HEADER    MEMBRANE PROTEIN                        23-OCT-11   3UB8              
TITLE     PERIPLASMIC PORTION OF THE HELICOBACTER PYLORI CHEMORECEPTOR TLPB WITH
TITLE    2 FORMAMIDE BOUND                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHEMORECEPTOR TLPB;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: PERIPLASMIC PORTION;                                       
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HELICOBACTER PYLORI;                            
SOURCE   3 ORGANISM_TAXID: 102617;                                              
SOURCE   4 STRAIN: SS1;                                                         
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PBH4                                      
KEYWDS    HOMODIMER, FOUR-HELIX BUNDLE, PAS DOMAIN, MEMBRANE PROTEIN            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.N.HENDERSON,E.G.SWEENEY,J.GOERS,C.WREDEN,K.G.HICKS,R.PARTHASARATHY, 
AUTHOR   2 K.J.GUILLEMIN,S.J.REMINGTON                                          
REVDAT   3   08-NOV-17 3UB8    1       REMARK                                   
REVDAT   2   09-JAN-13 3UB8    1       JRNL                                     
REVDAT   1   27-JUN-12 3UB8    0                                                
JRNL        AUTH   E.GOERS SWEENEY,J.N.HENDERSON,J.GOERS,C.WREDEN,K.G.HICKS,    
JRNL        AUTH 2 J.K.FOSTER,R.PARTHASARATHY,S.J.REMINGTON,K.GUILLEMIN         
JRNL        TITL   STRUCTURE AND PROPOSED MECHANISM FOR THE PH-SENSING          
JRNL        TITL 2 HELICOBACTER PYLORI CHEMORECEPTOR TLPB.                      
JRNL        REF    STRUCTURE                     V.  20  1177 2012              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   22705207                                                     
JRNL        DOI    10.1016/J.STR.2012.04.021                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.42 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
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) : 1.42                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.83                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 79.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 92865                          
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) : 0.140                           
REMARK   3   R VALUE            (WORKING SET) : 0.139                           
REMARK   3   FREE R VALUE                     : 0.165                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4683                            
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) : 1.42                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6702                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 83.06                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1910                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 353                          
REMARK   3   BIN FREE R VALUE                    : 0.2480                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2482                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 46                                      
REMARK   3   SOLVENT ATOMS            : 428                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.69                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.11000                                             
REMARK   3    B22 (A**2) : -0.16000                                             
REMARK   3    B33 (A**2) : 0.27000                                              
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): 0.048         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.019         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.044         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.962                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2631 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1755 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3549 ; 1.492 ; 1.969       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4293 ; 0.921 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   333 ; 5.603 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   122 ;36.329 ;24.918       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   454 ;10.684 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ; 6.132 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   372 ; 0.099 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2940 ; 0.014 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   532 ; 0.001 ; 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):  1601 ; 2.772 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   667 ; 1.463 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2560 ; 3.662 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1030 ; 5.678 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   980 ; 7.629 ; 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):  4386 ; 2.904 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   428 ;17.359 ; 3.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  4336 ; 8.026 ; 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   : 1.40                                          
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 U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 3UB8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-NOV-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000068536.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-NOV-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97                               
REMARK 200  MONOCHROMATOR                  : DOUBLE-CRYSTAL, SI(111)            
REMARK 200  OPTICS                         : RH/PT COATED SI                    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 92912                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.420                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 79.6                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.05200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.42                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.45                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: EPMR                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.72                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 6.5, 2.1 M AMMONIUM    
REMARK 280  SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       39.80500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       47.26900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.85650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       47.26900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.80500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.85650            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.                         
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: 5240 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13940 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    31                                                      
REMARK 465     SER A    32                                                      
REMARK 465     LYS A    33                                                      
REMARK 465     VAL A    34                                                      
REMARK 465     MET A    35                                                      
REMARK 465     GLN A    36                                                      
REMARK 465     LYS A    37                                                      
REMARK 465     ASP A    38                                                      
REMARK 465     VAL A    39                                                      
REMARK 465     LEU A    40                                                      
REMARK 465     ALA A    41                                                      
REMARK 465     GLN A    42                                                      
REMARK 465     LEU A    43                                                      
REMARK 465     ASN A   201                                                      
REMARK 465     LYS A   202                                                      
REMARK 465     VAL A   203                                                      
REMARK 465     PHE A   204                                                      
REMARK 465     ASN A   205                                                      
REMARK 465     GLU A   206                                                      
REMARK 465     ASN A   207                                                      
REMARK 465     THR A   208                                                      
REMARK 465     THR A   209                                                      
REMARK 465     ARG A   210                                                      
REMARK 465     LEU A   211                                                      
REMARK 465     GLY B    31                                                      
REMARK 465     SER B    32                                                      
REMARK 465     LYS B    33                                                      
REMARK 465     VAL B    34                                                      
REMARK 465     MET B    35                                                      
REMARK 465     GLN B    36                                                      
REMARK 465     LYS B    37                                                      
REMARK 465     ASP B    38                                                      
REMARK 465     VAL B    39                                                      
REMARK 465     LEU B    40                                                      
REMARK 465     ALA B    41                                                      
REMARK 465     GLN B    42                                                      
REMARK 465     LEU B    43                                                      
REMARK 465     LYS B   202                                                      
REMARK 465     VAL B   203                                                      
REMARK 465     PHE B   204                                                      
REMARK 465     ASN B   205                                                      
REMARK 465     GLU B   206                                                      
REMARK 465     ASN B   207                                                      
REMARK 465     THR B   208                                                      
REMARK 465     THR B   209                                                      
REMARK 465     ARG B   210                                                      
REMARK 465     LEU B   211                                                      
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     MET A  44    CG   SD   CE                                        
REMARK 470     GLU A  45    CG   CD   OE1  OE2                                  
REMARK 470     HIS A  46    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A  84    NZ                                                  
REMARK 470     LYS A 107    CE   NZ                                             
REMARK 470     LYS A 119    CE   NZ                                             
REMARK 470     LYS A 145    CE   NZ                                             
REMARK 470     LYS A 194    CE   NZ                                             
REMARK 470     LYS A 197    CG   CD   CE   NZ                                   
REMARK 470     GLU A 198    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  45    CB   CG   CD   OE1  OE2                             
REMARK 470     HIS B  46    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS B  75    CD   CE   NZ                                        
REMARK 470     LYS B 119    NZ                                                  
REMARK 470     LYS B 145    CD   CE   NZ                                        
REMARK 470     LYS B 194    CE   NZ                                             
REMARK 470     LYS B 197    CE   NZ                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG A  83   CG    ARG A  83   CD     -0.161                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP B  78   CB  -  CG  -  OD2 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ARG B  92   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 114       89.29   -168.27                                   
REMARK 500    ASP B 114       87.95   -166.01                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ASP A  78         0.07    SIDE CHAIN                              
REMARK 500    ASP B  78         0.11    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ARF A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ARF A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ARF A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ARF A 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ARF A 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ARF B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ARF B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ARF B 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 305                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3UB6   RELATED DB: PDB                                   
REMARK 900 PERIPLASMIC PORTION OF THE HELICOBACTER PYLORI CHEMORECEPTOR TLPB    
REMARK 900 WITH UREA BOUND                                                      
REMARK 900 RELATED ID: 3UB7   RELATED DB: PDB                                   
REMARK 900 PERIPLASMIC PORTION OF THE HELICOBACTER PYLORI CHEMORECEPTOR TLPB    
REMARK 900 WITH ACETAMIDE BOUND                                                 
REMARK 900 RELATED ID: 3UB9   RELATED DB: PDB                                   
REMARK 900 PERIPLASMIC PORTION OF THE HELICOBACTER PYLORI CHEMORECEPTOR TLPB    
REMARK 900 WITH HYDROXYUREA BOUND                                               
DBREF  3UB8 A   31   211  PDB    3UB8     3UB8             1    181             
DBREF  3UB8 B   31   211  PDB    3UB8     3UB8             1    181             
SEQRES   1 A  181  GLY SER LYS VAL MET GLN LYS ASP VAL LEU ALA GLN LEU          
SEQRES   2 A  181  MET GLU HIS LEU GLU THR GLY GLN TYR LYS LYS ARG GLU          
SEQRES   3 A  181  LYS THR LEU ALA TYR MET THR LYS ILE LEU GLU GLN GLY          
SEQRES   4 A  181  ILE HIS GLU TYR TYR LYS SER PHE ASP ASN ASP THR ALA          
SEQRES   5 A  181  ARG LYS MET ALA LEU ASP TYR PHE LYS ARG ILE ASN ASP          
SEQRES   6 A  181  ASP LYS GLY MET ILE TYR MET VAL VAL VAL ASP LYS ASN          
SEQRES   7 A  181  GLY VAL VAL LEU PHE ASP PRO VAL ASN PRO LYS THR VAL          
SEQRES   8 A  181  GLY GLN SER GLY LEU ASP ALA GLN SER VAL ASP GLY VAL          
SEQRES   9 A  181  TYR TYR VAL ARG GLY TYR LEU GLU ALA ALA LYS LYS GLY          
SEQRES  10 A  181  GLY GLY TYR THR TYR TYR LYS MET PRO LYS TYR ASP GLY          
SEQRES  11 A  181  GLY VAL PRO GLU LYS LYS PHE ALA TYR SER HIS TYR ASP          
SEQRES  12 A  181  GLU VAL SER GLN MET VAL ILE ALA ALA THR SER TYR TYR          
SEQRES  13 A  181  THR ASP ILE ASN THR GLU ASN LYS ALA ILE LYS GLU GLY          
SEQRES  14 A  181  VAL ASN LYS VAL PHE ASN GLU ASN THR THR ARG LEU              
SEQRES   1 B  181  GLY SER LYS VAL MET GLN LYS ASP VAL LEU ALA GLN LEU          
SEQRES   2 B  181  MET GLU HIS LEU GLU THR GLY GLN TYR LYS LYS ARG GLU          
SEQRES   3 B  181  LYS THR LEU ALA TYR MET THR LYS ILE LEU GLU GLN GLY          
SEQRES   4 B  181  ILE HIS GLU TYR TYR LYS SER PHE ASP ASN ASP THR ALA          
SEQRES   5 B  181  ARG LYS MET ALA LEU ASP TYR PHE LYS ARG ILE ASN ASP          
SEQRES   6 B  181  ASP LYS GLY MET ILE TYR MET VAL VAL VAL ASP LYS ASN          
SEQRES   7 B  181  GLY VAL VAL LEU PHE ASP PRO VAL ASN PRO LYS THR VAL          
SEQRES   8 B  181  GLY GLN SER GLY LEU ASP ALA GLN SER VAL ASP GLY VAL          
SEQRES   9 B  181  TYR TYR VAL ARG GLY TYR LEU GLU ALA ALA LYS LYS GLY          
SEQRES  10 B  181  GLY GLY TYR THR TYR TYR LYS MET PRO LYS TYR ASP GLY          
SEQRES  11 B  181  GLY VAL PRO GLU LYS LYS PHE ALA TYR SER HIS TYR ASP          
SEQRES  12 B  181  GLU VAL SER GLN MET VAL ILE ALA ALA THR SER TYR TYR          
SEQRES  13 B  181  THR ASP ILE ASN THR GLU ASN LYS ALA ILE LYS GLU GLY          
SEQRES  14 B  181  VAL ASN LYS VAL PHE ASN GLU ASN THR THR ARG LEU              
HET    ARF  A 301       3                                                       
HET    SO4  A 302       5                                                       
HET    ARF  A 303       3                                                       
HET    ARF  A 304       3                                                       
HET    ARF  A 305       3                                                       
HET    ARF  A 306       3                                                       
HET    GOL  A 307       6                                                       
HET    ARF  B 302       3                                                       
HET    SO4  B 301       5                                                       
HET    ARF  B 303       3                                                       
HET    ARF  B 304       3                                                       
HET    GOL  B 305       6                                                       
HETNAM     ARF FORMAMIDE                                                        
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  ARF    8(C H3 N O)                                                  
FORMUL   4  SO4    2(O4 S 2-)                                                   
FORMUL   9  GOL    2(C3 H8 O3)                                                  
FORMUL  15  HOH   *428(H2 O)                                                    
HELIX    1   1 MET A   44  PHE A   77  1                                  34    
HELIX    2   2 ASP A   78  ASP A   96  1                                  19    
HELIX    3   3 ASN A  117  VAL A  121  5                                   5    
HELIX    4   4 TYR A  135  LYS A  146  1                                  12    
HELIX    5   5 TYR A  186  ASN A  193  1                                   8    
HELIX    6   6 ASN A  193  VAL A  200  1                                   8    
HELIX    7   7 GLU B   45  LYS B   75  1                                  31    
HELIX    8   8 ASP B   78  LYS B   97  1                                  20    
HELIX    9   9 ASN B  117  VAL B  121  5                                   5    
HELIX   10  10 TYR B  135  LYS B  146  1                                  12    
HELIX   11  11 TYR B  186  ASN B  193  1                                   8    
HELIX   12  12 ASN B  193  ASN B  201  1                                   9    
SHEET    1   A 5 VAL A 111  PHE A 113  0                                        
SHEET    2   A 5 TYR A 101  VAL A 105 -1  N  VAL A 104   O  LEU A 112           
SHEET    3   A 5 MET A 178  TYR A 185 -1  O  VAL A 179   N  VAL A 105           
SHEET    4   A 5 GLU A 164  ASP A 173 -1  N  TYR A 169   O  ALA A 182           
SHEET    5   A 5 GLY A 149  MET A 155 -1  N  GLY A 149   O  SER A 170           
SHEET    1   B 5 VAL B 111  PHE B 113  0                                        
SHEET    2   B 5 TYR B 101  ASP B 106 -1  N  VAL B 104   O  LEU B 112           
SHEET    3   B 5 MET B 178  TYR B 185 -1  O  VAL B 179   N  VAL B 105           
SHEET    4   B 5 GLU B 164  ASP B 173 -1  N  TYR B 169   O  ALA B 182           
SHEET    5   B 5 GLY B 149  MET B 155 -1  N  MET B 155   O  GLU B 164           
SITE     1 AC1  5 LYS A  54  SO4 A 302  HOH A 535  ARG B  55                    
SITE     2 AC1  5 THR B  58                                                     
SITE     1 AC2  8 LYS A  54  ARG A  55  THR A  58  MET A  99                    
SITE     2 AC2  8 ARF A 301  HOH A 463  LYS B  54  SO4 B 301                    
SITE     1 AC3  7 VAL A 103  ASP A 114  VAL A 116  TYR A 153                    
SITE     2 AC3  7 MET A 155  LYS A 166  HOH A 406                               
SITE     1 AC4  6 VAL A 103  ASP A 114  TYR A 136  TYR A 140                    
SITE     2 AC4  6 TYR A 153  LYS A 166                                          
SITE     1 AC5  5 VAL A 103  ASP A 114  TYR A 136  TYR A 140                    
SITE     2 AC5  5 HOH A 406                                                     
SITE     1 AC6  5 ARG A  55  THR A  58  HOH A 463  LYS B  54                    
SITE     2 AC6  5 SO4 B 301                                                     
SITE     1 AC7  6 LYS A  97  GLY A  98  MET A  99  ASP A 188                    
SITE     2 AC7  6 GLU A 192  HOH A 448                                          
SITE     1 AC8  8 LYS A  54  SO4 A 302  ARF A 306  HOH A 535                    
SITE     2 AC8  8 LYS B  54  ARG B  55  THR B  58  MET B  99                    
SITE     1 AC9  7 VAL B 103  ASP B 114  TYR B 136  TYR B 140                    
SITE     2 AC9  7 TYR B 153  MET B 155  LYS B 166                               
SITE     1 BC1  7 VAL B 103  ASP B 114  VAL B 116  TYR B 153                    
SITE     2 BC1  7 MET B 155  LYS B 166  HOH B 407                               
SITE     1 BC2  6 VAL B 103  ASP B 114  VAL B 116  ASN B 117                    
SITE     2 BC2  6 TYR B 136  TYR B 140                                          
SITE     1 BC3 12 ASN B  94  ASP B  95  LYS B 157  TYR B 158                    
SITE     2 BC3 12 HOH B 408  HOH B 411  HOH B 415  HOH B 455                    
SITE     3 BC3 12 HOH B 468  HOH B 469  HOH B 619  HOH B 621                    
CRYST1   79.610   81.713   94.538  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012561  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012238  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010578        0.00000                         
ATOM      1  N   MET A  44      25.401  52.319  14.530  1.00 31.79           N  
ANISOU    1  N   MET A  44     3548   3610   4921  -1322    -93   -876       N  
ATOM      2  CA  MET A  44      24.546  51.579  15.488  1.00 33.01           C  
ANISOU    2  CA  MET A  44     4145   3754   4642   -741   -156   -889       C  
ATOM      3  C   MET A  44      23.053  51.834  15.223  1.00 31.66           C  
ANISOU    3  C   MET A  44     3745   3763   4519   -811    -50   -668       C  
ATOM      4  O   MET A  44      22.245  50.893  15.239  1.00 30.19           O  
ANISOU    4  O   MET A  44     3930   3363   4177  -1112    -43  -1266       O  
ATOM      5  CB  MET A  44      24.917  51.925  16.933  1.00 35.47           C  
ANISOU    5  CB  MET A  44     4367   4390   4718   -738   -234   -769       C  
ATOM      6  N   GLU A  45      22.683  53.088  14.968  1.00 33.03           N  
ANISOU    6  N   GLU A  45     4095   3893   4560   -806    -25   -593       N  
ATOM      7  CA  GLU A  45      21.286  53.429  14.648  1.00 32.41           C  
ANISOU    7  CA  GLU A  45     4123   3715   4477   -690      9   -312       C  
ATOM      8  C   GLU A  45      20.795  52.747  13.358  1.00 31.30           C  
ANISOU    8  C   GLU A  45     3939   3503   4449   -959     -7   -451       C  
ATOM      9  O   GLU A  45      19.741  52.111  13.353  1.00 29.12           O  
ANISOU    9  O   GLU A  45     3536   3357   4169  -1242    271   -461       O  
ATOM     10  CB  GLU A  45      21.070  54.952  14.552  1.00 35.75           C  
ANISOU   10  CB  GLU A  45     4728   4012   4843   -650    -30   -458       C  
ATOM     11  N   HIS A  46      21.586  52.827  12.295  1.00 31.53           N  
ANISOU   11  N   HIS A  46     4205   3602   4171  -1116    -36   -428       N  
ATOM     12  CA  HIS A  46      21.216  52.287  10.989  1.00 30.83           C  
ANISOU   12  CA  HIS A  46     4027   3767   3918   -989    236   -261       C  
ATOM     13  C   HIS A  46      21.236  50.760  11.066  1.00 29.09           C  
ANISOU   13  C   HIS A  46     3688   3554   3809  -1061    158   -339       C  
ATOM     14  O   HIS A  46      20.389  50.073  10.465  1.00 29.51           O  
ANISOU   14  O   HIS A  46     3599   4018   3593  -1615    401   -418       O  
ATOM     15  CB  HIS A  46      22.161  52.818   9.898  1.00 32.14           C  
ANISOU   15  CB  HIS A  46     4187   3862   4160  -1160    226   -127       C  
ATOM     16  N   LEU A  47      22.133  50.225  11.893  1.00 27.51           N  
ANISOU   16  N   LEU A  47     3388   3389   3673   -860    286   -496       N  
ATOM     17  CA  LEU A  47      22.170  48.793  12.138  1.00 25.33           C  
ANISOU   17  CA  LEU A  47     2970   3099   3554   -671    473   -669       C  
ATOM     18  C   LEU A  47      20.885  48.299  12.830  1.00 23.92           C  
ANISOU   18  C   LEU A  47     2836   2829   3422   -886    636   -812       C  
ATOM     19  O   LEU A  47      20.254  47.324  12.418  1.00 23.06           O  
ANISOU   19  O   LEU A  47     2747   2797   3218   -705    478   -999       O  
ATOM     20  CB  LEU A  47      23.355  48.477  13.022  1.00 28.68           C  
ANISOU   20  CB  LEU A  47     3387   3746   3764   -560    294   -669       C  
ATOM     21  CG  LEU A  47      23.617  47.032  13.386  1.00 26.30           C  
ANISOU   21  CG  LEU A  47     3245   2994   3753   -832     94   -738       C  
ATOM     22  CD1 LEU A  47      23.524  46.118  12.129  1.00 30.33           C  
ANISOU   22  CD1 LEU A  47     3876   3419   4229   -563    596  -1186       C  
ATOM     23  CD2 LEU A  47      24.990  46.947  14.034  1.00 32.82           C  
ANISOU   23  CD2 LEU A  47     4079   3939   4453   -158     81  -1108       C  
ATOM     24  N   GLU A  48      20.484  49.008  13.874  1.00 22.84           N  
ANISOU   24  N   GLU A  48     2687   2804   3187   -864    565  -1008       N  
ATOM     25  CA  GLU A  48      19.271  48.691  14.610  1.00 23.55           C  
ANISOU   25  CA  GLU A  48     3031   2729   3187   -636    536   -875       C  
ATOM     26  C   GLU A  48      18.028  48.769  13.720  1.00 20.72           C  
ANISOU   26  C   GLU A  48     2665   2246   2959   -308    610   -946       C  
ATOM     27  O   GLU A  48      17.230  47.824  13.664  1.00 21.09           O  
ANISOU   27  O   GLU A  48     2812   2338   2862   -835    612   -901       O  
ATOM     28  CB  GLU A  48      19.152  49.659  15.792  1.00 25.11           C  
ANISOU   28  CB  GLU A  48     3277   3037   3225   -651    309  -1058       C  
ATOM     29  CG  GLU A  48      17.975  49.433  16.673  1.00 29.73           C  
ANISOU   29  CG  GLU A  48     3925   3642   3729   -397    321   -767       C  
ATOM     30  CD  GLU A  48      17.914  50.450  17.804  1.00 33.38           C  
ANISOU   30  CD  GLU A  48     4383   4359   3942   -429     97   -901       C  
ATOM     31  OE1 GLU A  48      18.788  50.379  18.695  1.00 42.84           O  
ANISOU   31  OE1 GLU A  48     5954   6358   3965   -127   -527  -1375       O  
ATOM     32  OE2 GLU A  48      17.056  51.356  17.746  1.00 39.20           O  
ANISOU   32  OE2 GLU A  48     5404   4443   5045   -405    -50  -1624       O  
ATOM     33  N   THR A  49      17.893  49.851  12.971  1.00 21.95           N  
ANISOU   33  N   THR A  49     2827   2431   3080   -649    501   -851       N  
ATOM     34  CA  THR A  49      16.807  50.015  12.013  1.00 21.56           C  
ANISOU   34  CA  THR A  49     2928   2226   3036   -389    507   -510       C  
ATOM     35  C   THR A  49      16.782  48.874  10.975  1.00 19.22           C  
ANISOU   35  C   THR A  49     2561   1958   2784   -463    577   -549       C  
ATOM     36  O   THR A  49      15.728  48.300  10.706  1.00 19.61           O  
ANISOU   36  O   THR A  49     2365   2008   3077   -677    831   -505       O  
ATOM     37  CB  THR A  49      16.880  51.379  11.334  1.00 24.79           C  
ANISOU   37  CB  THR A  49     3505   2530   3385   -208    315   -591       C  
ATOM     38  OG1 THR A  49      16.732  52.386  12.337  1.00 28.60           O  
ANISOU   38  OG1 THR A  49     4603   2406   3856   -259    112   -940       O  
ATOM     39  CG2 THR A  49      15.778  51.536  10.276  1.00 29.04           C  
ANISOU   39  CG2 THR A  49     3727   3003   4303   -221    300   -323       C  
ATOM     40  N   GLY A  50      17.951  48.475  10.486  1.00 19.47           N  
ANISOU   40  N   GLY A  50     2558   2123   2715   -561    680   -620       N  
ATOM     41  CA  GLY A  50      18.012  47.404   9.514  1.00 18.43           C  
ANISOU   41  CA  GLY A  50     2357   2207   2438   -533    697   -483       C  
ATOM     42  C   GLY A  50      17.614  46.067  10.098  1.00 17.00           C  
ANISOU   42  C   GLY A  50     2120   2148   2187   -549    474   -227       C  
ATOM     43  O   GLY A  50      16.939  45.269   9.436  1.00 16.65           O  
ANISOU   43  O   GLY A  50     2160   1974   2192   -600    629   -503       O  
ATOM     44  N   GLN A  51      17.972  45.844  11.360  1.00 17.05           N  
ANISOU   44  N   GLN A  51     2227   2154   2095   -473    464   -576       N  
ATOM     45  CA  GLN A  51      17.581  44.614  12.063  1.00 15.86           C  
ANISOU   45  CA  GLN A  51     2034   2052   1936   -279    263   -498       C  
ATOM     46  C   GLN A  51      16.074  44.533  12.306  1.00 14.52           C  
ANISOU   46  C   GLN A  51     2151   1678   1687     44    202   -616       C  
ATOM     47  O   GLN A  51      15.477  43.463  12.139  1.00 15.03           O  
ANISOU   47  O   GLN A  51     2246   1728   1736   -200    297   -653       O  
ATOM     48  CB  GLN A  51      18.347  44.503  13.395  1.00 18.68           C  
ANISOU   48  CB  GLN A  51     2256   2554   2287   -198    101   -451       C  
ATOM     49  CG  GLN A  51      19.830  44.301  13.178  1.00 21.21           C  
ANISOU   49  CG  GLN A  51     2325   2664   3070   -375    -80   -579       C  
ATOM     50  CD  GLN A  51      20.718  44.458  14.401  1.00 23.41           C  
ANISOU   50  CD  GLN A  51     2647   3065   3183   -660    351   -595       C  
ATOM     51  OE1 GLN A  51      20.345  45.128  15.389  1.00 26.44           O  
ANISOU   51  OE1 GLN A  51     3284   3709   3052   -855    406  -1109       O  
ATOM     52  NE2 GLN A  51      21.953  43.887  14.310  1.00 26.76           N  
ANISOU   52  NE2 GLN A  51     2563   3739   3863   -712    642     84       N  
ATOM     53  N   TYR A  52      15.451  45.681  12.556  1.00 15.11           N  
ANISOU   53  N   TYR A  52     2108   1608   2025   -325    331   -491       N  
ATOM     54  CA  TYR A  52      14.006  45.707  12.745  1.00 13.96           C  
ANISOU   54  CA  TYR A  52     2014   1516   1775   -269    187   -170       C  
ATOM     55  C   TYR A  52      13.299  45.445  11.409  1.00 14.35           C  
ANISOU   55  C   TYR A  52     1974   1650   1827   -126    271   -331       C  
ATOM     56  O   TYR A  52      12.322  44.714  11.357  1.00 14.74           O  
ANISOU   56  O   TYR A  52     2123   1645   1831   -257    564   -433       O  
ATOM     57  CB  TYR A  52      13.542  47.032  13.356  1.00 13.71           C  
ANISOU   57  CB  TYR A  52     1895   1801   1511   -183    139   -245       C  
ATOM     58  CG  TYR A  52      14.112  47.348  14.732  1.00 14.20           C  
ANISOU   58  CG  TYR A  52     1816   1748   1831   -336    129   -419       C  
ATOM     59  CD1 TYR A  52      14.589  46.361  15.567  1.00 16.23           C  
ANISOU   59  CD1 TYR A  52     2351   1841   1973   -208    854   -620       C  
ATOM     60  CD2 TYR A  52      14.158  48.654  15.183  1.00 17.03           C  
ANISOU   60  CD2 TYR A  52     2751   1838   1882   -104     75   -308       C  
ATOM     61  CE1 TYR A  52      15.102  46.653  16.813  1.00 17.72           C  
ANISOU   61  CE1 TYR A  52     2468   2212   2051   -418    401   -312       C  
ATOM     62  CE2 TYR A  52      14.675  48.966  16.434  1.00 20.65           C  
ANISOU   62  CE2 TYR A  52     3671   1863   2309   -424     61   -796       C  
ATOM     63  CZ  TYR A  52      15.145  47.966  17.257  1.00 19.53           C  
ANISOU   63  CZ  TYR A  52     3270   2030   2119   -463     54   -527       C  
ATOM     64  OH  TYR A  52      15.693  48.324  18.486  1.00 24.25           O  
ANISOU   64  OH  TYR A  52     4066   3100   2048   -344   -323  -1035       O  
ATOM     65  N   LYS A  53      13.792  46.060  10.339  1.00 16.04           N  
ANISOU   65  N   LYS A  53     1997   1801   2297   -520    321   -205       N  
ATOM     66  CA  LYS A  53      13.237  45.838   9.007  1.00 14.86           C  
ANISOU   66  CA  LYS A  53     2012   1817   1814   -167    405   -160       C  
ATOM     67  C   LYS A  53      13.383  44.367   8.567  1.00 14.97           C  
ANISOU   67  C   LYS A  53     1984   1687   2015   -245    502    -86       C  
ATOM     68  O   LYS A  53      12.458  43.771   7.994  1.00 14.38           O  
ANISOU   68  O   LYS A  53     2087   1833   1541   -260    431    -66       O  
ATOM     69  CB  LYS A  53      13.903  46.765   7.988  1.00 17.45           C  
ANISOU   69  CB  LYS A  53     2421   1954   2255   -288    440     26       C  
ATOM     70  CG  LYS A  53      13.629  48.229   8.270  1.00 23.89           C  
ANISOU   70  CG  LYS A  53     3893   2816   2368    138    492   -514       C  
ATOM     71  CD  LYS A  53      12.273  48.713   7.883  1.00 30.91           C  
ANISOU   71  CD  LYS A  53     4566   3278   3898   -331    352    154       C  
ATOM     72  CE  LYS A  53      12.333  50.276   7.794  1.00 32.88           C  
ANISOU   72  CE  LYS A  53     5262   3368   3860    226   -229   -303       C  
ATOM     73  NZ  LYS A  53      10.993  50.902   7.868  1.00 36.05           N  
ANISOU   73  NZ  LYS A  53     5127   4149   4418    234    -55    509       N  
ATOM     74  N   LYS A  54      14.504  43.754   8.919  1.00 13.34           N  
ANISOU   74  N   LYS A  54     1873   1615   1578   -162    395   -251       N  
ATOM     75  CA  LYS A  54      14.696  42.329   8.615  1.00 13.04           C  
ANISOU   75  CA  LYS A  54     1862   1596   1494   -138    588   -417       C  
ATOM     76  C   LYS A  54      13.678  41.468   9.361  1.00 12.04           C  
ANISOU   76  C   LYS A  54     1886   1429   1258   -397    425   -451       C  
ATOM     77  O   LYS A  54      13.062  40.568   8.815  1.00 12.75           O  
ANISOU   77  O   LYS A  54     1904   1714   1226   -363    394   -393       O  
ATOM     78  CB  LYS A  54      16.121  41.876   8.940  1.00 14.94           C  
ANISOU   78  CB  LYS A  54     2167   1848   1662   -268    520   -136       C  
ATOM     79  CG  LYS A  54      16.400  40.426   8.590  1.00 16.83           C  
ANISOU   79  CG  LYS A  54     2188   2152   2054   -183    580   -348       C  
ATOM     80  CD  LYS A  54      17.788  39.996   9.075  1.00 20.20           C  
ANISOU   80  CD  LYS A  54     2911   2850   1912    169    791   -392       C  
ATOM     81  CE  LYS A  54      18.166  38.613   8.597  1.00 20.52           C  
ANISOU   81  CE  LYS A  54     2540   2674   2581   -196    109   -175       C  
ATOM     82  NZ  LYS A  54      17.073  37.605   8.657  1.00 24.51           N  
ANISOU   82  NZ  LYS A  54     2881   2772   3659   -365    699     65       N  
ATOM     83  N   ARG A  55      13.475  41.790  10.627  1.00 11.92           N  
ANISOU   83  N   ARG A  55     1725   1497   1305   -321    242   -542       N  
ATOM     84  CA  ARG A  55      12.511  41.032  11.425  1.00 11.80           C  
ANISOU   84  CA  ARG A  55     1781   1372   1329   -353    330   -259       C  
ATOM     85  C   ARG A  55      11.083  41.208  10.892  1.00 11.13           C  
ANISOU   85  C   ARG A  55     1805   1375   1048   -187    283   -216       C  
ATOM     86  O   ARG A  55      10.280  40.276  10.934  1.00 11.60           O  
ANISOU   86  O   ARG A  55     1788   1554   1066   -413    495   -296       O  
ATOM     87  CB  ARG A  55      12.591  41.461  12.887  1.00 13.14           C  
ANISOU   87  CB  ARG A  55     2043   1624   1325   -147    404   -175       C  
ATOM     88  CG  ARG A  55      11.576  40.768  13.857  1.00 13.53           C  
ANISOU   88  CG  ARG A  55     2162   1569   1407   -245    461   -440       C  
ATOM     89  CD  ARG A  55      11.677  39.246  13.818  1.00 15.14           C  
ANISOU   89  CD  ARG A  55     2461   1791   1500   -353    464    -67       C  
ATOM     90  NE  ARG A  55      11.466  38.663  15.145  1.00 12.99           N  
ANISOU   90  NE  ARG A  55     1862   1670   1404    -26    475    -95       N  
ATOM     91  CZ  ARG A  55      12.444  38.460  16.044  1.00 12.76           C  
ANISOU   91  CZ  ARG A  55     1504   1793   1549     -5    201   -350       C  
ATOM     92  NH1 ARG A  55      13.713  38.619  15.709  1.00 15.29           N  
ANISOU   92  NH1 ARG A  55     2102   2145   1562   -485    504   -237       N  
ATOM     93  NH2 ARG A  55      12.109  38.092  17.276  1.00 13.67           N  
ANISOU   93  NH2 ARG A  55     1845   2067   1281   -354    340   -331       N  
ATOM     94  N   GLU A  56      10.747  42.398  10.392  1.00 11.38           N  
ANISOU   94  N   GLU A  56     1752   1375   1194   -173    273   -159       N  
ATOM     95  CA  GLU A  56       9.466  42.580   9.715  1.00 12.34           C  
ANISOU   95  CA  GLU A  56     1751   1449   1486   -231    365   -231       C  
ATOM     96  C   GLU A  56       9.275  41.536   8.601  1.00 11.03           C  
ANISOU   96  C   GLU A  56     1697   1351   1141   -160    386    -15       C  
ATOM     97  O   GLU A  56       8.213  40.932   8.490  1.00 11.59           O  
ANISOU   97  O   GLU A  56     1807   1634    960   -250    369   -239       O  
ATOM     98  CB  GLU A  56       9.345  44.002   9.163  1.00 12.14           C  
ANISOU   98  CB  GLU A  56     2023   1234   1355   -120    341   -231       C  
ATOM     99  CG  GLU A  56       9.150  45.043  10.274  1.00 12.58           C  
ANISOU   99  CG  GLU A  56     2019   1270   1490    -98    339    -86       C  
ATOM    100  CD  GLU A  56       9.076  46.474   9.797  1.00 16.29           C  
ANISOU  100  CD  GLU A  56     2654   1448   2085     61    454   -352       C  
ATOM    101  OE1 GLU A  56       9.264  46.726   8.579  1.00 22.12           O  
ANISOU  101  OE1 GLU A  56     4201   2048   2155     79    601    -76       O  
ATOM    102  OE2 GLU A  56       8.768  47.359  10.643  1.00 16.65           O  
ANISOU  102  OE2 GLU A  56     3018   1748   1557     21    447   -177       O  
ATOM    103  N   LYS A  57      10.282  41.397   7.732  1.00 11.89           N  
ANISOU  103  N   LYS A  57     1814   1452   1250   -442    395   -117       N  
ATOM    104  CA  LYS A  57      10.171  40.433   6.654  1.00 12.64           C  
ANISOU  104  CA  LYS A  57     2066   1616   1121   -232    274   -206       C  
ATOM    105  C   LYS A  57      10.083  39.000   7.201  1.00 13.62           C  
ANISOU  105  C   LYS A  57     2007   1684   1483    -62    324   -284       C  
ATOM    106  O   LYS A  57       9.361  38.171   6.640  1.00 13.55           O  
ANISOU  106  O   LYS A  57     1916   1679   1553   -315    357   -288       O  
ATOM    107  CB  LYS A  57      11.324  40.603   5.646  1.00 14.86           C  
ANISOU  107  CB  LYS A  57     2328   1904   1412   -252    179   -264       C  
ATOM    108  CG  LYS A  57      11.245  41.985   4.935  1.00 18.59           C  
ANISOU  108  CG  LYS A  57     3009   2076   1976   -553    532   -375       C  
ATOM    109  CD  LYS A  57      12.413  42.308   4.073  1.00 25.04           C  
ANISOU  109  CD  LYS A  57     3594   3553   2365   -577    271    -78       C  
ATOM    110  CE  LYS A  57      12.392  43.821   3.698  1.00 30.16           C  
ANISOU  110  CE  LYS A  57     4631   3874   2955   -251    180     91       C  
ATOM    111  NZ  LYS A  57      12.524  44.849   4.849  1.00 29.68           N  
ANISOU  111  NZ  LYS A  57     4094   3572   3608   -305    463   -133       N  
ATOM    112  N   THR A  58      10.879  38.695   8.230  1.00 11.29           N  
ANISOU  112  N   THR A  58     1609   1482   1199   -277    427   -486       N  
ATOM    113  CA  THR A  58      10.819  37.388   8.866  1.00 11.17           C  
ANISOU  113  CA  THR A  58     1527   1496   1219   -239    187   -467       C  
ATOM    114  C   THR A  58       9.422  37.053   9.343  1.00 10.81           C  
ANISOU  114  C   THR A  58     1547   1397   1164   -230    140   -442       C  
ATOM    115  O   THR A  58       8.951  35.927   9.128  1.00 11.07           O  
ANISOU  115  O   THR A  58     1669   1407   1127   -240     86   -236       O  
ATOM    116  CB  THR A  58      11.834  37.285   9.983  1.00 10.58           C  
ANISOU  116  CB  THR A  58     1416   1879    725   -209    223   -509       C  
ATOM    117  OG1 THR A  58      13.154  37.475   9.437  1.00 13.59           O  
ANISOU  117  OG1 THR A  58     1540   2041   1583   -240     81   -111       O  
ATOM    118  CG2 THR A  58      11.737  35.957  10.744  1.00 12.73           C  
ANISOU  118  CG2 THR A  58     1822   1366   1647   -279      8     39       C  
ATOM    119  N   LEU A  59       8.736  38.026   9.948  1.00 10.72           N  
ANISOU  119  N   LEU A  59     1543   1378   1152   -216    165   -322       N  
ATOM    120  CA  LEU A  59       7.381  37.764  10.402  1.00 11.04           C  
ANISOU  120  CA  LEU A  59     1632   1430   1129   -247    194   -358       C  
ATOM    121  C   LEU A  59       6.402  37.471   9.279  1.00  9.64           C  
ANISOU  121  C   LEU A  59     1449   1108   1104   -150    366   -169       C  
ATOM    122  O   LEU A  59       5.509  36.646   9.470  1.00  9.45           O  
ANISOU  122  O   LEU A  59     1531   1325    733   -174     85   -100       O  
ATOM    123  CB  LEU A  59       6.815  38.886  11.279  1.00 11.50           C  
ANISOU  123  CB  LEU A  59     1660   1732    974   -403    488   -270       C  
ATOM    124  CG  LEU A  59       7.472  39.234  12.588  1.00 17.27           C  
ANISOU  124  CG  LEU A  59     1734   2507   2318    -19   -410   -677       C  
ATOM    125  CD1 LEU A  59       6.627  40.304  13.283  1.00 21.25           C  
ANISOU  125  CD1 LEU A  59     2214   4207   1653    -63    468  -1928       C  
ATOM    126  CD2 LEU A  59       7.622  37.988  13.391  1.00 19.87           C  
ANISOU  126  CD2 LEU A  59     4035   2518    996   -817    479   -184       C  
ATOM    127  N   ALA A  60       6.556  38.140   8.133  1.00 10.04           N  
ANISOU  127  N   ALA A  60     1535   1421    858   -227    181    -97       N  
ATOM    128  CA  ALA A  60       5.689  37.837   7.003  1.00  8.47           C  
ANISOU  128  CA  ALA A  60     1338   1401    478    -78    163   -226       C  
ATOM    129  C   ALA A  60       5.901  36.371   6.551  1.00  8.40           C  
ANISOU  129  C   ALA A  60     1130   1239    820     60    228     47       C  
ATOM    130  O   ALA A  60       4.938  35.645   6.258  1.00 10.30           O  
ANISOU  130  O   ALA A  60     1467   1429   1016   -137    369   -145       O  
ATOM    131  CB  ALA A  60       5.926  38.830   5.857  1.00 11.79           C  
ANISOU  131  CB  ALA A  60     1981   1397   1102     -9    500    416       C  
ATOM    132  N   TYR A  61       7.160  35.943   6.493  1.00  9.13           N  
ANISOU  132  N   TYR A  61     1242   1403    820    -97    313    -19       N  
ATOM    133  CA  TYR A  61       7.481  34.562   6.138  1.00  8.69           C  
ANISOU  133  CA  TYR A  61     1361   1247    690      0    303   -250       C  
ATOM    134  C   TYR A  61       6.999  33.524   7.140  1.00  9.20           C  
ANISOU  134  C   TYR A  61     1666   1030    799    -83    192   -358       C  
ATOM    135  O   TYR A  61       6.374  32.537   6.790  1.00  9.24           O  
ANISOU  135  O   TYR A  61     1422   1305    783   -165    113   -214       O  
ATOM    136  CB  TYR A  61       8.978  34.406   5.904  1.00  9.49           C  
ANISOU  136  CB  TYR A  61     1507   1589    509    -83    118   -148       C  
ATOM    137  CG  TYR A  61       9.444  32.986   5.630  1.00  8.80           C  
ANISOU  137  CG  TYR A  61     1330   1153    860    -46    186    -72       C  
ATOM    138  CD1 TYR A  61       9.228  32.372   4.408  1.00  9.40           C  
ANISOU  138  CD1 TYR A  61     1629   1433    511      9   -172    230       C  
ATOM    139  CD2 TYR A  61      10.001  32.217   6.635  1.00  9.25           C  
ANISOU  139  CD2 TYR A  61     1409   1435    668     75     22    111       C  
ATOM    140  CE1 TYR A  61       9.660  31.109   4.143  1.00 10.57           C  
ANISOU  140  CE1 TYR A  61     1739   1323    951    227    280    132       C  
ATOM    141  CE2 TYR A  61      10.409  30.942   6.405  1.00  9.11           C  
ANISOU  141  CE2 TYR A  61     1434   1671    353    141   -249    117       C  
ATOM    142  CZ  TYR A  61      10.213  30.357   5.157  1.00 10.18           C  
ANISOU  142  CZ  TYR A  61     1334   1332   1200     66    196    -60       C  
ATOM    143  OH  TYR A  61      10.702  29.099   4.962  1.00 10.91           O  
ANISOU  143  OH  TYR A  61     1520   1455   1168    148    116    -53       O  
ATOM    144  N   MET A  62       7.206  33.828   8.409  1.00  8.96           N  
ANISOU  144  N   MET A  62     1382   1112    911   -346    158   -245       N  
ATOM    145  CA AMET A  62       6.757  32.929   9.440  0.65  8.11           C  
ANISOU  145  CA AMET A  62     1384   1133    565   -216     79   -160       C  
ATOM    146  CA BMET A  62       6.761  32.924   9.440  0.35  8.74           C  
ANISOU  146  CA BMET A  62     1435   1205    678   -190     61   -167       C  
ATOM    147  C   MET A  62       5.237  32.796   9.427  1.00  8.54           C  
ANISOU  147  C   MET A  62     1432   1017    794   -123    -32   -200       C  
ATOM    148  O   MET A  62       4.716  31.708   9.642  1.00  8.84           O  
ANISOU  148  O   MET A  62     1502   1148    707   -126     87    -91       O  
ATOM    149  CB AMET A  62       7.276  33.391  10.793  0.65 10.79           C  
ANISOU  149  CB AMET A  62     1710   1432    956   -381    -19   -118       C  
ATOM    150  CB BMET A  62       7.278  33.375  10.800  0.35 10.44           C  
ANISOU  150  CB BMET A  62     1621   1450    894   -289     -2   -135       C  
ATOM    151  CG AMET A  62       8.789  33.253  10.929  0.65 12.68           C  
ANISOU  151  CG AMET A  62     1793   2061    962   -276   -176   -159       C  
ATOM    152  CG BMET A  62       8.759  33.076  11.031  0.35 11.53           C  
ANISOU  152  CG BMET A  62     1630   1816    932   -233    -72   -249       C  
ATOM    153  SD AMET A  62       9.433  33.632  12.578  0.65 15.98           S  
ANISOU  153  SD AMET A  62     2508   2345   1216   -284   -293   -269       S  
ATOM    154  SD BMET A  62       9.313  33.733  12.623  0.35 15.63           S  
ANISOU  154  SD BMET A  62     2259   2613   1066    -50   -299   -106       S  
ATOM    155  CE AMET A  62       9.166  32.047  13.320  0.65 22.02           C  
ANISOU  155  CE AMET A  62     3112   2294   2958    105   1032     63       C  
ATOM    156  CE BMET A  62      10.961  33.114  12.743  0.35  9.19           C  
ANISOU  156  CE BMET A  62     1011   1255   1222    296      0   -488       C  
ATOM    157  N   THR A  63       4.519  33.906   9.200  1.00  8.15           N  
ANISOU  157  N   THR A  63     1371   1143    580    -36      5   -163       N  
ATOM    158  CA  THR A  63       3.077  33.835   9.138  1.00  8.13           C  
ANISOU  158  CA  THR A  63     1370   1161    558    -28    -43     29       C  
ATOM    159  C   THR A  63       2.620  32.927   7.956  1.00  8.36           C  
ANISOU  159  C   THR A  63     1134   1244    797   -123    295    -61       C  
ATOM    160  O   THR A  63       1.730  32.095   8.135  1.00  8.60           O  
ANISOU  160  O   THR A  63     1298   1355    612   -125     64     32       O  
ATOM    161  CB  THR A  63       2.441  35.228   9.031  1.00  9.28           C  
ANISOU  161  CB  THR A  63     1419   1311    793   -161     90    -33       C  
ATOM    162  OG1 THR A  63       2.834  36.004  10.178  1.00  9.59           O  
ANISOU  162  OG1 THR A  63     1685   1469    488    -71      7   -201       O  
ATOM    163  CG2 THR A  63       0.910  35.196   8.959  1.00 10.35           C  
ANISOU  163  CG2 THR A  63     1272   1523   1136    -12   -105   -131       C  
ATOM    164  N   LYS A  64       3.320  33.028   6.819  1.00  8.63           N  
ANISOU  164  N   LYS A  64     1085   1303    890    -50    -29     48       N  
ATOM    165  CA  LYS A  64       3.009  32.159   5.691  1.00  8.93           C  
ANISOU  165  CA  LYS A  64     1496   1285    612   -303   -114     10       C  
ATOM    166  C   LYS A  64       3.199  30.683   6.084  1.00  8.52           C  
ANISOU  166  C   LYS A  64     1328   1328    580    -14   -220   -209       C  
ATOM    167  O   LYS A  64       2.322  29.834   5.784  1.00  8.79           O  
ANISOU  167  O   LYS A  64     1259   1328    750      0   -199   -251       O  
ATOM    168  CB  LYS A  64       3.858  32.537   4.471  1.00  9.49           C  
ANISOU  168  CB  LYS A  64     1440   1251    915   -107     -8    203       C  
ATOM    169  CG  LYS A  64       3.630  31.612   3.297  1.00 11.43           C  
ANISOU  169  CG  LYS A  64     2186   1535    620      4    207   -222       C  
ATOM    170  CD  LYS A  64       4.240  32.198   2.053  1.00 15.51           C  
ANISOU  170  CD  LYS A  64     2716   2726    449    -45   -193   -375       C  
ATOM    171  CE  LYS A  64       5.701  32.272   2.034  1.00 18.95           C  
ANISOU  171  CE  LYS A  64     3006   3424    768    101   -406   -405       C  
ATOM    172  NZ  LYS A  64       6.198  32.809   0.654  1.00 24.08           N  
ANISOU  172  NZ  LYS A  64     3938   3904   1304   -166    660    326       N  
ATOM    173  N   ILE A  65       4.348  30.335   6.658  1.00  7.97           N  
ANISOU  173  N   ILE A  65     1334   1269    425   -202   -105    -65       N  
ATOM    174  CA  ILE A  65       4.575  28.918   6.973  1.00  8.05           C  
ANISOU  174  CA  ILE A  65     1107   1353    597    -88    101    109       C  
ATOM    175  C   ILE A  65       3.667  28.412   8.089  1.00  7.44           C  
ANISOU  175  C   ILE A  65     1265    971    588   -130     61   -195       C  
ATOM    176  O   ILE A  65       3.269  27.261   8.084  1.00  7.60           O  
ANISOU  176  O   ILE A  65     1142   1246    500   -120     -2   -164       O  
ATOM    177  CB  ILE A  65       6.031  28.534   7.190  1.00 10.69           C  
ANISOU  177  CB  ILE A  65     1151   1702   1207   -166     58    487       C  
ATOM    178  CG1 ILE A  65       6.646  29.136   8.438  1.00 13.90           C  
ANISOU  178  CG1 ILE A  65     1630   2020   1630   -405     64     30       C  
ATOM    179  CG2 ILE A  65       6.891  28.864   5.964  1.00 12.44           C  
ANISOU  179  CG2 ILE A  65     1358   2134   1233   -147    393    638       C  
ATOM    180  CD1 ILE A  65       8.092  28.551   8.776  1.00 13.22           C  
ANISOU  180  CD1 ILE A  65     1516   2098   1407    189   -280    201       C  
ATOM    181  N   LEU A  66       3.284  29.311   9.018  1.00  7.24           N  
ANISOU  181  N   LEU A  66     1229    967    553   -193   -160    -78       N  
ATOM    182  CA  LEU A  66       2.322  28.893  10.042  1.00  7.62           C  
ANISOU  182  CA  LEU A  66     1259   1172    464   -358    -77    -91       C  
ATOM    183  C   LEU A  66       0.946  28.620   9.432  1.00  7.69           C  
ANISOU  183  C   LEU A  66     1363   1005    551   -120    256   -192       C  
ATOM    184  O   LEU A  66       0.242  27.697   9.845  1.00  9.00           O  
ANISOU  184  O   LEU A  66     1244   1481    694   -304     76     57       O  
ATOM    185  CB  LEU A  66       2.285  29.928  11.176  1.00  7.87           C  
ANISOU  185  CB  LEU A  66     1429   1270    290   -126    120     95       C  
ATOM    186  CG  LEU A  66       3.511  30.012  12.069  1.00  8.35           C  
ANISOU  186  CG  LEU A  66     1160   1550    462     59     16    -80       C  
ATOM    187  CD1 LEU A  66       3.431  31.207  13.044  1.00 11.54           C  
ANISOU  187  CD1 LEU A  66     2394   1437    552    -31   -285   -551       C  
ATOM    188  CD2 LEU A  66       3.671  28.699  12.826  1.00  9.57           C  
ANISOU  188  CD2 LEU A  66     2006   1321    307   -151   -290     11       C  
ATOM    189  N   GLU A  67       0.505  29.518   8.551  1.00  7.10           N  
ANISOU  189  N   GLU A  67     1214   1103    380   -115     22      3       N  
ATOM    190  CA  GLU A  67      -0.720  29.249   7.794  1.00  7.31           C  
ANISOU  190  CA  GLU A  67     1256   1218    303     78     95   -102       C  
ATOM    191  C   GLU A  67      -0.683  27.914   7.084  1.00  8.16           C  
ANISOU  191  C   GLU A  67     1339   1256    503    -13   -290    162       C  
ATOM    192  O   GLU A  67      -1.628  27.121   7.158  1.00  8.21           O  
ANISOU  192  O   GLU A  67     1358   1439    321   -154    -40     69       O  
ATOM    193  CB  GLU A  67      -1.021  30.394   6.795  1.00  8.47           C  
ANISOU  193  CB  GLU A  67     1450    999    767     34    -91     -9       C  
ATOM    194  CG  GLU A  67      -1.456  31.679   7.456  1.00  8.57           C  
ANISOU  194  CG  GLU A  67     1208   1130    915     15    -87     70       C  
ATOM    195  CD  GLU A  67      -1.608  32.852   6.518  1.00 10.33           C  
ANISOU  195  CD  GLU A  67     1640   1106   1177     -7   -308    115       C  
ATOM    196  OE1 GLU A  67      -1.091  32.754   5.367  1.00 13.88           O  
ANISOU  196  OE1 GLU A  67     2322   1665   1284    367    433    219       O  
ATOM    197  OE2 GLU A  67      -2.176  33.896   6.963  1.00 10.37           O  
ANISOU  197  OE2 GLU A  67     1768   1305    867    104   -107     85       O  
ATOM    198  N   GLN A  68       0.427  27.653   6.407  1.00  7.93           N  
ANISOU  198  N   GLN A  68     1209   1333    471   -159   -229    -88       N  
ATOM    199  CA  GLN A  68       0.528  26.397   5.656  1.00  7.99           C  
ANISOU  199  CA  GLN A  68     1233   1277    524   -116     66   -161       C  
ATOM    200  C   GLN A  68       0.459  25.196   6.592  1.00  8.66           C  
ANISOU  200  C   GLN A  68     1138   1228    922   -261    -99    -29       C  
ATOM    201  O   GLN A  68      -0.085  24.155   6.253  1.00  9.28           O  
ANISOU  201  O   GLN A  68     1274   1237   1015   -197   -115    153       O  
ATOM    202  CB  GLN A  68       1.788  26.368   4.816  1.00  9.28           C  
ANISOU  202  CB  GLN A  68     1242   1366    916     72   -321    -60       C  
ATOM    203  CG  GLN A  68       1.705  27.357   3.662  1.00  8.42           C  
ANISOU  203  CG  GLN A  68     1334   1243    620   -106   -337   -118       C  
ATOM    204  CD  GLN A  68       3.019  27.513   2.900  1.00 11.20           C  
ANISOU  204  CD  GLN A  68     1128   1898   1228   -234     77    143       C  
ATOM    205  OE1 GLN A  68       4.073  27.689   3.488  1.00 10.13           O  
ANISOU  205  OE1 GLN A  68     1313   1788    748     83    212    -63       O  
ATOM    206  NE2 GLN A  68       2.945  27.488   1.558  1.00 14.42           N  
ANISOU  206  NE2 GLN A  68     1979   2491   1007    258    -32    213       N  
ATOM    207  N   GLY A  69       0.997  25.357   7.800  1.00  8.05           N  
ANISOU  207  N   GLY A  69     1214   1328    516   -146    -73    -91       N  
ATOM    208  CA  GLY A  69       0.904  24.305   8.793  1.00  8.97           C  
ANISOU  208  CA  GLY A  69     1376   1355    678    -79    -55     51       C  
ATOM    209  C   GLY A  69      -0.509  24.074   9.285  1.00  8.75           C  
ANISOU  209  C   GLY A  69     1353   1291    679    -10   -122    158       C  
ATOM    210  O   GLY A  69      -0.985  22.929   9.271  1.00  8.87           O  
ANISOU  210  O   GLY A  69     1429   1362    578    -54   -231     56       O  
ATOM    211  N   ILE A  70      -1.213  25.144   9.675  1.00  8.79           N  
ANISOU  211  N   ILE A  70     1242   1232    866   -194   -102    219       N  
ATOM    212  CA  ILE A  70      -2.582  24.949  10.210  1.00  9.22           C  
ANISOU  212  CA  ILE A  70     1171   1351    979   -195   -210    175       C  
ATOM    213  C   ILE A  70      -3.553  24.507   9.068  1.00  9.83           C  
ANISOU  213  C   ILE A  70     1303   1441    988    -79   -100    120       C  
ATOM    214  O   ILE A  70      -4.580  23.920   9.345  1.00  8.64           O  
ANISOU  214  O   ILE A  70     1217   1335    728   -155   -129     37       O  
ATOM    215  CB  ILE A  70      -3.126  26.161  11.008  1.00  9.45           C  
ANISOU  215  CB  ILE A  70     1279   1619    690   -182    167    203       C  
ATOM    216  CG1 ILE A  70      -3.523  27.338  10.062  1.00  9.13           C  
ANISOU  216  CG1 ILE A  70     1362   1741    364   -221   -124    151       C  
ATOM    217  CG2 ILE A  70      -2.150  26.543  12.101  1.00 10.38           C  
ANISOU  217  CG2 ILE A  70     1503   2003    435   -451   -154   -128       C  
ATOM    218  CD1 ILE A  70      -4.218  28.530  10.752  1.00  9.46           C  
ANISOU  218  CD1 ILE A  70     1641   1548    405     34    108   -276       C  
ATOM    219  N   HIS A  71      -3.186  24.747   7.793  1.00  9.02           N  
ANISOU  219  N   HIS A  71     1235   1276    916   -310   -206    -30       N  
ATOM    220  CA  HIS A  71      -4.002  24.228   6.718  1.00  7.74           C  
ANISOU  220  CA  HIS A  71     1050   1370    518   -388   -202     51       C  
ATOM    221  C   HIS A  71      -4.131  22.689   6.813  1.00  8.17           C  
ANISOU  221  C   HIS A  71     1108   1328    667   -131   -249    106       C  
ATOM    222  O   HIS A  71      -5.146  22.128   6.400  1.00  8.79           O  
ANISOU  222  O   HIS A  71     1168   1509    661   -226   -284    -94       O  
ATOM    223  CB  HIS A  71      -3.461  24.604   5.361  1.00  7.70           C  
ANISOU  223  CB  HIS A  71     1157   1480    287   -241     60     60       C  
ATOM    224  CG  HIS A  71      -3.575  26.040   5.025  1.00  9.01           C  
ANISOU  224  CG  HIS A  71     1218   1331    873   -237   -245     -1       C  
ATOM    225  ND1 HIS A  71      -2.876  26.602   3.971  1.00 10.02           N  
ANISOU  225  ND1 HIS A  71     1486   1463    857   -335   -479    320       N  
ATOM    226  CD2 HIS A  71      -4.160  27.067   5.677  1.00  9.05           C  
ANISOU  226  CD2 HIS A  71     1565   1343    527    -77    416    155       C  
ATOM    227  CE1 HIS A  71      -3.098  27.904   3.949  1.00 10.90           C  
ANISOU  227  CE1 HIS A  71     1386   1926    829    324     45   -226       C  
ATOM    228  NE2 HIS A  71      -3.896  28.218   4.953  1.00  8.73           N  
ANISOU  228  NE2 HIS A  71     1444   1191    679      9    -45    -21       N  
ATOM    229  N   GLU A  72      -3.120  21.994   7.353  1.00  7.51           N  
ANISOU  229  N   GLU A  72     1141   1349    363     61   -177     12       N  
ATOM    230  CA  GLU A  72      -3.253  20.546   7.561  1.00  8.37           C  
ANISOU  230  CA  GLU A  72     1288   1453    438     96     17   -167       C  
ATOM    231  C   GLU A  72      -4.411  20.210   8.493  1.00  7.93           C  
ANISOU  231  C   GLU A  72     1127   1310    575    -28    -34    -65       C  
ATOM    232  O   GLU A  72      -5.116  19.235   8.289  1.00  9.58           O  
ANISOU  232  O   GLU A  72     1361   1628    649   -168    -73   -123       O  
ATOM    233  CB  GLU A  72      -1.968  19.892   8.049  1.00  8.52           C  
ANISOU  233  CB  GLU A  72     1099   1484    653     14    132    147       C  
ATOM    234  CG  GLU A  72      -0.806  19.972   7.055  1.00  9.42           C  
ANISOU  234  CG  GLU A  72     1135   1717    724    187    -97     26       C  
ATOM    235  CD  GLU A  72      -1.173  19.258   5.744  1.00 10.70           C  
ANISOU  235  CD  GLU A  72     1624   1287   1155     10    257      9       C  
ATOM    236  OE1 GLU A  72      -1.713  18.158   5.813  1.00 13.55           O  
ANISOU  236  OE1 GLU A  72     1758   2468    919     22   -120   -307       O  
ATOM    237  OE2 GLU A  72      -0.701  19.716   4.723  1.00 19.90           O  
ANISOU  237  OE2 GLU A  72     3932   2159   1470    762   1330    156       O  
ATOM    238  N   TYR A  73      -4.606  21.055   9.496  1.00  7.46           N  
ANISOU  238  N   TYR A  73     1205   1146    483   -175   -170    -76       N  
ATOM    239  CA  TYR A  73      -5.710  20.847  10.455  1.00  8.16           C  
ANISOU  239  CA  TYR A  73     1115   1390    596   -107    -36    -52       C  
ATOM    240  C   TYR A  73      -7.044  21.023   9.732  1.00  7.46           C  
ANISOU  240  C   TYR A  73     1100   1306    428   -176     33    -20       C  
ATOM    241  O   TYR A  73      -7.953  20.227   9.871  1.00  9.34           O  
ANISOU  241  O   TYR A  73     1306   1507    735   -177   -240     88       O  
ATOM    242  CB  TYR A  73      -5.642  21.826  11.637  1.00  7.80           C  
ANISOU  242  CB  TYR A  73     1022   1386    555     37    -63     -7       C  
ATOM    243  CG  TYR A  73      -4.306  21.997  12.351  1.00  8.33           C  
ANISOU  243  CG  TYR A  73     1013   1391    761   -135    -12     72       C  
ATOM    244  CD1 TYR A  73      -3.273  21.088  12.212  1.00  8.97           C  
ANISOU  244  CD1 TYR A  73      935   1387   1086    -44   -315   -176       C  
ATOM    245  CD2 TYR A  73      -4.091  23.103  13.169  1.00  8.25           C  
ANISOU  245  CD2 TYR A  73     1070   1286    776     43    -55   -111       C  
ATOM    246  CE1 TYR A  73      -2.076  21.277  12.852  1.00  9.46           C  
ANISOU  246  CE1 TYR A  73     1272   1475    846    154    -46   -277       C  
ATOM    247  CE2 TYR A  73      -2.934  23.280  13.818  1.00  8.98           C  
ANISOU  247  CE2 TYR A  73     1080   1451    881     88    -69   -322       C  
ATOM    248  CZ  TYR A  73      -1.895  22.431  13.625  1.00  8.04           C  
ANISOU  248  CZ  TYR A  73      894   1681    478     21    -57    -71       C  
ATOM    249  OH  TYR A  73      -0.690  22.673  14.265  1.00  9.87           O  
ANISOU  249  OH  TYR A  73     1237   1687    826     -8   -162   -304       O  
ATOM    250  N   TYR A  74      -7.156  22.113   8.979  1.00  8.14           N  
ANISOU  250  N   TYR A  74     1065   1334    690   -190     50     66       N  
ATOM    251  CA  TYR A  74      -8.406  22.401   8.270  1.00  7.77           C  
ANISOU  251  CA  TYR A  74      977   1351    622     27    -58   -143       C  
ATOM    252  C   TYR A  74      -8.734  21.396   7.160  1.00  8.81           C  
ANISOU  252  C   TYR A  74     1241   1279    826     20   -186    -24       C  
ATOM    253  O   TYR A  74      -9.904  21.172   6.867  1.00  9.65           O  
ANISOU  253  O   TYR A  74     1254   1565    848   -166   -126   -185       O  
ATOM    254  CB  TYR A  74      -8.401  23.802   7.707  1.00  8.65           C  
ANISOU  254  CB  TYR A  74     1221   1340    725     -3   -364     13       C  
ATOM    255  CG  TYR A  74      -8.626  24.848   8.794  1.00  9.62           C  
ANISOU  255  CG  TYR A  74     1411   1257    984    -41    -99     25       C  
ATOM    256  CD1 TYR A  74      -9.922  25.249   9.120  1.00 11.37           C  
ANISOU  256  CD1 TYR A  74     1494   1724   1099    117    -41    -15       C  
ATOM    257  CD2 TYR A  74      -7.585  25.300   9.609  1.00  9.20           C  
ANISOU  257  CD2 TYR A  74     1405   1584    506     21    175   -118       C  
ATOM    258  CE1 TYR A  74     -10.168  26.123  10.162  1.00 10.40           C  
ANISOU  258  CE1 TYR A  74     1324   1674    951    -26    270    -50       C  
