C   THR A 156      13.409  13.902  65.451  1.00 43.49           C  
ANISOU 1144  C   THR A 156     5555   5528   5442    -31     26     90       C  
ATOM   1145  O   THR A 156      13.629  13.928  66.658  1.00 43.97           O  
ANISOU 1145  O   THR A 156     5625   5568   5515    -79     84    120       O  
ATOM   1146  CB  THR A 156      11.157  12.971  64.979  1.00 42.82           C  
ANISOU 1146  CB  THR A 156     5492   5406   5370    -38     39     90       C  
ATOM   1147  OG1 THR A 156      11.779  11.936  64.217  1.00 43.59           O  
ANISOU 1147  OG1 THR A 156     5572   5561   5429     16    183    139       O  
ATOM   1148  CG2 THR A 156       9.772  13.238  64.422  1.00 43.12           C  
ANISOU 1148  CG2 THR A 156     5504   5430   5448    -34     43    120       C  
ATOM   1149  N   THR A 157      14.336  13.613  64.541  1.00 44.35           N  
ANISOU 1149  N   THR A 157     5659   5645   5546    -38     45     95       N  
ATOM   1150  CA  THR A 157      15.721  13.302  64.886  1.00 44.86           C  
ANISOU 1150  CA  THR A 157     5710   5710   5625    -50     37     89       C  
ATOM   1151  C   THR A 157      16.718  14.056  63.991  1.00 44.88           C  
ANISOU 1151  C   THR A 157     5696   5713   5644    -55     31     68       C  
ATOM   1152  O   THR A 157      16.584  14.062  62.766  1.00 45.13           O  
ANISOU 1152  O   THR A 157     5740   5751   5656   -105     80    139       O  
ATOM   1153  CB  THR A 157      16.004  11.800  64.727  1.00 45.11           C  
ANISOU 1153  CB  THR A 157     5740   5712   5688    -40     44     59       C  
ATOM   1154  OG1 THR A 157      16.140  11.481  63.338  1.00 45.59           O  
ANISOU 1154  OG1 THR A 157     5854   5777   5693   -108     24    157       O  
ATOM   1155  CG2 THR A 157      14.871  10.953  65.325  1.00 45.42           C  
ANISOU 1155  CG2 THR A 157     5757   5781   5720    -45     39     84       C  
ATOM   1156  N   ARG A 158      17.726  14.673  64.597  1.00 44.46           N  
ANISOU 1156  N   ARG A 158     5645   5647   5601    -37     17     54       N  
ATOM   1157  CA  ARG A 158      18.764  15.348  63.824  1.00 44.26           C  
ANISOU 1157  CA  ARG A 158     5616   5617   5584    -29     25     35       C  
ATOM   1158  C   ARG A 158      19.300  14.449  62.704  1.00 43.93           C  
ANISOU 1158  C   ARG A 158     5587   5555   5550    -31     20     56       C  
ATOM   1159  O   ARG A 158      19.614  14.922  61.606  1.00 43.43           O  
ANISOU 1159  O   ARG A 158     5516   5503   5481    -70     56    118       O  
ATOM   1160  CB  ARG A 158      19.912  15.778  64.738  1.00 44.43           C  
ANISOU 1160  CB  ARG A 158     5636   5672   5573    -13     26     25       C  
ATOM   1161  CG  ARG A 158      21.091  16.387  63.994  1.00 44.75           C  
ANISOU 1161  CG  ARG A 158     5669   5680   5653    -49    -20     36       C  
ATOM   1162  CD  ARG A 158      22.305  16.518  64.884  1.00 44.83           C  
ANISOU 1162  CD  ARG A 158     5652   5719   5661    -17     -9     20       C  
ATOM   1163  NE  ARG A 158      23.375  17.298  64.266  1.00 44.26           N  
ANISOU 1163  NE  ARG A 158     5599   5666   5552     -1      1    -10       N  
ATOM   1164  CZ  ARG A 158      23.442  18.626  64.283  1.00 44.66           C  
ANISOU 1164  CZ  ARG A 158     5652   5733   5584     12    -12     40       C  
ATOM   1165  NH1 ARG A 158      22.491  19.337  64.872  1.00 45.06           N  
ANISOU 1165  NH1 ARG A 158     5656   5813   5651     15     -9     25       N  
ATOM   1166  NH2 ARG A 158      24.462  19.249  63.712  1.00 44.57           N  
ANISOU 1166  NH2 ARG A 158     5635   5740   5560    -18     12     47       N  
ATOM   1167  N   ALA A 159      19.406  13.153  62.985  1.00 43.31           N  
ANISOU 1167  N   ALA A 159     5536   5435   5485    -23     33     77       N  
ATOM   1168  CA  ALA A 159      19.844  12.177  61.988  1.00 42.94           C  
ANISOU 1168  CA  ALA A 159     5487   5386   5441     -9     21     69       C  
ATOM   1169  C   ALA A 159      19.091  12.338  60.676  1.00 42.69           C  
ANISOU 1169  C   ALA A 159     5467   5323   5429    -10     33     78       C  
ATOM   1170  O   ALA A 159      19.693  12.295  59.603  1.00 42.63           O  
ANISOU 1170  O   ALA A 159     5478   5284   5436     53     50    102       O  
ATOM   1171  CB  ALA A 159      19.658  10.763  62.513  1.00 43.16           C  
ANISOU 1171  CB  ALA A 159     5525   5412   5462     -9     11     46       C  
HETATM 1172  N   MSE A 160      17.780  12.534  60.764  1.00 42.14           N  
ANISOU 1172  N   MSE A 160     5400   5225   5387    -49     31    126       N  
HETATM 1173  CA  MSE A 160      16.949  12.708  59.577  1.00 42.31           C  
ANISOU 1173  CA  MSE A 160     5419   5264   5393    -60     34    112       C  
HETATM 1174  C   MSE A 160      17.190  14.062  58.916  1.00 41.05           C  
ANISOU 1174  C   MSE A 160     5259   5100   5239    -72     33    101       C  
HETATM 1175  O   MSE A 160      16.989  14.218  57.711  1.00 40.61           O  
ANISOU 1175  O   MSE A 160     5169   4990   5272   -144     55    211       O  
HETATM 1176  CB  MSE A 160      15.469  12.552  59.932  1.00 43.24           C  
ANISOU 1176  CB  MSE A 160     5504   5404   5522    -82     41    122       C  
HETATM 1177  CG  MSE A 160      15.064  11.133  60.295  1.00 46.46           C  
ANISOU 1177  CG  MSE A 160     6013   5679   5960   -102     12    203       C  
HETATM 1178 SE   MSE A 160      13.165  10.975  60.708  1.00 53.45          SE  
ANISOU 1178 SE   MSE A 160     6911   6638   6761   -362    434    672      SE  
HETATM 1179  CE  MSE A 160      13.070  12.246  62.184  1.00 52.39           C  
ANISOU 1179  CE  MSE A 160     6652   6508   6747   -128    162    242       C  
ATOM   1180  N   ALA A 161      17.618  15.038  59.710  1.00 40.43           N  
ANISOU 1180  N   ALA A 161     5154   5046   5161    -34     52    133       N  
ATOM   1181  CA  ALA A 161      17.874  16.386  59.205  1.00 39.60           C  
ANISOU 1181  CA  ALA A 161     5056   4959   5032    -12     40     93       C  
ATOM   1182  C   ALA A 161      19.162  16.400  58.391  1.00 39.43           C  
ANISOU 1182  C   ALA A 161     5017   4954   5010      1     35    111       C  
ATOM   1183  O   ALA A 161      19.208  16.974  57.303  1.00 38.78           O  
ANISOU 1183  O   ALA A 161     4959   4897   4877     64     40    145       O  
ATOM   1184  CB  ALA A 161      17.947  17.373  60.346  1.00 39.65           C  
ANISOU 1184  CB  ALA A 161     5053   4992   5022    -25     46    114       C  
ATOM   1185  N   GLN A 162      20.195  15.744  58.913  1.00 39.28           N  
ANISOU 1185  N   GLN A 162     4993   4972   4959     20     39    149       N  
ATOM   1186  CA  GLN A 162      21.455  15.568  58.190  1.00 39.63           C  
ANISOU 1186  CA  GLN A 162     5024   5007   5026     32     19    122       C  
ATOM   1187  C   GLN A 162      21.254  14.844  56.864  1.00 38.77           C  
ANISOU 1187  C   GLN A 162     4917   4856   4956     34     64    111       C  
ATOM   1188  O   GLN A 162      21.835  15.216  55.844  1.00 38.92           O  
ANISOU 1188  O   GLN A 162     4985   4829   4975     30     96    230       O  
ATOM   1189  CB  GLN A 162      22.469  14.811  59.053  1.00 40.23           C  
ANISOU 1189  CB  GLN A 162     5086   5079   5122     60     19    100       C  
ATOM   1190  CG  GLN A 162      23.841  14.699  58.417  1.00 41.78           C  
ANISOU 1190  CG  GLN A 162     5251   5331   5294     30     29     75       C  
ATOM   1191  CD  GLN A 162      24.320  16.005  57.797  1.00 43.91           C  
ANISOU 1191  CD  GLN A 162     5638   5460   5585     63    -35     46       C  
ATOM   1192  OE1 GLN A 162      24.642  16.966  58.501  1.00 46.37           O  
ANISOU 1192  OE1 GLN A 162     5952   5734   5931     49   -141    -86       O  
ATOM   1193  NE2 GLN A 162      24.391  16.034  56.471  1.00 43.57           N  
ANISOU 1193  NE2 GLN A 162     5588   5494   5471     86     95    149       N  
ATOM   1194  N   THR A 163      20.419  13.813  56.863  1.00 37.76           N  
ANISOU 1194  N   THR A 163     4820   4728   4798     47     75    146       N  
ATOM   1195  CA  THR A 163      20.145  13.079  55.642  1.00 36.95           C  
ANISOU 1195  CA  THR A 163     4730   4588   4720     38     58    129       C  
ATOM   1196  C   THR A 163      19.488  13.972  54.577  1.00 35.61           C  
ANISOU 1196  C   THR A 163     4587   4392   4552     40     92    103       C  
ATOM   1197  O   THR A 163      19.858  13.921  53.405  1.00 34.43           O  
ANISOU 1197  O   THR A 163     4507   4166   4408      7    135    156       O  
ATOM   1198  CB  THR A 163      19.275  11.847  55.924  1.00 37.64           C  
ANISOU 1198  CB  THR A 163     4809   4709   4785     48     42    113       C  
ATOM   1199  OG1 THR A 163      20.019  10.929  56.739  1.00 38.65           O  
ANISOU 1199  OG1 THR A 163     4998   4606   5080     85     68    289       O  
ATOM   1200  CG2 THR A 163      18.880  11.168  54.635  1.00 38.05           C  
ANISOU 1200  CG2 THR A 163     4809   4759   4888     -5      0     56       C  
ATOM   1201  N   ALA A 164      18.519  14.785  54.992  1.00 33.92           N  
ANISOU 1201  N   ALA A 164     4359   4169   4360      3    112    132       N  
ATOM   1202  CA  ALA A 164      17.867  15.733  54.091  1.00 32.98           C  
ANISOU 1202  CA  ALA A 164     4222   4090   4219     -7     92     84       C  
ATOM   1203  C   ALA A 164      18.846  16.751  53.501  1.00 31.76           C  
ANISOU 1203  C   ALA A 164     4120   3862   4086      8     96     85       C  
ATOM   1204  O   ALA A 164      18.753  17.076  52.326  1.00 30.98           O  
ANISOU 1204  O   ALA A 164     4144   3645   3983    -49    218    134       O  
ATOM   1205  CB  ALA A 164      16.735  16.469  54.808  1.00 32.82           C  
ANISOU 1205  CB  ALA A 164     4216   4064   4191      0    111     62       C  
ATOM   1206  N   ILE A 165      19.741  17.268  54.332  1.00 30.99           N  
ANISOU 1206  N   ILE A 165     4008   3789   3978     56    115    118       N  
ATOM   1207  CA  ILE A 165      20.747  18.237  53.906  1.00 30.96           C  
ANISOU 1207  CA  ILE A 165     4017   3761   3987     77     84     73       C  
ATOM   1208  C   ILE A 165      21.623  17.670  52.783  1.00 31.31           C  
ANISOU 1208  C   ILE A 165     4052   3819   4027     97    125    123       C  
ATOM   1209  O   ILE A 165      21.780  18.272  51.719  1.00 30.35           O  
ANISOU 1209  O   ILE A 165     4031   3590   3912    147    139    193       O  
ATOM   1210  CB  ILE A 165      21.662  18.624  55.079  1.00 30.81           C  
ANISOU 1210  CB  ILE A 165     3968   3765   3973     72     62     73       C  
ATOM   1211  CG1 ILE A 165      20.904  19.491  56.083  1.00 29.79           C  
ANISOU 1211  CG1 ILE A 165     3827   3688   3802     58     43     60       C  
ATOM   1212  CG2 ILE A 165      22.885  19.368  54.573  1.00 31.33           C  
ANISOU 1212  CG2 ILE A 165     4022   3854   4027     80     77     77       C  
ATOM   1213  CD1 ILE A 165      21.670  19.764  57.351  1.00 29.22           C  
ANISOU 1213  CD1 ILE A 165     3761   3540   3800      8     61     19       C  
ATOM   1214  N   LYS A 166      22.180  16.487  53.020  1.00 31.01           N  
ANISOU 1214  N   LYS A 166     4034   3706   4044    113    150    143       N  
ATOM   1215  CA  LYS A 166      23.074  15.885  52.047  1.00 31.55           C  
ANISOU 1215  CA  LYS A 166     4102   3802   4083     85    101     96       C  
ATOM   1216  C   LYS A 166      22.357  15.625  50.739  1.00 30.57           C  
ANISOU 1216  C   LYS A 166     3967   3663   3984     91     97    123       C  
ATOM   1217  O   LYS A 166      22.932  15.777  49.665  1.00 29.70           O  
ANISOU 1217  O   LYS A 166     3915   3460   3908     98    203    201       O  
ATOM   1218  CB  LYS A 166      23.658  14.576  52.583  1.00 32.20           C  
ANISOU 1218  CB  LYS A 166     4197   3880   4159    119     87    145       C  
ATOM   1219  CG  LYS A 166      24.656  13.923  51.630  1.00 33.91           C  
ANISOU 1219  CG  LYS A 166     4387   4197   4299     79     87     24       C  
ATOM   1220  CD  LYS A 166      25.279  12.682  52.258  1.00 36.83           C  
ANISOU 1220  CD  LYS A 166     4716   4531   4745     85      3     81       C  
ATOM   1221  CE  LYS A 166      26.323  13.030  53.314  1.00 39.08           C  
ANISOU 1221  CE  LYS A 166     4950   4889   5008     43     -1     35       C  
ATOM   1222  NZ  LYS A 166      27.720  12.861  52.809  1.00 41.53           N  
ANISOU 1222  NZ  LYS A 166     5195   5235   5351     61    111     46       N  
ATOM   1223  N   ALA A 167      21.090  15.238  50.824  1.00 29.84           N  
ANISOU 1223  N   ALA A 167     3930   3540   3869     31    101    145       N  
ATOM   1224  CA  ALA A 167      20.340  14.903  49.634  1.00 29.23           C  
ANISOU 1224  CA  ALA A 167     3853   3493   3760     -4     65     76       C  
ATOM   1225  C   ALA A 167      19.784  16.129  48.912  1.00 28.62           C  
ANISOU 1225  C   ALA A 167     3827   3402   3647    -10     56     54       C  
ATOM   1226  O   ALA A 167      19.641  16.111  47.698  1.00 28.03           O  
ANISOU 1226  O   ALA A 167     3947   3200   3502    -37    103     52       O  
ATOM   1227  CB  ALA A 167      19.204  13.979  49.993  1.00 30.26           C  
ANISOU 1227  CB  ALA A 167     3969   3665   3863    -15     86     51       C  
HETATM 1228  N   MSE A 168      19.441  17.178  49.649  1.00 27.26           N  
ANISOU 1228  N   MSE A 168     3647   3208   3502    -64     51     42       N  
HETATM 1229  CA  MSE A 168      18.622  18.244  49.078  1.00 26.98           C  
ANISOU 1229  CA  MSE A 168     3560   3162   3530    -75     51     30       C  
HETATM 1230  C   MSE A 168      19.330  19.602  48.925  1.00 25.02           C  
ANISOU 1230  C   MSE A 168     3278   2983   3247    -66     68     41       C  
HETATM 1231  O   MSE A 168      18.880  20.445  48.151  1.00 24.08           O  
ANISOU 1231  O   MSE A 168     3247   2625   3277   -115    139    -40       O  
HETATM 1232  CB  MSE A 168      17.378  18.451  49.934  1.00 27.96           C  
ANISOU 1232  CB  MSE A 168     3606   3316   3701   -105     62     46       C  
HETATM 1233  CG  MSE A 168      16.436  17.256  49.995  1.00 32.54           C  
ANISOU 1233  CG  MSE A 168     4142   3705   4517   -167    165    114       C  
HETATM 1234 SE   MSE A 168      15.559  16.984  48.301  1.00 41.94          SE  
ANISOU 1234 SE   MSE A 168     5626   4436   5872   -860    222     77      SE  
HETATM 1235  CE  MSE A 168      14.043  18.200  48.428  1.00 41.06           C  
ANISOU 1235  CE  MSE A 168     5279   4954   5368   -306     62     17       C  
ATOM   1236  N   HIS A 169      20.407  19.834  49.663  1.00 23.54           N  
ANISOU 1236  N   HIS A 169     3142   2765   3038    -36    101     31       N  
ATOM   1237  CA  HIS A 169      21.083  21.119  49.567  1.00 22.57           C  
ANISOU 1237  CA  HIS A 169     2987   2706   2884      7     83      2       C  
ATOM   1238  C   HIS A 169      21.581  21.349  48.138  1.00 22.34           C  
ANISOU 1238  C   HIS A 169     2946   2669   2874      5    125     33       C  
ATOM   1239  O   HIS A 169      22.302  20.514  47.569  1.00 21.46           O  
ANISOU 1239  O   HIS A 169     3052   2445   2655    -22    233     40       O  
ATOM   1240  CB  HIS A 169      22.226  21.217  50.563  1.00 22.78           C  
ANISOU 1240  CB  HIS A 169     3029   2715   2912     23     62     27       C  
ATOM   1241  CG  HIS A 169      22.944  22.532  50.522  1.00 22.82           C  
ANISOU 1241  CG  HIS A 169     2923   2781   2968     38    -11     12       C  
ATOM   1242  ND1 HIS A 169      22.333  23.728  50.842  1.00 22.53           N  
ANISOU 1242  ND1 HIS A 169     3059   2714   2787    -28    155    -96       N  
ATOM   1243  CD2 HIS A 169      24.211  22.842  50.165  1.00 23.39           C  
ANISOU 1243  CD2 HIS A 169     2997   2801   3090     72    122     40       C  
ATOM   1244  CE1 HIS A 169      23.205  24.710  50.715  1.00 22.95           C  
ANISOU 1244  CE1 HIS A 169     2931   2831   2958    -37     42    -82       C  
ATOM   1245  NE2 HIS A 169      24.356  24.199  50.314  1.00 23.09           N  
ANISOU 1245  NE2 HIS A 169     3072   2698   3002    109     46    -54       N  
ATOM   1246  N   GLN A 170      21.156  22.483  47.587  1.00 22.07           N  
ANISOU 1246  N   GLN A 170     2955   2608   2824    -40    126    -28       N  
ATOM   1247  CA  GLN A 170      21.397  22.911  46.211  1.00 22.13           C  
ANISOU 1247  CA  GLN A 170     2930   2678   2799    -46     85    -39       C  
ATOM   1248  C   GLN A 170      21.114  21.852  45.149  1.00 22.81           C  
ANISOU 1248  C   GLN A 170     3048   2680   2939    -82    114    -79       C  
ATOM   1249  O   GLN A 170      21.755  21.836  44.101  1.00 22.63           O  
ANISOU 1249  O   GLN A 170     3112   2696   2790   -123    138   -120       O  
ATOM   1250  CB  GLN A 170      22.814  23.466  46.057  1.00 21.60           C  
ANISOU 1250  CB  GLN A 170     2850   2597   2759    -31     70     -9       C  
ATOM   1251  CG  GLN A 170      23.099  24.592  47.036  1.00 20.97           C  
ANISOU 1251  CG  GLN A 170     2776   2420   2771    -21     50     46       C  
ATOM   1252  CD  GLN A 170      24.472  25.201  46.873  1.00 21.31           C  
ANISOU 1252  CD  GLN A 170     2687   2508   2901    149     91    -38       C  
ATOM   1253  OE1 GLN A 170      25.467  24.504  46.982  1.00 20.87           O  
ANISOU 1253  OE1 GLN A 170     2661   2245   3023    292    200   -123       O  
ATOM   1254  NE2 GLN A 170      24.534  26.522  46.671  1.00 20.64           N  
ANISOU 1254  NE2 GLN A 170     2662   2117   3064    237    253     10       N  
ATOM   1255  N   ALA A 171      20.127  20.996  45.396  1.00 23.93           N  
ANISOU 1255  N   ALA A 171     3163   2839   3091    -80    133   -108       N  
ATOM   1256  CA  ALA A 171      19.851  19.902  44.464  1.00 24.20           C  
ANISOU 1256  CA  ALA A 171     3213   2856   3127   -125     77    -75       C  
ATOM   1257  C   ALA A 171      19.063  20.367  43.243  1.00 24.01           C  
ANISOU 1257  C   ALA A 171     3241   2789   3092    -79     96    -63       C  
ATOM   1258  O   ALA A 171      19.103  19.723  42.197  1.00 23.66           O  
ANISOU 1258  O   ALA A 171     3439   2401   3149    -82     41   -151       O  
ATOM   1259  CB  ALA A 171      19.102  18.781  45.181  1.00 25.03           C  
ANISOU 1259  CB  ALA A 171     3379   2919   3213    -71    116    -23       C  
ATOM   1260  N   GLN A 172      18.354  21.488  43.361  1.00 23.94           N  
ANISOU 1260  N   GLN A 172     3178   2808   3109   -101     86   -107       N  
ATOM   1261  CA  GLN A 172      17.538  22.018  42.276  1.00 23.93           C  
ANISOU 1261  CA  GLN A 172     3142   2845   3105    -86     81    -88       C  
ATOM   1262  C   GLN A 172      17.320  23.504  42.492  1.00 22.46           C  
ANISOU 1262  C   GLN A 172     2938   2669   2926   -175     87    -55       C  
ATOM   1263  O   GLN A 172      17.519  23.991  43.594  1.00 22.06           O  
ANISOU 1263  O   GLN A 172     2983   2496   2903   -252    240    -75       O  
ATOM   1264  CB  GLN A 172      16.163  21.345  42.267  1.00 25.16           C  
ANISOU 1264  CB  GLN A 172     3300   2953   3307   -137     34    -67       C  
ATOM   1265  CG  GLN A 172      15.400  21.448  43.577  1.00 28.46           C  
ANISOU 1265  CG  GLN A 172     3693   3500   3622   -106     44    -69       C  
ATOM   1266  CD  GLN A 172      14.331  20.358  43.741  1.00 33.98           C  
ANISOU 1266  CD  GLN A 172     4241   4283   4388   -221    -50    100       C  
ATOM   1267  OE1 GLN A 172      13.354  20.309  42.985  1.00 37.53           O  
ANISOU 1267  OE1 GLN A 172     4550   4841   4868   -225   -186    -52       O  