ATOM    259  CE2 TYR A  74      -7.830  26.137  10.660  1.00 11.59           C  
ANISOU  259  CE2 TYR A  74     1490   1728   1183    110    -52   -102       C  
ATOM    260  CZ  TYR A  74      -9.089  26.602  10.903  1.00 11.04           C  
ANISOU  260  CZ  TYR A  74     1930   1400    863    -69    274   -171       C  
ATOM    261  OH  TYR A  74      -9.265  27.460  11.979  1.00 14.09           O  
ANISOU  261  OH  TYR A  74     2783   1870    698    -22    301   -349       O  
ATOM    262  N   LYS A  75      -7.715  20.783   6.559  1.00  8.23           N  
ANISOU  262  N   LYS A  75     1107   1337    681    -92   -240    -55       N  
ATOM    263  CA  LYS A  75      -7.974  19.786   5.516  1.00  9.93           C  
ANISOU  263  CA  LYS A  75     1225   1554    992   -174   -314    -59       C  
ATOM    264  C   LYS A  75      -8.487  18.489   6.093  1.00  9.97           C  
ANISOU  264  C   LYS A  75     1237   1411   1139   -295   -145    -96       C  
ATOM    265  O   LYS A  75      -9.120  17.712   5.396  1.00 12.09           O  
ANISOU  265  O   LYS A  75     1738   1604   1251   -571   -200   -208       O  
ATOM    266  CB  LYS A  75      -6.724  19.535   4.672  1.00  9.57           C  
ANISOU  266  CB  LYS A  75     1313   1602    720    -81   -296   -388       C  
ATOM    267  CG  LYS A  75      -6.434  20.672   3.687  1.00  9.33           C  
ANISOU  267  CG  LYS A  75     1163   1490    891    -83   -312   -110       C  
ATOM    268  CD  LYS A  75      -5.203  20.439   2.797  1.00 10.41           C  
ANISOU  268  CD  LYS A  75     1118   1986    851    171   -221    -66       C  
ATOM    269  CE  LYS A  75      -3.911  20.328   3.575  1.00 11.80           C  
ANISOU  269  CE  LYS A  75     1396   2407    680     38     -3     -6       C  
ATOM    270  NZ  LYS A  75      -2.752  20.111   2.689  1.00 15.74           N  
ANISOU  270  NZ  LYS A  75     1335   3854    791    349    281      4       N  
ATOM    271  N   SER A  76      -8.195  18.194   7.365  1.00 10.42           N  
ANISOU  271  N   SER A  76     1533   1468    958   -101   -138    -79       N  
ATOM    272  CA  SER A  76      -8.386  16.854   7.895  1.00 10.97           C  
ANISOU  272  CA  SER A  76     1520   1757    890   -214     28   -201       C  
ATOM    273  C   SER A  76      -9.331  16.727   9.076  1.00 11.06           C  
ANISOU  273  C   SER A  76     1585   1600   1017    -63   -197     93       C  
ATOM    274  O   SER A  76      -9.602  15.598   9.550  1.00 12.52           O  
ANISOU  274  O   SER A  76     1679   1573   1502   -187    -59     89       O  
ATOM    275  CB  SER A  76      -7.041  16.216   8.200  1.00 13.69           C  
ANISOU  275  CB  SER A  76     2026   1724   1450     25    418    210       C  
ATOM    276  OG  SER A  76      -6.341  15.999   6.973  1.00 18.36           O  
ANISOU  276  OG  SER A  76     2438   2477   2059    248    929    356       O  
ATOM    277  N   PHE A  77      -9.745  17.872   9.631  1.00  9.69           N  
ANISOU  277  N   PHE A  77     1454   1520    707   -113   -240     26       N  
ATOM    278  CA  PHE A  77     -10.627  17.892  10.811  1.00 10.75           C  
ANISOU  278  CA  PHE A  77     1458   1653    973   -311   -216      4       C  
ATOM    279  C   PHE A  77     -11.799  18.800  10.523  1.00  9.54           C  
ANISOU  279  C   PHE A  77     1246   1479    898   -264    -76   -137       C  
ATOM    280  O   PHE A  77     -11.681  19.703   9.698  1.00  9.72           O  
ANISOU  280  O   PHE A  77     1400   1529    762   -134   -119    -30       O  
ATOM    281  CB  PHE A  77      -9.876  18.345  12.048  1.00 10.58           C  
ANISOU  281  CB  PHE A  77     1430   1695    892   -317   -220    283       C  
ATOM    282  CG  PHE A  77      -8.717  17.442  12.419  1.00 11.17           C  
ANISOU  282  CG  PHE A  77     1757   1941    545   -231   -467    305       C  
ATOM    283  CD1 PHE A  77      -8.887  16.424  13.329  1.00 14.99           C  
ANISOU  283  CD1 PHE A  77     1936   2444   1313   -396   -486    893       C  
ATOM    284  CD2 PHE A  77      -7.493  17.510  11.744  1.00 12.74           C  
ANISOU  284  CD2 PHE A  77     1340   2070   1428   -140   -504    181       C  
ATOM    285  CE1 PHE A  77      -7.852  15.522  13.599  1.00 14.78           C  
ANISOU  285  CE1 PHE A  77     2108   2344   1160     26   -260   1072       C  
ATOM    286  CE2 PHE A  77      -6.469  16.604  11.999  1.00 13.76           C  
ANISOU  286  CE2 PHE A  77     1608   2053   1566   -371   -390    295       C  
ATOM    287  CZ  PHE A  77      -6.650  15.595  12.897  1.00 15.00           C  
ANISOU  287  CZ  PHE A  77     2133   2053   1513   -223   -234    373       C  
ATOM    288  N   ASP A  78     -12.898  18.653  11.260  1.00 10.85           N  
ANISOU  288  N   ASP A  78     1257   1696   1169   -133     87     37       N  
ATOM    289  CA  ASP A  78     -14.017  19.560  11.062  1.00 11.20           C  
ANISOU  289  CA  ASP A  78     1449   2045    758   -258     68   -129       C  
ATOM    290  C   ASP A  78     -13.624  20.987  11.503  1.00 11.07           C  
ANISOU  290  C   ASP A  78     1473   1975    759   -173    -33   -228       C  
ATOM    291  O   ASP A  78     -12.609  21.203  12.168  1.00 11.59           O  
ANISOU  291  O   ASP A  78     1537   1967    897   -118   -216   -232       O  
ATOM    292  CB  ASP A  78     -15.289  19.058  11.723  1.00 13.45           C  
ANISOU  292  CB  ASP A  78     1407   2514   1189   -286     18    103       C  
ATOM    293  CG  ASP A  78     -15.175  18.917  13.206  1.00 14.56           C  
ANISOU  293  CG  ASP A  78     1707   2620   1202   -953    977   -254       C  
ATOM    294  OD1 ASP A  78     -14.749  19.880  13.847  1.00 21.61           O  
ANISOU  294  OD1 ASP A  78     2535   3984   1689  -1686    216   -296       O  
ATOM    295  OD2 ASP A  78     -15.915  18.049  13.734  1.00 23.90           O  
ANISOU  295  OD2 ASP A  78     3145   3272   2661   -915    267    417       O  
ATOM    296  N   ASN A  79     -14.402  21.988  11.089  1.00 12.54           N  
ANISOU  296  N   ASN A  79     1398   2146   1219    -59   -399   -242       N  
ATOM    297  CA AASN A  79     -14.037  23.378  11.253  0.50 14.62           C  
ANISOU  297  CA AASN A  79     1992   2149   1413    214   -255   -360       C  
ATOM    298  CA BASN A  79     -13.952  23.360  11.227  0.50 14.28           C  
ANISOU  298  CA BASN A  79     1845   2151   1430    220   -241   -304       C  
ATOM    299  C   ASN A  79     -13.727  23.726  12.705  1.00 13.90           C  
ANISOU  299  C   ASN A  79     1646   2295   1339    128   -259   -358       C  
ATOM    300  O   ASN A  79     -12.735  24.363  13.033  1.00 13.37           O  
ANISOU  300  O   ASN A  79     1555   2514   1010    -81   -417   -569       O  
ATOM    301  CB AASN A  79     -15.194  24.268  10.793  0.50 16.17           C  
ANISOU  301  CB AASN A  79     2595   2193   1353    322   -306   -285       C  
ATOM    302  CB BASN A  79     -14.939  24.329  10.553  0.50 15.83           C  
ANISOU  302  CB BASN A  79     2138   2273   1604    199   -351   -142       C  
ATOM    303  CG AASN A  79     -14.960  25.703  11.122  0.50 17.54           C  
ANISOU  303  CG AASN A  79     2208   2262   2193     54   -294   -459       C  
ATOM    304  CG BASN A  79     -14.281  25.599  10.060  0.50 16.86           C  
ANISOU  304  CG BASN A  79     1874   2571   1958    252   -158     55       C  
ATOM    305  OD1AASN A  79     -14.010  26.301  10.626  0.50 21.26           O  
ANISOU  305  OD1AASN A  79     3198   2689   2188    115   -232   -643       O  
ATOM    306  OD1BASN A  79     -14.303  26.610  10.756  0.50 27.58           O  
ANISOU  306  OD1BASN A  79     4024   3321   3133    348     52    110       O  
ATOM    307  ND2AASN A  79     -15.731  26.230  12.066  0.50 23.41           N  
ANISOU  307  ND2AASN A  79     3036   3534   2325    421    249    -55       N  
ATOM    308  ND2BASN A  79     -13.689  25.561   8.859  0.50 22.23           N  
ANISOU  308  ND2BASN A  79     2245   3370   2829   -522   1057    757       N  
ATOM    309  N   ASP A  80     -14.617  23.313  13.585  1.00 14.14           N  
ANISOU  309  N   ASP A  80     1654   2553   1163    -48   -168   -613       N  
ATOM    310  CA  ASP A  80     -14.488  23.678  15.024  1.00 14.38           C  
ANISOU  310  CA  ASP A  80     1619   2829   1014   -148    -87   -692       C  
ATOM    311  C   ASP A  80     -13.246  23.032  15.656  1.00 13.27           C  
ANISOU  311  C   ASP A  80     1406   2589   1044   -398    188   -300       C  
ATOM    312  O   ASP A  80     -12.491  23.679  16.393  1.00 13.81           O  
ANISOU  312  O   ASP A  80     1448   2946    851   -492    150   -530       O  
ATOM    313  CB  ASP A  80     -15.733  23.324  15.817  1.00 18.02           C  
ANISOU  313  CB  ASP A  80     2026   3849    971    -74     45   -685       C  
ATOM    314  CG  ASP A  80     -16.938  24.214  15.473  1.00 23.36           C  
ANISOU  314  CG  ASP A  80     2462   4005   2409    -35    107   -502       C  
ATOM    315  OD1 ASP A  80     -16.785  25.307  14.854  1.00 25.23           O  
ANISOU  315  OD1 ASP A  80     2465   4052   3066    178    127   -653       O  
ATOM    316  OD2 ASP A  80     -18.056  23.830  15.856  1.00 30.33           O  
ANISOU  316  OD2 ASP A  80     2430   5034   4058   -174    299   -598       O  
ATOM    317  N   THR A  81     -12.970  21.795  15.264  1.00 12.44           N  
ANISOU  317  N   THR A  81     1496   2259    969   -409     69     25       N  
ATOM    318  CA  THR A  81     -11.774  21.071  15.747  1.00 12.18           C  
ANISOU  318  CA  THR A  81     1449   2268    910   -351    123    -16       C  
ATOM    319  C   THR A  81     -10.488  21.660  15.164  1.00 11.95           C  
ANISOU  319  C   THR A  81     1296   2101   1143   -422   -133     52       C  
ATOM    320  O   THR A  81      -9.496  21.865  15.875  1.00 11.28           O  
ANISOU  320  O   THR A  81     1447   2288    548   -445    -64    -56       O  
ATOM    321  CB  THR A  81     -11.878  19.578  15.407  1.00 12.74           C  
ANISOU  321  CB  THR A  81     1599   2152   1090   -573     93    207       C  
ATOM    322  OG1 THR A  81     -13.065  19.032  16.020  1.00 15.95           O  
ANISOU  322  OG1 THR A  81     1790   3116   1152   -983    137    389       O  
ATOM    323  CG2 THR A  81     -10.655  18.784  15.879  1.00 14.23           C  
ANISOU  323  CG2 THR A  81     1554   2517   1333   -284   -190    266       C  
ATOM    324  N   ALA A  82     -10.521  22.021  13.879  1.00 10.56           N  
ANISOU  324  N   ALA A  82     1409   1806    796   -351    -53    -17       N  
ATOM    325  CA  ALA A  82      -9.361  22.630  13.234  1.00  8.84           C  
ANISOU  325  CA  ALA A  82     1120   1797    441   -229   -196    -58       C  
ATOM    326  C   ALA A  82      -9.031  23.971  13.903  1.00 10.25           C  
ANISOU  326  C   ALA A  82     1288   1869    734   -371    -38    -87       C  
ATOM    327  O   ALA A  82      -7.856  24.284  14.170  1.00  9.87           O  
ANISOU  327  O   ALA A  82     1447   1878    423   -235     65   -131       O  
ATOM    328  CB  ALA A  82      -9.612  22.793  11.750  1.00 10.75           C  
ANISOU  328  CB  ALA A  82     1546   2135    400   -128   -235    -92       C  
ATOM    329  N   ARG A  83     -10.060  24.776  14.198  1.00 10.36           N  
ANISOU  329  N   ARG A  83     1382   1921    631   -215    133   -322       N  
ATOM    330  CA  ARG A  83      -9.802  26.035  14.887  1.00 13.34           C  
ANISOU  330  CA  ARG A  83     1465   2228   1374    -69     79    -64       C  
ATOM    331  C   ARG A  83      -9.200  25.810  16.285  1.00 11.97           C  
ANISOU  331  C   ARG A  83     1532   2025    991   -402    127   -341       C  
ATOM    332  O   ARG A  83      -8.256  26.494  16.696  1.00 11.65           O  
ANISOU  332  O   ARG A  83     1396   2058    970   -306    186   -316       O  
ATOM    333  CB  ARG A  83     -10.996  26.943  14.960  1.00 14.99           C  
ANISOU  333  CB  ARG A  83     2109   2569   1015    111   -229   -691       C  
ATOM    334  CG  ARG A  83     -10.520  28.313  15.498  1.00 20.38           C  
ANISOU  334  CG  ARG A  83     2966   3175   1602    250   -560   -801       C  
ATOM    335  CD  ARG A  83     -11.517  29.208  15.694  1.00 24.08           C  
ANISOU  335  CD  ARG A  83     3951   3363   1834     34   -485   -465       C  
ATOM    336  NE  ARG A  83     -11.872  29.906  14.503  1.00 20.54           N  
ANISOU  336  NE  ARG A  83     3035   2778   1990   -178   -124   -535       N  
ATOM    337  CZ  ARG A  83     -12.830  30.802  14.526  1.00 25.94           C  
ANISOU  337  CZ  ARG A  83     3587   3182   3085   -558    809   -137       C  
ATOM    338  NH1 ARG A  83     -13.435  31.023  15.686  1.00 26.99           N  
ANISOU  338  NH1 ARG A  83     3181   3524   3549   -587    575  -1126       N  
ATOM    339  NH2 ARG A  83     -13.244  31.365  13.425  1.00 30.05           N  
ANISOU  339  NH2 ARG A  83     3952   3724   3739    -73   -872    -51       N  
ATOM    340  N   LYS A  84      -9.762  24.846  17.016  1.00 12.18           N  
ANISOU  340  N   LYS A  84     1186   2338   1102   -442    -46    -95       N  
ATOM    341  CA  LYS A  84      -9.213  24.483  18.344  1.00 12.77           C  
ANISOU  341  CA  LYS A  84     1764   2376    710   -237    -37   -147       C  
ATOM    342  C   LYS A  84      -7.742  24.095  18.264  1.00 12.74           C  
ANISOU  342  C   LYS A  84     1506   2002   1329   -458     79     -5       C  
ATOM    343  O   LYS A  84      -6.900  24.483  19.092  1.00 13.66           O  
ANISOU  343  O   LYS A  84     1646   2578    963   -749     73   -203       O  
ATOM    344  CB  LYS A  84     -10.049  23.384  18.997  1.00 15.56           C  
ANISOU  344  CB  LYS A  84     1957   2707   1245   -312    176     13       C  
ATOM    345  CG  LYS A  84     -11.295  23.914  19.636  1.00 20.76           C  
ANISOU  345  CG  LYS A  84     3327   3637    920    226   -316   -181       C  
ATOM    346  CD  LYS A  84     -12.155  22.804  20.293  1.00 23.61           C  
ANISOU  346  CD  LYS A  84     3603   3919   1448   -225     12   -147       C  
ATOM    347  CE  LYS A  84     -13.449  23.418  20.847  1.00 34.60           C  
ANISOU  347  CE  LYS A  84     4399   5264   3481    250    503   -180       C  
ATOM    348  N   MET A  85      -7.414  23.312  17.269  1.00 12.18           N  
ANISOU  348  N   MET A  85     1610   1927   1090   -458     29    -81       N  
ATOM    349  CA  MET A  85      -6.055  22.876  17.054  1.00 11.26           C  
ANISOU  349  CA  MET A  85     1646   1804    828   -182      7    163       C  
ATOM    350  C   MET A  85      -5.140  24.054  16.764  1.00  9.14           C  
ANISOU  350  C   MET A  85     1287   1606    578   -204    -37     29       C  
ATOM    351  O   MET A  85      -4.039  24.153  17.288  1.00 10.17           O  
ANISOU  351  O   MET A  85     1338   1814    711   -324    -23    -30       O  
ATOM    352  CB  MET A  85      -6.001  21.865  15.893  1.00  9.73           C  
ANISOU  352  CB  MET A  85     1715   1406    575   -291     50     82       C  
ATOM    353  CG  MET A  85      -6.682  20.559  16.183  1.00 11.19           C  
ANISOU  353  CG  MET A  85     1809   1691    751      7    -75    -12       C  
ATOM    354  SD  MET A  85      -6.866  19.456  14.770  1.00 12.87           S  
ANISOU  354  SD  MET A  85     1762   1960   1166   -314   -285     87       S  
ATOM    355  CE  MET A  85      -5.187  18.965  14.433  1.00 14.06           C  
ANISOU  355  CE  MET A  85     1527   2264   1549   -206   -258    322       C  
ATOM    356  N   ALA A  86      -5.596  24.961  15.908  1.00  9.22           N  
ANISOU  356  N   ALA A  86     1507   1454    542   -305    -38    -35       N  
ATOM    357  CA  ALA A  86      -4.801  26.123  15.560  1.00  8.40           C  
ANISOU  357  CA  ALA A  86     1343   1406    440   -274    201   -186       C  
ATOM    358  C   ALA A  86      -4.519  26.987  16.796  1.00  9.08           C  
ANISOU  358  C   ALA A  86     1300   1544    603    -72    141   -255       C  
ATOM    359  O   ALA A  86      -3.389  27.439  17.011  1.00  9.25           O  
ANISOU  359  O   ALA A  86     1311   1740    464    -93     52   -206       O  
ATOM    360  CB  ALA A  86      -5.531  26.962  14.461  1.00 10.31           C  
ANISOU  360  CB  ALA A  86     1670   1403    845    -14    -52    168       C  
ATOM    361  N   LEU A  87      -5.553  27.235  17.607  1.00  9.96           N  
ANISOU  361  N   LEU A  87     1299   1835    649   -290    183   -399       N  
ATOM    362  CA  LEU A  87      -5.370  28.112  18.767  1.00 10.54           C  
ANISOU  362  CA  LEU A  87     1356   1870    777   -118     -4   -550       C  
ATOM    363  C   LEU A  87      -4.599  27.403  19.886  1.00  9.21           C  
ANISOU  363  C   LEU A  87     1428   1527    544   -120    218   -344       C  
ATOM    364  O   LEU A  87      -3.850  28.083  20.616  1.00 11.16           O  
ANISOU  364  O   LEU A  87     1462   2098    678   -327     11   -574       O  
ATOM    365  CB  LEU A  87      -6.715  28.667  19.250  1.00 12.01           C  
ANISOU  365  CB  LEU A  87     1467   2484    610   -110   -148   -583       C  
ATOM    366  CG  LEU A  87      -7.495  29.459  18.169  1.00 12.42           C  
ANISOU  366  CG  LEU A  87     1533   2011   1174    210   -263   -585       C  
ATOM    367  CD1 LEU A  87      -8.735  30.102  18.769  1.00 16.80           C  
ANISOU  367  CD1 LEU A  87     1824   2661   1897    368    -72   -825       C  
ATOM    368  CD2 LEU A  87      -6.629  30.487  17.403  1.00 14.85           C  
ANISOU  368  CD2 LEU A  87     2425   2246    971     47   -115     -9       C  
ATOM    369  N   ASP A  88      -4.725  26.089  20.014  1.00 10.22           N  
ANISOU  369  N   ASP A  88     1223   1927    731   -310    120   -247       N  
ATOM    370  CA  ASP A  88      -3.869  25.332  20.948  1.00 11.52           C  
ANISOU  370  CA  ASP A  88     1617   1906    852   -267   -123    -13       C  
ATOM    371  C   ASP A  88      -2.417  25.404  20.514  1.00 10.81           C  
ANISOU  371  C   ASP A  88     1382   2052    671   -388     28     78       C  
ATOM    372  O   ASP A  88      -1.506  25.604  21.327  1.00  9.95           O  
ANISOU  372  O   ASP A  88     1498   1885    397   -422     54    -36       O  
ATOM    373  CB  ASP A  88      -4.294  23.866  21.079  1.00 13.12           C  
ANISOU  373  CB  ASP A  88     1652   2139   1192   -223    323    306       C  
ATOM    374  CG  ASP A  88      -3.357  23.070  22.007  1.00 16.19           C  
ANISOU  374  CG  ASP A  88     2452   2494   1205     20    397    386       C  
ATOM    375  OD1 ASP A  88      -3.645  23.059  23.218  1.00 22.89           O  
ANISOU  375  OD1 ASP A  88     3102   4384   1211    278    651    479       O  
ATOM    376  OD2 ASP A  88      -2.462  22.309  21.519  1.00 17.19           O  
ANISOU  376  OD2 ASP A  88     2804   2660   1065    -13   -375   -168       O  
ATOM    377  N   TYR A  89      -2.179  25.293  19.210  1.00  9.18           N  
ANISOU  377  N   TYR A  89     1296   1569    623   -293      5      9       N  
ATOM    378  CA  TYR A  89      -0.847  25.431  18.674  1.00  9.03           C  
ANISOU  378  CA  TYR A  89     1341   1438    650    -57    158   -117       C  
ATOM    379  C   TYR A  89      -0.273  26.806  18.993  1.00  9.04           C  
ANISOU  379  C   TYR A  89     1186   1556    690   -101    159     19       C  
ATOM    380  O   TYR A  89       0.877  26.936  19.437  1.00  9.11           O  
ANISOU  380  O   TYR A  89     1252   1549    660    -62     35   -141       O  
ATOM    381  CB  TYR A  89      -0.844  25.122  17.149  1.00  9.18           C  
ANISOU  381  CB  TYR A  89     1404   1260    824      0    197   -144       C  
ATOM    382  CG  TYR A  89       0.464  25.301  16.416  1.00  7.66           C  
ANISOU  382  CG  TYR A  89      992   1196    719     50    240     20       C  
ATOM    383  CD1 TYR A  89       1.691  25.088  17.030  1.00  6.71           C  
ANISOU  383  CD1 TYR A  89     1076   1194    276    -32    104     92       C  
ATOM    384  CD2 TYR A  89       0.462  25.845  15.163  1.00 10.00           C  
ANISOU  384  CD2 TYR A  89     1290   1289   1219    -61   -377     79       C  
ATOM    385  CE1 TYR A  89       2.882  25.245  16.346  1.00  8.20           C  
ANISOU  385  CE1 TYR A  89     1230   1412    471    -14    -75    145       C  
ATOM    386  CE2 TYR A  89       1.614  25.944  14.438  1.00  9.23           C  
ANISOU  386  CE2 TYR A  89     1354   1415    736    143     15   -257       C  
ATOM    387  CZ  TYR A  89       2.830  25.671  15.010  1.00  8.54           C  
ANISOU  387  CZ  TYR A  89     1029   1417    798    158     60    253       C  
ATOM    388  OH  TYR A  89       4.000  25.780  14.258  1.00  9.29           O  
ANISOU  388  OH  TYR A  89     1316   1606    608     97    128    -11       O  
ATOM    389  N   PHE A  90      -1.051  27.842  18.697  1.00  9.10           N  
ANISOU  389  N   PHE A  90     1161   1426    871     29    -52    -25       N  
ATOM    390  CA  PHE A  90      -0.593  29.200  18.938  1.00  9.02           C  
ANISOU  390  CA  PHE A  90     1392   1271    760    -95     -5    -81       C  
ATOM    391  C   PHE A  90      -0.308  29.443  20.440  1.00  8.57           C  
ANISOU  391  C   PHE A  90      997   1440    816    -84     12    -25       C  
ATOM    392  O   PHE A  90       0.636  30.167  20.756  1.00  9.14           O  
ANISOU  392  O   PHE A  90     1231   1530    710      0    -89   -168       O  
ATOM    393  CB  PHE A  90      -1.523  30.254  18.353  1.00  9.45           C  
ANISOU  393  CB  PHE A  90     1396   1290    903    -69     50   -250       C  
ATOM    394  CG  PHE A  90      -1.594  30.238  16.807  1.00  9.50           C  
ANISOU  394  CG  PHE A  90     1397   1459    754   -141     48   -265       C  
ATOM    395  CD1 PHE A  90      -0.733  29.466  16.037  1.00 10.71           C  
ANISOU  395  CD1 PHE A  90     1582   1461   1026    -99    -79   -234       C  
ATOM    396  CD2 PHE A  90      -2.518  31.033  16.148  1.00 11.44           C  
ANISOU  396  CD2 PHE A  90     1613   1923    810    289   -221   -113       C  
ATOM    397  CE1 PHE A  90      -0.798  29.517  14.615  1.00 11.82           C  
ANISOU  397  CE1 PHE A  90     1659   1547   1283    111     89   -250       C  
ATOM    398  CE2 PHE A  90      -2.569  31.060  14.752  1.00 14.13           C  
ANISOU  398  CE2 PHE A  90     2157   2114   1098    526   -202   -144       C  
ATOM    399  CZ  PHE A  90      -1.727  30.301  14.006  1.00 11.93           C  
ANISOU  399  CZ  PHE A  90     1972   1506   1053    105     28   -204       C  
ATOM    400  N   LYS A  91      -1.117  28.855  21.333  1.00  8.55           N  
ANISOU  400  N   LYS A  91     1154   1560    534   -314    -50   -285       N  
ATOM    401  CA ALYS A  91      -0.821  28.897  22.780  0.50  9.44           C  
ANISOU  401  CA ALYS A  91     1443   1553    590   -197    -75   -393       C  
ATOM    402  CA BLYS A  91      -0.791  28.950  22.765  0.50  9.04           C  
ANISOU  402  CA BLYS A  91     1421   1457    554   -232    -83   -395       C  
ATOM    403  C   LYS A  91       0.561  28.321  23.049  1.00  8.79           C  
ANISOU  403  C   LYS A  91     1438   1449    452   -261    -57    -84       C  
ATOM    404  O   LYS A  91       1.339  28.879  23.814  1.00  9.70           O  
ANISOU  404  O   LYS A  91     1615   1618    453   -181     59   -317       O  
ATOM    405  CB ALYS A  91      -1.882  28.089  23.562  0.50 11.16           C  
ANISOU  405  CB ALYS A  91     1432   1994    815   -119    137   -375       C  
ATOM    406  CB BLYS A  91      -1.867  28.298  23.652  0.50 11.17           C  
ANISOU  406  CB BLYS A  91     1420   2008    814   -205    102   -207       C  
ATOM    407  CG ALYS A  91      -1.810  28.219  25.088  0.50 13.70           C  
ANISOU  407  CG ALYS A  91     1579   2515   1111   -260    175   -276       C  
ATOM    408  CG BLYS A  91      -1.390  28.026  25.089  0.50 13.44           C  
ANISOU  408  CG BLYS A  91     1845   2076   1186   -231    225   -176       C  
ATOM    409  CD ALYS A  91      -2.606  27.075  25.779  0.50 15.41           C  
ANISOU  409  CD ALYS A  91     1989   3024    841   -516    545    411       C  
ATOM    410  CD BLYS A  91      -2.554  27.723  26.047  0.50 16.40           C  
ANISOU  410  CD BLYS A  91     2222   2335   1674    -76    280     81       C  
ATOM    411  CE ALYS A  91      -2.568  27.154  27.308  0.50 22.43           C  
ANISOU  411  CE ALYS A  91     3113   3569   1839   -277   -149    144       C  
ATOM    412  CE BLYS A  91      -2.036  27.290  27.434  0.50 22.71           C  
ANISOU  412  CE BLYS A  91     2655   3483   2490    -37     89    305       C  
ATOM    413  NZ ALYS A  91      -1.254  26.712  27.870  0.50 20.54           N  
ANISOU  413  NZ ALYS A  91     3157   3562   1084      8   -533   -196       N  
ATOM    414  NZ BLYS A  91      -1.032  28.227  28.038  0.50 22.32           N  
ANISOU  414  NZ BLYS A  91     2336   3059   3083   -158   1135    -63       N  
ATOM    415  N   ARG A  92       0.872  27.180  22.416  1.00  9.15           N  
ANISOU  415  N   ARG A  92     1325   1653    498    -33    -54   -107       N  
ATOM    416  CA  ARG A  92       2.171  26.579  22.594  1.00  8.83           C  
ANISOU  416  CA  ARG A  92     1400   1649    304    -76    -45    -25       C  
ATOM    417  C   ARG A  92       3.337  27.429  22.057  1.00  7.68           C  
ANISOU  417  C   ARG A  92     1041   1347    527     55    -41   -184       C  
ATOM    418  O   ARG A  92       4.384  27.542  22.721  1.00  9.23           O  
ANISOU  418  O   ARG A  92     1219   1643    642    -65   -126     94       O  
ATOM    419  CB  ARG A  92       2.195  25.179  21.959  1.00  9.96           C  
ANISOU  419  CB  ARG A  92     1654   1682    446   -168    -43     29       C  
ATOM    420  CG  ARG A  92       1.270  24.214  22.689  1.00 14.06           C  
ANISOU  420  CG  ARG A  92     1893   2142   1305      0   -279     69       C  
ATOM    421  CD  ARG A  92       1.211  22.844  22.084  1.00 18.65           C  
ANISOU  421  CD  ARG A  92     2770   2442   1871   -243    335    -88       C  
ATOM    422  NE  ARG A  92       0.224  21.972  22.725  1.00 20.68           N  
ANISOU  422  NE  ARG A  92     2555   2729   2571   -299    159     63       N  
ATOM    423  CZ  ARG A  92       0.489  21.147  23.732  1.00 30.21           C  
ANISOU  423  CZ  ARG A  92     3601   3827   4048   -315   -192    656       C  
ATOM    424  NH1 ARG A  92       1.701  21.093  24.266  1.00 28.84           N  
ANISOU  424  NH1 ARG A  92     3651   3643   3663   -984   -402    736       N  
ATOM    425  NH2 ARG A  92      -0.439  20.288  24.131  1.00 34.44           N  
ANISOU  425  NH2 ARG A  92     4332   4618   4135   -965   -246    983       N  
ATOM    426  N   ILE A  93       3.123  28.123  20.950  1.00  8.70           N  
ANISOU  426  N   ILE A  93     1412   1420    470    -82   -105     21       N  
ATOM    427  CA  ILE A  93       4.132  29.068  20.434  1.00  8.30           C  
ANISOU  427  CA  ILE A  93     1381   1085    688    -30    -36    -40       C  
ATOM    428  C   ILE A  93       4.333  30.182  21.479  1.00  8.37           C  
ANISOU  428  C   ILE A  93     1294   1292    592    -32     21    -64       C  
ATOM    429  O   ILE A  93       5.473  30.487  21.898  1.00  9.00           O  
ANISOU  429  O   ILE A  93     1334   1669    417    -68     95   -157       O  
ATOM    430  CB  ILE A  93       3.745  29.655  19.081  1.00  8.24           C  
ANISOU  430  CB  ILE A  93     1348   1185    595    138    -36   -152       C  
ATOM    431  CG1 ILE A  93       3.716  28.556  18.017  1.00  8.31           C  
ANISOU  431  CG1 ILE A  93     1249   1149    759    -46   -167    -80       C  
ATOM    432  CG2 ILE A  93       4.671  30.814  18.647  1.00  9.88           C  
ANISOU  432  CG2 ILE A  93     1589   1284    880   -351     43   -137       C  
ATOM    433  CD1 ILE A  93       3.271  29.017  16.630  1.00  9.72           C  
ANISOU  433  CD1 ILE A  93     1752   1654    285   -117   -159   -133       C  
ATOM    434  N   ASN A  94       3.240  30.781  21.942  1.00  8.51           N  
ANISOU  434  N   ASN A  94     1246   1400    584    -70    -90   -170       N  
ATOM    435  CA  ASN A  94       3.395  31.894  22.873  1.00  8.65           C  
ANISOU  435  CA  ASN A  94     1311   1510    465     18   -125   -151       C  
ATOM    436  C   ASN A  94       4.100  31.426  24.175  1.00  9.23           C  
ANISOU  436  C   ASN A  94     1355   1432    716    -63    113   -258       C  
ATOM    437  O   ASN A  94       4.918  32.152  24.740  1.00  9.82           O  
ANISOU  437  O   ASN A  94     1529   1760    441    -90   -144   -376       O  
ATOM    438  CB  ASN A  94       2.086  32.600  23.155  1.00  8.24           C  
ANISOU  438  CB  ASN A  94     1377   1228    522      0    -92   -164       C  
ATOM    439  CG  ASN A  94       1.573  33.417  21.972  1.00  8.63           C  
ANISOU  439  CG  ASN A  94     1316   1264    698    188   -127   -341       C  
ATOM    440  OD1 ASN A  94       1.901  33.084  20.815  1.00  9.70           O  
ANISOU  440  OD1 ASN A  94     1568   1637    481     72    224   -315       O  
ATOM    441  ND2 ASN A  94       0.813  34.485  22.256  1.00  9.94           N  
ANISOU  441  ND2 ASN A  94     1442   1595    740     26     66   -326       N  
ATOM    442  N   ASP A  95       3.715  30.248  24.654  1.00  9.60           N  
ANISOU  442  N   ASP A  95     1409   1597    642   -138   -102   -189       N  
ATOM    443  CA  ASP A  95       4.335  29.649  25.839  1.00 10.15           C  
ANISOU  443  CA  ASP A  95     1733   1723    397    113   -210   -308       C  
ATOM    444  C   ASP A  95       5.809  29.387  25.694  1.00 10.87           C  
ANISOU  444  C   ASP A  95     1641   1731    757    -95   -169   -148       C  
ATOM    445  O   ASP A  95       6.532  29.284  26.694  1.00 12.31           O  
ANISOU  445  O   ASP A  95     1773   2122    779    -31   -198   -107       O  
ATOM    446  CB  ASP A  95       3.600  28.377  26.261  1.00 11.14           C  
ANISOU  446  CB  ASP A  95     1820   1990    421     54    -70     13       C  
ATOM    447  CG  ASP A  95       2.215  28.625  26.847  1.00 13.08           C  
ANISOU  447  CG  ASP A  95     2069   1890   1008    -24    -78      0       C  
ATOM    448  OD1 ASP A  95       1.867  29.779  27.199  1.00 16.00           O  
ANISOU  448  OD1 ASP A  95     2348   2216   1515    110    405   -174       O  
ATOM    449  OD2 ASP A  95       1.477  27.599  27.010  1.00 15.83           O  
ANISOU  449  OD2 ASP A  95     2240   2280   1493   -381    347    -33       O  
ATOM    450  N   ASP A  96       6.299  29.248  24.461  1.00  9.27           N  
ANISOU  450  N   ASP A  96     1304   1812    407    -80   -391    -81       N  
ATOM    451  CA  ASP A  96       7.709  29.078  24.174  1.00  9.59           C  
ANISOU  451  CA  ASP A  96     1450   1506    688    -91   -292   -119       C  
ATOM    452  C   ASP A  96       8.532  30.325  24.559  1.00 10.77           C  
ANISOU  452  C   ASP A  96     1642   1697    751    -93   -104   -185       C  
ATOM    453  O   ASP A  96       9.754  30.232  24.730  1.00 11.44           O  
ANISOU  453  O   ASP A  96     1628   1956    761    -66   -376   -246       O  
ATOM    454  CB  ASP A  96       8.029  28.703  22.710  1.00 10.44           C  
ANISOU  454  CB  ASP A  96     1508   1513    943    105    -88   -105       C  
ATOM    455  CG  ASP A  96       7.525  27.391  22.297  1.00 11.18           C  
ANISOU  455  CG  ASP A  96     1539   1540   1167    -66   -198    137       C  
ATOM    456  OD1 ASP A  96       7.327  26.474  23.124  1.00 10.59           O  
ANISOU  456  OD1 ASP A  96     1741   1596    686    -89   -409   -169       O  
ATOM    457  OD2 ASP A  96       7.271  27.249  21.064  1.00 10.98           O  
ANISOU  457  OD2 ASP A  96     1612   1983    576   -143   -231   -115       O  
ATOM    458  N   LYS A  97       7.880  31.491  24.604  1.00 11.02           N  
ANISOU  458  N   LYS A  97     1507   1577   1102   -116   -327   -320       N  
ATOM    459  CA  LYS A  97       8.551  32.748  24.973  1.00 10.93           C  
ANISOU  459  CA  LYS A  97     1784   1726    640   -211   -174   -450       C  
ATOM    460  C   LYS A  97       9.824  32.989  24.152  1.00 11.67           C  
ANISOU  460  C   LYS A  97     1578   1845   1011   -393   -197   -216       C  
ATOM    461  O   LYS A  97      10.891  33.350  24.670  1.00 13.48           O  
ANISOU  461  O   LYS A  97     1703   2251   1166   -275   -100   -172       O  
ATOM    462  CB  LYS A  97       8.818  32.807  26.480  1.00 12.48           C  
ANISOU  462  CB  LYS A  97     2103   1812    827   -236    -22   -382       C  
ATOM    463  CG  LYS A  97       7.521  32.790  27.295  1.00 15.43           C  
ANISOU  463  CG  LYS A  97     2393   2460   1009    -94    -97   -594       C  
ATOM    464  CD  LYS A  97       7.759  32.937  28.784  1.00 19.81           C  
ANISOU  464  CD  LYS A  97     2681   3415   1429   -257    -39   -698       C  
ATOM    465  CE  LYS A  97       8.516  31.791  29.347  1.00 32.11           C  
ANISOU  465  CE  LYS A  97     4442   4602   3156    169    -94   -309       C  
ATOM    466  NZ  LYS A  97       7.749  30.528  29.242  1.00 40.40           N  
ANISOU  466  NZ  LYS A  97     5391   5658   4299   -132    -91   -116       N  
ATOM    467  N   GLY A  98       9.681  32.827  22.828  1.00 11.07           N  
ANISOU  467  N   GLY A  98     1378   1911    916   -175   -219   -410       N  
ATOM    468  CA  GLY A  98      10.796  32.996  21.899  1.00 11.68           C  
ANISOU  468  CA  GLY A  98     1450   1771   1217     36   -255   -345       C  
ATOM    469  C   GLY A  98      10.580  34.164  20.961  1.00 10.56           C  
ANISOU  469  C   GLY A  98     1369   1529   1114    106    -75   -264       C  
ATOM    470  O   GLY A  98      10.194  35.254  21.356  1.00 11.73           O  
ANISOU  470  O   GLY A  98     1877   1635    943   -146    -64   -378       O  
ATOM    471  N   MET A  99      10.879  33.932  19.683  1.00 10.78           N  
ANISOU  471  N   MET A  99     1598   1673    823    169     91   -348       N  
ATOM    472  CA  MET A  99      10.928  35.013  18.728  1.00 10.37           C  
ANISOU  472  CA  MET A  99     1314   1535   1089    -21    -47   -231       C  
ATOM    473  C   MET A  99       9.598  35.723  18.518  1.00  9.66           C  
ANISOU  473  C   MET A  99     1312   1368    990      2    166   -334       C  
ATOM    474  O   MET A  99       9.598  36.942  18.295  1.00 10.48           O  
ANISOU  474  O   MET A  99     1476   1429   1075   -151    101   -348       O  
ATOM    475  CB  MET A  99      11.477  34.542  17.375  1.00 12.08           C  
ANISOU  475  CB  MET A  99     1432   1649   1509     77    338   -311       C  
ATOM    476  CG  MET A  99      12.889  34.017  17.411  1.00 13.46           C  
ANISOU  476  CG  MET A  99     1842   1783   1489    -86    137   -453       C  
ATOM    477  SD  MET A  99      13.494  33.502  15.799  1.00 14.94           S  
ANISOU  477  SD  MET A  99     2169   2115   1392    155    484   -353       S  
ATOM    478  CE  MET A  99      13.682  35.092  14.974  1.00 17.58           C  
ANISOU  478  CE  MET A  99     2831   1921   1927   -215    834    117       C  
ATOM    479  N   ILE A 100       8.516  34.951  18.463  1.00  8.42           N  
ANISOU  479  N   ILE A 100     1205   1451    543    -40     42   -288       N  
ATOM    480  CA  ILE A 100       7.228  35.473  18.095  1.00  8.67           C  
ANISOU  480  CA  ILE A 100     1098   1426    767    -92     40   -302       C  
ATOM    481  C   ILE A 100       6.141  35.123  19.110  1.00  7.94           C  
ANISOU  481  C   ILE A 100     1203   1123    689    -88    -53   -422       C  
ATOM    482  O   ILE A 100       6.223  34.102  19.816  1.00  9.05           O  
ANISOU  482  O   ILE A 100     1446   1412    580     69     -7   -238       O  
ATOM    483  CB  ILE A 100       6.793  35.055  16.674  1.00 10.42           C  
ANISOU  483  CB  ILE A 100     1469   1718    770    -89     14   -303       C  
ATOM    484  CG1 ILE A 100       6.508  33.581  16.583  1.00 12.06           C  
ANISOU  484  CG1 ILE A 100     1861   1632   1090    139     10   -200       C  
ATOM    485  CG2 ILE A 100       7.837  35.474  15.615  1.00 13.29           C  
ANISOU  485  CG2 ILE A 100     1911   2385    752   -443    142     41       C  
ATOM    486  CD1 ILE A 100       5.966  33.028  15.240  1.00 11.91           C  
ANISOU  486  CD1 ILE A 100     1993   2042    489   -307    138   -459       C  
ATOM    487  N   TYR A 101       5.101  35.951  19.100  1.00  8.72           N  
ANISOU  487  N   TYR A 101     1285   1366    661    152   -126   -206       N  
ATOM    488  CA  TYR A 101       3.876  35.723  19.873  1.00  8.72           C  
ANISOU  488  CA  TYR A 101     1222   1535    555     82    162   -280       C  
ATOM    489  C   TYR A 101       2.711  36.014  18.936  1.00  7.98           C  
ANISOU  489  C   TYR A 101     1250   1426    355   -146    138   -120       C  
ATOM    490  O   TYR A 101       2.697  37.057  18.217  1.00  9.26           O  
ANISOU  490  O   TYR A 101     1479   1420    619    -52     43   -137       O  
ATOM    491  CB  TYR A 101       3.800  36.668  21.104  1.00  9.75           C  
ANISOU  491  CB  TYR A 101     1429   1472    802    121     55   -350       C  
ATOM    492  CG  TYR A 101       4.948  36.466  22.083  1.00  8.88           C  
ANISOU  492  CG  TYR A 101     1384   1447    543     16    157   -411       C  
ATOM    493  CD1 TYR A 101       4.823  35.625  23.169  1.00  9.75           C  
ANISOU  493  CD1 TYR A 101     1265   1573    866   -317    271   -415       C  
ATOM    494  CD2 TYR A 101       6.152  37.126  21.918  1.00 10.35           C  
ANISOU  494  CD2 TYR A 101     1515   1636    781    -56    -11   -502       C  
ATOM    495  CE1 TYR A 101       5.856  35.434  24.057  1.00 10.26           C  
ANISOU  495  CE1 TYR A 101     1394   1728    772   -213     28   -538       C  
ATOM    496  CE2 TYR A 101       7.189  36.962  22.844  1.00 10.38           C  
ANISOU  496  CE2 TYR A 101     1459   1640    843   -220    113   -406       C  
ATOM    497  CZ  TYR A 101       7.032  36.084  23.905  1.00 10.04           C  
ANISOU  497  CZ  TYR A 101     1728   1602    484    -68   -310   -457       C  
ATOM    498  OH  TYR A 101       8.014  35.917  24.879  1.00 11.68           O  
ANISOU  498  OH  TYR A 101     1859   2068    509   -113   -319   -567       O  
ATOM    499  N   MET A 102       1.767  35.103  18.897  1.00  8.59           N  
ANISOU  499  N   MET A 102     1260   1316    684    -12    -43   -102       N  
ATOM    500  CA  MET A 102       0.634  35.221  18.007  1.00  8.33           C  
ANISOU  500  CA  MET A 102     1166   1469    528    117     12   -186       C  
ATOM    501  C   MET A 102      -0.520  35.994  18.650  1.00  9.62           C  
ANISOU  501  C   MET A 102     1307   1476    873     39    161   -127       C  
ATOM    502  O   MET A 102      -0.737  35.912  19.885  1.00  9.27           O  
ANISOU  502  O   MET A 102     1428   1538    556     65    -11   -290       O  
ATOM    503  CB  MET A 102       0.125  33.824  17.648  1.00  8.71           C  
ANISOU  503  CB  MET A 102     1317   1593    399   -158    137   -219       C  
ATOM    504  CG  MET A 102       1.188  32.871  17.105  1.00  8.83           C  
ANISOU  504  CG  MET A 102     1349   1339    664   -129    213   -198       C  
ATOM    505  SD  MET A 102       2.168  33.525  15.728  1.00  9.96           S  
ANISOU  505  SD  MET A 102     1453   1690    638     38     30   -295       S  
ATOM    506  CE  MET A 102       0.894  33.691  14.472  1.00 10.92           C  
ANISOU  506  CE  MET A 102     1496   2066    586      5    -67   -380       C  
ATOM    507  N   VAL A 103      -1.303  36.652  17.803  1.00  9.30           N  
ANISOU  507  N   VAL A 103     1302   1442    788    160     -2   -229       N  
ATOM    508  CA  VAL A 103      -2.602  37.225  18.154  1.00 10.33           C  
ANISOU  508  CA  VAL A 103     1502   1556    866    129      5   -159       C  
ATOM    509  C   VAL A 103      -3.536  36.884  16.964  1.00 10.12           C  
ANISOU  509  C   VAL A 103     1234   1792    816    171     22   -166       C  
ATOM    510  O   VAL A 103      -3.053  36.853  15.827  1.00 10.92           O  
ANISOU  510  O   VAL A 103     1578   1819    749    187     63   -194       O  
ATOM    511  CB  VAL A 103      -2.571  38.743  18.352  1.00 10.27           C  
ANISOU  511  CB  VAL A 103     1686   1524    692    113     -4   -215       C  
ATOM    512  CG1 VAL A 103      -3.949  39.285  18.816  1.00 11.74           C  
ANISOU  512  CG1 VAL A 103     1765   1847    847    351    487   -296       C  
ATOM    513  CG2 VAL A 103      -1.456  39.176  19.337  1.00 11.65           C  
ANISOU  513  CG2 VAL A 103     1771   1631   1022     33   -227   -416       C  
ATOM    514  N   VAL A 104      -4.795  36.536  17.221  1.00 10.22           N  
ANISOU  514  N   VAL A 104     1312   1721    851     84    -50   -292       N  
ATOM    515  CA  VAL A 104      -5.729  36.192  16.148  1.00 10.08           C  
ANISOU  515  CA  VAL A 104     1246   1790    793      4    -23   -150       C  
ATOM    516  C   VAL A 104      -7.035  36.904  16.355  1.00 10.11           C  
ANISOU  516  C   VAL A 104     1170   1963    707     30     85     -7       C  
ATOM    517  O   VAL A 104      -7.586  36.913  17.469  1.00 11.03           O  
ANISOU  517  O   VAL A 104     1308   2128    753    155    147   -260       O  
ATOM    518  CB  VAL A 104      -5.956  34.662  15.989  1.00 10.68           C  
ANISOU  518  CB  VAL A 104     1555   1691    812   -211    180   -210       C  
ATOM    519  CG1 VAL A 104      -6.847  34.330  14.791  1.00 11.77           C  
ANISOU  519  CG1 VAL A 104     1766   2026    677   -203   -375   -347       C  
ATOM    520  CG2 VAL A 104      -4.607  33.880  15.982  1.00 11.71           C  
ANISOU  520  CG2 VAL A 104     1436   2032    980    476    170   -302       C  
ATOM    521  N   VAL A 105      -7.577  37.459  15.268  1.00 10.77           N  
ANISOU  521  N   VAL A 105     1377   1972    741    247    -71   -126       N  
ATOM    522  CA  VAL A 105      -8.904  38.042  15.270  1.00 12.44           C  
ANISOU  522  CA  VAL A 105     1517   1975   1233    109   -133   -154       C  
ATOM    523  C   VAL A 105      -9.658  37.519  14.051  1.00 12.07           C  
ANISOU  523  C   VAL A 105     1462   1893   1231    216    -77   -388       C  
ATOM    524  O   VAL A 105      -9.033  37.025  13.111  1.00 12.34           O  
ANISOU  524  O   VAL A 105     1524   2122   1041    338   -111   -447       O  
ATOM    525  CB  VAL A 105      -8.874  39.599  15.285  1.00 11.20           C  
ANISOU  525  CB  VAL A 105     1308   1896   1050    153   -116   -139       C  
ATOM    526  CG1 VAL A 105      -8.048  40.108  16.486  1.00 11.75           C  
ANISOU  526  CG1 VAL A 105     1448   2268    748     73   -257   -398       C  
ATOM    527  CG2 VAL A 105      -8.376  40.188  13.974  1.00 11.34           C  
ANISOU  527  CG2 VAL A 105     1765   1893    650     71     29    -87       C  
ATOM    528  N   ASP A 106     -10.990  37.585  14.080  1.00 12.96           N  
ANISOU  528  N   ASP A 106     1401   2530    991     97   -218   -484       N  
ATOM    529  CA  ASP A 106     -11.751  37.267  12.892  1.00 14.98           C  
ANISOU  529  CA  ASP A 106     1638   2643   1409     97   -169   -657       C  
ATOM    530  C   ASP A 106     -11.869  38.491  11.968  1.00 14.26           C  
ANISOU  530  C   ASP A 106     1641   2522   1254    137    -59   -611       C  
ATOM    531  O   ASP A 106     -11.395  39.571  12.291  1.00 15.22           O  
ANISOU  531  O   ASP A 106     1703   2919   1159    132   -190    -60       O  
ATOM    532  CB  ASP A 106     -13.076  36.541  13.206  1.00 16.01           C  
ANISOU  532  CB  ASP A 106     1843   2787   1450    183   -246   -878       C  
ATOM    533  CG  ASP A 106     -14.201  37.450  13.679  1.00 14.74           C  
ANISOU  533  CG  ASP A 106     1771   2408   1418     87   -194   -331       C  
ATOM    534  OD1 ASP A 106     -14.107  38.686  13.576  1.00 15.79           O  
ANISOU  534  OD1 ASP A 106     1784   2663   1553    343   -102   -394       O  
ATOM    535  OD2 ASP A 106     -15.230  36.844  14.082  1.00 18.73           O  
ANISOU  535  OD2 ASP A 106     1800   3037   2277    215    109   -393       O  
ATOM    536  N   LYS A 107     -12.472  38.314  10.788  1.00 16.61           N  
ANISOU  536  N   LYS A 107     1733   3236   1339    260   -307   -650       N  
ATOM    537  CA  LYS A 107     -12.475  39.404   9.786  1.00 19.59           C  
ANISOU  537  CA  LYS A 107     2468   3341   1632     86   -474   -353       C  
ATOM    538  C   LYS A 107     -13.296  40.618  10.226  1.00 18.41           C  
ANISOU  538  C   LYS A 107     2138   3041   1813    153   -586    -71       C  
ATOM    539  O   LYS A 107     -13.145  41.716   9.691  1.00 22.50           O  
ANISOU  539  O   LYS A 107     2689   3710   2148    291   -777    347       O  
ATOM    540  CB  LYS A 107     -13.020  38.926   8.424  1.00 21.76           C  
ANISOU  540  CB  LYS A 107     2886   3677   1705    439   -331   -556       C  
ATOM    541  CG  LYS A 107     -14.495  38.475   8.435  1.00 24.35           C  
ANISOU  541  CG  LYS A 107     2797   3689   2765    303   -801   -379       C  
ATOM    542  CD  LYS A 107     -14.937  37.809   7.111  1.00 30.95           C  
ANISOU  542  CD  LYS A 107     3618   5154   2985   -140   -597   -920       C  
ATOM    543  N   ASN A 108     -14.178  40.404  11.195  1.00 17.40           N  
ANISOU  543  N   ASN A 108     2107   2915   1587    355   -455   -208       N  
ATOM    544  CA  ASN A 108     -14.963  41.464  11.821  1.00 18.28           C  
ANISOU  544  CA  ASN A 108     2480   2761   1702    368   -430   -340       C  
ATOM    545  C   ASN A 108     -14.354  42.082  13.063  1.00 19.24           C  
ANISOU  545  C   ASN A 108     2452   2866   1992    544   -482   -323       C  
ATOM    546  O   ASN A 108     -14.919  43.033  13.638  1.00 21.83           O  
ANISOU  546  O   ASN A 108     2669   3019   2606    683   -390   -506       O  
ATOM    547  CB  ASN A 108     -16.335  40.917  12.146  1.00 18.98           C  
ANISOU  547  CB  ASN A 108     2246   3208   1757    345   -677   -627       C  
ATOM    548  CG  ASN A 108     -17.056  40.426  10.917  1.00 20.62           C  
ANISOU  548  CG  ASN A 108     2194   3941   1698    410      0   -452       C  
ATOM    549  OD1 ASN A 108     -16.998  41.062   9.881  1.00 28.13           O  
ANISOU  549  OD1 ASN A 108     2625   5298   2763    523   -597    300       O  
ATOM    550  ND2 ASN A 108     -17.664  39.276  11.010  1.00 25.70           N  
ANISOU  550  ND2 ASN A 108     2449   3995   3318    343   -472   -655       N  
ATOM    551  N   GLY A 109     -13.175  41.596  13.449  1.00 17.07           N  
ANISOU  551  N   GLY A 109     2032   2603   1850    382   -418   -325       N  
ATOM    552  CA  GLY A 109     -12.476  42.161  14.601  1.00 14.89           C  
ANISOU  552  CA  GLY A 109     2042   2483   1131    170    -61   -407       C  
ATOM    553  C   GLY A 109     -12.801  41.546  15.953  1.00 14.86           C  
ANISOU  553  C   GLY A 109     1691   2490   1463    137     40   -316       C  
ATOM    554  O   GLY A 109     -12.372  42.093  16.970  1.00 15.99           O  
ANISOU  554  O   GLY A 109     1959   2579   1535    205   -108   -431       O  
ATOM    555  N   VAL A 110     -13.484  40.409  15.969  1.00 13.91           N  
ANISOU  555  N   VAL A 110     1403   2483   1397    392   -284   -142       N  
ATOM    556  CA  VAL A 110     -13.679  39.629  17.206  1.00 15.00           C  
ANISOU  556  CA  VAL A 110     1611   2588   1497    212    157   -311       C  
ATOM    557  C   VAL A 110     -12.374  38.955  17.572  1.00 13.48           C  
ANISOU  557  C   VAL A 110     1555   2353   1213    354    141   -434       C  
ATOM    558  O   VAL A 110     -11.733  38.324  16.741  1.00 13.73           O  
ANISOU  558  O   VAL A 110     1673   2454   1086    415    -38   -242       O  
ATOM    559  CB  VAL A 110     -14.801  38.587  17.110  1.00 14.66           C  
ANISOU  559  CB  VAL A 110     1604   2745   1220    190    311   -568       C  
ATOM    560  CG1 VAL A 110     -14.944  37.811  18.440  1.00 15.13           C  
ANISOU  560  CG1 VAL A 110     1804   2811   1131     34    530   -210       C  
ATOM    561  CG2 VAL A 110     -16.147  39.268  16.710  1.00 17.64           C  
ANISOU  561  CG2 VAL A 110     1301   3651   1751    507   -353   -347       C  
ATOM    562  N   VAL A 111     -11.895  39.194  18.788  1.00 12.94           N  
ANISOU  562  N   VAL A 111     1525   2389   1000    345    198   -569       N  
ATOM    563  CA  VAL A 111     -10.638  38.598  19.231  1.00 12.66           C  
ANISOU  563  CA  VAL A 111     1481   2193   1135     74    122   -477       C  
ATOM    564  C   VAL A 111     -10.811  37.095  19.460  1.00 12.51           C  
ANISOU  564  C   VAL A 111     1530   2157   1064     42     90   -538       C  
ATOM    565  O   VAL A 111     -11.712  36.669  20.190  1.00 13.84           O  
ANISOU  565  O   VAL A 111     1541   2477   1239     25    451   -396       O  
ATOM    566  CB  VAL A 111     -10.065  39.306  20.518  1.00 12.90           C  
ANISOU  566  CB  VAL A 111     1705   2113   1080    148     72   -461       C  
ATOM    567  CG1 VAL A 111      -8.735  38.669  20.913  1.00 12.35           C  
ANISOU  567  CG1 VAL A 111     1742   1813   1137    467    -77   -356       C  
ATOM    568  CG2 VAL A 111      -9.919  40.808  20.263  1.00 14.51           C  
ANISOU  568  CG2 VAL A 111     2205   2084   1223    121   -128    -78       C  
ATOM    569  N   LEU A 112     -10.022  36.287  18.744  1.00 11.62           N  
ANISOU  569  N   LEU A 112     1477   2156    780    161    260   -400       N  
ATOM    570  CA  LEU A 112     -10.038  34.862  18.912  1.00 11.30           C  
ANISOU  570  CA  LEU A 112     1403   2041    846     91    506   -421       C  
ATOM    571  C   LEU A 112      -8.935  34.290  19.784  1.00 11.94           C  
ANISOU  571  C   LEU A 112     1567   1828   1138   -111    177   -498       C  
ATOM    572  O   LEU A 112      -9.126  33.237  20.379  1.00 12.42           O  
ANISOU  572  O   LEU A 112     1594   2113   1012   -262    299   -428       O  
ATOM    573  CB  LEU A 112      -9.981  34.169  17.569  1.00 12.09           C  
ANISOU  573  CB  LEU A 112     1519   2160    914    103    187   -292       C  
ATOM    574  CG  LEU A 112     -11.050  34.546  16.529  1.00 11.98           C  
ANISOU  574  CG  LEU A 112     1615   2076    858   -170   -385   -315       C  
ATOM    575  CD1 LEU A 112     -10.840  33.746  15.262  1.00 14.71           C  
ANISOU  575  CD1 LEU A 112     1763   2935    888    -58   -409   -864       C  
ATOM    576  CD2 LEU A 112     -12.446  34.279  17.083  1.00 16.21           C  
ANISOU  576  CD2 LEU A 112     1161   2956   2041     70    -52   -456       C  
ATOM    577  N   PHE A 113      -7.816  35.004  19.898  1.00 11.59           N  
ANISOU  577  N   PHE A 113     1587   1836    980    107    198   -501       N  
ATOM    578  CA  PHE A 113      -6.647  34.487  20.638  1.00 10.30           C  
ANISOU  578  CA  PHE A 113     1389   1698    825    101    163   -230       C  
ATOM    579  C   PHE A 113      -5.773  35.652  21.022  1.00 10.93           C  
ANISOU  579  C   PHE A 113     1483   1686    983    -13    281   -332       C  
ATOM    580  O   PHE A 113      -5.298  36.417  20.155  1.00 10.62           O  
ANISOU  580  O   PHE A 113     1517   1747    769     -5    204   -300       O  
ATOM    581  CB  PHE A 113      -5.861  33.513  19.774  1.00 10.30           C  
ANISOU  581  CB  PHE A 113     1587   1468    855     18    136   -157       C  
ATOM    582  CG  PHE A 113      -4.581  32.997  20.435  1.00  9.27           C  
ANISOU  582  CG  PHE A 113     1599   1364    559     34     22   -462       C  
ATOM    583  CD1 PHE A 113      -4.583  31.915  21.278  1.00 11.23           C  
ANISOU  583  CD1 PHE A 113     1678   1654    933      5    304   -342       C  
ATOM    584  CD2 PHE A 113      -3.372  33.558  20.135  1.00  9.87           C  
ANISOU  584  CD2 PHE A 113     1352   1772    623    -26     37   -330       C  
ATOM    585  CE1 PHE A 113      -3.423  31.472  21.861  1.00 12.59           C  
ANISOU  585  CE1 PHE A 113     1842   1936   1003     96    225   -145       C  
ATOM    586  CE2 PHE A 113      -2.205  33.139  20.737  1.00 10.51           C  
ANISOU  586  CE2 PHE A 113     1492   1543    957     33     24   -213       C  
ATOM    587  CZ  PHE A 113      -2.229  32.058  21.575  1.00 10.04           C  
ANISOU  587  CZ  PHE A 113     1672   1690    450    -67    149   -517       C  
ATOM    588  N   ASP A 114      -5.556  35.817  22.334  1.00 11.35           N  
ANISOU  588  N   ASP A 114     1579   1895    836      8    222   -254       N  
ATOM    589  CA  ASP A 114      -4.622  36.806  22.872  1.00 11.36           C  
ANISOU  589  CA  ASP A 114     1700   1723    893    182    168   -157       C  
ATOM    590  C   ASP A 114      -4.395  36.539  24.359  1.00 10.37           C  
ANISOU  590  C   ASP A 114     1511   1582    846    263    166   -165       C  
ATOM    591  O   ASP A 114      -5.055  37.150  25.190  1.00 10.67           O  
ANISOU  591  O   ASP A 114     1632   1815    604    233    127   -301       O  
ATOM    592  CB  ASP A 114      -5.114  38.242  22.661  1.00 11.97           C  
ANISOU  592  CB  ASP A 114     1737   1877    934    -35   -125   -441       C  
ATOM    593  CG  ASP A 114      -4.078  39.280  23.069  1.00 11.65           C  
ANISOU  593  CG  ASP A 114     1536   1702   1187    127    211   -423       C  
ATOM    594  OD1 ASP A 114      -2.948  38.890  23.442  1.00 10.96           O  
ANISOU  594  OD1 ASP A 114     1594   1877    691    164    163   -379       O  
ATOM    595  OD2 ASP A 114      -4.356  40.495  22.943  1.00 12.29           O  
ANISOU  595  OD2 ASP A 114     1775   1652   1243    196    210   -277       O  
ATOM    596  N   PRO A 115      -3.406  35.709  24.683  1.00 11.08           N  
ANISOU  596  N   PRO A 115     1676   1750    780    163    286   -212       N  
ATOM    597  CA  PRO A 115      -3.196  35.380  26.096  1.00 12.14           C  
ANISOU  597  CA  PRO A 115     1995   1676    940     53    -96   -101       C  
ATOM    598  C   PRO A 115      -2.770  36.544  26.979  1.00 11.49           C  
ANISOU  598  C   PRO A 115     1803   1588    975      6   -142   -371       C  
ATOM    599  O   PRO A 115      -2.818  36.429  28.209  1.00 13.47           O  
ANISOU  599  O   PRO A 115     2235   2118    762     65      0   -351       O  
ATOM    600  CB  PRO A 115      -2.073  34.329  26.053  1.00 13.03           C  
ANISOU  600  CB  PRO A 115     2254   1563   1134    169     95   -459       C  
ATOM    601  CG  PRO A 115      -2.269  33.649  24.673  1.00 11.91           C  
ANISOU  601  CG  PRO A 115     1854   1825    845    304   -155   -380       C  
ATOM    602  CD  PRO A 115      -2.675  34.800  23.785  1.00  9.59           C  
ANISOU  602  CD  PRO A 115     1657   1592    394    181    270   -223       C  
ATOM    603  N   VAL A 116      -2.268  37.617  26.382  1.00 10.81           N  
ANISOU  603  N   VAL A 116     1769   1549    789    -61    126   -339       N  
ATOM    604  CA  VAL A 116      -1.930  38.822  27.146  1.00 11.89           C  
ANISOU  604  CA  VAL A 116     1895   1672    951     78   -151   -296       C  
ATOM    605  C   VAL A 116      -3.184  39.526  27.658  1.00 12.74           C  
ANISOU  605  C   VAL A 116     1715   1878   1245     35    180   -474       C  
ATOM    606  O   VAL A 116      -3.151  40.167  28.718  1.00 14.13           O  
ANISOU  606  O   VAL A 116     2145   2270    952    112      8   -569       O  
ATOM    607  CB  VAL A 116      -1.017  39.815  26.345  1.00 10.44           C  
ANISOU  607  CB  VAL A 116     1789   1668    507    -91     47   -360       C  
ATOM    608  CG1 VAL A 116      -0.655  41.063  27.152  1.00 12.76           C  
ANISOU  608  CG1 VAL A 116     2065   1863    920    -32   -204   -591       C  
ATOM    609  CG2 VAL A 116       0.248  39.083  25.910  1.00 12.94           C  
ANISOU  609  CG2 VAL A 116     1571   2022   1321    197    398   -675       C  
ATOM    610  N   ASN A 117      -4.274  39.424  26.888  1.00 11.28           N  
ANISOU  610  N   ASN A 117     1679   1739    866    191    167   -442       N  
ATOM    611  CA  ASN A 117      -5.531  40.100  27.169  1.00 12.50           C  
ANISOU  611  CA  ASN A 117     1803   1950    994     62    171   -273       C  
ATOM    612  C   ASN A 117      -6.710  39.115  27.124  1.00 11.84           C  
ANISOU  612  C   ASN A 117     1639   1875    982    -62    370   -311       C  
ATOM    613  O   ASN A 117      -7.596  39.186  26.267  1.00 13.01           O  
ANISOU  613  O   ASN A 117     1768   2228    946     41    144   -494       O  
ATOM    614  CB  ASN A 117      -5.734  41.268  26.203  1.00 12.27           C  
ANISOU  614  CB  ASN A 117     1788   2112    761    147    428   -605       C  
ATOM    615  CG  ASN A 117      -4.596  42.262  26.262  1.00 12.68           C  
ANISOU  615  CG  ASN A 117     1780   1309   1727     29    272   -175       C  
ATOM    616  OD1 ASN A 117      -4.417  42.959  27.274  1.00 15.22           O  
ANISOU  616  OD1 ASN A 117     2384   2110   1287    -36     62   -758       O  
ATOM    617  ND2 ASN A 117      -3.775  42.308  25.208  1.00 11.73           N  
ANISOU  617  ND2 ASN A 117     1785   1783    890     80    216   -276       N  
ATOM    618  N   PRO A 118      -6.683  38.112  28.003  1.00 12.70           N  
ANISOU  618  N   PRO A 118     1848   1980    997    -81    175   -244       N  
ATOM    619  CA  PRO A 118      -7.612  36.991  27.886  1.00 13.99           C  
ANISOU  619  CA  PRO A 118     1899   2263   1151    -85    301   -367       C  
ATOM    620  C   PRO A 118      -9.092  37.365  27.948  1.00 14.20           C  
ANISOU  620  C   PRO A 118     2011   2295   1086   -138    524   -299       C  
ATOM    621  O   PRO A 118      -9.935  36.680  27.350  1.00 16.64           O  
ANISOU  621  O   PRO A 118     2084   2702   1534   -423    363   -508       O  
ATOM    622  CB  PRO A 118      -7.241  36.096  29.085  1.00 15.11           C  
ANISOU  622  CB  PRO A 118     2212   2428   1099   -200    248     -9       C  
ATOM    623  CG  PRO A 118      -6.561  36.990  30.013  1.00 15.99           C  
ANISOU  623  CG  PRO A 118     2332   2306   1438   -263    232   -209       C  
ATOM    624  CD  PRO A 118      -5.790  37.956  29.158  1.00 14.14           C  
ANISOU  624  CD  PRO A 118     1821   2271   1280     26    -17   -540       C  
ATOM    625  N   LYS A 119      -9.414  38.449  28.631  1.00 15.87           N  
ANISOU  625  N   LYS A 119     1967   2574   1486    143    113   -391       N  
ATOM    626  CA  LYS A 119     -10.807  38.852  28.759  1.00 17.51           C  
ANISOU  626  CA  LYS A 119     2037   3078   1537    274    337   -527       C  
ATOM    627  C   LYS A 119     -11.370  39.422  27.454  1.00 15.61           C  
ANISOU  627  C   LYS A 119     1548   2835   1545    228    503   -324       C  
ATOM    628  O   LYS A 119     -12.583  39.535  27.295  1.00 17.87           O  
ANISOU  628  O   LYS A 119     1835   3280   1673    187    401   -217       O  
ATOM    629  CB  LYS A 119     -10.964  39.872  29.914  1.00 19.75           C  
ANISOU  629  CB  LYS A 119     2283   3573   1645    406    361   -605       C  
ATOM    630  CG  LYS A 119     -10.602  39.343  31.318  1.00 23.83           C  
ANISOU  630  CG  LYS A 119     2864   4359   1830    326    387   -345       C  
ATOM    631  CD  LYS A 119     -10.739  40.457  32.442  1.00 29.73           C  
ANISOU  631  CD  LYS A 119     3728   4888   2677    924    833  -1222       C  
ATOM    632  N   THR A 120     -10.504  39.784  26.506  1.00 13.71           N  
ANISOU  632  N   THR A 120     1751   2546    912     69    387   -404       N  
ATOM    633  CA  THR A 120     -10.976  40.269  25.227  1.00 13.70           C  
ANISOU  633  CA  THR A 120     1829   2031   1345    276    255   -573       C  
ATOM    634  C   THR A 120     -11.419  39.151  24.266  1.00 14.86           C  
ANISOU  634  C   THR A 120     1779   2192   1673    143    272   -357       C  
ATOM    635  O   THR A 120     -12.084  39.448  23.270  1.00 15.44           O  
ANISOU  635  O   THR A 120     1700   2679   1486    322    471   -396       O  
ATOM    636  CB  THR A 120      -9.906  41.160  24.507  1.00 13.99           C  
ANISOU  636  CB  THR A 120     2010   1919   1387    227    590   -439       C  
ATOM    637  OG1 THR A 120      -8.800  40.368  24.079  1.00 13.44           O  
ANISOU  637  OG1 THR A 120     1962   2107   1036     41    475   -563       O  
ATOM    638  CG2 THR A 120      -9.384  42.297  25.393  1.00 15.15           C  
ANISOU  638  CG2 THR A 120     2068   1950   1738     86    405   -735       C  
ATOM    639  N   VAL A 121     -11.064  37.901  24.560  1.00 14.14           N  
ANISOU  639  N   VAL A 121     1735   2278   1357     63    142   -389       N  
ATOM    640  CA  VAL A 121     -11.367  36.785  23.658  1.00 13.81           C  
ANISOU  640  CA  VAL A 121     1662   2176   1408     63    416   -263       C  
ATOM    641  C   VAL A 121     -12.875  36.593  23.614  1.00 15.14           C  
ANISOU  641  C   VAL A 121     1831   2766   1154    -49    215   -126       C  
ATOM    642  O   VAL A 121     -13.550  36.569  24.665  1.00 17.40           O  
ANISOU  642  O   VAL A 121     2284   2925   1399   -167    338   -441       O  
ATOM    643  CB  VAL A 121     -10.618  35.483  24.076  1.00 15.51           C  
ANISOU  643  CB  VAL A 121     1959   2493   1439    112    359   -275       C  
ATOM    644  CG1 VAL A 121     -11.086  34.230  23.263  1.00 15.65           C  
ANISOU  644  CG1 VAL A 121     2636   2696    614   -239    168   -608       C  
ATOM    645  CG2 VAL A 121      -9.094  35.677  23.981  1.00 17.29           C  
ANISOU  645  CG2 VAL A 121     1629   2905   2033    298    376   -135       C  
ATOM    646  N   GLY A 122     -13.397  36.539  22.395  1.00 14.82           N  
ANISOU  646  N   GLY A 122     1517   2723   1391      5    312   -377       N  
ATOM    647  CA  GLY A 122     -14.789  36.352  22.164  1.00 15.22           C  
ANISOU  647  CA  GLY A 122     1692   2762   1327      0    392   -417       C  
ATOM    648  C   GLY A 122     -15.592  37.639  22.019  1.00 16.79           C  
ANISOU  648  C   GLY A 122     1786   2816   1776    162    444   -355       C  
ATOM    649  O   GLY A 122     -16.816  37.596  21.746  1.00 20.25           O  
ANISOU  649  O   GLY A 122     1832   3583   2278    147    194   -584       O  
ATOM    650  N   GLN A 123     -14.935  38.755  22.314  1.00 16.51           N  
ANISOU  650  N   GLN A 123     1789   2710   1771    131    494   -306       N  
ATOM    651  CA  GLN A 123     -15.506  40.072  22.191  1.00 18.50           C  
ANISOU  651  CA  GLN A 123     2228   2912   1887    244    326   -216       C  
ATOM    652  C   GLN A 123     -15.009  40.831  20.965  1.00 16.08           C  
ANISOU  652  C   GLN A 123     1848   2636   1624    326     63   -428       C  