ATOM   1268  NE2 GLN A 172      14.508  19.492  44.746  1.00 35.18           N  
ANISOU 1268  NE2 GLN A 172     4530   4362   4474   -210     18     94       N  
ATOM   1269  N   THR A 173      16.884  24.207  41.460  1.00 21.32           N  
ANISOU 1269  N   THR A 173     2788   2528   2783   -150     94   -101       N  
ATOM   1270  CA  THR A 173      16.471  25.600  41.604  1.00 21.25           C  
ANISOU 1270  CA  THR A 173     2759   2593   2723   -142     57    -41       C  
ATOM   1271  C   THR A 173      14.985  25.706  41.339  1.00 21.93           C  
ANISOU 1271  C   THR A 173     2816   2738   2778   -139     34    -45       C  
ATOM   1272  O   THR A 173      14.479  25.151  40.357  1.00 22.64           O  
ANISOU 1272  O   THR A 173     2942   2872   2790   -259     59    -77       O  
ATOM   1273  CB  THR A 173      17.205  26.518  40.612  1.00 20.47           C  
ANISOU 1273  CB  THR A 173     2668   2443   2665   -116     65    -17       C  
ATOM   1274  OG1 THR A 173      18.614  26.399  40.831  1.00 18.49           O  
ANISOU 1274  OG1 THR A 173     2526   2035   2466   -189    -45      6       O  
ATOM   1275  CG2 THR A 173      16.764  27.962  40.794  1.00 19.86           C  
ANISOU 1275  CG2 THR A 173     2533   2527   2485    -38    124    -29       C  
HETATM 1276  N   MSE A 174      14.282  26.397  42.219  1.00 22.10           N  
ANISOU 1276  N   MSE A 174     2902   2739   2755   -141     16   -120       N  
HETATM 1277  CA  MSE A 174      12.841  26.537  42.093  1.00 23.39           C  
ANISOU 1277  CA  MSE A 174     3003   2934   2952   -129     28   -111       C  
HETATM 1278  C   MSE A 174      12.436  27.792  41.329  1.00 22.80           C  
ANISOU 1278  C   MSE A 174     2925   2868   2870   -124     58   -128       C  
HETATM 1279  O   MSE A 174      13.260  28.683  41.108  1.00 21.83           O  
ANISOU 1279  O   MSE A 174     2701   2837   2757   -186     95   -161       O  
HETATM 1280  CB  MSE A 174      12.196  26.542  43.478  1.00 24.44           C  
ANISOU 1280  CB  MSE A 174     3106   3121   3060   -134     54   -124       C  
HETATM 1281  CG  MSE A 174      12.521  25.320  44.298  1.00 28.48           C  
ANISOU 1281  CG  MSE A 174     3679   3487   3654   -138     31    -19       C  
HETATM 1282 SE   MSE A 174      11.264  25.047  45.778  1.00 37.49          SE  
ANISOU 1282 SE   MSE A 174     4762   4614   4867   -949    358    -96      SE  
HETATM 1283  CE  MSE A 174       9.789  24.288  44.721  1.00 34.84           C  
ANISOU 1283  CE  MSE A 174     4410   4392   4435   -269     65    -30       C  
ATOM   1284  N   GLU A 175      11.160  27.860  40.948  1.00 22.55           N  
ANISOU 1284  N   GLU A 175     2826   2874   2867   -214     28   -135       N  
ATOM   1285  CA  GLU A 175      10.594  28.984  40.219  1.00 23.22           C  
ANISOU 1285  CA  GLU A 175     2928   2922   2974   -134     35   -105       C  
ATOM   1286  C   GLU A 175      10.921  30.324  40.874  1.00 23.22           C  
ANISOU 1286  C   GLU A 175     2910   2962   2952   -123    -16    -94       C  
ATOM   1287  O   GLU A 175      10.682  30.512  42.076  1.00 22.65           O  
ANISOU 1287  O   GLU A 175     2807   2894   2905   -239    -31   -220       O  
ATOM   1288  CB  GLU A 175       9.075  28.829  40.104  1.00 25.07           C  
ANISOU 1288  CB  GLU A 175     3205   3133   3189   -107    -52    -95       C  
ATOM   1289  CG  GLU A 175       8.385  29.869  39.246  1.00 28.71           C  
ANISOU 1289  CG  GLU A 175     3698   3510   3700    -42    -39     31       C  
ATOM   1290  CD  GLU A 175       6.862  29.741  39.254  1.00 34.65           C  
ANISOU 1290  CD  GLU A 175     4160   4372   4634    -29    -80     20       C  
ATOM   1291  OE1 GLU A 175       6.331  28.639  39.537  1.00 37.76           O  
ANISOU 1291  OE1 GLU A 175     4609   4684   5053   -124     -9    -55       O  
ATOM   1292  OE2 GLU A 175       6.190  30.764  38.991  1.00 39.31           O  
ANISOU 1292  OE2 GLU A 175     4819   4833   5284     97   -185     -2       O  
ATOM   1293  N   GLY A 176      11.449  31.245  40.064  1.00 22.63           N  
ANISOU 1293  N   GLY A 176     2847   2815   2938   -108    -42   -112       N  
ATOM   1294  CA  GLY A 176      11.679  32.616  40.491  1.00 22.35           C  
ANISOU 1294  CA  GLY A 176     2800   2751   2941    -34    -50    -66       C  
ATOM   1295  C   GLY A 176      12.933  32.820  41.328  1.00 21.70           C  
ANISOU 1295  C   GLY A 176     2728   2639   2879    -15    -82    -94       C  
ATOM   1296  O   GLY A 176      13.251  33.960  41.682  1.00 21.97           O  
ANISOU 1296  O   GLY A 176     2821   2515   3012    178   -117   -161       O  
ATOM   1297  N   CYS A 177      13.677  31.746  41.599  1.00 20.33           N  
ANISOU 1297  N   CYS A 177     2625   2368   2732    -17    -58   -104       N  
ATOM   1298  CA  CYS A 177      14.821  31.815  42.512  1.00 20.38           C  
ANISOU 1298  CA  CYS A 177     2581   2463   2701    -30      0    -78       C  
ATOM   1299  C   CYS A 177      16.172  31.991  41.807  1.00 19.87           C  
ANISOU 1299  C   CYS A 177     2476   2416   2658      4      0    -82       C  
ATOM   1300  O   CYS A 177      16.446  31.327  40.811  1.00 19.97           O  
ANISOU 1300  O   CYS A 177     2369   2432   2788   -109     32    -35       O  
ATOM   1301  CB  CYS A 177      14.865  30.572  43.394  1.00 20.16           C  
ANISOU 1301  CB  CYS A 177     2621   2425   2612    -27     -6    -96       C  
ATOM   1302  SG  CYS A 177      13.465  30.409  44.529  1.00 22.11           S  
ANISOU 1302  SG  CYS A 177     2678   2739   2985   -206     35    -97       S  
ATOM   1303  N   SER A 178      17.006  32.897  42.321  1.00 19.25           N  
ANISOU 1303  N   SER A 178     2393   2360   2562     49     -1    -71       N  
ATOM   1304  CA  SER A 178      18.278  33.221  41.679  1.00 19.64           C  
ANISOU 1304  CA  SER A 178     2516   2379   2568      2    -43    -21       C  
ATOM   1305  C   SER A 178      19.350  32.148  41.827  1.00 18.90           C  
ANISOU 1305  C   SER A 178     2472   2257   2453     15    -30    -28       C  
ATOM   1306  O   SER A 178      20.345  32.185  41.102  1.00 18.54           O  
ANISOU 1306  O   SER A 178     2636   2101   2309    174   -149     -1       O  
ATOM   1307  CB  SER A 178      18.841  34.523  42.241  1.00 19.94           C  
ANISOU 1307  CB  SER A 178     2523   2476   2579     13    -55    -69       C  
ATOM   1308  OG  SER A 178      19.148  34.338  43.608  1.00 22.26           O  
ANISOU 1308  OG  SER A 178     2557   3020   2880     95    -44    -25       O  
ATOM   1309  N   SER A 179      19.184  31.249  42.799  1.00 19.43           N  
ANISOU 1309  N   SER A 179     2590   2285   2509    -15     -4    -44       N  
ATOM   1310  CA  SER A 179      20.168  30.209  43.093  1.00 19.49           C  
ANISOU 1310  CA  SER A 179     2566   2304   2535    -59    -12      6       C  
ATOM   1311  C   SER A 179      19.452  28.943  43.547  1.00 19.00           C  
ANISOU 1311  C   SER A 179     2487   2242   2492    -54     36      8       C  
ATOM   1312  O   SER A 179      18.289  29.002  43.935  1.00 18.78           O  
ANISOU 1312  O   SER A 179     2381   2201   2552    -60     -5     75       O  
ATOM   1313  CB  SER A 179      21.108  30.605  44.240  1.00 20.39           C  
ANISOU 1313  CB  SER A 179     2763   2372   2612   -129    -34    -15       C  
ATOM   1314  OG  SER A 179      21.489  31.963  44.164  1.00 23.77           O  
ANISOU 1314  OG  SER A 179     3164   2726   3140   -257    -24     49       O  
ATOM   1315  N   PRO A 180      20.167  27.808  43.551  1.00 18.38           N  
ANISOU 1315  N   PRO A 180     2373   2159   2452     21     95     30       N  
ATOM   1316  CA  PRO A 180      19.592  26.533  44.015  1.00 18.09           C  
ANISOU 1316  CA  PRO A 180     2312   2165   2396     30     85     21       C  
ATOM   1317  C   PRO A 180      19.125  26.572  45.486  1.00 18.58           C  
ANISOU 1317  C   PRO A 180     2346   2239   2473     31    108    -16       C  
ATOM   1318  O   PRO A 180      19.678  27.330  46.292  1.00 17.70           O  
ANISOU 1318  O   PRO A 180     2230   2213   2284     89    182    -61       O  
ATOM   1319  CB  PRO A 180      20.762  25.540  43.846  1.00 18.29           C  
ANISOU 1319  CB  PRO A 180     2414   2145   2391     30    104     14       C  
ATOM   1320  CG  PRO A 180      21.661  26.145  42.783  1.00 18.43           C  
ANISOU 1320  CG  PRO A 180     2345   2160   2497     28    115    -67       C  
ATOM   1321  CD  PRO A 180      21.502  27.647  42.943  1.00 18.95           C  
ANISOU 1321  CD  PRO A 180     2446   2132   2624    -55     72     46       C  
HETATM 1322  N   MSE A 181      18.144  25.730  45.824  1.00 19.30           N  
ANISOU 1322  N   MSE A 181     2427   2348   2560    -76    132     -7       N  
HETATM 1323  CA  MSE A 181      17.654  25.574  47.196  1.00 21.05           C  
ANISOU 1323  CA  MSE A 181     2674   2536   2787   -126    126    -27       C  
HETATM 1324  C   MSE A 181      18.776  25.415  48.214  1.00 20.75           C  
ANISOU 1324  C   MSE A 181     2684   2460   2741    -77    143      4       C  
HETATM 1325  O   MSE A 181      19.763  24.724  47.978  1.00 20.77           O  
ANISOU 1325  O   MSE A 181     2777   2418   2698    -46    195    -27       O  
HETATM 1326  CB  MSE A 181      16.729  24.337  47.283  1.00 22.32           C  
ANISOU 1326  CB  MSE A 181     2852   2650   2979   -214    163    -53       C  
HETATM 1327  CG  MSE A 181      15.895  24.281  48.544  1.00 27.09           C  
ANISOU 1327  CG  MSE A 181     3489   3311   3494   -211    171    -21       C  
HETATM 1328 SE   MSE A 181      14.656  22.778  48.492  1.00 42.25          SE  
ANISOU 1328 SE   MSE A 181     5364   4717   5972   -857    544    149      SE  
HETATM 1329  CE  MSE A 181      14.291  22.821  46.598  1.00 29.95           C  
ANISOU 1329  CE  MSE A 181     3593   3314   4474   -458    181    -26       C  
ATOM   1330  N   VAL A 182      18.613  26.079  49.350  1.00 20.68           N  
ANISOU 1330  N   VAL A 182     2650   2484   2722    -25    145      0       N  
ATOM   1331  CA  VAL A 182      19.557  26.047  50.447  1.00 21.24           C  
ANISOU 1331  CA  VAL A 182     2737   2517   2815    -26    146      3       C  
ATOM   1332  C   VAL A 182      18.936  25.183  51.535  1.00 21.66           C  
ANISOU 1332  C   VAL A 182     2775   2624   2830    -15    141     51       C  
ATOM   1333  O   VAL A 182      17.780  25.378  51.905  1.00 21.63           O  
ANISOU 1333  O   VAL A 182     2777   2607   2836   -145    211      8       O  
ATOM   1334  CB  VAL A 182      19.847  27.491  50.956  1.00 21.23           C  
ANISOU 1334  CB  VAL A 182     2749   2536   2780    -19    101     -2       C  
ATOM   1335  CG1 VAL A 182      20.514  27.478  52.305  1.00 22.22           C  
ANISOU 1335  CG1 VAL A 182     2891   2640   2913    -56     60     -8       C  
ATOM   1336  CG2 VAL A 182      20.724  28.207  49.947  1.00 21.24           C  
ANISOU 1336  CG2 VAL A 182     2738   2427   2905    -52    137    -41       C  
ATOM   1337  N   VAL A 183      19.683  24.200  52.013  1.00 22.24           N  
ANISOU 1337  N   VAL A 183     2893   2652   2907    -44    166     73       N  
ATOM   1338  CA  VAL A 183      19.184  23.328  53.069  1.00 23.06           C  
ANISOU 1338  CA  VAL A 183     3013   2787   2963    -24    109     76       C  
ATOM   1339  C   VAL A 183      20.287  23.138  54.079  1.00 23.43           C  
ANISOU 1339  C   VAL A 183     3061   2848   2994     -9    101    118       C  
ATOM   1340  O   VAL A 183      21.327  22.569  53.771  1.00 24.30           O  
ANISOU 1340  O   VAL A 183     3256   2882   3096    109     97    186       O  
ATOM   1341  CB  VAL A 183      18.754  21.955  52.521  1.00 22.74           C  
ANISOU 1341  CB  VAL A 183     2980   2706   2955    -21     78    100       C  
ATOM   1342  CG1 VAL A 183      18.175  21.104  53.655  1.00 23.11           C  
ANISOU 1342  CG1 VAL A 183     2894   2863   3024    -26    147    105       C  
ATOM   1343  CG2 VAL A 183      17.756  22.114  51.402  1.00 22.70           C  
ANISOU 1343  CG2 VAL A 183     2910   2709   3005    -67    113     90       C  
ATOM   1344  N   LYS A 184      20.075  23.645  55.283  1.00 23.98           N  
ANISOU 1344  N   LYS A 184     3164   2958   2988    -14     79    104       N  
ATOM   1345  CA  LYS A 184      21.131  23.656  56.273  1.00 25.30           C  
ANISOU 1345  CA  LYS A 184     3256   3238   3119    -15     54     92       C  
ATOM   1346  C   LYS A 184      20.527  23.720  57.668  1.00 25.93           C  
ANISOU 1346  C   LYS A 184     3344   3398   3110     -2     66     74       C  
ATOM   1347  O   LYS A 184      19.368  24.091  57.823  1.00 24.57           O  
ANISOU 1347  O   LYS A 184     3190   3358   2787     38    133    195       O  
ATOM   1348  CB  LYS A 184      22.023  24.877  56.066  1.00 25.35           C  
ANISOU 1348  CB  LYS A 184     3316   3213   3102    -25     41     95       C  
ATOM   1349  CG  LYS A 184      21.294  26.180  56.250  1.00 26.54           C  
ANISOU 1349  CG  LYS A 184     3447   3374   3264      6     47     54       C  
ATOM   1350  CD  LYS A 184      22.070  27.350  55.637  1.00 28.29           C  
ANISOU 1350  CD  LYS A 184     3659   3547   3544    -84      0     58       C  
ATOM   1351  CE  LYS A 184      23.408  27.504  56.288  1.00 30.02           C  
ANISOU 1351  CE  LYS A 184     3812   3746   3849    -15     10    100       C  
ATOM   1352  NZ  LYS A 184      23.626  28.892  56.734  1.00 31.45           N  
ANISOU 1352  NZ  LYS A 184     4044   3875   4031     16    -58    -10       N  
ATOM   1353  N   PHE A 185      21.309  23.377  58.685  1.00 27.63           N  
ANISOU 1353  N   PHE A 185     3486   3677   3335     55     19     85       N  
ATOM   1354  CA  PHE A 185      20.836  23.608  60.052  1.00 29.26           C  
ANISOU 1354  CA  PHE A 185     3685   3903   3530      4      1     74       C  
ATOM   1355  C   PHE A 185      20.553  25.072  60.321  1.00 30.14           C  
ANISOU 1355  C   PHE A 185     3800   4013   3638     -9    -11     43       C  
ATOM   1356  O   PHE A 185      21.361  25.962  60.015  1.00 29.43           O  
ANISOU 1356  O   PHE A 185     3506   4178   3499    -23     73     57       O  
ATOM   1357  CB  PHE A 185      21.804  23.043  61.092  1.00 29.78           C  
ANISOU 1357  CB  PHE A 185     3747   3952   3617     11    -10     59       C  
ATOM   1358  CG  PHE A 185      21.761  21.557  61.171  1.00 30.48           C  
ANISOU 1358  CG  PHE A 185     3925   3954   3703      2    -58     54       C  
ATOM   1359  CD1 PHE A 185      20.634  20.928  61.655  1.00 32.11           C  
ANISOU 1359  CD1 PHE A 185     4100   4163   3937     -5     45     54       C  
ATOM   1360  CD2 PHE A 185      22.820  20.792  60.727  1.00 31.50           C  
ANISOU 1360  CD2 PHE A 185     4030   4110   3827     33     42     48       C  
ATOM   1361  CE1 PHE A 185      20.559  19.553  61.706  1.00 32.98           C  
ANISOU 1361  CE1 PHE A 185     4294   4154   4082     64     24     81       C  
ATOM   1362  CE2 PHE A 185      22.760  19.418  60.777  1.00 32.09           C  
ANISOU 1362  CE2 PHE A 185     4122   4124   3946     10      6     82       C  
ATOM   1363  CZ  PHE A 185      21.625  18.798  61.265  1.00 33.45           C  
ANISOU 1363  CZ  PHE A 185     4272   4284   4154     61     21     88       C  
ATOM   1364  N   ALA A 186      19.386  25.307  60.911  1.00 31.49           N  
ANISOU 1364  N   ALA A 186     3868   4229   3867    -46     -9     64       N  
ATOM   1365  CA  ALA A 186      18.925  26.644  61.221  1.00 33.29           C  
ANISOU 1365  CA  ALA A 186     4154   4383   4112    -15     -5     39       C  
ATOM   1366  C   ALA A 186      19.839  27.328  62.225  1.00 34.93           C  
ANISOU 1366  C   ALA A 186     4353   4630   4287    -13     -5     33       C  
ATOM   1367  O   ALA A 186      20.468  26.664  63.044  1.00 34.89           O  
ANISOU 1367  O   ALA A 186     4305   4759   4194    -22      1     62       O  
ATOM   1368  CB  ALA A 186      17.498  26.596  61.767  1.00 33.37           C  
ANISOU 1368  CB  ALA A 186     4181   4378   4120    -29      4     23       C  
ATOM   1369  N   ASP A 187      19.899  28.651  62.134  1.00 37.09           N  
ANISOU 1369  N   ASP A 187     4691   4836   4564     -3      5      8       N  
ATOM   1370  CA  ASP A 187      20.629  29.482  63.076  1.00 38.96           C  
ANISOU 1370  CA  ASP A 187     4972   5022   4808     -3      3     -8       C  
ATOM   1371  C   ASP A 187      19.870  29.493  64.400  1.00 39.58           C  
ANISOU 1371  C   ASP A 187     5083   5098   4859     14     -4    -14       C  
ATOM   1372  O   ASP A 187      20.467  29.295  65.457  1.00 40.69           O  
ANISOU 1372  O   ASP A 187     5288   5221   4950      4     -3     -9       O  
ATOM   1373  CB  ASP A 187      20.764  30.913  62.547  1.00 39.65           C  
ANISOU 1373  CB  ASP A 187     5088   5081   4898      6      8    -17       C  
ATOM   1374  CG  ASP A 187      21.776  31.035  61.418  1.00 41.65           C  
ANISOU 1374  CG  ASP A 187     5280   5329   5215    -28     38     11       C  
ATOM   1375  OD1 ASP A 187      22.676  30.171  61.306  1.00 44.07           O  
ANISOU 1375  OD1 ASP A 187     5524   5632   5589     76     24     49       O  
ATOM   1376  OD2 ASP A 187      21.663  32.004  60.634  1.00 43.87           O  
ANISOU 1376  OD2 ASP A 187     5687   5492   5490   -101    -19     65       O  
TER    1377      ASP A 187                                                      
ATOM   1378  P     U B   1      13.017  40.704  47.239  1.00 46.59           P  
ANISOU 1378  P     U B   1     5661   5920   6121     -6     72    -65       P  
ATOM   1379  OP1   U B   1      12.513  39.316  47.234  1.00 47.37           O  
ANISOU 1379  OP1   U B   1     5785   5940   6274    -56     15    -14       O  
ATOM   1380  OP2   U B   1      13.131  41.406  48.537  1.00 47.55           O  
ANISOU 1380  OP2   U B   1     5996   6152   5916    -60     75    -46       O  
ATOM   1381  O5'   U B   1      14.478  40.735  46.589  1.00 40.79           O  
ANISOU 1381  O5'   U B   1     5101   5222   5175    -35    -19    -92       O  
ATOM   1382  C5'   U B   1      14.767  40.160  45.329  1.00 33.89           C  
ANISOU 1382  C5'   U B   1     4138   4223   4514    -42    -47     50       C  
ATOM   1383  C4'   U B   1      16.256  39.896  45.276  1.00 29.16           C  
ANISOU 1383  C4'   U B   1     3837   3457   3784    -85    -67     29       C  
ATOM   1384  O4'   U B   1      16.974  41.151  45.069  1.00 25.48           O  
ANISOU 1384  O4'   U B   1     3490   2721   3470     21   -292    -33       O  
ATOM   1385  C3'   U B   1      16.810  39.300  46.563  1.00 25.77           C  
ANISOU 1385  C3'   U B   1     3313   2997   3481      0     18    -61       C  
ATOM   1386  O3'   U B   1      17.895  38.445  46.303  1.00 23.13           O  
ANISOU 1386  O3'   U B   1     3268   2339   3181    -29      3    -43       O  
ATOM   1387  C2'   U B   1      17.334  40.539  47.273  1.00 22.78           C  
ANISOU 1387  C2'   U B   1     2949   2539   3166    -13     -8    -75       C  
ATOM   1388  O2'   U B   1      18.387  40.268  48.166  1.00 22.93           O  
ANISOU 1388  O2'   U B   1     3278   2245   3189    -26    -95   -127       O  
ATOM   1389  C1'   U B   1      17.913  41.302  46.100  1.00 23.50           C  
ANISOU 1389  C1'   U B   1     3188   2553   3189     78    -77   -159       C  
ATOM   1390  N1    U B   1      18.113  42.748  46.378  1.00 21.79           N  
ANISOU 1390  N1    U B   1     2889   2428   2961     31   -138    -24       N  
ATOM   1391  C2    U B   1      19.386  43.236  46.473  1.00 21.51           C  
ANISOU 1391  C2    U B   1     2845   2489   2836     37    -66   -166       C  