ATOM    653  O   GLN A 123     -13.900  40.596  20.486  1.00 15.85           O  
ANISOU  653  O   GLN A 123     1724   3069   1226    548    309   -399       O  
ATOM    654  CB  GLN A 123     -15.138  40.909  23.433  1.00 20.99           C  
ANISOU  654  CB  GLN A 123     3196   2883   1894    438    569   -463       C  
ATOM    655  CG  GLN A 123     -15.344  40.226  24.812  1.00 25.80           C  
ANISOU  655  CG  GLN A 123     3537   3740   2526    337    860   -205       C  
ATOM    656  CD  GLN A 123     -14.922  41.154  25.991  1.00 29.54           C  
ANISOU  656  CD  GLN A 123     4081   4221   2922    203   1148   -425       C  
ATOM    657  OE1 GLN A 123     -14.040  42.039  25.846  1.00 35.06           O  
ANISOU  657  OE1 GLN A 123     4251   4934   4135    500    489    176       O  
ATOM    658  NE2 GLN A 123     -15.547  40.945  27.156  1.00 34.15           N  
ANISOU  658  NE2 GLN A 123     4550   5322   3102    384   1559   -139       N  
ATOM    659  N   SER A 124     -15.801  41.773  20.478  1.00 17.93           N  
ANISOU  659  N   SER A 124     1846   2817   2147    373    104   -465       N  
ATOM    660  CA  SER A 124     -15.290  42.701  19.495  1.00 17.41           C  
ANISOU  660  CA  SER A 124     1863   2701   2049    405    114   -316       C  
ATOM    661  C   SER A 124     -14.086  43.448  20.047  1.00 15.26           C  
ANISOU  661  C   SER A 124     1753   2396   1649    363   -173   -426       C  
ATOM    662  O   SER A 124     -14.094  43.963  21.188  1.00 18.98           O  
ANISOU  662  O   SER A 124     2213   2998   1997    388    -83   -710       O  
ATOM    663  CB  SER A 124     -16.325  43.737  19.094  1.00 17.72           C  
ANISOU  663  CB  SER A 124     1960   2771   2001    391     13   -481       C  
ATOM    664  OG  SER A 124     -15.770  44.665  18.187  1.00 19.16           O  
ANISOU  664  OG  SER A 124     2028   3007   2245    421    -37   -320       O  
ATOM    665  N   GLY A 125     -13.029  43.525  19.245  1.00 14.01           N  
ANISOU  665  N   GLY A 125     1879   2463    980    402     82   -467       N  
ATOM    666  CA  GLY A 125     -11.867  44.324  19.568  1.00 14.93           C  
ANISOU  666  CA  GLY A 125     2086   2310   1273    374    281   -514       C  
ATOM    667  C   GLY A 125     -11.737  45.622  18.779  1.00 15.05           C  
ANISOU  667  C   GLY A 125     1933   2231   1553    435      8   -320       C  
ATOM    668  O   GLY A 125     -10.714  46.302  18.844  1.00 15.41           O  
ANISOU  668  O   GLY A 125     1873   2627   1355    364   -104   -654       O  
ATOM    669  N   LEU A 126     -12.817  46.051  18.115  1.00 16.09           N  
ANISOU  669  N   LEU A 126     1990   2607   1517    599   -199   -343       N  
ATOM    670  CA  LEU A 126     -12.725  47.242  17.257  1.00 16.10           C  
ANISOU  670  CA  LEU A 126     2100   2523   1492    573    -13   -398       C  
ATOM    671  C   LEU A 126     -12.431  48.528  18.032  1.00 18.57           C  
ANISOU  671  C   LEU A 126     2476   2692   1887    464   -146   -230       C  
ATOM    672  O   LEU A 126     -11.846  49.454  17.499  1.00 20.21           O  
ANISOU  672  O   LEU A 126     3068   3009   1602    336     88   -145       O  
ATOM    673  CB  LEU A 126     -13.992  47.421  16.424  1.00 16.50           C  
ANISOU  673  CB  LEU A 126     2096   2624   1550    672    -13   -396       C  
ATOM    674  CG  LEU A 126     -14.205  46.277  15.444  1.00 16.90           C  
ANISOU  674  CG  LEU A 126     2125   2737   1558    660   -327    -72       C  
ATOM    675  CD1 LEU A 126     -15.588  46.480  14.780  1.00 21.58           C  
ANISOU  675  CD1 LEU A 126     2294   3592   2313    509   -806   -225       C  
ATOM    676  CD2 LEU A 126     -13.070  46.241  14.389  1.00 20.53           C  
ANISOU  676  CD2 LEU A 126     2669   3222   1907    471    408   -515       C  
ATOM    677  N   ASP A 127     -12.823  48.570  19.303  1.00 17.29           N  
ANISOU  677  N   ASP A 127     2160   2574   1835    666   -126   -320       N  
ATOM    678  CA  ASP A 127     -12.569  49.748  20.144  1.00 17.30           C  
ANISOU  678  CA  ASP A 127     2080   2650   1841    556     72   -391       C  
ATOM    679  C   ASP A 127     -11.466  49.505  21.162  1.00 17.36           C  
ANISOU  679  C   ASP A 127     2143   2365   2085    547    -27   -457       C  
ATOM    680  O   ASP A 127     -11.186  50.396  21.946  1.00 18.85           O  
ANISOU  680  O   ASP A 127     2415   2820   1926    699   -327   -957       O  
ATOM    681  CB  ASP A 127     -13.855  50.186  20.845  1.00 18.68           C  
ANISOU  681  CB  ASP A 127     2300   2737   2058    728      7   -224       C  
ATOM    682  CG  ASP A 127     -14.912  50.695  19.859  1.00 22.25           C  
ANISOU  682  CG  ASP A 127     2506   3606   2343   1181    195   -208       C  
ATOM    683  OD1 ASP A 127     -14.561  51.160  18.741  1.00 28.95           O  
ANISOU  683  OD1 ASP A 127     3217   4566   3216   1090   -124    550       O  
ATOM    684  OD2 ASP A 127     -16.094  50.585  20.188  1.00 29.74           O  
ANISOU  684  OD2 ASP A 127     2764   5378   3156   1055    487    291       O  
ATOM    685  N   ALA A 128     -10.750  48.389  21.046  1.00 15.55           N  
ANISOU  685  N   ALA A 128     2052   2536   1321    403   -241   -336       N  
ATOM    686  CA  ALA A 128      -9.612  48.122  21.910  1.00 15.46           C  
ANISOU  686  CA  ALA A 128     1993   2612   1266    525   -153   -369       C  
ATOM    687  C   ALA A 128      -8.461  49.043  21.593  1.00 15.04           C  
ANISOU  687  C   ALA A 128     2157   2233   1322    128   -191   -339       C  
ATOM    688  O   ALA A 128      -8.105  49.257  20.431  1.00 16.19           O  
ANISOU  688  O   ALA A 128     2344   2688   1118    161    -71   -493       O  
ATOM    689  CB  ALA A 128      -9.181  46.666  21.782  1.00 15.77           C  
ANISOU  689  CB  ALA A 128     2276   2205   1510    601   -404   -536       C  
ATOM    690  N   GLN A 129      -7.857  49.613  22.625  1.00 14.21           N  
ANISOU  690  N   GLN A 129     2017   2367   1013    363    -57   -310       N  
ATOM    691  CA  GLN A 129      -6.697  50.451  22.468  1.00 15.31           C  
ANISOU  691  CA  GLN A 129     1973   2361   1482    450    153   -356       C  
ATOM    692  C   GLN A 129      -5.558  49.951  23.315  1.00 13.35           C  
ANISOU  692  C   GLN A 129     1787   2092   1190    296   -180   -357       C  
ATOM    693  O   GLN A 129      -5.742  49.527  24.447  1.00 15.69           O  
ANISOU  693  O   GLN A 129     2168   2434   1358    232    -49     13       O  
ATOM    694  CB  GLN A 129      -6.947  51.899  22.840  1.00 18.14           C  
ANISOU  694  CB  GLN A 129     2219   2617   2056    521   -101   -184       C  
ATOM    695  CG  GLN A 129      -7.832  52.635  21.867  1.00 21.64           C  
ANISOU  695  CG  GLN A 129     2795   2716   2711    651     14   -168       C  
ATOM    696  CD  GLN A 129      -7.973  54.089  22.266  1.00 21.65           C  
ANISOU  696  CD  GLN A 129     3400   2690   2133    733    421   -391       C  
ATOM    697  OE1 GLN A 129      -6.989  54.809  22.448  1.00 29.23           O  
ANISOU  697  OE1 GLN A 129     3975   2778   4352    713    -12   -817       O  
ATOM    698  NE2 GLN A 129      -9.189  54.505  22.465  1.00 22.65           N  
ANISOU  698  NE2 GLN A 129     3190   3714   1700    903    622    185       N  
ATOM    699  N   SER A 130      -4.369  49.990  22.732  1.00 12.68           N  
ANISOU  699  N   SER A 130     1628   2167   1021    302     22   -589       N  
ATOM    700  CA  SER A 130      -3.144  49.816  23.474  1.00 12.11           C  
ANISOU  700  CA  SER A 130     1557   1844   1199    220      8   -420       C  
ATOM    701  C   SER A 130      -2.989  51.003  24.433  1.00 11.89           C  
ANISOU  701  C   SER A 130     1713   1721   1082    398     32   -603       C  
ATOM    702  O   SER A 130      -3.563  52.071  24.202  1.00 14.59           O  
ANISOU  702  O   SER A 130     2320   1984   1238    563   -147   -610       O  
ATOM    703  CB  SER A 130      -1.936  49.738  22.549  1.00 12.14           C  
ANISOU  703  CB  SER A 130     1779   1731   1101    365   -104   -660       C  
ATOM    704  OG  SER A 130      -1.797  50.941  21.822  1.00 13.80           O  
ANISOU  704  OG  SER A 130     2351   1959    932    451     25   -469       O  
ATOM    705  N   VAL A 131      -2.019  50.903  25.343  1.00 13.30           N  
ANISOU  705  N   VAL A 131     1925   1882   1246    441   -166   -704       N  
ATOM    706  CA  VAL A 131      -1.781  51.971  26.307  1.00 13.00           C  
ANISOU  706  CA  VAL A 131     2190   1662   1087    516   -372   -730       C  
ATOM    707  C   VAL A 131      -1.174  53.210  25.658  1.00 15.18           C  
ANISOU  707  C   VAL A 131     2523   1737   1505    419   -143   -806       C  
ATOM    708  O   VAL A 131      -1.251  54.270  26.231  1.00 17.76           O  
ANISOU  708  O   VAL A 131     3482   1596   1667    420   -163  -1075       O  
ATOM    709  CB  VAL A 131      -0.956  51.495  27.530  1.00 14.65           C  
ANISOU  709  CB  VAL A 131     2307   1885   1373    593   -237   -855       C  
ATOM    710  CG1 VAL A 131      -1.794  50.518  28.337  1.00 17.35           C  
ANISOU  710  CG1 VAL A 131     3163   1969   1458    455   -223   -371       C  
ATOM    711  CG2 VAL A 131       0.425  50.943  27.128  1.00 16.51           C  
ANISOU  711  CG2 VAL A 131     2446   2262   1562   1102   -788  -1016       C  
ATOM    712  N   ASP A 132      -0.560  53.076  24.483  1.00 14.13           N  
ANISOU  712  N   ASP A 132     2306   1812   1248    452    -11   -900       N  
ATOM    713  CA  ASP A 132      -0.130  54.206  23.699  1.00 15.26           C  
ANISOU  713  CA  ASP A 132     2557   1521   1721    358   -127   -748       C  
ATOM    714  C   ASP A 132      -1.169  54.689  22.671  1.00 15.59           C  
ANISOU  714  C   ASP A 132     2522   1650   1750    332    -65   -605       C  
ATOM    715  O   ASP A 132      -0.858  55.517  21.826  1.00 20.25           O  
ANISOU  715  O   ASP A 132     3539   2035   2120    310   -183   -250       O  
ATOM    716  CB  ASP A 132       1.241  53.981  23.053  1.00 17.12           C  
ANISOU  716  CB  ASP A 132     2761   1759   1982     22   -127   -602       C  
ATOM    717  CG  ASP A 132       1.301  52.793  22.071  1.00 15.02           C  
ANISOU  717  CG  ASP A 132     2553   1544   1609    157    267    -43       C  
ATOM    718  OD1 ASP A 132       0.620  51.788  22.274  1.00 14.22           O  
ANISOU  718  OD1 ASP A 132     2497   1745   1161    308    163   -579       O  
ATOM    719  OD2 ASP A 132       2.132  52.882  21.131  1.00 18.91           O  
ANISOU  719  OD2 ASP A 132     3183   2090   1912    250    487    -44       O  
ATOM    720  N   GLY A 133      -2.409  54.236  22.821  1.00 14.26           N  
ANISOU  720  N   GLY A 133     2537   1781   1100    424   -131   -528       N  
ATOM    721  CA  GLY A 133      -3.533  54.820  22.101  1.00 16.21           C  
ANISOU  721  CA  GLY A 133     2631   2046   1480    507   -293   -492       C  
ATOM    722  C   GLY A 133      -3.765  54.292  20.693  1.00 16.26           C  
ANISOU  722  C   GLY A 133     2782   1952   1441    682   -187   -377       C  
ATOM    723  O   GLY A 133      -4.462  54.912  19.903  1.00 20.57           O  
ANISOU  723  O   GLY A 133     3930   2594   1290   1250   -246   -506       O  
ATOM    724  N   VAL A 134      -3.231  53.119  20.390  1.00 15.24           N  
ANISOU  724  N   VAL A 134     2584   1758   1446    398   -159   -480       N  
ATOM    725  CA  VAL A 134      -3.407  52.510  19.058  1.00 13.75           C  
ANISOU  725  CA  VAL A 134     2473   1735   1016    409    -86   -204       C  
ATOM    726  C   VAL A 134      -4.545  51.525  19.057  1.00 12.87           C  
ANISOU  726  C   VAL A 134     2032   1742   1115    513   -191   -286       C  
ATOM    727  O   VAL A 134      -4.609  50.658  19.926  1.00 13.83           O  
ANISOU  727  O   VAL A 134     2431   1741   1081    429   -216   -350       O  
ATOM    728  CB  VAL A 134      -2.118  51.806  18.631  1.00 12.63           C  
ANISOU  728  CB  VAL A 134     2277   1592    927    347      0   -294       C  
ATOM    729  CG1 VAL A 134      -2.247  51.171  17.251  1.00 14.95           C  
ANISOU  729  CG1 VAL A 134     2754   1887   1037    188     72   -485       C  
ATOM    730  CG2 VAL A 134      -0.924  52.789  18.693  1.00 15.18           C  
ANISOU  730  CG2 VAL A 134     2152   1794   1821    156    164   -440       C  
ATOM    731  N   TYR A 135      -5.446  51.642  18.067  1.00 13.86           N  
ANISOU  731  N   TYR A 135     2299   1887   1079    559   -176   -233       N  
ATOM    732  CA  TYR A 135      -6.505  50.665  17.866  1.00 14.31           C  
ANISOU  732  CA  TYR A 135     2280   1855   1300    631   -189   -238       C  
ATOM    733  C   TYR A 135      -5.866  49.475  17.161  1.00 14.03           C  
ANISOU  733  C   TYR A 135     2078   1828   1423    638   -321   -414       C  
ATOM    734  O   TYR A 135      -5.933  49.339  15.946  1.00 14.95           O  
ANISOU  734  O   TYR A 135     2355   2029   1295    484   -117   -275       O  
ATOM    735  CB  TYR A 135      -7.656  51.243  17.041  1.00 16.53           C  
ANISOU  735  CB  TYR A 135     2652   1780   1848    658     16   -447       C  
ATOM    736  CG  TYR A 135      -8.430  52.309  17.790  1.00 17.29           C  
ANISOU  736  CG  TYR A 135     2370   2261   1938    560   -618   -426       C  
ATOM    737  CD1 TYR A 135      -9.467  51.970  18.632  1.00 19.99           C  
ANISOU  737  CD1 TYR A 135     2399   2665   2531    656     73   -920       C  
ATOM    738  CD2 TYR A 135      -8.142  53.643  17.626  1.00 21.27           C  
ANISOU  738  CD2 TYR A 135     3503   2209   2368   1031   -101   -208       C  
ATOM    739  CE1 TYR A 135     -10.222  52.932  19.293  1.00 23.55           C  
ANISOU  739  CE1 TYR A 135     2987   3024   2935    518    383   -610       C  
ATOM    740  CE2 TYR A 135      -8.902  54.640  18.303  1.00 24.76           C  
ANISOU  740  CE2 TYR A 135     3597   2477   3333   1111    -82   -300       C  
ATOM    741  CZ  TYR A 135      -9.904  54.260  19.163  1.00 22.35           C  
ANISOU  741  CZ  TYR A 135     2992   2400   3100   1399     82   -790       C  
ATOM    742  OH  TYR A 135     -10.674  55.233  19.829  1.00 29.31           O  
ANISOU  742  OH  TYR A 135     4170   3777   3188   1451   -339  -1177       O  
ATOM    743  N   TYR A 136      -5.287  48.580  17.947  1.00 12.85           N  
ANISOU  743  N   TYR A 136     1887   1771   1222    568      9   -165       N  
ATOM    744  CA  TYR A 136      -4.426  47.566  17.416  1.00 12.31           C  
ANISOU  744  CA  TYR A 136     1639   1723   1315    458    -16   -370       C  
ATOM    745  C   TYR A 136      -5.215  46.589  16.544  1.00 12.15           C  
ANISOU  745  C   TYR A 136     1676   1747   1192    435   -230   -163       C  
ATOM    746  O   TYR A 136      -4.672  46.065  15.559  1.00 13.19           O  
ANISOU  746  O   TYR A 136     1986   1767   1256    351    133   -226       O  
ATOM    747  CB  TYR A 136      -3.566  46.886  18.508  1.00 13.03           C  
ANISOU  747  CB  TYR A 136     1673   1774   1503    338    -36   -414       C  
ATOM    748  CG  TYR A 136      -4.322  46.172  19.608  1.00 12.40           C  
ANISOU  748  CG  TYR A 136     1727   1884   1098    324    -41     -5       C  
ATOM    749  CD1 TYR A 136      -4.634  44.814  19.498  1.00 13.26           C  
ANISOU  749  CD1 TYR A 136     1752   2040   1244    355   -230    157       C  
ATOM    750  CD2 TYR A 136      -4.684  46.841  20.776  1.00 14.97           C  
ANISOU  750  CD2 TYR A 136     2278   1559   1850    464    -81   -375       C  
ATOM    751  CE1 TYR A 136      -5.333  44.161  20.506  1.00 12.92           C  
ANISOU  751  CE1 TYR A 136     2016   1770   1122    100    423   -468       C  
ATOM    752  CE2 TYR A 136      -5.362  46.178  21.785  1.00 13.60           C  
ANISOU  752  CE2 TYR A 136     1853   1883   1429    148    -85   -574       C  
ATOM    753  CZ  TYR A 136      -5.681  44.872  21.659  1.00 13.13           C  
ANISOU  753  CZ  TYR A 136     1872   1920   1196     95      0   -249       C  
ATOM    754  OH  TYR A 136      -6.421  44.242  22.656  1.00 13.95           O  
ANISOU  754  OH  TYR A 136     2105   1994   1202    314     69   -125       O  
ATOM    755  N   VAL A 137      -6.443  46.242  16.933  1.00 12.09           N  
ANISOU  755  N   VAL A 137     1628   1972    991    258    -32   -356       N  
ATOM    756  CA  VAL A 137      -7.254  45.321  16.084  1.00 12.05           C  
ANISOU  756  CA  VAL A 137     1600   1828   1148    299   -176   -224       C  
ATOM    757  C   VAL A 137      -7.616  45.975  14.750  1.00 13.57           C  
ANISOU  757  C   VAL A 137     1972   1576   1607    499   -289   -489       C  
ATOM    758  O   VAL A 137      -7.591  45.318  13.692  1.00 12.69           O  
ANISOU  758  O   VAL A 137     2036   1784   1001    384   -235   -318       O  
ATOM    759  CB  VAL A 137      -8.511  44.765  16.849  1.00 12.91           C  
ANISOU  759  CB  VAL A 137     1817   1723   1363    549   -126   -144       C  
ATOM    760  CG1 VAL A 137      -9.442  43.944  15.943  1.00 13.85           C  
ANISOU  760  CG1 VAL A 137     2032   2248    979    203   -407   -624       C  
ATOM    761  CG2 VAL A 137      -8.049  43.979  18.045  1.00 12.76           C  
ANISOU  761  CG2 VAL A 137     2154   2237    458    401    -29   -315       C  
ATOM    762  N   ARG A 138      -8.002  47.250  14.790  1.00 13.66           N  
ANISOU  762  N   ARG A 138     2137   1763   1287    635    -98   -419       N  
ATOM    763  CA  ARG A 138      -8.205  47.992  13.534  1.00 13.87           C  
ANISOU  763  CA  ARG A 138     1892   1725   1653    558   -245   -160       C  
ATOM    764  C   ARG A 138      -6.950  47.901  12.674  1.00 14.63           C  
ANISOU  764  C   ARG A 138     1900   1890   1767    606      1   -297       C  
ATOM    765  O   ARG A 138      -7.045  47.726  11.462  1.00 15.75           O  
ANISOU  765  O   ARG A 138     2584   2134   1263    393   -108   -286       O  
ATOM    766  CB  ARG A 138      -8.600  49.441  13.763  1.00 14.93           C  
ANISOU  766  CB  ARG A 138     2128   2104   1439    513   -343    -91       C  
ATOM    767  CG  ARG A 138      -9.885  49.604  14.539  1.00 16.00           C  
ANISOU  767  CG  ARG A 138     2093   2281   1703    584   -421   -252       C  
ATOM    768  CD  ARG A 138     -10.324  51.062  14.609  1.00 17.12           C  
ANISOU  768  CD  ARG A 138     2691   2525   1286    768   -275   -164       C  
ATOM    769  NE  ARG A 138     -11.395  51.261  15.575  1.00 18.90           N  
ANISOU  769  NE  ARG A 138     2830   2198   2151    988   -288   -311       N  
ATOM    770  CZ  ARG A 138     -11.890  52.448  15.895  1.00 22.29           C  
ANISOU  770  CZ  ARG A 138     3622   2676   2169    940    209     66       C  
ATOM    771  NH1 ARG A 138     -11.450  53.545  15.279  1.00 23.40           N  
ANISOU  771  NH1 ARG A 138     3978   2981   1929   1532    216    -96       N  
ATOM    772  NH2 ARG A 138     -12.795  52.535  16.859  1.00 24.81           N  
ANISOU  772  NH2 ARG A 138     3881   3346   2200   1368    472    158       N  
ATOM    773  N   GLY A 139      -5.783  48.058  13.285  1.00 13.77           N  
ANISOU  773  N   GLY A 139     2029   1709   1492    461     20   -176       N  
ATOM    774  CA  GLY A 139      -4.526  47.951  12.548  1.00 13.16           C  
ANISOU  774  CA  GLY A 139     2133   1529   1336    292     35   -133       C  
ATOM    775  C   GLY A 139      -4.369  46.579  11.931  1.00 12.30           C  
ANISOU  775  C   GLY A 139     2059   1360   1252    420    220   -314       C  
ATOM    776  O   GLY A 139      -3.983  46.436  10.760  1.00 12.92           O  
ANISOU  776  O   GLY A 139     2103   1803   1001    310     -5   -204       O  
ATOM    777  N   TYR A 140      -4.661  45.524  12.688  1.00 11.34           N  
ANISOU  777  N   TYR A 140     2004   1455    850    367    -21   -117       N  
ATOM    778  CA  TYR A 140      -4.549  44.178  12.116  1.00 11.17           C  
ANISOU  778  CA  TYR A 140     1709   1586    948    286   -132   -150       C  
ATOM    779  C   TYR A 140      -5.452  44.033  10.858  1.00 12.23           C  
ANISOU  779  C   TYR A 140     1814   1693   1141    416   -151    156       C  
ATOM    780  O   TYR A 140      -5.043  43.432   9.848  1.00 12.82           O  
ANISOU  780  O   TYR A 140     2020   2009    840    476     61   -143       O  
ATOM    781  CB  TYR A 140      -4.984  43.101  13.093  1.00 11.49           C  
ANISOU  781  CB  TYR A 140     1653   1651   1061    284    -90     38       C  
ATOM    782  CG  TYR A 140      -4.241  42.962  14.396  1.00 10.87           C  
ANISOU  782  CG  TYR A 140     1402   1585   1142    246   -100   -112       C  
ATOM    783  CD1 TYR A 140      -2.966  43.448  14.591  1.00 11.63           C  
ANISOU  783  CD1 TYR A 140     1735   1687    995    232    103     -1       C  
ATOM    784  CD2 TYR A 140      -4.876  42.351  15.472  1.00 11.44           C  
ANISOU  784  CD2 TYR A 140     1363   1699   1286    -24   -254   -221       C  
ATOM    785  CE1 TYR A 140      -2.325  43.317  15.842  1.00 11.40           C  
ANISOU  785  CE1 TYR A 140     1888   1616    826    202     68   -213       C  
ATOM    786  CE2 TYR A 140      -4.242  42.221  16.681  1.00 11.83           C  
ANISOU  786  CE2 TYR A 140     1603   1982    910     88   -171    -22       C  
ATOM    787  CZ  TYR A 140      -2.983  42.684  16.869  1.00 11.72           C  
ANISOU  787  CZ  TYR A 140     1423   1640   1389    119   -135   -165       C  
ATOM    788  OH  TYR A 140      -2.371  42.566  18.122  1.00 13.02           O  
ANISOU  788  OH  TYR A 140     1880   2110    955    212    -54   -218       O  
ATOM    789  N   LEU A 141      -6.678  44.531  10.945  1.00 12.38           N  
ANISOU  789  N   LEU A 141     1852   1809   1042    381   -239    -52       N  
ATOM    790  CA  LEU A 141      -7.656  44.388   9.855  1.00 12.74           C  
ANISOU  790  CA  LEU A 141     1742   1772   1324    235   -246   -196       C  
ATOM    791  C   LEU A 141      -7.265  45.250   8.636  1.00 14.09           C  
ANISOU  791  C   LEU A 141     2267   1586   1500    298    -75   -186       C  
ATOM    792  O   LEU A 141      -7.400  44.790   7.496  1.00 14.60           O  
ANISOU  792  O   LEU A 141     2728   1966    852    483   -193   -314       O  
ATOM    793  CB  LEU A 141      -9.057  44.791  10.361  1.00 13.12           C  
ANISOU  793  CB  LEU A 141     2150   1819   1015    237   -384   -195       C  
ATOM    794  CG  LEU A 141      -9.654  43.882  11.438  1.00 14.35           C  
ANISOU  794  CG  LEU A 141     1975   2114   1363    167   -188   -262       C  
ATOM    795  CD1 LEU A 141     -11.033  44.439  11.864  1.00 17.23           C  
ANISOU  795  CD1 LEU A 141     2445   2482   1619    533    495   -232       C  
ATOM    796  CD2 LEU A 141      -9.765  42.397  10.977  1.00 17.18           C  
ANISOU  796  CD2 LEU A 141     2231   2150   2145     67   -200   -362       C  
ATOM    797  N   GLU A 142      -6.769  46.464   8.876  1.00 13.78           N  
ANISOU  797  N   GLU A 142     2450   1815    968    369     24   -102       N  
ATOM    798  CA  GLU A 142      -6.371  47.372   7.796  1.00 15.21           C  
ANISOU  798  CA  GLU A 142     2583   1838   1356    164   -173    172       C  
ATOM    799  C   GLU A 142      -5.217  46.740   7.033  1.00 15.13           C  
ANISOU  799  C   GLU A 142     2640   1932   1176    317   -177   -203       C  
ATOM    800  O   GLU A 142      -5.203  46.718   5.795  1.00 16.50           O  
ANISOU  800  O   GLU A 142     3129   2017   1123    451   -192     52       O  
ATOM    801  CB  GLU A 142      -5.969  48.720   8.364  1.00 16.51           C  
ANISOU  801  CB  GLU A 142     2846   2169   1258    368    198    177       C  
ATOM    802  CG  GLU A 142      -7.102  49.521   8.906  1.00 24.44           C  
ANISOU  802  CG  GLU A 142     3642   3231   2412    390     99    126       C  
ATOM    803  CD  GLU A 142      -6.658  50.841   9.499  1.00 30.80           C  
ANISOU  803  CD  GLU A 142     4119   3770   3813    454    -33   -746       C  
ATOM    804  OE1 GLU A 142      -5.454  51.228   9.333  1.00 34.84           O  
ANISOU  804  OE1 GLU A 142     4668   3082   5485    789   -208   -843       O  
ATOM    805  OE2 GLU A 142      -7.539  51.503  10.113  1.00 36.05           O  
ANISOU  805  OE2 GLU A 142     4907   4251   4538   1247     63  -1190       O  
ATOM    806  N   ALA A 143      -4.249  46.187   7.768  1.00 13.57           N  
ANISOU  806  N   ALA A 143     2295   1745   1115    341     18    143       N  
ATOM    807  CA  ALA A 143      -3.089  45.539   7.151  1.00 13.91           C  
ANISOU  807  CA  ALA A 143     2254   1732   1297    278    134    -11       C  
ATOM    808  C   ALA A 143      -3.541  44.320   6.315  1.00 13.33           C  
ANISOU  808  C   ALA A 143     2322   1591   1152    203    189    -29       C  
ATOM    809  O   ALA A 143      -3.033  44.072   5.202  1.00 15.01           O  
ANISOU  809  O   ALA A 143     2729   2097    874    307    140   -180       O  
ATOM    810  CB  ALA A 143      -2.069  45.140   8.216  1.00 14.54           C  
ANISOU  810  CB  ALA A 143     2197   1968   1357    354   -174   -252       C  
ATOM    811  N   ALA A 144      -4.433  43.492   6.877  1.00 13.67           N  
ANISOU  811  N   ALA A 144     2110   1677   1404    264   -300    -27       N  
ATOM    812  CA  ALA A 144      -4.883  42.301   6.179  1.00 13.07           C  
ANISOU  812  CA  ALA A 144     2335   1577   1052    368    -55   -120       C  
ATOM    813  C   ALA A 144      -5.675  42.652   4.916  1.00 14.82           C  
ANISOU  813  C   ALA A 144     2355   1756   1520    449   -200    -84       C  
ATOM    814  O   ALA A 144      -5.573  41.948   3.916  1.00 14.58           O  
ANISOU  814  O   ALA A 144     2879   2001    659    434    -95     40       O  
ATOM    815  CB  ALA A 144      -5.698  41.384   7.114  1.00 14.61           C  
ANISOU  815  CB  ALA A 144     2707   1787   1055      9   -345    222       C  
ATOM    816  N   LYS A 145      -6.484  43.701   4.965  1.00 15.98           N  
ANISOU  816  N   LYS A 145     2727   2208   1136    382   -270   -173       N  
ATOM    817  CA  LYS A 145      -7.267  44.121   3.794  1.00 17.56           C  
ANISOU  817  CA  LYS A 145     3037   2287   1346    594   -239   -222       C  
ATOM    818  C   LYS A 145      -6.330  44.503   2.616  1.00 17.76           C  
ANISOU  818  C   LYS A 145     3145   2192   1410    539   -283     75       C  
ATOM    819  O   LYS A 145      -6.713  44.369   1.441  1.00 22.92           O  
ANISOU  819  O   LYS A 145     3872   3163   1673    828   -520   -277       O  
ATOM    820  CB  LYS A 145      -8.126  45.309   4.177  1.00 20.33           C  
ANISOU  820  CB  LYS A 145     3084   2825   1813    740   -653     79       C  
ATOM    821  CG  LYS A 145      -9.453  45.006   4.760  1.00 25.84           C  
ANISOU  821  CG  LYS A 145     4148   3197   2470    342   -341   -217       C  
ATOM    822  CD  LYS A 145     -10.364  46.275   4.695  1.00 31.91           C  
ANISOU  822  CD  LYS A 145     4095   4466   3562   1306    125   -888       C  
ATOM    823  N   LYS A 146      -5.116  44.959   2.921  1.00 17.15           N  
ANISOU  823  N   LYS A 146     3237   2213   1065    423   -224    266       N  
ATOM    824  CA  LYS A 146      -4.119  45.341   1.902  1.00 20.36           C  
ANISOU  824  CA  LYS A 146     3630   2286   1820    251    255    139       C  
ATOM    825  C   LYS A 146      -3.293  44.129   1.365  1.00 18.45           C  
ANISOU  825  C   LYS A 146     3273   2424   1311    352    317    359       C  
ATOM    826  O   LYS A 146      -2.298  44.313   0.659  1.00 22.55           O  
ANISOU  826  O   LYS A 146     3965   2754   1848    229    403    329       O  
ATOM    827  CB  LYS A 146      -3.142  46.390   2.480  1.00 23.32           C  
ANISOU  827  CB  LYS A 146     3798   2810   2252   -121    797    325       C  
ATOM    828  CG  LYS A 146      -3.727  47.774   2.723  1.00 29.07           C  
ANISOU  828  CG  LYS A 146     4521   3953   2568    191    257     61       C  
ATOM    829  CD  LYS A 146      -2.880  48.595   3.725  1.00 36.55           C  
ANISOU  829  CD  LYS A 146     5083   4656   4146   -512    149    108       C  
ATOM    830  CE  LYS A 146      -1.407  48.217   3.700  1.00 41.04           C  
ANISOU  830  CE  LYS A 146     5702   5294   4596    -46     58   -121       C  
ATOM    831  NZ  LYS A 146      -0.630  48.632   4.923  1.00 47.24           N  
ANISOU  831  NZ  LYS A 146     6555   6043   5348   -306    -67   -518       N  
ATOM    832  N   GLY A 147      -3.557  42.933   1.904  1.00 16.05           N  
ANISOU  832  N   GLY A 147     2996   2154    946    422   -198    249       N  
ATOM    833  CA  GLY A 147      -2.781  41.758   1.538  1.00 15.17           C  
ANISOU  833  CA  GLY A 147     2954   2177    630    292   -229    126       C  
ATOM    834  C   GLY A 147      -1.691  41.359   2.533  1.00 14.91           C  
ANISOU  834  C   GLY A 147     2559   1947   1156    402    101    198       C  
ATOM    835  O   GLY A 147      -0.905  40.443   2.299  1.00 15.64           O  
ANISOU  835  O   GLY A 147     2845   2115    981    394    -68      4       O  
ATOM    836  N   GLY A 148      -1.668  42.064   3.663  1.00 13.37           N  
ANISOU  836  N   GLY A 148     2532   1828    717    218     98    155       N  
ATOM    837  CA  GLY A 148      -0.660  41.842   4.701  1.00 13.84           C  
ANISOU  837  CA  GLY A 148     2476   1761   1018    113     -8     63       C  
ATOM    838  C   GLY A 148       0.064  43.144   5.014  1.00 14.10           C  
ANISOU  838  C   GLY A 148     2458   1787   1111    -46    121     33       C  
ATOM    839  O   GLY A 148       0.297  43.991   4.139  1.00 15.88           O  
ANISOU  839  O   GLY A 148     3246   2086    702   -200     81     52       O  
ATOM    840  N   GLY A 149       0.395  43.341   6.275  1.00 13.77           N  
ANISOU  840  N   GLY A 149     2383   1757   1091     20     34    -44       N  
ATOM    841  CA  GLY A 149       1.105  44.530   6.684  1.00 14.57           C  
ANISOU  841  CA  GLY A 149     2387   1918   1232     -1    112     16       C  
ATOM    842  C   GLY A 149       1.276  44.623   8.182  1.00 13.36           C  
ANISOU  842  C   GLY A 149     2424   1419   1231    -65    192     90       C  
ATOM    843  O   GLY A 149       1.069  43.644   8.895  1.00 11.88           O  
ANISOU  843  O   GLY A 149     2268   1348    894    132    106    -21       O  
ATOM    844  N   TYR A 150       1.649  45.820   8.640  1.00 13.41           N  
ANISOU  844  N   TYR A 150     2372   1417   1303    113    203     33       N  
ATOM    845  CA  TYR A 150       2.248  46.001   9.971  1.00 12.93           C  
ANISOU  845  CA  TYR A 150     2091   1663   1157    103    301     28       C  
ATOM    846  C   TYR A 150       1.436  46.993  10.831  1.00 12.82           C  
ANISOU  846  C   TYR A 150     2167   1539   1166    258    318   -153       C  
ATOM    847  O   TYR A 150       0.837  47.968  10.329  1.00 14.77           O  
ANISOU  847  O   TYR A 150     2594   1907   1109    521     18   -222       O  
ATOM    848  CB  TYR A 150       3.699  46.460   9.861  1.00 14.01           C  
ANISOU  848  CB  TYR A 150     2224   1750   1347    -12    347      8       C  
ATOM    849  CG  TYR A 150       4.514  45.453   9.091  1.00 12.53           C  
ANISOU  849  CG  TYR A 150     2056   1437   1265     76    621    147       C  
ATOM    850  CD1 TYR A 150       4.703  45.568   7.737  1.00 15.99           C  
ANISOU  850  CD1 TYR A 150     2723   2023   1330    451    661    458       C  
ATOM    851  CD2 TYR A 150       5.093  44.382   9.721  1.00 13.71           C  
ANISOU  851  CD2 TYR A 150     2288   1417   1504    -45    287      8       C  
ATOM    852  CE1 TYR A 150       5.335  44.565   7.024  1.00 15.13           C  
ANISOU  852  CE1 TYR A 150     2808   2053    886    408    456      1       C  
ATOM    853  CE2 TYR A 150       5.775  43.413   9.021  1.00 14.11           C  
ANISOU  853  CE2 TYR A 150     2243   1567   1548     44    258    253       C  
ATOM    854  CZ  TYR A 150       5.899  43.512   7.680  1.00 13.72           C  
ANISOU  854  CZ  TYR A 150     1984   1670   1559    204    309   -261       C  
ATOM    855  OH  TYR A 150       6.557  42.497   6.989  1.00 15.97           O  
ANISOU  855  OH  TYR A 150     2344   2100   1621    309    254   -302       O  
ATOM    856  N   THR A 151       1.387  46.678  12.125  1.00 12.13           N  
ANISOU  856  N   THR A 151     2198   1305   1105    201    278    -21       N  
ATOM    857  CA  THR A 151       0.762  47.525  13.152  1.00 12.09           C  
ANISOU  857  CA  THR A 151     1872   1462   1258    166     47   -161       C  
ATOM    858  C   THR A 151       1.789  47.676  14.267  1.00 11.71           C  
ANISOU  858  C   THR A 151     1804   1114   1527    125    125    -92       C  
ATOM    859  O   THR A 151       2.378  46.675  14.729  1.00 13.49           O  
ANISOU  859  O   THR A 151     2347   1259   1518    187     99   -234       O  
ATOM    860  CB  THR A 151      -0.538  46.864  13.641  1.00 12.47           C  
ANISOU  860  CB  THR A 151     1872   1542   1323     97     92   -189       C  
ATOM    861  OG1 THR A 151      -1.423  46.640  12.521  1.00 12.97           O  
ANISOU  861  OG1 THR A 151     2017   1822   1085    110      1   -278       O  
ATOM    862  CG2 THR A 151      -1.267  47.718  14.685  1.00 13.18           C  
ANISOU  862  CG2 THR A 151     2167   1847    992    481     -2   -397       C  
ATOM    863  N   TYR A 152       1.902  48.907  14.780  1.00 13.04           N  
ANISOU  863  N   TYR A 152     2189   1338   1426    203     45   -227       N  
ATOM    864  CA  TYR A 152       2.936  49.248  15.760  1.00 12.36           C  
ANISOU  864  CA  TYR A 152     2132   1343   1222    -14    188   -247       C  
ATOM    865  C   TYR A 152       2.268  49.794  17.005  1.00 12.87           C  
ANISOU  865  C   TYR A 152     2072   1268   1548    177    121   -338       C  
ATOM    866  O   TYR A 152       1.492  50.720  16.926  1.00 13.65           O  
ANISOU  866  O   TYR A 152     2434   1624   1127    266    182   -159       O  
ATOM    867  CB  TYR A 152       3.905  50.300  15.186  1.00 12.67           C  
ANISOU  867  CB  TYR A 152     2321   1398   1094    155     78   -174       C  
ATOM    868  CG  TYR A 152       4.609  49.846  13.927  1.00 13.57           C  
ANISOU  868  CG  TYR A 152     1971   1672   1509   -102    200   -162       C  
ATOM    869  CD1 TYR A 152       5.807  49.159  13.992  1.00 13.84           C  
ANISOU  869  CD1 TYR A 152     2218   1516   1522   -136    -41   -522       C  
ATOM    870  CD2 TYR A 152       4.048  50.091  12.679  1.00 14.05           C  
ANISOU  870  CD2 TYR A 152     2212   1578   1546    352     72    -96       C  
ATOM    871  CE1 TYR A 152       6.424  48.692  12.833  1.00 13.17           C  
ANISOU  871  CE1 TYR A 152     2332   1542   1129    205    278   -136       C  
ATOM    872  CE2 TYR A 152       4.645  49.610  11.514  1.00 13.32           C  
ANISOU  872  CE2 TYR A 152     2498   1620    942    178    195   -187       C  
ATOM    873  CZ  TYR A 152       5.832  48.946  11.589  1.00 12.84           C  
ANISOU  873  CZ  TYR A 152     2062   1559   1257    122    281     40       C  
ATOM    874  OH  TYR A 152       6.411  48.475  10.394  1.00 16.63           O  
ANISOU  874  OH  TYR A 152     2881   1858   1578   -138    664   -280       O  
ATOM    875  N   TYR A 153       2.622  49.250  18.161  1.00 12.24           N  
ANISOU  875  N   TYR A 153     1913   1592   1145    252    351   -282       N  
ATOM    876  CA  TYR A 153       1.907  49.597  19.388  1.00 11.84           C  
ANISOU  876  CA  TYR A 153     1969   1371   1156    355    193   -299       C  
ATOM    877  C   TYR A 153       2.655  49.038  20.609  1.00 11.80           C  
ANISOU  877  C   TYR A 153     1583   1622   1278    251    120   -232       C  
ATOM    878  O   TYR A 153       3.583  48.262  20.450  1.00 12.85           O  
ANISOU  878  O   TYR A 153     1956   1660   1265    255    106   -545       O  
ATOM    879  CB  TYR A 153       0.457  49.053  19.345  1.00 12.21           C  
ANISOU  879  CB  TYR A 153     1935   1710    993    299    121   -263       C  
ATOM    880  CG  TYR A 153       0.329  47.551  19.214  1.00 11.32           C  
ANISOU  880  CG  TYR A 153     1897   1538    864    138    109   -276       C  
ATOM    881  CD1 TYR A 153      -0.013  46.750  20.312  1.00 12.39           C  
ANISOU  881  CD1 TYR A 153     1954   1741   1011    202    104   -415       C  
ATOM    882  CD2 TYR A 153       0.553  46.920  18.005  1.00 13.38           C  
ANISOU  882  CD2 TYR A 153     2065   1724   1294    -84    270   -329       C  
ATOM    883  CE1 TYR A 153      -0.125  45.375  20.184  1.00 12.79           C  
ANISOU  883  CE1 TYR A 153     1992   1761   1105    293    332   -232       C  
ATOM    884  CE2 TYR A 153       0.473  45.572  17.893  1.00 12.17           C  
ANISOU  884  CE2 TYR A 153     2105   1428   1090     22    175   -307       C  
ATOM    885  CZ  TYR A 153       0.186  44.777  18.975  1.00 11.19           C  
ANISOU  885  CZ  TYR A 153     1581   1586   1084     41    200   -128       C  
ATOM    886  OH  TYR A 153       0.090  43.395  18.821  1.00 12.43           O  
ANISOU  886  OH  TYR A 153     1986   1548   1187    -92      6   -243       O  
ATOM    887  N   LYS A 154       2.245  49.468  21.808  1.00 12.81           N  
ANISOU  887  N   LYS A 154     2054   1455   1359    276    226   -350       N  
ATOM    888  CA  LYS A 154       2.839  48.942  23.058  1.00 12.28           C  
ANISOU  888  CA  LYS A 154     1842   1425   1398    254    114   -438       C  
ATOM    889  C   LYS A 154       1.885  47.953  23.690  1.00 12.71           C  
ANISOU  889  C   LYS A 154     1966   1594   1267    285     35   -420       C  
ATOM    890  O   LYS A 154       0.652  48.136  23.710  1.00 13.59           O  
ANISOU  890  O   LYS A 154     1866   1994   1302    370    146   -422       O  
ATOM    891  CB  LYS A 154       3.149  50.053  24.094  1.00 14.85           C  
ANISOU  891  CB  LYS A 154     2323   1891   1425      6    277   -642       C  
ATOM    892  CG  LYS A 154       4.211  50.961  23.691  1.00 17.44           C  
ANISOU  892  CG  LYS A 154     2464   2037   2126      7    610   -918       C  
ATOM    893  CD  LYS A 154       4.657  51.956  24.772  1.00 18.64           C  
ANISOU  893  CD  LYS A 154     2482   2044   2553    -72    220  -1449       C  
ATOM    894  CE  LYS A 154       5.732  51.439  25.696  1.00 19.47           C  
ANISOU  894  CE  LYS A 154     2806   2817   1774     28    630  -1166       C  
ATOM    895  NZ  LYS A 154       6.269  52.500  26.669  1.00 20.32           N  
ANISOU  895  NZ  LYS A 154     2881   3177   1663   -361    276  -1409       N  
ATOM    896  N   MET A 155       2.478  46.948  24.298  1.00 11.49           N  
ANISOU  896  N   MET A 155     1575   1676   1111    234    185   -328       N  
ATOM    897  CA  MET A 155       1.706  45.922  24.962  1.00 11.58           C  
ANISOU  897  CA  MET A 155     1595   1567   1236     48     60   -501       C  
ATOM    898  C   MET A 155       2.647  45.191  25.894  1.00 11.86           C  
ANISOU  898  C   MET A 155     1643   1755   1105    202     74   -566       C  
ATOM    899  O   MET A 155       3.814  44.978  25.539  1.00 12.15           O  
ANISOU  899  O   MET A 155     1796   1777   1041    280    149   -315       O  
ATOM    900  CB  MET A 155       1.138  44.966  23.900  1.00 12.53           C  
ANISOU  900  CB  MET A 155     1745   1679   1336     68    -91   -549       C  
ATOM    901  CG  MET A 155       0.074  44.026  24.410  1.00 12.05           C  
ANISOU  901  CG  MET A 155     2087   1664    826    247   -284   -579       C  
ATOM    902  SD  MET A 155      -1.463  44.768  25.027  1.00 12.51           S  
ANISOU  902  SD  MET A 155     1883   1975    896    139    121   -528       S  
ATOM    903  CE  MET A 155      -2.167  45.469  23.519  1.00 14.04           C  
ANISOU  903  CE  MET A 155     1941   1959   1433    281    -18    -39       C  
ATOM    904  N   PRO A 156       2.115  44.607  26.981  1.00 11.38           N  
ANISOU  904  N   PRO A 156     1680   1592   1051    270     93   -493       N  
ATOM    905  CA  PRO A 156       2.956  43.714  27.780  1.00 11.64           C  
ANISOU  905  CA  PRO A 156     1646   1516   1258    181    -75   -479       C  
ATOM    906  C   PRO A 156       3.301  42.447  27.007  1.00 11.73           C  
ANISOU  906  C   PRO A 156     1640   1507   1310    283    -56   -641       C  
ATOM    907  O   PRO A 156       2.620  42.100  26.023  1.00 13.04           O  
ANISOU  907  O   PRO A 156     1793   2053   1107     -7    102   -696       O  
ATOM    908  CB  PRO A 156       2.097  43.415  29.006  1.00 12.95           C  
ANISOU  908  CB  PRO A 156     1826   1774   1318    344     -4   -455       C  
ATOM    909  CG  PRO A 156       1.211  44.608  29.172  1.00 11.59           C  
ANISOU  909  CG  PRO A 156     1653   1738   1011    -13   -102   -363       C  
ATOM    910  CD  PRO A 156       0.867  44.934  27.701  1.00 12.44           C  
ANISOU  910  CD  PRO A 156     1937   2036    754    225    133   -655       C  
ATOM    911  N   LYS A 157       4.274  41.706  27.528  1.00 12.49           N  
ANISOU  911  N   LYS A 157     1840   1800   1106    349      2   -799       N  
ATOM    912  CA  LYS A 157       4.576  40.366  27.012  1.00 15.13           C  
ANISOU  912  CA  LYS A 157     2015   1925   1808    471   -100   -674       C  
ATOM    913  C   LYS A 157       3.661  39.308  27.627  1.00 13.78           C  
ANISOU  913  C   LYS A 157     2216   1413   1607    398   -126   -666       C  
ATOM    914  O   LYS A 157       3.552  38.215  27.115  1.00 14.81           O  
ANISOU  914  O   LYS A 157     2073   1614   1937    414   -417   -850       O  
ATOM    915  CB  LYS A 157       6.038  39.999  27.294  1.00 15.21           C  
ANISOU  915  CB  LYS A 157     2050   1984   1742    380   -265   -920       C  
ATOM    916  CG  LYS A 157       7.032  40.737  26.430  1.00 16.49           C  
ANISOU  916  CG  LYS A 157     1729   2579   1956    232   -195  -1062       C  
ATOM    917  CD  LYS A 157       8.436  40.386  26.861  1.00 18.22           C  
ANISOU  917  CD  LYS A 157     2002   3363   1557    145   -408   -977       C  
ATOM    918  CE  LYS A 157       9.394  40.235  25.758  1.00 26.72           C  
ANISOU  918  CE  LYS A 157     2604   5097   2451    494   -499   -537       C  
ATOM    919  NZ  LYS A 157      10.696  39.713  26.364  1.00 26.41           N  
ANISOU  919  NZ  LYS A 157     1293   5781   2961   1338   -363   -587       N  
ATOM    920  N   TYR A 158       3.085  39.620  28.787  1.00 12.80           N  
ANISOU  920  N   TYR A 158     2134   1548   1182    130   -361   -580       N  
ATOM    921  CA  TYR A 158       2.163  38.721  29.503  1.00 12.19           C  
ANISOU  921  CA  TYR A 158     2188   1446    995     42   -280   -567       C  
ATOM    922  C   TYR A 158       1.186  39.567  30.309  1.00 14.37           C  
ANISOU  922  C   TYR A 158     2396   1781   1283    -35    -55   -336       C  
ATOM    923  O   TYR A 158       1.448  40.740  30.591  1.00 13.37           O  
ANISOU  923  O   TYR A 158     2164   1617   1297      8   -122   -337       O  
ATOM    924  CB  TYR A 158       2.929  37.745  30.399  1.00 15.62           C  
ANISOU  924  CB  TYR A 158     2222   1654   2058     -9   -365   -284       C  
ATOM    925  CG  TYR A 158       3.790  38.440  31.402  1.00 16.58           C  
ANISOU  925  CG  TYR A 158     2616   1887   1797    201   -456   -101       C  
ATOM    926  CD1 TYR A 158       3.274  38.870  32.615  1.00 17.47           C  
ANISOU  926  CD1 TYR A 158     2691   2119   1826    257   -913   -344       C  
ATOM    927  CD2 TYR A 158       5.120  38.678  31.147  1.00 19.26           C  
ANISOU  927  CD2 TYR A 158     2749   2979   1590     11   -626    388       C  
ATOM    928  CE1 TYR A 158       4.051  39.536  33.514  1.00 17.86           C  
ANISOU  928  CE1 TYR A 158     3044   2297   1443    362   -954   -296       C  
ATOM    929  CE2 TYR A 158       5.908  39.345  32.055  1.00 21.95           C  
ANISOU  929  CE2 TYR A 158     3133   3275   1932   -170   -581     21       C  
ATOM    930  CZ  TYR A 158       5.358  39.785  33.234  1.00 17.86           C  
ANISOU  930  CZ  TYR A 158     2757   2841   1187      8  -1389   -186       C  
ATOM    931  OH  TYR A 158       6.160  40.463  34.165  1.00 26.12           O  
ANISOU  931  OH  TYR A 158     4706   3120   2097   -513  -2017    138       O  
ATOM    932  N   ASP A 159       0.029  38.978  30.612  1.00 14.34           N  
ANISOU  932  N   ASP A 159     2329   1702   1415    125    -30   -212       N  
ATOM    933  CA  ASP A 159      -1.049  39.655  31.286  1.00 13.36           C  
ANISOU  933  CA  ASP A 159     1978   1905   1190     53   -156   -262       C  
ATOM    934  C   ASP A 159      -0.544  40.267  32.592  1.00 13.35           C  
ANISOU  934  C   ASP A 159     2246   1707   1119   -175   -122   -167       C  
ATOM    935  O   ASP A 159      -0.028  39.567  33.458  1.00 15.76           O  
ANISOU  935  O   ASP A 159     2801   1909   1278     38   -391    -70       O  
ATOM    936  CB  ASP A 159      -2.171  38.647  31.517  1.00 14.60           C  
ANISOU  936  CB  ASP A 159     2321   2262    962     22   -173   -206       C  
ATOM    937  CG  ASP A 159      -3.445  39.265  32.062  1.00 16.01           C  
ANISOU  937  CG  ASP A 159     2290   2448   1346   -288     77   -191       C  
ATOM    938  OD1 ASP A 159      -3.550  40.502  32.216  1.00 18.01           O  
ANISOU  938  OD1 ASP A 159     2310   2473   2057    159    -92   -557       O  
ATOM    939  OD2 ASP A 159      -4.329  38.443  32.418  1.00 21.05           O  
ANISOU  939  OD2 ASP A 159     3000   3142   1854   -668    530   -577       O  
ATOM    940  N   GLY A 160      -0.682  41.576  32.701  1.00 14.51           N  
ANISOU  940  N   GLY A 160     2297   2062   1151   -126    -46   -371       N  
ATOM    941  CA  GLY A 160      -0.261  42.312  33.898  1.00 14.37           C  
ANISOU  941  CA  GLY A 160     2552   2031    876    -96    251   -272       C  
ATOM    942  C   GLY A 160       1.180  42.779  33.940  1.00 13.29           C  
ANISOU  942  C   GLY A 160     2376   1613   1058     80     76   -202       C  
ATOM    943  O   GLY A 160       1.592  43.478  34.898  1.00 17.22           O  
ANISOU  943  O   GLY A 160     2991   1972   1579   -302   -188   -715       O  
ATOM    944  N   GLY A 161       1.935  42.507  32.874  1.00 13.96           N  
ANISOU  944  N   GLY A 161     2443   1751   1110     65     60   -392       N  
ATOM    945  CA  GLY A 161       3.329  42.913  32.781  1.00 13.56           C  
ANISOU  945  CA  GLY A 161     2349   1740   1063    156   -145   -265       C  
ATOM    946  C   GLY A 161       3.512  44.361  32.319  1.00 11.22           C  
ANISOU  946  C   GLY A 161     1991   1598    673    126    -39   -539       C  
ATOM    947  O   GLY A 161       2.560  45.088  32.042  1.00 12.71           O  
ANISOU  947  O   GLY A 161     2034   1715   1077    214   -155   -440       O  
ATOM    948  N   VAL A 162       4.756  44.799  32.318  1.00 12.07           N  
ANISOU  948  N   VAL A 162     1909   1841    834    212   -243   -530       N  
ATOM    949  CA  VAL A 162       5.117  46.131  31.878  1.00 12.52           C  
ANISOU  949  CA  VAL A 162     2038   1738    981    137   -125   -583       C  
ATOM    950  C   VAL A 162       4.928  46.246  30.348  1.00 11.64           C  
ANISOU  950  C   VAL A 162     1687   1711   1024    348     50   -515       C  
ATOM    951  O   VAL A 162       5.370  45.380  29.588  1.00 14.48           O  
ANISOU  951  O   VAL A 162     2245   1730   1524    449    282   -670       O  
ATOM    952  CB  VAL A 162       6.575  46.457  32.281  1.00 14.68           C  
ANISOU  952  CB  VAL A 162     2009   2095   1471    416    132   -840       C  
ATOM    953  CG1 VAL A 162       7.019  47.801  31.724  1.00 17.50           C  
ANISOU  953  CG1 VAL A 162     2487   2061   2100    -71    111   -136       C  
ATOM    954  CG2 VAL A 162       6.727  46.460  33.800  1.00 19.18           C  
ANISOU  954  CG2 VAL A 162     2830   2527   1932     62     14   -778       C  
ATOM    955  N   PRO A 163       4.281  47.318  29.883  1.00 11.93           N  
ANISOU  955  N   PRO A 163     1885   1626   1022    277      0   -658       N  
ATOM    956  CA  PRO A 163       4.072  47.443  28.436  1.00 13.12           C  
ANISOU  956  CA  PRO A 163     1974   1762   1247     65   -159   -425       C  
ATOM    957  C   PRO A 163       5.379  47.777  27.695  1.00 12.81           C  
ANISOU  957  C   PRO A 163     1693   1751   1421     95    115   -343       C  
ATOM    958  O   PRO A 163       6.198  48.530  28.210  1.00 15.72           O  
ANISOU  958  O   PRO A 163     2324   2288   1360   -247    -90   -397       O  
ATOM    959  CB  PRO A 163       3.025  48.586  28.336  1.00 14.81           C  
ANISOU  959  CB  PRO A 163     1929   2108   1588    263     80   -642       C  
ATOM    960  CG  PRO A 163       3.183  49.353  29.576  1.00 16.74           C  
ANISOU  960  CG  PRO A 163     2616   1753   1991    374   -175   -489       C  
ATOM    961  CD  PRO A 163       3.616  48.387  30.631  1.00 12.07           C  
ANISOU  961  CD  PRO A 163     1982   1678    923    256    209   -624       C  
ATOM    962  N   GLU A 164       5.564  47.156  26.534  1.00 13.39           N  
ANISOU  962  N   GLU A 164     1774   2101   1212     35    140   -420       N  
ATOM    963  CA AGLU A 164       6.742  47.381  25.705  0.60 16.09           C  
ANISOU  963  CA AGLU A 164     1832   2536   1743    105    -22     43       C  
ATOM    964  CA BGLU A 164       6.787  47.143  25.709  0.40 14.98           C  
ANISOU  964  CA BGLU A 164     1903   2093   1694    -45    106   -107       C  
ATOM    965  C   GLU A 164       6.389  47.531  24.274  1.00 12.98           C  
ANISOU  965  C   GLU A 164     1704   1858   1368   -101    183   -422       C  
ATOM    966  O   GLU A 164       5.382  47.037  23.800  1.00 13.28           O  
ANISOU  966  O   GLU A 164     1631   1908   1506    -41     85   -185       O  
ATOM    967  CB AGLU A 164       7.648  46.161  25.669  0.60 20.26           C  
ANISOU  967  CB AGLU A 164     1965   3424   2308    430    119   -165       C  
ATOM    968  CB BGLU A 164       7.361  45.680  25.657  0.40 12.72           C  
ANISOU  968  CB BGLU A 164     1629   1914   1287   -271    145   -652       C  
ATOM    969  CG AGLU A 164       8.156  45.732  26.928  0.60 22.08           C  
ANISOU  969  CG AGLU A 164     2407   3533   2448    421    114   -158       C  
ATOM    970  CG BGLU A 164       8.125  45.227  26.892  0.40 16.10           C  
ANISOU  970  CG BGLU A 164     2060   1787   2267   -104    213     27       C  
ATOM    971  CD AGLU A 164       9.016  44.524  26.756  0.60 20.96           C  
ANISOU  971  CD AGLU A 164     2372   2932   2659    816     86   -577       C  
ATOM    972  CD BGLU A 164       9.458  45.972  27.093  0.40 15.49           C  
ANISOU  972  CD BGLU A 164     2066   2482   1335   -412   -411   -334       C  
ATOM    973  OE1AGLU A 164       9.534  44.246  25.621  0.60 19.09           O  
ANISOU  973  OE1AGLU A 164     2470   2475   2306      2   -422   -537       O  
ATOM    974  OE1BGLU A 164       9.931  46.630  26.130  0.40 16.54           O  
ANISOU  974  OE1BGLU A 164     1683   3062   1539   -337   -311   -460       O  
ATOM    975  OE2AGLU A 164       9.167  43.861  27.777  0.60 23.30           O  
ANISOU  975  OE2AGLU A 164     3406   3881   1564    731   -219   -432       O  
ATOM    976  OE2BGLU A 164       9.991  45.959  28.245  0.40 16.44           O  
ANISOU  976  OE2BGLU A 164     2486   3426    335   -190    -63   -239       O  
ATOM    977  N   LYS A 165       7.236  48.270  23.571  1.00 13.24           N  
ANISOU  977  N   LYS A 165     1690   1955   1385   -274    131   -367       N  
ATOM    978  CA  LYS A 165       6.995  48.471  22.142  1.00 13.10           C  
ANISOU  978  CA  LYS A 165     1952   1657   1368   -176    223   -422       C  
ATOM    979  C   LYS A 165       7.120  47.163  21.368  1.00 11.42           C  
ANISOU  979  C   LYS A 165     1311   1653   1372      4    361   -470       C  
ATOM    980  O   LYS A 165       8.032  46.370  21.580  1.00 11.68           O  
ANISOU  980  O   LYS A 165     1644   1843    948     19    150   -588       O  
ATOM    981  CB  LYS A 165       7.960  49.505  21.561  1.00 14.51           C  
ANISOU  981  CB  LYS A 165     2216   1784   1510   -108    473   -596       C  
ATOM    982  CG  LYS A 165       7.767  50.924  22.107  1.00 15.10           C  
ANISOU  982  CG  LYS A 165     2464   1702   1571   -404    334   -870       C  
ATOM    983  CD  LYS A 165       8.612  51.913  21.340  1.00 21.83           C  
ANISOU  983  CD  LYS A 165     3527   1729   3038   -783    593   -840       C  
ATOM    984  CE  LYS A 165       8.090  53.327  21.576  1.00 31.41           C  
ANISOU  984  CE  LYS A 165     4403   3415   4114   -438    638   -233       C  
ATOM    985  NZ  LYS A 165       8.898  54.379  20.871  1.00 37.85           N  
ANISOU  985  NZ  LYS A 165     5374   3993   5014  -1264    123    323       N  
ATOM    986  N   LYS A 166       6.175  46.971  20.451  1.00 11.37           N  
ANISOU  986  N   LYS A 166     1696   1331   1292   -153    346   -513       N  
ATOM    987  CA  LYS A 166       6.162  45.787  19.600  1.00 11.56           C  
ANISOU  987  CA  LYS A 166     1793   1422   1175     13    128   -526       C  
ATOM    988  C   LYS A 166       5.606  46.130  18.224  1.00 12.00           C  
ANISOU  988  C   LYS A 166     1757   1398   1403      8    279   -347       C  
ATOM    989  O   LYS A 166       5.130  47.244  17.989  1.00 12.60           O  
ANISOU  989  O   LYS A 166     2051   1429   1308      5    255   -554       O  
ATOM    990  CB  LYS A 166       5.364  44.652  20.273  1.00 11.51           C  
ANISOU  990  CB  LYS A 166     1848   1268   1255    -28    111   -581       C  
ATOM    991  CG  LYS A 166       3.876  44.891  20.388  1.00 11.78           C  
ANISOU  991  CG  LYS A 166     1731   1356   1389     66    144   -398       C  
ATOM    992  CD  LYS A 166       3.147  43.741  21.113  1.00 12.11           C  
ANISOU  992  CD  LYS A 166     1712   1678   1212     42     18   -610       C  
ATOM    993  CE  LYS A 166       3.217  42.418  20.337  1.00 11.93           C  
ANISOU  993  CE  LYS A 166     1648   1409   1475    171    256   -623       C  
ATOM    994  NZ  LYS A 166       2.459  41.319  20.997  1.00 11.89           N  
ANISOU  994  NZ  LYS A 166     1863   1575   1080    -31    376   -345       N  
ATOM    995  N   PHE A 167       5.609  45.114  17.360  1.00 11.14           N  
ANISOU  995  N   PHE A 167     1689   1216   1324     89    236   -288       N  
ATOM    996  CA  PHE A 167       4.878  45.226  16.104  1.00 12.01           C  
ANISOU  996  CA  PHE A 167     1644   1491   1426     25   -150   -160       C  
ATOM    997  C   PHE A 167       4.322  43.882  15.714  1.00 12.05           C  
ANISOU  997  C   PHE A 167     1585   1409   1581    173     77   -380       C  
ATOM    998  O   PHE A 167       4.769  42.811  16.190  1.00 11.32           O  
ANISOU  998  O   PHE A 167     1899   1437    962     34     65   -429       O  
ATOM    999  CB  PHE A 167       5.763  45.786  14.969  1.00 12.45           C  
ANISOU  999  CB  PHE A 167     1774   1610   1346     14     58   -286       C  
ATOM   1000  CG  PHE A 167       6.997  44.976  14.710  1.00 18.56           C  
ANISOU 1000  CG  PHE A 167     2829   2393   1828   -594    530    242       C  
ATOM   1001  CD1 PHE A 167       7.107  44.086  13.680  1.00 25.12           C  
ANISOU 1001  CD1 PHE A 167     4103   3441   1998    291    637   1235       C  
ATOM   1002  CD2 PHE A 167       8.134  45.260  15.486  1.00 22.82           C  
ANISOU 1002  CD2 PHE A 167     2351   3955   2364    500    456     10       C  
ATOM   1003  CE1 PHE A 167       8.371  43.313  13.580  1.00 20.40           C  
ANISOU 1003  CE1 PHE A 167     1842   3726   2181    218    414   1088       C  
ATOM   1004  CE2 PHE A 167       9.313  44.651  15.307  1.00 27.90           C  
ANISOU 1004  CE2 PHE A 167     3719   4072   2809    568    195   -420       C  
ATOM   1005  CZ  PHE A 167       9.444  43.719  14.288  1.00 19.77           C  
ANISOU 1005  CZ  PHE A 167     3109   2501   1899    612    856   -803       C  
ATOM   1006  N   ALA A 168       3.282  43.964  14.890  1.00 11.24           N  
ANISOU 1006  N   ALA A 168     1768   1289   1213    227     27   -148       N  
ATOM   1007  CA  ALA A 168       2.558  42.819  14.394  1.00 12.85           C  
ANISOU 1007  CA  ALA A 168     1970   1451   1461    -41    117   -316       C  
ATOM   1008  C   ALA A 168       2.550  42.838  12.873  1.00 12.37           C  
ANISOU 1008  C   ALA A 168     1994   1181   1526    151    102    -62       C  
ATOM   1009  O   ALA A 168       2.294  43.886  12.272  1.00 13.56           O  
ANISOU 1009  O   ALA A 168     2735   1365   1052    195    -35   -253       O  
ATOM   1010  CB  ALA A 168       1.129  42.877  14.909  1.00 12.94           C  
ANISOU 1010  CB  ALA A 168     1833   1734   1349     99    101   -331       C  
ATOM   1011  N   TYR A 169       2.807  41.679  12.264  1.00 11.17           N  
ANISOU 1011  N   TYR A 169     1666   1401   1177    138   -175    -84       N  
ATOM   1012  CA  TYR A 169       2.444  41.441  10.863  1.00 11.62           C  
ANISOU 1012  CA  TYR A 169     1860   1221   1332     90   -155   -252       C  
ATOM   1013  C   TYR A 169       1.147  40.668  10.845  1.00 10.16           C  
ANISOU 1013  C   TYR A 169     1697   1211    952    222     54   -373       C  
ATOM   1014  O   TYR A 169       1.047  39.615  11.484  1.00 11.38           O  
ANISOU 1014  O   TYR A 169     1755   1522   1047     22    107    -35       O  
ATOM   1015  CB  TYR A 169       3.528  40.603  10.154  1.00 10.62           C  
ANISOU 1015  CB  TYR A 169     1805   1187   1041   -144    126   -208       C  
ATOM   1016  CG  TYR A 169       3.085  40.164   8.786  1.00 10.11           C  
ANISOU 1016  CG  TYR A 169     1643   1238    960     83    140   -260       C  
ATOM   1017  CD1 TYR A 169       3.180  41.026   7.687  1.00 12.99           C  
ANISOU 1017  CD1 TYR A 169     2261   1321   1353    -28    255   -139       C  
ATOM   1018  CD2 TYR A 169       2.510  38.942   8.585  1.00 10.34           C  
ANISOU 1018  CD2 TYR A 169     1800   1336    791    179    384   -178       C  
ATOM   1019  CE1 TYR A 169       2.758  40.615   6.404  1.00 12.94           C  
ANISOU 1019  CE1 TYR A 169     2235   1724    956    -85    547    -65       C  
ATOM   1020  CE2 TYR A 169       2.077  38.514   7.320  1.00 10.67           C  
ANISOU 1020  CE2 TYR A 169     2005   1348    701    110    509   -187       C  
ATOM   1021  CZ  TYR A 169       2.222  39.360   6.224  1.00 11.87           C  
ANISOU 1021  CZ  TYR A 169     1889   1596   1023    -60     22   -197       C  
ATOM   1022  OH  TYR A 169       1.772  38.915   5.011  1.00 14.38           O  
ANISOU 1022  OH  TYR A 169     2281   1986   1195    258   -274   -242       O  
ATOM   1023  N   SER A 170       0.138  41.177  10.145  1.00 10.65           N  
ANISOU 1023  N   SER A 170     1788   1426    829    158     54   -145       N  
ATOM   1024  CA  SER A 170      -1.139  40.440  10.059  1.00 10.58           C  
ANISOU 1024  CA  SER A 170     1851   1525    641     59    -74   -177       C  
ATOM   1025  C   SER A 170      -1.494  40.121   8.583  1.00  9.75           C  
ANISOU 1025  C   SER A 170     1521   1302    880    -83    121    -76       C  
ATOM   1026  O   SER A 170      -1.078  40.835   7.673  1.00 11.58           O  
ANISOU 1026  O   SER A 170     1960   1604    834   -118     88     83       O  
ATOM   1027  CB  SER A 170      -2.258  41.242  10.753  1.00 11.76           C  
ANISOU 1027  CB  SER A 170     1702   1753   1012    151    -27    -61       C  
ATOM   1028  OG  SER A 170      -2.452  42.442  10.057  1.00 12.27           O  
ANISOU 1028  OG  SER A 170     1983   1648   1031    173     -4   -154       O  
ATOM   1029  N   HIS A 171      -2.259  39.075   8.414  1.00 10.80           N  
ANISOU 1029  N   HIS A 171     1783   1448    870   -109     14      1       N  
ATOM   1030  CA  HIS A 171      -2.623  38.523   7.138  1.00 11.15           C  
ANISOU 1030  CA  HIS A 171     1878   1413    944     54   -128     -8       C  
ATOM   1031  C   HIS A 171      -3.909  37.742   7.289  1.00 10.30           C  
ANISOU 1031  C   HIS A 171     1709   1236    967    188    -77    159       C  
ATOM   1032  O   HIS A 171      -4.110  37.024   8.276  1.00  9.95           O  
ANISOU 1032  O   HIS A 171     1641   1514    623     70    -37    -16       O  
ATOM   1033  CB  HIS A 171      -1.480  37.657   6.616  1.00 11.38           C  
ANISOU 1033  CB  HIS A 171     1877   1491    955     11      6    -83       C  
ATOM   1034  CG  HIS A 171      -1.748  37.006   5.288  1.00 12.16           C  
ANISOU 1034  CG  HIS A 171     2024   1534   1060    291   -136   -104       C  
ATOM   1035  ND1 HIS A 171      -2.201  35.709   5.162  1.00 11.40           N  
ANISOU 1035  ND1 HIS A 171     1845   1602    884    114    -79   -430       N  
ATOM   1036  CD2 HIS A 171      -1.692  37.516   4.030  1.00 13.73           C  
ANISOU 1036  CD2 HIS A 171     2834   1473    909    123    144    207       C  
ATOM   1037  CE1 HIS A 171      -2.351  35.426   3.874  1.00 13.16           C  
ANISOU 1037  CE1 HIS A 171     2402   1385   1211    -72    -28   -330       C  
ATOM   1038  NE2 HIS A 171      -2.028  36.503   3.169  1.00 14.37           N  
ANISOU 1038  NE2 HIS A 171     2525   1704   1230    133     16   -400       N  
ATOM   1039  N   TYR A 172      -4.801  37.860   6.310  1.00 10.67           N  
ANISOU 1039  N   TYR A 172     1818   1535    699    218   -169    232       N  
ATOM   1040  CA  TYR A 172      -6.043  37.059   6.273  1.00 11.39           C  
ANISOU 1040  CA  TYR A 172     1717   1553   1055    227   -164     85       C  
ATOM   1041  C   TYR A 172      -5.823  35.713   5.597  1.00 11.09           C  
ANISOU 1041  C   TYR A 172     1665   1470   1076    296   -243    105       C  
ATOM   1042  O   TYR A 172      -5.451  35.632   4.416  1.00 14.13           O  
ANISOU 1042  O   TYR A 172     2295   1745   1325     23     87     86       O  
ATOM   1043  CB  TYR A 172      -7.152  37.794   5.537  1.00 12.28           C  
ANISOU 1043  CB  TYR A 172     1829   1725   1111    248   -303     59       C  
ATOM   1044  CG  TYR A 172      -8.464  37.060   5.551  1.00 12.45           C  
ANISOU 1044  CG  TYR A 172     2186   1674    870    322   -524    -71       C  
ATOM   1045  CD1 TYR A 172      -9.135  36.851   6.755  1.00 13.88           C  
ANISOU 1045  CD1 TYR A 172     1760   2307   1207    125   -280    106       C  
ATOM   1046  CD2 TYR A 172      -9.001  36.493   4.395  1.00 16.95           C  
ANISOU 1046  CD2 TYR A 172     2753   2216   1472   -224   -606     95       C  
ATOM   1047  CE1 TYR A 172     -10.346  36.188   6.794  1.00 19.61           C  