ATOM   1392  O2    U B   1      20.369  42.543  46.364  1.00 22.93           O  
ANISOU 1392  O2    U B   1     2889   2499   3322     51    -80   -140       O  
ATOM   1393  N3    U B   1      19.469  44.574  46.724  1.00 20.77           N  
ANISOU 1393  N3    U B   1     2852   2187   2852     46   -138    -42       N  
ATOM   1394  C4    U B   1      18.419  45.451  46.885  1.00 21.20           C  
ANISOU 1394  C4    U B   1     2806   2438   2809     38    -89    -42       C  
ATOM   1395  O4    U B   1      18.665  46.636  47.119  1.00 21.89           O  
ANISOU 1395  O4    U B   1     3186   2116   3014     55   -180     86       O  
ATOM   1396  C5    U B   1      17.114  44.872  46.777  1.00 21.12           C  
ANISOU 1396  C5    U B   1     2900   2362   2762     77   -189    -44       C  
ATOM   1397  C6    U B   1      17.007  43.562  46.528  1.00 21.90           C  
ANISOU 1397  C6    U B   1     2956   2553   2810     58    -60    -78       C  
ATOM   1398  P     U B   2      17.757  36.855  46.325  1.00 22.87           P  
ANISOU 1398  P     U B   2     3112   2367   3210     17    -46    127       P  
ATOM   1399  OP1   U B   2      18.715  36.375  45.299  1.00 22.87           O  
ANISOU 1399  OP1   U B   2     3588   2260   2842   -181    -87    156       O  
ATOM   1400  OP2   U B   2      16.307  36.592  46.339  1.00 25.69           O  
ANISOU 1400  OP2   U B   2     3380   2940   3441   -111   -128    127       O  
ATOM   1401  O5'   U B   2      18.325  36.441  47.765  1.00 20.95           O  
ANISOU 1401  O5'   U B   2     2877   2239   2842   -109    -44     17       O  
ATOM   1402  C5'   U B   2      17.610  36.695  48.963  1.00 19.90           C  
ANISOU 1402  C5'   U B   2     2480   2354   2724     18    -88    -86       C  
ATOM   1403  C4'   U B   2      18.515  36.461  50.159  1.00 20.54           C  
ANISOU 1403  C4'   U B   2     2582   2486   2733     31   -109    -39       C  
ATOM   1404  O4'   U B   2      18.998  35.087  50.150  1.00 20.72           O  
ANISOU 1404  O4'   U B   2     2596   2576   2697   -110    -16    -85       O  
ATOM   1405  C3'   U B   2      19.776  37.335  50.144  1.00 20.62           C  
ANISOU 1405  C3'   U B   2     2619   2549   2667    -40    -18     14       C  
ATOM   1406  O3'   U B   2      20.125  37.747  51.450  1.00 21.17           O  
ANISOU 1406  O3'   U B   2     2670   2548   2825    -17    -75    -99       O  
ATOM   1407  C2'   U B   2      20.850  36.386  49.635  1.00 20.20           C  
ANISOU 1407  C2'   U B   2     2565   2525   2585    -25    -40     -3       C  
ATOM   1408  O2'   U B   2      22.155  36.699  50.066  1.00 21.43           O  
ANISOU 1408  O2'   U B   2     2660   2538   2942   -138     -9   -151       O  
ATOM   1409  C1'   U B   2      20.407  35.086  50.283  1.00 20.32           C  
ANISOU 1409  C1'   U B   2     2513   2556   2649    -10     32    -97       C  
ATOM   1410  N1    U B   2      20.949  33.876  49.610  1.00 20.86           N  
ANISOU 1410  N1    U B   2     2485   2633   2806    -43     51    -29       N  
ATOM   1411  C2    U B   2      21.808  33.053  50.290  1.00 21.24           C  
ANISOU 1411  C2    U B   2     2468   2705   2896   -138    142     36       C  
ATOM   1412  O2    U B   2      22.163  33.265  51.437  1.00 22.43           O  
ANISOU 1412  O2    U B   2     2347   3022   3151   -194     -6     91       O  
ATOM   1413  N3    U B   2      22.232  31.974  49.568  1.00 21.83           N  
ANISOU 1413  N3    U B   2     2534   2709   3049   -106    180     75       N  
ATOM   1414  C4    U B   2      21.880  31.661  48.275  1.00 23.63           C  
ANISOU 1414  C4    U B   2     2831   2963   3182    -54     88    -42       C  
ATOM   1415  O4    U B   2      22.332  30.651  47.750  1.00 26.67           O  
ANISOU 1415  O4    U B   2     3128   3187   3816     85    242   -168       O  
ATOM   1416  C5    U B   2      20.983  32.576  47.632  1.00 23.92           C  
ANISOU 1416  C5    U B   2     2981   2901   3204    -42     67   -128       C  
ATOM   1417  C6    U B   2      20.558  33.636  48.318  1.00 22.45           C  
ANISOU 1417  C6    U B   2     2724   2845   2959    -28    127    -94       C  
ATOM   1418  P     G B   3      19.526  39.058  52.122  1.00 24.25           P  
ANISOU 1418  P     G B   3     3341   2806   3065    -37    -12   -116       P  
ATOM   1419  OP1   G B   3      19.431  40.116  51.094  1.00 25.30           O  
ANISOU 1419  OP1   G B   3     3527   2987   3098    111    -46   -160       O  
ATOM   1420  OP2   G B   3      20.321  39.244  53.350  1.00 23.84           O  
ANISOU 1420  OP2   G B   3     3294   2676   3086     19    -89   -232       O  
ATOM   1421  O5'   G B   3      18.034  38.664  52.546  1.00 22.17           O  
ANISOU 1421  O5'   G B   3     2911   2618   2894    105    -37   -275       O  
ATOM   1422  C5'   G B   3      17.859  37.770  53.606  1.00 22.66           C  
ANISOU 1422  C5'   G B   3     2917   2842   2850     17      7   -185       C  
ATOM   1423  C4'   G B   3      16.424  37.294  53.670  1.00 23.82           C  
ANISOU 1423  C4'   G B   3     2933   3149   2969     78     37   -147       C  
ATOM   1424  O4'   G B   3      16.062  36.633  52.429  1.00 22.60           O  
ANISOU 1424  O4'   G B   3     2643   3009   2932     90    168   -164       O  
ATOM   1425  C3'   G B   3      16.172  36.278  54.776  1.00 25.07           C  
ANISOU 1425  C3'   G B   3     3218   3177   3128     81    121   -127       C  
ATOM   1426  O3'   G B   3      15.743  36.931  55.981  1.00 26.86           O  
ANISOU 1426  O3'   G B   3     3362   3568   3273     32    247   -182       O  
ATOM   1427  C2'   G B   3      15.050  35.429  54.213  1.00 24.51           C  
ANISOU 1427  C2'   G B   3     3036   3193   3083     83     79    -95       C  
ATOM   1428  O2'   G B   3      13.795  35.975  54.570  1.00 26.08           O  
ANISOU 1428  O2'   G B   3     3182   3328   3396    128    211   -363       O  
ATOM   1429  C1'   G B   3      15.244  35.508  52.699  1.00 23.40           C  
ANISOU 1429  C1'   G B   3     2987   2906   2997     28     41    -92       C  
ATOM   1430  N9    G B   3      15.868  34.324  52.124  1.00 21.38           N  
ANISOU 1430  N9    G B   3     2592   2758   2770    -32    -27   -183       N  
ATOM   1431  C8    G B   3      15.273  33.463  51.220  1.00 22.32           C  
ANISOU 1431  C8    G B   3     2763   2780   2934     39    -27   -126       C  
ATOM   1432  N7    G B   3      16.037  32.476  50.863  1.00 20.53           N  
ANISOU 1432  N7    G B   3     2647   2604   2550    -15     57   -225       N  
ATOM   1433  C5    G B   3      17.216  32.699  51.574  1.00 21.08           C  
ANISOU 1433  C5    G B   3     2617   2721   2670     30     49   -115       C  
ATOM   1434  C6    G B   3      18.420  31.945  51.603  1.00 21.68           C  
ANISOU 1434  C6    G B   3     2688   2733   2814     28    -69    -39       C  
ATOM   1435  O6    G B   3      18.708  30.912  50.969  1.00 21.20           O  
ANISOU 1435  O6    G B   3     2572   2755   2727     41     50   -122       O  
ATOM   1436  N1    G B   3      19.360  32.520  52.452  1.00 20.24           N  
ANISOU 1436  N1    G B   3     2477   2628   2586     16    -25    -81       N  
ATOM   1437  C2    G B   3      19.183  33.657  53.203  1.00 20.91           C  
ANISOU 1437  C2    G B   3     2551   2644   2748    -11    -46    -19       C  
ATOM   1438  N2    G B   3      20.230  34.034  53.970  1.00 19.69           N  
ANISOU 1438  N2    G B   3     2676   2624   2181     16   -164   -107       N  
ATOM   1439  N3    G B   3      18.053  34.360  53.198  1.00 20.49           N  
ANISOU 1439  N3    G B   3     2677   2518   2587     82    -58   -122       N  
ATOM   1440  C4    G B   3      17.121  33.826  52.363  1.00 20.73           C  
ANISOU 1440  C4    G B   3     2656   2524   2695   -101    -30     -8       C  
ATOM   1441  P     U B   4      16.552  36.733  57.336  1.00 29.52           P  
ANISOU 1441  P     U B   4     3779   4020   3417     88    356   -236       P  
ATOM   1442  OP1   U B   4      15.825  37.546  58.349  1.00 31.56           O  
ANISOU 1442  OP1   U B   4     4203   4117   3669     73     34   -374       O  
ATOM   1443  OP2   U B   4      17.988  36.981  57.135  1.00 28.77           O  
ANISOU 1443  OP2   U B   4     3618   3812   3502    -36     13   -350       O  
ATOM   1444  O5'   U B   4      16.369  35.188  57.676  1.00 29.62           O  
ANISOU 1444  O5'   U B   4     3758   3935   3558     44     79   -221       O  
ATOM   1445  C5'   U B   4      15.073  34.712  58.013  1.00 31.01           C  
ANISOU 1445  C5'   U B   4     3964   4125   3691    -55     70    -96       C  
ATOM   1446  C4'   U B   4      15.203  33.751  59.171  1.00 32.52           C  
ANISOU 1446  C4'   U B   4     4197   4138   4021    -11     19     19       C  
ATOM   1447  O4'   U B   4      15.990  32.600  58.776  1.00 31.05           O  
ANISOU 1447  O4'   U B   4     3972   4301   3522    -93     34    -69       O  
ATOM   1448  C3'   U B   4      15.917  34.344  60.379  1.00 34.70           C  
ANISOU 1448  C3'   U B   4     4472   4437   4275      8    -48    -96       C  
ATOM   1449  O3'   U B   4      15.310  33.893  61.564  1.00 41.52           O  
ANISOU 1449  O3'   U B   4     5403   5362   5007    -23     28     13       O  
ATOM   1450  C2'   U B   4      17.338  33.816  60.212  1.00 33.26           C  
ANISOU 1450  C2'   U B   4     4267   4327   4041    -47    -46     -2       C  
ATOM   1451  O2'   U B   4      18.052  33.748  61.425  1.00 32.54           O  
ANISOU 1451  O2'   U B   4     4297   4261   3806    -94      2     30       O  
ATOM   1452  C1'   U B   4      17.093  32.424  59.630  1.00 31.27           C  
ANISOU 1452  C1'   U B   4     3909   4133   3837    -46     76     36       C  
ATOM   1453  N1    U B   4      18.217  31.905  58.808  1.00 29.70           N  
ANISOU 1453  N1    U B   4     3814   3830   3640    -65    -16    -17       N  
ATOM   1454  C2    U B   4      18.855  30.743  59.162  1.00 28.22           C  
ANISOU 1454  C2    U B   4     3716   3501   3504    -95     81    -58       C  
ATOM   1455  O2    U B   4      18.532  30.076  60.128  1.00 28.43           O  
ANISOU 1455  O2    U B   4     3769   3721   3310    -43    194   -240       O  
ATOM   1456  N3    U B   4      19.884  30.373  58.332  1.00 28.40           N  
ANISOU 1456  N3    U B   4     3770   3464   3556   -230    150     40       N  
ATOM   1457  C4    U B   4      20.325  31.050  57.209  1.00 28.55           C  
ANISOU 1457  C4    U B   4     3749   3708   3388    -29    136     19       C  
ATOM   1458  O4    U B   4      21.265  30.601  56.562  1.00 28.11           O  
ANISOU 1458  O4    U B   4     3513   3721   3443    -69    184      5       O  
ATOM   1459  C5    U B   4      19.611  32.257  56.911  1.00 28.22           C  
ANISOU 1459  C5    U B   4     3727   3597   3395    -54    131    -28       C  
ATOM   1460  C6    U B   4      18.602  32.635  57.698  1.00 28.83           C  
ANISOU 1460  C6    U B   4     3634   3745   3572   -141     58    -29       C  
ATOM   1461  P     U B   5      14.675  34.977  62.570  1.00 47.50           P  
ANISOU 1461  P     U B   5     6349   6126   5570     80    188   -194       P  
ATOM   1462  OP1   U B   5      15.702  36.018  62.812  1.00 46.48           O  
ANISOU 1462  OP1   U B   5     6167   5949   5542    138     28   -246       O  
ATOM   1463  OP2   U B   5      14.031  34.196  63.638  1.00 49.53           O  
ANISOU 1463  OP2   U B   5     6510   6369   5939     32    118    -82       O  
ATOM   1464  O5'   U B   5      13.498  35.616  61.689  1.00 54.88           O  
ANISOU 1464  O5'   U B   5     7045   6996   6808    133    -82      5       O  
ATOM   1465  C5'   U B   5      12.230  35.901  62.251  1.00 61.51           C  
ANISOU 1465  C5'   U B   5     7751   7899   7721    122    101      9       C  
ATOM   1466  C4'   U B   5      11.209  34.822  61.944  1.00 66.24           C  
ANISOU 1466  C4'   U B   5     8379   8389   8398    -35    -44    -24       C  
ATOM   1467  O4'   U B   5      11.846  33.526  61.832  1.00 67.86           O  
ANISOU 1467  O4'   U B   5     8640   8597   8547     41     31    -63       O  
ATOM   1468  C3'   U B   5      10.164  34.680  63.045  1.00 69.77           C  
ANISOU 1468  C3'   U B   5     8845   8861   8801     -7     69    -14       C  
ATOM   1469  O3'   U B   5       8.895  35.052  62.544  1.00 73.17           O  
ANISOU 1469  O3'   U B   5     9193   9346   9259     37    -57    -12       O  
ATOM   1470  C2'   U B   5      10.209  33.225  63.500  1.00 70.07           C  
ANISOU 1470  C2'   U B   5     8867   8871   8882      8     23    -12       C  
ATOM   1471  O2'   U B   5       8.928  32.640  63.643  1.00 71.03           O  
ANISOU 1471  O2'   U B   5     8949   9015   9024    -28     29    -14       O  
ATOM   1472  C1'   U B   5      10.995  32.544  62.389  1.00 69.38           C  
ANISOU 1472  C1'   U B   5     8797   8783   8779    -17     19     -8       C  
ATOM   1473  N1    U B   5      11.804  31.425  62.932  1.00 69.93           N  
ANISOU 1473  N1    U B   5     8865   8844   8861     14     11    -11       N  
ATOM   1474  C2    U B   5      11.227  30.173  63.052  1.00 70.06           C  
ANISOU 1474  C2    U B   5     8863   8870   8885     -8     -7    -18       C  
ATOM   1475  O2    U B   5      10.079  29.924  62.725  1.00 69.73           O  
ANISOU 1475  O2    U B   5     8827   8835   8830    -21      5    -64       O  
ATOM   1476  N3    U B   5      12.055  29.211  63.576  1.00 70.02           N  
ANISOU 1476  N3    U B   5     8892   8831   8880     -3      0    -21       N  
ATOM   1477  C4    U B   5      13.368  29.377  63.982  1.00 70.05           C  
ANISOU 1477  C4    U B   5     8891   8870   8854     12     -7    -12       C  
ATOM   1478  O4    U B   5      13.985  28.417  64.431  1.00 69.91           O  
ANISOU 1478  O4    U B   5     8917   8833   8813     12     10    -12       O  
ATOM   1479  C5    U B   5      13.896  30.711  63.830  1.00 69.92           C  
ANISOU 1479  C5    U B   5     8849   8860   8858    -15    -15     -4       C  
ATOM   1480  C6    U B   5      13.107  31.667  63.325  1.00 69.85           C  
ANISOU 1480  C6    U B   5     8850   8835   8853    -11     -3    -18       C  
ATOM   1481  P     U B   6       8.558  36.614  62.568  1.00 76.18           P  
ANISOU 1481  P     U B   6     9672   9596   9676     56    -44    -47       P  
ATOM   1482  OP1   U B   6       9.505  37.311  61.659  1.00 75.94           O  
ANISOU 1482  OP1   U B   6     9626   9631   9595      6    -19    -51       O  
ATOM   1483  OP2   U B   6       8.471  37.004  63.998  1.00 76.33           O  
ANISOU 1483  OP2   U B   6     9653   9694   9653     30    -13    -58       O  
ATOM   1484  O5'   U B   6       7.080  36.652  61.947  1.00 76.95           O  
ANISOU 1484  O5'   U B   6     9704   9785   9746     36    -56    -37       O  
TER    1485        U B   6                                                      
HETATM 1486  O   HOH A   2      15.928  27.486  44.266  1.00 18.53           O  
ANISOU 1486  O   HOH A   2     2772   2024   2243   -246   -202   -213       O  
HETATM 1487  O   HOH A   3      30.177  33.583  97.177  1.00 18.45           O  
ANISOU 1487  O   HOH A   3     2619   1727   2666    -37   -105   -276       O  
HETATM 1488  O   HOH A   4       9.721  27.109  99.272  1.00 22.44           O  
ANISOU 1488  O   HOH A   4     2337   2965   3223   -120    222     17       O  
HETATM 1489  O   HOH A   5      21.541  15.730  91.231  1.00 23.30           O  
ANISOU 1489  O   HOH A   5     2905   2133   3815    -69    368     85       O  
HETATM 1490  O   HOH A   7      12.895   6.996  99.465  1.00 26.36           O  
ANISOU 1490  O   HOH A   7     3309   3082   3624   -282    204    334       O  
HETATM 1491  O   HOH A   8      35.640  30.057 103.223  1.00 25.35           O  
ANISOU 1491  O   HOH A   8     3246   2914   3471    244    -22   -197       O  
HETATM 1492  O   HOH A   9      20.384  25.744  99.753  1.00 22.25           O  
ANISOU 1492  O   HOH A   9     2947   2666   2842    514     96    -63       O  
HETATM 1493  O   HOH A  10       9.398  25.749  41.548  1.00 24.32           O  
ANISOU 1493  O   HOH A  10     2924   2646   3670   -160     23   -363       O  
HETATM 1494  O   HOH A  12      29.379  34.677 100.399  1.00 22.97           O  
ANISOU 1494  O   HOH A  12     3354   2799   2575    337    -27   -155       O  
HETATM 1495  O   HOH A 188      11.365  30.256  37.020  1.00 24.34           O  
ANISOU 1495  O   HOH A 188     2860   3195   3194   -377    -50    304       O  
HETATM 1496  O   HOH A 189      23.864  22.592  57.962  1.00 36.08           O  
ANISOU 1496  O   HOH A 189     3934   5048   4727    252    258    205       O  
HETATM 1497  O   HOH A 190      17.498   7.688  98.726  1.00 29.72           O  
ANISOU 1497  O   HOH A 190     3828   3445   4018   -298    -12    353       O  
HETATM 1498  O   HOH A 191      34.280  31.113  97.204  1.00 25.80           O  
ANISOU 1498  O   HOH A 191     3096   2953   3753   -101     91    114       O  
HETATM 1499  O   HOH A 192      21.597  28.517  59.349  1.00 30.76           O  
ANISOU 1499  O   HOH A 192     3688   4536   3462     52    197    261       O  
HETATM 1500  O   HOH A 193      38.306  28.910  96.228  1.00 34.63           O  
ANISOU 1500  O   HOH A 193     4535   4150   4474      4     75   -265       O  
HETATM 1501  O   HOH A 194      20.980  26.083  82.010  1.00 27.66           O  
ANISOU 1501  O   HOH A 194     3743   3363   3403    320    194      0       O  
HETATM 1502  O   HOH A 195      13.548  32.182  47.725  1.00 26.21           O  
ANISOU 1502  O   HOH A 195     2888   3327   3744     43    401    -70       O  
HETATM 1503  O   HOH A 196      36.003  30.595  99.517  1.00 28.54           O  
ANISOU 1503  O   HOH A 196     4364   2445   4034    157     49    270       O  
HETATM 1504  O   HOH A 197       7.260  29.744  49.780  1.00 27.00           O  
ANISOU 1504  O   HOH A 197     2649   3985   3624   -126    282     46       O  
HETATM 1505  O   HOH A 198      20.103  24.374  39.831  1.00 20.55           O  
ANISOU 1505  O   HOH A 198     3503   1582   2723   -316    309      1       O  
HETATM 1506  O   HOH A 199      30.801  36.702 101.470  1.00 27.32           O  
ANISOU 1506  O   HOH A 199     3525   3095   3762   -110   -261   -156       O  
HETATM 1507  O   HOH A 200      23.741  34.894  45.858  0.50 34.59           O  
ANISOU 1507  O   HOH A 200     4070   4518   4553     86      0      9       O  
HETATM 1508  O   HOH A 201      22.584  34.570  90.279  1.00 31.88           O  
ANISOU 1508  O   HOH A 201     3308   4224   4580    474    165    234       O  
HETATM 1509  O   HOH A 202      13.801   6.939  92.666  1.00 29.87           O  
ANISOU 1509  O   HOH A 202     4326   3460   3563   -311     49    -80       O  
HETATM 1510  O   HOH A 203      24.092  22.524  54.451  1.00 34.05           O  
ANISOU 1510  O   HOH A 203     4149   4231   4556    178      1    -23       O  
HETATM 1511  O   HOH A 204      10.898  33.198  98.482  1.00 29.73           O  
ANISOU 1511  O   HOH A 204     3472   4040   3785    150    252   -126       O  
HETATM 1512  O   HOH A 205      24.313  31.761  45.192  1.00 37.36           O  
ANISOU 1512  O   HOH A 205     4478   4506   5210   -304     49   -150       O  
HETATM 1513  O   HOH A 206       4.014  16.040 101.165  1.00 29.01           O  
ANISOU 1513  O   HOH A 206     3326   3666   4032     -5   -183    -23       O  
HETATM 1514  O   HOH A 207      24.450  33.889  94.661  1.00 39.10           O  
ANISOU 1514  O   HOH A 207     4913   4338   5604    341    226    147       O  
HETATM 1515  O   HOH A 208      21.851  15.808  83.606  1.00 38.93           O  
ANISOU 1515  O   HOH A 208     5409   4548   4834    142    -25   -305       O  