ANISOU 1047  CE1 TYR A 172     2135   2738   2574    371   -324    143       C  
ATOM   1048  CE2 TYR A 172     -10.220  35.839   4.434  1.00 17.11           C  
ANISOU 1048  CE2 TYR A 172     2408   2080   2012    -34  -1181    385       C  
ATOM   1049  CZ  TYR A 172     -10.891  35.684   5.639  1.00 19.88           C  
ANISOU 1049  CZ  TYR A 172     2507   2253   2790     78   -803    633       C  
ATOM   1050  OH  TYR A 172     -12.119  35.012   5.677  1.00 25.82           O  
ANISOU 1050  OH  TYR A 172     2520   3256   4033   -466  -1403   1164       O  
ATOM   1051  N   ASP A 173      -5.942  34.657   6.392  1.00 11.06           N  
ANISOU 1051  N   ASP A 173     1982   1381    837    193   -233     87       N  
ATOM   1052  CA  ASP A 173      -5.811  33.293   5.897  1.00 10.03           C  
ANISOU 1052  CA  ASP A 173     1777   1270    763    112    356     32       C  
ATOM   1053  C   ASP A 173      -7.168  32.836   5.371  1.00 12.13           C  
ANISOU 1053  C   ASP A 173     1836   1822    950     26   -129   -308       C  
ATOM   1054  O   ASP A 173      -8.122  32.676   6.111  1.00 11.38           O  
ANISOU 1054  O   ASP A 173     1590   1906    825     53   -192   -281       O  
ATOM   1055  CB  ASP A 173      -5.363  32.351   7.019  1.00 10.84           C  
ANISOU 1055  CB  ASP A 173     1638   1271   1207     88     64    131       C  
ATOM   1056  CG  ASP A 173      -5.240  30.949   6.556  1.00 10.29           C  
ANISOU 1056  CG  ASP A 173     1496   1092   1320     84    -81    -62       C  
ATOM   1057  OD1 ASP A 173      -4.536  30.758   5.548  1.00 14.21           O  
ANISOU 1057  OD1 ASP A 173     2461   1726   1213    395    320   -246       O  
ATOM   1058  OD2 ASP A 173      -5.764  30.006   7.183  1.00 11.38           O  
ANISOU 1058  OD2 ASP A 173     1690   1610   1021   -404    142   -226       O  
ATOM   1059  N   GLU A 174      -7.269  32.626   4.065  1.00 14.80           N  
ANISOU 1059  N   GLU A 174     2811   1861    950   -205   -420   -321       N  
ATOM   1060  CA  GLU A 174      -8.518  32.268   3.433  1.00 16.41           C  
ANISOU 1060  CA  GLU A 174     3007   1910   1315     55   -621    384       C  
ATOM   1061  C   GLU A 174      -9.081  30.896   3.836  1.00 14.91           C  
ANISOU 1061  C   GLU A 174     2591   1812   1262     93   -537     96       C  
ATOM   1062  O   GLU A 174     -10.289  30.738   3.949  1.00 21.72           O  
ANISOU 1062  O   GLU A 174     2659   2578   3013    172  -1325    122       O  
ATOM   1063  CB  GLU A 174      -8.347  32.362   1.896  1.00 18.31           C  
ANISOU 1063  CB  GLU A 174     3893   1985   1075     86   -719    417       C  
ATOM   1064  CG  GLU A 174      -7.662  33.680   1.374  1.00 20.57           C  
ANISOU 1064  CG  GLU A 174     3490   2747   1578    -76   -924    239       C  
ATOM   1065  CD  GLU A 174      -7.554  33.759  -0.173  1.00 33.80           C  
ANISOU 1065  CD  GLU A 174     5052   4981   2807   -461    583    700       C  
ATOM   1066  OE1 GLU A 174      -8.621  33.790  -0.905  1.00 31.95           O  
ANISOU 1066  OE1 GLU A 174     6477   3158   2502  -1106   1450    195       O  
ATOM   1067  OE2 GLU A 174      -6.371  33.833  -0.629  1.00 32.09           O  
ANISOU 1067  OE2 GLU A 174     4068   5465   2660  -1489   -317    350       O  
ATOM   1068  N   VAL A 175      -8.205  29.960   4.183  1.00 12.60           N  
ANISOU 1068  N   VAL A 175     2406   1643    737     66   -586    109       N  
ATOM   1069  CA  VAL A 175      -8.649  28.624   4.560  1.00 11.62           C  
ANISOU 1069  CA  VAL A 175     1980   1693    740   -116   -342    287       C  
ATOM   1070  C   VAL A 175      -9.332  28.658   5.937  1.00 11.36           C  
ANISOU 1070  C   VAL A 175     1545   1664   1104   -393   -277    211       C  
ATOM   1071  O   VAL A 175     -10.428  28.155   6.090  1.00 13.59           O  
ANISOU 1071  O   VAL A 175     1592   2505   1065   -362   -373   -204       O  
ATOM   1072  CB  VAL A 175      -7.469  27.612   4.530  1.00 12.00           C  
ANISOU 1072  CB  VAL A 175     2027   1705    826   -338   -303    -20       C  
ATOM   1073  CG1 VAL A 175      -7.808  26.332   5.318  1.00 11.67           C  
ANISOU 1073  CG1 VAL A 175     2109   1354    968   -364   -140    189       C  
ATOM   1074  CG2 VAL A 175      -7.048  27.333   3.107  1.00 15.02           C  
ANISOU 1074  CG2 VAL A 175     2893   1917    896   -142    -19   -112       C  
ATOM   1075  N   SER A 176      -8.637  29.212   6.941  1.00 10.92           N  
ANISOU 1075  N   SER A 176     1564   1836    749   -334   -144   -184       N  
ATOM   1076  CA  SER A 176      -9.189  29.254   8.308  1.00 12.10           C  
ANISOU 1076  CA  SER A 176     1541   1882   1172      7    -13    -42       C  
ATOM   1077  C   SER A 176     -10.172  30.389   8.528  1.00 12.15           C  
ANISOU 1077  C   SER A 176     1270   2092   1252   -182   -252    -91       C  
ATOM   1078  O   SER A 176     -10.882  30.417   9.528  1.00 15.04           O  
ANISOU 1078  O   SER A 176     1831   2440   1442   -124    208    212       O  
ATOM   1079  CB  SER A 176      -8.051  29.374   9.324  1.00 11.25           C  
ANISOU 1079  CB  SER A 176     1764   1902    609    -57    -20    103       C  
ATOM   1080  OG  SER A 176      -7.388  30.618   9.218  1.00 11.06           O  
ANISOU 1080  OG  SER A 176     1688   1587    924    -41   -138    -49       O  
ATOM   1081  N   GLN A 177     -10.136  31.380   7.631  1.00 11.65           N  
ANISOU 1081  N   GLN A 177     1622   2089    714     31   -196     89       N  
ATOM   1082  CA  GLN A 177     -10.932  32.594   7.785  1.00 12.19           C  
ANISOU 1082  CA  GLN A 177     1464   2335    832    175   -506   -133       C  
ATOM   1083  C   GLN A 177     -10.580  33.292   9.075  1.00 14.90           C  
ANISOU 1083  C   GLN A 177     1978   2355   1328    479   -293   -255       C  
ATOM   1084  O   GLN A 177     -11.447  33.841   9.757  1.00 21.01           O  
ANISOU 1084  O   GLN A 177     2105   3961   1914    934   -367   -841       O  
ATOM   1085  CB  GLN A 177     -12.442  32.349   7.654  1.00 16.87           C  
ANISOU 1085  CB  GLN A 177     2162   2768   1476    363   -444     79       C  
ATOM   1086  CG  GLN A 177     -12.791  31.699   6.337  1.00 19.86           C  
ANISOU 1086  CG  GLN A 177     2216   3129   2200     51   -647   -231       C  
ATOM   1087  CD  GLN A 177     -14.261  31.521   6.132  1.00 26.28           C  
ANISOU 1087  CD  GLN A 177     3034   3805   3145     54    -84   -480       C  
ATOM   1088  OE1 GLN A 177     -15.057  32.387   6.473  1.00 32.99           O  
ANISOU 1088  OE1 GLN A 177     2816   6487   3231    599  -1308   -749       O  
ATOM   1089  NE2 GLN A 177     -14.637  30.358   5.610  1.00 30.81           N  
ANISOU 1089  NE2 GLN A 177     2939   5494   3272   -425   -423  -1007       N  
ATOM   1090  N   MET A 178      -9.291  33.360   9.349  1.00 11.51           N  
ANISOU 1090  N   MET A 178     1570   2008    795     84   -117   -194       N  
ATOM   1091  CA  MET A 178      -8.776  34.091  10.502  1.00 11.75           C  
ANISOU 1091  CA  MET A 178     1828   1601   1035     23     12   -315       C  
ATOM   1092  C   MET A 178      -7.784  35.154  10.021  1.00  9.44           C  
ANISOU 1092  C   MET A 178     1250   1639    695     72    -30    -13       C  
ATOM   1093  O   MET A 178      -7.009  34.909   9.084  1.00 10.92           O  
ANISOU 1093  O   MET A 178     1560   1983    603    110    163   -109       O  
ATOM   1094  CB  MET A 178      -8.087  33.118  11.487  1.00 12.09           C  
ANISOU 1094  CB  MET A 178     1765   1849    976   -130    -96   -118       C  
ATOM   1095  CG  MET A 178      -9.057  32.139  12.128  1.00 12.11           C  
ANISOU 1095  CG  MET A 178     2007   2052    541     53     -9   -243       C  
ATOM   1096  SD  MET A 178      -8.465  31.188  13.479  1.00 14.78           S  
ANISOU 1096  SD  MET A 178     2320   2239   1055    -73   -257   -246       S  
ATOM   1097  CE  MET A 178      -7.012  30.466  12.787  1.00 15.80           C  
ANISOU 1097  CE  MET A 178     2091   2923    986    928   -260    -21       C  
ATOM   1098  N   VAL A 179      -7.770  36.289  10.712  1.00 10.31           N  
ANISOU 1098  N   VAL A 179     1535   1670    710     60   -216   -240       N  
ATOM   1099  CA  VAL A 179      -6.718  37.293  10.570  1.00 10.08           C  
ANISOU 1099  CA  VAL A 179     1497   1640    691    261     76   -201       C  
ATOM   1100  C   VAL A 179      -5.659  36.948  11.600  1.00  9.71           C  
ANISOU 1100  C   VAL A 179     1178   1684    827    159     22   -128       C  
ATOM   1101  O   VAL A 179      -5.865  37.121  12.806  1.00 11.86           O  
ANISOU 1101  O   VAL A 179     1603   2151    750    217     22   -284       O  
ATOM   1102  CB  VAL A 179      -7.218  38.764  10.712  1.00 12.55           C  
ANISOU 1102  CB  VAL A 179     1678   1883   1205     96    -84   -352       C  
ATOM   1103  CG1 VAL A 179      -6.043  39.739  10.682  1.00 13.31           C  
ANISOU 1103  CG1 VAL A 179     2049   1749   1258    -38    143   -164       C  
ATOM   1104  CG2 VAL A 179      -8.250  39.106   9.610  1.00 13.98           C  
ANISOU 1104  CG2 VAL A 179     1947   2269   1095    313   -663   -326       C  
ATOM   1105  N   ILE A 180      -4.562  36.396  11.111  1.00  9.70           N  
ANISOU 1105  N   ILE A 180     1433   1892    357    241   -113    -33       N  
ATOM   1106  CA  ILE A 180      -3.473  35.937  11.912  1.00  9.55           C  
ANISOU 1106  CA  ILE A 180     1288   1578    759    217     71      3       C  
ATOM   1107  C   ILE A 180      -2.393  36.970  12.014  1.00  9.98           C  
ANISOU 1107  C   ILE A 180     1470   1529    792    -53     26   -311       C  
ATOM   1108  O   ILE A 180      -1.919  37.489  10.987  1.00 11.05           O  
ANISOU 1108  O   ILE A 180     1679   1779    740   -194     60     -3       O  
ATOM   1109  CB  ILE A 180      -2.911  34.620  11.320  1.00  9.90           C  
ANISOU 1109  CB  ILE A 180     1669   1687    404    -84   -201   -131       C  
ATOM   1110  CG1 ILE A 180      -4.033  33.521  11.381  1.00 12.91           C  
ANISOU 1110  CG1 ILE A 180     1635   2074   1196    322   -588   -356       C  
ATOM   1111  CG2 ILE A 180      -1.653  34.155  12.098  1.00 12.53           C  
ANISOU 1111  CG2 ILE A 180     1403   1881   1476    258   -319    -91       C  
ATOM   1112  CD1 ILE A 180      -3.691  32.270  10.660  1.00 15.71           C  
ANISOU 1112  CD1 ILE A 180     2405   1903   1659    335   -601   -571       C  
ATOM   1113  N   ALA A 181      -1.945  37.261  13.250  1.00 10.36           N  
ANISOU 1113  N   ALA A 181     1456   1754    724    -28    -20     -5       N  
ATOM   1114  CA  ALA A 181      -0.867  38.222  13.494  1.00 10.31           C  
ANISOU 1114  CA  ALA A 181     1275   1877    765    -80     14   -103       C  
ATOM   1115  C   ALA A 181       0.299  37.542  14.211  1.00  9.86           C  
ANISOU 1115  C   ALA A 181     1338   1522    884   -136    -97     35       C  
ATOM   1116  O   ALA A 181       0.124  36.942  15.257  1.00 11.09           O  
ANISOU 1116  O   ALA A 181     1473   1744    996    -59    190     59       O  
ATOM   1117  CB  ALA A 181      -1.359  39.419  14.338  1.00 11.91           C  
ANISOU 1117  CB  ALA A 181     1948   1670    908    336    -62   -115       C  
ATOM   1118  N   ALA A 182       1.473  37.568  13.578  1.00  9.78           N  
ANISOU 1118  N   ALA A 182     1317   1692    704   -122     42   -311       N  
ATOM   1119  CA  ALA A 182       2.719  37.198  14.201  1.00  8.33           C  
ANISOU 1119  CA  ALA A 182     1169   1269    726    -19     82     17       C  
ATOM   1120  C   ALA A 182       3.323  38.482  14.737  1.00 10.13           C  
ANISOU 1120  C   ALA A 182     1496   1290   1063    -51     25   -294       C  
ATOM   1121  O   ALA A 182       3.419  39.469  13.995  1.00 10.18           O  
ANISOU 1121  O   ALA A 182     1734   1323    808   -151      4   -118       O  
ATOM   1122  CB  ALA A 182       3.696  36.492  13.233  1.00  9.84           C  
ANISOU 1122  CB  ALA A 182     1564   1611    563    226    216   -439       C  
ATOM   1123  N   THR A 183       3.796  38.459  15.987  1.00  9.33           N  
ANISOU 1123  N   THR A 183     1420   1191    932     54     34   -293       N  
ATOM   1124  CA  THR A 183       4.281  39.680  16.638  1.00 10.37           C  
ANISOU 1124  CA  THR A 183     1485   1250   1202    215    130   -159       C  
ATOM   1125  C   THR A 183       5.625  39.466  17.279  1.00  9.86           C  
ANISOU 1125  C   THR A 183     1456   1273   1016     74    307   -449       C  
ATOM   1126  O   THR A 183       5.948  38.366  17.709  1.00  9.80           O  
ANISOU 1126  O   THR A 183     1506   1355    860     33     30   -387       O  
ATOM   1127  CB  THR A 183       3.261  40.246  17.675  1.00 10.13           C  
ANISOU 1127  CB  THR A 183     1679   1101   1068    176     17   -318       C  
ATOM   1128  OG1 THR A 183       3.379  39.556  18.919  1.00 10.47           O  
ANISOU 1128  OG1 THR A 183     1572   1517    886    104    236   -197       O  
ATOM   1129  CG2 THR A 183       1.823  40.172  17.140  1.00 10.65           C  
ANISOU 1129  CG2 THR A 183     1297   1770    979    206    129   -438       C  
ATOM   1130  N   SER A 184       6.415  40.543  17.346  1.00  9.56           N  
ANISOU 1130  N   SER A 184     1580   1288    765     13    161   -310       N  
ATOM   1131  CA  SER A 184       7.683  40.508  18.070  1.00 10.11           C  
ANISOU 1131  CA  SER A 184     1388   1418   1033     26    209   -395       C  
ATOM   1132  C   SER A 184       7.859  41.825  18.832  1.00  9.24           C  
ANISOU 1132  C   SER A 184     1272   1465    771    130    176   -281       C  
ATOM   1133  O   SER A 184       7.339  42.868  18.435  1.00 11.21           O  
ANISOU 1133  O   SER A 184     1606   1468   1184      2     84   -478       O  
ATOM   1134  CB  SER A 184       8.890  40.264  17.174  1.00 11.08           C  
ANISOU 1134  CB  SER A 184     1493   1666   1050   -201     94   -265       C  
ATOM   1135  OG  SER A 184       8.868  38.996  16.549  1.00 10.89           O  
ANISOU 1135  OG  SER A 184     1731   1568    836    -86    150   -627       O  
ATOM   1136  N   TYR A 185       8.636  41.722  19.901  1.00 10.51           N  
ANISOU 1136  N   TYR A 185     1518   1611    864      7    -25   -414       N  
ATOM   1137  CA  TYR A 185       8.957  42.838  20.785  1.00 12.21           C  
ANISOU 1137  CA  TYR A 185     1685   1584   1367   -159    104   -515       C  
ATOM   1138  C   TYR A 185      10.346  43.355  20.467  1.00 11.95           C  
ANISOU 1138  C   TYR A 185     1807   1644   1087   -134     59   -692       C  
ATOM   1139  O   TYR A 185      11.285  42.573  20.323  1.00 12.16           O  
ANISOU 1139  O   TYR A 185     1601   1830   1189    -26      4   -613       O  
ATOM   1140  CB  TYR A 185       8.881  42.331  22.228  1.00 12.95           C  
ANISOU 1140  CB  TYR A 185     1922   1827   1169    -91     49   -788       C  
ATOM   1141  CG  TYR A 185       7.494  42.009  22.701  1.00 12.82           C  
ANISOU 1141  CG  TYR A 185     1652   2018   1198     56     27   -443       C  
ATOM   1142  CD1 TYR A 185       6.728  42.956  23.393  1.00 13.42           C  
ANISOU 1142  CD1 TYR A 185     2011   1805   1281     56   -140   -834       C  
ATOM   1143  CD2 TYR A 185       6.890  40.775  22.396  1.00 12.28           C  
ANISOU 1143  CD2 TYR A 185     1610   1923   1131     39    353   -744       C  
ATOM   1144  CE1 TYR A 185       5.419  42.707  23.704  1.00 14.42           C  
ANISOU 1144  CE1 TYR A 185     1893   1740   1844    100    428   -954       C  
ATOM   1145  CE2 TYR A 185       5.576  40.517  22.730  1.00 10.66           C  
ANISOU 1145  CE2 TYR A 185     1951   1664    434     60     58   -499       C  
ATOM   1146  CZ  TYR A 185       4.833  41.504  23.363  1.00 12.35           C  
ANISOU 1146  CZ  TYR A 185     1785   1730   1177    -88     95   -651       C  
ATOM   1147  OH  TYR A 185       3.523  41.186  23.685  1.00 11.85           O  
ANISOU 1147  OH  TYR A 185     1627   2077    799    -97    154   -654       O  
ATOM   1148  N   TYR A 186      10.509  44.673  20.434  1.00 12.69           N  
ANISOU 1148  N   TYR A 186     1963   1742   1114   -206    139   -891       N  
ATOM   1149  CA  TYR A 186      11.799  45.230  20.116  1.00 12.62           C  
ANISOU 1149  CA  TYR A 186     1788   1790   1215   -243     95   -739       C  
ATOM   1150  C   TYR A 186      12.880  44.835  21.137  1.00 13.49           C  
ANISOU 1150  C   TYR A 186     1885   1978   1261   -296    206   -624       C  
ATOM   1151  O   TYR A 186      14.028  44.594  20.755  1.00 14.30           O  
ANISOU 1151  O   TYR A 186     1646   2114   1670   -372     23   -889       O  
ATOM   1152  CB  TYR A 186      11.746  46.756  19.901  1.00 13.55           C  
ANISOU 1152  CB  TYR A 186     2207   2137    803     51    266   -709       C  
ATOM   1153  CG  TYR A 186      10.951  47.153  18.682  1.00 13.48           C  
ANISOU 1153  CG  TYR A 186     1644   1892   1585    133    123   -322       C  
ATOM   1154  CD1 TYR A 186      11.515  47.069  17.420  1.00 17.24           C  
ANISOU 1154  CD1 TYR A 186     2251   3072   1227    249    589   -132       C  
ATOM   1155  CD2 TYR A 186       9.657  47.653  18.780  1.00 15.13           C  
ANISOU 1155  CD2 TYR A 186     2313   1978   1454     93    413   -512       C  
ATOM   1156  CE1 TYR A 186      10.770  47.403  16.265  1.00 20.21           C  
ANISOU 1156  CE1 TYR A 186     2389   3546   1744    510    571    234       C  
ATOM   1157  CE2 TYR A 186       8.929  48.040  17.658  1.00 17.28           C  
ANISOU 1157  CE2 TYR A 186     2022   2529   2011    263    407   -178       C  
ATOM   1158  CZ  TYR A 186       9.470  47.865  16.398  1.00 20.81           C  
ANISOU 1158  CZ  TYR A 186     2325   3692   1889    639     67    116       C  
ATOM   1159  OH  TYR A 186       8.750  48.227  15.284  1.00 25.02           O  
ANISOU 1159  OH  TYR A 186     2418   4309   2779    705    447    736       O  
ATOM   1160  N   THR A 187      12.518  44.691  22.423  1.00 13.57           N  
ANISOU 1160  N   THR A 187     1918   2176   1060    -23    126   -757       N  
ATOM   1161  CA ATHR A 187      13.493  44.219  23.423  0.60 16.47           C  
ANISOU 1161  CA ATHR A 187     2042   2545   1671   -124    -17   -586       C  
ATOM   1162  CA BTHR A 187      13.488  44.274  23.404  0.40 14.93           C  
ANISOU 1162  CA BTHR A 187     1925   2459   1286   -106      2   -582       C  
ATOM   1163  C   THR A 187      14.072  42.886  23.026  1.00 14.84           C  
ANISOU 1163  C   THR A 187     1958   2292   1386   -194   -153   -593       C  
ATOM   1164  O   THR A 187      15.267  42.631  23.230  1.00 15.73           O  
ANISOU 1164  O   THR A 187     1891   2651   1434   -271   -167   -487       O  
ATOM   1165  CB ATHR A 187      12.916  43.999  24.838  0.60 18.87           C  
ANISOU 1165  CB ATHR A 187     2286   2973   1911   -278    -17   -635       C  
ATOM   1166  CB BTHR A 187      12.860  44.316  24.819  0.40 15.15           C  
ANISOU 1166  CB BTHR A 187     2045   2585   1125   -240    -25   -728       C  
ATOM   1167  OG1ATHR A 187      11.657  43.310  24.758  0.60 17.97           O  
ANISOU 1167  OG1ATHR A 187     2000   2522   2305   -459     67   -274       O  
ATOM   1168  OG1BTHR A 187      13.892  44.409  25.803  0.40 15.59           O  
ANISOU 1168  OG1BTHR A 187     2010   2868   1043    139   -260  -1010       O  
ATOM   1169  CG2ATHR A 187      12.791  45.300  25.564  0.60 18.52           C  
ANISOU 1169  CG2ATHR A 187     2487   2356   2194    -21   -623   -935       C  
ATOM   1170  CG2BTHR A 187      11.999  43.074  25.068  0.40 13.71           C  
ANISOU 1170  CG2BTHR A 187     1883   2543    783   -177    -27    -60       C  
ATOM   1171  N   ASP A 188      13.224  42.000  22.503  1.00 13.53           N  
ANISOU 1171  N   ASP A 188     1743   2185   1211   -304    -37   -618       N  
ATOM   1172  CA  ASP A 188      13.642  40.671  22.143  1.00 13.76           C  
ANISOU 1172  CA  ASP A 188     1744   2128   1354   -200   -204   -295       C  
ATOM   1173  C   ASP A 188      14.564  40.721  20.902  1.00 14.64           C  
ANISOU 1173  C   ASP A 188     1598   2235   1728   -154     26   -330       C  
ATOM   1174  O   ASP A 188      15.539  39.968  20.813  1.00 14.83           O  
ANISOU 1174  O   ASP A 188     1835   2240   1559    -47   -182   -441       O  
ATOM   1175  CB  ASP A 188      12.447  39.756  21.887  1.00 12.30           C  
ANISOU 1175  CB  ASP A 188     1492   2183    997   -131    -96   -420       C  
ATOM   1176  CG  ASP A 188      11.662  39.443  23.135  1.00 15.90           C  
ANISOU 1176  CG  ASP A 188     1935   2692   1412   -411    243   -352       C  
ATOM   1177  OD1 ASP A 188      12.222  39.633  24.260  1.00 18.61           O  
ANISOU 1177  OD1 ASP A 188     2168   3322   1581   -672   -349     28       O  
ATOM   1178  OD2 ASP A 188      10.517  38.969  22.973  1.00 12.49           O  
ANISOU 1178  OD2 ASP A 188     1937   2034    772   -162    -38   -341       O  
ATOM   1179  N   ILE A 189      14.213  41.548  19.930  1.00 13.17           N  
ANISOU 1179  N   ILE A 189     1713   2139   1152   -207    150   -561       N  
ATOM   1180  CA  ILE A 189      15.058  41.674  18.721  1.00 15.10           C  
ANISOU 1180  CA  ILE A 189     1904   2099   1731    -51    220   -395       C  
ATOM   1181  C   ILE A 189      16.434  42.174  19.152  1.00 15.02           C  
ANISOU 1181  C   ILE A 189     2051   2017   1639   -195     55   -373       C  
ATOM   1182  O   ILE A 189      17.475  41.650  18.722  1.00 15.52           O  
ANISOU 1182  O   ILE A 189     1901   2267   1728   -114    152   -434       O  
ATOM   1183  CB  ILE A 189      14.413  42.607  17.670  1.00 13.19           C  
ANISOU 1183  CB  ILE A 189     1954   1629   1427   -315    214   -507       C  
ATOM   1184  CG1 ILE A 189      13.015  42.119  17.281  1.00 13.97           C  
ANISOU 1184  CG1 ILE A 189     2005   1650   1651   -239    197   -684       C  
ATOM   1185  CG2 ILE A 189      15.286  42.750  16.444  1.00 17.22           C  
ANISOU 1185  CG2 ILE A 189     2598   2502   1442   -473    617   -136       C  
ATOM   1186  CD1 ILE A 189      12.199  43.142  16.463  1.00 16.35           C  
ANISOU 1186  CD1 ILE A 189     2517   1753   1940     93    -81   -677       C  
ATOM   1187  N   ASN A 190      16.456  43.129  20.089  1.00 14.87           N  
ANISOU 1187  N   ASN A 190     1785   2177   1689   -407    274   -562       N  
ATOM   1188  CA  ASN A 190      17.715  43.654  20.586  1.00 15.93           C  
ANISOU 1188  CA  ASN A 190     2015   2378   1660   -446    186   -560       C  
ATOM   1189  C   ASN A 190      18.531  42.579  21.313  1.00 16.67           C  
ANISOU 1189  C   ASN A 190     2004   2580   1748   -477    101   -672       C  
ATOM   1190  O   ASN A 190      19.741  42.436  21.095  1.00 19.36           O  
ANISOU 1190  O   ASN A 190     1818   3269   2266   -393    202   -693       O  
ATOM   1191  CB  ASN A 190      17.460  44.845  21.519  1.00 16.27           C  
ANISOU 1191  CB  ASN A 190     2120   2197   1862   -521     -3   -836       C  
ATOM   1192  CG  ASN A 190      16.922  46.077  20.796  1.00 18.97           C  
ANISOU 1192  CG  ASN A 190     2516   2515   2175   -754     85   -628       C  
ATOM   1193  OD1 ASN A 190      17.010  46.185  19.586  1.00 22.04           O  
ANISOU 1193  OD1 ASN A 190     3832   2797   1745   -799     66   -572       O  
ATOM   1194  ND2 ASN A 190      16.355  47.024  21.562  1.00 24.81           N  
ANISOU 1194  ND2 ASN A 190     2841   3017   3567   -342    320  -1215       N  
ATOM   1195  N   THR A 191      17.870  41.778  22.136  1.00 16.39           N  
ANISOU 1195  N   THR A 191     1848   2683   1693   -256    249   -685       N  
ATOM   1196  CA  THR A 191      18.546  40.675  22.824  1.00 17.87           C  
ANISOU 1196  CA  THR A 191     1966   2787   2035   -286     21   -363       C  
ATOM   1197  C   THR A 191      19.195  39.719  21.830  1.00 18.40           C  
ANISOU 1197  C   THR A 191     1840   2923   2225   -283   -164   -396       C  
ATOM   1198  O   THR A 191      20.362  39.296  21.995  1.00 19.39           O  
ANISOU 1198  O   THR A 191     1972   2917   2476   -175   -251   -297       O  
ATOM   1199  CB  THR A 191      17.538  39.930  23.746  1.00 19.38           C  
ANISOU 1199  CB  THR A 191     2419   3032   1911   -209    228   -313       C  
ATOM   1200  OG1 THR A 191      17.144  40.814  24.806  1.00 21.60           O  
ANISOU 1200  OG1 THR A 191     2716   3366   2122     41   -231   -424       O  
ATOM   1201  CG2 THR A 191      18.162  38.625  24.331  1.00 20.87           C  
ANISOU 1201  CG2 THR A 191     3022   3462   1443     73   -255    179       C  
ATOM   1202  N   GLU A 192      18.432  39.330  20.820  1.00 16.87           N  
ANISOU 1202  N   GLU A 192     1632   2828   1950   -134   -107   -273       N  
ATOM   1203  CA  GLU A 192      18.931  38.395  19.811  1.00 16.15           C  
ANISOU 1203  CA  GLU A 192     1826   2616   1691   -115     37   -284       C  
ATOM   1204  C   GLU A 192      20.115  38.937  18.995  1.00 16.76           C  
ANISOU 1204  C   GLU A 192     1806   2646   1916    -86     34   -400       C  
ATOM   1205  O   GLU A 192      20.944  38.172  18.506  1.00 19.57           O  
ANISOU 1205  O   GLU A 192     1811   2862   2763    -65    225   -472       O  
ATOM   1206  CB  GLU A 192      17.806  38.042  18.833  1.00 16.06           C  
ANISOU 1206  CB  GLU A 192     1698   2883   1522    -51    -28   -341       C  
ATOM   1207  CG  GLU A 192      16.611  37.301  19.429  1.00 16.23           C  
ANISOU 1207  CG  GLU A 192     1547   2600   2018   -170      2   -425       C  
ATOM   1208  CD  GLU A 192      15.404  37.329  18.533  1.00 18.58           C  
ANISOU 1208  CD  GLU A 192     1518   3290   2251    136    -66   -266       C  
ATOM   1209  OE1 GLU A 192      15.595  37.725  17.363  1.00 24.22           O  
ANISOU 1209  OE1 GLU A 192     1984   5282   1935    -48      9   -215       O  
ATOM   1210  OE2 GLU A 192      14.279  37.072  19.010  1.00 16.39           O  
ANISOU 1210  OE2 GLU A 192     1750   2534   1941   -167   -194   -547       O  
ATOM   1211  N   ASN A 193      20.181  40.253  18.859  1.00 17.48           N  
ANISOU 1211  N   ASN A 193     1915   2763   1961   -295    253   -487       N  
ATOM   1212  CA  ASN A 193      21.214  40.922  18.081  1.00 16.91           C  
ANISOU 1212  CA  ASN A 193     1893   2639   1890   -370    292   -430       C  
ATOM   1213  C   ASN A 193      22.346  41.471  18.975  1.00 17.95           C  
ANISOU 1213  C   ASN A 193     2042   2868   1907   -486    308   -431       C  
ATOM   1214  O   ASN A 193      23.250  42.146  18.472  1.00 20.75           O  
ANISOU 1214  O   ASN A 193     2340   2987   2557   -767    349   -697       O  
ATOM   1215  CB  ASN A 193      20.573  42.048  17.272  1.00 16.20           C  
ANISOU 1215  CB  ASN A 193     1814   2597   1744   -480    311   -387       C  
ATOM   1216  CG  ASN A 193      19.806  41.523  16.069  1.00 18.36           C  
ANISOU 1216  CG  ASN A 193     2068   2750   2156   -335    421  -1055       C  
ATOM   1217  OD1 ASN A 193      20.409  40.853  15.221  1.00 25.93           O  
ANISOU 1217  OD1 ASN A 193     3150   4049   2652    407    586  -1521       O  
ATOM   1218  ND2 ASN A 193      18.619  42.025  15.850  1.00 19.54           N  
ANISOU 1218  ND2 ASN A 193     2107   3301   2016   -496    498   -511       N  
ATOM   1219  N   LYS A 194      22.319  41.152  20.282  1.00 20.73           N  
ANISOU 1219  N   LYS A 194     1950   3570   2356   -608    129   -941       N  
ATOM   1220  CA  LYS A 194      23.288  41.711  21.228  1.00 22.15           C  
ANISOU 1220  CA  LYS A 194     2307   3674   2433   -500    -11   -930       C  
ATOM   1221  C   LYS A 194      24.719  41.302  20.883  1.00 22.79           C  
ANISOU 1221  C   LYS A 194     2128   3729   2801   -481   -178  -1026       C  
ATOM   1222  O   LYS A 194      25.636  42.101  21.058  1.00 25.45           O  
ANISOU 1222  O   LYS A 194     2099   4467   3101   -692   -319  -1129       O  
ATOM   1223  CB  LYS A 194      22.933  41.318  22.667  1.00 23.93           C  
ANISOU 1223  CB  LYS A 194     2319   4120   2654   -854   -365   -943       C  
ATOM   1224  CG  LYS A 194      23.763  42.049  23.718  1.00 28.76           C  
ANISOU 1224  CG  LYS A 194     2946   4894   3086   -341   -387  -1009       C  
ATOM   1225  CD  LYS A 194      23.189  41.863  25.098  1.00 34.67           C  
ANISOU 1225  CD  LYS A 194     4197   5703   3271   -341    225   -946       C  
ATOM   1226  N   ALA A 195      24.945  40.037  20.532  1.00 23.37           N  
ANISOU 1226  N   ALA A 195     1933   3960   2985   -280    -11   -854       N  
ATOM   1227  CA  ALA A 195      26.293  39.592  20.174  1.00 24.81           C  
ANISOU 1227  CA  ALA A 195     2309   3922   3194   -165   -187   -704       C  
ATOM   1228  C   ALA A 195      26.830  40.298  18.925  1.00 25.01           C  
ANISOU 1228  C   ALA A 195     2265   4112   3124   -217     75   -839       C  
ATOM   1229  O   ALA A 195      28.028  40.650  18.878  1.00 27.94           O  
ANISOU 1229  O   ALA A 195     2474   4570   3569   -439   -112   -921       O  
ATOM   1230  CB  ALA A 195      26.333  38.076  20.023  1.00 26.14           C  
ANISOU 1230  CB  ALA A 195     2758   3964   3209    138   -100   -683       C  
ATOM   1231  N   ILE A 196      25.973  40.480  17.907  1.00 24.25           N  
ANISOU 1231  N   ILE A 196     2339   3661   3211   -406    178   -660       N  
ATOM   1232  CA  ILE A 196      26.318  41.277  16.730  1.00 23.42           C  
ANISOU 1232  CA  ILE A 196     2344   3329   3225   -541    433   -747       C  
ATOM   1233  C   ILE A 196      26.736  42.706  17.123  1.00 27.24           C  
ANISOU 1233  C   ILE A 196     2691   3680   3976   -714    418   -647       C  
ATOM   1234  O   ILE A 196      27.774  43.216  16.676  1.00 30.11           O  
ANISOU 1234  O   ILE A 196     2729   4210   4502   -940    559   -444       O  
ATOM   1235  CB  ILE A 196      25.180  41.293  15.684  1.00 24.12           C  
ANISOU 1235  CB  ILE A 196     2782   3063   3320   -453    417   -392       C  
ATOM   1236  CG1 ILE A 196      25.042  39.915  15.027  1.00 23.71           C  
ANISOU 1236  CG1 ILE A 196     2672   2979   3356     74    752   -503       C  
ATOM   1237  CG2 ILE A 196      25.409  42.379  14.644  1.00 25.11           C  
ANISOU 1237  CG2 ILE A 196     2556   3757   3225   -584    553   -173       C  
ATOM   1238  CD1 ILE A 196      23.708  39.698  14.315  1.00 25.64           C  
ANISOU 1238  CD1 ILE A 196     2713   2920   4107    -67    707   -488       C  
ATOM   1239  N   LYS A 197      25.958  43.312  18.010  1.00 27.88           N  
ANISOU 1239  N   LYS A 197     3003   3641   3947   -833    475   -769       N  
ATOM   1240  CA  LYS A 197      26.177  44.683  18.441  1.00 29.24           C  
ANISOU 1240  CA  LYS A 197     3350   3736   4020   -712    136   -640       C  
ATOM   1241  C   LYS A 197      27.491  44.803  19.182  1.00 30.61           C  
ANISOU 1241  C   LYS A 197     3405   4072   4151   -793     66   -599       C  
ATOM   1242  O   LYS A 197      28.303  45.699  18.897  1.00 33.36           O  
ANISOU 1242  O   LYS A 197     3682   4470   4523  -1280    -45   -702       O  
ATOM   1243  CB  LYS A 197      25.020  45.123  19.332  1.00 28.13           C  
ANISOU 1243  CB  LYS A 197     3427   3449   3808   -847    237  -1057       C  
ATOM   1244  N   GLU A 198      27.769  43.828  20.033  1.00 30.60           N  
ANISOU 1244  N   GLU A 198     2965   4451   4209   -856   -191   -550       N  
ATOM   1245  CA  GLU A 198      29.012  43.836  20.806  1.00 33.93           C  
ANISOU 1245  CA  GLU A 198     3238   5102   4550   -769   -341   -559       C  
ATOM   1246  C   GLU A 198      30.235  43.573  19.905  1.00 35.01           C  
ANISOU 1246  C   GLU A 198     3214   5349   4740   -693   -228   -550       C  
ATOM   1247  O   GLU A 198      31.308  44.161  20.098  1.00 37.13           O  
ANISOU 1247  O   GLU A 198     2777   6045   5282  -1045   -469   -514       O  
ATOM   1248  CB  GLU A 198      28.920  42.798  21.919  1.00 33.32           C  
ANISOU 1248  CB  GLU A 198     3326   5052   4279   -632   -791   -454       C  
ATOM   1249  N   GLY A 199      30.061  42.749  18.877  1.00 36.56           N  
ANISOU 1249  N   GLY A 199     3352   5557   4982   -617   -109   -482       N  
ATOM   1250  CA  GLY A 199      31.118  42.528  17.874  1.00 36.30           C  
ANISOU 1250  CA  GLY A 199     3319   5507   4964   -570    -43   -387       C  
ATOM   1251  C   GLY A 199      31.496  43.785  17.116  1.00 36.15           C  
ANISOU 1251  C   GLY A 199     3226   5417   5093   -605    119   -287       C  
ATOM   1252  O   GLY A 199      32.686  44.029  16.851  1.00 38.61           O  
ANISOU 1252  O   GLY A 199     3040   6203   5424   -645    340    -62       O  
ATOM   1253  N   VAL A 200      30.497  44.587  16.762  1.00 35.78           N  
ANISOU 1253  N   VAL A 200     3085   5279   5228   -838    123   -175       N  
ATOM   1254  CA  VAL A 200      30.696  45.904  16.178  1.00 37.75           C  
ANISOU 1254  CA  VAL A 200     3450   5388   5503   -589    139   -129       C  
ATOM   1255  C   VAL A 200      31.268  46.896  17.188  1.00 33.96           C  
ANISOU 1255  C   VAL A 200     2165   5178   5558  -1250    -70   -167       C  
ATOM   1256  O   VAL A 200      32.367  47.473  16.954  1.00 38.43           O  
ANISOU 1256  O   VAL A 200     3089   5616   5895  -1219    734    189       O  
ATOM   1257  CB  VAL A 200      29.373  46.476  15.654  1.00 38.12           C  
ANISOU 1257  CB  VAL A 200     3678   5258   5546   -453     40    -94       C  
ATOM   1258  CG1 VAL A 200      29.613  47.827  15.003  1.00 42.36           C  
ANISOU 1258  CG1 VAL A 200     4766   5413   5913   -682    138     91       C  
ATOM   1259  CG2 VAL A 200      28.721  45.512  14.681  1.00 39.42           C  
ANISOU 1259  CG2 VAL A 200     3876   5275   5827   -522    176   -122       C  
TER    1260      VAL A 200                                                      
ATOM   1261  N   MET B  44      33.021  43.887   9.057  1.00 32.39           N  
ANISOU 1261  N   MET B  44     3510   3946   4848  -1216    566   -176       N  
ATOM   1262  CA  MET B  44      32.110  43.174   8.091  1.00 34.81           C  
ANISOU 1262  CA  MET B  44     3951   4467   4805   -648    648     12       C  
ATOM   1263  C   MET B  44      32.191  41.662   8.253  1.00 32.40           C  
ANISOU 1263  C   MET B  44     3607   4146   4554   -777    706    -49       C  
ATOM   1264  O   MET B  44      31.176  40.960   8.157  1.00 30.75           O  
ANISOU 1264  O   MET B  44     3260   4063   4358  -1314   1256    159       O  
ATOM   1265  CB  MET B  44      32.460  43.545   6.652  1.00 37.52           C  
ANISOU 1265  CB  MET B  44     4482   4754   5019   -457    482     60       C  
ATOM   1266  CG  MET B  44      31.293  43.563   5.709  1.00 42.63           C  
ANISOU 1266  CG  MET B  44     5257   5587   5351   -378    350     18       C  
ATOM   1267  SD  MET B  44      30.213  45.004   5.921  1.00 48.90           S  
ANISOU 1267  SD  MET B  44     6336   5400   6841   -784   -181   -266       S  
ATOM   1268  CE  MET B  44      31.173  46.010   7.079  1.00 41.89           C  
ANISOU 1268  CE  MET B  44     6364   3753   5797   -643    336   -746       C  
ATOM   1269  N   GLU B  45      33.385  41.157   8.536  1.00 30.69           N  
ANISOU 1269  N   GLU B  45     3419   3912   4329   -867    754     54       N  
ATOM   1270  CA  GLU B  45      33.586  39.735   8.768  1.00 31.66           C  
ANISOU 1270  CA  GLU B  45     3429   4007   4591   -675    514    -41       C  
ATOM   1271  C   GLU B  45      32.950  39.297  10.089  1.00 31.06           C  
ANISOU 1271  C   GLU B  45     3281   4047   4472   -961    484   -134       C  
ATOM   1272  O   GLU B  45      32.251  38.272  10.153  1.00 30.40           O  
ANISOU 1272  O   GLU B  45     2725   4164   4659  -1207    367   -244       O  
ATOM   1273  N   HIS B  46      33.101  40.120  11.118  1.00 32.80           N  
ANISOU 1273  N   HIS B  46     3622   4311   4526   -975    314   -197       N  
ATOM   1274  CA  HIS B  46      32.537  39.820  12.440  1.00 32.15           C  
ANISOU 1274  CA  HIS B  46     3700   4194   4319   -931    129   -333       C  
ATOM   1275  C   HIS B  46      31.006  39.960  12.376  1.00 30.87           C  
ANISOU 1275  C   HIS B  46     3530   4015   4184   -849    194   -310       C  
ATOM   1276  O   HIS B  46      30.264  39.163  12.984  1.00 29.50           O  
ANISOU 1276  O   HIS B  46     3719   3884   3603  -1274    213   -320       O  
ATOM   1277  CB  HIS B  46      33.150  40.738  13.516  1.00 33.62           C  
ANISOU 1277  CB  HIS B  46     3804   4397   4573  -1006    -37   -226       C  
ATOM   1278  N   LEU B  47      30.536  40.884  11.538  1.00 27.57           N  
ANISOU 1278  N   LEU B  47     3406   3446   3622   -895    295   -635       N  
ATOM   1279  CA  LEU B  47      29.103  41.076  11.316  1.00 27.54           C  
ANISOU 1279  CA  LEU B  47     3487   3238   3737   -640    442   -722       C  
ATOM   1280  C   LEU B  47      28.492  39.833  10.670  1.00 24.73           C  
ANISOU 1280  C   LEU B  47     2991   2871   3532   -812    614   -763       C  
ATOM   1281  O   LEU B  47      27.446  39.327  11.117  1.00 24.42           O  
ANISOU 1281  O   LEU B  47     2751   2824   3703   -851    910   -657       O  
ATOM   1282  CB  LEU B  47      28.870  42.249  10.385  1.00 29.60           C  
ANISOU 1282  CB  LEU B  47     3919   3499   3827   -467    420   -556       C  
ATOM   1283  CG  LEU B  47      27.447  42.627   9.987  1.00 29.02           C  
ANISOU 1283  CG  LEU B  47     3341   3857   3826   -457    659   -430       C  
ATOM   1284  CD1 LEU B  47      26.521  42.748  11.201  1.00 31.74           C  
ANISOU 1284  CD1 LEU B  47     3806   4320   3930   -219   1012   -247       C  
ATOM   1285  CD2 LEU B  47      27.481  43.967   9.241  1.00 34.91           C  
ANISOU 1285  CD2 LEU B  47     4185   4563   4513   -115    887    -86       C  
ATOM   1286  N   GLU B  48      29.095  39.393   9.572  1.00 23.56           N  
ANISOU 1286  N   GLU B  48     2803   2855   3292   -940    932   -654       N  
ATOM   1287  CA  GLU B  48      28.609  38.230   8.856  1.00 22.61           C  
ANISOU 1287  CA  GLU B  48     2238   3219   3132   -579    729   -778       C  
ATOM   1288  C   GLU B  48      28.626  36.980   9.736  1.00 19.62           C  
ANISOU 1288  C   GLU B  48     2041   2776   2637   -440    839   -870       C  
ATOM   1289  O   GLU B  48      27.651  36.228   9.790  1.00 19.91           O  
ANISOU 1289  O   GLU B  48     2262   2758   2545   -784    795   -952       O  
ATOM   1290  CB  GLU B  48      29.408  38.014   7.554  1.00 25.82           C  
ANISOU 1290  CB  GLU B  48     2780   3710   3316   -501    726   -625       C  
ATOM   1291  CG  GLU B  48      30.855  37.680   7.708  1.00 37.32           C  
ANISOU 1291  CG  GLU B  48     4455   4839   4882   -209    132   -402       C  
ATOM   1292  CD  GLU B  48      31.461  37.010   6.465  1.00 45.13           C  
ANISOU 1292  CD  GLU B  48     5849   6112   5186   -568    412   -572       C  
ATOM   1293  OE1 GLU B  48      30.827  36.077   5.901  1.00 38.26           O  
ANISOU 1293  OE1 GLU B  48     4998   5155   4383  -1584   1057   -484       O  
ATOM   1294  OE2 GLU B  48      32.629  37.343   6.133  1.00 53.70           O  
ANISOU 1294  OE2 GLU B  48     6793   7175   6432   -444    394   -140       O  
ATOM   1295  N   THR B  49      29.707  36.740  10.455  1.00 20.44           N  
ANISOU 1295  N   THR B  49     2109   2914   2741   -613    880   -714       N  
ATOM   1296  CA  THR B  49      29.768  35.611  11.387  1.00 21.94           C  
ANISOU 1296  CA  THR B  49     2172   3069   3093   -489    551   -533       C  
ATOM   1297  C   THR B  49      28.636  35.698  12.421  1.00 19.04           C  
ANISOU 1297  C   THR B  49     1948   2760   2525   -594    374   -859       C  
ATOM   1298  O   THR B  49      27.967  34.701  12.728  1.00 18.53           O  
ANISOU 1298  O   THR B  49     1894   2679   2466   -634    129   -565       O  
ATOM   1299  CB  THR B  49      31.127  35.533  12.090  1.00 24.74           C  
ANISOU 1299  CB  THR B  49     2465   3540   3395   -467    770   -470       C  
ATOM   1300  OG1 THR B  49      32.143  35.304  11.114  1.00 29.38           O  
ANISOU 1300  OG1 THR B  49     2417   4768   3975   -380    759   -770       O  
ATOM   1301  CG2 THR B  49      31.156  34.415  13.131  1.00 28.14           C  
ANISOU 1301  CG2 THR B  49     2515   3818   4358   -253    216   -213       C  
ATOM   1302  N   GLY B  50      28.394  36.897  12.935  1.00 18.78           N  
ANISOU 1302  N   GLY B  50     1853   2815   2466   -665    297   -850       N  
ATOM   1303  CA  GLY B  50      27.310  37.101  13.902  1.00 17.97           C  
ANISOU 1303  CA  GLY B  50     1875   2590   2360   -607    348   -808       C  
ATOM   1304  C   GLY B  50      25.954  36.771  13.316  1.00 16.72           C  
ANISOU 1304  C   GLY B  50     1963   2360   2028   -512    138   -614       C  
ATOM   1305  O   GLY B  50      25.067  36.235  14.002  1.00 17.21           O  
ANISOU 1305  O   GLY B  50     1942   2340   2257   -577    527   -565       O  
ATOM   1306  N   GLN B  51      25.736  37.204  12.083  1.00 16.57           N  
ANISOU 1306  N   GLN B  51     2031   2250   2012   -581    310   -548       N  
ATOM   1307  CA  GLN B  51      24.485  36.937  11.377  1.00 14.87           C  
ANISOU 1307  CA  GLN B  51     1826   1963   1860    -84    259   -430       C  
ATOM   1308  C   GLN B  51      24.274  35.459  11.138  1.00 14.88           C  
ANISOU 1308  C   GLN B  51     1695   2200   1759   -131    145   -346       C  
ATOM   1309  O   GLN B  51      23.151  34.984  11.291  1.00 14.75           O  
ANISOU 1309  O   GLN B  51     1777   2027   1801   -147    479   -401       O  
ATOM   1310  CB  GLN B  51      24.425  37.727  10.063  1.00 19.52           C  
ANISOU 1310  CB  GLN B  51     2589   2408   2418   -133    411   -189       C  
ATOM   1311  CG  GLN B  51      24.383  39.232  10.289  1.00 20.90           C  
ANISOU 1311  CG  GLN B  51     2803   2392   2743   -117   -143     96       C  
ATOM   1312  CD  GLN B  51      24.607  40.082   9.059  1.00 25.11           C  
ANISOU 1312  CD  GLN B  51     3365   3066   3107   -264     55   -238       C  
ATOM   1313  OE1 GLN B  51      25.272  39.653   8.087  1.00 24.73           O  
ANISOU 1313  OE1 GLN B  51     3376   2951   3069   -827    679   -329       O  
ATOM   1314  NE2 GLN B  51      24.201  41.362   9.164  1.00 27.00           N  
ANISOU 1314  NE2 GLN B  51     3068   2903   4286   -828   -569   -354       N  
ATOM   1315  N   TYR B  52      25.340  34.714  10.840  1.00 13.66           N  
ANISOU 1315  N   TYR B  52     1644   2084   1461   -246    323   -547       N  
ATOM   1316  CA  TYR B  52      25.220  33.284  10.715  1.00 13.40           C  
ANISOU 1316  CA  TYR B  52     1438   2009   1644   -264    285   -422       C  
ATOM   1317  C   TYR B  52      24.908  32.583  12.047  1.00 13.88           C  
ANISOU 1317  C   TYR B  52     1660   1747   1866   -244    127   -474       C  
ATOM   1318  O   TYR B  52      24.081  31.701  12.085  1.00 14.07           O  
ANISOU 1318  O   TYR B  52     1602   1914   1829   -212    385   -517       O  
ATOM   1319  CB  TYR B  52      26.475  32.676  10.079  1.00 15.00           C  
ANISOU 1319  CB  TYR B  52     1697   2021   1980   -298    529   -635       C  
ATOM   1320  CG  TYR B  52      26.862  33.246   8.715  1.00 13.79           C  
ANISOU 1320  CG  TYR B  52     1413   2204   1620   -294     72   -757       C  
ATOM   1321  CD1 TYR B  52      25.917  33.786   7.844  1.00 14.43           C  
ANISOU 1321  CD1 TYR B  52     1865   1958   1660   -265    225   -406       C  
ATOM   1322  CD2 TYR B  52      28.169  33.135   8.243  1.00 16.42           C  
ANISOU 1322  CD2 TYR B  52     1602   2964   1672   -382     79   -227       C  
ATOM   1323  CE1 TYR B  52      26.284  34.340   6.620  1.00 15.35           C  
ANISOU 1323  CE1 TYR B  52     1919   1995   1917   -225    268   -418       C  
ATOM   1324  CE2 TYR B  52      28.514  33.596   6.999  1.00 19.61           C  
ANISOU 1324  CE2 TYR B  52     1862   2784   2804   -188    732    134       C  
ATOM   1325  CZ  TYR B  52      27.593  34.226   6.206  1.00 18.34           C  
ANISOU 1325  CZ  TYR B  52     2041   2744   2180   -120    443   -115       C  
ATOM   1326  OH  TYR B  52      27.990  34.715   4.991  1.00 23.08           O  
ANISOU 1326  OH  TYR B  52     2552   3911   2306   -241    453    285       O  
ATOM   1327  N   LYS B  53      25.540  33.018  13.138  1.00 14.51           N  
ANISOU 1327  N   LYS B  53     1674   2189   1650   -402    341   -653       N  
ATOM   1328  CA  LYS B  53      25.252  32.464  14.454  1.00 14.23           C  
ANISOU 1328  CA  LYS B  53     1525   2197   1685   -281    -30   -478       C  
ATOM   1329  C   LYS B  53      23.818  32.762  14.863  1.00 12.16           C  
ANISOU 1329  C   LYS B  53     1547   1877   1193   -283    -83   -572       C  
ATOM   1330  O   LYS B  53      23.154  31.898  15.449  1.00 14.95           O  
ANISOU 1330  O   LYS B  53     1784   2053   1840   -320    282   -400       O  
ATOM   1331  CB  LYS B  53      26.258  32.973  15.505  1.00 16.96           C  
ANISOU 1331  CB  LYS B  53     1876   2639   1929   -221     98   -407       C  
ATOM   1332  CG  LYS B  53      27.665  32.416  15.190  1.00 24.94           C  
ANISOU 1332  CG  LYS B  53     2419   4066   2989   -279    185   -352       C  
ATOM   1333  CD  LYS B  53      28.724  32.838  16.164  1.00 31.49           C  
ANISOU 1333  CD  LYS B  53     3366   4686   3912    -50   -169   -307       C  
ATOM   1334  CE  LYS B  53      30.001  32.003  15.974  1.00 33.38           C  
ANISOU 1334  CE  LYS B  53     3647   4811   4225    353   -365   -217       C  
ATOM   1335  NZ  LYS B  53      29.751  30.499  15.989  1.00 38.61           N  
ANISOU 1335  NZ  LYS B  53     4015   5727   4926   -180   -436     29       N  
ATOM   1336  N   LYS B  54      23.326  33.962  14.543  1.00 13.58           N  
ANISOU 1336  N   LYS B  54     1553   2002   1603   -199    152   -706       N  
ATOM   1337  CA  LYS B  54      21.945  34.292  14.832  1.00 13.25           C  
ANISOU 1337  CA  LYS B  54     1579   1995   1459   -169    170   -630       C  
ATOM   1338  C   LYS B  54      20.999  33.351  14.088  1.00 12.11           C  
ANISOU 1338  C   LYS B  54     1355   1878   1366   -316    139   -648       C  
ATOM   1339  O   LYS B  54      20.038  32.837  14.650  1.00 12.71           O  
ANISOU 1339  O   LYS B  54     1539   2030   1260   -433    198   -505       O  
ATOM   1340  CB  LYS B  54      21.637  35.754  14.499  1.00 14.17           C  
ANISOU 1340  CB  LYS B  54     1866   1989   1527   -407      6   -522       C  
ATOM   1341  CG  LYS B  54      20.243  36.195  14.834  1.00 16.37           C  
ANISOU 1341  CG  LYS B  54     2047   2696   1476   -271    341   -527       C  
ATOM   1342  CD  LYS B  54      19.968  37.619  14.435  1.00 22.93           C  
ANISOU 1342  CD  LYS B  54     3117   3097   2496    383    295   -626       C  
ATOM   1343  CE  LYS B  54      18.634  38.095  14.990  1.00 20.88           C  
ANISOU 1343  CE  LYS B  54     3309   2989   1633   -483    387   -119       C  
ATOM   1344  NZ  LYS B  54      17.504  37.131  14.777  1.00 24.05           N  
ANISOU 1344  NZ  LYS B  54     2936   2900   3302   -282    -12   -734       N  
ATOM   1345  N   ARG B  55      21.292  33.103  12.817  1.00 11.91           N  
ANISOU 1345  N   ARG B  55     1441   1705   1378   -402    266   -645       N  
ATOM   1346  CA  ARG B  55      20.445  32.217  12.017  1.00 11.69           C  
ANISOU 1346  CA  ARG B  55     1432   1888   1120   -310    159   -268       C  
ATOM   1347  C   ARG B  55      20.466  30.775  12.559  1.00 10.79           C  
ANISOU 1347  C   ARG B  55     1388   1814    896   -110    -93   -519       C  
ATOM   1348  O   ARG B  55      19.445  30.066  12.546  1.00 11.19           O  
ANISOU 1348  O   ARG B  55     1340   1910   1000   -333    121   -575       O  
ATOM   1349  CB  ARG B  55      20.849  32.288  10.537  1.00 12.13           C  
ANISOU 1349  CB  ARG B  55     1357   2013   1239   -115     77   -379       C  
ATOM   1350  CG  ARG B  55      20.047  31.345   9.635  1.00 12.35           C  
ANISOU 1350  CG  ARG B  55     1711   2087    895    -76    124   -222       C  
ATOM   1351  CD  ARG B  55      18.553  31.600   9.663  1.00 13.82           C  
ANISOU 1351  CD  ARG B  55     1475   2461   1314    -44   -263   -395       C  
ATOM   1352  NE  ARG B  55      17.968  31.451   8.316  1.00 12.58           N  
ANISOU 1352  NE  ARG B  55     1487   1704   1587    -22     26   -418       N  
ATOM   1353  CZ  ARG B  55      17.881  32.444   7.431  1.00 12.65           C  
ANISOU 1353  CZ  ARG B  55     1333   1800   1673   -156      6     93       C  
ATOM   1354  NH1 ARG B  55      18.146  33.703   7.781  1.00 13.88           N  
ANISOU 1354  NH1 ARG B  55     1884   2075   1314   -466    337   -431       N  
ATOM   1355  NH2 ARG B  55      17.452  32.186   6.209  1.00 13.14           N  
ANISOU 1355  NH2 ARG B  55     1761   1745   1485   -220    206   -200       N  
ATOM   1356  N   GLU B  56      21.618  30.315  13.047  1.00 11.51           N  
ANISOU 1356  N   GLU B  56     1333   1949   1088   -189    -55   -485       N  
ATOM   1357  CA  GLU B  56      21.666  29.004  13.716  1.00 11.65           C  
ANISOU 1357  CA  GLU B  56     1434   1778   1214   -158    174   -560       C  
ATOM   1358  C   GLU B  56      20.638  28.922  14.842  1.00 11.55           C  
ANISOU 1358  C   GLU B  56     1542   1770   1075      5    -28   -375       C  
ATOM   1359  O   GLU B  56      19.913  27.912  14.995  1.00 11.77           O  
ANISOU 1359  O   GLU B  56     1543   1989    940   -308     29   -286       O  
ATOM   1360  CB  GLU B  56      23.078  28.729  14.268  1.00 13.00           C  
ANISOU 1360  CB  GLU B  56     1540   1787   1612    -33    134   -548       C  
ATOM   1361  CG  GLU B  56      24.098  28.521  13.151  1.00 13.41           C  
ANISOU 1361  CG  GLU B  56     1310   2091   1693   -225    108   -623       C  
ATOM   1362  CD  GLU B  56      25.498  28.253  13.652  1.00 15.42           C  
ANISOU 1362  CD  GLU B  56     1456   2701   1702    255     64   -928       C  
ATOM   1363  OE1 GLU B  56      25.746  28.474  14.849  1.00 19.58           O  
ANISOU 1363  OE1 GLU B  56     1828   4013   1596    145    -16   -842       O  
ATOM   1364  OE2 GLU B  56      26.373  27.936  12.832  1.00 16.21           O  
ANISOU 1364  OE2 GLU B  56     1755   2552   1851    241    209   -257       O  
ATOM   1365  N   LYS B  57      20.595  29.976  15.667  1.00 12.28           N  
ANISOU 1365  N   LYS B  57     1458   1962   1245   -238    123   -398       N  
ATOM   1366  CA  LYS B  57      19.625  29.992  16.753  1.00 12.77           C  
ANISOU 1366  CA  LYS B  57     1668   2115   1068   -257    147   -305       C  
ATOM   1367  C   LYS B  57      18.179  30.010  16.240  1.00 11.82           C  
ANISOU 1367  C   LYS B  57     1521   1583   1387    -40    240   -442       C  
ATOM   1368  O   LYS B  57      17.273  29.364  16.791  1.00 12.46           O  
ANISOU 1368  O   LYS B  57     1829   1955    949   -316    200   -377       O  
ATOM   1369  CB  LYS B  57      19.925  31.145  17.721  1.00 15.66           C  
ANISOU 1369  CB  LYS B  57     1963   2249   1736   -417     65   -483       C  
ATOM   1370  CG  LYS B  57      21.283  30.969  18.411  1.00 20.33           C  
ANISOU 1370  CG  LYS B  57     2253   3102   2367   -482    421   -948       C  
ATOM   1371  CD  LYS B  57      21.604  32.021  19.428  1.00 25.49           C  
ANISOU 1371  CD  LYS B  57     3044   3501   3138   -530     28   -662       C  
ATOM   1372  CE  LYS B  57      23.058  31.822  19.886  1.00 30.41           C  
ANISOU 1372  CE  LYS B  57     3460   4808   3284     74   -370   -656       C  
ATOM   1373  NZ  LYS B  57      24.146  31.864  18.789  1.00 31.11           N  
ANISOU 1373  NZ  LYS B  57     3995   4261   3563    110   -266   -335       N  
ATOM   1374  N   THR B  58      17.942  30.815  15.214  1.00 10.94           N  
ANISOU 1374  N   THR B  58     1439   1631   1085   -191    337   -461       N  
ATOM   1375  CA  THR B  58      16.629  30.871  14.586  1.00 10.93           C  
ANISOU 1375  CA  THR B  58     1340   1405   1406    -85    304   -293       C  
ATOM   1376  C   THR B  58      16.168  29.508  14.127  1.00  9.88           C  
ANISOU 1376  C   THR B  58     1170   1521   1061    -72      9   -230       C  
ATOM   1377  O   THR B  58      15.006  29.164  14.297  1.00 11.07           O  
ANISOU 1377  O   THR B  58     1122   1801   1282   -168     83   -250       O  
ATOM   1378  CB  THR B  58      16.651  31.889  13.441  1.00 11.46           C  
ANISOU 1378  CB  THR B  58     1597   1238   1519    -89    321   -163       C  
ATOM   1379  OG1 THR B  58      16.978  33.170  14.016  1.00 13.92           O  
ANISOU 1379  OG1 THR B  58     1919   1535   1832   -326    278   -158       O  
ATOM   1380  CG2 THR B  58      15.310  31.961  12.718  1.00 12.26           C  
ANISOU 1380  CG2 THR B  58     1411   2004   1240     45      4    117       C  
ATOM   1381  N   LEU B  59      17.064  28.754  13.500  1.00  9.82           N  
ANISOU 1381  N   LEU B  59     1341   1438    949     23     50    -83       N  
ATOM   1382  CA  LEU B  59      16.662  27.428  13.020  1.00  8.67           C  
ANISOU 1382  CA  LEU B  59     1359   1263    669      5   -159   -171       C  
ATOM   1383  C   LEU B  59      16.275  26.468  14.158  1.00  8.88           C  
ANISOU 1383  C   LEU B  59     1216   1307    851    -75    -42   -139       C  
ATOM   1384  O   LEU B  59      15.378  25.639  14.000  1.00  9.39           O  
ANISOU 1384  O   LEU B  59     1391   1571    604   -174    -15   -162       O  
ATOM   1385  CB  LEU B  59      17.751  26.732  12.194  1.00 10.73           C  
ANISOU 1385  CB  LEU B  59     1654   1710    711   -118   -165   -164       C  
ATOM   1386  CG  LEU B  59      18.229  27.367  10.928  1.00 16.44           C  
ANISOU 1386  CG  LEU B  59     2476   2022   1747    -80    126   -109       C  
ATOM   1387  CD1 LEU B  59      19.285  26.476  10.255  1.00 18.19           C  
ANISOU 1387  CD1 LEU B  59     3380   2210   1320      9   1429   -267       C  
ATOM   1388  CD2 LEU B  59      17.014  27.665  10.053  1.00 22.03           C  
ANISOU 1388  CD2 LEU B  59     2297   4038   2032   -718    138    125       C  
ATOM   1389  N   ALA B  60      16.964  26.564  15.307  1.00  9.99           N  
ANISOU 1389  N   ALA B  60     1174   1669    951   -193    -74   -293       N  
ATOM   1390  CA  ALA B  60      16.576  25.736  16.459  1.00  9.92           C  
ANISOU 1390  CA  ALA B  60     1147   1649    973   -101     89    -95       C  
ATOM   1391  C   ALA B  60      15.162  26.076  16.934  1.00  9.17           C  
ANISOU 1391  C   ALA B  60     1363   1493    626    -73    -65   -119       C  
ATOM   1392  O   ALA B  60      14.350  25.185  17.247  1.00 10.03           O  
ANISOU 1392  O   ALA B  60     1524   1431    856   -127    111    -11       O  
ATOM   1393  CB  ALA B  60      17.620  25.895  17.576  1.00 10.98           C  
ANISOU 1393  CB  ALA B  60     1253   2197    721     20   -264   -338       C  
ATOM   1394  N   TYR B  61      14.861  27.365  17.010  1.00  9.26           N  
ANISOU 1394  N   TYR B  61     1295   1435    788   -116    146   -236       N  
ATOM   1395  CA  TYR B  61      13.537  27.827  17.391  1.00  9.56           C  
ANISOU 1395  CA  TYR B  61     1263   1625    743   -182    215   -399       C  
ATOM   1396  C   TYR B  61      12.473  27.419  16.380  1.00  9.92           C  
ANISOU 1396  C   TYR B  61     1303   1377   1089   -138    101   -188       C  
ATOM   1397  O   TYR B  61      11.404  26.936  16.745  1.00  9.53           O  
ANISOU 1397  O   TYR B  61     1220   1534    864   -121     41   -305       O  
ATOM   1398  CB  TYR B  61      13.513  29.340  17.568  1.00 11.02           C  
ANISOU 1398  CB  TYR B  61     1527   1771    886   -275    336   -439       C  
ATOM   1399  CG  TYR B  61      12.147  29.914  17.854  1.00  9.26           C  
ANISOU 1399  CG  TYR B  61     1266   1346    902     54    217   -211       C  
ATOM   1400  CD1 TYR B  61      11.546  29.804  19.091  1.00  9.56           C  
ANISOU 1400  CD1 TYR B  61     1265   1682    685    -34   -187    -37       C  
ATOM   1401  CD2 TYR B  61      11.442  30.569  16.874  1.00  9.10           C  
ANISOU 1401  CD2 TYR B  61     1481   1658    320    -88    160     35       C  
ATOM   1402  CE1 TYR B  61      10.312  30.332  19.334  1.00  9.10           C  
ANISOU 1402  CE1 TYR B  61     1333   1620    502    126   -117   -231       C  
ATOM   1403  CE2 TYR B  61      10.197  31.098  17.098  1.00  9.43           C  
ANISOU 1403  CE2 TYR B  61     1543   1661    376    183     36    -60       C  
ATOM   1404  CZ  TYR B  61       9.618  30.985  18.352  1.00  9.33           C  
ANISOU 1404  CZ  TYR B  61     1073   1628    841    -89   -105   -143       C  
ATOM   1405  OH  TYR B  61       8.382  31.573  18.579  1.00 10.97           O  
ANISOU 1405  OH  TYR B  61     1402   1839    927     39    -42   -228       O  
ATOM   1406  N   MET B  62      12.757  27.626  15.089  1.00  9.39           N  
ANISOU 1406  N   MET B  62     1216   1423    930   -173     49    -75       N  
ATOM   1407  CA AMET B  62      11.797  27.232  14.063  0.65  8.79           C  
ANISOU 1407  CA AMET B  62      975   1425    938   -117    -14   -107       C  
ATOM   1408  CA BMET B  62      11.802  27.231  14.058  0.35  9.53           C  
ANISOU 1408  CA BMET B  62     1158   1529    934   -106    -58    -81       C  
ATOM   1409  C   MET B  62      11.514  25.733  14.089  1.00  8.98           C  
ANISOU 1409  C   MET B  62     1222   1580    608   -147   -172   -170       C  
ATOM   1410  O   MET B  62      10.369  25.303  13.944  1.00  8.73           O  
ANISOU 1410  O   MET B  62     1176   1483    658     -1   -190   -101       O  
ATOM   1411  CB AMET B  62      12.273  27.675  12.685  0.65 11.16           C  
ANISOU 1411  CB AMET B  62     1719   1789    730   -377     76    -75       C  
ATOM   1412  CB BMET B  62      12.304  27.660  12.687  0.35 11.17           C  
ANISOU 1412  CB BMET B  62     1620   1823    798   -253     13   -101       C  
ATOM   1413  CG AMET B  62      12.093  29.165  12.432  0.65 12.53           C  
ANISOU 1413  CG AMET B  62     1523   2001   1233   -301    471    251       C  
ATOM   1414  CG BMET B  62      12.498  29.155  12.593  0.35 12.86           C  
ANISOU 1414  CG BMET B  62     1521   2153   1209   -112   -200    295       C  
ATOM   1415  SD AMET B  62      12.855  29.701  10.888  0.65 16.64           S  
ANISOU 1415  SD AMET B  62     2498   2456   1367   -182    301    113       S  
ATOM   1416  SD BMET B  62      12.830  29.746  10.940  0.35 16.68           S  
ANISOU 1416  SD BMET B  62     2445   2735   1155   -204    352    -15       S  
ATOM   1417  CE AMET B  62      12.306  31.385  10.687  0.65 16.11           C  
ANISOU 1417  CE AMET B  62     2390   1902   1829    594    273    150       C  
ATOM   1418  CE BMET B  62      11.184  29.703  10.331  0.35 14.33           C  
ANISOU 1418  CE BMET B  62     1719   1954   1772   -174   -237  -1072       C  
ATOM   1419  N   THR B  63      12.538  24.935  14.336  1.00  9.80           N  
ANISOU 1419  N   THR B  63     1232   1447   1043   -112   -128    -69       N  
ATOM   1420  CA  THR B  63      12.332  23.499  14.436  1.00  9.25           C  
ANISOU 1420  CA  THR B  63     1240   1601    674     94   -164     -1       C  
ATOM   1421  C   THR B  63      11.398  23.148  15.597  1.00  8.46           C  
ANISOU 1421  C   THR B  63     1285   1363    566    -47   -116   -213       C  
ATOM   1422  O   THR B  63      10.496  22.322  15.441  1.00  8.93           O  
ANISOU 1422  O   THR B  63     1331   1355    703    -75    -51      8       O  
ATOM   1423  CB  THR B  63      13.667  22.720  14.500  1.00  9.75           C  
ANISOU 1423  CB  THR B  63     1146   1677    881     -3    -62      9       C  
ATOM   1424  OG1 THR B  63      14.466  23.033  13.353  1.00  9.62           O  
ANISOU 1424  OG1 THR B  63     1259   1701    693    -40     58   -139       O  
ATOM   1425  CG2 THR B  63      13.461  21.244  14.606  1.00 11.01           C  
ANISOU 1425  CG2 THR B  63     1476   1368   1339    128    -95     41       C  
ATOM   1426  N   LYS B  64      11.592  23.811  16.717  1.00  8.05           N  
ANISOU 1426  N   LYS B  64      964   1468    627   -171   -155    -64       N  
ATOM   1427  CA  LYS B  64      10.706  23.613  17.862  1.00  9.42           C  
ANISOU 1427  CA  LYS B  64     1047   1724    807   -312    -58    261       C  
ATOM   1428  C   LYS B  64       9.253  23.938  17.537  1.00  8.08           C  
ANISOU 1428  C   LYS B  64     1220   1333    516   -221     75   -135       C  
ATOM   1429  O   LYS B  64       8.365  23.139  17.816  1.00  8.13           O  
ANISOU 1429  O   LYS B  64     1347   1452    288    -10     92     -3       O  
ATOM   1430  CB  LYS B  64      11.223  24.420  19.068  1.00 10.89           C  
ANISOU 1430  CB  LYS B  64     1197   1865   1072   -176   -170     35       C  
ATOM   1431  CG  LYS B  64      10.297  24.290  20.240  1.00 12.38           C  
ANISOU 1431  CG  LYS B  64     1476   2653    574    -19    -37    -10       C  
ATOM   1432  CD  LYS B  64      10.868  24.869  21.518  1.00 16.76           C  
ANISOU 1432  CD  LYS B  64     2050   3433    883     30   -471   -108       C  
ATOM   1433  CE  LYS B  64      11.116  26.298  21.482  1.00 22.80           C  
ANISOU 1433  CE  LYS B  64     3428   3719   1512   -394   -118   -333       C  
ATOM   1434  NZ  LYS B  64      11.790  26.825  22.790  1.00 23.93           N  
ANISOU 1434  NZ  LYS B  64     3624   3688   1780   -249   -432   -923       N  
ATOM   1435  N   ILE B  65       9.019  25.090  16.904  1.00  8.39           N  
ANISOU 1435  N   ILE B  65     1211   1287    688   -140   -131     18       N  
ATOM   1436  CA  ILE B  65       7.633  25.446  16.612  1.00  9.05           C  
ANISOU 1436  CA  ILE B  65     1197   1500    742    -94    -92    -66       C  
ATOM   1437  C   ILE B  65       7.011  24.582  15.492  1.00  7.78           C  
ANISOU 1437  C   ILE B  65      964   1395    595    100    -63    -44       C  
ATOM   1438  O   ILE B  65       5.829  24.317  15.540  1.00  8.01           O  
ANISOU 1438  O   ILE B  65     1121   1429    490    -13     70    -32       O  
ATOM   1439  CB  ILE B  65       7.390  26.944  16.415  1.00  9.85           C  
ANISOU 1439  CB  ILE B  65     1157   1480   1104   -160     84   -179       C  
ATOM   1440  CG1 ILE B  65       7.975  27.476  15.118  1.00 10.72           C  
ANISOU 1440  CG1 ILE B  65     1450   1671    950   -245      6   -304       C  
ATOM   1441  CG2 ILE B  65       7.915  27.736  17.624  1.00 12.17           C  
ANISOU 1441  CG2 ILE B  65     1966   1422   1233   -183   -503   -728       C  
ATOM   1442  CD1 ILE B  65       7.562  28.950  14.757  1.00 13.01           C  
ANISOU 1442  CD1 ILE B  65     2125   1443   1374     70   -277   -273       C  
ATOM   1443  N   LEU B  66       7.838  24.080  14.561  1.00  8.11           N  
ANISOU 1443  N   LEU B  66     1090   1435    553   -114   -106    173       N  
ATOM   1444  CA  LEU B  66       7.321  23.170  13.545  1.00  8.23           C  
ANISOU 1444  CA  LEU B  66     1119   1381    628   -166     58    -45       C  
ATOM   1445  C   LEU B  66       6.905  21.842  14.189  1.00  8.39           C  
ANISOU 1445  C   LEU B  66     1129   1273    785   -131    -18    -74       C  
ATOM   1446  O   LEU B  66       5.871  21.267  13.853  1.00  8.19           O  
ANISOU 1446  O   LEU B  66     1270   1323    515   -231    -45     -3       O  
ATOM   1447  CB  LEU B  66       8.317  22.978  12.401  1.00  8.77           C  
ANISOU 1447  CB  LEU B  66     1227   1411    691    103    -80   -154       C  
ATOM   1448  CG  LEU B  66       8.551  24.221  11.538  1.00  7.23           C  
ANISOU 1448  CG  LEU B  66     1213   1258    273    -11    -19   -140       C  
ATOM   1449  CD1 LEU B  66       9.759  23.980  10.620  1.00 11.07           C  
ANISOU 1449  CD1 LEU B  66     1503   2236    464    116    132   -138       C  
ATOM   1450  CD2 LEU B  66       7.299  24.569  10.764  1.00  9.63           C  
ANISOU 1450  CD2 LEU B  66     1127   1960    569      0   -169    301       C  
ATOM   1451  N   GLU B  67       7.758  21.318  15.065  1.00  8.28           N  
ANISOU 1451  N   GLU B  67     1095   1387    660    -80      9      4       N  
ATOM   1452  CA  GLU B  67       7.409  20.133  15.834  1.00  8.67           C  
ANISOU 1452  CA  GLU B  67     1105   1302    887     33    -19     78       C  
ATOM   1453  C   GLU B  67       6.088  20.312  16.571  1.00  7.16           C  
ANISOU 1453  C   GLU B  67     1197   1088    432    -49   -234    300       C  
ATOM   1454  O   GLU B  67       5.213  19.440  16.517  1.00  8.44           O  
ANISOU 1454  O   GLU B  67     1322   1281    601   -176    -42    -24       O  
ATOM   1455  CB  GLU B  67       8.516  19.753  16.809  1.00  8.94           C  
ANISOU 1455  CB  GLU B  67     1287   1563    546    199     32    188       C  
ATOM   1456  CG  GLU B  67       9.774  19.240  16.144  1.00  8.57           C  
ANISOU 1456  CG  GLU B  67     1404   1135    715     -9   -189     83       C  
ATOM   1457  CD  GLU B  67      10.967  19.018  17.079  1.00 10.72           C  
ANISOU 1457  CD  GLU B  67     1255   1704   1112    217     22    198       C  
ATOM   1458  OE1 GLU B  67      10.946  19.609  18.183  1.00 13.60           O  
ANISOU 1458  OE1 GLU B  67     1773   2297   1097    309   -360   -133       O  
ATOM   1459  OE2 GLU B  67      11.965  18.415  16.634  1.00 10.50           O  
ANISOU 1459  OE2 GLU B  67     1267   1707   1013    153    157    139       O  
ATOM   1460  N   GLN B  68       5.944  21.437  17.271  1.00  8.20           N  
ANISOU 1460  N   GLN B  68     1227   1271    614   -132    -28     34       N  
ATOM   1461  CA  GLN B  68       4.733  21.683  17.992  1.00  7.89           C  
ANISOU 1461  CA  GLN B  68     1087   1442    468   -140   -130    173       C  
ATOM   1462  C   GLN B  68       3.490  21.705  17.088  1.00  8.03           C  
ANISOU 1462  C   GLN B  68     1050   1117    881   -178     39    -18       C  
ATOM   1463  O   GLN B  68       2.402  21.313  17.459  1.00 10.47           O  
ANISOU 1463  O   GLN B  68     1266   1785    925   -382   -212    113       O  
ATOM   1464  CB  GLN B  68       4.881  22.959  18.848  1.00  7.83           C  
ANISOU 1464  CB  GLN B  68     1376   1291    307     10      2    236       C  
ATOM   1465  CG  GLN B  68       5.825  22.736  19.996  1.00  8.88           C  
ANISOU 1465  CG  GLN B  68     1416   1508    449    -48    -75    422       C  
ATOM   1466  CD  GLN B  68       6.177  23.996  20.742  1.00 10.71           C  
ANISOU 1466  CD  GLN B  68     1809   1611    646   -375   -128     91       C  
ATOM   1467  OE1 GLN B  68       6.358  25.063  20.151  1.00 10.79           O  
ANISOU 1467  OE1 GLN B  68     1995   1525    578   -216   -343    -95       O  
ATOM   1468  NE2 GLN B  68       6.361  23.858  22.045  1.00 18.36           N  
ANISOU 1468  NE2 GLN B  68     4017   2566    391   -920   -713    253       N  
ATOM   1469  N   GLY B  69       3.692  22.183  15.876  1.00  7.75           N  
ANISOU 1469  N   GLY B  69     1101   1232    610    -50    158    -29       N  
ATOM   1470  CA  GLY B  69       2.602  22.220  14.905  1.00  8.62           C  
ANISOU 1470  CA  GLY B  69     1232   1445    599     24    -53   -117       C  
ATOM   1471  C   GLY B  69       2.167  20.826  14.447  1.00  7.62           C  
ANISOU 1471  C   GLY B  69     1092   1406    395     30   -187   -115       C  
ATOM   1472  O   GLY B  69       0.978  20.523  14.432  1.00  9.20           O  
ANISOU 1472  O   GLY B  69     1225   1679    589    -10   -108   -228       O  
ATOM   1473  N   ILE B  70       3.125  19.979  14.088  1.00  6.92           N  
ANISOU 1473  N   ILE B  70      975   1226    425   -137   -132    -17       N  
ATOM   1474  CA  ILE B  70       2.772  18.668  13.585  1.00  7.66           C  
ANISOU 1474  CA  ILE B  70     1235   1097    579   -201   -139   -144       C  
ATOM   1475  C   ILE B  70       2.224  17.757  14.689  1.00  8.84           C  
ANISOU 1475  C   ILE B  70     1516   1029    811   -407     37    -96       C  
ATOM   1476  O   ILE B  70       1.450  16.870  14.438  1.00  9.57           O  
ANISOU 1476  O   ILE B  70     1705   1481    447   -536    143    118       O  
ATOM   1477  CB  ILE B  70       3.894  18.003  12.772  1.00  7.53           C  
ANISOU 1477  CB  ILE B  70     1330   1126    404    -97   -276    -16       C  
ATOM   1478  CG1 ILE B  70       5.015  17.468  13.662  1.00  9.29           C  
ANISOU 1478  CG1 ILE B  70     1709   1382    437    -83    -21     32       C  
ATOM   1479  CG2 ILE B  70       4.405  18.959  11.682  1.00  9.35           C  
ANISOU 1479  CG2 ILE B  70     1653   1262    635   -184    217    221       C  
ATOM   1480  CD1 ILE B  70       6.172  16.755  12.950  1.00 10.23           C  
ANISOU 1480  CD1 ILE B  70     1326   1615    943    140    151    -27       C  
ATOM   1481  N   HIS B  71       2.595  18.020  15.941  1.00  8.68           N  
ANISOU 1481  N   HIS B  71     1495   1166    635   -256    199   -143       N  
ATOM   1482  CA  HIS B  71       2.076  17.178  17.028  1.00  9.66           C  
ANISOU 1482  CA  HIS B  71     1481   1666    521   -315     80    106       C  
ATOM   1483  C   HIS B  71       0.552  17.247  17.130  1.00 11.19           C  
ANISOU 1483  C   HIS B  71     1545   1566   1141   -331     26    316       C  
ATOM   1484  O   HIS B  71      -0.057  16.326  17.641  1.00 11.38           O  
ANISOU 1484  O   HIS B  71     1847   2022    452   -319   -123    213       O  
ATOM   1485  CB  HIS B  71       2.653  17.630  18.371  1.00  9.41           C  
ANISOU 1485  CB  HIS B  71     1409   1647    519    -59     90     69       C  
ATOM   1486  CG  HIS B  71       4.115  17.417  18.527  1.00  9.47           C  
ANISOU 1486  CG  HIS B  71     1462   1435    701   -207    -93    268       C  
ATOM   1487  ND1 HIS B  71       4.841  18.052  19.501  1.00 11.91           N  
ANISOU 1487  ND1 HIS B  71     1473   1968   1082   -466   -487    491       N  
ATOM   1488  CD2 HIS B  71       5.005  16.712  17.789  1.00 14.08           C  
ANISOU 1488  CD2 HIS B  71     1579   1894   1877    118    233    562       C  
ATOM   1489  CE1 HIS B  71       6.121  17.738  19.371  1.00 16.00           C  
ANISOU 1489  CE1 HIS B  71     1337   2602   2138   -574   -563    704       C  
ATOM   1490  NE2 HIS B  71       6.245  16.899  18.360  1.00 13.89           N  
ANISOU 1490  NE2 HIS B  71     1550   2141   1584     78    229   1248       N  
ATOM   1491  N   GLU B  72      -0.071  18.335  16.675  1.00 10.69           N  
ANISOU 1491  N   GLU B  72     1322   1838    901   -257    -71    266       N  
ATOM   1492  CA  GLU B  72      -1.537  18.487  16.816  1.00 11.06           C  
ANISOU 1492  CA  GLU B  72     1533   1579   1090   -222     21    115       C  
ATOM   1493  C   GLU B  72      -2.278  17.358  16.162  1.00 12.22           C  
ANISOU 1493  C   GLU B  72     1498   1636   1507   -173     -5    292       C  
ATOM   1494  O   GLU B  72      -3.307  16.927  16.656  1.00 12.08           O  
ANISOU 1494  O   GLU B  72     1572   2420    595   -431    108    182       O  
ATOM   1495  CB  GLU B  72      -2.015  19.841  16.269  1.00 12.64           C  
ANISOU 1495  CB  GLU B  72     1463   1741   1599   -114   -120    259       C  
ATOM   1496  CG  GLU B  72      -1.553  21.057  17.023  1.00 10.41           C  
ANISOU 1496  CG  GLU B  72     1968   1597    390   -201   -149    244       C  
ATOM   1497  CD  GLU B  72      -2.153  21.218  18.390  1.00 12.54           C  
ANISOU 1497  CD  GLU B  72     2026   1721   1016   -471    138     33       C  
ATOM   1498  OE1 GLU B  72      -3.239  20.633  18.660  1.00 15.86           O  
ANISOU 1498  OE1 GLU B  72     2085   2045   1893   -180    191   -187       O  
ATOM   1499  OE2 GLU B  72      -1.578  22.063  19.132  1.00 13.25           O  
ANISOU 1499  OE2 GLU B  72     2232   1887    913   -175   -197   -229       O  
ATOM   1500  N   TYR B  73      -1.757  16.802  15.080  1.00 11.31           N  
ANISOU 1500  N   TYR B  73     1434   1520   1343   -276     53    214       N  
ATOM   1501  CA  TYR B  73      -2.403  15.658  14.460  1.00 13.94           C  
ANISOU 1501  CA  TYR B  73     1784   1736   1774   -250    -87    186       C  
ATOM   1502  C   TYR B  73      -1.700  14.316  14.664  1.00  9.69           C  
ANISOU 1502  C   TYR B  73     1618   1347    713   -208   -177     95       C  
ATOM   1503  O   TYR B  73      -2.329  13.292  14.517  1.00 11.68           O  
ANISOU 1503  O   TYR B  73     1940   1654    843   -375   -199    326       O  
ATOM   1504  CB  TYR B  73      -2.624  15.873  12.933  1.00 11.96           C  
ANISOU 1504  CB  TYR B  73     1743   1613   1188   -256    -68   -194       C  
ATOM   1505  CG  TYR B  73      -1.474  16.517  12.135  1.00 10.28           C  
ANISOU 1505  CG  TYR B  73     1512   1598    793     18   -179    168       C  
ATOM   1506  CD1 TYR B  73      -0.410  15.766  11.647  1.00  9.96           C  
ANISOU 1506  CD1 TYR B  73     1496   1410    877     18    -14    -42       C  
ATOM   1507  CD2 TYR B  73      -1.481  17.854  11.889  1.00  9.97           C  
ANISOU 1507  CD2 TYR B  73     1653   1313    823     16     -9    -10       C  
ATOM   1508  CE1 TYR B  73       0.616  16.360  10.910  1.00  9.19           C  
ANISOU 1508  CE1 TYR B  73     1600   1426    463    122    -91    -83       C  
ATOM   1509  CE2 TYR B  73      -0.456  18.503  11.160  1.00  9.09           C  
ANISOU 1509  CE2 TYR B  73     1675   1410    368    -50   -189     47       C  
ATOM   1510  CZ  TYR B  73       0.557  17.718  10.626  1.00 11.51           C  
ANISOU 1510  CZ  TYR B  73     1725   1737    911   -152    132   -348       C  
ATOM   1511  OH  TYR B  73       1.525  18.309   9.878  1.00 10.64           O  
ANISOU 1511  OH  TYR B  73     1578   2067    397   -202   -157    173       O  
ATOM   1512  N   TYR B  74      -0.431  14.320  15.077  1.00 10.87           N  
ANISOU 1512  N   TYR B  74     1517   1880    731   -235   -153    452       N  
ATOM   1513  CA  TYR B  74       0.125  13.082  15.593  1.00 12.07           C  
ANISOU 1513  CA  TYR B  74     1525   1944   1116      0    -80    167       C  
ATOM   1514  C   TYR B  74      -0.722  12.560  16.762  1.00 12.69           C  
ANISOU 1514  C   TYR B  74     1755   1836   1228    158    -38    286       C  
ATOM   1515  O   TYR B  74      -0.750  11.358  17.036  1.00 13.84           O  
ANISOU 1515  O   TYR B  74     2398   1722   1139    301   -189    364       O  
ATOM   1516  CB  TYR B  74       1.603  13.233  16.003  1.00 13.31           C  
ANISOU 1516  CB  TYR B  74     1855   2066   1135     74   -160    171       C  
ATOM   1517  CG  TYR B  74       2.562  12.911  14.843  1.00 12.11           C  
ANISOU 1517  CG  TYR B  74     1571   1926   1102   -193   -351    345       C  
ATOM   1518  CD1 TYR B  74       2.902  13.881  13.871  1.00 12.57           C  
ANISOU 1518  CD1 TYR B  74     1976   1502   1295   -365   -146      5       C  
ATOM   1519  CD2 TYR B  74       3.043  11.631  14.676  1.00 13.41           C  
ANISOU 1519  CD2 TYR B  74     1928   1974   1192     78     50    616       C  
ATOM   1520  CE1 TYR B  74       3.738  13.570  12.838  1.00 12.27           C  
ANISOU 1520  CE1 TYR B  74     1673   1766   1223   -201   -219    537       C  
ATOM   1521  CE2 TYR B  74       3.847  11.293  13.565  1.00 12.41           C  
ANISOU 1521  CE2 TYR B  74     1969   1994    752    -22    -99    525       C  
ATOM   1522  CZ  TYR B  74       4.202  12.294  12.666  1.00 11.39           C  
ANISOU 1522  CZ  TYR B  74     1205   2040   1083   -243   -156    444       C  
ATOM   1523  OH  TYR B  74       5.084  12.056  11.636  1.00 13.27           O  
ANISOU 1523  OH  TYR B  74     1629   2500    913   -433    216    305       O  
ATOM   1524  N   LYS B  75      -1.286  13.485  17.519  1.00 12.47           N  
ANISOU 1524  N   LYS B  75     2122   1945    669    -20    324    599       N  
ATOM   1525  CA  LYS B  75      -2.076  13.112  18.677  1.00 13.56           C  
ANISOU 1525  CA  LYS B  75     2137   2039    977    -85    345    559       C  
ATOM   1526  C   LYS B  75      -3.414  12.429  18.310  1.00 15.20           C  
ANISOU 1526  C   LYS B  75     2469   1859   1446   -392    271    667       C  
ATOM   1527  O   LYS B  75      -4.015  11.752  19.140  1.00 16.73           O  
ANISOU 1527  O   LYS B  75     2563   2252   1538   -260    477    767       O  
ATOM   1528  CB  LYS B  75      -2.233  14.346  19.586  1.00 17.50           C  
ANISOU 1528  CB  LYS B  75     2905   2616   1127   -372    973    412       C  
ATOM   1529  CG  LYS B  75      -3.130  15.394  19.100  1.00 24.66           C  
ANISOU 1529  CG  LYS B  75     4339   3362   1667   -181    267   -435       C  
ATOM   1530  N   SER B  76      -3.832  12.523  17.044  1.00 13.37           N  
ANISOU 1530  N   SER B  76     1869   2228    983   -279    400    186       N  
ATOM   1531  CA  SER B  76      -5.164  12.128  16.613  1.00 14.15           C  
ANISOU 1531  CA  SER B  76     2108   1934   1333   -387    115    409       C  
ATOM   1532  C   SER B  76      -5.191  11.030  15.550  1.00 12.99           C  
ANISOU 1532  C   SER B  76     1687   1965   1282   -320      8    397       C  
ATOM   1533  O   SER B  76      -6.117  10.231  15.510  1.00 16.26           O  
ANISOU 1533  O   SER B  76     1923   2522   1733   -405     54    255       O  
ATOM   1534  CB  SER B  76      -5.926  13.354  16.098  1.00 20.78           C  
ANISOU 1534  CB  SER B  76     2480   3074   2341    254   -416   -484       C  
ATOM   1535  OG  SER B  76      -6.266  14.116  17.209  1.00 31.15           O  
ANISOU 1535  OG  SER B  76     3408   4973   3451    325     98   -755       O  
ATOM   1536  N   PHE B  77      -4.183  11.008  14.678  1.00 12.24           N  
ANISOU 1536  N   PHE B  77     1735   1500   1415   -246    -13    435       N  
ATOM   1537  CA  PHE B  77      -4.156  10.115  13.527  1.00 11.30           C  
ANISOU 1537  CA  PHE B  77     1639   1412   1242   -228    271    531       C  
ATOM   1538  C   PHE B  77      -3.098   9.032  13.691  1.00 12.03           C  
ANISOU 1538  C   PHE B  77     1614   1677   1280   -253    236    650       C  
ATOM   1539  O   PHE B  77      -2.103   9.222  14.370  1.00 12.46           O  
ANISOU 1539  O   PHE B  77     1846   1856   1029   -185    106    656       O  
ATOM   1540  CB  PHE B  77      -3.915  10.890  12.216  1.00 11.37           C  
ANISOU 1540  CB  PHE B  77     1557   1684   1077   -130    159    658       C  
ATOM   1541  CG  PHE B  77      -5.090  11.726  11.745  1.00 13.06           C  
ANISOU 1541  CG  PHE B  77     1576   1823   1561   -232   -129    210       C  
ATOM   1542  CD1 PHE B  77      -6.384  11.549  12.206  1.00 19.28           C  
ANISOU 1542  CD1 PHE B  77     1743   2397   3184     38   -242    791       C  
ATOM   1543  CD2 PHE B  77      -4.896  12.692  10.854  1.00 18.37           C  
ANISOU 1543  CD2 PHE B  77     1798   2031   3147    -15    162    864       C  
ATOM   1544  CE1 PHE B  77      -7.423  12.263  11.668  1.00 16.72           C  
ANISOU 1544  CE1 PHE B  77     2146   1974   2233   -273    298    511       C  
ATOM   1545  CE2 PHE B  77      -5.947  13.329  10.284  1.00 19.77           C  
ANISOU 1545  CE2 PHE B  77     1811   2864   2837    209   -435    986       C  
ATOM   1546  CZ  PHE B  77      -7.195  13.150  10.734  1.00 15.64           C  
ANISOU 1546  CZ  PHE B  77     1784   2386   1772     81   -210   1086       C  
ATOM   1547  N   ASP B  78      -3.255   7.937  12.947  1.00 11.12           N  
ANISOU 1547  N   ASP B  78     1629   1567   1027   -117   -103    353       N  
ATOM   1548  CA  ASP B  78      -2.232   6.940  12.888  1.00 12.44           C  
ANISOU 1548  CA  ASP B  78     1830   1632   1265   -282     35    500       C  
ATOM   1549  C   ASP B  78      -0.904   7.471  12.338  1.00 11.91           C  
ANISOU 1549  C   ASP B  78     1525   1629   1368    -62    -57    360       C  
ATOM   1550  O   ASP B  78      -0.869   8.483  11.640  1.00 12.27           O  
ANISOU 1550  O   ASP B  78     1932   1630   1097    -71    135    571       O  
ATOM   1551  CB  ASP B  78      -2.689   5.683  12.144  1.00 12.03           C  
ANISOU 1551  CB  ASP B  78     1927   1778    864   -264     81    156       C  
ATOM   1552  CG  ASP B  78      -3.022   5.874  10.712  1.00 16.80           C  
ANISOU 1552  CG  ASP B  78     2449   2677   1257  -1343    143   -384       C  
ATOM   1553  OD1 ASP B  78      -2.170   6.311   9.956  1.00 18.62           O  
ANISOU 1553  OD1 ASP B  78     2865   2941   1269  -1091    194    377       O  
ATOM   1554  OD2 ASP B  78      -3.797   4.973  10.288  1.00 27.92           O  
ANISOU 1554  OD2 ASP B  78     4087   3448   3072  -1108   -212    364       O  
ATOM   1555  N   ASN B  79       0.174   6.780  12.669  1.00 12.93           N  
ANISOU 1555  N   ASN B  79     1638   1907   1365   -155   -174    841       N  
ATOM   1556  CA  ASN B  79       1.496   7.255  12.279  1.00 14.47           C  
ANISOU 1556  CA  ASN B  79     1601   2241   1655    -65    -42    659       C  
ATOM   1557  C   ASN B  79       1.647   7.498  10.785  1.00 14.38           C  
ANISOU 1557  C   ASN B  79     1907   1853   1703     -2    120    338       C  
ATOM   1558  O   ASN B  79       2.215   8.517  10.382  1.00 14.68           O  
ANISOU 1558  O   ASN B  79     1814   2024   1738   -231    -64    405       O  
ATOM   1559  CB  ASN B  79       2.586   6.311  12.737  1.00 17.96           C  
ANISOU 1559  CB  ASN B  79     2088   2464   2270     67   -410    578       C  
ATOM   1560  CG  ASN B  79       3.984   6.828  12.399  1.00 18.70           C  
ANISOU 1560  CG  ASN B  79     2171   2308   2625    152   -184    463       C  
ATOM   1561  OD1 ASN B  79       4.422   7.852  12.920  1.00 22.88           O  
ANISOU 1561  OD1 ASN B  79     2673   1979   4040   -385   -284    162       O  
ATOM   1562  ND2 ASN B  79       4.721   6.064  11.604  1.00 29.95           N  
ANISOU 1562  ND2 ASN B  79     3979   3254   4146    712    355    136       N  
ATOM   1563  N   ASP B  80       1.146   6.585   9.958  1.00 14.03           N  
ANISOU 1563  N   ASP B  80     1985   1829   1514   -108    334    383       N  
ATOM   1564  CA  ASP B  80       1.387   6.744   8.513  1.00 15.64           C  
ANISOU 1564  CA  ASP B  80     2413   1857   1672   -270    437    282       C  
ATOM   1565  C   ASP B  80       0.696   8.010   8.023  1.00 12.73           C  
ANISOU 1565  C   ASP B  80     1844   1595   1396   -277    159    -95       C  
ATOM   1566  O   ASP B  80       1.244   8.772   7.219  1.00 12.57           O  
ANISOU 1566  O   ASP B  80     2099   1572   1102   -228    423     60       O  
ATOM   1567  CB  ASP B  80       0.916   5.511   7.726  1.00 16.75           C  
ANISOU 1567  CB  ASP B  80     2979   1706   1678    -21    615    257       C  
ATOM   1568  CG  ASP B  80       1.853   4.309   7.906  1.00 23.91           C  
ANISOU 1568  CG  ASP B  80     3412   2479   3192   -304    521    629       C  
ATOM   1569  OD1 ASP B  80       3.010   4.454   8.389  1.00 31.92           O  
ANISOU 1569  OD1 ASP B  80     4265   3017   4845    175    238    532       O  
ATOM   1570  OD2 ASP B  80       1.376   3.194   7.699  1.00 33.70           O  
ANISOU 1570  OD2 ASP B  80     4952   2936   4914   -492    915   -177       O  
ATOM   1571  N   THR B  81      -0.527   8.226   8.496  1.00 10.75           N  
ANISOU 1571  N   THR B  81     1634   1510    940   -224     95    105       N  
ATOM   1572  CA  THR B  81      -1.330   9.377   8.064  1.00 11.21           C  
ANISOU 1572  CA  THR B  81     1552   1647   1060   -101   -134     47       C  
ATOM   1573  C   THR B  81      -0.700  10.680   8.538  1.00 10.68           C  
ANISOU 1573  C   THR B  81     1595   1523    939   -249   -127    -18       C  
ATOM   1574  O   THR B  81      -0.551  11.637   7.773  1.00 10.15           O  
ANISOU 1574  O   THR B  81     1688   1547    620   -229     81     13       O  
ATOM   1575  CB  THR B  81      -2.797   9.244   8.525  1.00 11.06           C  
ANISOU 1575  CB  THR B  81     1605   1904    693   -397    -76     19       C  
ATOM   1576  OG1 THR B  81      -3.328   8.024   7.994  1.00 13.94           O  
ANISOU 1576  OG1 THR B  81     1965   1734   1597   -647   -210    -88       O  
ATOM   1577  CG2 THR B  81      -3.644  10.445   8.084  1.00 13.98           C  
ANISOU 1577  CG2 THR B  81     1675   2246   1389     43   -385    -84       C  
ATOM   1578  N   ALA B  82      -0.303  10.712   9.811  1.00 10.64           N  
ANISOU 1578  N   ALA B  82     1486   1599    956   -322     70    267       N  
ATOM   1579  CA  ALA B  82       0.265  11.911  10.423  1.00 10.40           C  
ANISOU 1579  CA  ALA B  82     1481   1681    787   -271    -64    169       C  
ATOM   1580  C   ALA B  82       1.596  12.240   9.724  1.00  8.64           C  
ANISOU 1580  C   ALA B  82     1356   1437    487   -143    237   -152       C  
ATOM   1581  O   ALA B  82       1.882  13.411   9.482  1.00  9.81           O  
ANISOU 1581  O   ALA B  82     1601   1514    610   -283    196     -9       O  
ATOM   1582  CB  ALA B  82       0.497  11.671  11.884  1.00 10.82           C  
ANISOU 1582  CB  ALA B  82     1790   1711    607   -359    -32    119       C  
ATOM   1583  N   ARG B  83       2.431  11.228   9.450  1.00  9.28           N  
ANISOU 1583  N   ARG B  83     1321   1412    793    -77    203     -8       N  
ATOM   1584  CA  ARG B  83       3.690  11.457   8.750  1.00 10.04           C  
ANISOU 1584  CA  ARG B  83     1266   1659    890    -72   -107    175       C  
ATOM   1585  C   ARG B  83       3.428  12.044   7.359  1.00  9.06           C  
ANISOU 1585  C   ARG B  83     1400   1225    816   -186     58     73       C  
ATOM   1586  O   ARG B  83       4.125  12.955   6.923  1.00 10.17           O  
ANISOU 1586  O   ARG B  83     1431   1473    959   -217    274     95       O  
ATOM   1587  CB  ARG B  83       4.553  10.199   8.675  1.00 10.55           C  
ANISOU 1587  CB  ARG B  83     1541   1915    552   -168      5    305       C  
ATOM   1588  CG  ARG B  83       5.920  10.470   8.074  1.00 13.30           C  
ANISOU 1588  CG  ARG B  83     1863   1838   1353     19    306    139       C  
ATOM   1589  CD  ARG B  83       6.794   9.292   8.061  1.00 14.19           C  
ANISOU 1589  CD  ARG B  83     2063   2197   1128   -106    505    -17       C  
ATOM   1590  NE  ARG B  83       7.271   8.955   9.378  1.00 16.44           N  
ANISOU 1590  NE  ARG B  83     2089   2223   1932    287    202    605       N  
ATOM   1591  CZ  ARG B  83       8.083   7.961   9.653  1.00 21.09           C  
ANISOU 1591  CZ  ARG B  83     3128   2579   2304    246    863    630       C  
ATOM   1592  NH1 ARG B  83       8.407   7.082   8.721  1.00 23.34           N  
ANISOU 1592  NH1 ARG B  83     3178   2126   3562    163   1346    -40       N  
ATOM   1593  NH2 ARG B  83       8.539   7.852  10.893  1.00 25.61           N  
ANISOU 1593  NH2 ARG B  83     3953   3858   1919    820    496   1251       N  
ATOM   1594  N   LYS B  84       2.482  11.449   6.621  1.00  9.65           N  
ANISOU 1594  N   LYS B  84     1546   1136    982   -213     18    -71       N  
ATOM   1595  CA  LYS B  84       2.164  11.989   5.278  1.00 11.45           C  
ANISOU 1595  CA  LYS B  84     1713   1470   1166    -68    184    115       C  
ATOM   1596  C   LYS B  84       1.787  13.457   5.349  1.00  9.80           C  
ANISOU 1596  C   LYS B  84     1437   1438    847   -244    -56   -143       C  
ATOM   1597  O   LYS B  84       2.204  14.280   4.503  1.00 10.27           O  
ANISOU 1597  O   LYS B  84     1822   1553    526   -308     98    -25       O  
ATOM   1598  CB  LYS B  84       1.067  11.135   4.564  1.00 14.31           C  
ANISOU 1598  CB  LYS B  84     2250   1607   1580   -360     72   -165       C  
ATOM   1599  CG  LYS B  84       1.586   9.862   3.960  1.00 21.97           C  
ANISOU 1599  CG  LYS B  84     3554   3004   1787     32    -56    629       C  
ATOM   1600  CD  LYS B  84       0.507   8.885   3.468  1.00 28.28           C  
ANISOU 1600  CD  LYS B  84     4463   3658   2621   -653    243     96       C  
ATOM   1601  CE  LYS B  84       1.143   7.493   3.151  1.00 31.24           C  
ANISOU 1601  CE  LYS B  84     5024   4409   2437   -404    166   -596       C  
ATOM   1602  NZ  LYS B  84       0.157   6.430   2.755  1.00 39.62           N  
ANISOU 1602  NZ  LYS B  84     5602   4912   4536   -848    -74     31       N  
ATOM   1603  N   MET B  85       1.005  13.834   6.359  1.00  9.31           N  
ANISOU 1603  N   MET B  85     1258   1526    753   -165     67    -15       N  
ATOM   1604  CA  MET B  85       0.615  15.225   6.549  1.00  8.27           C  
ANISOU 1604  CA  MET B  85     1213   1381    548    -92      1     70       C  
ATOM   1605  C   MET B  85       1.796  16.149   6.845  1.00  7.98           C  
ANISOU 1605  C   MET B  85      883   1360    789    -32     75    -49       C  
ATOM   1606  O   MET B  85       1.946  17.218   6.241  1.00  8.69           O  
ANISOU 1606  O   MET B  85     1386   1370    544   -217     70     -3       O  
ATOM   1607  CB  MET B  85      -0.460  15.351   7.644  1.00  9.01           C  
ANISOU 1607  CB  MET B  85     1167   1437    819   -223    -29     73       C  
ATOM   1608  CG  MET B  85      -1.758  14.720   7.227  1.00  9.56           C  
ANISOU 1608  CG  MET B  85     1251   1475    905   -143    166    100       C  
ATOM   1609  SD  MET B  85      -2.855  14.400   8.611  1.00 12.25           S  
ANISOU 1609  SD  MET B  85     1495   1980   1177   -299    152     46       S  
ATOM   1610  CE  MET B  85      -3.268  16.061   9.099  1.00 12.61           C  
ANISOU 1610  CE  MET B  85     1604   2216    968    -77    358   -278       C  
ATOM   1611  N   ALA B  86       2.668  15.694   7.718  1.00  8.73           N  
ANISOU 1611  N   ALA B  86     1296   1349    669     57    -51   -110       N  
ATOM   1612  CA  ALA B  86       3.846  16.480   8.093  1.00  8.45           C  
ANISOU 1612  CA  ALA B  86     1146   1348    715   -235    -25   -176       C  
ATOM   1613  C   ALA B  86       4.749  16.686   6.897  1.00  7.38           C  
ANISOU 1613  C   ALA B  86     1176   1128    498   -155   -115     70       C  
ATOM   1614  O   ALA B  86       5.239  17.782   6.653  1.00  8.44           O  
ANISOU 1614  O   ALA B  86     1204   1358    642   -199    -18    -94       O  
ATOM   1615  CB  ALA B  86       4.601  15.772   9.253  1.00 10.66           C  
ANISOU 1615  CB  ALA B  86     1525   1914    610   -138   -324     87       C  
ATOM   1616  N   LEU B  87       4.964  15.616   6.130  1.00  9.13           N  
ANISOU 1616  N   LEU B  87     1368   1301    800   -290    248     57       N  
ATOM   1617  CA  LEU B  87       5.856  15.733   4.978  1.00  9.90           C  
ANISOU 1617  CA  LEU B  87     1468   1359    932     -6    456    195       C  
ATOM   1618  C   LEU B  87       5.227  16.504   3.801  1.00  8.89           C  
ANISOU 1618  C   LEU B  87     1356   1015   1005   -277    215   -133       C  
ATOM   1619  O   LEU B  87       5.946  17.159   3.036  1.00  9.24           O  
ANISOU 1619  O   LEU B  87     1619   1322    568   -243    336    105       O  
ATOM   1620  CB  LEU B  87       6.387  14.370   4.562  1.00 10.53           C  
ANISOU 1620  CB  LEU B  87     1668   1508    823   -121    445     26       C  
ATOM   1621  CG  LEU B  87       7.177  13.639   5.656  1.00 11.16           C  
ANISOU 1621  CG  LEU B  87     1775   1606    857    225    439    290       C  
ATOM   1622  CD1 LEU B  87       7.749  12.349   5.106  1.00 13.81           C  
ANISOU 1622  CD1 LEU B  87     1961   1777   1507    113    523    -25       C  
ATOM   1623  CD2 LEU B  87       8.272  14.487   6.305  1.00 14.20           C  
ANISOU 1623  CD2 LEU B  87     1626   2016   1753    -36    225   -188       C  
ATOM   1624  N   ASP B  88       3.903  16.462   3.696  1.00  8.71           N  
ANISOU 1624  N   ASP B  88     1557   1234    517   -248    -20    115       N  
ATOM   1625  CA  ASP B  88       3.207  17.345   2.767  1.00  9.80           C  
ANISOU 1625  CA  ASP B  88     1572   1428    720   -306     36    210       C  
ATOM   1626  C   ASP B  88       3.391  18.823   3.129  1.00  8.98           C  
ANISOU 1626  C   ASP B  88     1523   1102    784    -40    -47   -103       C  
ATOM   1627  O   ASP B  88       3.703  19.676   2.270  1.00  9.01           O  
ANISOU 1627  O   ASP B  88     1379   1379    665   -153    -27    -61       O  
ATOM   1628  CB  ASP B  88       1.729  16.986   2.691  1.00 10.47           C  
ANISOU 1628  CB  ASP B  88     1747   1696    532   -238   -495     34       C  
ATOM   1629  CG  ASP B  88       1.071  17.548   1.469  1.00 17.19           C  
ANISOU 1629  CG  ASP B  88     2151   2766   1614   -591   -548    464       C  
ATOM   1630  OD1 ASP B  88       1.704  17.600   0.395  1.00 23.00           O  
ANISOU 1630  OD1 ASP B  88     3335   3901   1500   -631    -87    873       O  
ATOM   1631  OD2 ASP B  88      -0.079  17.845   1.563  1.00 16.07           O  
ANISOU 1631  OD2 ASP B  88     2447   2580   1078    259   -311    140       O  
ATOM   1632  N   TYR B  89       3.226  19.122   4.400  1.00  8.95           N  
ANISOU 1632  N   TYR B  89     1169   1419    810   -173      2    -58       N  
ATOM   1633  CA  TYR B  89       3.544  20.441   4.903  1.00  9.20           C  
ANISOU 1633  CA  TYR B  89     1380   1284    830    -83    119    110       C  
ATOM   1634  C   TYR B  89       5.001  20.875   4.608  1.00  6.38           C  
ANISOU 1634  C   TYR B  89      966   1121    337    -18      6   -257       C  
ATOM   1635  O   TYR B  89       5.232  21.972   4.087  1.00  8.16           O  
ANISOU 1635  O   TYR B  89     1291   1207    600    -61    150     30       O  
ATOM   1636  CB  TYR B  89       3.263  20.459   6.406  1.00  8.84           C  
ANISOU 1636  CB  TYR B  89     1262   1257    837     39    147    -34       C  
ATOM   1637  CG  TYR B  89       3.593  21.741   7.167  1.00  7.70           C  
ANISOU 1637  CG  TYR B  89     1228   1102    593     56    182     71       C  
ATOM   1638  CD1 TYR B  89       3.533  22.989   6.556  1.00  7.56           C  
ANISOU 1638  CD1 TYR B  89     1066   1152    653     34    -99    -51       C  
ATOM   1639  CD2 TYR B  89       4.066  21.673   8.456  1.00  8.89           C  
ANISOU 1639  CD2 TYR B  89     1212   1269    895   -209     98    119       C  
ATOM   1640  CE1 TYR B  89       3.842  24.162   7.261  1.00  9.67           C  
ANISOU 1640  CE1 TYR B  89     1220   1121   1332     46    141    164       C  
ATOM   1641  CE2 TYR B  89       4.330  22.823   9.186  1.00  7.74           C  
ANISOU 1641  CE2 TYR B  89     1446   1073    418    -33     19    -36       C  
ATOM   1642  CZ  TYR B  89       4.290  24.049   8.567  1.00  8.81           C  
ANISOU 1642  CZ  TYR B  89     1502   1014    828     29   -153    176       C  
ATOM   1643  OH  TYR B  89       4.515  25.205   9.306  1.00  9.96           O  
ANISOU 1643  OH  TYR B  89     1685   1211    888     -1   -133   -113       O  
ATOM   1644  N   PHE B  90       5.937  19.997   4.917  1.00  7.75           N  
ANISOU 1644  N   PHE B  90     1071   1120    751    119     17    -42       N  
ATOM   1645  CA  PHE B  90       7.309  20.330   4.697  1.00  7.69           C  
ANISOU 1645  CA  PHE B  90     1088   1271    562    -56     13     35       C  
ATOM   1646  C   PHE B  90       7.597  20.572   3.188  1.00  7.14           C  
ANISOU 1646  C   PHE B  90     1036   1126    550   -129    140    -81       C  
ATOM   1647  O   PHE B  90       8.411  21.426   2.839  1.00  7.92           O  
ANISOU 1647  O   PHE B  90     1183   1388    438    -92     59     70       O  
ATOM   1648  CB  PHE B  90       8.272  19.322   5.289  1.00  8.20           C  
ANISOU 1648  CB  PHE B  90     1046   1414    654    -70     -8     65       C  
ATOM   1649  CG  PHE B  90       8.261  19.281   6.808  1.00  7.96           C  
ANISOU 1649  CG  PHE B  90     1144   1221    658     34     17    -63       C  
ATOM   1650  CD1 PHE B  90       7.573  20.203   7.565  1.00  8.74           C  
ANISOU 1650  CD1 PHE B  90     1313   1488    520     83    388    169       C  
ATOM   1651  CD2 PHE B  90       9.033  18.350   7.447  1.00 10.03           C  
ANISOU 1651  CD2 PHE B  90     1485   1470    855    265     95     22       C  
ATOM   1652  CE1 PHE B  90       7.562  20.111   8.954  1.00  9.24           C  
ANISOU 1652  CE1 PHE B  90     1307   1385    816    161    177     60       C  
ATOM   1653  CE2 PHE B  90       9.062  18.260   8.834  1.00 11.74           C  
ANISOU 1653  CE2 PHE B  90     1738   1963    757    491     99    427       C  
ATOM   1654  CZ  PHE B  90       8.319  19.151   9.573  1.00 10.20           C  
ANISOU 1654  CZ  PHE B  90     1401   1596    877     82    107    -79       C  
ATOM   1655  N   LYS B  91       6.926  19.808   2.319  1.00  7.81           N  
ANISOU 1655  N   LYS B  91     1218   1086    661   -282     24    180       N  
ATOM   1656  CA  LYS B  91       7.057  20.083   0.881  1.00  9.35           C  
ANISOU 1656  CA  LYS B  91     1374   1297    880   -191    185    165       C  
ATOM   1657  C   LYS B  91       6.646  21.503   0.576  1.00  7.83           C  
ANISOU 1657  C   LYS B  91     1201   1252    521   -169     81   -221       C  
ATOM   1658  O   LYS B  91       7.304  22.210  -0.217  1.00  8.94           O  
ANISOU 1658  O   LYS B  91     1356   1477    561    -85    -92      3       O  
ATOM   1659  CB  LYS B  91       6.227  19.080   0.054  1.00  9.63           C  
ANISOU 1659  CB  LYS B  91     1557   1203    897    -32    -17     90       C  
ATOM   1660  CG  LYS B  91       6.218  19.407  -1.435  1.00 14.32           C  
ANISOU 1660  CG  LYS B  91     2020   2030   1391   -312   -431   -232       C  
ATOM   1661  CD  LYS B  91       5.485  18.375  -2.320  1.00 20.05           C  
ANISOU 1661  CD  LYS B  91     2750   2517   2348   -272   -115   -713       C  
ATOM   1662  CE  LYS B  91       5.214  18.992  -3.735  1.00 27.26           C  
ANISOU 1662  CE  LYS B  91     3072   4624   2662   -906   -365   -711       C  
ATOM   1663  NZ  LYS B  91       6.394  19.786  -4.414  1.00 29.54           N  
ANISOU 1663  NZ  LYS B  91     3519   4884   2818     28    426  -1227       N  
ATOM   1664  N   ARG B  92       5.558  21.963   1.174  1.00  8.37           N  
ANISOU 1664  N   ARG B  92     1267   1310    601     51     13     -1       N  
ATOM   1665  CA  ARG B  92       5.113  23.326   0.941  1.00  7.91           C  
ANISOU 1665  CA  ARG B  92     1234   1371    400    -43   -143    138       C  
ATOM   1666  C   ARG B  92       6.074  24.413   1.485  1.00  6.81           C  
ANISOU 1666  C   ARG B  92     1089    926    571    -20     42      6       C  
ATOM   1667  O   ARG B  92       6.307  25.430   0.826  1.00  8.36           O  
ANISOU 1667  O   ARG B  92     1472   1223    481    -93     19    180       O  
ATOM   1668  CB  ARG B  92       3.701  23.536   1.505  1.00  8.83           C  
ANISOU 1668  CB  ARG B  92     1317   1483    553     53   -282    -75       C  
ATOM   1669  CG  ARG B  92       2.703  22.669   0.797  1.00 10.89           C  
ANISOU 1669  CG  ARG B  92     1357   2133    647    120    145    235       C  
ATOM   1670  CD  ARG B  92       1.306  23.161   0.938  1.00 15.09           C  
ANISOU 1670  CD  ARG B  92     1715   2133   1885   -248    -77   -573       C  
ATOM   1671  NE  ARG B  92       0.841  23.151   2.318  1.00 17.88           N  
ANISOU 1671  NE  ARG B  92     3118   2458   1216   -383   -472    754       N  
ATOM   1672  CZ  ARG B  92       0.521  22.060   2.967  1.00 19.92           C  
ANISOU 1672  CZ  ARG B  92     3167   2694   1709   1105    468    172       C  
ATOM   1673  NH1 ARG B  92       0.545  20.921   2.274  1.00 21.20           N  
ANISOU 1673  NH1 ARG B  92     2738   2360   2954    321    925   -410       N  
ATOM   1674  NH2 ARG B  92       0.196  22.126   4.267  1.00 16.69           N  
ANISOU 1674  NH2 ARG B  92     3332   2013    995   -516   -426   -213       N  
ATOM   1675  N   ILE B  93       6.724  24.113   2.606  1.00  7.65           N  
ANISOU 1675  N   ILE B  93     1057   1347    502     65     71    298       N  
ATOM   1676  CA  ILE B  93       7.755  24.993   3.135  1.00  7.95           C  
ANISOU 1676  CA  ILE B  93     1053   1297    671     16     52    196       C  
ATOM   1677  C   ILE B  93       8.884  25.096   2.102  1.00  7.35           C  
ANISOU 1677  C   ILE B  93     1148   1090    555     20    -37    165       C  
ATOM   1678  O   ILE B  93       9.276  26.206   1.685  1.00  8.65           O  
ANISOU 1678  O   ILE B  93     1452   1228    606    -67     54    134       O  
ATOM   1679  CB  ILE B  93       8.311  24.514   4.460  1.00  7.56           C  
ANISOU 1679  CB  ILE B  93     1163   1150    558    136    292    -15       C  
ATOM   1680  CG1 ILE B  93       7.218  24.607   5.560  1.00  8.65           C  
ANISOU 1680  CG1 ILE B  93      970   1303   1012     41    -97    154       C  
ATOM   1681  CG2 ILE B  93       9.546  25.347   4.879  1.00  9.87           C  
ANISOU 1681  CG2 ILE B  93     1187   1477   1087   -233    160   -173       C  
ATOM   1682  CD1 ILE B  93       7.650  24.091   6.934  1.00  9.55           C  
ANISOU 1682  CD1 ILE B  93     1348   1789    488    109     59    282       C  
ATOM   1683  N   ASN B  94       9.358  23.943   1.601  1.00  8.36           N  
ANISOU 1683  N   ASN B  94     1212   1184    779     -3    122     56       N  
ATOM   1684  CA  ASN B  94      10.484  24.012   0.710  1.00  9.22           C  
ANISOU 1684  CA  ASN B  94     1157   1548    798    -91    -16    144       C  
ATOM   1685  C   ASN B  94      10.086  24.724  -0.593  1.00  8.09           C  
ANISOU 1685  C   ASN B  94     1081   1405    587    -62    111   -101       C  
ATOM   1686  O   ASN B  94      10.906  25.469  -1.187  1.00  8.59           O  
ANISOU 1686  O   ASN B  94     1254   1603    404    -83    124    170       O  
ATOM   1687  CB  ASN B  94      11.089  22.632   0.413  1.00  7.97           C  
ANISOU 1687  CB  ASN B  94     1140   1515    372     61    -26     83       C  
ATOM   1688  CG  ASN B  94      11.822  22.026   1.607  1.00  8.68           C  
ANISOU 1688  CG  ASN B  94     1196   1230    871     26     69     79       C  
ATOM   1689  OD1 ASN B  94      11.498  22.368   2.765  1.00  9.42           O  
ANISOU 1689  OD1 ASN B  94     1398   1461    718     11     38   -226       O  
ATOM   1690  ND2 ASN B  94      12.808  21.170   1.335  1.00  9.64           N  
ANISOU 1690  ND2 ASN B  94     1328   1256   1077     64     85    117       N  
ATOM   1691  N   ASP B  95       8.866  24.462  -1.051  1.00  8.24           N  
ANISOU 1691  N   ASP B  95     1293   1281    554    -96     69     75       N  
ATOM   1692  CA  ASP B  95       8.352  25.098  -2.290  1.00  9.34           C  
ANISOU 1692  CA  ASP B  95     1649   1486    414    -34   -118    334       C  
ATOM   1693  C   ASP B  95       8.214  26.617  -2.162  1.00 10.47           C  
ANISOU 1693  C   ASP B  95     1684   1474    820   -161   -324    -51       C  
ATOM   1694  O   ASP B  95       8.189  27.348  -3.169  1.00 12.06           O  
ANISOU 1694  O   ASP B  95     2092   1799    688    -79   -177    308       O  
ATOM   1695  CB  ASP B  95       7.003  24.498  -2.735  1.00  9.93           C  
ANISOU 1695  CB  ASP B  95     1697   1571    503     90    -54     43       C  
ATOM   1696  CG  ASP B  95       7.094  23.097  -3.288  1.00 11.68           C  
ANISOU 1696  CG  ASP B  95     1815   1951    669    137   -182   -254       C  
ATOM   1697  OD1 ASP B  95       8.174  22.616  -3.605  1.00 14.28           O  
ANISOU 1697  OD1 ASP B  95     2032   2376   1015    176     29   -403       O  
ATOM   1698  OD2 ASP B  95       6.013  22.468  -3.449  1.00 14.43           O  
ANISOU 1698  OD2 ASP B  95     2353   2258    871   -222   -503     -4       O  
ATOM   1699  N   ASP B  96       8.143  27.128  -0.934  1.00  8.23           N  
ANISOU 1699  N   ASP B  96     1491   1339    297      1    -48    144       N  
ATOM   1700  CA  ASP B  96       8.109  28.563  -0.674  1.00  9.72           C  
ANISOU 1700  CA  ASP B  96     1262   1635    795    265    -24    108       C  
ATOM   1701  C   ASP B  96       9.443  29.246  -1.043  1.00 10.61           C  
ANISOU 1701  C   ASP B  96     1474   1525   1031     78     69     39       C  
ATOM   1702  O   ASP B  96       9.472  30.451  -1.300  1.00 10.44           O  
ANISOU 1702  O   ASP B  96     1728   1602    636    149    187    149       O  
ATOM   1703  CB  ASP B  96       7.814  28.896   0.797  1.00  9.80           C  
ANISOU 1703  CB  ASP B  96     1362   1669    691    136     52    -24       C  
ATOM   1704  CG  ASP B  96       6.448  28.541   1.264  1.00 10.07           C  
ANISOU 1704  CG  ASP B  96     1099   1558   1169     12    -51    -30       C  
ATOM   1705  OD1 ASP B  96       5.498  28.422   0.451  1.00 10.31           O  
ANISOU 1705  OD1 ASP B  96     1386   1786    742     26    164    193       O  
ATOM   1706  OD2 ASP B  96       6.289  28.365   2.554  1.00 10.20           O  
ANISOU 1706  OD2 ASP B  96     1804   1661    411      9     46     66       O  
ATOM   1707  N   LYS B  97      10.543  28.484  -1.063  1.00  9.89           N  
ANISOU 1707  N   LYS B  97     1461   1375    919    -56    315    196       N  
ATOM   1708  CA  LYS B  97      11.844  29.020  -1.466  1.00 10.50           C  
ANISOU 1708  CA  LYS B  97     1476   1435   1075   -187    329    315       C  
ATOM   1709  C   LYS B  97      12.238  30.273  -0.665  1.00 12.65           C  
ANISOU 1709  C   LYS B  97     1586   1809   1412   -229     38    214       C  
ATOM   1710  O   LYS B  97      12.702  31.274  -1.185  1.00 12.85           O  
ANISOU 1710  O   LYS B  97     1808   1742   1331   -250    223    333       O  
ATOM   1711  CB  LYS B  97      11.920  29.260  -2.986  1.00 12.92           C  
ANISOU 1711  CB  LYS B  97     1706   1897   1305   -151    324    459       C  
ATOM   1712  CG  LYS B  97      11.777  27.962  -3.811  1.00 12.93           C  
ANISOU 1712  CG  LYS B  97     1823   2173    915   -344    239    194       C  
ATOM   1713  CD  LYS B  97      11.938  28.211  -5.281  1.00 17.85           C  
ANISOU 1713  CD  LYS B  97     2677   3101   1003   -296    563    350       C  
ATOM   1714  CE  LYS B  97      11.781  26.929  -6.061  1.00 26.28           C  
ANISOU 1714  CE  LYS B  97     4114   3814   2057   -262    444     67       C  
ATOM   1715  NZ  LYS B  97      11.780  27.161  -7.552  1.00 34.78           N  
ANISOU 1715  NZ  LYS B  97     4893   5845   2475    -87    -13    389       N  
ATOM   1716  N   GLY B  98      12.015  30.161   0.640  1.00 11.37           N  
ANISOU 1716  N   GLY B  98     1676   1618   1026   -251     29    147       N  
ATOM   1717  CA  GLY B  98      12.292  31.254   1.596  1.00 10.63           C  
ANISOU 1717  CA  GLY B  98     1666   1634    738    -15     49    288       C  
ATOM   1718  C   GLY B  98      13.426  30.964   2.539  1.00 10.39           C  
ANISOU 1718  C   GLY B  98     1195   1642   1108    -16    127    354       C  
ATOM   1719  O   GLY B  98      14.479  30.505   2.148  1.00 10.85           O  
ANISOU 1719  O   GLY B  98     1401   1785    935   -136    101    -14       O  
ATOM   1720  N   MET B  99      13.218  31.260   3.807  1.00 10.47           N  
ANISOU 1720  N   MET B  99     1235   1518   1223   -106    338     50       N  
ATOM   1721  CA  MET B  99      14.327  31.223   4.750  1.00  9.42           C  
ANISOU 1721  CA  MET B  99     1197   1302   1077   -173    221   -182       C  
ATOM   1722  C   MET B  99      14.888  29.849   4.960  1.00  8.14           C  
ANISOU 1722  C   MET B  99     1070   1331    690    -68    176    -40       C  
ATOM   1723  O   MET B  99      16.088  29.704   5.176  1.00  9.01           O  
ANISOU 1723  O   MET B  99     1245   1490    685    -91    208   -131       O  
ATOM   1724  CB  MET B  99      13.896  31.775   6.124  1.00  9.99           C  
ANISOU 1724  CB  MET B  99     1517   1309    969    165    146   -309       C  
ATOM   1725  CG  MET B  99      13.596  33.274   6.113  1.00 12.30           C  
ANISOU 1725  CG  MET B  99     1733   1745   1195     95    370   -357       C  
ATOM   1726  SD  MET B  99      13.082  33.962   7.655  1.00 13.03           S  
ANISOU 1726  SD  MET B  99     1880   2009   1060     43    265   -505       S  
ATOM   1727  CE  MET B  99      14.644  34.036   8.530  1.00 16.89           C  
ANISOU 1727  CE  MET B  99     1683   2558   2176   -464     85   -748       C  
ATOM   1728  N   ILE B 100      14.019  28.867   5.059  1.00  8.94           N  
ANISOU 1728  N   ILE B 100     1162   1230   1003      0    130    -76       N  
ATOM   1729  CA  ILE B 100      14.407  27.532   5.408  1.00  8.11           C  
ANISOU 1729  CA  ILE B 100     1125   1242    715   -130     27    -46       C  
ATOM   1730  C   ILE B 100      13.955  26.453   4.419  1.00  6.89           C  
ANISOU 1730  C   ILE B 100      975   1126    516     19    305    -12       C  
ATOM   1731  O   ILE B 100      12.939  26.615   3.730  1.00  8.26           O  
ANISOU 1731  O   ILE B 100     1284   1355    497    164     49     68       O  
ATOM   1732  CB  ILE B 100      13.951  27.169   6.863  1.00 10.35           C  
ANISOU 1732  CB  ILE B 100     1321   1441   1170   -127    166     71       C  
ATOM   1733  CG1 ILE B 100      12.442  26.938   6.990  1.00  9.83           C  
ANISOU 1733  CG1 ILE B 100     1610   1497    628   -113    179   -158       C  
ATOM   1734  CG2 ILE B 100      14.395  28.225   7.860  1.00 12.84           C  
ANISOU 1734  CG2 ILE B 100     1848   2092    938   -594    107   -801       C  
ATOM   1735  CD1 ILE B 100      11.902  26.492   8.341  1.00 11.66           C  
ANISOU 1735  CD1 ILE B 100     1743   1980    705   -143    413    430       C  
ATOM   1736  N   TYR B 101      14.673  25.336   4.451  1.00  8.26           N  
ANISOU 1736  N   TYR B 101     1299   1033    805    207     92     33       N  
ATOM   1737  CA  TYR B 101      14.324  24.127   3.703  1.00  6.83           C  
ANISOU 1737  CA  TYR B 101     1155   1045    392    153    178   -133       C  
ATOM   1738  C   TYR B 101      14.477  22.956   4.640  1.00  7.75           C  
ANISOU 1738  C   TYR B 101     1139    973    832   -108    -74   -208       C  
ATOM   1739  O   TYR B 101      15.494  22.856   5.348  1.00  7.68           O  
ANISOU 1739  O   TYR B 101     1098   1388    428   -157     46     46       O  
ATOM   1740  CB  TYR B 101      15.249  23.967   2.510  1.00  8.87           C  
ANISOU 1740  CB  TYR B 101     1191   1345    833    -47     78   -157       C  
ATOM   1741  CG  TYR B 101      15.173  25.102   1.499  1.00  8.22           C  
ANISOU 1741  CG  TYR B 101     1188   1245    686     52    318     56       C  
ATOM   1742  CD1 TYR B 101      14.281  25.050   0.420  1.00  8.06           C  
ANISOU 1742  CD1 TYR B 101     1264   1276    519   -151    409   -101       C  
ATOM   1743  CD2 TYR B 101      15.941  26.235   1.641  1.00  8.48           C  
ANISOU 1743  CD2 TYR B 101     1220   1518    481    -61    280      1       C  
ATOM   1744  CE1 TYR B 101      14.222  26.068  -0.524  1.00  8.72           C  
ANISOU 1744  CE1 TYR B 101     1386   1336    590   -146    371    142       C  
ATOM   1745  CE2 TYR B 101      15.875  27.271   0.697  1.00  9.18           C  
ANISOU 1745  CE2 TYR B 101     1308   1367    813    -54    119     35       C  
ATOM   1746  CZ  TYR B 101      14.992  27.177  -0.382  1.00  8.86           C  
ANISOU 1746  CZ  TYR B 101     1215   1366    785    -83    273    189       C  
ATOM   1747  OH  TYR B 101      14.942  28.183  -1.323  1.00  9.69           O  
ANISOU 1747  OH  TYR B 101     1417   1636    628    -47    179    255       O  
ATOM   1748  N   MET B 102      13.488  22.084   4.682  1.00  7.23           N  
ANISOU 1748  N   MET B 102     1265   1088    392     16    -20    -75       N  
ATOM   1749  CA  MET B 102      13.510  20.964   5.578  1.00  6.81           C  
ANISOU 1749  CA  MET B 102     1133   1001    452   -125     15     22       C  
ATOM   1750  C   MET B 102      14.167  19.746   4.938  1.00  9.30           C  
ANISOU 1750  C   MET B 102     1240   1239   1052     37      2   -102       C  
ATOM   1751  O   MET B 102      14.078  19.533   3.704  1.00  8.21           O  
ANISOU 1751  O   MET B 102     1332   1359    426     94      0   -114       O  
ATOM   1752  CB  MET B 102      12.094  20.586   5.988  1.00  8.45           C  
ANISOU 1752  CB  MET B 102     1435   1293    481   -103    122     -7       C  
ATOM   1753  CG  MET B 102      11.260  21.723   6.524  1.00  8.22           C  
ANISOU 1753  CG  MET B 102     1320   1385    415   -108    233   -209       C  
ATOM   1754  SD  MET B 102      11.987  22.649   7.860  1.00  9.39           S  
ANISOU 1754  SD  MET B 102     1518   1441    606      3    131   -100       S  
ATOM   1755  CE  MET B 102      12.026  21.338   9.114  1.00  9.98           C  
ANISOU 1755  CE  MET B 102     2031   1416    344   -157    104    302       C  
ATOM   1756  N   VAL B 103      14.751  18.881   5.779  1.00  8.95           N  
ANISOU 1756  N   VAL B 103     1244   1399    756    130    -27     -9       N  
ATOM   1757  CA  VAL B 103      15.211  17.542   5.420  1.00  9.36           C  
ANISOU 1757  CA  VAL B 103     1223   1302   1031    118    105    180       C  
ATOM   1758  C   VAL B 103      14.792  16.660   6.599  1.00  8.71           C  
ANISOU 1758  C   VAL B 103     1331   1194    785      4   -166    -23       C  
ATOM   1759  O   VAL B 103      14.892  17.146   7.725  1.00  9.42           O  
ANISOU 1759  O   VAL B 103     1617   1452    508    -47    204    -47       O  
ATOM   1760  CB  VAL B 103      16.747  17.460   5.221  1.00  9.68           C  
ANISOU 1760  CB  VAL B 103     1421   1608    649    131     37    -91       C  
ATOM   1761  CG1 VAL B 103      17.139  16.031   4.791  1.00 11.07           C  
ANISOU 1761  CG1 VAL B 103     1789   1459    957    163    327   -204       C  
ATOM   1762  CG2 VAL B 103      17.266  18.524   4.211  1.00 10.12           C  
ANISOU 1762  CG2 VAL B 103     1412   1741    689    -20    102    538       C  
ATOM   1763  N   VAL B 104      14.346  15.433   6.360  1.00  8.57           N  
ANISOU 1763  N   VAL B 104     1386   1180    687      0    -19    133       N  
ATOM   1764  CA  VAL B 104      13.923  14.567   7.468  1.00  8.15           C  
ANISOU 1764  CA  VAL B 104     1518   1269    311     34     76    115       C  
ATOM   1765  C   VAL B 104      14.465  13.176   7.262  1.00  9.22           C  
ANISOU 1765  C   VAL B 104     1341   1224    936    125     71    185       C  
ATOM   1766  O   VAL B 104      14.405  12.627   6.153  1.00  9.28           O  
ANISOU 1766  O   VAL B 104     1645   1294    584     68    104     44       O  
ATOM   1767  CB  VAL B 104      12.362  14.484   7.613  1.00  8.50           C  
ANISOU 1767  CB  VAL B 104     1434   1429    364    -41     34     32       C  
ATOM   1768  CG1 VAL B 104      11.984  13.680   8.865  1.00 10.22           C  
ANISOU 1768  CG1 VAL B 104     1783   1717    380   -119    208    321       C  
ATOM   1769  CG2 VAL B 104      11.732  15.866   7.679  1.00 10.52           C  
ANISOU 1769  CG2 VAL B 104     1551   1431   1015    256    286    -12       C  
ATOM   1770  N   VAL B 105      15.005  12.581   8.316  1.00  9.12           N  
ANISOU 1770  N   VAL B 105     1537   1187    740    231    -14     70       N  
ATOM   1771  CA  VAL B 105      15.444  11.186   8.328  1.00 10.03           C  
ANISOU 1771  CA  VAL B 105     1560   1442    807    -51     37    149       C  
ATOM   1772  C   VAL B 105      14.876  10.500   9.564  1.00 11.54           C  
ANISOU 1772  C   VAL B 105     1754   1370   1259    132    397    210       C  
ATOM   1773  O   VAL B 105      14.435  11.177  10.481  1.00 11.74           O  
ANISOU 1773  O   VAL B 105     2108   1509    841    245    173    219       O  
ATOM   1774  CB  VAL B 105      17.007  11.066   8.292  1.00 10.23           C  
ANISOU 1774  CB  VAL B 105     1582   1311    993    151    112     16       C  
ATOM   1775  CG1 VAL B 105      17.579  11.889   7.081  1.00 12.34           C  
ANISOU 1775  CG1 VAL B 105     1782   1789   1118     15    429    217       C  
ATOM   1776  CG2 VAL B 105      17.643  11.550   9.562  1.00 11.16           C  
ANISOU 1776  CG2 VAL B 105     1672   2041    524    -38   -170    158       C  
ATOM   1777  N   ASP B 106      14.787   9.184   9.533  1.00 12.57           N  
ANISOU 1777  N   ASP B 106     2170   1512   1092    166    464    283       N  
ATOM   1778  CA  ASP B 106      14.387   8.469  10.720  1.00 15.57           C  
ANISOU 1778  CA  ASP B 106     2562   1529   1824    307    608    498       C  
ATOM   1779  C   ASP B 106      15.572   8.246  11.640  1.00 15.77           C  
ANISOU 1779  C   ASP B 106     2888   1523   1578     56    504    551       C  
ATOM   1780  O   ASP B 106      16.689   8.665  11.344  1.00 16.38           O  
ANISOU 1780  O   ASP B 106     2928   1898   1397     32     -1    412       O  
ATOM   1781  CB  ASP B 106      13.574   7.219  10.380  1.00 16.18           C  
ANISOU 1781  CB  ASP B 106     2391   1935   1821    421    964    397       C  
ATOM   1782  CG  ASP B 106      14.392   6.014   9.929  1.00 13.89           C  
ANISOU 1782  CG  ASP B 106     2097   1951   1226     73    519    391       C  
ATOM   1783  OD1 ASP B 106      15.630   5.993  10.062  1.00 14.60           O  
ANISOU 1783  OD1 ASP B 106     2093   1793   1658    246    488    352       O  
ATOM   1784  OD2 ASP B 106      13.689   5.019   9.646  1.00 18.06           O  
ANISOU 1784  OD2 ASP B 106     2755   1727   2378     77    300    267       O  
ATOM   1785  N   LYS B 107      15.307   7.639  12.802  1.00 18.92           N  
ANISOU 1785  N   LYS B 107     3545   1846   1796    199    492    523       N  
ATOM   1786  CA  LYS B 107      16.333   7.508  13.840  1.00 22.37           C  
ANISOU 1786  CA  LYS B 107     3914   2540   2042    118    251    487       C  
ATOM   1787  C   LYS B 107      17.541   6.665  13.398  1.00 19.45           C  
ANISOU 1787  C   LYS B 107     3146   2414   1828    193   -261    624       C  
ATOM   1788  O   LYS B 107      18.667   6.732  13.962  1.00 23.14           O  
ANISOU 1788  O   LYS B 107     4258   2797   1734    192   -300   1112       O  
ATOM   1789  CB  LYS B 107      15.679   6.915  15.092  1.00 26.03           C  
ANISOU 1789  CB  LYS B 107     4441   3128   2319    220    342    600       C  
ATOM   1790  CG  LYS B 107      15.170   5.473  14.912  1.00 27.78           C  
ANISOU 1790  CG  LYS B 107     4406   3234   2914     70    502    621       C  
ATOM   1791  CD  LYS B 107      14.335   4.982  16.105  1.00 31.07           C  
ANISOU 1791  CD  LYS B 107     4352   3946   3505      3    373    389       C  
ATOM   1792  CE  LYS B 107      12.971   5.689  16.222  1.00 29.97           C  
ANISOU 1792  CE  LYS B 107     3877   4096   3411     94    196    104       C  
ATOM   1793  NZ  LYS B 107      11.854   5.015  15.510  1.00 28.54           N  
ANISOU 1793  NZ  LYS B 107     4332   3626   2884     95    348   1015       N  
ATOM   1794  N   ASN B 108      17.310   5.840  12.382  1.00 16.93           N  
ANISOU 1794  N   ASN B 108     2958   2130   1342    149    216    586       N  
ATOM   1795  CA  ASN B 108      18.351   4.981  11.842  1.00 17.65           C  
ANISOU 1795  CA  ASN B 108     2719   2257   1730    363    153    715       C  
ATOM   1796  C   ASN B 108      19.033   5.518  10.589  1.00 17.15           C  
ANISOU 1796  C   ASN B 108     2448   2199   1869    419    200    599       C  
ATOM   1797  O   ASN B 108      19.903   4.870  10.042  1.00 19.76           O  
ANISOU 1797  O   ASN B 108     2465   2789   2252    373    412    746       O  
ATOM   1798  CB  ASN B 108      17.752   3.615  11.558  1.00 17.45           C  
ANISOU 1798  CB  ASN B 108     2991   1852   1787    429    565    755       C  
ATOM   1799  CG  ASN B 108      17.219   2.946  12.816  1.00 21.80           C  
ANISOU 1799  CG  ASN B 108     3652   2227   2404    247    324    859       C  
ATOM   1800  OD1 ASN B 108      17.868   2.946  13.877  1.00 26.03           O  
ANISOU 1800  OD1 ASN B 108     4056   2953   2879    543    328    899       O  
ATOM   1801  ND2 ASN B 108      16.019   2.441  12.718  1.00 25.76           N  
ANISOU 1801  ND2 ASN B 108     3540   2411   3836    -55   1154    560       N  
ATOM   1802  N   GLY B 109      18.643   6.709  10.179  1.00 15.79           N  
ANISOU 1802  N   GLY B 109     2297   2040   1660    135     27    411       N  
ATOM   1803  CA  GLY B 109      19.223   7.368   9.019  1.00 15.82           C  
ANISOU 1803  CA  GLY B 109     2089   2213   1710     23      1    379       C  
ATOM   1804  C   GLY B 109      18.553   7.087   7.676  1.00 13.81           C  
ANISOU 1804  C   GLY B 109     1803   1797   1647     58    127    412       C  
ATOM   1805  O   GLY B 109      19.115   7.442   6.634  1.00 14.98           O  
ANISOU 1805  O   GLY B 109     2226   1901   1564     58    318    261       O  
ATOM   1806  N   VAL B 110      17.388   6.461   7.669  1.00 13.30           N  
ANISOU 1806  N   VAL B 110     2074   1455   1522    235    106    297       N  
ATOM   1807  CA  VAL B 110      16.626   6.304   6.424  1.00 13.31           C  
ANISOU 1807  CA  VAL B 110     1835   1579   1642     49    160     24       C  
ATOM   1808  C   VAL B 110      16.084   7.669   6.042  1.00 12.08           C  
ANISOU 1808  C   VAL B 110     1960   1319   1310    177    245   -128       C  
ATOM   1809  O   VAL B 110      15.510   8.381   6.864  1.00 13.12           O  
ANISOU 1809  O   VAL B 110     2241   1466   1275    302    221    155       O  
ATOM   1810  CB  VAL B 110      15.492   5.291   6.567  1.00 14.93           C  
ANISOU 1810  CB  VAL B 110     2186   1452   2032    105    256    -42       C  
ATOM   1811  CG1 VAL B 110      14.665   5.216   5.304  1.00 15.88           C  
ANISOU 1811  CG1 VAL B 110     2245   1938   1847   -116    -13   -403       C  
ATOM   1812  CG2 VAL B 110      16.034   3.885   6.969  1.00 18.03           C  
ANISOU 1812  CG2 VAL B 110     2756   1407   2687    205    201     51       C  
ATOM   1813  N   VAL B 111      16.296   8.084   4.803  1.00 11.18           N  
ANISOU 1813  N   VAL B 111     1970   1374    903    298    372   -100       N  
ATOM   1814  CA  VAL B 111      15.832   9.388   4.355  1.00 10.98           C  
ANISOU 1814  CA  VAL B 111     1676   1462   1031     44    419   -266       C  
ATOM   1815  C   VAL B 111      14.319   9.378   4.147  1.00 10.29           C  
ANISOU 1815  C   VAL B 111     1733   1257    918    128    202    -23       C  
ATOM   1816  O   VAL B 111      13.802   8.562   3.406  1.00 13.00           O  
ANISOU 1816  O   VAL B 111     1928   1523   1486     79    284   -420       O  
ATOM   1817  CB  VAL B 111      16.582   9.911   3.086  1.00 12.11           C  
ANISOU 1817  CB  VAL B 111     1756   1812   1033     46    173   -154       C  
ATOM   1818  CG1 VAL B 111      16.040  11.293   2.674  1.00 11.41           C  
ANISOU 1818  CG1 VAL B 111     1713   1401   1219    278    -26    374       C  
ATOM   1819  CG2 VAL B 111      18.102   9.927   3.335  1.00 12.68           C  
ANISOU 1819  CG2 VAL B 111     1246   2087   1484    214    122     90       C  
ATOM   1820  N   LEU B 112      13.593  10.252   4.852  1.00 10.31           N  
ANISOU 1820  N   LEU B 112     1556   1444    916    190    293   -158       N  
ATOM   1821  CA  LEU B 112      12.166  10.364   4.708  1.00 10.06           C  
ANISOU 1821  CA  LEU B 112     1734   1372    716    107    249   -125       C  
ATOM   1822  C   LEU B 112      11.724  11.500   3.792  1.00  9.10           C  
ANISOU 1822  C   LEU B 112     1208   1502    745    -87    218   -126       C  
ATOM   1823  O   LEU B 112      10.654  11.392   3.156  1.00 11.15           O  
ANISOU 1823  O   LEU B 112     1575   1673    986   -224    -11   -144       O  
ATOM   1824  CB  LEU B 112      11.497  10.507   6.080  1.00 11.16           C  
ANISOU 1824  CB  LEU B 112     1701   1547    992     33    230    -76       C  
ATOM   1825  CG  LEU B 112      11.780   9.398   7.095  1.00 12.22           C  
ANISOU 1825  CG  LEU B 112     1721   1621   1302     77    213    344       C  
ATOM   1826  CD1 LEU B 112      11.015   9.744   8.364  1.00 13.39           C  
ANISOU 1826  CD1 LEU B 112     1974   1733   1380   -103    270    148       C  
ATOM   1827  CD2 LEU B 112      11.396   8.039   6.525  1.00 15.61           C  
ANISOU 1827  CD2 LEU B 112     2821   1510   1600   -174     56    137       C  
ATOM   1828  N   PHE B 113      12.502  12.572   3.745  1.00  8.41           N  
ANISOU 1828  N   PHE B 113     1316   1266    611    -63    124     -9       N  
ATOM   1829  CA  PHE B 113      12.092  13.764   3.010  1.00  8.95           C  
ANISOU 1829  CA  PHE B 113     1312   1457    629    181    196    -53       C  
ATOM   1830  C   PHE B 113      13.332  14.534   2.613  1.00  8.96           C  
ANISOU 1830  C   PHE B 113     1202   1482    720   -123    294    -19       C  
ATOM   1831  O   PHE B 113      14.127  14.937   3.460  1.00  8.90           O  
ANISOU 1831  O   PHE B 113     1242   1452    685    -88    -19    -74       O  
ATOM   1832  CB  PHE B 113      11.159  14.633   3.826  1.00  8.21           C  
ANISOU 1832  CB  PHE B 113     1094   1435    588    126     51    -74       C  
ATOM   1833  CG  PHE B 113      10.824  15.957   3.183  1.00  9.54           C  
ANISOU 1833  CG  PHE B 113     1105   1433   1087    168    256    -97       C  
ATOM   1834  CD1 PHE B 113       9.745  16.064   2.307  1.00  9.78           C  
ANISOU 1834  CD1 PHE B 113     1173   1479   1063   -100    396   -264       C  
ATOM   1835  CD2 PHE B 113      11.475  17.107   3.541  1.00  8.92           C  
ANISOU 1835  CD2 PHE B 113     1499   1220    670      0    294    -22       C  