HETATM 1516  O   HOH A 209      10.263  24.029  61.866  1.00 35.97           O  
ANISOU 1516  O   HOH A 209     4735   4625   4307   -143    210     68       O  
HETATM 1517  O   HOH A 210      30.375  38.501  94.987  1.00 29.21           O  
ANISOU 1517  O   HOH A 210     3553   3361   4184    -58    -11    244       O  
HETATM 1518  O   HOH A 211      21.123  11.840  52.038  1.00 35.30           O  
ANISOU 1518  O   HOH A 211     4846   3863   4703     19    225    306       O  
HETATM 1519  O   HOH A 212      25.747  22.670  90.929  1.00 32.84           O  
ANISOU 1519  O   HOH A 212     4930   3498   4051   -258    195    111       O  
HETATM 1520  O   HOH A 213      10.037   5.012  92.533  1.00 35.25           O  
ANISOU 1520  O   HOH A 213     4784   4267   4342   -306    247    145       O  
HETATM 1521  O   HOH A 214      28.285  23.106  94.719  1.00 37.08           O  
ANISOU 1521  O   HOH A 214     4531   4937   4622    254    -30    314       O  
HETATM 1522  O   HOH A 215      23.001  12.998  88.884  1.00 34.60           O  
ANISOU 1522  O   HOH A 215     4848   3814   4486     56    277   -131       O  
HETATM 1523  O   HOH A 216       2.186  19.907  92.151  1.00 34.74           O  
ANISOU 1523  O   HOH A 216     3863   4525   4812     56   -237    280       O  
HETATM 1524  O   HOH A 217      36.076  33.675  95.387  1.00 38.02           O  
ANISOU 1524  O   HOH A 217     4879   5012   4555   -181   -164    116       O  
HETATM 1525  O   HOH A 218       9.577  32.411  43.645  1.00 30.72           O  
ANISOU 1525  O   HOH A 218     4252   3867   3554    -85    411    -18       O  
HETATM 1526  O   HOH A 219      15.069  18.317 105.822  1.00 44.57           O  
ANISOU 1526  O   HOH A 219     5590   5780   5563     24      8     49       O  
HETATM 1527  O   HOH A 220      34.757  36.494  91.697  1.00 36.11           O  
ANISOU 1527  O   HOH A 220     4808   4429   4483   -420    -78    135       O  
HETATM 1528  O   HOH A 221      13.567  34.160  45.911  1.00 35.64           O  
ANISOU 1528  O   HOH A 221     4246   4243   5054     72    -86    -24       O  
HETATM 1529  O   HOH A 222      15.456   9.670 104.287  1.00 30.48           O  
ANISOU 1529  O   HOH A 222     4106   3777   3697   -253    271     71       O  
HETATM 1530  O   HOH A 223      13.370  11.569 104.996  1.00 28.88           O  
ANISOU 1530  O   HOH A 223     3884   3571   3519   -473     81    421       O  
HETATM 1531  O   HOH A 224       8.320   6.897  94.116  1.00 35.00           O  
ANISOU 1531  O   HOH A 224     4456   4139   4705   -350    298    426       O  
HETATM 1532  O   HOH A 225      32.245  36.557  89.746  1.00 39.56           O  
ANISOU 1532  O   HOH A 225     5024   5043   4964   -132    -51    307       O  
HETATM 1533  O   HOH A 226       3.658  27.713  57.074  1.00 40.53           O  
ANISOU 1533  O   HOH A 226     4830   5583   4987    124    -20    260       O  
HETATM 1534  O   HOH A 227      12.895  22.537  41.661  1.00 42.74           O  
ANISOU 1534  O   HOH A 227     4990   5446   5804   -166      0   -284       O  
HETATM 1535  O   HOH A 228      22.361  17.897  47.330  1.00 33.39           O  
ANISOU 1535  O   HOH A 228     4973   3342   4371    -96    365   -234       O  
HETATM 1536  O   HOH A 229      26.599  36.944  94.259  1.00 41.15           O  
ANISOU 1536  O   HOH A 229     5616   4841   5180   -225   -160     73       O  
HETATM 1537  O   HOH A 230      30.088  38.561  90.686  1.00 48.62           O  
ANISOU 1537  O   HOH A 230     6283   6107   6085    -12     53     99       O  
HETATM 1538  O   HOH A 231      16.290  20.876  46.583  1.00 36.61           O  
ANISOU 1538  O   HOH A 231     4708   4371   4833   -402    -90    103       O  
HETATM 1539  O   HOH A 232      24.594  19.869  46.259  1.00 36.02           O  
ANISOU 1539  O   HOH A 232     4776   4190   4719     49    500     17       O  
HETATM 1540  O   HOH A 233       3.449  39.913  52.337  1.00 57.71           O  
ANISOU 1540  O   HOH A 233     7298   7361   7268    100     85     51       O  
HETATM 1541  O   HOH A 234      18.447  17.778  68.011  1.00 56.44           O  
ANISOU 1541  O   HOH A 234     7288   6866   7291     66    -84    -24       O  
HETATM 1542  O   HOH A 235       3.905  34.107  48.478  1.00 42.84           O  
ANISOU 1542  O   HOH A 235     5054   5701   5523    145   -180    -46       O  
HETATM 1543  O   HOH A 236      24.236  25.532 102.214  1.00 53.08           O  
ANISOU 1543  O   HOH A 236     6860   6690   6618     85    -18    138       O  
HETATM 1544  O   HOH A 237      17.670  31.711 103.093  1.00 37.82           O  
ANISOU 1544  O   HOH A 237     4604   4915   4852   -156    305     60       O  
HETATM 1545  O   HOH A 238      16.055  21.311 107.713  1.00 58.95           O  
ANISOU 1545  O   HOH A 238     7441   7571   7387    -10     -3     65       O  
HETATM 1546  O   HOH A 239      21.880  34.215  44.224  1.00 34.34           O  
ANISOU 1546  O   HOH A 239     4140   4332   4576    -25   -107    -32       O  
HETATM 1547  O   HOH A 240       8.905  38.160  99.262  1.00 42.27           O  
ANISOU 1547  O   HOH A 240     5583   5262   5215   -142     89     36       O  
HETATM 1548  O   HOH A 241       7.114  11.993 104.891  1.00 41.00           O  
ANISOU 1548  O   HOH A 241     5773   4825   4981    -55   -279    341       O  
HETATM 1549  O   HOH A 242      24.941  29.028 101.625  1.00 44.41           O  
ANISOU 1549  O   HOH A 242     5924   5711   5239   -239      0    129       O  
HETATM 1550  O   HOH A 243       0.100  46.185  52.848  1.00 49.84           O  
ANISOU 1550  O   HOH A 243     6083   6544   6311   -146   -132   -129       O  
HETATM 1551  O   HOH A 244      14.963  23.341  83.456  1.00 39.49           O  
ANISOU 1551  O   HOH A 244     5381   4327   5296   -103    144     26       O  
HETATM 1552  O   HOH A 245       3.971  24.448 102.963  1.00 43.17           O  
ANISOU 1552  O   HOH A 245     5283   5593   5526   -194    178     38       O  
HETATM 1553  O   HOH A 246      18.066  23.606 108.813  1.00 66.89           O  
ANISOU 1553  O   HOH A 246     8568   8420   8429     22    -15      0       O  
HETATM 1554  O   HOH A 247      27.471  34.114 102.306  1.00 37.28           O  
ANISOU 1554  O   HOH A 247     4708   4788   4668    -66     64    -66       O  
HETATM 1555  O   HOH A 248      33.131  36.500 104.708  1.00 42.16           O  
ANISOU 1555  O   HOH A 248     5328   5112   5578   -214   -143    -11       O  
HETATM 1556  O   HOH A 249       7.139   9.594 103.129  1.00 33.07           O  
ANISOU 1556  O   HOH A 249     4371   3863   4331   -202     99    329       O  
HETATM 1557  O   HOH A 250       9.210  37.368 106.113  1.00 47.76           O  
ANISOU 1557  O   HOH A 250     6217   5899   6029    -26   -186    -72       O  
HETATM 1558  O   HOH A 251      17.269  27.944  81.853  1.00 47.41           O  
ANISOU 1558  O   HOH A 251     5959   5799   6256     78      7    -53       O  
HETATM 1559  O   HOH A 252      15.050   6.154  99.599  1.00 40.17           O  
ANISOU 1559  O   HOH A 252     5417   4734   5112     -1    103    246       O  
HETATM 1560  O   HOH A 253       3.882  22.631  60.880  1.00 42.16           O  
ANISOU 1560  O   HOH A 253     5089   5814   5114   -133     98    264       O  
HETATM 1561  O   HOH A 254      15.730  24.277  71.228  1.00 59.84           O  
ANISOU 1561  O   HOH A 254     7750   7471   7516     -4      3     28       O  
HETATM 1562  O   HOH A 255      20.290  33.229 103.920  1.00 45.76           O  
ANISOU 1562  O   HOH A 255     6085   5208   6093     81   -101     23       O  
HETATM 1563  O   HOH A 256      14.968  30.366  94.375  1.00 31.37           O  
ANISOU 1563  O   HOH A 256     3353   3862   4705   -218    190    347       O  
HETATM 1564  O   HOH A 257       2.053  27.955  54.087  1.00 49.17           O  
ANISOU 1564  O   HOH A 257     6078   6550   6054    128    178    183       O  
HETATM 1565  O   HOH A 258       9.240   2.972  88.338  1.00 38.55           O  
ANISOU 1565  O   HOH A 258     5302   4164   5182   -277    224    144       O  
HETATM 1566  O   HOH A 259      25.072  28.751  62.492  1.00 62.17           O  
ANISOU 1566  O   HOH A 259     7831   7993   7797    -72    -68    -52       O  
HETATM 1567  O   HOH B  12      23.771  35.004  48.774  0.50 19.25           O  
ANISOU 1567  O   HOH B  12     2289   2513   2512      1     -1      0       O  
HETATM 1568  O   HOH B  13      22.284  28.313  46.456  1.00 19.45           O  
ANISOU 1568  O   HOH B  13     2403   2097   2889   -110   -130   -155       O  
HETATM 1569  O   HOH B  14      21.593  31.220  53.762  1.00 28.06           O  
ANISOU 1569  O   HOH B  14     3479   3243   3939    285     36    592       O  
HETATM 1570  O   HOH B  16      21.082  48.286  47.890  1.00 26.71           O  
ANISOU 1570  O   HOH B  16     3316   3373   3459    -70   -314    139       O  
HETATM 1571  O   HOH B  17      21.118  41.319  49.345  1.00 27.97           O  
ANISOU 1571  O   HOH B  17     3788   2752   4089    202   -110    -11       O  
HETATM 1572  O   HOH B  28      10.303  34.992  66.105  0.50 53.78           O  
ANISOU 1572  O   HOH B  28     6806   6881   6748      0      0    -16       O  
HETATM 1573  O   HOH B  32      15.716  34.713  44.204  1.00 23.78           O  
ANISOU 1573  O   HOH B  32     2517   3240   3279   -138   -193   -229       O  
HETATM 1574  O   HOH B  35      24.527  33.683  52.796  1.00 33.64           O  
ANISOU 1574  O   HOH B  35     3872   4781   4129   -192    192    105       O  
HETATM 1575  O   HOH B  40      24.438  30.609  50.696  1.00 32.34           O  
ANISOU 1575  O   HOH B  40     4239   3561   4487    264   -360    134       O  
HETATM 1576  O   HOH B  65      14.215  36.515  47.208  1.00 35.76           O  
ANISOU 1576  O   HOH B  65     4490   4370   4726    -88      2   -102       O  
HETATM 1577  O   HOH B  68      20.297  35.823  56.062  1.00 34.13           O  
ANISOU 1577  O   HOH B  68     4316   4506   4147     33   -186   -223       O  