ATOM   1836  CE1 PHE B 113       9.408  17.269   1.708  1.00  9.89           C  
ANISOU 1836  CE1 PHE B 113     1255   1589    913     46   -127     13       C  
ATOM   1837  CE2 PHE B 113      11.149  18.313   2.934  1.00  9.61           C  
ANISOU 1837  CE2 PHE B 113     1230   1416   1006    -51    324   -159       C  
ATOM   1838  CZ  PHE B 113      10.111  18.395   2.056  1.00  9.93           C  
ANISOU 1838  CZ  PHE B 113     1363   1339   1069    -29    114    -46       C  
ATOM   1839  N   ASP B 114      13.532  14.689   1.292  1.00  9.36           N  
ANISOU 1839  N   ASP B 114     1316   1471    767     27    198    -24       N  
ATOM   1840  CA  ASP B 114      14.589  15.522   0.761  1.00  8.55           C  
ANISOU 1840  CA  ASP B 114     1159   1445    643    135    196     32       C  
ATOM   1841  C   ASP B 114      14.368  15.787  -0.735  1.00  8.91           C  
ANISOU 1841  C   ASP B 114     1194   1148   1041    240    167     42       C  
ATOM   1842  O   ASP B 114      14.926  15.054  -1.568  1.00 10.02           O  
ANISOU 1842  O   ASP B 114     1458   1412    937    162    162   -183       O  
ATOM   1843  CB  ASP B 114      15.968  14.923   0.996  1.00  9.46           C  
ANISOU 1843  CB  ASP B 114     1570   1447    575   -129    213    -52       C  
ATOM   1844  CG  ASP B 114      17.102  15.878   0.582  1.00  9.58           C  
ANISOU 1844  CG  ASP B 114     1350   1346    942    125    166    -71       C  
ATOM   1845  OD1 ASP B 114      16.788  17.022   0.165  1.00  9.50           O  
ANISOU 1845  OD1 ASP B 114     1505   1448    654     26     68    -20       O  
ATOM   1846  OD2 ASP B 114      18.288  15.464   0.710  1.00  9.48           O  
ANISOU 1846  OD2 ASP B 114     1425   1588    587    204     93     63       O  
ATOM   1847  N   PRO B 115      13.609  16.845  -1.067  1.00  9.06           N  
ANISOU 1847  N   PRO B 115     1239   1474    727    160     83    -48       N  
ATOM   1848  CA  PRO B 115      13.302  17.094  -2.491  1.00  9.70           C  
ANISOU 1848  CA  PRO B 115     1251   1772    663   -135     88    250       C  
ATOM   1849  C   PRO B 115      14.520  17.390  -3.377  1.00 10.85           C  
ANISOU 1849  C   PRO B 115     1299   1773   1050   -122    106    -53       C  
ATOM   1850  O   PRO B 115      14.402  17.304  -4.582  1.00 12.62           O  
ANISOU 1850  O   PRO B 115     1784   2096    913    -48     93    -37       O  
ATOM   1851  CB  PRO B 115      12.341  18.286  -2.446  1.00 11.31           C  
ANISOU 1851  CB  PRO B 115     1253   2090    952    100    237     69       C  
ATOM   1852  CG  PRO B 115      11.651  18.178  -1.147  1.00 11.31           C  
ANISOU 1852  CG  PRO B 115     1289   1932   1076    173    188   -116       C  
ATOM   1853  CD  PRO B 115      12.737  17.634  -0.194  1.00  8.00           C  
ANISOU 1853  CD  PRO B 115     1082   1425    530    219    287   -212       C  
ATOM   1854  N   VAL B 116      15.644  17.784  -2.786  1.00  9.97           N  
ANISOU 1854  N   VAL B 116     1215   1769    803   -194    117   -128       N  
ATOM   1855  CA  VAL B 116      16.875  18.016  -3.540  1.00  9.83           C  
ANISOU 1855  CA  VAL B 116     1357   1500    877     -5    194    180       C  
ATOM   1856  C   VAL B 116      17.458  16.700  -4.061  1.00 10.96           C  
ANISOU 1856  C   VAL B 116     1736   1582    845      1    168      9       C  
ATOM   1857  O   VAL B 116      18.106  16.658  -5.111  1.00 12.01           O  
ANISOU 1857  O   VAL B 116     1648   1993    921   -125    286    -85       O  
ATOM   1858  CB  VAL B 116      17.913  18.843  -2.722  1.00  9.24           C  
ANISOU 1858  CB  VAL B 116     1610   1352    546   -201     54     -5       C  
ATOM   1859  CG1 VAL B 116      19.221  19.090  -3.485  1.00 11.26           C  
ANISOU 1859  CG1 VAL B 116     1384   1971    923   -297    497     66       C  
ATOM   1860  CG2 VAL B 116      17.297  20.120  -2.251  1.00 11.05           C  
ANISOU 1860  CG2 VAL B 116     1655   1563    979     49    336    -51       C  
ATOM   1861  N   ASN B 117      17.254  15.632  -3.295  1.00 11.12           N  
ANISOU 1861  N   ASN B 117     1674   1566    982    -27    174   -106       N  
ATOM   1862  CA  ASN B 117      17.865  14.337  -3.547  1.00 10.61           C  
ANISOU 1862  CA  ASN B 117     1620   1623    787     24    206   -151       C  
ATOM   1863  C   ASN B 117      16.781  13.249  -3.489  1.00 10.55           C  
ANISOU 1863  C   ASN B 117     1514   1456   1036    -38    356   -256       C  
ATOM   1864  O   ASN B 117      16.785  12.343  -2.637  1.00 11.53           O  
ANISOU 1864  O   ASN B 117     1808   1558   1013    -98    252   -280       O  
ATOM   1865  CB  ASN B 117      18.947  14.072  -2.504  1.00 10.61           C  
ANISOU 1865  CB  ASN B 117     1567   1692    771    194    385   -217       C  
ATOM   1866  CG  ASN B 117      20.038  15.099  -2.569  1.00 11.62           C  
ANISOU 1866  CG  ASN B 117     1366   1479   1568    -29     45   -293       C  
ATOM   1867  OD1 ASN B 117      20.742  15.185  -3.592  1.00 13.28           O  
ANISOU 1867  OD1 ASN B 117     1721   2065   1257   -158    293   -106       O  
ATOM   1868  ND2 ASN B 117      20.172  15.901  -1.518  1.00 10.19           N  
ANISOU 1868  ND2 ASN B 117     1389   1636    843    118    126   -197       N  
ATOM   1869  N   PRO B 118      15.837  13.302  -4.425  1.00 12.61           N  
ANISOU 1869  N   PRO B 118     1791   1802   1197   -285    273   -221       N  
ATOM   1870  CA  PRO B 118      14.670  12.433  -4.292  1.00 12.99           C  
ANISOU 1870  CA  PRO B 118     1653   1876   1405   -311    230   -251       C  
ATOM   1871  C   PRO B 118      14.961  10.946  -4.391  1.00 12.15           C  
ANISOU 1871  C   PRO B 118     1711   1855   1048   -458    145   -362       C  
ATOM   1872  O   PRO B 118      14.240  10.119  -3.800  1.00 14.12           O  
ANISOU 1872  O   PRO B 118     2048   1845   1473   -400    205   -256       O  
ATOM   1873  CB  PRO B 118      13.782  12.870  -5.464  1.00 14.58           C  
ANISOU 1873  CB  PRO B 118     1713   2200   1623   -342    -49   -414       C  
ATOM   1874  CG  PRO B 118      14.759  13.457  -6.449  1.00 12.92           C  
ANISOU 1874  CG  PRO B 118     1872   2108    927   -165   -153   -238       C  
ATOM   1875  CD  PRO B 118      15.743  14.196  -5.584  1.00 11.83           C  
ANISOU 1875  CD  PRO B 118     1835   1829    828   -130    165   -323       C  
ATOM   1876  N   LYS B 119      16.069  10.595  -5.034  1.00 12.88           N  
ANISOU 1876  N   LYS B 119     2052   1884    957   -257    356   -341       N  
ATOM   1877  CA  LYS B 119      16.422   9.189  -5.172  1.00 15.40           C  
ANISOU 1877  CA  LYS B 119     2490   2121   1237    -84    358   -544       C  
ATOM   1878  C   LYS B 119      16.848   8.576  -3.839  1.00 14.29           C  
ANISOU 1878  C   LYS B 119     2277   1618   1532     59    292   -481       C  
ATOM   1879  O   LYS B 119      16.859   7.343  -3.707  1.00 16.29           O  
ANISOU 1879  O   LYS B 119     2806   1924   1459     12    230   -554       O  
ATOM   1880  CB  LYS B 119      17.491   8.963  -6.264  1.00 16.53           C  
ANISOU 1880  CB  LYS B 119     2750   2040   1491    -69    346   -512       C  
ATOM   1881  CG  LYS B 119      17.039   9.323  -7.687  1.00 21.84           C  
ANISOU 1881  CG  LYS B 119     3522   3287   1487    139     85   -433       C  
ATOM   1882  CD  LYS B 119      18.200   9.166  -8.747  1.00 27.54           C  
ANISOU 1882  CD  LYS B 119     4417   3738   2308    530    570   -559       C  
ATOM   1883  CE  LYS B 119      18.473   7.719  -9.131  1.00 35.27           C  
ANISOU 1883  CE  LYS B 119     5913   4466   3021    168    -26     54       C  
ATOM   1884  N   THR B 120      17.224   9.422  -2.864  1.00 11.83           N  
ANISOU 1884  N   THR B 120     2103   1437    952    -28    161   -384       N  
ATOM   1885  CA  THR B 120      17.658   8.912  -1.580  1.00 11.34           C  
ANISOU 1885  CA  THR B 120     1674   1438   1194    154    313   -337       C  
ATOM   1886  C   THR B 120      16.472   8.614  -0.654  1.00 12.37           C  
ANISOU 1886  C   THR B 120     1803   1514   1380     22    154   -510       C  
ATOM   1887  O   THR B 120      16.642   7.879   0.301  1.00 13.35           O  
ANISOU 1887  O   THR B 120     2071   1613   1386    -47    320   -345       O  
ATOM   1888  CB  THR B 120      18.603   9.913  -0.842  1.00 12.93           C  
ANISOU 1888  CB  THR B 120     1760   1518   1635     95    172   -233       C  
ATOM   1889  OG1 THR B 120      17.886  11.098  -0.434  1.00 11.59           O  
ANISOU 1889  OG1 THR B 120     1646   1586   1169    -15    529   -470       O  
ATOM   1890  CG2 THR B 120      19.844  10.243  -1.666  1.00 13.76           C  
ANISOU 1890  CG2 THR B 120     1247   2002   1979    -97    660   -130       C  
ATOM   1891  N   VAL B 121      15.276   9.080  -0.985  1.00 12.40           N  
ANISOU 1891  N   VAL B 121     1716   1788   1208    -20    393   -336       N  
ATOM   1892  CA  VAL B 121      14.111   8.864  -0.118  1.00 12.91           C  
ANISOU 1892  CA  VAL B 121     1900   1497   1508     68    243   -336       C  
ATOM   1893  C   VAL B 121      13.757   7.375  -0.062  1.00 13.40           C  
ANISOU 1893  C   VAL B 121     2032   1664   1393   -147    342   -244       C  
ATOM   1894  O   VAL B 121      13.683   6.677  -1.099  1.00 15.66           O  
ANISOU 1894  O   VAL B 121     2261   2082   1606   -357    411   -694       O  
ATOM   1895  CB  VAL B 121      12.908   9.762  -0.542  1.00 13.66           C  
ANISOU 1895  CB  VAL B 121     1893   1891   1406    231    380   -159       C  
ATOM   1896  CG1 VAL B 121      11.642   9.387   0.239  1.00 14.54           C  
ANISOU 1896  CG1 VAL B 121     1728   2439   1358    243    490   -218       C  
ATOM   1897  CG2 VAL B 121      13.268  11.260  -0.376  1.00 14.10           C  
ANISOU 1897  CG2 VAL B 121     2354   1275   1728     62    219   -548       C  
ATOM   1898  N   GLY B 122      13.593   6.871   1.162  1.00 12.89           N  
ANISOU 1898  N   GLY B 122     1853   1695   1348    -78    116   -431       N  
ATOM   1899  CA  GLY B 122      13.280   5.479   1.389  1.00 14.50           C  
ANISOU 1899  CA  GLY B 122     2167   1777   1566   -202    277   -596       C  
ATOM   1900  C   GLY B 122      14.486   4.556   1.500  1.00 16.13           C  
ANISOU 1900  C   GLY B 122     2515   1613   1999   -199    347   -230       C  
ATOM   1901  O   GLY B 122      14.326   3.372   1.808  1.00 19.68           O  
ANISOU 1901  O   GLY B 122     3029   1695   2753   -100    228   -304       O  
ATOM   1902  N   GLN B 123      15.681   5.137   1.283  1.00 15.84           N  
ANISOU 1902  N   GLN B 123     2159   1887   1970     72    268   -333       N  
ATOM   1903  CA  GLN B 123      16.959   4.452   1.397  1.00 17.78           C  
ANISOU 1903  CA  GLN B 123     2368   2030   2356     85     47   -336       C  
ATOM   1904  C   GLN B 123      17.659   4.823   2.696  1.00 14.14           C  
ANISOU 1904  C   GLN B 123     2110   1626   1633    223    116   -193       C  
ATOM   1905  O   GLN B 123      17.520   5.946   3.164  1.00 14.59           O  
ANISOU 1905  O   GLN B 123     2322   1559   1662    238    320   -323       O  
ATOM   1906  CB  GLN B 123      17.907   4.864   0.250  1.00 20.32           C  
ANISOU 1906  CB  GLN B 123     2712   2408   2598    395    587   -422       C  
ATOM   1907  CG  GLN B 123      17.378   4.671  -1.159  1.00 25.08           C  
ANISOU 1907  CG  GLN B 123     3622   2664   3242    219    294   -596       C  
ATOM   1908  CD  GLN B 123      18.411   4.929  -2.292  1.00 30.23           C  
ANISOU 1908  CD  GLN B 123     4120   3533   3832    -60    198   -454       C  
ATOM   1909  OE1 GLN B 123      18.285   4.334  -3.362  1.00 34.11           O  
ANISOU 1909  OE1 GLN B 123     4975   4124   3861    720    197   -763       O  
ATOM   1910  NE2 GLN B 123      19.359   5.867  -2.094  1.00 22.89           N  
ANISOU 1910  NE2 GLN B 123     3706   2777   2211    383    550    124       N  
ATOM   1911  N   SER B 124      18.576   3.986   3.146  1.00 15.45           N  
ANISOU 1911  N   SER B 124     2238   1635   1995    217     16   -130       N  
ATOM   1912  CA  SER B 124      19.529   4.428   4.166  1.00 17.10           C  
ANISOU 1912  CA  SER B 124     2641   1601   2253    135    129    -49       C  
ATOM   1913  C   SER B 124      20.356   5.567   3.621  1.00 15.62           C  
ANISOU 1913  C   SER B 124     2328   1727   1880     33    400    145       C  
ATOM   1914  O   SER B 124      20.883   5.501   2.512  1.00 16.55           O  
ANISOU 1914  O   SER B 124     2489   2111   1685    134    244   -219       O  
ATOM   1915  CB  SER B 124      20.466   3.311   4.590  1.00 17.55           C  
ANISOU 1915  CB  SER B 124     2593   1769   2304    426    268    202       C  
ATOM   1916  OG  SER B 124      21.449   3.772   5.502  1.00 19.00           O  
ANISOU 1916  OG  SER B 124     2480   2219   2518    288    -11    283       O  
ATOM   1917  N   GLY B 125      20.478   6.627   4.412  1.00 15.25           N  
ANISOU 1917  N   GLY B 125     2443   1703   1645     80    -41    -43       N  
ATOM   1918  CA  GLY B 125      21.362   7.698   4.059  1.00 15.84           C  
ANISOU 1918  CA  GLY B 125     2345   1808   1862    358    327    -81       C  
ATOM   1919  C   GLY B 125      22.690   7.704   4.787  1.00 13.28           C  
ANISOU 1919  C   GLY B 125     2109   1320   1614    236    399    -37       C  
ATOM   1920  O   GLY B 125      23.437   8.679   4.688  1.00 14.21           O  
ANISOU 1920  O   GLY B 125     2250   1491   1654     64    234    159       O  
ATOM   1921  N   LEU B 126      23.026   6.600   5.458  1.00 13.25           N  
ANISOU 1921  N   LEU B 126     2082   1417   1535    166    239    258       N  
ATOM   1922  CA  LEU B 126      24.235   6.562   6.270  1.00 16.20           C  
ANISOU 1922  CA  LEU B 126     2182   2055   1916    130    168    299       C  
ATOM   1923  C   LEU B 126      25.504   6.745   5.483  1.00 15.69           C  
ANISOU 1923  C   LEU B 126     2329   1813   1817     86    163    363       C  
ATOM   1924  O   LEU B 126      26.446   7.331   5.998  1.00 18.85           O  
ANISOU 1924  O   LEU B 126     2580   2651   1929   -461     85    519       O  
ATOM   1925  CB  LEU B 126      24.323   5.302   7.134  1.00 16.05           C  
ANISOU 1925  CB  LEU B 126     2107   2235   1754    -13    230    484       C  
ATOM   1926  CG  LEU B 126      23.252   5.194   8.212  1.00 16.53           C  
ANISOU 1926  CG  LEU B 126     2458   2055   1764     51    195    547       C  
ATOM   1927  CD1 LEU B 126      23.337   3.819   8.884  1.00 19.09           C  
ANISOU 1927  CD1 LEU B 126     2860   2123   2268    176    195    866       C  
ATOM   1928  CD2 LEU B 126      23.293   6.323   9.212  1.00 17.93           C  
ANISOU 1928  CD2 LEU B 126     2914   2964    934    382    133    -88       C  
ATOM   1929  N   ASP B 127      25.498   6.354   4.211  1.00 15.20           N  
ANISOU 1929  N   ASP B 127     2226   1756   1790    190    345    393       N  
ATOM   1930  CA  ASP B 127      26.694   6.530   3.360  1.00 15.91           C  
ANISOU 1930  CA  ASP B 127     2361   1691   1992    279    539    249       C  
ATOM   1931  C   ASP B 127      26.545   7.639   2.336  1.00 15.85           C  
ANISOU 1931  C   ASP B 127     2507   1662   1852    324    515    -33       C  
ATOM   1932  O   ASP B 127      27.442   7.839   1.511  1.00 18.08           O  
ANISOU 1932  O   ASP B 127     2835   1938   2097     57    878    178       O  
ATOM   1933  CB  ASP B 127      27.072   5.214   2.672  1.00 18.22           C  
ANISOU 1933  CB  ASP B 127     2763   1620   2538     77    582    414       C  
ATOM   1934  CG  ASP B 127      27.433   4.120   3.672  1.00 20.15           C  
ANISOU 1934  CG  ASP B 127     3428   1860   2366    352    532    343       C  
ATOM   1935  OD1 ASP B 127      27.916   4.464   4.779  1.00 24.10           O  
ANISOU 1935  OD1 ASP B 127     3266   2348   3541    558   -276    477       O  
ATOM   1936  OD2 ASP B 127      27.379   2.921   3.284  1.00 25.41           O  
ANISOU 1936  OD2 ASP B 127     4431   1994   3229    500    542    177       O  
ATOM   1937  N   ALA B 128      25.470   8.428   2.457  1.00 14.88           N  
ANISOU 1937  N   ALA B 128     2519   1566   1566    157    517    357       N  
ATOM   1938  CA  ALA B 128      25.269   9.587   1.591  1.00 14.68           C  
ANISOU 1938  CA  ALA B 128     2639   1470   1466      0    271    209       C  
ATOM   1939  C   ALA B 128      26.343  10.624   1.893  1.00 15.03           C  
ANISOU 1939  C   ALA B 128     2611   1460   1637     61    294    352       C  
ATOM   1940  O   ALA B 128      26.566  11.008   3.024  1.00 17.30           O  
ANISOU 1940  O   ALA B 128     3111   2001   1461     43    107    192       O  
ATOM   1941  CB  ALA B 128      23.883  10.171   1.810  1.00 15.53           C  
ANISOU 1941  CB  ALA B 128     2435   1842   1622    181    221    421       C  
ATOM   1942  N   GLN B 129      26.956  11.155   0.854  1.00 14.06           N  
ANISOU 1942  N   GLN B 129     2498   1737   1103    183    177     97       N  
ATOM   1943  CA AGLN B 129      27.981  12.194   1.019  0.50 12.60           C  
ANISOU 1943  CA AGLN B 129     1477   1933   1375    330    -42    125       C  
ATOM   1944  CA BGLN B 129      27.953  12.146   1.002  0.50 13.54           C  
ANISOU 1944  CA BGLN B 129     1626   2037   1480    284     25    170       C  
ATOM   1945  C   GLN B 129      27.638  13.373   0.142  1.00 11.55           C  
ANISOU 1945  C   GLN B 129     1344   1717   1327     64    239    219       C  
ATOM   1946  O   GLN B 129      27.243  13.223  -1.025  1.00 13.26           O  
ANISOU 1946  O   GLN B 129     1807   1622   1606    -74   -126    -39       O  
ATOM   1947  CB AGLN B 129      29.403  11.756   0.623  0.50 13.48           C  
ANISOU 1947  CB AGLN B 129     1874   2075   1170    559    151     80       C  
ATOM   1948  CB BGLN B 129      29.245  11.524   0.556  0.50 16.14           C  
ANISOU 1948  CB BGLN B 129     2191   2439   1500    629    175    281       C  
ATOM   1949  CG AGLN B 129      30.169  10.942   1.628  0.50 11.10           C  
ANISOU 1949  CG AGLN B 129     1483   1663   1070    294   -215   -169       C  
ATOM   1950  CG BGLN B 129      30.382  12.184   1.130  0.50 15.00           C  
ANISOU 1950  CG BGLN B 129     1860   2301   1537     15    259    -14       C  
ATOM   1951  CD AGLN B 129      31.571  10.657   1.185  0.50  9.64           C  
ANISOU 1951  CD AGLN B 129     1338   1338    985   -126   -599    -81       C  
ATOM   1952  CD BGLN B 129      31.669  11.488   0.800  0.50 17.76           C  
ANISOU 1952  CD BGLN B 129     2195   2678   1874    598     87    233       C  
ATOM   1953  OE1AGLN B 129      32.325  11.577   0.829  0.50 14.66           O  
ANISOU 1953  OE1AGLN B 129     1730   1607   2233    307    112    278       O  
ATOM   1954  OE1BGLN B 129      32.108  11.502  -0.339  0.50 16.75           O  
ANISOU 1954  OE1BGLN B 129     2540   2768   1056     63    187    365       O  
ATOM   1955  NE2AGLN B 129      31.939   9.397   1.191  0.50 17.14           N  
ANISOU 1955  NE2AGLN B 129     2778   2172   1561    494   -386    113       N  
ATOM   1956  NE2BGLN B 129      32.269  10.852   1.792  0.50 15.64           N  
ANISOU 1956  NE2BGLN B 129     1678   3204   1059    519     13    678       N  
ATOM   1957  N   SER B 130      27.812  14.552   0.707  1.00 11.26           N  
ANISOU 1957  N   SER B 130     1510   1539   1229    154    229    135       N  
ATOM   1958  CA  SER B 130      27.715  15.782  -0.037  1.00  9.50           C  
ANISOU 1958  CA  SER B 130     1077   1411   1121    153    108    -21       C  
ATOM   1959  C   SER B 130      28.896  15.853  -1.008  1.00  8.91           C  
ANISOU 1959  C   SER B 130     1062   1392    931    225   -196   -123       C  
ATOM   1960  O   SER B 130      29.898  15.148  -0.869  1.00 10.68           O  
ANISOU 1960  O   SER B 130     1239   1746   1070    232     57   -116       O  
ATOM   1961  CB  SER B 130      27.765  16.967   0.928  1.00 10.81           C  
ANISOU 1961  CB  SER B 130     1294   1609   1200    161    406    176       C  
ATOM   1962  OG  SER B 130      28.986  17.043   1.637  1.00 11.33           O  
ANISOU 1962  OG  SER B 130     1321   1877   1107    296    137      3       O  
ATOM   1963  N   VAL B 131      28.843  16.830  -1.900  1.00 10.03           N  
ANISOU 1963  N   VAL B 131     1114   1544   1150    191    183     50       N  
ATOM   1964  CA  VAL B 131      29.925  16.976  -2.894  1.00  9.82           C  
ANISOU 1964  CA  VAL B 131     1105   1564   1060    -48    185    -35       C  
ATOM   1965  C   VAL B 131      31.253  17.363  -2.249  1.00 10.46           C  
ANISOU 1965  C   VAL B 131     1056   1597   1319     95    301   -130       C  
ATOM   1966  O   VAL B 131      32.311  17.154  -2.839  1.00 10.39           O  
ANISOU 1966  O   VAL B 131     1086   1932    928    200    276    -56       O  
ATOM   1967  CB  VAL B 131      29.530  17.967  -4.031  1.00  9.13           C  
ANISOU 1967  CB  VAL B 131     1066   1821    581    -50    510     78       C  
ATOM   1968  CG1 VAL B 131      28.437  17.348  -4.903  1.00 12.46           C  
ANISOU 1968  CG1 VAL B 131     1350   2423    959   -365    131    -36       C  
ATOM   1969  CG2 VAL B 131      29.132  19.328  -3.492  1.00 11.31           C  
ANISOU 1969  CG2 VAL B 131     1548   1556   1191    265    394   -170       C  
ATOM   1970  N   ASP B 132      31.195  18.042  -1.096  1.00  9.58           N  
ANISOU 1970  N   ASP B 132     1035   1780    824    315    356    -95       N  
ATOM   1971  CA  ASP B 132      32.375  18.334  -0.289  1.00  9.81           C  
ANISOU 1971  CA  ASP B 132     1145   1664    917    171    242    -25       C  
ATOM   1972  C   ASP B 132      32.739  17.278   0.742  1.00 10.75           C  
ANISOU 1972  C   ASP B 132     1389   1450   1244     66    176   -248       C  
ATOM   1973  O   ASP B 132      33.582  17.530   1.620  1.00 12.44           O  
ANISOU 1973  O   ASP B 132     1399   1913   1413     27    124    -73       O  
ATOM   1974  CB  ASP B 132      32.304  19.748   0.364  1.00 10.08           C  
ANISOU 1974  CB  ASP B 132     1050   1654   1124    146    -50     40       C  
ATOM   1975  CG  ASP B 132      31.120  19.962   1.305  1.00 11.66           C  
ANISOU 1975  CG  ASP B 132     1199   1833   1397    200   -261   -319       C  
ATOM   1976  OD1 ASP B 132      30.053  19.377   1.105  1.00 10.95           O  
ANISOU 1976  OD1 ASP B 132     1275   1780   1104    176    312   -229       O  
ATOM   1977  OD2 ASP B 132      31.244  20.880   2.137  1.00 17.98           O  
ANISOU 1977  OD2 ASP B 132     1801   2997   2032    345   -228  -1441       O  
ATOM   1978  N   GLY B 133      32.197  16.087   0.585  1.00 10.86           N  
ANISOU 1978  N   GLY B 133     1275   1656   1193    184     79     49       N  
ATOM   1979  CA  GLY B 133      32.651  14.948   1.334  1.00 10.92           C  
ANISOU 1979  CA  GLY B 133     1281   1790   1076     18    226    212       C  
ATOM   1980  C   GLY B 133      32.119  14.768   2.717  1.00 12.52           C  
ANISOU 1980  C   GLY B 133     1359   1916   1480    466    275    246       C  
ATOM   1981  O   GLY B 133      32.723  14.035   3.507  1.00 16.47           O  
ANISOU 1981  O   GLY B 133     1885   2637   1733    884    293    417       O  
ATOM   1982  N   VAL B 134      30.988  15.402   3.010  1.00 11.67           N  
ANISOU 1982  N   VAL B 134     1146   2110   1178    453    163    408       N  
ATOM   1983  CA  VAL B 134      30.402  15.312   4.339  1.00 12.21           C  
ANISOU 1983  CA  VAL B 134     1427   2126   1086    287    104    233       C  
ATOM   1984  C   VAL B 134      29.303  14.248   4.355  1.00 11.36           C  
ANISOU 1984  C   VAL B 134     1514   1608   1192    472     27    153       C  
ATOM   1985  O   VAL B 134      28.411  14.272   3.515  1.00 11.30           O  
ANISOU 1985  O   VAL B 134     1454   1902    935    302    168     89       O  
ATOM   1986  CB  VAL B 134      29.812  16.685   4.769  1.00 12.90           C  
ANISOU 1986  CB  VAL B 134     1530   2023   1346    209    393    121       C  
ATOM   1987  CG1 VAL B 134      29.170  16.593   6.123  1.00 13.59           C  
ANISOU 1987  CG1 VAL B 134     1633   2691    839    285     33    221       C  
ATOM   1988  CG2 VAL B 134      30.878  17.771   4.727  1.00 12.50           C  
ANISOU 1988  CG2 VAL B 134     1628   2303    818   -132    148   -158       C  
ATOM   1989  N   TYR B 135      29.345  13.345   5.335  1.00 12.77           N  
ANISOU 1989  N   TYR B 135     1535   1945   1371    617    226    523       N  
ATOM   1990  CA  TYR B 135      28.269  12.390   5.534  1.00 12.65           C  
ANISOU 1990  CA  TYR B 135     1626   2006   1172    538    138    388       C  
ATOM   1991  C   TYR B 135      27.157  13.141   6.241  1.00 11.79           C  
ANISOU 1991  C   TYR B 135     1416   1897   1165    393    204    269       C  
ATOM   1992  O   TYR B 135      27.053  13.135   7.483  1.00 13.05           O  
ANISOU 1992  O   TYR B 135     1628   2313   1015    488    157    306       O  
ATOM   1993  CB  TYR B 135      28.747  11.192   6.388  1.00 14.17           C  
ANISOU 1993  CB  TYR B 135     1715   2135   1532    718    387    136       C  
ATOM   1994  CG  TYR B 135      29.702  10.281   5.665  1.00 16.53           C  
ANISOU 1994  CG  TYR B 135     2134   2494   1652    537    627    755       C  
ATOM   1995  CD1 TYR B 135      29.245   9.410   4.684  1.00 19.31           C  
ANISOU 1995  CD1 TYR B 135     2091   2322   2923    699   1031    136       C  
ATOM   1996  CD2 TYR B 135      31.039  10.277   5.985  1.00 20.81           C  
ANISOU 1996  CD2 TYR B 135     2319   3966   1622    866    575   -110       C  
ATOM   1997  CE1 TYR B 135      30.108   8.535   4.030  1.00 24.95           C  
ANISOU 1997  CE1 TYR B 135     3190   2474   3813    487   1045    -14       C  
ATOM   1998  CE2 TYR B 135      31.927   9.462   5.289  1.00 24.40           C  
ANISOU 1998  CE2 TYR B 135     2255   3748   3264   1434    408     35       C  
ATOM   1999  CZ  TYR B 135      31.436   8.536   4.353  1.00 19.65           C  
ANISOU 1999  CZ  TYR B 135     3040   2461   1966   1139    632    499       C  
ATOM   2000  OH  TYR B 135      32.290   7.614   3.712  1.00 25.12           O  
ANISOU 2000  OH  TYR B 135     3519   3182   2841   1640   1325    223       O  
ATOM   2001  N   TYR B 136      26.309  13.813   5.492  1.00 11.10           N  
ANISOU 2001  N   TYR B 136     1524   1685   1007    300    319    164       N  
ATOM   2002  CA  TYR B 136      25.393  14.752   6.093  1.00  9.81           C  
ANISOU 2002  CA  TYR B 136     1468   1423    837    128     63      0       C  
ATOM   2003  C   TYR B 136      24.340  14.078   6.990  1.00 10.47           C  
ANISOU 2003  C   TYR B 136     1108   1524   1344    156    109     69       C  
ATOM   2004  O   TYR B 136      23.899  14.675   7.974  1.00 10.75           O  
ANISOU 2004  O   TYR B 136     1473   1780    829    267    208    -25       O  
ATOM   2005  CB  TYR B 136      24.759  15.704   5.049  1.00 10.64           C  
ANISOU 2005  CB  TYR B 136     1605   1482    956    100    330      4       C  
ATOM   2006  CG  TYR B 136      23.979  15.046   3.931  1.00  9.91           C  
ANISOU 2006  CG  TYR B 136     1537   1339    887     71    158    -99       C  
ATOM   2007  CD1 TYR B 136      22.613  14.837   4.051  1.00 10.78           C  
ANISOU 2007  CD1 TYR B 136     1632   1876    585     94    205     -6       C  
ATOM   2008  CD2 TYR B 136      24.607  14.610   2.767  1.00 10.26           C  
ANISOU 2008  CD2 TYR B 136     1502   1583    812    161    138    -80       C  
ATOM   2009  CE1 TYR B 136      21.884  14.203   3.065  1.00 10.95           C  
ANISOU 2009  CE1 TYR B 136     1431   1726   1002    122    248     44       C  
ATOM   2010  CE2 TYR B 136      23.889  13.983   1.773  1.00 11.29           C  
ANISOU 2010  CE2 TYR B 136     1611   1370   1305    -34    350    -76       C  
ATOM   2011  CZ  TYR B 136      22.535  13.816   1.887  1.00 12.06           C  
ANISOU 2011  CZ  TYR B 136     1511   1562   1507    -36    186     75       C  
ATOM   2012  OH  TYR B 136      21.861  13.147   0.899  1.00 12.51           O  
ANISOU 2012  OH  TYR B 136     1760   1620   1371    125    -13    -68       O  
ATOM   2013  N   VAL B 137      23.880  12.896   6.622  1.00 10.42           N  
ANISOU 2013  N   VAL B 137     1424   1476   1057     18    219    150       N  
ATOM   2014  CA  VAL B 137      22.898  12.210   7.456  1.00  9.19           C  
ANISOU 2014  CA  VAL B 137     1388   1245    858    138     50    191       C  
ATOM   2015  C   VAL B 137      23.536  11.738   8.775  1.00 11.67           C  
ANISOU 2015  C   VAL B 137     1531   1760   1140    448     95    246       C  
ATOM   2016  O   VAL B 137      22.920  11.871   9.817  1.00 12.32           O  
ANISOU 2016  O   VAL B 137     1738   1856   1086    294    289    107       O  
ATOM   2017  CB  VAL B 137      22.192  11.058   6.723  1.00 11.98           C  
ANISOU 2017  CB  VAL B 137     1438   1394   1718    320    285    178       C  
ATOM   2018  CG1 VAL B 137      21.300  10.218   7.671  1.00 13.08           C  
ANISOU 2018  CG1 VAL B 137     2026   1794   1146   -130    212    425       C  
ATOM   2019  CG2 VAL B 137      21.442  11.586   5.499  1.00 12.16           C  
ANISOU 2019  CG2 VAL B 137     1923   1475   1221    392   -269    240       C  
ATOM   2020  N   ARG B 138      24.770  11.280   8.738  1.00 12.37           N  
ANISOU 2020  N   ARG B 138     1833   1657   1207    520     63    211       N  
ATOM   2021  CA  ARG B 138      25.502  10.986   9.982  1.00 11.96           C  
ANISOU 2021  CA  ARG B 138     1606   1797   1142    400     85    267       C  
ATOM   2022  C   ARG B 138      25.587  12.249  10.849  1.00 11.96           C  
ANISOU 2022  C   ARG B 138     1743   1799    999    445     34    216       C  
ATOM   2023  O   ARG B 138      25.382  12.197  12.060  1.00 14.05           O  
ANISOU 2023  O   ARG B 138     1821   2329   1188    341     87    385       O  
ATOM   2024  CB  ARG B 138      26.889  10.465   9.691  1.00 13.43           C  
ANISOU 2024  CB  ARG B 138     1739   2181   1181    512   -177    132       C  
ATOM   2025  CG  ARG B 138      26.925   9.173   8.960  1.00 13.73           C  
ANISOU 2025  CG  ARG B 138     1985   2131   1099    435    285    515       C  
ATOM   2026  CD  ARG B 138      28.334   8.623   8.859  1.00 15.13           C  
ANISOU 2026  CD  ARG B 138     2323   2072   1353    563    269    577       C  
ATOM   2027  NE  ARG B 138      28.423   7.549   7.866  1.00 15.90           N  
ANISOU 2027  NE  ARG B 138     1943   2194   1902    795    511    341       N  
ATOM   2028  CZ  ARG B 138      29.554   6.911   7.565  1.00 18.39           C  
ANISOU 2028  CZ  ARG B 138     2630   2310   2045    612    229    241       C  
ATOM   2029  NH1 ARG B 138      30.671   7.174   8.240  1.00 21.80           N  
ANISOU 2029  NH1 ARG B 138     3255   3584   1440   1270   -172    -24       N  
ATOM   2030  NH2 ARG B 138      29.539   5.971   6.619  1.00 18.77           N  
ANISOU 2030  NH2 ARG B 138     2700   2409   2021    601    158     51       N  
ATOM   2031  N   GLY B 139      25.831  13.395  10.231  1.00 12.08           N  
ANISOU 2031  N   GLY B 139     1500   1801   1286    383    -21    216       N  
ATOM   2032  CA  GLY B 139      25.841  14.658  10.945  1.00 11.92           C  
ANISOU 2032  CA  GLY B 139     1263   1903   1360    286   -133    267       C  
ATOM   2033  C   GLY B 139      24.491  14.903  11.593  1.00 11.29           C  
ANISOU 2033  C   GLY B 139     1530   1593   1166    217     20   -132       C  
ATOM   2034  O   GLY B 139      24.433  15.389  12.744  1.00 11.79           O  
ANISOU 2034  O   GLY B 139     1553   1937    989    168   -198    -35       O  
ATOM   2035  N   TYR B 140      23.400  14.734  10.847  1.00 11.07           N  
ANISOU 2035  N   TYR B 140     1299   1962    942    232    -50     53       N  
ATOM   2036  CA  TYR B 140      22.081  14.982  11.423  1.00 10.64           C  
ANISOU 2036  CA  TYR B 140     1408   1823    810    265    -94    224       C  
ATOM   2037  C   TYR B 140      21.882  14.133  12.711  1.00 10.67           C  
ANISOU 2037  C   TYR B 140     1283   1797    972    278    -99    201       C  
ATOM   2038  O   TYR B 140      21.316  14.601  13.714  1.00 12.41           O  
ANISOU 2038  O   TYR B 140     1632   1970   1111    392    154    159       O  
ATOM   2039  CB  TYR B 140      20.938  14.648  10.452  1.00  9.99           C  
ANISOU 2039  CB  TYR B 140     1359   1632    806    340   -113     98       C  
ATOM   2040  CG  TYR B 140      20.825  15.406   9.153  1.00 10.00           C  
ANISOU 2040  CG  TYR B 140     1472   1133   1195    273    119    175       C  
ATOM   2041  CD1 TYR B 140      21.453  16.611   8.916  1.00  9.62           C  
ANISOU 2041  CD1 TYR B 140     1495   1432    725    125   -142    155       C  
ATOM   2042  CD2 TYR B 140      20.156  14.806   8.104  1.00 10.55           C  
ANISOU 2042  CD2 TYR B 140     1437   1430   1140    -45    176     28       C  
ATOM   2043  CE1 TYR B 140      21.371  17.267   7.701  1.00  9.39           C  
ANISOU 2043  CE1 TYR B 140     1472   1467    626    -58    191    152       C  
ATOM   2044  CE2 TYR B 140      20.066  15.438   6.880  1.00 11.25           C  
ANISOU 2044  CE2 TYR B 140     1937   1635    701    -33     30    295       C  
ATOM   2045  CZ  TYR B 140      20.664  16.661   6.663  1.00 10.31           C  
ANISOU 2045  CZ  TYR B 140     1317   1461   1139     65    106     13       C  
ATOM   2046  OH  TYR B 140      20.553  17.295   5.426  1.00 11.30           O  
ANISOU 2046  OH  TYR B 140     1829   1566    895     91    -41    109       O  
ATOM   2047  N   LEU B 141      22.253  12.881  12.619  1.00 11.11           N  
ANISOU 2047  N   LEU B 141     1563   1767    892    379    288    282       N  
ATOM   2048  CA  LEU B 141      22.057  11.912  13.698  1.00 11.24           C  
ANISOU 2048  CA  LEU B 141     1555   1805    909    145     24    375       C  
ATOM   2049  C   LEU B 141      22.963  12.207  14.909  1.00 13.22           C  
ANISOU 2049  C   LEU B 141     1660   2156   1207    387   -181    190       C  
ATOM   2050  O   LEU B 141      22.522  12.106  16.053  1.00 15.19           O  
ANISOU 2050  O   LEU B 141     2124   2392   1254    372    254    251       O  
ATOM   2051  CB  LEU B 141      22.300  10.486  13.184  1.00 11.47           C  
ANISOU 2051  CB  LEU B 141     1666   1980    710    338    130    566       C  
ATOM   2052  CG  LEU B 141      21.334   9.955  12.105  1.00 13.31           C  
ANISOU 2052  CG  LEU B 141     1831   1878   1348     55     85    330       C  
ATOM   2053  CD1 LEU B 141      21.714   8.527  11.726  1.00 16.01           C  
ANISOU 2053  CD1 LEU B 141     2329   1988   1763    470     38   -160       C  
ATOM   2054  CD2 LEU B 141      19.896  10.013  12.536  1.00 16.00           C  
ANISOU 2054  CD2 LEU B 141     2000   2663   1416    258    326    376       C  
ATOM   2055  N   GLU B 142      24.205  12.583  14.660  1.00 12.68           N  
ANISOU 2055  N   GLU B 142     1667   2331    818    270    -46     99       N  
ATOM   2056  CA  GLU B 142      25.162  12.929  15.731  1.00 14.41           C  
ANISOU 2056  CA  GLU B 142     1650   2438   1386    290     27    228       C  
ATOM   2057  C   GLU B 142      24.648  14.150  16.471  1.00 14.87           C  
ANISOU 2057  C   GLU B 142     1875   2478   1296    387     23    380       C  
ATOM   2058  O   GLU B 142      24.645  14.166  17.699  1.00 16.78           O  
ANISOU 2058  O   GLU B 142     2014   3123   1236    402   -134    459       O  
ATOM   2059  CB  GLU B 142      26.545  13.187  15.126  1.00 15.38           C  
ANISOU 2059  CB  GLU B 142     1792   2876   1174    298   -277   -153       C  
ATOM   2060  CG AGLU B 142      27.227  11.962  14.591  0.70 15.94           C  
ANISOU 2060  CG AGLU B 142     2196   2848   1011    227   -229    270       C  
ATOM   2061  CD AGLU B 142      28.496  12.283  13.804  0.70 20.86           C  
ANISOU 2061  CD AGLU B 142     2799   3310   1814    240    498    336       C  
ATOM   2062  OE1AGLU B 142      29.001  13.448  13.837  0.70 26.49           O  
ANISOU 2062  OE1AGLU B 142     2671   3613   3781    332    716    144       O  
ATOM   2063  OE2AGLU B 142      29.015  11.329  13.185  0.70 28.28           O  
ANISOU 2063  OE2AGLU B 142     3103   4504   3137    656    654   -592       O  
ATOM   2064  N   ALA B 143      24.165  15.156  15.727  1.00 12.72           N  
ANISOU 2064  N   ALA B 143     1596   2130   1105    446   -130    294       N  
ATOM   2065  CA  ALA B 143      23.623  16.354  16.338  1.00 12.73           C  
ANISOU 2065  CA  ALA B 143     1431   2235   1170    178    -89    139       C  
ATOM   2066  C   ALA B 143      22.396  15.990  17.180  1.00 13.82           C  
ANISOU 2066  C   ALA B 143     1573   2346   1331     17    -17     92       C  
ATOM   2067  O   ALA B 143      22.225  16.511  18.299  1.00 14.40           O  
ANISOU 2067  O   ALA B 143     1705   2518   1245    317    -84    180       O  
ATOM   2068  CB  ALA B 143      23.319  17.436  15.305  1.00 12.57           C  
ANISOU 2068  CB  ALA B 143     2024   2003    748    192     61    186       C  
ATOM   2069  N   ALA B 144      21.503  15.164  16.625  1.00 12.97           N  
ANISOU 2069  N   ALA B 144     1514   2200   1212    166    154     37       N  
ATOM   2070  CA  ALA B 144      20.266  14.828  17.316  1.00 13.14           C  
ANISOU 2070  CA  ALA B 144     1634   2224   1134    310     49    425       C  
ATOM   2071  C   ALA B 144      20.563  14.043  18.581  1.00 14.65           C  
ANISOU 2071  C   ALA B 144     1844   2491   1229    216   -219    297       C  
ATOM   2072  O   ALA B 144      19.877  14.236  19.602  1.00 15.56           O  
ANISOU 2072  O   ALA B 144     1913   2767   1231    375    337    573       O  
ATOM   2073  CB  ALA B 144      19.321  14.026  16.417  1.00 13.69           C  
ANISOU 2073  CB  ALA B 144     1662   2646    890   -121     85    133       C  
ATOM   2074  N   LYS B 145      21.584  13.199  18.559  1.00 15.70           N  
ANISOU 2074  N   LYS B 145     2137   2591   1234    377    -29    563       N  
ATOM   2075  CA ALYS B 145      21.915  12.410  19.755  0.50 17.23           C  
ANISOU 2075  CA ALYS B 145     2458   2659   1427    499   -118    568       C  
ATOM   2076  CA BLYS B 145      21.954  12.423  19.748  0.50 17.34           C  
ANISOU 2076  CA BLYS B 145     2451   2728   1407    446    -83    584       C  
ATOM   2077  C   LYS B 145      22.353  13.296  20.932  1.00 17.54           C  
ANISOU 2077  C   LYS B 145     2412   2744   1506    599   -188    739       C  
ATOM   2078  O   LYS B 145      22.187  12.898  22.090  1.00 22.19           O  
ANISOU 2078  O   LYS B 145     3513   3601   1317    663    -39    911       O  
ATOM   2079  CB ALYS B 145      22.943  11.306  19.451  0.50 17.39           C  
ANISOU 2079  CB ALYS B 145     2498   2726   1380    383     41    665       C  
ATOM   2080  CB BLYS B 145      23.061  11.430  19.417  0.50 18.39           C  
ANISOU 2080  CB BLYS B 145     2544   2903   1539    349     65    645       C  
ATOM   2081  CG ALYS B 145      23.125  10.286  20.596  0.50 17.95           C  
ANISOU 2081  CG ALYS B 145     3009   2637   1173    580   -254    548       C  
ATOM   2082  CG BLYS B 145      22.530  10.130  18.901  0.50 18.93           C  
ANISOU 2082  CG BLYS B 145     3033   3142   1016     79    239    742       C  
ATOM   2083  N   LYS B 146      22.937  14.450  20.639  1.00 17.67           N  
ANISOU 2083  N   LYS B 146     2179   3065   1469    389   -424    394       N  
ATOM   2084  CA  LYS B 146      23.380  15.418  21.604  1.00 18.58           C  
ANISOU 2084  CA  LYS B 146     2409   3290   1360    204   -515    240       C  
ATOM   2085  C   LYS B 146      22.255  16.295  22.143  1.00 17.95           C  
ANISOU 2085  C   LYS B 146     2319   3224   1277    166   -295     52       C  
ATOM   2086  O   LYS B 146      22.526  17.287  22.821  1.00 20.21           O  
ANISOU 2086  O   LYS B 146     2658   3595   1424     76   -419    -84       O  
ATOM   2087  CB  LYS B 146      24.457  16.341  20.985  1.00 20.68           C  
ANISOU 2087  CB  LYS B 146     2321   3645   1891   -116   -546   -337       C  
ATOM   2088  CG  LYS B 146      25.780  15.703  20.648  1.00 27.98           C  
ANISOU 2088  CG  LYS B 146     3839   3976   2816   -160   -452   -472       C  
ATOM   2089  CD  LYS B 146      26.567  16.693  19.759  1.00 33.59           C  
ANISOU 2089  CD  LYS B 146     4006   5237   3520   -269   -152    -57       C  
ATOM   2090  CE  LYS B 146      27.798  16.049  19.128  1.00 40.26           C  
ANISOU 2090  CE  LYS B 146     4900   5759   4638    -63   -100    -39       C  
ATOM   2091  NZ  LYS B 146      28.496  16.970  18.181  1.00 40.55           N  
ANISOU 2091  NZ  LYS B 146     4700   6030   4677    -55   -597    618       N  
ATOM   2092  N   GLY B 147      21.054  16.138  21.597  1.00 16.68           N  
ANISOU 2092  N   GLY B 147     2105   2897   1334    182   -251    235       N  
ATOM   2093  CA  GLY B 147      19.952  17.016  21.965  1.00 15.66           C  
ANISOU 2093  CA  GLY B 147     2097   2886    965    158   -147    333       C  
ATOM   2094  C   GLY B 147      19.606  18.102  20.956  1.00 13.26           C  
ANISOU 2094  C   GLY B 147     1449   2817    771    176   -247    260       C  
ATOM   2095  O   GLY B 147      18.748  18.928  21.214  1.00 16.22           O  
ANISOU 2095  O   GLY B 147     2057   3003   1103    418   -300    307       O  
ATOM   2096  N   GLY B 148      20.328  18.108  19.841  1.00 13.79           N  
ANISOU 2096  N   GLY B 148     1491   2888    860    175    -40    189       N  
ATOM   2097  CA  GLY B 148      20.146  19.105  18.794  1.00 13.46           C  
ANISOU 2097  CA  GLY B 148     1711   2475    928    226   -142    129       C  
ATOM   2098  C   GLY B 148      21.502  19.663  18.456  1.00 14.25           C  
ANISOU 2098  C   GLY B 148     1686   2551   1177    136    -80     81       C  
ATOM   2099  O   GLY B 148      22.348  19.847  19.331  1.00 14.89           O  
ANISOU 2099  O   GLY B 148     2100   3183    372    -95    -87    107       O  
ATOM   2100  N   GLY B 149      21.704  20.002  17.194  1.00 13.97           N  
ANISOU 2100  N   GLY B 149     1627   2496   1185     73      8    108       N  
ATOM   2101  CA  GLY B 149      22.981  20.554  16.761  1.00 13.64           C  
ANISOU 2101  CA  GLY B 149     1873   2331    978     46     11   -156       C  
ATOM   2102  C   GLY B 149      23.065  20.757  15.264  1.00 12.03           C  
ANISOU 2102  C   GLY B 149     1329   2083   1159      0   -173     44       C  
ATOM   2103  O   GLY B 149      22.042  20.660  14.586  1.00 10.58           O  
ANISOU 2103  O   GLY B 149     1224   2104    691     23   -117    -36       O  
ATOM   2104  N   TYR B 150      24.285  21.041  14.803  1.00 11.27           N  
ANISOU 2104  N   TYR B 150     1247   2199    834    146    -99    -98       N  
ATOM   2105  CA  TYR B 150      24.506  21.584  13.474  1.00 10.97           C  
ANISOU 2105  CA  TYR B 150     1121   2046    998    116   -167     51       C  
ATOM   2106  C   TYR B 150      25.390  20.707  12.609  1.00 11.10           C  
ANISOU 2106  C   TYR B 150     1130   2118    969    475    -56    -97       C  
ATOM   2107  O   TYR B 150      26.320  20.064  13.093  1.00 12.46           O  
ANISOU 2107  O   TYR B 150     1442   2442    847    314    -22     -5       O  
ATOM   2108  CB  TYR B 150      25.091  22.975  13.564  1.00 12.41           C  
ANISOU 2108  CB  TYR B 150     1408   2115   1192   -150    -49   -171       C  
ATOM   2109  CG  TYR B 150      24.170  23.924  14.322  1.00 12.68           C  
ANISOU 2109  CG  TYR B 150     1413   2247   1158    -55     37   -326       C  
ATOM   2110  CD1 TYR B 150      23.109  24.533  13.691  1.00 11.76           C  
ANISOU 2110  CD1 TYR B 150     1389   2258    821    -94   -137   -298       C  
ATOM   2111  CD2 TYR B 150      24.263  24.075  15.710  1.00 15.01           C  
ANISOU 2111  CD2 TYR B 150     2061   2552   1089    385   -267   -631       C  
ATOM   2112  CE1 TYR B 150      22.213  25.321  14.374  1.00 12.75           C  
ANISOU 2112  CE1 TYR B 150     1605   2151   1086   -102   -121   -304       C  
ATOM   2113  CE2 TYR B 150      23.343  24.854  16.421  1.00 13.78           C  
ANISOU 2113  CE2 TYR B 150     2133   2420    682    316    112   -570       C  
ATOM   2114  CZ  TYR B 150      22.306  25.437  15.745  1.00 12.24           C  
ANISOU 2114  CZ  TYR B 150     1308   2266   1074    257    204    -90       C  
ATOM   2115  OH  TYR B 150      21.355  26.155  16.390  1.00 15.65           O  
ANISOU 2115  OH  TYR B 150     2055   2533   1358    288    351   -337       O  
ATOM   2116  N   THR B 151      25.088  20.693  11.302  1.00 10.59           N  
ANISOU 2116  N   THR B 151     1181   2056    783    246    -80   -240       N  
ATOM   2117  CA  THR B 151      25.871  19.982  10.306  1.00 10.34           C  
ANISOU 2117  CA  THR B 151     1201   1768    957    270    -18    219       C  
ATOM   2118  C   THR B 151      26.088  20.972   9.149  1.00 10.58           C  
ANISOU 2118  C   THR B 151     1315   1822    879    285    105   -108       C  
ATOM   2119  O   THR B 151      25.159  21.643   8.720  1.00 10.85           O  
ANISOU 2119  O   THR B 151     1231   2004    886     84    109    -63       O  
ATOM   2120  CB  THR B 151      25.110  18.724   9.819  1.00 10.74           C  
ANISOU 2120  CB  THR B 151     1227   1718   1135    145     53    130       C  
ATOM   2121  OG1 THR B 151      24.811  17.867  10.932  1.00 11.27           O  
ANISOU 2121  OG1 THR B 151     1519   1860    902     56    165    162       O  
ATOM   2122  CG2 THR B 151      25.876  17.911   8.777  1.00 11.57           C  
ANISOU 2122  CG2 THR B 151     1587   1933    873    252    353   -198       C  
ATOM   2123  N   TYR B 152      27.324  21.012   8.642  1.00 10.76           N  
ANISOU 2123  N   TYR B 152     1084   1874   1129    229     50   -132       N  
ATOM   2124  CA  TYR B 152      27.755  22.010   7.654  1.00 10.31           C  
ANISOU 2124  CA  TYR B 152     1197   1823    895     76    -71   -311       C  
ATOM   2125  C   TYR B 152      28.261  21.269   6.405  1.00  9.78           C  
ANISOU 2125  C   TYR B 152      921   1742   1052    261    -64   -185       C  
ATOM   2126  O   TYR B 152      29.082  20.374   6.509  1.00 11.76           O  
ANISOU 2126  O   TYR B 152     1359   1979   1127    271     25   -185       O  
ATOM   2127  CB  TYR B 152      28.897  22.843   8.228  1.00 10.66           C  
ANISOU 2127  CB  TYR B 152     1046   1924   1079     27     92      8       C  
ATOM   2128  CG  TYR B 152      28.528  23.573   9.495  1.00 11.37           C  
ANISOU 2128  CG  TYR B 152     1265   1847   1206    -20    -18   -348       C  
ATOM   2129  CD1 TYR B 152      27.945  24.820   9.472  1.00 11.64           C  
ANISOU 2129  CD1 TYR B 152     1241   2124   1058    -83   -131   -188       C  
ATOM   2130  CD2 TYR B 152      28.745  22.983  10.733  1.00 13.18           C  
ANISOU 2130  CD2 TYR B 152     1703   2326    978    419   -218   -405       C  
ATOM   2131  CE1 TYR B 152      27.547  25.482  10.660  1.00 13.08           C  
ANISOU 2131  CE1 TYR B 152     1336   2260   1374    117     39   -395       C  
ATOM   2132  CE2 TYR B 152      28.314  23.610  11.908  1.00 13.47           C  
ANISOU 2132  CE2 TYR B 152     1621   2505    990    -20     50   -540       C  
ATOM   2133  CZ  TYR B 152      27.741  24.855  11.871  1.00 12.72           C  
ANISOU 2133  CZ  TYR B 152     1512   2028   1290    -54    313   -385       C  
ATOM   2134  OH  TYR B 152      27.365  25.482  13.046  1.00 13.92           O  
ANISOU 2134  OH  TYR B 152     1517   2758   1012     26    120   -624       O  
ATOM   2135  N   TYR B 153      27.702  21.621   5.228  1.00  9.96           N  
ANISOU 2135  N   TYR B 153     1145   1703    936    279      3   -227       N  
ATOM   2136  CA  TYR B 153      28.010  20.865   4.028  1.00 10.25           C  
ANISOU 2136  CA  TYR B 153     1143   1623   1129    266     41   -364       C  
ATOM   2137  C   TYR B 153      27.546  21.702   2.816  1.00  9.37           C  
ANISOU 2137  C   TYR B 153     1299   1478    782    321    -99   -193       C  
ATOM   2138  O   TYR B 153      26.858  22.696   2.980  1.00 10.48           O  
ANISOU 2138  O   TYR B 153     1469   1547    966    115    236    -85       O  
ATOM   2139  CB  TYR B 153      27.331  19.491   4.045  1.00 10.81           C  
ANISOU 2139  CB  TYR B 153     1572   1744    791    235    -89   -120       C  
ATOM   2140  CG  TYR B 153      25.844  19.497   4.205  1.00 10.05           C  
ANISOU 2140  CG  TYR B 153     1181   1636    999    256    -38   -322       C  
ATOM   2141  CD1 TYR B 153      25.002  19.274   3.138  1.00  9.36           C  
ANISOU 2141  CD1 TYR B 153     1320   1824    412    -94    267     57       C  
ATOM   2142  CD2 TYR B 153      25.249  19.811   5.427  1.00 10.73           C  
ANISOU 2142  CD2 TYR B 153     1427   1710    938     52   -102   -274       C  
ATOM   2143  CE1 TYR B 153      23.618  19.283   3.285  1.00 10.05           C  
ANISOU 2143  CE1 TYR B 153     1301   1591    927    123    -88   -118       C  
ATOM   2144  CE2 TYR B 153      23.913  19.789   5.593  1.00 11.17           C  
ANISOU 2144  CE2 TYR B 153     1507   2075    659   -136    311    -49       C  
ATOM   2145  CZ  TYR B 153      23.065  19.584   4.517  1.00  9.84           C  
ANISOU 2145  CZ  TYR B 153     1144   1633    959   -101    209   -251       C  
ATOM   2146  OH  TYR B 153      21.698  19.636   4.664  1.00 11.01           O  
ANISOU 2146  OH  TYR B 153     1348   1860    973   -130    279     45       O  
ATOM   2147  N   LYS B 154      27.919  21.264   1.609  1.00 10.08           N  
ANISOU 2147  N   LYS B 154     1373   1388   1067    204     45   -376       N  
ATOM   2148  CA  LYS B 154      27.493  21.927   0.381  1.00 10.29           C  
ANISOU 2148  CA  LYS B 154     1308   1527   1073    201    172   -185       C  
ATOM   2149  C   LYS B 154      26.421  21.079  -0.278  1.00 10.15           C  
ANISOU 2149  C   LYS B 154     1563   1473    818    335    221   -365       C  
ATOM   2150  O   LYS B 154      26.546  19.863  -0.354  1.00 11.42           O  
ANISOU 2150  O   LYS B 154     1627   1695   1016    229   -240   -183       O  
ATOM   2151  CB  LYS B 154      28.686  22.051  -0.567  1.00 14.08           C  
ANISOU 2151  CB  LYS B 154     1671   2020   1658    263    401   -128       C  
ATOM   2152  CG  LYS B 154      28.823  23.323  -1.259  1.00 17.31           C  
ANISOU 2152  CG  LYS B 154     2562   2470   1544    306    759   -323       C  
ATOM   2153  CD  LYS B 154      30.155  23.512  -1.968  1.00 15.40           C  
ANISOU 2153  CD  LYS B 154     2122   1789   1941   -163    998   -164       C  
ATOM   2154  CE  LYS B 154      30.151  24.814  -2.688  1.00 17.95           C  
ANISOU 2154  CE  LYS B 154     2473   2035   2311    124     26   -668       C  
ATOM   2155  NZ  LYS B 154      31.316  25.128  -3.532  1.00 16.40           N  
ANISOU 2155  NZ  LYS B 154     2217   2664   1350   -433    792   -122       N  
ATOM   2156  N   MET B 155      25.424  21.747  -0.856  1.00  9.02           N  
ANISOU 2156  N   MET B 155     1301   1208    918     81    214   -108       N  
ATOM   2157  CA  MET B 155      24.295  21.039  -1.468  1.00  9.51           C  
ANISOU 2157  CA  MET B 155     1490   1361    761     36    208   -113       C  
ATOM   2158  C   MET B 155      23.597  22.037  -2.395  1.00 10.04           C  
ANISOU 2158  C   MET B 155     1273   1330   1212    134    231     10       C  
ATOM   2159  O   MET B 155      23.509  23.216  -2.087  1.00 10.37           O  
ANISOU 2159  O   MET B 155     1429   1544    967    140    179   -237       O  
ATOM   2160  CB  MET B 155      23.355  20.550  -0.388  1.00 10.41           C  
ANISOU 2160  CB  MET B 155     1192   1860    903   -122    328    135       C  
ATOM   2161  CG  MET B 155      22.258  19.598  -0.825  1.00 10.47           C  
ANISOU 2161  CG  MET B 155     1317   1926    734    170    534     82       C  
ATOM   2162  SD  MET B 155      22.840  18.018  -1.479  1.00 10.52           S  
ANISOU 2162  SD  MET B 155     1433   1704    860     41    238     34       S  
ATOM   2163  CE  MET B 155      23.450  17.223   0.007  1.00 10.67           C  
ANISOU 2163  CE  MET B 155     1564   1794    694    234     50    280       C  
ATOM   2164  N   PRO B 156      23.002  21.541  -3.481  1.00  8.47           N  
ANISOU 2164  N   PRO B 156     1085   1386    744    101    265    -51       N  
ATOM   2165  CA  PRO B 156      22.160  22.460  -4.264  1.00  8.64           C  
ANISOU 2165  CA  PRO B 156     1162   1295    824    105    358   -153       C  
ATOM   2166  C   PRO B 156      20.952  22.927  -3.473  1.00  8.37           C  
ANISOU 2166  C   PRO B 156     1220   1342    617     49     29    -88       C  
ATOM   2167  O   PRO B 156      20.549  22.263  -2.507  1.00  9.52           O  
ANISOU 2167  O   PRO B 156     1438   1441    734     39    277    -73       O  
ATOM   2168  CB  PRO B 156      21.738  21.608  -5.454  1.00  9.60           C  
ANISOU 2168  CB  PRO B 156     1275   1775    596     47    342     81       C  
ATOM   2169  CG  PRO B 156      22.857  20.618  -5.582  1.00  9.83           C  
ANISOU 2169  CG  PRO B 156     1531   1640    561    -93     29    121       C  
ATOM   2170  CD  PRO B 156      23.134  20.247  -4.164  1.00 10.83           C  
ANISOU 2170  CD  PRO B 156     1489   1699    924     90    470    158       C  
ATOM   2171  N   LYS B 157      20.282  23.958  -3.973  1.00 10.28           N  
ANISOU 2171  N   LYS B 157     1338   1576    990    277    525     98       N  
ATOM   2172  CA  LYS B 157      18.989  24.383  -3.440  1.00 10.58           C  
ANISOU 2172  CA  LYS B 157     1288   1676   1056    161    379    247       C  
ATOM   2173  C   LYS B 157      17.829  23.588  -4.051  1.00 11.85           C  
ANISOU 2173  C   LYS B 157     1436   1550   1513    249    158    163       C  
ATOM   2174  O   LYS B 157      16.731  23.549  -3.501  1.00 12.37           O  
ANISOU 2174  O   LYS B 157     1261   1939   1497    193    380    -27       O  
ATOM   2175  CB  LYS B 157      18.746  25.865  -3.714  1.00 12.33           C  
ANISOU 2175  CB  LYS B 157     1758   1834   1091    216    404    373       C  
ATOM   2176  CG  LYS B 157      19.619  26.798  -2.935  1.00 13.35           C  
ANISOU 2176  CG  LYS B 157     2312   1466   1292    119    659    -69       C  
ATOM   2177  CD  LYS B 157      19.425  28.215  -3.376  1.00 15.70           C  
ANISOU 2177  CD  LYS B 157     3000   1878   1085   -195    549     32       C  
ATOM   2178  CE  LYS B 157      19.363  29.195  -2.268  1.00 23.58           C  
ANISOU 2178  CE  LYS B 157     5062   3008    888    322    718    421       C  
ATOM   2179  NZ  LYS B 157      18.969  30.540  -2.801  1.00 24.91           N  
ANISOU 2179  NZ  LYS B 157     5609   1246   2607    939    156    353       N  
ATOM   2180  N   TYR B 158      18.064  22.939  -5.185  1.00 10.78           N  
ANISOU 2180  N   TYR B 158     1331   1852    912    155    227    130       N  
ATOM   2181  CA  TYR B 158      17.066  22.106  -5.868  1.00 11.03           C  
ANISOU 2181  CA  TYR B 158     1373   1801   1015    213    119    222       C  
ATOM   2182  C   TYR B 158      17.776  21.027  -6.632  1.00 11.69           C  
ANISOU 2182  C   TYR B 158     1332   1831   1278      8     -2    117       C  
ATOM   2183  O   TYR B 158      18.952  21.167  -6.956  1.00 11.51           O  
ANISOU 2183  O   TYR B 158     1308   2283    779    -39    -15     32       O  
ATOM   2184  CB  TYR B 158      16.144  22.944  -6.781  1.00 12.91           C  
ANISOU 2184  CB  TYR B 158     1458   2178   1267    206    304    159       C  
ATOM   2185  CG  TYR B 158      16.877  23.763  -7.794  1.00 14.76           C  
ANISOU 2185  CG  TYR B 158     1588   2299   1721    267   -191    385       C  
ATOM   2186  CD1 TYR B 158      17.232  23.226  -9.020  1.00 15.61           C  
ANISOU 2186  CD1 TYR B 158     1877   2553   1499    273    -74    679       C  
ATOM   2187  CD2 TYR B 158      17.300  25.042  -7.491  1.00 16.97           C  
ANISOU 2187  CD2 TYR B 158     2225   2369   1854   -130   -316    616       C  
ATOM   2188  CE1 TYR B 158      17.965  23.990  -9.958  1.00 17.26           C  
ANISOU 2188  CE1 TYR B 158     2090   2744   1720    487    137   1158       C  
ATOM   2189  CE2 TYR B 158      18.017  25.799  -8.398  1.00 18.29           C  
ANISOU 2189  CE2 TYR B 158     2802   2655   1492   -396    -74    584       C  
ATOM   2190  CZ  TYR B 158      18.363  25.249  -9.624  1.00 15.95           C  
ANISOU 2190  CZ  TYR B 158     1958   3064   1038    127    166   1110       C  
ATOM   2191  OH  TYR B 158      19.060  26.003 -10.543  1.00 24.39           O  
ANISOU 2191  OH  TYR B 158     2610   4772   1885   -107    283   1699       O  
ATOM   2192  N   ASP B 159      17.032  19.991  -7.002  1.00 11.94           N  
ANISOU 2192  N   ASP B 159     1382   2096   1056    -75     30    -26       N  
ATOM   2193  CA  ASP B 159      17.600  18.829  -7.681  1.00 12.39           C  
ANISOU 2193  CA  ASP B 159     1694   2122    891   -193     16   -146       C  
ATOM   2194  C   ASP B 159      18.204  19.298  -9.027  1.00 13.96           C  
ANISOU 2194  C   ASP B 159     1585   2290   1427   -203     56    -34       C  
ATOM   2195  O   ASP B 159      17.503  19.866  -9.847  1.00 14.86           O  
ANISOU 2195  O   ASP B 159     1957   2847    842     88    230    166       O  
ATOM   2196  CB  ASP B 159      16.508  17.791  -7.866  1.00 15.03           C  
ANISOU 2196  CB  ASP B 159     2225   2332   1154   -230    171     -9       C  
ATOM   2197  CG  ASP B 159      16.990  16.497  -8.519  1.00 15.00           C  
ANISOU 2197  CG  ASP B 159     2360   2553    785   -433    -48   -354       C  
ATOM   2198  OD1 ASP B 159      18.216  16.256  -8.665  1.00 19.03           O  
ANISOU 2198  OD1 ASP B 159     2461   2868   1901   -189    228   -342       O  
ATOM   2199  OD2 ASP B 159      16.092  15.684  -8.821  1.00 19.35           O  
ANISOU 2199  OD2 ASP B 159     2950   3225   1176   -992    441   -681       O  
ATOM   2200  N   GLY B 160      19.489  19.070  -9.211  1.00 13.82           N  
ANISOU 2200  N   GLY B 160     1817   2393   1038   -173     54   -291       N  
ATOM   2201  CA  GLY B 160      20.198  19.468 -10.409  1.00 15.18           C  
ANISOU 2201  CA  GLY B 160     1780   2723   1264   -317     83   -356       C  
ATOM   2202  C   GLY B 160      20.791  20.859 -10.415  1.00 13.40           C  
ANISOU 2202  C   GLY B 160     1384   2529   1178   -357    248   -234       C  
ATOM   2203  O   GLY B 160      21.389  21.269 -11.415  1.00 17.55           O  
ANISOU 2203  O   GLY B 160     1824   3455   1387   -601    402   -149       O  
ATOM   2204  N   GLY B 161      20.687  21.588  -9.300  1.00 12.65           N  
ANISOU 2204  N   GLY B 161     1508   2315    981   -102      0   -163       N  
ATOM   2205  CA  GLY B 161      21.235  22.912  -9.218  1.00 14.04           C  
ANISOU 2205  CA  GLY B 161     1549   2243   1543     85     -2     17       C  
ATOM   2206  C   GLY B 161      22.716  22.950  -8.825  1.00 11.97           C  
ANISOU 2206  C   GLY B 161     1343   1798   1406    111    319     65       C  
ATOM   2207  O   GLY B 161      23.332  21.914  -8.551  1.00 11.59           O  
ANISOU 2207  O   GLY B 161     1492   1780   1131    114    262   -107       O  
ATOM   2208  N   VAL B 162      23.299  24.138  -8.873  1.00 12.01           N  
ANISOU 2208  N   VAL B 162     1485   1904   1175    106    133    282       N  
ATOM   2209  CA  VAL B 162      24.695  24.307  -8.474  1.00 12.47           C  
ANISOU 2209  CA  VAL B 162     1437   1958   1342    -16    307     19       C  
ATOM   2210  C   VAL B 162      24.794  24.148  -6.929  1.00 10.86           C  
ANISOU 2210  C   VAL B 162     1334   1654   1138    194    426     41       C  
ATOM   2211  O   VAL B 162      24.022  24.757  -6.180  1.00 11.51           O  
ANISOU 2211  O   VAL B 162     1519   1976    876    365    337   -124       O  
ATOM   2212  CB  VAL B 162      25.252  25.668  -8.931  1.00 12.71           C  
ANISOU 2212  CB  VAL B 162     1738   1906   1183    306    651    -59       C  
ATOM   2213  CG1 VAL B 162      26.705  25.889  -8.422  1.00 14.40           C  
ANISOU 2213  CG1 VAL B 162     1386   2168   1916   -372     83   -107       C  
ATOM   2214  CG2 VAL B 162      25.197  25.776 -10.456  1.00 18.21           C  
ANISOU 2214  CG2 VAL B 162     2502   2880   1537   -227    249    251       C  
ATOM   2215  N   PRO B 163      25.763  23.379  -6.457  1.00  9.63           N  
ANISOU 2215  N   PRO B 163     1274   1728    658    393    374     70       N  
ATOM   2216  CA  PRO B 163      25.898  23.251  -4.982  1.00  9.99           C  
ANISOU 2216  CA  PRO B 163     1358   1831    605    307    251     97       C  
ATOM   2217  C   PRO B 163      26.310  24.553  -4.327  1.00 11.28           C  
ANISOU 2217  C   PRO B 163     1379   1845   1059     60    360     84       C  
ATOM   2218  O   PRO B 163      27.108  25.329  -4.913  1.00 11.80           O  
ANISOU 2218  O   PRO B 163     1680   2163    640   -166    232    122       O  
ATOM   2219  CB  PRO B 163      27.003  22.220  -4.794  1.00 12.56           C  
ANISOU 2219  CB  PRO B 163     1798   2008    963    280    488   -134       C  
ATOM   2220  CG  PRO B 163      27.143  21.566  -6.094  1.00 15.60           C  
ANISOU 2220  CG  PRO B 163     2186   2636   1103   1074   -199   -104       C  
ATOM   2221  CD  PRO B 163      26.692  22.484  -7.158  1.00 11.62           C  
ANISOU 2221  CD  PRO B 163     1370   2160    883    531    355   -112       C  
ATOM   2222  N  AGLU B 164      25.883  24.765  -3.107  0.50 10.56           N  
ANISOU 2222  N  AGLU B 164     1398   1601   1013     14     47   -193       N  
ATOM   2223  N  BGLU B 164      25.716  24.776  -3.139  0.50  9.76           N  
ANISOU 2223  N  BGLU B 164     1375   1468    865    -57    125   -193       N  
ATOM   2224  CA AGLU B 164      26.377  25.893  -2.413  0.50 11.99           C  
ANISOU 2224  CA AGLU B 164     1811   1664   1080    107    115   -164       C  
ATOM   2225  CA BGLU B 164      25.843  25.980  -2.306  0.50  9.35           C  
ANISOU 2225  CA BGLU B 164     1425   1226    902     85    -56    -59       C  
ATOM   2226  C  AGLU B 164      26.302  25.583  -0.938  0.50 10.45           C  
ANISOU 2226  C  AGLU B 164     1568   1448    952     91    147   -134       C  
ATOM   2227  C  BGLU B 164      26.195  25.586  -0.863  0.50  9.13           C  
ANISOU 2227  C  BGLU B 164     1376   1296    795     -6    220   -187       C  
ATOM   2228  O  AGLU B 164      25.696  24.610  -0.502  0.50 10.07           O  
ANISOU 2228  O  AGLU B 164     1435   1570    818    285    263   -194       O  
ATOM   2229  O  BGLU B 164      25.615  24.648  -0.319  0.50 10.59           O  
ANISOU 2229  O  BGLU B 164     1434   1525   1064   -190    -99   -250       O  