HETATM 1578  O   HOH B  71      12.800  38.727  53.800  1.00 52.08           O  
ANISOU 1578  O   HOH B  71     6604   6849   6335      0    137     24       O  
HETATM 1579  O   HOH B  83      11.518  39.401  49.619  1.00 64.08           O  
ANISOU 1579  O   HOH B  83     8151   8116   8081     -1    -19    -45       O  
HETATM 1580  O   HOH B  90      10.428  27.145  63.612  1.00 54.40           O  
ANISOU 1580  O   HOH B  90     7027   7078   6563     47      1      1       O  
HETATM 1581  O   HOH B  91      21.779  37.572  54.806  1.00 39.24           O  
ANISOU 1581  O   HOH B  91     4677   5339   4894   -229    -98   -257       O  
CONECT   30   37                                                                
CONECT   37   30   38                                                           
CONECT   38   37   39   41                                                      
CONECT   39   38   40   45                                                      
CONECT   40   39                                                                
CONECT   41   38   42                                                           
CONECT   42   41   43                                                           
CONECT   43   42   44                                                           
CONECT   44   43                                                                
CONECT   45   39                                                                
CONECT  555  561                                                                
CONECT  561  555  562                                                           
CONECT  562  561  563  565                                                      
CONECT  563  562  564  569                                                      
CONECT  564  563                                                                
CONECT  565  562  566                                                           
CONECT  566  565  567                                                           
CONECT  567  566  568                                                           
CONECT  568  567                                                                
CONECT  569  563                                                                
CONECT  602  604                                                                
CONECT  604  602  605                                                           
CONECT  605  604  606  608                                                      
CONECT  606  605  607  612                                                      
CONECT  607  606                                                                
CONECT  608  605  609                                                           
CONECT  609  608  610                                                           
CONECT  610  609  611                                                           
CONECT  611  610                                                                
CONECT  612  606                                                                
CONECT  649  656                                                                
CONECT  656  649  657                                                           
CONECT  657  656  658  660                                                      
CONECT  658  657  659  664                                                      
CONECT  659  658                                                                
CONECT  660  657  661                                                           
CONECT  661  660  662                                                           
CONECT  662  661  663                                                           
CONECT  663  662                                                                
CONECT  664  658                                                                
CONECT  811  813                                                                
CONECT  813  811  814                                                           
CONECT  814  813  815  817                                                      
CONECT  815  814  816  821                                                      
CONECT  816  815                                                                
CONECT  817  814  818                                                           
CONECT  818  817  819                                                           
CONECT  819  818  820                                                           
CONECT  820  819                                                                
CONECT  821  815                                                                
CONECT  912  917                                                                
CONECT  917  912  918                                                           
CONECT  918  917  919  921                                                      
CONECT  919  918  920  925                                                      
CONECT  920  919                                                                
CONECT  921  918  922                                                           
CONECT  922  921  923                                                           
CONECT  923  922  924                                                           
CONECT  924  923                                                                
CONECT  925  919                                                                
CONECT 1169 1172                                                                
CONECT 1172 1169 1173                                                           
CONECT 1173 1172 1174 1176                                                      
CONECT 1174 1173 1175 1180                                                      
CONECT 1175 1174                                                                
CONECT 1176 1173 1177                                                           
CONECT 1177 1176 1178                                                           
CONECT 1178 1177 1179                                                           
CONECT 1179 1178                                                                
CONECT 1180 1174                                                                
CONECT 1225 1228                                                                
CONECT 1228 1225 1229                                                           
CONECT 1229 1228 1230 1232                                                      
CONECT 1230 1229 1231 1236                                                      
CONECT 1231 1230                                                                
CONECT 1232 1229 1233                                                           
CONECT 1233 1232 1234                                                           
CONECT 1234 1233 1235                                                           
CONECT 1235 1234                                                                
CONECT 1236 1230                                                                
CONECT 1271 1276                                                                
CONECT 1276 1271 1277                                                           
CONECT 1277 1276 1278 1280                                                      
CONECT 1278 1277 1279 1284                                                      
CONECT 1279 1278                                                                
CONECT 1280 1277 1281                                                           
CONECT 1281 1280 1282                                                           
CONECT 1282 1281 1283                                                           
CONECT 1283 1282                                                                
CONECT 1284 1278                                                                
CONECT 1317 1322                                                                
CONECT 1322 1317 1323                                                           
CONECT 1323 1322 1324 1326                                                      
CONECT 1324 1323 1325 1330                                                      
CONECT 1325 1324                                                                
CONECT 1326 1323 1327                                                           
CONECT 1327 1326 1328                                                           
CONECT 1328 1327 1329                                                           
CONECT 1329 1328                                                                
CONECT 1330 1324                                                                
MASTER      315    0   10    7    8    0    0    6 1578    2  100   15          
END

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Related entries of code: 3nmr

Entries with 90% protein sequence similarity cutoff in PDBbind
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Complexes with the same small molecule ligand
PDB Code	Check Database	Ligand Name
2kkf	RCSB PDB PDBbind	12-mer
2xnr	RCSB PDB PDBbind	12-mer
3bsu	RCSB PDB PDBbind	12-mer
3kjp	RCSB PDB PDBbind	12-mer
3lwl	RCSB PDB PDBbind	12-mer
3lwm	RCSB PDB PDBbind	12-mer
3m8r	RCSB PDB PDBbind	12-mer
3m8s	RCSB PDB PDBbind	12-mer
3odh	RCSB PDB PDBbind	12-mer
5exh	RCSB PDB PDBbind	12-mer
5mpf	RCSB PDB PDBbind	12-mer

Entry Information

PDB ID	3nmr
Complex Type	Protein-Nucleic Acid
PDBbind Subset	general set
Protein Name	CUGBP Elav-like family member 1 RRM1-RRM2 domain
Ligand Name	12-mer
EC.Number	E.C.-.-.-.-
Resolution	1.85(Å)
Affinity (Kd/Ki/IC50)	Kd=0.65uM
Release Year	2010
Protein/NA Sequence	Check fasta file
Primary Reference	(2010) Structure Vol. 18: pp. 1364-1377

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): Q92879
Entrez Gene ID	NCBI Entrez Gene ID: 10658
ASD	Information of known allosteric effects of PDB entries

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