ATOM   2230  CB AGLU B 164      25.586  27.139  -2.799  0.50 11.48           C  
ANISOU 2230  CB AGLU B 164     1752   1566   1042    -23    333   -303       C  
ATOM   2231  CB BGLU B 164      24.530  26.769  -2.274  0.50  8.94           C  
ANISOU 2231  CB BGLU B 164     1065   1391    940    -83    281   -139       C  
ATOM   2232  CG AGLU B 164      24.081  26.955  -2.748  0.50 13.66           C  
ANISOU 2232  CG AGLU B 164     1842   1840   1507    399    258   -262       C  
ATOM   2233  CG BGLU B 164      24.256  27.529  -3.580  0.50 12.13           C  
ANISOU 2233  CG BGLU B 164     1690   1491   1428    289   -191    174       C  
ATOM   2234  CD AGLU B 164      23.366  28.257  -2.955  0.50 11.90           C  
ANISOU 2234  CD AGLU B 164     1408   1984   1127    453     49   -343       C  
ATOM   2235  CD BGLU B 164      25.022  28.817  -3.692  0.50 12.54           C  
ANISOU 2235  CD BGLU B 164     1542   1485   1737    283    -75   -140       C  
ATOM   2236  OE1AGLU B 164      23.266  29.003  -1.966  0.50 13.09           O  
ANISOU 2236  OE1AGLU B 164     1920   1675   1378    265    365   -252       O  
ATOM   2237  OE1BGLU B 164      25.827  29.143  -2.773  0.50 17.72           O  
ANISOU 2237  OE1BGLU B 164     2314   2440   1976   -475   -665     11       O  
ATOM   2238  OE2AGLU B 164      22.904  28.530  -4.095  0.50 17.05           O  
ANISOU 2238  OE2AGLU B 164     2186   2295   1997    310     52   -359       O  
ATOM   2239  OE2BGLU B 164      24.804  29.547  -4.690  0.50 15.22           O  
ANISOU 2239  OE2BGLU B 164     2241   2230   1311    277     42    361       O  
ATOM   2240  N   LYS B 165      27.031  26.373  -0.194  1.00 11.40           N  
ANISOU 2240  N   LYS B 165     1569   1504   1258   -238    270    -88       N  
ATOM   2241  CA  LYS B 165      27.271  26.087   1.213  1.00  9.53           C  
ANISOU 2241  CA  LYS B 165     1195   1542    882   -113    210    -73       C  
ATOM   2242  C   LYS B 165      25.991  26.296   2.026  1.00  9.81           C  
ANISOU 2242  C   LYS B 165     1283   1285   1156   -167    180   -207       C  
ATOM   2243  O   LYS B 165      25.286  27.295   1.851  1.00 10.22           O  
ANISOU 2243  O   LYS B 165     1490   1641    750      5    221   -146       O  
ATOM   2244  CB  LYS B 165      28.385  26.964   1.749  1.00 10.26           C  
ANISOU 2244  CB  LYS B 165     1292   1990    614   -200    300   -133       C  
ATOM   2245  CG  LYS B 165      29.746  26.629   1.189  1.00 13.27           C  
ANISOU 2245  CG  LYS B 165     1469   2731    839   -253    194   -121       C  
ATOM   2246  CD  LYS B 165      30.882  27.442   1.852  1.00 18.92           C  
ANISOU 2246  CD  LYS B 165     1478   3439   2269   -494    477   -610       C  
ATOM   2247  CE  LYS B 165      32.229  27.026   1.270  1.00 27.70           C  
ANISOU 2247  CE  LYS B 165     2649   4412   3462   -315    396   -328       C  
ATOM   2248  NZ  LYS B 165      33.373  27.493   2.104  1.00 35.88           N  
ANISOU 2248  NZ  LYS B 165     3322   5681   4629  -1012    131   -533       N  
ATOM   2249  N   LYS B 166      25.746  25.384   2.968  1.00  9.28           N  
ANISOU 2249  N   LYS B 166     1151   1483    890    -42    176   -239       N  
ATOM   2250  CA  LYS B 166      24.558  25.483   3.838  1.00  9.01           C  
ANISOU 2250  CA  LYS B 166     1118   1542    762    -56    212   -238       C  
ATOM   2251  C   LYS B 166      24.861  24.880   5.183  1.00  8.85           C  
ANISOU 2251  C   LYS B 166     1080   1587    694    168    103   -345       C  
ATOM   2252  O   LYS B 166      25.935  24.325   5.402  1.00  9.43           O  
ANISOU 2252  O   LYS B 166     1168   1706    706     -7    294   -339       O  
ATOM   2253  CB  LYS B 166      23.372  24.777   3.200  1.00  9.49           C  
ANISOU 2253  CB  LYS B 166     1111   1717    778   -127    299   -178       C  
ATOM   2254  CG  LYS B 166      23.507  23.284   3.063  1.00 10.98           C  
ANISOU 2254  CG  LYS B 166     1390   1669   1112    -66    104   -283       C  
ATOM   2255  CD  LYS B 166      22.273  22.644   2.389  1.00  9.35           C  
ANISOU 2255  CD  LYS B 166     1371   1510    669    224    243   -146       C  
ATOM   2256  CE  LYS B 166      21.015  22.864   3.212  1.00  9.25           C  
ANISOU 2256  CE  LYS B 166     1204   1677    632   -190     75     -8       C  
ATOM   2257  NZ  LYS B 166      19.822  22.170   2.580  1.00 10.42           N  
ANISOU 2257  NZ  LYS B 166     1286   1658   1012   -134    300   -376       N  
ATOM   2258  N   PHE B 167      23.883  25.001   6.083  1.00  9.70           N  
ANISOU 2258  N   PHE B 167     1153   1596    933    242    190   -213       N  
ATOM   2259  CA  PHE B 167      23.954  24.266   7.336  1.00 10.47           C  
ANISOU 2259  CA  PHE B 167     1147   1685   1144     30    -59     -3       C  
ATOM   2260  C   PHE B 167      22.558  23.840   7.755  1.00  9.54           C  
ANISOU 2260  C   PHE B 167     1087   1555    983    221    235   -120       C  
ATOM   2261  O   PHE B 167      21.530  24.368   7.242  1.00  9.69           O  
ANISOU 2261  O   PHE B 167     1199   1694    785     43    126    -54       O  
ATOM   2262  CB  PHE B 167      24.587  25.095   8.414  1.00 11.46           C  
ANISOU 2262  CB  PHE B 167     1352   1929   1072   -102    178   -175       C  
ATOM   2263  CG  PHE B 167      23.920  26.421   8.660  1.00 16.87           C  
ANISOU 2263  CG  PHE B 167     1903   2933   1572   -416   -499   -842       C  
ATOM   2264  CD1 PHE B 167      22.999  26.562   9.603  1.00 21.09           C  
ANISOU 2264  CD1 PHE B 167     2370   4492   1152    330   -176  -1569       C  
ATOM   2265  CD2 PHE B 167      24.345  27.562   7.970  1.00 22.02           C  
ANISOU 2265  CD2 PHE B 167     3891   2297   2177    265     69   -458       C  
ATOM   2266  CE1 PHE B 167      22.373  27.904   9.835  1.00 17.51           C  
ANISOU 2266  CE1 PHE B 167     3189   2446   1018    330   -673   -474       C  
ATOM   2267  CE2 PHE B 167      23.885  28.826   8.270  1.00 23.80           C  
ANISOU 2267  CE2 PHE B 167     3798   2960   2285   -206    387   -444       C  
ATOM   2268  CZ  PHE B 167      22.892  28.982   9.254  1.00 18.41           C  
ANISOU 2268  CZ  PHE B 167     2760   3422    810    933    261   -392       C  
ATOM   2269  N   ALA B 168      22.556  22.808   8.604  1.00  8.83           N  
ANISOU 2269  N   ALA B 168     1094   1677    581     37    -12    112       N  
ATOM   2270  CA  ALA B 168      21.343  22.184   9.086  1.00  9.98           C  
ANISOU 2270  CA  ALA B 168     1098   1804    889     64    114    164       C  
ATOM   2271  C   ALA B 168      21.352  22.160  10.610  1.00 10.34           C  
ANISOU 2271  C   ALA B 168      969   1868   1092    -26    -47     43       C  
ATOM   2272  O   ALA B 168      22.362  21.774  11.203  1.00 11.80           O  
ANISOU 2272  O   ALA B 168     1006   2515    962    203      0   -207       O  
ATOM   2273  CB  ALA B 168      21.224  20.722   8.524  1.00 10.83           C  
ANISOU 2273  CB  ALA B 168     1286   1551   1275     67    -55    -35       C  
ATOM   2274  N   TYR B 169      20.235  22.546  11.219  1.00  9.86           N  
ANISOU 2274  N   TYR B 169     1291   1681    773     67    -94     62       N  
ATOM   2275  CA  TYR B 169      19.969  22.224  12.604  1.00  9.74           C  
ANISOU 2275  CA  TYR B 169     1219   1664    816     94    -68    293       C  
ATOM   2276  C   TYR B 169      19.083  20.989  12.627  1.00  8.56           C  
ANISOU 2276  C   TYR B 169     1152   1515    586    -42     53   -156       C  
ATOM   2277  O   TYR B 169      18.052  20.972  11.975  1.00  9.37           O  
ANISOU 2277  O   TYR B 169     1310   1719    529    -84   -163     37       O  
ATOM   2278  CB  TYR B 169      19.210  23.354  13.312  1.00  9.57           C  
ANISOU 2278  CB  TYR B 169     1063   1747    824     19      8     22       C  
ATOM   2279  CG  TYR B 169      18.740  22.952  14.680  1.00 10.22           C  
ANISOU 2279  CG  TYR B 169     1208   1636   1037      2    185    -84       C  
ATOM   2280  CD1 TYR B 169      19.615  22.968  15.763  1.00 12.03           C  
ANISOU 2280  CD1 TYR B 169     1146   2033   1392   -117     27    190       C  
ATOM   2281  CD2 TYR B 169      17.463  22.516  14.894  1.00 10.43           C  
ANISOU 2281  CD2 TYR B 169     1464   1551    948    104     93   -231       C  
ATOM   2282  CE1 TYR B 169      19.152  22.587  17.033  1.00 12.11           C  
ANISOU 2282  CE1 TYR B 169     1526   1943   1130     17     66     78       C  
ATOM   2283  CE2 TYR B 169      17.004  22.097  16.157  1.00 10.99           C  
ANISOU 2283  CE2 TYR B 169     1312   1793   1070    -30   -111    137       C  
ATOM   2284  CZ  TYR B 169      17.861  22.156  17.222  1.00 11.20           C  
ANISOU 2284  CZ  TYR B 169     1451   1979    822     73    296    117       C  
ATOM   2285  OH  TYR B 169      17.386  21.783  18.475  1.00 13.16           O  
ANISOU 2285  OH  TYR B 169     1967   2279    751    -63    337    108       O  
ATOM   2286  N   SER B 170      19.480  19.934  13.334  1.00 10.05           N  
ANISOU 2286  N   SER B 170     1317   1698    801    110   -124     25       N  
ATOM   2287  CA  SER B 170      18.681  18.737  13.462  1.00  9.34           C  
ANISOU 2287  CA  SER B 170     1347   1551    648     77     75    150       C  
ATOM   2288  C   SER B 170      18.327  18.442  14.920  1.00 10.52           C  
ANISOU 2288  C   SER B 170     1096   1818   1080   -211    110    106       C  
ATOM   2289  O   SER B 170      19.083  18.793  15.813  1.00 11.21           O  
ANISOU 2289  O   SER B 170     1341   2177    739    -65     79     13       O  
ATOM   2290  CB  SER B 170      19.387  17.535  12.836  1.00 11.22           C  
ANISOU 2290  CB  SER B 170     1541   1642   1078   -132     53     -9       C  
ATOM   2291  OG  SER B 170      20.601  17.270  13.478  1.00 11.30           O  
ANISOU 2291  OG  SER B 170     1388   2053    851    214    -20    238       O  
ATOM   2292  N   HIS B 171      17.198  17.784  15.110  1.00  9.79           N  
ANISOU 2292  N   HIS B 171     1222   1811    684   -151     17    140       N  
ATOM   2293  CA  HIS B 171      16.645  17.460  16.423  1.00  9.52           C  
ANISOU 2293  CA  HIS B 171     1271   1808    537    -43     23    399       C  
ATOM   2294  C   HIS B 171      15.785  16.230  16.278  1.00  9.82           C  
ANISOU 2294  C   HIS B 171     1206   1891    634    297     95    245       C  
ATOM   2295  O   HIS B 171      15.022  16.113  15.294  1.00 10.60           O  
ANISOU 2295  O   HIS B 171     1477   1948    603    -58    -40    237       O  
ATOM   2296  CB  HIS B 171      15.840  18.662  16.892  1.00 10.21           C  
ANISOU 2296  CB  HIS B 171     1320   1836    723    -12     80    210       C  
ATOM   2297  CG  HIS B 171      15.194  18.478  18.222  1.00 10.80           C  
ANISOU 2297  CG  HIS B 171     1267   2278    557    225   -140    362       C  
ATOM   2298  ND1 HIS B 171      13.856  18.208  18.361  1.00 12.03           N  
ANISOU 2298  ND1 HIS B 171     1582   2072    917    153    479    483       N  
ATOM   2299  CD2 HIS B 171      15.724  18.472  19.470  1.00 13.61           C  
ANISOU 2299  CD2 HIS B 171     1175   2820   1174    375   -396     43       C  
ATOM   2300  CE1 HIS B 171      13.582  18.054  19.641  1.00 13.61           C  
ANISOU 2300  CE1 HIS B 171     1480   2516   1174    285    600    552       C  
ATOM   2301  NE2 HIS B 171      14.698  18.205  20.333  1.00 14.92           N  
ANISOU 2301  NE2 HIS B 171     1495   3104   1069    506    136    202       N  
ATOM   2302  N   TYR B 172      15.872  15.319  17.250  1.00 11.59           N  
ANISOU 2302  N   TYR B 172     1667   1900    833     94    -79    440       N  
ATOM   2303  CA  TYR B 172      15.002  14.154  17.283  1.00 11.20           C  
ANISOU 2303  CA  TYR B 172     1423   1781   1050     92    -76    475       C  
ATOM   2304  C   TYR B 172      13.693  14.446  18.018  1.00 10.74           C  
ANISOU 2304  C   TYR B 172     1346   1853    880    261    124    291       C  
ATOM   2305  O   TYR B 172      13.697  14.886  19.173  1.00 13.63           O  
ANISOU 2305  O   TYR B 172     1701   2458   1018    145    -61     45       O  
ATOM   2306  CB  TYR B 172      15.662  12.971  17.976  1.00 12.50           C  
ANISOU 2306  CB  TYR B 172     1602   1953   1193    221   -144    569       C  
ATOM   2307  CG  TYR B 172      14.796  11.727  17.983  1.00 13.42           C  
ANISOU 2307  CG  TYR B 172     1900   1906   1294    249     62    782       C  
ATOM   2308  CD1 TYR B 172      14.423  11.120  16.798  1.00 15.05           C  
ANISOU 2308  CD1 TYR B 172     1933   2052   1730    -84    -32    472       C  
ATOM   2309  CD2 TYR B 172      14.293  11.214  19.162  1.00 15.57           C  
ANISOU 2309  CD2 TYR B 172     1768   2732   1415     30   -220    856       C  
ATOM   2310  CE1 TYR B 172      13.688   9.986  16.769  1.00 16.39           C  
ANISOU 2310  CE1 TYR B 172     2071   2251   1904    135    -51    501       C  
ATOM   2311  CE2 TYR B 172      13.500  10.092  19.156  1.00 19.54           C  
ANISOU 2311  CE2 TYR B 172     2434   2533   2458    -21   -387   1188       C  
ATOM   2312  CZ  TYR B 172      13.182   9.488  17.952  1.00 17.96           C  
ANISOU 2312  CZ  TYR B 172     1873   2470   2480   -101   -242    921       C  
ATOM   2313  OH  TYR B 172      12.426   8.329  17.937  1.00 23.50           O  
ANISOU 2313  OH  TYR B 172     2605   2607   3717   -378   -860   1014       O  
ATOM   2314  N   ASP B 173      12.606  14.440  17.258  1.00 10.47           N  
ANISOU 2314  N   ASP B 173     1397   1804    777    161    109    311       N  
ATOM   2315  CA  ASP B 173      11.291  14.715  17.768  1.00 10.78           C  
ANISOU 2315  CA  ASP B 173     1536   1651    906    124     11     27       C  
ATOM   2316  C   ASP B 173      10.680  13.424  18.297  1.00 11.93           C  
ANISOU 2316  C   ASP B 173     1692   1587   1251    102    231    102       C  
ATOM   2317  O   ASP B 173      10.360  12.536  17.524  1.00 10.82           O  
ANISOU 2317  O   ASP B 173     1765   1517    829     29     50    112       O  
ATOM   2318  CB  ASP B 173      10.392  15.279  16.673  1.00 10.14           C  
ANISOU 2318  CB  ASP B 173     1561   1611    678    157    -70    204       C  
ATOM   2319  CG  ASP B 173       9.021  15.613  17.195  1.00 11.89           C  
ANISOU 2319  CG  ASP B 173     1666   1998    853    461    223    346       C  
ATOM   2320  OD1 ASP B 173       8.934  16.398  18.157  1.00 13.95           O  
ANISOU 2320  OD1 ASP B 173     2016   2098   1185    383    427      4       O  
ATOM   2321  OD2 ASP B 173       7.996  15.182  16.608  1.00 11.92           O  
ANISOU 2321  OD2 ASP B 173     1763   1982    780     99    271    107       O  
ATOM   2322  N   GLU B 174      10.575  13.267  19.609  1.00 14.18           N  
ANISOU 2322  N   GLU B 174     1711   2221   1456   -257     39    364       N  
ATOM   2323  CA  GLU B 174      10.115  11.983  20.151  1.00 13.91           C  
ANISOU 2323  CA  GLU B 174     1949   2210   1124    113      9    496       C  
ATOM   2324  C   GLU B 174       8.689  11.627  19.785  1.00 11.51           C  
ANISOU 2324  C   GLU B 174     1735   1712    925    -25    -19    504       C  
ATOM   2325  O   GLU B 174       8.409  10.456  19.485  1.00 15.48           O  
ANISOU 2325  O   GLU B 174     2331   1775   1773    -99    182    475       O  
ATOM   2326  CB  GLU B 174      10.266  11.902  21.638  1.00 16.40           C  
ANISOU 2326  CB  GLU B 174     2062   2951   1217   -109   -252    661       C  
ATOM   2327  CG  GLU B 174       9.601  10.625  22.278  1.00 22.35           C  
ANISOU 2327  CG  GLU B 174     3633   3436   1421    -49    433    617       C  
ATOM   2328  CD  GLU B 174       9.957   9.182  21.784  1.00 27.26           C  
ANISOU 2328  CD  GLU B 174     2431   4691   3234     95   -543     69       C  
ATOM   2329  OE1 GLU B 174      11.184   8.885  21.614  1.00 25.19           O  
ANISOU 2329  OE1 GLU B 174     2301   5172   2097    165    153    617       O  
ATOM   2330  OE2 GLU B 174       9.013   8.269  21.885  1.00 24.12           O  
ANISOU 2330  OE2 GLU B 174     2611   4608   1942    232    425   -117       O  
ATOM   2331  N   VAL B 175       7.807  12.611  19.676  1.00 11.36           N  
ANISOU 2331  N   VAL B 175     2004   1795    515     71     15    301       N  
ATOM   2332  CA  VAL B 175       6.424  12.309  19.320  1.00 11.75           C  
ANISOU 2332  CA  VAL B 175     1904   1712    848   -254     40    194       C  
ATOM   2333  C   VAL B 175       6.300  11.685  17.931  1.00 10.03           C  
ANISOU 2333  C   VAL B 175     1602   1615    593   -299    100    412       C  
ATOM   2334  O   VAL B 175       5.645  10.686  17.768  1.00 13.63           O  
ANISOU 2334  O   VAL B 175     2318   2007    852   -358    206    434       O  
ATOM   2335  CB  VAL B 175       5.539  13.561  19.452  1.00 12.65           C  
ANISOU 2335  CB  VAL B 175     1928   1917    960   -270    110    161       C  
ATOM   2336  CG1 VAL B 175       4.166  13.433  18.658  1.00 13.49           C  
ANISOU 2336  CG1 VAL B 175     1627   2185   1313   -336    -16    171       C  
ATOM   2337  CG2 VAL B 175       5.342  13.862  20.965  1.00 15.04           C  
ANISOU 2337  CG2 VAL B 175     1949   2671   1094    174    173   -235       C  
ATOM   2338  N   SER B 176       6.929  12.304  16.935  1.00 10.23           N  
ANISOU 2338  N   SER B 176     1404   1578    905   -263    135    216       N  
ATOM   2339  CA  SER B 176       6.868  11.771  15.573  1.00 11.15           C  
ANISOU 2339  CA  SER B 176     1508   1644   1083   -164      2     37       C  
ATOM   2340  C   SER B 176       7.922  10.718  15.265  1.00 10.47           C  
ANISOU 2340  C   SER B 176     1596   1384    997      0     76    165       C  
ATOM   2341  O   SER B 176       7.815  10.014  14.249  1.00 13.03           O  
ANISOU 2341  O   SER B 176     2101   1850   1000   -197    222    -63       O  
ATOM   2342  CB  SER B 176       7.038  12.920  14.572  1.00 11.22           C  
ANISOU 2342  CB  SER B 176     1494   1828    939    -70     72    315       C  
ATOM   2343  OG  SER B 176       8.337  13.493  14.562  1.00 10.44           O  
ANISOU 2343  OG  SER B 176     1407   1732    826    -42     94    277       O  
ATOM   2344  N   GLN B 177       8.894  10.580  16.166  1.00 10.96           N  
ANISOU 2344  N   GLN B 177     1568   1611    983     99    -26    403       N  
ATOM   2345  CA  GLN B 177      10.048   9.713  15.959  1.00 12.41           C  
ANISOU 2345  CA  GLN B 177     1815   1837   1062    -98    -43    398       C  
ATOM   2346  C   GLN B 177      10.780  10.004  14.651  1.00 11.84           C  
ANISOU 2346  C   GLN B 177     1860   1637   1001    221     60    278       C  
ATOM   2347  O   GLN B 177      11.289   9.110  13.987  1.00 17.36           O  
ANISOU 2347  O   GLN B 177     3110   1701   1784    454   1051    595       O  
ATOM   2348  CB  GLN B 177       9.664   8.230  16.124  1.00 15.31           C  
ANISOU 2348  CB  GLN B 177     2132   1830   1853    291    239    331       C  
ATOM   2349  CG  GLN B 177       8.980   7.959  17.442  1.00 16.80           C  
ANISOU 2349  CG  GLN B 177     2566   1876   1940   -324    237    542       C  
ATOM   2350  CD  GLN B 177       8.858   6.498  17.778  1.00 19.87           C  
ANISOU 2350  CD  GLN B 177     2872   2584   2092    308    575    329       C  
ATOM   2351  OE1 GLN B 177       9.650   5.656  17.350  1.00 23.30           O  
ANISOU 2351  OE1 GLN B 177     3559   2556   2737    394    600    625       O  
ATOM   2352  NE2 GLN B 177       7.829   6.183  18.548  1.00 22.08           N  
ANISOU 2352  NE2 GLN B 177     3165   2724   2500   -368   1048    579       N  
ATOM   2353  N   MET B 178      10.882  11.279  14.327  1.00 11.31           N  
ANISOU 2353  N   MET B 178     1502   1606   1189     25    231    191       N  
ATOM   2354  CA  MET B 178      11.662  11.706  13.182  1.00  9.87           C  
ANISOU 2354  CA  MET B 178     1334   1615    801   -203    326    290       C  
ATOM   2355  C   MET B 178      12.805  12.593  13.622  1.00 10.07           C  
ANISOU 2355  C   MET B 178     1662   1423    739     46    145    422       C  
ATOM   2356  O   MET B 178      12.625  13.423  14.509  1.00 10.56           O  
ANISOU 2356  O   MET B 178     1571   1757    681     65    213     88       O  
ATOM   2357  CB  MET B 178      10.745  12.491  12.215  1.00 11.69           C  
ANISOU 2357  CB  MET B 178     1538   1753   1151   -128    297   -132       C  
ATOM   2358  CG  MET B 178       9.606  11.659  11.654  1.00 12.40           C  
ANISOU 2358  CG  MET B 178     1657   2185    867     44   -132     74       C  
ATOM   2359  SD  MET B 178       8.726  12.327  10.241  1.00 12.74           S  
ANISOU 2359  SD  MET B 178     1667   2238    936   -152    195    -38       S  
ATOM   2360  CE  MET B 178       8.026  13.859  10.921  1.00 14.98           C  
ANISOU 2360  CE  MET B 178     2276   1875   1541   -151    194    384       C  
ATOM   2361  N   VAL B 179      13.925  12.514  12.910  1.00 10.23           N  
ANISOU 2361  N   VAL B 179     1334   1573    977     37    199    242       N  
ATOM   2362  CA  VAL B 179      15.007  13.475  13.051  1.00  9.83           C  
ANISOU 2362  CA  VAL B 179     1424   1473    834    159    184    297       C  
ATOM   2363  C   VAL B 179      14.727  14.561  11.989  1.00  9.66           C  
ANISOU 2363  C   VAL B 179     1216   1433   1021    131    160    153       C  
ATOM   2364  O   VAL B 179      14.862  14.333  10.786  1.00 11.27           O  
ANISOU 2364  O   VAL B 179     1667   1499   1116    222    100    124       O  
ATOM   2365  CB  VAL B 179      16.397  12.837  12.863  1.00 10.55           C  
ANISOU 2365  CB  VAL B 179     1591   1822    595    190    -76    160       C  
ATOM   2366  CG1 VAL B 179      17.490  13.939  12.862  1.00 13.19           C  
ANISOU 2366  CG1 VAL B 179     1390   2181   1439    -96     74    364       C  
ATOM   2367  CG2 VAL B 179      16.649  11.745  13.885  1.00 13.10           C  
ANISOU 2367  CG2 VAL B 179     2085   1970    921    561     37    612       C  
ATOM   2368  N   ILE B 180      14.290  15.715  12.478  1.00  8.88           N  
ANISOU 2368  N   ILE B 180     1398   1337    638    280   -107     56       N  
ATOM   2369  CA  ILE B 180      13.846  16.848  11.661  1.00  8.26           C  
ANISOU 2369  CA  ILE B 180     1408   1132    599    201    -33     97       C  
ATOM   2370  C   ILE B 180      15.000  17.832  11.555  1.00  9.70           C  
ANISOU 2370  C   ILE B 180     1220   1473    990   -160     38     30       C  
ATOM   2371  O   ILE B 180      15.570  18.241  12.551  1.00  9.38           O  
ANISOU 2371  O   ILE B 180     1454   1619    492   -165    -90    245       O  
ATOM   2372  CB  ILE B 180      12.598  17.523  12.256  1.00  9.54           C  
ANISOU 2372  CB  ILE B 180     1327   1568    728     67     69     42       C  
ATOM   2373  CG1 ILE B 180      11.459  16.481  12.327  1.00 11.51           C  
ANISOU 2373  CG1 ILE B 180     1683   1686   1003    159    241    386       C  
ATOM   2374  CG2 ILE B 180      12.213  18.786  11.431  1.00 10.27           C  
ANISOU 2374  CG2 ILE B 180     1494   1276   1128    283   -144    244       C  
ATOM   2375  CD1 ILE B 180      10.196  16.928  13.056  1.00 12.04           C  
ANISOU 2375  CD1 ILE B 180     1639   2136    797    138    424     59       C  
ATOM   2376  N   ALA B 181      15.357  18.229  10.331  1.00  9.43           N  
ANISOU 2376  N   ALA B 181     1419   1516    646   -163    -30    141       N  
ATOM   2377  CA  ALA B 181      16.376  19.218  10.061  1.00  9.27           C  
ANISOU 2377  CA  ALA B 181     1268   1246   1007   -105   -157    -54       C  
ATOM   2378  C   ALA B 181      15.838  20.441   9.334  1.00  8.40           C  
ANISOU 2378  C   ALA B 181     1211   1202    778    -78    -89     70       C  
ATOM   2379  O   ALA B 181      15.185  20.290   8.292  1.00  9.83           O  
ANISOU 2379  O   ALA B 181     1452   1490    793    -17   -219   -210       O  
ATOM   2380  CB  ALA B 181      17.549  18.620   9.240  1.00 10.89           C  
ANISOU 2380  CB  ALA B 181     1197   1724   1215    204    109    169       C  
ATOM   2381  N   ALA B 182      15.971  21.602   9.966  1.00  8.05           N  
ANISOU 2381  N   ALA B 182     1400   1270    390    -50    159   -160       N  
ATOM   2382  CA  ALA B 182      15.722  22.879   9.334  1.00  7.11           C  
ANISOU 2382  CA  ALA B 182     1045   1254    403    -10    -98   -239       C  
ATOM   2383  C   ALA B 182      17.057  23.354   8.812  1.00  9.37           C  
ANISOU 2383  C   ALA B 182     1168   1511    879      0    121    112       C  
ATOM   2384  O   ALA B 182      18.043  23.360   9.550  1.00  9.70           O  
ANISOU 2384  O   ALA B 182     1292   1769    625   -135    -55    -99       O  
ATOM   2385  CB  ALA B 182      15.112  23.903  10.285  1.00 10.24           C  
ANISOU 2385  CB  ALA B 182     1592   1328    971    100    230   -288       C  
ATOM   2386  N   THR B 183      17.096  23.803   7.548  1.00  8.18           N  
ANISOU 2386  N   THR B 183     1043   1574    490     91     28    -85       N  
ATOM   2387  CA  THR B 183      18.342  24.153   6.909  1.00  7.57           C  
ANISOU 2387  CA  THR B 183     1033   1376    467     79    205    -12       C  
ATOM   2388  C   THR B 183      18.233  25.518   6.238  1.00  7.89           C  
ANISOU 2388  C   THR B 183     1035   1425    538     65    330    -91       C  
ATOM   2389  O   THR B 183      17.160  25.944   5.815  1.00  8.30           O  
ANISOU 2389  O   THR B 183     1234   1453    465     -7    198   -107       O  
ATOM   2390  CB  THR B 183      18.795  23.081   5.888  1.00  8.22           C  
ANISOU 2390  CB  THR B 183     1063   1467    593    173    -10   -193       C  
ATOM   2391  OG1 THR B 183      18.112  23.247   4.632  1.00  9.08           O  
ANISOU 2391  OG1 THR B 183     1274   1540    635    -10     12     15       O  
ATOM   2392  CG2 THR B 183      18.590  21.666   6.428  1.00 10.52           C  
ANISOU 2392  CG2 THR B 183     1843   1141   1013     90    266     23       C  
ATOM   2393  N   SER B 184      19.379  26.185   6.119  1.00  8.83           N  
ANISOU 2393  N   SER B 184     1129   1366    858     31     84    -91       N  
ATOM   2394  CA  SER B 184      19.480  27.448   5.396  1.00  7.89           C  
ANISOU 2394  CA  SER B 184     1143   1344    509    120    225   -183       C  
ATOM   2395  C   SER B 184      20.793  27.516   4.632  1.00  8.47           C  
ANISOU 2395  C   SER B 184     1276   1285    655    216    290   -282       C  
ATOM   2396  O   SER B 184      21.795  26.905   5.016  1.00 10.30           O  
ANISOU 2396  O   SER B 184     1226   1494   1194     -1    445   -190       O  
ATOM   2397  CB  SER B 184      19.373  28.675   6.331  1.00  9.54           C  
ANISOU 2397  CB  SER B 184     1338   1382    904     64     92   -113       C  
ATOM   2398  OG  SER B 184      18.100  28.805   6.946  1.00  9.66           O  
ANISOU 2398  OG  SER B 184     1443   1580    646     78    454   -165       O  
ATOM   2399  N   TYR B 185      20.756  28.286   3.551  1.00  9.48           N  
ANISOU 2399  N   TYR B 185     1332   1373    894     90    228     60       N  
ATOM   2400  CA  TYR B 185      21.895  28.502   2.685  1.00 10.03           C  
ANISOU 2400  CA  TYR B 185     1261   1613    934    -70    297   -191       C  
ATOM   2401  C   TYR B 185      22.534  29.851   2.988  1.00 10.48           C  
ANISOU 2401  C   TYR B 185     1418   1688    873   -176    209   -139       C  
ATOM   2402  O   TYR B 185      21.835  30.851   3.143  1.00 10.96           O  
ANISOU 2402  O   TYR B 185     1510   1633   1018   -180    320   -127       O  
ATOM   2403  CB  TYR B 185      21.410  28.459   1.236  1.00 10.45           C  
ANISOU 2403  CB  TYR B 185     1560   1570    837   -169    353    -16       C  
ATOM   2404  CG  TYR B 185      20.929  27.102   0.793  1.00  9.03           C  
ANISOU 2404  CG  TYR B 185     1476   1521    432   -177    242    -85       C  
ATOM   2405  CD1 TYR B 185      21.787  26.224   0.179  1.00 11.48           C  
ANISOU 2405  CD1 TYR B 185     1394   1717   1248     13    613   -239       C  
ATOM   2406  CD2 TYR B 185      19.656  26.640   1.102  1.00 11.09           C  
ANISOU 2406  CD2 TYR B 185     1417   1409   1387    -46    296   -234       C  
ATOM   2407  CE1 TYR B 185      21.377  24.966  -0.218  1.00 11.60           C  
ANISOU 2407  CE1 TYR B 185     1623   1601   1182     41    395   -252       C  
ATOM   2408  CE2 TYR B 185      19.260  25.369   0.764  1.00  9.36           C  
ANISOU 2408  CE2 TYR B 185     1338   1444    774    -20    243   -158       C  
ATOM   2409  CZ  TYR B 185      20.123  24.516   0.101  1.00 10.40           C  
ANISOU 2409  CZ  TYR B 185     1411   1524   1015   -134    259     57       C  
ATOM   2410  OH  TYR B 185      19.720  23.196  -0.178  1.00 10.82           O  
ANISOU 2410  OH  TYR B 185     1429   1348   1332   -131    231   -111       O  
ATOM   2411  N   TYR B 186      23.862  29.888   3.012  1.00 11.75           N  
ANISOU 2411  N   TYR B 186     1446   1625   1391   -160    550   -327       N  
ATOM   2412  CA  TYR B 186      24.566  31.141   3.317  1.00 11.97           C  
ANISOU 2412  CA  TYR B 186     1510   1692   1344   -265    450   -373       C  
ATOM   2413  C   TYR B 186      24.250  32.261   2.308  1.00 13.11           C  
ANISOU 2413  C   TYR B 186     1760   1590   1631   -256    254   -214       C  
ATOM   2414  O   TYR B 186      24.099  33.407   2.677  1.00 13.11           O  
ANISOU 2414  O   TYR B 186     1918   1600   1464   -306    453   -135       O  
ATOM   2415  CB  TYR B 186      26.069  30.935   3.473  1.00 12.84           C  
ANISOU 2415  CB  TYR B 186     1786   1830   1261   -273    317   -634       C  
ATOM   2416  CG  TYR B 186      26.436  30.111   4.698  1.00 13.81           C  
ANISOU 2416  CG  TYR B 186     1804   1849   1593     29    298   -272       C  
ATOM   2417  CD1 TYR B 186      26.389  30.678   5.964  1.00 17.38           C  
ANISOU 2417  CD1 TYR B 186     3184   1856   1562     66     83   -515       C  
ATOM   2418  CD2 TYR B 186      26.801  28.798   4.600  1.00 14.21           C  
ANISOU 2418  CD2 TYR B 186     1988   1974   1434    -84   -158   -382       C  
ATOM   2419  CE1 TYR B 186      26.668  29.924   7.092  1.00 20.52           C  
ANISOU 2419  CE1 TYR B 186     4200   2089   1507     -3   -252   -342       C  
ATOM   2420  CE2 TYR B 186      27.088  28.029   5.701  1.00 14.74           C  
ANISOU 2420  CE2 TYR B 186     2292   2073   1235    252   -455   -257       C  
ATOM   2421  CZ  TYR B 186      27.034  28.597   6.966  1.00 21.56           C  
ANISOU 2421  CZ  TYR B 186     3786   2413   1991    199   -818   -547       C  
ATOM   2422  OH  TYR B 186      27.298  27.843   8.106  1.00 25.27           O  
ANISOU 2422  OH  TYR B 186     5021   2381   2199    392  -1166   -503       O  
ATOM   2423  N   THR B 187      24.041  31.906   1.044  1.00 12.56           N  
ANISOU 2423  N   THR B 187     1816   1573   1383   -311    488   -149       N  
ATOM   2424  CA ATHR B 187      23.670  32.926   0.035  0.50 13.97           C  
ANISOU 2424  CA ATHR B 187     2277   1664   1365   -456    273    -65       C  
ATOM   2425  CA BTHR B 187      23.731  32.913   0.065  0.50 13.99           C  
ANISOU 2425  CA BTHR B 187     2294   1633   1386   -420    293    -16       C  
ATOM   2426  C   THR B 187      22.402  33.628   0.409  1.00 13.75           C  
ANISOU 2426  C   THR B 187     2139   1578   1507   -387     83   -249       C  
ATOM   2427  O   THR B 187      22.257  34.834   0.193  1.00 15.28           O  
ANISOU 2427  O   THR B 187     2568   1778   1457   -344    489    -14       O  
ATOM   2428  CB ATHR B 187      23.370  32.416  -1.408  0.50 18.51           C  
ANISOU 2428  CB ATHR B 187     2906   2050   2076   -405    203   -296       C  
ATOM   2429  CB BTHR B 187      23.709  32.266  -1.309  0.50 16.45           C  
ANISOU 2429  CB BTHR B 187     2519   1739   1991   -428    201   -196       C  
ATOM   2430  OG1ATHR B 187      22.503  31.264  -1.416  0.50 11.68           O  
ANISOU 2430  OG1ATHR B 187     2353   1179    902   -796     12    -27       O  
ATOM   2431  OG1BTHR B 187      24.862  31.446  -1.459  0.50 26.38           O  
ANISOU 2431  OG1BTHR B 187     4148   2939   2937   -193    -74    346       O  
ATOM   2432  CG2ATHR B 187      24.603  32.178  -2.163  0.50 18.61           C  
ANISOU 2432  CG2ATHR B 187     2507   2728   1834   -237    216    314       C  
ATOM   2433  CG2BTHR B 187      23.737  33.287  -2.374  0.50 10.35           C  
ANISOU 2433  CG2BTHR B 187     2167    960    805   -202    329     34       C  
ATOM   2434  N   ASP B 188      21.432  32.877   0.909  1.00 12.62           N  
ANISOU 2434  N   ASP B 188     1925   1442   1425   -301    118   -169       N  
ATOM   2435  CA  ASP B 188      20.160  33.431   1.300  1.00 13.55           C  
ANISOU 2435  CA  ASP B 188     1894   1633   1619   -279    -60    -49       C  
ATOM   2436  C   ASP B 188      20.296  34.339   2.545  1.00 13.20           C  
ANISOU 2436  C   ASP B 188     1781   1515   1717   -211    135      2       C  
ATOM   2437  O   ASP B 188      19.657  35.387   2.620  1.00 14.67           O  
ANISOU 2437  O   ASP B 188     2111   1662   1799    -98    206   -151       O  
ATOM   2438  CB  ASP B 188      19.163  32.329   1.568  1.00 11.64           C  
ANISOU 2438  CB  ASP B 188     1914   1473   1034   -225   -121     65       C  
ATOM   2439  CG  ASP B 188      18.769  31.539   0.328  1.00 12.28           C  
ANISOU 2439  CG  ASP B 188     2021   1331   1310   -554   -125   -297       C  
ATOM   2440  OD1 ASP B 188      19.007  32.045  -0.798  1.00 18.78           O  
ANISOU 2440  OD1 ASP B 188     3009   2601   1525   -929      4    777       O  
ATOM   2441  OD2 ASP B 188      18.180  30.452   0.530  1.00 11.06           O  
ANISOU 2441  OD2 ASP B 188     1897   1700    605   -354     68   -176       O  
ATOM   2442  N   ILE B 189      21.086  33.901   3.533  1.00 11.91           N  
ANISOU 2442  N   ILE B 189     1779   1545   1198   -151    217   -133       N  
ATOM   2443  CA  ILE B 189      21.320  34.734   4.698  1.00 12.29           C  
ANISOU 2443  CA  ILE B 189     1784   1626   1257    -65    380   -339       C  
ATOM   2444  C   ILE B 189      21.950  36.057   4.271  1.00 12.96           C  
ANISOU 2444  C   ILE B 189     1683   1839   1399   -234    -43   -377       C  
ATOM   2445  O   ILE B 189      21.540  37.139   4.735  1.00 15.49           O  
ANISOU 2445  O   ILE B 189     2314   1896   1674   -258    404   -388       O  
ATOM   2446  CB  ILE B 189      22.170  34.003   5.792  1.00 11.68           C  
ANISOU 2446  CB  ILE B 189     1420   1801   1215   -140    341   -249       C  
ATOM   2447  CG1 ILE B 189      21.559  32.614   6.146  1.00 12.81           C  
ANISOU 2447  CG1 ILE B 189     1600   2199   1066    -56    597   -269       C  
ATOM   2448  CG2 ILE B 189      22.366  34.913   7.008  1.00 16.06           C  
ANISOU 2448  CG2 ILE B 189     2221   2156   1725   -601    249   -824       C  
ATOM   2449  CD1 ILE B 189      22.508  31.744   6.891  1.00 15.33           C  
ANISOU 2449  CD1 ILE B 189     1553   2729   1541    -38    479    506       C  
ATOM   2450  N   ASN B 190      22.938  35.976   3.383  1.00 13.57           N  
ANISOU 2450  N   ASN B 190     1730   1625   1800   -195    489   -267       N  
ATOM   2451  CA  ASN B 190      23.565  37.174   2.853  1.00 15.03           C  
ANISOU 2451  CA  ASN B 190     2072   1732   1905   -233    415   -308       C  
ATOM   2452  C   ASN B 190      22.578  38.081   2.120  1.00 16.13           C  
ANISOU 2452  C   ASN B 190     2079   1791   2257   -355    549     -7       C  
ATOM   2453  O   ASN B 190      22.550  39.292   2.366  1.00 17.70           O  
ANISOU 2453  O   ASN B 190     2806   1679   2240   -270    469   -154       O  
ATOM   2454  CB  ASN B 190      24.741  36.823   1.926  1.00 16.62           C  
ANISOU 2454  CB  ASN B 190     2086   2231   1995   -459    734    -83       C  
ATOM   2455  CG  ASN B 190      25.888  36.146   2.649  1.00 18.31           C  
ANISOU 2455  CG  ASN B 190     1940   2462   2554   -850    483   -196       C  
ATOM   2456  OD1 ASN B 190      26.033  36.259   3.868  1.00 20.03           O  
ANISOU 2456  OD1 ASN B 190     2312   3438   1859   -424    203     50       O  
ATOM   2457  ND2 ASN B 190      26.787  35.494   1.872  1.00 20.92           N  
ANISOU 2457  ND2 ASN B 190     2554   3172   2223     57   1014     61       N  
ATOM   2458  N   THR B 191      21.689  37.492   1.326  1.00 15.74           N  
ANISOU 2458  N   THR B 191     2457   1826   1697   -234    489    104       N  
ATOM   2459  CA  THR B 191      20.668  38.275   0.631  1.00 16.84           C  
ANISOU 2459  CA  THR B 191     2630   1783   1984   -243    429    230       C  
ATOM   2460  C   THR B 191      19.766  39.007   1.607  1.00 16.51           C  
ANISOU 2460  C   THR B 191     2478   1766   2029   -133    469     59       C  
ATOM   2461  O   THR B 191      19.463  40.192   1.439  1.00 18.70           O  
ANISOU 2461  O   THR B 191     2912   1840   2353    -34    372    -41       O  
ATOM   2462  CB  THR B 191      19.829  37.389  -0.277  1.00 17.22           C  
ANISOU 2462  CB  THR B 191     2975   1859   1708     -1     73     49       C  
ATOM   2463  OG1 THR B 191      20.671  36.873  -1.310  1.00 19.47           O  
ANISOU 2463  OG1 THR B 191     3515   2216   1666    227    359     42       O  
ATOM   2464  CG2 THR B 191      18.656  38.178  -0.913  1.00 21.03           C  
ANISOU 2464  CG2 THR B 191     3421   2368   2199     30   -214    251       C  
ATOM   2465  N   GLU B 192      19.360  38.303   2.658  1.00 16.63           N  
ANISOU 2465  N   GLU B 192     2619   1688   2010    -55    250    -71       N  
ATOM   2466  CA  GLU B 192      18.439  38.875   3.647  1.00 16.95           C  
ANISOU 2466  CA  GLU B 192     2199   1939   2300   -173    304   -149       C  
ATOM   2467  C   GLU B 192      19.091  39.995   4.441  1.00 17.15           C  
ANISOU 2467  C   GLU B 192     2448   1840   2225   -109    277   -245       C  
ATOM   2468  O   GLU B 192      18.424  40.882   4.937  1.00 19.56           O  
ANISOU 2468  O   GLU B 192     2863   1850   2720   -230    444   -632       O  
ATOM   2469  CB  GLU B 192      17.989  37.792   4.641  1.00 14.76           C  
ANISOU 2469  CB  GLU B 192     2158   1715   1733    -58    421    -31       C  
ATOM   2470  CG  GLU B 192      17.086  36.696   4.092  1.00 13.73           C  
ANISOU 2470  CG  GLU B 192     1943   1650   1621   -192     88     25       C  
ATOM   2471  CD  GLU B 192      16.990  35.492   4.976  1.00 18.09           C  
ANISOU 2471  CD  GLU B 192     2850   1574   2448    -75    198    159       C  
ATOM   2472  OE1 GLU B 192      17.465  35.613   6.106  1.00 24.07           O  
ANISOU 2472  OE1 GLU B 192     5099   2045   2000    -19   -114   -123       O  
ATOM   2473  OE2 GLU B 192      16.709  34.375   4.469  1.00 17.32           O  
ANISOU 2473  OE2 GLU B 192     2475   1858   2247   -374    280    187       O  
ATOM   2474  N   ASN B 193      20.404  39.931   4.576  1.00 16.55           N  
ANISOU 2474  N   ASN B 193     2300   1633   2354   -274    486   -380       N  
ATOM   2475  CA  ASN B 193      21.194  40.914   5.331  1.00 17.41           C  
ANISOU 2475  CA  ASN B 193     2389   1906   2317   -295    568   -534       C  
ATOM   2476  C   ASN B 193      21.864  41.992   4.470  1.00 18.12           C  
ANISOU 2476  C   ASN B 193     2414   2068   2400   -559    414   -392       C  
ATOM   2477  O   ASN B 193      22.611  42.811   4.992  1.00 19.98           O  
ANISOU 2477  O   ASN B 193     2660   2256   2673   -631    604   -397       O  
ATOM   2478  CB  ASN B 193      22.259  40.174   6.137  1.00 16.80           C  
ANISOU 2478  CB  ASN B 193     2260   2150   1971   -573    507   -770       C  
ATOM   2479  CG  ASN B 193      21.677  39.488   7.367  1.00 18.74           C  
ANISOU 2479  CG  ASN B 193     2100   2680   2338   -253    774   -442       C  
ATOM   2480  OD1 ASN B 193      21.077  40.160   8.224  1.00 23.87           O  
ANISOU 2480  OD1 ASN B 193     3507   2820   2740    -21   1284   -519       O  
ATOM   2481  ND2 ASN B 193      21.983  38.228   7.554  1.00 20.38           N  
ANISOU 2481  ND2 ASN B 193     3120   2742   1881   -535    370   -884       N  
ATOM   2482  N   LYS B 194      21.559  42.032   3.171  1.00 20.45           N  
ANISOU 2482  N   LYS B 194     2900   2251   2618   -518    848   -257       N  
ATOM   2483  CA  LYS B 194      22.229  42.925   2.232  1.00 22.03           C  
ANISOU 2483  CA  LYS B 194     3154   2295   2919   -462    749     27       C  
ATOM   2484  C   LYS B 194      21.944  44.392   2.579  1.00 21.71           C  
ANISOU 2484  C   LYS B 194     3192   2435   2622   -567    967    -95       C  
ATOM   2485  O   LYS B 194      22.856  45.209   2.527  1.00 25.46           O  
ANISOU 2485  O   LYS B 194     3878   2372   3423   -887   1515   -132       O  
ATOM   2486  CB  LYS B 194      21.772  42.605   0.815  1.00 25.06           C  
ANISOU 2486  CB  LYS B 194     3412   2739   3371   -675    807    199       C  
ATOM   2487  CG  LYS B 194      22.441  43.389  -0.299  1.00 27.90           C  
ANISOU 2487  CG  LYS B 194     3981   3220   3399   -539    327    530       C  
ATOM   2488  CD  LYS B 194      21.945  42.895  -1.643  1.00 36.35           C  
ANISOU 2488  CD  LYS B 194     5366   4702   3742   -256    187    333       C  
ATOM   2489  N   ALA B 195      20.692  44.739   2.896  1.00 22.00           N  
ANISOU 2489  N   ALA B 195     3473   2110   2775   -278    793   -154       N  
ATOM   2490  CA  ALA B 195      20.361  46.133   3.241  1.00 23.59           C  
ANISOU 2490  CA  ALA B 195     3633   2261   3068   -361    592    -99       C  
ATOM   2491  C   ALA B 195      21.118  46.594   4.491  1.00 23.85           C  
ANISOU 2491  C   ALA B 195     3716   2279   3066   -438    487   -377       C  
ATOM   2492  O   ALA B 195      21.568  47.762   4.557  1.00 27.59           O  
ANISOU 2492  O   ALA B 195     4200   2322   3958   -624    664   -516       O  
ATOM   2493  CB  ALA B 195      18.862  46.335   3.410  1.00 23.74           C  
ANISOU 2493  CB  ALA B 195     3635   2475   2907    -64    638    -53       C  
ATOM   2494  N   ILE B 196      21.284  45.692   5.462  1.00 23.81           N  
ANISOU 2494  N   ILE B 196     3522   2334   3191   -554    434   -610       N  
ATOM   2495  CA  ILE B 196      22.077  46.004   6.671  1.00 23.32           C  
ANISOU 2495  CA  ILE B 196     3249   2440   3172   -426    446   -650       C  
ATOM   2496  C   ILE B 196      23.554  46.239   6.306  1.00 25.17           C  
ANISOU 2496  C   ILE B 196     3357   2548   3657   -792    608   -589       C  
ATOM   2497  O   ILE B 196      24.152  47.243   6.689  1.00 29.01           O  
ANISOU 2497  O   ILE B 196     3896   2479   4646   -904    390   -555       O  
ATOM   2498  CB  ILE B 196      21.957  44.886   7.749  1.00 21.66           C  
ANISOU 2498  CB  ILE B 196     3075   2468   2684   -234    373   -632       C  
ATOM   2499  CG1 ILE B 196      20.553  44.886   8.373  1.00 22.44           C  
ANISOU 2499  CG1 ILE B 196     2676   2543   3307   -103    136   -734       C  
ATOM   2500  CG2 ILE B 196      23.034  45.035   8.838  1.00 23.63           C  
ANISOU 2500  CG2 ILE B 196     3207   3445   2323   -186    370   -467       C  
ATOM   2501  CD1 ILE B 196      20.185  43.578   9.052  1.00 23.73           C  
ANISOU 2501  CD1 ILE B 196     2863   2455   3697    -50    630   -428       C  
ATOM   2502  N   LYS B 197      24.082  45.386   5.438  1.00 27.70           N  
ANISOU 2502  N   LYS B 197     3413   2816   4296   -775    749   -644       N  
ATOM   2503  CA  LYS B 197      25.462  45.504   4.967  1.00 29.84           C  
ANISOU 2503  CA  LYS B 197     3501   3343   4493   -750    485   -351       C  
ATOM   2504  C   LYS B 197      25.679  46.819   4.241  1.00 30.40           C  
ANISOU 2504  C   LYS B 197     3732   3296   4521   -923    479   -260       C  
ATOM   2505  O   LYS B 197      26.658  47.532   4.508  1.00 31.08           O  
ANISOU 2505  O   LYS B 197     3470   3460   4879  -1412    994   -351       O  
ATOM   2506  CB  LYS B 197      25.809  44.327   4.044  1.00 29.72           C  
ANISOU 2506  CB  LYS B 197     3373   3236   4683   -661    558   -480       C  
ATOM   2507  CG  LYS B 197      27.211  44.362   3.427  1.00 32.64           C  
ANISOU 2507  CG  LYS B 197     3651   3923   4827   -613    506   -258       C  
ATOM   2508  CD  LYS B 197      27.516  43.108   2.600  1.00 36.57           C  
ANISOU 2508  CD  LYS B 197     4431   4322   5139   -172    420   -714       C  
ATOM   2509  N   GLU B 198      24.737  47.184   3.378  1.00 30.58           N  
ANISOU 2509  N   GLU B 198     3890   3232   4494  -1139    461    -23       N  
ATOM   2510  CA  GLU B 198      24.843  48.411   2.598  1.00 32.20           C  
ANISOU 2510  CA  GLU B 198     4391   3263   4580  -1023    544     56       C  
ATOM   2511  C   GLU B 198      24.729  49.636   3.498  1.00 34.00           C  
ANISOU 2511  C   GLU B 198     4760   3390   4766  -1002    519   -138       C  
ATOM   2512  O   GLU B 198      25.381  50.659   3.237  1.00 35.30           O  
ANISOU 2512  O   GLU B 198     4858   3502   5049  -1304    709    310       O  
ATOM   2513  CB  GLU B 198      23.759  48.478   1.516  1.00 33.06           C  
ANISOU 2513  CB  GLU B 198     4677   3339   4544   -848    468    192       C  
ATOM   2514  CG  GLU B 198      23.963  47.504   0.361  1.00 37.93           C  
ANISOU 2514  CG  GLU B 198     5335   4185   4891   -624    342     85       C  
ATOM   2515  CD  GLU B 198      22.785  47.447  -0.606  1.00 45.72           C  
ANISOU 2515  CD  GLU B 198     6211   5662   5498   -124      3    137       C  
ATOM   2516  OE1 GLU B 198      21.652  47.833  -0.223  1.00 53.15           O  
ANISOU 2516  OE1 GLU B 198     6728   7072   6395    196    -49   -118       O  
ATOM   2517  OE2 GLU B 198      22.988  46.954  -1.738  1.00 52.57           O  
ANISOU 2517  OE2 GLU B 198     7433   6781   5759    127     61   -214       O  
ATOM   2518  N   GLY B 199      23.924  49.532   4.558  1.00 33.71           N  
ANISOU 2518  N   GLY B 199     4784   3148   4876  -1037    336   -305       N  
ATOM   2519  CA  GLY B 199      23.778  50.624   5.538  1.00 35.64           C  
ANISOU 2519  CA  GLY B 199     4894   3592   5055   -821    291   -217       C  
ATOM   2520  C   GLY B 199      25.084  50.886   6.274  1.00 35.33           C  
ANISOU 2520  C   GLY B 199     4991   3457   4974   -906     69   -383       C  
ATOM   2521  O   GLY B 199      25.522  52.033   6.385  1.00 35.69           O  
ANISOU 2521  O   GLY B 199     5173   3086   5298  -1366    216   -372       O  
ATOM   2522  N   VAL B 200      25.716  49.825   6.761  1.00 35.99           N  
ANISOU 2522  N   VAL B 200     4939   3525   5207  -1058     64   -416       N  
ATOM   2523  CA  VAL B 200      27.037  49.900   7.373  1.00 37.91           C  
ANISOU 2523  CA  VAL B 200     5131   4020   5253   -787     59   -344       C  
ATOM   2524  C   VAL B 200      28.037  50.535   6.407  1.00 37.88           C  
ANISOU 2524  C   VAL B 200     5107   3889   5394  -1219    104   -283       C  
ATOM   2525  O   VAL B 200      28.751  51.491   6.754  1.00 39.96           O  
ANISOU 2525  O   VAL B 200     5519   3630   6032  -1445      5   -522       O  
ATOM   2526  CB  VAL B 200      27.521  48.505   7.790  1.00 36.95           C  
ANISOU 2526  CB  VAL B 200     4987   3893   5158   -922    104   -299       C  
ATOM   2527  CG1 VAL B 200      29.035  48.489   8.022  1.00 37.02           C  
ANISOU 2527  CG1 VAL B 200     5156   4162   4745   -301     -9   -535       C  
ATOM   2528  CG2 VAL B 200      26.739  48.019   9.030  1.00 39.54           C  
ANISOU 2528  CG2 VAL B 200     5375   4305   5344   -732    104   -123       C  
ATOM   2529  N   ASN B 201      28.022  50.086   5.157  1.00 38.47           N  
ANISOU 2529  N   ASN B 201     5170   3906   5541  -1377    120   -347       N  
ATOM   2530  CA  ASN B 201      28.881  50.677   4.129  1.00 39.76           C  
ANISOU 2530  CA  ASN B 201     5257   4333   5514  -1076    231     -4       C  
ATOM   2531  C   ASN B 201      28.521  52.142   3.865  1.00 38.36           C  
ANISOU 2531  C   ASN B 201     5392   3444   5737  -1573    231   -102       C  
ATOM   2532  O   ASN B 201      29.423  52.990   3.656  1.00 41.39           O  
ANISOU 2532  O   ASN B 201     5336   4448   5941  -2002    500    272       O  
ATOM   2533  CB  ASN B 201      28.802  49.880   2.828  1.00 40.85           C  
ANISOU 2533  CB  ASN B 201     5416   4420   5683  -1034    255    -25       C  
ATOM   2534  CG  ASN B 201      29.511  48.547   2.914  1.00 45.01           C  
ANISOU 2534  CG  ASN B 201     5750   5472   5878   -507    192     24       C  
ATOM   2535  OD1 ASN B 201      30.361  48.334   3.779  1.00 53.10           O  
ANISOU 2535  OD1 ASN B 201     6254   7166   6755   -389    103    148       O  
ATOM   2536  ND2 ASN B 201      29.160  47.635   2.012  1.00 46.66           N  
ANISOU 2536  ND2 ASN B 201     6054   5269   6405   -632    319   -249       N  
TER    2537      ASN B 201                                                      
HETATM 2538  N  AARF A 301      17.415  35.040  11.655  0.66 23.00           N  
ANISOU 2538  N  AARF A 301     3934   1820   2982    226    169    714       N  
HETATM 2539  C  AARF A 301      18.275  35.799  10.948  0.66 26.47           C  
ANISOU 2539  C  AARF A 301     4055   2990   3010     96     71     96       C  
HETATM 2540  O  AARF A 301      18.951  35.331  10.009  0.66 25.16           O  
ANISOU 2540  O  AARF A 301     3982   2883   2693    142     57    137       O  
HETATM 2541  S  BSO4 A 302      15.483  38.276  12.408  0.34 11.84           S  
ANISOU 2541  S  BSO4 A 302     1511   1827   1160   -876   -106   -270       S  
HETATM 2542  O1 BSO4 A 302      16.777  38.608  11.829  0.34 15.72           O  
ANISOU 2542  O1 BSO4 A 302     2050   2839   1083   -643    458   -776       O  
HETATM 2543  O2 BSO4 A 302      14.417  38.399  11.429  0.34 19.28           O  
ANISOU 2543  O2 BSO4 A 302     2409   2684   2232   -379   -469   -742       O  
HETATM 2544  O3 BSO4 A 302      15.595  36.942  13.011  0.34 16.56           O  
ANISOU 2544  O3 BSO4 A 302     2784   1586   1921    207    558   -402       O  
HETATM 2545  O4 BSO4 A 302      15.215  39.222  13.492  0.34 10.09           O  
ANISOU 2545  O4 BSO4 A 302     1734   1495    601   -259    514   -374       O  
HETATM 2546  N  AARF A 303      -0.493  40.635  22.919  0.33  8.63           N  
ANISOU 2546  N  AARF A 303      757   1532    990    216   -326   -387       N  
HETATM 2547  C  AARF A 303      -0.852  41.570  22.048  0.33 10.21           C  
ANISOU 2547  C  AARF A 303     1000   1469   1409    240   -174   -509       C  
HETATM 2548  O  AARF A 303      -0.064  41.998  21.203  0.33  7.31           O  
ANISOU 2548  O  AARF A 303      570   1442    763    372   -136   -251       O  
HETATM 2549  N  BARF A 304      -2.617  42.392  21.171  0.33  8.56           N  
ANISOU 2549  N  BARF A 304     1267   1246    739    143   -106     23       N  
HETATM 2550  C  BARF A 304      -1.436  41.874  21.483  0.33 11.14           C  
ANISOU 2550  C  BARF A 304     1773   1526    932    116   -148   -162       C  
HETATM 2551  O  BARF A 304      -0.399  42.286  20.971  0.33  7.89           O  
ANISOU 2551  O  BARF A 304     1524   1161    312     93     89    -77       O  
HETATM 2552  N  CARF A 305      -2.585  42.033  21.529  0.34  8.68           N  
ANISOU 2552  N  CARF A 305     1127   1410    761     65   -402    313       N  
HETATM 2553  C  CARF A 305      -1.351  41.566  21.760  0.34 12.44           C  
ANISOU 2553  C  CARF A 305     1764   1673   1288    175   -229   -132       C  
HETATM 2554  O  CARF A 305      -1.142  40.750  22.670  0.34  7.18           O  
ANISOU 2554  O  CARF A 305      934   1199    593    296   -133    246       O  
HETATM 2555  N  AARF A 306      14.894  37.770  11.902  0.66 23.08           N  
ANISOU 2555  N  AARF A 306     2026   3900   2842   -285  -1188   -177       N  
HETATM 2556  C  AARF A 306      15.840  38.352  12.641  0.66 26.30           C  
ANISOU 2556  C  AARF A 306     2791   4041   3160   -388   -456   -384       C  
HETATM 2557  O  AARF A 306      15.530  39.139  13.551  0.66 25.00           O  
ANISOU 2557  O  AARF A 306     2598   4048   2853   -150   -692   -621       O  
HETATM 2558  C1  GOL A 307      13.856  36.345  21.912  1.00 30.23           C  
ANISOU 2558  C1  GOL A 307     4482   3809   3192    109    363   -373       C  
HETATM 2559  O1  GOL A 307      13.930  35.327  20.949  1.00 22.01           O  
ANISOU 2559  O1  GOL A 307     2790   3189   2384   -278    -29   -636       O  
HETATM 2560  C2  GOL A 307      13.653  35.788  23.315  1.00 35.73           C  
ANISOU 2560  C2  GOL A 307     5681   4542   3350    -95   -502   -664       C  
HETATM 2561  O2  GOL A 307      13.913  34.400  23.382  1.00 45.23           O  
ANISOU 2561  O2  GOL A 307     7212   5744   4228    373    -35    215       O  
HETATM 2562  C3  GOL A 307      14.611  36.574  24.211  1.00 33.24           C  
ANISOU 2562  C3  GOL A 307     5684   4236   2707   -188   -748  -1124       C  
HETATM 2563  O3  GOL A 307      14.724  35.950  25.469  1.00 44.40           O  
ANISOU 2563  O3  GOL A 307     6560   6004   4304    329   -408   -158       O  
HETATM 2564  N  AARF B 302      20.312  17.061   2.534  0.34  7.96           N  
ANISOU 2564  N  AARF B 302      960    986   1075    119    -77     51       N  
HETATM 2565  C  AARF B 302      20.260  18.253   1.956  0.34 10.02           C  
ANISOU 2565  C  AARF B 302      861   1703   1240     26   -105    -93       C  
HETATM 2566  O  AARF B 302      20.407  19.284   2.612  0.34  7.24           O  
ANISOU 2566  O  AARF B 302      977   1362    410    111    166   -303       O  
HETATM 2567  S  BSO4 B 301      18.004  35.524  10.980  0.34 17.03           S  
ANISOU 2567  S  BSO4 B 301     1958   2286   2225  -1160    298   -185       S  
HETATM 2568  O1 BSO4 B 301      18.885  35.301   9.822  0.34 10.00           O  
ANISOU 2568  O1 BSO4 B 301     1209   1868    722   -348    417   -805       O  
HETATM 2569  O2 BSO4 B 301      16.689  35.881  10.465  0.34 18.44           O  
ANISOU 2569  O2 BSO4 B 301     1750   2775   2479   -199    170   -244       O  
HETATM 2570  O3 BSO4 B 301      17.874  34.291  11.754  0.34 19.55           O  
ANISOU 2570  O3 BSO4 B 301     2835   2528   2063     -3    295    432       O  
HETATM 2571  O4 BSO4 B 301      18.535  36.655  11.736  0.34 20.60           O  
ANISOU 2571  O4 BSO4 B 301     2736   3309   1780  -1023    552   -791       O  
HETATM 2572  N  BARF B 303      18.905  19.227   0.624  0.33  5.59           N  
ANISOU 2572  N  BARF B 303      911    511    702     22     52   -231       N  
HETATM 2573  C  BARF B 303      19.448  18.891   1.791  0.33  9.42           C  
ANISOU 2573  C  BARF B 303     1482    551   1546    205     74    146       C  
HETATM 2574  O  BARF B 303      20.282  19.601   2.350  0.33  6.22           O  
ANISOU 2574  O  BARF B 303     1267    534    562    -47    171    160       O  
HETATM 2575  N  CARF B 304      20.067  17.070   1.897  0.33  6.78           N  
ANISOU 2575  N  CARF B 304      942    992    640    182   -291     86       N  
HETATM 2576  C  CARF B 304      19.652  18.321   1.672  0.33  8.27           C  
ANISOU 2576  C  CARF B 304      728   1554    859    472    288   -312       C  
HETATM 2577  O  CARF B 304      18.881  18.568   0.735  0.33  6.44           O  
ANISOU 2577  O  CARF B 304      923    943    578    210   -261    290       O  
HETATM 2578  C1 BGOL B 305      13.196  24.043  -3.548  0.34 10.49           C  
ANISOU 2578  C1 BGOL B 305     1043   1314   1629    262    173   -334       C  
HETATM 2579  O1 BGOL B 305      14.303  24.714  -4.108  0.34 15.62           O  
ANISOU 2579  O1 BGOL B 305     2046   2068   1820   -351    247    -97       O  
HETATM 2580  C2 BGOL B 305      12.937  22.751  -4.313  0.34  8.76           C  
ANISOU 2580  C2 BGOL B 305     1000   1425    904   -142    140   -139       C  
HETATM 2581  O2 BGOL B 305      13.907  21.780  -3.956  0.34  8.15           O  
ANISOU 2581  O2 BGOL B 305      882   1413    800    232     37    360       O  
HETATM 2582  C3 BGOL B 305      11.549  22.229  -3.965  0.34 13.02           C  
ANISOU 2582  C3 BGOL B 305     1207   1912   1828     38    403      8       C  
HETATM 2583  O3 BGOL B 305      10.537  23.105  -4.409  0.34 11.95           O  
ANISOU 2583  O3 BGOL B 305     1029   2027   1482     64    105   -242       O  
HETATM 2584  O   HOH A 401      11.064  28.111   2.475  1.00  8.68           O  
ANISOU 2584  O   HOH A 401     1437   1351    509      6     67     63       O  
HETATM 2585  O   HOH A 402      -0.753  37.317  22.330  1.00 11.56           O  
ANISOU 2585  O   HOH A 402     1802   1616    975     17     89   -298       O  
HETATM 2586  O   HOH A 403      -6.161  33.564  24.136  1.00 15.07           O  
ANISOU 2586  O   HOH A 403     2157   2390   1179    -90    214     54       O  
HETATM 2587  O   HOH A 404       4.733  25.327  24.624  1.00 16.64           O  
ANISOU 2587  O   HOH A 404     2494   2700   1127    155    348    267       O  
HETATM 2588  O   HOH A 405       3.302  24.841  11.767  1.00 13.44           O  
ANISOU 2588  O   HOH A 405     1807   2332    965   -326    217   -474       O  
HETATM 2589  O   HOH A 406       1.437  39.085  22.404  1.00 13.10           O  
ANISOU 2589  O   HOH A 406     1822   2064   1090    -98    191   -610       O  
HETATM 2590  O   HOH A 407       9.361  38.937  20.497  1.00 11.53           O  
ANISOU 2590  O   HOH A 407     1665   1742    973     61    -36   -364       O  
HETATM 2591  O   HOH A 408      -1.289  48.162  25.712  1.00 13.94           O  
ANISOU 2591  O   HOH A 408     2237   1799   1260    370      2   -614       O  
HETATM 2592  O   HOH A 409      10.082  46.032  23.333  1.00 16.09           O  
ANISOU 2592  O   HOH A 409     1856   2844   1414    150      7  -1067       O  
HETATM 2593  O   HOH A 410     -11.574  31.899  20.498  1.00 17.53           O  
ANISOU 2593  O   HOH A 410     1922   2591   2148   -375    498   -726       O  
HETATM 2594  O   HOH A 411     -12.752  35.967  27.235  1.00 27.29           O  
ANISOU 2594  O   HOH A 411     2735   4227   3404   -573    552   -188       O  
HETATM 2595  O   HOH A 412       0.795  34.282   3.971  1.00 14.19           O  
ANISOU 2595  O   HOH A 412     1942   2277   1170    112    -58      8       O  
HETATM 2596  O   HOH A 413      -0.067  45.698  32.399  1.00 13.69           O  
ANISOU 2596  O   HOH A 413     2208   2012    981     24     -1   -757       O  
HETATM 2597  O   HOH A 414      -6.788  41.638  22.405  1.00 13.28           O  
ANISOU 2597  O   HOH A 414     1752   2076   1215    206     12   -328       O  
HETATM 2598  O   HOH A 415      10.352  45.654   6.228  1.00 30.33           O  
ANISOU 2598  O   HOH A 415     5394   2867   3262   -560    841   -110       O  
HETATM 2599  O   HOH A 416      -8.573  48.039  18.054  1.00 16.12           O  
ANISOU 2599  O   HOH A 416     2145   2511   1466    525    110   -594       O  
HETATM 2600  O   HOH A 417      21.383  44.608  20.660  1.00 30.96           O  
ANISOU 2600  O   HOH A 417     3003   4087   4672  -1222    497  -1033       O  
HETATM 2601  O   HOH A 418      -6.876  33.640  26.583  1.00 27.09           O  
ANISOU 2601  O   HOH A 418     5490   3478   1326    -19    521   -589       O  
HETATM 2602  O   HOH A 419      18.297  44.943  17.081  1.00 28.09           O  
ANISOU 2602  O   HOH A 419     3572   4036   3062   -251    452  -1323       O  
HETATM 2603  O   HOH A 420      -4.238  39.507   4.014  1.00 13.56           O  
ANISOU 2603  O   HOH A 420     2491   2018    643    346     52    329       O  
HETATM 2604  O   HOH A 421       5.929  49.919  18.672  1.00 16.38           O  
ANISOU 2604  O   HOH A 421     2150   1934   2140   -154    308   -680       O  
HETATM 2605  O   HOH A 422       1.744  47.868   6.556  1.00 23.28           O  
ANISOU 2605  O   HOH A 422     4998   2424   1422    318    282     40       O  
HETATM 2606  O   HOH A 423       4.639  35.698  27.832  1.00 16.98           O  
ANISOU 2606  O   HOH A 423     2573   2199   1676    168    405   -607       O  
HETATM 2607  O   HOH A 424      -0.723  44.154  11.521  1.00 12.60           O  
ANISOU 2607  O   HOH A 424     2044   1589   1155    108    115   -186       O  
HETATM 2608  O   HOH A 425       1.133  35.641  24.891  1.00 13.74           O  
ANISOU 2608  O   HOH A 425     2214   2135    870    156   -171   -541       O  
HETATM 2609  O   HOH A 426       7.178  36.483  27.483  1.00 15.68           O  
ANISOU 2609  O   HOH A 426     2752   2289    915   -137    -48   -676       O  
HETATM 2610  O   HOH A 427       0.094  31.296  25.730  1.00 19.21           O  
ANISOU 2610  O   HOH A 427     2658   2841   1797     51     73    328       O  
HETATM 2611  O   HOH A 428      -9.658  13.444   7.820  1.00 16.67           O  
ANISOU 2611  O   HOH A 428     2537   2258   1538     91   -381     25       O  
HETATM 2612  O   HOH A 429       2.601  36.226   4.791  1.00 14.28           O  
ANISOU 2612  O   HOH A 429     2492   1878   1055     85    -62   -218       O  
HETATM 2613  O   HOH A 430       3.005  37.824  24.459  1.00 15.08           O  
ANISOU 2613  O   HOH A 430     2048   1955   1726   -109     85   -745       O  
HETATM 2614  O   HOH A 431      -1.949  48.356   9.966  1.00 18.33           O  
ANISOU 2614  O   HOH A 431     3000   2056   1906     32     91    160       O  
HETATM 2615  O   HOH A 432     -10.914  34.041   0.448  1.00 30.18           O  
ANISOU 2615  O   HOH A 432     3095   3598   4772   -276   -306    574       O  
HETATM 2616  O   HOH A 433     -12.763  27.930   7.573  1.00 28.68           O  
ANISOU 2616  O   HOH A 433     2636   4607   3654   -277    858    619       O  
HETATM 2617  O   HOH A 434      -2.853  22.786   1.480  1.00 21.84           O  
ANISOU 2617  O   HOH A 434     2177   2101   4018    202   1443    177       O  
HETATM 2618  O   HOH A 435      -1.654  16.591   3.624  1.00 19.47           O  
ANISOU 2618  O   HOH A 435     2186   2986   2225   -207    -64   -280       O  
HETATM 2619  O   HOH A 436      10.354  36.442  23.864  1.00 13.81           O  
ANISOU 2619  O   HOH A 436     1936   2169   1139   -201   -210   -418       O  
HETATM 2620  O   HOH A 437     -14.041  46.736  21.239  1.00 29.23           O  
ANISOU 2620  O   HOH A 437     4327   3413   3365    266   1794   -856       O  
HETATM 2621  O   HOH A 438       5.500  42.652  29.794  1.00 16.92           O  
ANISOU 2621  O   HOH A 438     2478   2258   1693    310   -617   -962       O  
HETATM 2622  O   HOH A 439      -6.735  48.673   4.389  1.00 29.05           O  
ANISOU 2622  O   HOH A 439     5393   3125   2520    722   -673    952       O  
HETATM 2623  O   HOH A 440      15.164  43.830   5.382  1.00 21.06           O  
ANISOU 2623  O   HOH A 440     3090   2761   2151    -95    692   -402       O  
HETATM 2624  O   HOH A 441       5.186  31.110  -1.373  1.00 31.45           O  
ANISOU 2624  O   HOH A 441     4548   4359   3041   -153   -894    291       O  
HETATM 2625  O   HOH A 442       0.316  36.854  33.808  1.00 30.81           O  
ANISOU 2625  O   HOH A 442     5038   2627   4042   -257   -804    450       O  
HETATM 2626  O   HOH A 443      16.921  44.029  25.057  1.00 26.44           O  
ANISOU 2626  O   HOH A 443     3067   3993   2985   -512   -428  -1118       O  
HETATM 2627  O   HOH A 444       1.171  53.055  15.528  1.00 29.25           O  
ANISOU 2627  O   HOH A 444     4943   2572   3599    597   1415    604       O  
HETATM 2628  O   HOH A 445     -14.470  38.443  28.858  1.00 35.50           O  
ANISOU 2628  O   HOH A 445     2994   5234   5258   -264   1081    367       O  
HETATM 2629  O   HOH A 446       0.424  50.991  13.334  1.00 18.27           O  
ANISOU 2629  O   HOH A 446     2999   1893   2049    262    -97     -4       O  
HETATM 2630  O   HOH A 447      -1.706  46.835  28.217  1.00 15.97           O  
ANISOU 2630  O   HOH A 447     2653   1905   1509    234     66   -444       O  
HETATM 2631  O   HOH A 448      13.734  32.659  20.283  1.00 22.90           O  
ANISOU 2631  O   HOH A 448     2775   2943   2982      4    186    218       O  
HETATM 2632  O   HOH A 449      -4.908  53.608  15.971  1.00 23.83           O  
ANISOU 2632  O   HOH A 449     3990   3075   1986    364   -676    521       O  
HETATM 2633  O   HOH A 450      -0.353  36.254  29.630  1.00 17.27           O  
ANISOU 2633  O   HOH A 450     2786   2405   1370   -143   -318   -387       O  
HETATM 2634  O   HOH A 451      -1.788  30.752  27.555  1.00 25.24           O  
ANISOU 2634  O   HOH A 451     3699   3135   2755   -151   1029     39       O  
HETATM 2635  O   HOH A 452       1.311  22.989  11.947  1.00 12.83           O  
ANISOU 2635  O   HOH A 452     1603   2323    949   -155    -88    240       O  
HETATM 2636  O   HOH A 453     -13.814  33.548  20.679  1.00 22.67           O  
ANISOU 2636  O   HOH A 453     2586   3911   2116    121    190  -1101       O  
HETATM 2637  O   HOH A 454       8.115  41.917  30.464  1.00 22.53           O  
ANISOU 2637  O   HOH A 454     2454   3098   3006    277   -648   -849       O  
HETATM 2638  O   HOH A 455     -11.529  27.656  18.953  1.00 26.37           O  
ANISOU 2638  O   HOH A 455     3831   3530   2656   -218   -628  -1404       O  
HETATM 2639  O   HOH A 456      -4.339  17.323   5.845  1.00 19.51           O  
ANISOU 2639  O   HOH A 456     2225   1987   3201     45     46    588       O  
HETATM 2640  O   HOH A 457     -12.554  16.358  13.076  1.00 19.68           O  
ANISOU 2640  O   HOH A 457     2322   3181   1972   -539   -412    810       O  
HETATM 2641  O   HOH A 458      -1.885  43.794  31.358  1.00 16.91           O  
ANISOU 2641  O   HOH A 458     2633   2634   1156   -130   -297   -164       O  
HETATM 2642  O   HOH A 459     -10.925  14.214  11.622  1.00 17.32           O  
ANISOU 2642  O   HOH A 459     2165   2854   1560   -504   -185    737       O  
HETATM 2643  O   HOH A 460       9.133  37.917   3.886  1.00 20.66           O  
ANISOU 2643  O   HOH A 460     3228   2827   1792   -311    500     60       O  
HETATM 2644  O   HOH A 461      -0.104  47.645  30.241  1.00 17.20           O  
ANISOU 2644  O   HOH A 461     3424   2049   1059     -9     12   -472       O  
HETATM 2645  O   HOH A 462       9.438  49.558  24.940  1.00 24.07           O  
ANISOU 2645  O   HOH A 462     2973   3746   2424   -858   -521   -777       O  
HETATM 2646  O   HOH A 463      16.941  41.320  13.314  1.00 20.93           O  
ANISOU 2646  O   HOH A 463     3189   3228   1534   -422    287   -442       O  
HETATM 2647  O   HOH A 464      -9.062  42.521   7.194  1.00 21.46           O  
ANISOU 2647  O   HOH A 464     3276   3266   1609    194   -173    -94       O  
HETATM 2648  O   HOH A 465      -9.349  42.818  28.933  1.00 30.27           O  
ANISOU 2648  O   HOH A 465     4099   4390   3012    613    598   -190       O  
HETATM 2649  O   HOH A 466      -5.458  28.632  22.909  1.00 23.10           O  
ANISOU 2649  O   HOH A 466     2930   3901   1945   -219    165   -734       O  
HETATM 2650  O   HOH A 467     -18.536  41.895  16.230  1.00 32.99           O  
ANISOU 2650  O   HOH A 467     3305   5292   3936    397   -236   -838       O  
HETATM 2651  O   HOH A 468     -19.114  39.935  14.736  1.00 34.23           O  
ANISOU 2651  O   HOH A 468     2678   5081   5246    913   -186  -1570       O  
HETATM 2652  O   HOH A 469      -8.121  31.842  22.662  1.00 18.54           O  
ANISOU 2652  O   HOH A 469     2639   2758   1645    -62     -1     29       O  
HETATM 2653  O   HOH A 470      13.780  30.867  22.330  1.00 27.18           O  
ANISOU 2653  O   HOH A 470     2453   4532   3342    239     18   1277       O  
HETATM 2654  O   HOH A 471       1.436  33.523  27.020  1.00 22.75           O  
ANISOU 2654  O   HOH A 471     2977   2773   2893   -359   -123   -757       O  
HETATM 2655  O   HOH A 472       4.075  33.239  27.235  1.00 23.36           O  
ANISOU 2655  O   HOH A 472     2632   4411   1831   -461    505   -321       O  
HETATM 2656  O   HOH A 473      20.862  35.453  18.557  1.00 24.43           O  
ANISOU 2656  O   HOH A 473     3557   3125   2598    346    367   -308       O  
HETATM 2657  O   HOH A 474      -0.359  44.713  36.554  1.00 22.82           O  
ANISOU 2657  O   HOH A 474     3772   2308   2590   -117    523   -797       O  
HETATM 2658  O   HOH A 475     -15.967  42.987  16.057  1.00 25.36           O  
ANISOU 2658  O   HOH A 475     3499   3631   2504    409   -157   -712       O  
HETATM 2659  O   HOH A 476       7.290  51.441  16.867  1.00 32.40           O  
ANISOU 2659  O   HOH A 476     4191   3586   4530   -921    150    992       O  
HETATM 2660  O   HOH A 477     -11.851  53.010  22.150  1.00 25.45           O  
ANISOU 2660  O   HOH A 477     4432   3695   1539    960     56   -244       O  
HETATM 2661  O   HOH A 478      11.657  48.301  23.639  1.00 29.92           O  
ANISOU 2661  O   HOH A 478     3443   3941   3984   -246     28  -1432       O  
HETATM 2662  O   HOH A 479      14.967  37.423   7.503  1.00 31.56           O  
ANISOU 2662  O   HOH A 479     4648   4650   2693   -662    469   -178       O  
HETATM 2663  O   HOH A 480      -7.693  40.562  29.638  1.00 21.06           O  
ANISOU 2663  O   HOH A 480     2707   3269   2024     38    598   -826       O  
HETATM 2664  O   HOH A 481      -1.385  13.987   3.447  1.00 23.70           O  
ANISOU 2664  O   HOH A 481     4281   3257   1465   -587   -385     63       O  
HETATM 2665  O   HOH A 482      -5.513  32.641  28.700  1.00 28.30           O  
ANISOU 2665  O   HOH A 482     4375   3409   2970   -585   -506   -527       O  
HETATM 2666  O   HOH A 483     -13.495  25.924  17.768  1.00 20.38           O  
ANISOU 2666  O   HOH A 483     2283   3592   1867     49     -5  -1282       O  
HETATM 2667  O   HOH A 484     -10.782  13.790   5.521  1.00 39.75           O  
ANISOU 2667  O   HOH A 484     5710   5663   3727   2363   -785   -665       O  
HETATM 2668  O   HOH A 485       9.225  39.422  30.354  1.00 29.89           O  
ANISOU 2668  O   HOH A 485     3301   3900   4153    543   -205   -814       O  
HETATM 2669  O   HOH A 486      -2.265  44.114  28.575  1.00 15.33           O  
ANISOU 2669  O   HOH A 486     2328   2310   1186    -40    191   -486       O  
HETATM 2670  O   HOH A 487      -4.904  46.986  25.676  1.00 23.20           O  
ANISOU 2670  O   HOH A 487     3985   2553   2276    850   -149   -633       O  
HETATM 2671  O   HOH A 488     -17.291  22.115  12.935  1.00 25.98           O  
ANISOU 2671  O   HOH A 488     1933   5179   2756    423   -687  -2074       O  
HETATM 2672  O   HOH A 489      17.007  47.813   6.001  1.00 30.60           O  
ANISOU 2672  O   HOH A 489     6150   2477   2997    276    805    380       O  
HETATM 2673  O   HOH A 490       6.986  42.955  33.037  1.00 23.17           O  
ANISOU 2673  O   HOH A 490     2682   2516   3605    292   -754   -526       O  
HETATM 2674  O   HOH A 491     -12.553  30.110  18.670  1.00 22.56           O  
ANISOU 2674  O   HOH A 491     2741   3100   2731   -263    -28  -1186       O  
HETATM 2675  O   HOH A 492      19.677  40.745  12.742  1.00 29.32           O  
ANISOU 2675  O   HOH A 492     4343   3854   2942   -452   1012   -805       O  
HETATM 2676  O   HOH A 493       4.377  51.901  19.930  1.00 22.24           O  
ANISOU 2676  O   HOH A 493     3394   2147   2906     71    846   -898       O  
HETATM 2677  O   HOH A 494      11.274  42.142  28.062  1.00 29.54           O  
ANISOU 2677  O   HOH A 494     3676   5568   1977   -625   -104    161       O  
HETATM 2678  O   HOH A 495      18.577  41.025  27.094  1.00 35.88           O  
ANISOU 2678  O   HOH A 495     5015   5504   3113     77  -1051   -104       O  
HETATM 2679  O   HOH A 496      17.170  45.158   6.702  1.00 19.42           O  
ANISOU 2679  O   HOH A 496     2778   2040   2558   -169   1014   -247       O  
HETATM 2680  O   HOH A 497       8.661  37.007  29.673  1.00 26.68           O  
ANISOU 2680  O   HOH A 497     3985   3575   2576    382   -758   -351       O  
HETATM 2681  O   HOH A 498      -6.770  39.437  32.787  1.00 33.02           O  
ANISOU 2681  O   HOH A 498     3793   6347   2405   -558    574  -1763       O  
HETATM 2682  O   HOH A 499     -10.086  27.114  21.242  1.00 28.02           O  
ANISOU 2682  O   HOH A 499     4426   3806   2411   -222    706   -606       O  
HETATM 2683  O   HOH A 500      -7.925  25.301  21.449  1.00 23.63           O  
ANISOU 2683  O   HOH A 500     2309   4896   1771   -268     28   -571       O  
HETATM 2684  O   HOH A 501      -9.232  49.043   5.709  1.00 34.92           O  
ANISOU 2684  O   HOH A 501     4896   4258   4114   1339   -287    833       O  
HETATM 2685  O   HOH A 502       2.349  40.517   2.983  1.00 28.65           O  
ANISOU 2685  O   HOH A 502     5301   3359   2224    162   -186    550       O  
HETATM 2686  O   HOH A 503     -18.263  42.262  21.782  1.00 34.80           O  
ANISOU 2686  O   HOH A 503     2734   4843   5645   1073   1228    649       O  
HETATM 2687  O   HOH A 504      16.396  46.659  24.330  1.00 30.14           O  
ANISOU 2687  O   HOH A 504     3933   4378   3140   -830   -258  -1232       O  
HETATM 2688  O   HOH A 505     -11.859  32.933   2.400  1.00 32.94           O  
ANISOU 2688  O   HOH A 505     4473   3279   4764   -834    743   -813       O  
HETATM 2689  O   HOH A 506       5.618  29.284  29.378  1.00 26.58           O  
ANISOU 2689  O   HOH A 506     4123   4582   1394      1   -186   -100       O  
HETATM 2690  O   HOH A 507      22.941  37.944  21.333  1.00 29.36           O  
ANISOU 2690  O   HOH A 507     3432   4249   3471   -298    -59     75       O  
HETATM 2691  O   HOH A 508       0.864  46.639   3.734  1.00 35.87           O  
ANISOU 2691  O   HOH A 508     6325   3709   3594   -404   -138   -397       O  
HETATM 2692  O   HOH A 509      -8.913  40.924   5.041  1.00 29.12           O  
ANISOU 2692  O   HOH A 509     4060   3349   3655    535    480   -529       O  
HETATM 2693  O   HOH A 510     -17.855  16.661  12.656  1.00 27.09           O  
ANISOU 2693  O   HOH A 510     3239   4213   2839   -788   -337    849       O  
HETATM 2694  O   HOH A 511       4.483  36.427   2.569  1.00 31.25           O  
ANISOU 2694  O   HOH A 511     5196   3494   3182    440    992    -57       O  
HETATM 2695  O   HOH A 512       7.424  35.663   3.014  1.00 24.67           O  
ANISOU 2695  O   HOH A 512     4555   2960   1855    246   -240    311       O  
HETATM 2696  O   HOH A 513     -11.962  22.119   8.404  1.00  9.88           O  
ANISOU 2696  O   HOH A 513     1456   1663    633   -113   -283    -26       O  
HETATM 2697  O   HOH A 514     -13.283  35.702   9.855  1.00 21.28           O  
ANISOU 2697  O   HOH A 514     2847   4004   1233    895   -495  -1240       O  
HETATM 2698  O   HOH A 515     -12.023  11.904  10.826  1.00 33.38           O  
ANISOU 2698  O   HOH A 515     4861   2852   4968   -839  -1400    -80       O  
HETATM 2699  O   HOH A 516      -2.391  51.170  13.102  1.00 30.88           O  
ANISOU 2699  O   HOH A 516     3542   4405   3785    348   -379    811       O  
HETATM 2700  O   HOH A 517      -2.835  50.836  10.490  1.00 32.61           O  
ANISOU 2700  O   HOH A 517     5478   3201   3712   1178    276     10       O  
HETATM 2701  O   HOH A 518      -4.893  51.322  14.178  1.00 27.79           O  
ANISOU 2701  O   HOH A 518     4748   3808   2002    344    -27   -134       O  
HETATM 2702  O   HOH A 519       0.729  34.040  29.467  1.00 32.64           O  
ANISOU 2702  O   HOH A 519     5289   4159   2953     23    -21   -454       O  
HETATM 2703  O   HOH A 520      -7.436  32.250  30.759  1.00 39.61           O  
ANISOU 2703  O   HOH A 520     4185   6014   4848   -181    375    928       O  
HETATM 2704  O   HOH A 521      -9.740  33.231  29.906  1.00 37.93           O  
ANISOU 2704  O   HOH A 521     5727   4472   4213   -579    138    181       O  
HETATM 2705  O   HOH A 522     -10.490  35.640  30.806  1.00 38.53           O  
ANISOU 2705  O   HOH A 522     4882   5879   3878    -26   1267    -71       O  
HETATM 2706  O   HOH A 523      -8.392  36.628  33.015  1.00 35.26           O  
ANISOU 2706  O   HOH A 523     4901   5572   2920     12    998    108       O  
HETATM 2707  O   HOH A 524      -6.443  34.651  33.120  1.00 36.55           O  
ANISOU 2707  O   HOH A 524     5124   5500   3262  -1076   1161    338       O  
HETATM 2708  O   HOH A 525      -1.387  35.073  32.988  1.00 40.10           O  
ANISOU 2708  O   HOH A 525     5851   4314   5070     35   -776   -251       O  
HETATM 2709  O   HOH A 526       1.295  39.788  35.818  1.00 36.39           O  
ANISOU 2709  O   HOH A 526     6380   4422   3022    -30   -694   -370       O  
HETATM 2710  O   HOH A 527       4.805  43.618  36.004  1.00 34.95           O  
ANISOU 2710  O   HOH A 527     5127   4016   4137    894   -384   -223       O  
HETATM 2711  O   HOH A 528      22.546  42.099  11.778  1.00 32.38           O  
ANISOU 2711  O   HOH A 528     3352   3871   5078   -679   -706    -33       O  
HETATM 2712  O   HOH A 529      23.680  38.605  17.918  1.00 21.04           O  
ANISOU 2712  O   HOH A 529     1900   3369   2724   -211    -45  -1117       O  
HETATM 2713  O   HOH A 530      -3.924  35.697  32.294  1.00 22.21           O  
ANISOU 2713  O   HOH A 530     3245   3054   2138   -355    -24     48       O  
HETATM 2714  O   HOH A 531     -11.373  28.953  11.735  1.00 18.95           O  
ANISOU 2714  O   HOH A 531     2831   2520   1847    565    450    165       O  
HETATM 2715  O   HOH A 532      -6.968  45.224  25.175  1.00 23.50           O  
ANISOU 2715  O   HOH A 532     4486   3003   1438   -135    461   -530       O  
HETATM 2716  O   HOH A 533      -9.480  33.886  27.321  1.00 25.06           O  
ANISOU 2716  O   HOH A 533     4403   3497   1619   -377    -23   -164       O  
HETATM 2717  O   HOH A 534      -4.583  42.162  30.290  1.00 21.47           O  
ANISOU 2717  O   HOH A 534     3468   2927   1762   -130    -60   -516       O  
HETATM 2718  O   HOH A 535      21.177  36.579  10.164  1.00 21.18           O  
ANISOU 2718  O   HOH A 535     2990   3027   2030   -113   -213   -487       O  
HETATM 2719  O   HOH A 536      -9.233  54.136  13.387  1.00 31.39           O  
ANISOU 2719  O   HOH A 536     5592   2831   3502    975    720    331       O  
HETATM 2720  O   HOH A 537      -3.703  34.378  29.796  1.00 20.68           O  
ANISOU 2720  O   HOH A 537     3831   2887   1139    -61    330    368       O  
HETATM 2721  O   HOH A 538      14.570  40.072  25.548  1.00 24.52           O  
ANISOU 2721  O   HOH A 538     2533   4344   2438   -578   -250   -275       O  
HETATM 2722  O   HOH A 539     -17.656  37.932  13.637  1.00 27.33           O  
ANISOU 2722  O   HOH A 539     2359   4384   3640    164   -165   -941       O  
HETATM 2723  O   HOH A 540     -14.330  22.659   7.217  1.00 22.38           O  
ANISOU 2723  O   HOH A 540     1354   4722   2425    175    233   1498       O  
HETATM 2724  O   HOH A 541      -5.121  13.393   6.352  1.00 30.98           O  
ANISOU 2724  O   HOH A 541     3231   3692   4845   -239   -787    688       O  
HETATM 2725  O   HOH A 542       9.873  49.803   9.854  1.00 36.42           O  
ANISOU 2725  O   HOH A 542     5227   2935   5676   -623    303    588       O  
HETATM 2726  O   HOH A 543      11.449  49.912  12.519  1.00 41.81           O  
ANISOU 2726  O   HOH A 543     5095   4681   6107    135   -110    105       O  
HETATM 2727  O   HOH A 544      -5.199  30.868  24.755  1.00 27.31           O  
ANISOU 2727  O   HOH A 544     4575   4437   1362    783     21   -154       O  
HETATM 2728  O   HOH A 545     -17.529  46.774  18.282  1.00 30.76           O  
ANISOU 2728  O   HOH A 545     3132   4111   4445   1127    736    100       O  
HETATM 2729  O   HOH A 546       9.993  47.692  12.983  1.00 25.57           O  
ANISOU 2729  O   HOH A 546     2782   4110   2824    656    394    109       O  
HETATM 2730  O   HOH A 547      -1.714  32.419  29.817  1.00 28.00           O  
ANISOU 2730  O   HOH A 547     5281   3333   2022    366   -575   -498       O  
HETATM 2731  O   HOH A 548      -7.419  11.997   7.175  1.00 29.81           O  
ANISOU 2731  O   HOH A 548     3475   4518   3332    226   -363   -779       O  
HETATM 2732  O   HOH A 549     -14.964  27.505  15.702  1.00 36.80           O  
ANISOU 2732  O   HOH A 549     3189   4517   6274    289   -161   -783       O  
HETATM 2733  O   HOH A 550     -11.750  30.160  22.436  1.00 34.34           O  
ANISOU 2733  O   HOH A 550     4923   4309   3813  -1011   -212    349       O  
HETATM 2734  O   HOH A 551     -14.901  32.828  23.252  1.00 34.97           O  
ANISOU 2734  O   HOH A 551     4595   4576   4116    -69   1444   -406       O  
HETATM 2735  O   HOH A 552     -15.770  33.796  18.700  1.00 30.99           O  
ANISOU 2735  O   HOH A 552     3319   5368   3085     19  -1088   -829       O  
HETATM 2736  O   HOH A 553     -15.187  29.747  19.577  1.00 41.28           O  
ANISOU 2736  O   HOH A 553     4661   6321   4701    -49    255    -72       O  
HETATM 2737  O   HOH A 554     -16.117  35.152  16.160  1.00 33.67           O  
ANISOU 2737  O   HOH A 554     3830   5069   3892   -809  -1131    125       O  
HETATM 2738  O   HOH A 555     -15.312  33.998  13.866  1.00 40.91           O  
ANISOU 2738  O   HOH A 555     4272   6008   5263    495   -250   -415       O  
HETATM 2739  O   HOH A 556     -13.947  29.335   9.532  1.00 28.83           O  
ANISOU 2739  O   HOH A 556     3191   4928   2832   -756    646   -370       O  
HETATM 2740  O   HOH A 557     -13.616  34.401   3.773  1.00 33.29           O  
ANISOU 2740  O   HOH A 557     3984   4993   3671    152  -1563   -526       O  
HETATM 2741  O   HOH A 558     -13.372  42.119   5.563  1.00 40.97           O  
ANISOU 2741  O   HOH A 558     5676   5395   4496   -312  -1081  -1168       O  
HETATM 2742  O   HOH A 559     -11.769  42.979   7.804  1.00 26.81           O  
ANISOU 2742  O   HOH A 559     2835   4537   2813    490   -283   -198       O  
HETATM 2743  O   HOH A 560     -12.027  45.729   7.892  1.00 30.44           O  
ANISOU 2743  O   HOH A 560     4245   4948   2370    408   -849   -115       O  
HETATM 2744  O   HOH A 561     -13.499  46.586  10.081  1.00 32.92           O  
ANISOU 2744  O   HOH A 561     4755   4788   2965    382  -1080    635       O  
HETATM 2745  O   HOH A 562      -9.979  47.502   7.721  1.00 30.19           O  
ANISOU 2745  O   HOH A 562     3853   4159   3456    929   -882   -174       O  
HETATM 2746  O   HOH A 563      -1.773  48.688   7.171  1.00 30.13           O  
ANISOU 2746  O   HOH A 563     6432   3739   1277  -1225    213    -27       O  
HETATM 2747  O   HOH A 564       0.477  43.826   1.344  1.00 27.23           O  
ANISOU 2747  O   HOH A 564     4324   3726   2296   -168     78   -118       O  
HETATM 2748  O   HOH A 565       7.540  40.111   2.899  1.00 29.83           O  
ANISOU 2748  O   HOH A 565     5552   3622   2157    -19    530    361       O  
HETATM 2749  O   HOH A 566       6.844  42.346   4.225  1.00 32.51           O  
ANISOU 2749  O   HOH A 566     5922   3631   2798    452    587    629       O  
HETATM 2750  O   HOH A 567       8.565  44.685   4.450  1.00 32.01           O  
ANISOU 2750  O   HOH A 567     4909   4461   2790   -231    570     32       O  
HETATM 2751  O   HOH A 568      -5.348  36.878   2.023  1.00 35.49           O  
ANISOU 2751  O   HOH A 568     4135   6767   2581    489    131   1796       O  
HETATM 2752  O   HOH A 569      -1.612  38.069   0.815  1.00 36.81           O  
ANISOU 2752  O   HOH A 569     5747   5386   2852    217    718    301       O  
HETATM 2753  O   HOH A 570       0.744  34.246   1.288  1.00 29.32           O  
ANISOU 2753  O   HOH A 570     4261   4893   1986   -164     86    215       O  
HETATM 2754  O   HOH A 571       5.025  35.302   0.434  1.00 40.31           O  
ANISOU 2754  O   HOH A 571     5473   4730   5111    769   1056    399       O  
HETATM 2755  O   HOH A 572      19.704  43.688  24.682  1.00 28.76           O  
ANISOU 2755  O   HOH A 572     3554   5189   2185   -657   -457   -390       O  
HETATM 2756  O   HOH A 573      -4.196  38.665   1.333  1.00 31.94           O  
ANISOU 2756  O   HOH A 573     5642   3478   3014     50     30    138       O  
HETATM 2757  O   HOH A 574     -11.356  48.295  11.431  1.00 37.09           O  
ANISOU 2757  O   HOH A 574     5686   3793   4611    964  -1597    250       O  
HETATM 2758  O   HOH A 575     -16.070  50.699  16.572  1.00 37.14           O  
ANISOU 2758  O   HOH A 575     4569   5819   3722    848   -646   -304       O  
HETATM 2759  O   HOH A 576     -13.491  54.231  20.307  1.00 38.08           O  
ANISOU 2759  O   HOH A 576     5154   5999   3313   1006   -353    288       O  
HETATM 2760  O   HOH A 577     -13.763  53.252  24.098  1.00 36.71           O  
ANISOU 2760  O   HOH A 577     4498   4212   5236   1124  -1194     17       O  
HETATM 2761  O   HOH A 578      15.845  31.994  18.946  1.00 38.65           O  
ANISOU 2761  O   HOH A 578     4195   3574   6916    435    177   -618       O  
HETATM 2762  O   HOH A 579      -2.096  22.874  25.473  1.00 34.81           O  
ANISOU 2762  O   HOH A 579     5370   5273   2582   -484   -897    663       O  
HETATM 2763  O   HOH A 580      -9.522  46.205  25.350  1.00 28.85           O  
ANISOU 2763  O   HOH A 580     4832   3447   2683    623    221   -327       O  
HETATM 2764  O   HOH A 581     -12.013  42.995  28.053  1.00 39.40           O  
ANISOU 2764  O   HOH A 581     5273   4855   4839    467    669   -264       O  
HETATM 2765  O   HOH A 582       5.084  39.152   2.040  1.00 36.52           O  
ANISOU 2765  O   HOH A 582     5289   4756   3828    326   1057    351       O  
HETATM 2766  O   HOH A 583      -6.217  26.330  23.295  1.00 30.47           O  
ANISOU 2766  O   HOH A 583     3883   7162    530   -264    543    160       O  
HETATM 2767  O   HOH A 584       2.643  35.456  33.767  1.00 41.45           O  
ANISOU 2767  O   HOH A 584     5262   4610   5877   -635   -190    649       O  
HETATM 2768  O   HOH A 585      -6.942  52.648  12.818  1.00 36.78           O  
ANISOU 2768  O   HOH A 585     5297   4140   4538     65   1310   -188       O  
HETATM 2769  O   HOH A 586       2.286  25.215  26.233  1.00 28.93           O  
ANISOU 2769  O   HOH A 586     5917   2945   2128   -397   1601     20       O  
HETATM 2770  O   HOH A 587       3.660  31.191  29.353  1.00 34.92           O  
ANISOU 2770  O   HOH A 587     5740   4408   3117    868    216    155       O  
HETATM 2771  O   HOH A 588     -18.706  24.323  12.304  1.00 36.10           O  
ANISOU 2771  O   HOH A 588     4681   4777   4259    677   -412  -1259       O  
HETATM 2772  O   HOH A 589      18.157  54.535  10.833  1.00 41.81           O  
ANISOU 2772  O   HOH A 589     6148   3299   6437   -832    -30     39       O  
HETATM 2773  O   HOH A 590      12.349  31.347  26.014  1.00 38.57           O  
ANISOU 2773  O   HOH A 590     3481   6579   4594   1108  -1266    478       O  
HETATM 2774  O   HOH A 591      11.312  29.753  27.633  1.00 41.52           O  
ANISOU 2774  O   HOH A 591     4881   6312   4582    541   -891    910       O  
HETATM 2775  O   HOH A 592       8.950  28.768  28.025  1.00 34.61           O  
ANISOU 2775  O   HOH A 592     4004   5966   3180    414  -1511    223       O  
HETATM 2776  O   HOH A 593       6.539  25.487  26.040  1.00 40.05           O  
ANISOU 2776  O   HOH A 593     6018   4570   4628  -1278   1041   -366       O  
HETATM 2777  O   HOH A 594       2.314  54.928  19.430  1.00 36.00           O  
ANISOU 2777  O   HOH A 594     5427   3531   4720     84    287    562       O  
HETATM 2778  O   HOH A 595      11.160  37.540  27.801  1.00 31.29           O  
ANISOU 2778  O   HOH A 595     5297   4777   1812    642  -1215   -525       O  
HETATM 2779  O   HOH A 596      14.143  42.010  27.464  1.00 32.67           O  
ANISOU 2779  O   HOH A 596     3936   5367   3110    120   -497   -195       O  
HETATM 2780  O   HOH A 597      -4.145  44.265  32.867  1.00 31.68           O  
ANISOU 2780  O   HOH A 597     5025   5843   1166   -555    992   -634       O  
HETATM 2781  O   HOH A 598      -8.102  40.209   2.590  1.00 39.69           O  
ANISOU 2781  O   HOH A 598     5510   5791   3779   -503  -1453     82       O  
HETATM 2782  O   HOH A 599      -5.840  40.700   0.568  1.00 40.09           O  
ANISOU 2782  O   HOH A 599     5291   5133   4809   -299   -697    287       O  
HETATM 2783  O   HOH A 600       0.689  30.844   0.992  1.00 35.91           O  
ANISOU 2783  O   HOH A 600     3827   7804   2013    847   -280  -1115       O  
HETATM 2784  O   HOH A 601     -11.066  45.384  27.668  1.00 30.72           O  
ANISOU 2784  O   HOH A 601     4574   4142   2956     27    661    209       O  
HETATM 2785  O   HOH A 602      16.050  43.310  27.794  1.00 39.42           O  
ANISOU 2785  O   HOH A 602     5811   6234   2931   -206   -768   -972       O  
HETATM 2786  O   HOH A 603       8.861  32.253   0.784  1.00 17.75           O  
ANISOU 2786  O   HOH A 603     3477   2181   1085    203    203     28       O  
HETATM 2787  O   HOH B 401      18.062  29.301   3.002  1.00 11.28           O  
ANISOU 2787  O   HOH B 401     1522   1649   1115     65    226   -140       O  
HETATM 2788  O   HOH B 402      15.490  19.324   1.274  1.00  9.60           O  
ANISOU 2788  O   HOH B 402     1383   1460    803    -49    -14     25       O  
HETATM 2789  O   HOH B 403      11.245  14.298  -0.484  1.00 12.99           O  
ANISOU 2789  O   HOH B 403     1850   2069   1015   -140   -190   -278       O  
HETATM 2790  O   HOH B 404       7.509  32.090  21.053  1.00  9.74           O  
ANISOU 2790  O   HOH B 404     1441   1582    675    -37   -149   -210       O  
HETATM 2791  O   HOH B 405      26.206  17.778  -2.189  1.00 10.39           O  
ANISOU 2791  O   HOH B 405     1371   1901    674     91    384    -16       O  
HETATM 2792  O   HOH B 406      22.423  18.812  11.949  1.00 11.01           O  
ANISOU 2792  O   HOH B 406     1187   1971   1025      0     60   -173       O  
HETATM 2793  O   HOH B 407      17.466  21.348   1.150  1.00 10.63           O  
ANISOU 2793  O   HOH B 407     1549   1806    681   -158    253   -316       O  
HETATM 2794  O   HOH B 408      15.377  27.304  -3.948  1.00 14.85           O  
ANISOU 2794  O   HOH B 408     1803   2448   1392     90    193   -144       O  
HETATM 2795  O   HOH B 409       1.088  20.995   9.956  1.00 11.26           O  
ANISOU 2795  O   HOH B 409     1555   2081    642   -248    129    172       O  
HETATM 2796  O   HOH B 410      34.919  16.531  -2.176  1.00 12.70           O  
ANISOU 2796  O   HOH B 410     1363   2173   1289     24    264   -329       O  
HETATM 2797  O   HOH B 411      13.970  21.385  -1.261  1.00 12.40           O  
ANISOU 2797  O   HOH B 411     1881   1972    858    105    403   -126       O  
HETATM 2798  O   HOH B 412      29.303  19.316  10.019  1.00 16.20           O  
ANISOU 2798  O   HOH B 412     1561   2833   1760    516   -243     77       O  
HETATM 2799  O   HOH B 413      17.601  15.795  19.519  1.00 14.40           O  
ANISOU 2799  O   HOH B 413     1933   2894    642    212   -261    407       O  
HETATM 2800  O   HOH B 414      23.530  19.255  -8.883  1.00 11.01           O  
ANISOU 2800  O   HOH B 414     1498   2016    670    202    296   -276       O  
HETATM 2801  O  AHOH B 415      14.416  24.895  -4.246  0.66 14.18           O  
ANISOU 2801  O  AHOH B 415     1561   2514   1312    292    393   -384       O  
HETATM 2802  O   HOH B 416      18.433  29.106  -6.896  1.00 27.05           O  
ANISOU 2802  O   HOH B 416     3754   2873   3651    898    176    353       O  
HETATM 2803  O   HOH B 417      25.115  29.357   0.101  1.00 12.67           O  
ANISOU 2803  O   HOH B 417     2301   1703    810     96    527    135       O  
HETATM 2804  O   HOH B 418      13.405  16.202  -8.711  1.00 21.33           O  
ANISOU 2804  O   HOH B 418     3038   3703   1363   -717    135   -104       O  
HETATM 2805  O   HOH B 419       1.579  20.660  19.946  1.00 19.81           O  
ANISOU 2805  O   HOH B 419     2663   2820   2040    -70    165    -63       O  
HETATM 2806  O   HOH B 420      27.565  30.557  -0.234  1.00 25.90           O  
ANISOU 2806  O   HOH B 420     3541   4132   2165   -339   1078    -96       O  
HETATM 2807  O   HOH B 421      25.458  10.666   5.468  1.00 15.35           O  
ANISOU 2807  O   HOH B 421     1973   1784   2075    375    394    155       O  
HETATM 2808  O   HOH B 422       5.170   4.034  17.029  1.00 33.76           O  
ANISOU 2808  O   HOH B 422     3837   4493   4497  -1107   1273   -858       O  
HETATM 2809  O   HOH B 423       6.401  15.524   0.698  1.00 17.47           O  
ANISOU 2809  O   HOH B 423     2959   2323   1354   -281    311   -197       O  
HETATM 2810  O   HOH B 424      15.680  30.487  -0.368  1.00 12.14           O  
ANISOU 2810  O   HOH B 424     2022   1692    899   -151    223   -188       O  
HETATM 2811  O   HOH B 425      14.992  34.138   2.496  1.00 21.21           O  
ANISOU 2811  O   HOH B 425     3278   2532   2247   -123   -327    -36       O  
HETATM 2812  O   HOH B 426      24.854  17.432  -4.674  1.00 13.83           O  
ANISOU 2812  O   HOH B 426     1428   2395   1428     80    328   -171       O  
HETATM 2813  O   HOH B 427       3.405   7.849   5.764  1.00 22.06           O  
ANISOU 2813  O   HOH B 427     3087   2476   2819   -347   1234   -176       O  
HETATM 2814  O   HOH B 428      26.770  29.061  10.495  1.00 23.44           O  
ANISOU 2814  O   HOH B 428     4470   2533   1903    427    155   -167       O  
HETATM 2815  O   HOH B 429       3.005   8.269  15.303  1.00 23.87           O  
ANISOU 2815  O   HOH B 429     3376   2985   2706   -260    -89     15       O  
HETATM 2816  O   HOH B 430      -7.420   9.788  18.257  1.00 31.17           O  
ANISOU 2816  O   HOH B 430     2943   3615   5285    366    107   1619       O  
HETATM 2817  O   HOH B 431      19.091   1.591   1.648  1.00 32.00           O  
ANISOU 2817  O   HOH B 431     4735   3281   4143    880   -725   -929       O  
HETATM 2818  O   HOH B 432      28.847  20.587  13.996  1.00 32.18           O  
ANISOU 2818  O   HOH B 432     2651   4806   4767   -685  -1397   1468       O  
HETATM 2819  O   HOH B 433      12.578   6.941  13.615  1.00 28.79           O  
ANISOU 2819  O   HOH B 433     5133   3391   2414   1478   1946    942       O  
HETATM 2820  O   HOH B 434      -5.515  16.443  17.993  1.00 30.39           O  
ANISOU 2820  O   HOH B 434     2785   5751   3010    651    722   2080       O  
HETATM 2821  O   HOH B 435       6.715   8.392  20.102  1.00 25.00           O  
ANISOU 2821  O   HOH B 435     4590   2473   2434   -289   1604    859       O  
HETATM 2822  O   HOH B 436      21.277  25.059  -6.318  1.00 12.72           O  
ANISOU 2822  O   HOH B 436     1711   2141    981    317    426    311       O  
HETATM 2823  O   HOH B 437      12.704  21.219  19.566  1.00 13.92           O  
ANISOU 2823  O   HOH B 437     2117   2106   1066    231   -359     -9       O  
HETATM 2824  O   HOH B 438       9.531  20.697  -2.053  1.00 19.27           O  
ANISOU 2824  O   HOH B 438     2641   2430   2248     53   -953   -463       O  
HETATM 2825  O   HOH B 439      28.523  28.450  -1.541  1.00 18.49           O  
ANISOU 2825  O   HOH B 439     2768   2493   1763   -568    218    449       O  
HETATM 2826  O   HOH B 440      15.698  41.172   4.839  1.00 23.06           O  
ANISOU 2826  O   HOH B 440     2953   2887   2920    301    187   -588       O  
HETATM 2827  O   HOH B 441      28.877  16.004  12.987  1.00 30.72           O  
ANISOU 2827  O   HOH B 441     2913   5306   3452   1082   -400   -380       O  
HETATM 2828  O   HOH B 442      -9.039  10.724  14.548  1.00 31.27           O  
ANISOU 2828  O   HOH B 442     3489   5270   3119   -728   -328   1981       O  
HETATM 2829  O   HOH B 443       8.374  15.273  20.745  1.00 16.39           O  
ANISOU 2829  O   HOH B 443     2107   2735   1383      8   -176    327       O  
HETATM 2830  O   HOH B 444      29.217  16.463  10.258  1.00 28.14           O  
ANISOU 2830  O   HOH B 444     4040   3742   2909    173   -157    701       O  
HETATM 2831  O   HOH B 445       0.305   9.224  15.581  1.00 12.76           O  
ANISOU 2831  O   HOH B 445     1925   2249    672   -117    -73    641       O  
HETATM 2832  O   HOH B 446      23.419   1.918   5.297  1.00 29.70           O  
ANISOU 2832  O   HOH B 446     4083   3476   3724   1085   -245   -449       O  
HETATM 2833  O   HOH B 447      28.692  24.866   4.646  1.00 14.68           O  
ANISOU 2833  O   HOH B 447     1652   1854   2071    -49    480   -190       O  
HETATM 2834  O   HOH B 448      26.272  10.116  -1.828  1.00 19.94           O  
ANISOU 2834  O   HOH B 448     2514   2780   2281   -287     63   -202       O  
HETATM 2835  O   HOH B 449      16.324  23.050  -0.876  1.00 12.51           O  
ANISOU 2835  O   HOH B 449     1793   1753   1207     84    509   -113       O  
HETATM 2836  O   HOH B 450       4.300  26.135  -1.179  1.00 17.99           O  
ANISOU 2836  O   HOH B 450     2904   2817   1113    356    -72   -470       O  
HETATM 2837  O   HOH B 451      19.248  12.968   1.234  1.00 12.14           O  
ANISOU 2837  O   HOH B 451     1679   1507   1426    163    -25     53       O  
HETATM 2838  O   HOH B 452       3.653  19.704  21.323  1.00 20.46           O  
ANISOU 2838  O   HOH B 452     3479   2568   1723   -768    389    -50       O  
HETATM 2839  O   HOH B 453      22.093  17.185  -4.989  1.00 13.74           O  
ANISOU 2839  O   HOH B 453     1645   2239   1337    -61    251   -187       O  
HETATM 2840  O   HOH B 454      14.799  22.818  18.676  1.00 13.51           O  
ANISOU 2840  O   HOH B 454     1959   2724    450    349    242    237       O  
HETATM 2841  O  AHOH B 455      11.880  24.444  -3.585  0.66 16.87           O  
ANISOU 2841  O  AHOH B 455     3247   2563    596   -275    568   -179       O  
HETATM 2842  O   HOH B 456      -0.389  18.713  20.231  1.00 22.11           O  
ANISOU 2842  O   HOH B 456     3280   3365   1756   -260    382    687       O  
HETATM 2843  O   HOH B 457     -10.298  13.163  14.200  1.00 29.00           O  
ANISOU 2843  O   HOH B 457     4185   3944   2887  -1109    336    883       O  
HETATM 2844  O   HOH B 458      -9.868  15.195  16.634  1.00 30.99           O  
ANISOU 2844  O   HOH B 458     3580   3686   4509   -638    258   1470       O  
HETATM 2845  O   HOH B 459      23.499   9.932  -2.009  1.00 25.06           O  
ANISOU 2845  O   HOH B 459     2750   3964   2807    162    480   -853       O  
HETATM 2846  O   HOH B 460      26.344  20.908  16.774  1.00 22.82           O  
ANISOU 2846  O   HOH B 460     2385   5128   1157    117   -608     21       O  
HETATM 2847  O   HOH B 461      21.706  26.575  -9.487  1.00 17.20           O  
ANISOU 2847  O   HOH B 461     2172   2787   1573    400    167    420       O  
HETATM 2848  O   HOH B 462       8.961  18.808  -3.907  1.00 24.40           O  
ANISOU 2848  O   HOH B 462     2840   3942   2488    134   -310  -1669       O  
HETATM 2849  O   HOH B 463      10.622   6.602   2.926  1.00 27.34           O  
ANISOU 2849  O   HOH B 463     3538   2930   3918    141   1614   -668       O  
HETATM 2850  O   HOH B 464       7.428   8.331   4.800  1.00 24.04           O  
ANISOU 2850  O   HOH B 464     2738   3679   2714    290    700    128       O  
HETATM 2851  O   HOH B 465      24.928  37.644   6.316  1.00 27.90           O  
ANISOU 2851  O   HOH B 465     3838   3357   3403   -132   1602   -801       O  
HETATM 2852  O   HOH B 466      24.853  29.690  17.123  1.00 27.94           O  
ANISOU 2852  O   HOH B 466     3016   5126   2471   -412   -513  -1095       O  
HETATM 2853  O   HOH B 467       8.646  15.393  -1.113  1.00 20.92           O  
ANISOU 2853  O   HOH B 467     2584   3860   1502    374    -37   -521       O  
HETATM 2854  O  AHOH B 468      12.049  21.744  -3.433  0.66 23.84           O  
ANISOU 2854  O  AHOH B 468     4224   2073   2759    -56   -233   -466       O  
HETATM 2855  O   HOH B 469      14.367  19.863  -5.952  1.00 16.60           O  
ANISOU 2855  O   HOH B 469     1942   2569   1796   -413    106    250       O  
HETATM 2856  O   HOH B 470      23.145   7.654  -0.937  1.00 28.80           O  
ANISOU 2856  O   HOH B 470     3499   3516   3928   -199    402   -904       O  
HETATM 2857  O   HOH B 471       9.252   9.017   2.883  1.00 19.10           O  
ANISOU 2857  O   HOH B 471     2408   2052   2795   -402    201   -187       O  
HETATM 2858  O   HOH B 472      18.429  42.917   2.187  1.00 29.90           O  
ANISOU 2858  O   HOH B 472     4476   3416   3468   -218    581    -76       O  
HETATM 2859  O   HOH B 473       6.374   9.687  12.013  1.00 15.17           O  
ANISOU 2859  O   HOH B 473     1986   2304   1472   -105     72     13       O  
HETATM 2860  O   HOH B 474      17.012  29.151  19.518  1.00 22.49           O  
ANISOU 2860  O   HOH B 474     3249   3473   1820   -275    340   -339       O  
HETATM 2861  O   HOH B 475      20.195  10.578  16.435  1.00 25.29           O  
ANISOU 2861  O   HOH B 475     3991   3691   1924   -835    380     -1       O  
HETATM 2862  O   HOH B 476      11.424  29.343  22.677  1.00 21.19           O  
ANISOU 2862  O   HOH B 476     2051   4450   1551     29     21   -569       O  
HETATM 2863  O   HOH B 477      -5.575   8.002  11.060  1.00 26.00           O  
ANISOU 2863  O   HOH B 477     3526   3283   3070   -940  -1345    911       O  
HETATM 2864  O   HOH B 478      27.984  13.940  -3.810  1.00 25.14           O  
ANISOU 2864  O   HOH B 478     2561   4332   2658    557    381   -860       O  
HETATM 2865  O   HOH B 479      14.681  27.733  20.543  1.00 25.34           O  
ANISOU 2865  O   HOH B 479     2866   5794    966    -58   -379    404       O  
HETATM 2866  O   HOH B 480      10.457  14.925  -5.020  1.00 21.65           O  
ANISOU 2866  O   HOH B 480     2724   3023   2476     -8    221    131       O  
HETATM 2867  O   HOH B 481      18.355  12.116  -5.888  1.00 22.64           O  
ANISOU 2867  O   HOH B 481     2672   3080   2848   -716   1554  -1609       O  
HETATM 2868  O   HOH B 482      19.633  34.356  -2.063  1.00 21.86           O  
ANISOU 2868  O   HOH B 482     4325   2534   1444   -972     -9    440       O  
HETATM 2869  O  BHOH B 483      26.663  29.489  -6.322  0.50 21.39           O  
ANISOU 2869  O  BHOH B 483     4223   2759   1144    953    808     77       O  
HETATM 2870  O  AHOH B 484      23.783  36.348  -1.666  0.50 14.60           O  
ANISOU 2870  O  AHOH B 484     2786   2018    744   -610    923    151       O  
HETATM 2871  O   HOH B 485       6.696  12.839   1.028  1.00 29.40           O  
ANISOU 2871  O   HOH B 485     3941   3433   3795   -116    953    375       O  
HETATM 2872  O   HOH B 486      29.189  14.030   9.324  1.00 28.70           O  
ANISOU 2872  O   HOH B 486     3170   4796   2937    168    -80    471       O  
HETATM 2873  O   HOH B 487      12.317  16.569  -6.145  1.00 19.29           O  
ANISOU 2873  O   HOH B 487     2227   3238   1862    102   -219   -539       O  
HETATM 2874  O   HOH B 488      31.408  13.696   7.386  1.00 21.78           O  
ANISOU 2874  O   HOH B 488     2643   3746   1884    379   -182    662       O  
HETATM 2875  O   HOH B 489      20.907  39.201  10.824  1.00 30.22           O  
ANISOU 2875  O   HOH B 489     3689   4207   3586   -613   1023  -1001       O  
HETATM 2876  O   HOH B 490      20.708   7.034  -0.049  1.00 27.37           O  
ANISOU 2876  O   HOH B 490     3678   3132   3589    139     54    524       O  
HETATM 2877  O   HOH B 491       5.700  20.965  23.238  1.00 31.54           O  
ANISOU 2877  O   HOH B 491     5144   3960   2880  -1458  -1057    874       O  
HETATM 2878  O   HOH B 492       4.864   6.002   7.022  1.00 31.93           O  
ANISOU 2878  O   HOH B 492     3847   4122   4163    -70    259    188       O  
HETATM 2879  O   HOH B 493      15.674  14.900  21.103  1.00 28.17           O  
ANISOU 2879  O   HOH B 493     3793   6056    853     -6   -444    311       O  
HETATM 2880  O   HOH B 494      12.128   7.045  20.055  1.00 29.26           O  
ANISOU 2880  O   HOH B 494     4883   3250   2983   -466   -727   1033       O  
HETATM 2881  O   HOH B 495      26.510  17.244  13.516  1.00 16.05           O  
ANISOU 2881  O   HOH B 495     1802   2747   1546    157   -491   -133       O  
HETATM 2882  O   HOH B 496      31.517   9.440  10.079  1.00 32.15           O  
ANISOU 2882  O   HOH B 496     2777   4499   4940    914     23   -166       O  
HETATM 2883  O   HOH B 497      33.994  10.519  -2.884  1.00 23.17           O  
ANISOU 2883  O   HOH B 497     3193   3376   2232    714   -121    -48       O  
HETATM 2884  O   HOH B 498      22.879  12.554  -1.604  1.00 21.16           O  
ANISOU 2884  O   HOH B 498     2440   3705   1893    -57    168   -599       O  
HETATM 2885  O   HOH B 499       8.556  16.296  -3.526  1.00 23.38           O  
ANISOU 2885  O   HOH B 499     3273   3789   1820    -68      2   -468       O  
HETATM 2886  O   HOH B 500      35.523  14.343  -0.666  1.00 15.76           O  
ANISOU 2886  O   HOH B 500     1846   2961   1179     76    359     79       O  
HETATM 2887  O   HOH B 501      30.387  26.094   6.421  1.00 31.43           O  
ANISOU 2887  O   HOH B 501     2968   4053   4918   -808   -999   -319       O  
HETATM 2888  O   HOH B 502      30.438  23.213   3.290  1.00 20.60           O  
ANISOU 2888  O   HOH B 502     1947   2621   3256   -124    505  -1092       O  
HETATM 2889  O   HOH B 503      27.233  11.760  -3.717  1.00 29.60           O  
ANISOU 2889  O   HOH B 503     3072   4486   3686    502   1413    210       O  
HETATM 2890  O   HOH B 504      11.415  13.412  -2.969  1.00 22.34           O  
ANISOU 2890  O   HOH B 504     2829   4140   1518    316    116   -501       O  
HETATM 2891  O   HOH B 505      16.289  30.929  -3.954  1.00 38.97           O  
ANISOU 2891  O   HOH B 505     6166   3633   5005    588  -1922     67       O  
HETATM 2892  O   HOH B 506      10.539  18.824  -6.103  1.00 27.61           O  
ANISOU 2892  O   HOH B 506     3657   4233   2599    783    737    609       O  
HETATM 2893  O   HOH B 507      12.288  34.283   3.027  1.00 21.32           O  
ANISOU 2893  O   HOH B 507     3191   2615   2291    173     51   -177       O  
HETATM 2894  O   HOH B 508       3.730  23.475  -2.798  1.00 29.04           O  
ANISOU 2894  O   HOH B 508     3185   6746   1102   -388     70   -877       O  
HETATM 2895  O   HOH B 509      21.157  30.945  -4.656  1.00 30.71           O  
ANISOU 2895  O   HOH B 509     6184   3523   1960  -1090    929    474       O  
HETATM 2896  O   HOH B 510      19.098  27.556  20.491  1.00 29.39           O  
ANISOU 2896  O   HOH B 510     3679   5659   1827     48    215   -314       O  
HETATM 2897  O   HOH B 511      11.891  36.460   4.473  1.00 34.86           O  
ANISOU 2897  O   HOH B 511     3724   3287   6234     67    897    -32       O  
HETATM 2898  O   HOH B 512      20.354   7.982  15.651  1.00 28.61           O  
ANISOU 2898  O   HOH B 512     4325   3351   3194   -205    -20    610       O  
HETATM 2899  O   HOH B 513       9.361  12.453   0.896  1.00 19.27           O  
ANISOU 2899  O   HOH B 513     2830   2846   1643   -230   -393    214       O  
HETATM 2900  O   HOH B 514       3.852  16.878  22.917  1.00 32.00           O  
ANISOU 2900  O   HOH B 514     6954   2966   2237   -823    774    259       O  
HETATM 2901  O   HOH B 515      19.762   3.767   7.617  1.00 23.75           O  
ANISOU 2901  O   HOH B 515     2900   3543   2580    365    195    659       O  
HETATM 2902  O   HOH B 516      33.222  23.083   0.635  1.00 31.42           O  
ANISOU 2902  O   HOH B 516     3949   3514   4474   -668    402   -560       O  
HETATM 2903  O   HOH B 517      25.318  14.698  -4.623  1.00 29.21           O  
ANISOU 2903  O   HOH B 517     3985   2930   4182    677     55   -658       O  
HETATM 2904  O   HOH B 518      20.412   7.340  -4.158  1.00 32.99           O  
ANISOU 2904  O   HOH B 518     4969   4889   2677   -540   1243     83       O  
HETATM 2905  O  AHOH B 519      23.642  39.133  -1.046  0.50 23.52           O  
ANISOU 2905  O  AHOH B 519     3639   1678   3616   -532   1070   -312       O  
HETATM 2906  O   HOH B 520      27.481  33.516  -1.450  1.00 38.92           O  
ANISOU 2906  O   HOH B 520     5014   7306   2467   -435   1354   -882       O  
HETATM 2907  O   HOH B 521      15.926  28.757  -6.119  1.00 25.35           O  
ANISOU 2907  O   HOH B 521     3186   4599   1847    607    860   1008       O  
HETATM 2908  O   HOH B 522       4.778  11.193   2.220  1.00 23.35           O  
ANISOU 2908  O   HOH B 522     3593   3366   1912    521    394     90       O  
HETATM 2909  O   HOH B 523      -7.701  17.006  16.810  1.00 28.84           O  
ANISOU 2909  O   HOH B 523     4491   4116   2349  -1334   -614   1351       O  
HETATM 2910  O   HOH B 524      35.926  18.994   1.362  1.00 27.12           O  
ANISOU 2910  O   HOH B 524     2332   5727   2246   -982    169   -687       O  
HETATM 2911  O   HOH B 525      19.935  15.013  -6.679  1.00 22.42           O  
ANISOU 2911  O   HOH B 525     3239   3304   1973    -34    500   -375       O  
HETATM 2912  O   HOH B 526      26.399  35.484  -0.938  1.00 27.36           O  
ANISOU 2912  O   HOH B 526     3780   4058   2554   -577   1057   -667       O  
HETATM 2913  O   HOH B 527      26.470  12.572  19.162  1.00 27.66           O  
ANISOU 2913  O   HOH B 527     3119   4598   2791    813   -794    923       O  
HETATM 2914  O   HOH B 528      13.314   7.427  -3.818  1.00 23.82           O  
ANISOU 2914  O   HOH B 528     3603   2856   2590   -613    -49   -339       O  
HETATM 2915  O   HOH B 529      10.415  34.435   1.147  1.00 27.17           O  
ANISOU 2915  O   HOH B 529     3968   2461   3891     43   -897    637       O  
HETATM 2916  O   HOH B 530       5.130   9.739   4.565  1.00 21.35           O  
ANISOU 2916  O   HOH B 530     2771   2668   2671   -207    777     94       O  
HETATM 2917  O   HOH B 531       1.636  16.148  21.347  1.00 30.90           O  
ANISOU 2917  O   HOH B 531     6962   2458   2319  -1067   1183     42       O  
HETATM 2918  O   HOH B 532      24.877  14.265  -2.055  1.00 24.03           O  
ANISOU 2918  O   HOH B 532     2593   3723   2813      2     95   -297       O  
HETATM 2919  O   HOH B 533       5.192   8.155  16.805  1.00 22.12           O  
ANISOU 2919  O   HOH B 533     2851   2493   3057   -412    200   -157       O  
HETATM 2920  O   HOH B 534      21.600  17.622  -7.819  1.00 17.10           O  
ANISOU 2920  O   HOH B 534     1883   2935   1678    -37    155     79       O  
HETATM 2921  O   HOH B 535      12.667  21.194  22.209  1.00 29.42           O  
ANISOU 2921  O   HOH B 535     4363   5390   1425     16    428    295       O  
HETATM 2922  O   HOH B 536      25.017  36.471  16.754  1.00 19.43           O  
ANISOU 2922  O   HOH B 536     1981   2917   2482   -347    135  -1007       O  
HETATM 2923  O   HOH B 537      20.735  10.835  -5.647  1.00 35.13           O  
ANISOU 2923  O   HOH B 537     4768   4980   3600    663   -615  -1297       O  
HETATM 2924  O   HOH B 538      17.886  21.168 -12.284  1.00 34.26           O  
ANISOU 2924  O   HOH B 538     4812   5329   2874    711   -602    486       O  
HETATM 2925  O   HOH B 539      14.813  20.436 -10.112  1.00 30.46           O  
ANISOU 2925  O   HOH B 539     2685   4914   3975    263   -287   1266       O  
HETATM 2926  O   HOH B 540      13.026  18.544  -9.955  1.00 36.81           O  
ANISOU 2926  O   HOH B 540     4286   5199   4501   -508    100    394       O  
HETATM 2927  O   HOH B 541       9.985  13.193  -7.140  1.00 35.74           O  
ANISOU 2927  O   HOH B 541     5892   5373   2313  -1224  -1178   -107       O  
HETATM 2928  O   HOH B 542       6.168  15.537  -4.647  1.00 34.40           O  
ANISOU 2928  O   HOH B 542     3829   5362   3878    125   -305  -1290       O  
HETATM 2929  O   HOH B 543      10.984  10.458  -6.354  1.00 31.69           O  
ANISOU 2929  O   HOH B 543     3997   5001   3041   -854   -747   -270       O  
HETATM 2930  O   HOH B 544      13.391   9.790  -7.356  1.00 31.69           O  
ANISOU 2930  O   HOH B 544     4245   5225   2568   -633   -247  -1013       O  
HETATM 2931  O   HOH B 545      14.457  11.506  -9.348  1.00 32.10           O  
ANISOU 2931  O   HOH B 545     5439   4825   1930   -797   -610   -651       O  
HETATM 2932  O   HOH B 546      15.783   5.511  -5.391  1.00 30.41           O  
ANISOU 2932  O   HOH B 546     4984   3636   2931   -330   -375   -910       O  
HETATM 2933  O   HOH B 547      13.591   4.065  -1.887  1.00 32.76           O  
ANISOU 2933  O   HOH B 547     5749   2791   3906   -379    310  -1170       O  
HETATM 2934  O   HOH B 548      34.694  11.612  -0.577  1.00 18.86           O  
ANISOU 2934  O   HOH B 548     2402   2866   1898    487    -29    575       O  
HETATM 2935  O   HOH B 549      19.157  43.592   5.519  1.00 20.89           O  
ANISOU 2935  O   HOH B 549     2855   2195   2888   -272    881   -400       O  
HETATM 2936  O   HOH B 550      20.725  27.703  -6.985  1.00 19.02           O  
ANISOU 2936  O   HOH B 550     2815   2385   2024    509    341    506       O  
HETATM 2937  O   HOH B 551      16.389   0.916   8.929  1.00 31.46           O  
ANISOU 2937  O   HOH B 551     4965   2998   3990    469   1266    414       O  
HETATM 2938  O   HOH B 552      18.429   1.337   7.396  1.00 33.82           O  
ANISOU 2938  O   HOH B 552     4484   2945   5418    469    774    459       O  
HETATM 2939  O   HOH B 553      11.986   4.216   7.603  1.00 31.27           O  
ANISOU 2939  O   HOH B 553     4196   3328   4357   -741     22    587       O  
HETATM 2940  O   HOH B 554      10.603   5.018   9.563  1.00 40.96           O  
ANISOU 2940  O   HOH B 554     6645   3316   5600   1578      0    -87       O  
HETATM 2941  O   HOH B 555      10.210   5.823  12.008  1.00 36.31           O  
ANISOU 2941  O   HOH B 555     4053   4680   5063    261    663    402       O  
HETATM 2942  O   HOH B 556       7.184   3.435  19.523  1.00 21.23           O  
ANISOU 2942  O   HOH B 556     4432   2244   1389   -315    143    611       O  
HETATM 2943  O   HOH B 557      -3.202   4.639   7.512  1.00 37.60           O  
ANISOU 2943  O   HOH B 557     6892   4566   2828   -513   -487  -1057       O  
HETATM 2944  O   HOH B 558       4.473   6.174  18.881  1.00 24.46           O  
ANISOU 2944  O   HOH B 558     3141   3284   2866   -477    303    202       O  
HETATM 2945  O   HOH B 559      24.783  40.661   2.689  1.00 32.17           O  
ANISOU 2945  O   HOH B 559     3646   2888   5688  -1032    806   -736       O  
HETATM 2946  O   HOH B 560      33.454  24.393  -1.838  1.00 32.81           O  
ANISOU 2946  O   HOH B 560     3200   6948   2318   -576   -523   -524       O  
HETATM 2947  O   HOH B 561      35.611  21.586   0.870  1.00 34.05           O  
ANISOU 2947  O   HOH B 561     3383   4759   4795   -662   -176   -263       O  
HETATM 2948  O   HOH B 562      33.311  20.859   3.909  1.00 33.51           O  
ANISOU 2948  O   HOH B 562     3228   5171   4332    307   -834  -1241       O  
HETATM 2949  O   HOH B 563      10.778   4.867   5.044  1.00 33.96           O  
ANISOU 2949  O   HOH B 563     5259   3474   4169   -801   -448     56       O  
HETATM 2950  O   HOH B 564       7.734   6.409   6.268  1.00 30.07           O  
ANISOU 2950  O   HOH B 564     5461   2913   3048   -416     25   -104       O  
HETATM 2951  O   HOH B 565       8.244  26.424  -5.723  1.00 26.46           O  
ANISOU 2951  O   HOH B 565     4106   4243   1705    113   -239   -392       O  
HETATM 2952  O   HOH B 566      14.631   2.501  10.091  1.00 26.89           O  
ANISOU 2952  O   HOH B 566     4126   2117   3971     34    591    783       O  
HETATM 2953  O   HOH B 567      11.496  10.744  -3.820  1.00 20.90           O  
ANISOU 2953  O   HOH B 567     2533   3170   2237     48     22   -207       O  
HETATM 2954  O   HOH B 568       3.780  15.224  -0.018  1.00 26.16           O  
ANISOU 2954  O   HOH B 568     3476   4350   2112   -777    -18  -1336       O  
HETATM 2955  O   HOH B 569      23.499  34.635  18.133  1.00 21.19           O  
ANISOU 2955  O   HOH B 569     2802   3419   1830   -257    -33   -104       O  
HETATM 2956  O   HOH B 570      23.658   5.116   2.485  1.00 27.26           O  
ANISOU 2956  O   HOH B 570     2734   4493   3129    346    380  -1678       O  
HETATM 2957  O   HOH B 571      31.388  19.799   7.862  1.00 27.37           O  
ANISOU 2957  O   HOH B 571     2116   5024   3260    775   -524  -1275       O  
HETATM 2958  O   HOH B 572       3.122  13.383   2.095  1.00 20.13           O  
ANISOU 2958  O   HOH B 572     3810   2352   1484   -198    591   -582       O  
HETATM 2959  O   HOH B 573       7.787  29.846  -4.371  1.00 33.55           O  
ANISOU 2959  O   HOH B 573     6317   3776   2653   -328  -1332    974       O  
HETATM 2960  O   HOH B 574      28.870  28.817  13.571  1.00 37.46           O  
ANISOU 2960  O   HOH B 574     3173   5970   5087   -632   -816   -264       O  
HETATM 2961  O   HOH B 575      25.531   7.648  11.914  1.00 28.58           O  
ANISOU 2961  O   HOH B 575     4341   5150   1367    334   -394    908       O  
HETATM 2962  O  BHOH B 576      26.092   9.672  13.394  0.30 15.09           O  
ANISOU 2962  O  BHOH B 576     1982   2847    903   1095   -360    817       O  
HETATM 2963  O   HOH B 577      28.237   8.894  13.094  1.00 38.60           O  
ANISOU 2963  O   HOH B 577     5416   4790   4458   1268    447    837       O  
HETATM 2964  O   HOH B 578      24.907   9.246  15.670  1.00 33.69           O  
ANISOU 2964  O   HOH B 578     4793   4307   3700    773    198    898       O  
HETATM 2965  O   HOH B 579      26.608   9.904  17.746  1.00 35.12           O  
ANISOU 2965  O   HOH B 579     4269   5128   3947    879    119   1100       O  
HETATM 2966  O   HOH B 580      23.030   7.356  15.742  1.00 40.37           O  
ANISOU 2966  O   HOH B 580     4706   5974   4657   -254    276   1346       O  
HETATM 2967  O   HOH B 581      23.832   5.897  13.378  1.00 34.69           O  
ANISOU 2967  O   HOH B 581     4661   4869   3648    461   -445    970       O  
HETATM 2968  O   HOH B 582      21.752   4.225  12.433  1.00 39.35           O  
ANISOU 2968  O   HOH B 582     4783   5914   4253    928   -132   1133       O  
HETATM 2969  O  AHOH B 583      29.566  14.627  16.160  0.70 37.91           O  
ANISOU 2969  O  AHOH B 583     3533   5565   5306    -72    720    350       O  
HETATM 2970  O   HOH B 584      24.793  42.866   6.725  1.00 39.24           O  
ANISOU 2970  O   HOH B 584     4437   4186   6284   -593    508   -476       O  
HETATM 2971  O   HOH B 585      27.462   2.981   6.966  1.00 33.68           O  
ANISOU 2971  O   HOH B 585     4562   4047   4186    477    398   1701       O  
HETATM 2972  O   HOH B 586      25.585   1.367   7.033  1.00 33.81           O  
ANISOU 2972  O   HOH B 586     5153   4217   3476    848    -87    141       O  
HETATM 2973  O   HOH B 587      28.447   0.700   4.198  1.00 44.02           O  
ANISOU 2973  O   HOH B 587     6077   4696   5950   1089    296    503       O  
HETATM 2974  O   HOH B 588      34.726  12.187   3.439  1.00 31.67           O  
ANISOU 2974  O   HOH B 588     3525   4845   3663   1906   -428   -168       O  
HETATM 2975  O   HOH B 589      33.394  15.628   6.575  1.00 38.12           O  
ANISOU 2975  O   HOH B 589     4570   5383   4531    128  -2264    583       O  
HETATM 2976  O   HOH B 590      30.577  20.206  12.229  1.00 38.07           O  
ANISOU 2976  O   HOH B 590     5111   5190   4161    518  -1233   -692       O  
HETATM 2977  O   HOH B 591      28.065  24.747  15.360  1.00 35.04           O  
ANISOU 2977  O   HOH B 591     4917   5252   3145     49   -270   -338       O  
HETATM 2978  O   HOH B 592      28.624  22.324  16.148  1.00 38.93           O  
ANISOU 2978  O   HOH B 592     4550   5661   4578   -487   -604    -87       O  
HETATM 2979  O   HOH B 593      26.845  17.596  16.369  1.00 31.54           O  
ANISOU 2979  O   HOH B 593     2947   6134   2899  -1254   -275    626       O  
HETATM 2980  O   HOH B 594      23.716  35.225  20.411  1.00 41.66           O  
ANISOU 2980  O   HOH B 594     6990   6213   2626   -337   -135    122       O  
HETATM 2981  O   HOH B 595      27.632  36.146  17.473  1.00 31.16           O  
ANISOU 2981  O   HOH B 595     2698   5645   3495    629   -254   -679       O  
HETATM 2982  O   HOH B 596      34.378  36.513  12.609  1.00 39.74           O  
ANISOU 2982  O   HOH B 596     3206   6613   5278   -815    -64    180       O  
HETATM 2983  O   HOH B 597      15.283  24.691  20.867  1.00 28.32           O  
ANISOU 2983  O   HOH B 597     3706   4669   2384    120   -547   -653       O  
HETATM 2984  O   HOH B 598      19.031  22.232  20.638  1.00 30.43           O  
ANISOU 2984  O   HOH B 598     3351   5886   2324    478   -165   -378       O  
HETATM 2985  O   HOH B 599      21.688  23.337  19.684  1.00 37.03           O  
ANISOU 2985  O   HOH B 599     5101   5585   3382   -230  -1146    168       O  
HETATM 2986  O   HOH B 600      22.129  20.107  22.103  1.00 28.60           O  
ANISOU 2986  O   HOH B 600     3533   5157   2176   -676    -98   -243       O  
HETATM 2987  O   HOH B 601      21.265  26.476  18.987  1.00 33.24           O  
ANISOU 2987  O   HOH B 601     3611   6436   2581    826      1   -798       O  
HETATM 2988  O   HOH B 602       0.713  20.087  -0.634  1.00 34.83           O  
ANISOU 2988  O   HOH B 602     7865   3972   1396   -965  -1053    334       O  
HETATM 2989  O   HOH B 603      -2.347  11.864   5.289  1.00 28.19           O  
ANISOU 2989  O   HOH B 603     4221   3738   2750   -978    797   -280       O  
HETATM 2990  O   HOH B 604      -3.177   9.542   4.175  1.00 35.86           O  
ANISOU 2990  O   HOH B 604     5450   3800   4375  -1103   -339   -861       O  
HETATM 2991  O   HOH B 605      -2.420   7.225   5.353  1.00 35.27           O  
ANISOU 2991  O   HOH B 605     6168   4688   2542   -555   -133   -995       O  
HETATM 2992  O   HOH B 606      -5.251  20.141  20.260  1.00 37.17           O  
ANISOU 2992  O   HOH B 606     4934   5276   3912  -1112   1163   1121       O  
HETATM 2993  O   HOH B 607       6.994  16.031  23.023  1.00 31.28           O  
ANISOU 2993  O   HOH B 607     5314   5040   1529    -64    282   -429       O  
HETATM 2994  O   HOH B 608       6.665   6.754  14.836  1.00 33.74           O  
ANISOU 2994  O   HOH B 608     4328   5524   2967    -24     -5   -407       O  
HETATM 2995  O   HOH B 609      29.200  30.239  11.021  1.00 40.48           O  
ANISOU 2995  O   HOH B 609     3682   6350   5347   -206   -102    612       O  
HETATM 2996  O   HOH B 610      18.607  10.881  18.707  1.00 30.91           O  
ANISOU 2996  O   HOH B 610     3874   5117   2751    460    141   -109       O  
HETATM 2997  O   HOH B 611      24.812   6.269  -0.259  1.00 33.64           O  
ANISOU 2997  O   HOH B 611     5580   4754   2446   -444    651   -757       O  
HETATM 2998  O   HOH B 612      22.506  29.597  -6.214  0.80 24.36           O  
ANISOU 2998  O   HOH B 612     3291   3339   2626     -8   -551     34       O  
HETATM 2999  O  AHOH B 613      21.541  33.659  -3.914  0.50 26.77           O  
ANISOU 2999  O  AHOH B 613     4393   2630   3146    232   -144   -110       O  
HETATM 3000  O   HOH B 614      20.839  38.272  -3.753  1.00 34.63           O  
ANISOU 3000  O   HOH B 614     5828   5044   2283    207    395    864       O  
HETATM 3001  O   HOH B 615       9.805   5.358   0.567  1.00 34.83           O  
ANISOU 3001  O   HOH B 615     4505   5001   3727    192   -540  -1262       O  
HETATM 3002  O   HOH B 616      23.001  49.068   8.486  1.00 37.37           O  
ANISOU 3002  O   HOH B 616     5269   3859   5070   -709    787   -598       O  
HETATM 3003  O   HOH B 617      22.923  28.527 -10.944  1.00 34.97           O  
ANISOU 3003  O   HOH B 617     4946   4869   3470    342     95   1714       O  
HETATM 3004  O   HOH B 618      10.898  33.011  -2.607  1.00 43.20           O  
ANISOU 3004  O   HOH B 618     7223   4079   5110    235   -830    768       O  
HETATM 3005  O  AHOH B 619      12.135  21.168  -5.963  0.66 30.47           O  
ANISOU 3005  O  AHOH B 619     5172   3960   2445    220   1095  -1058       O  
HETATM 3006  O   HOH B 620      30.036  27.274   8.332  1.00 33.42           O  
ANISOU 3006  O   HOH B 620     4813   4625   3258   -133   -186   -358       O  
HETATM 3007  O  AHOH B 621       9.872  24.234  -5.767  0.66 30.52           O  
ANISOU 3007  O  AHOH B 621     3445   5166   2982    499   -782   -878       O  
HETATM 3008  O   HOH B 622       9.997  21.590  22.695  1.00 33.14           O  
ANISOU 3008  O   HOH B 622     4697   4701   3193   -331   -475    -59       O  
HETATM 3009  O   HOH B 623      10.005  16.360  24.193  1.00 36.43           O  
ANISOU 3009  O   HOH B 623     5229   4619   3992   -589    -12   1121       O  
HETATM 3010  O   HOH B 624      11.077  17.367  22.177  1.00 38.71           O  
ANISOU 3010  O   HOH B 624     4476   6048   4181   -602    252  -1581       O  
HETATM 3011  O   HOH B 625      11.690  15.278  21.299  1.00 24.08           O  
ANISOU 3011  O   HOH B 625     4315   3427   1407  -1205   -647    252       O  
CONECT 2538 2539                                                                
CONECT 2539 2538 2540                                                           
CONECT 2540 2539                                                                
CONECT 2541 2542 2543 2544 2545                                                 
CONECT 2542 2541                                                                
CONECT 2543 2541                                                                
CONECT 2544 2541                                                                
CONECT 2545 2541                                                                
CONECT 2546 2547                                                                
CONECT 2547 2546 2548                                                           
CONECT 2548 2547                                                                
CONECT 2549 2550                                                                
CONECT 2550 2549 2551                                                           
CONECT 2551 2550                                                                
CONECT 2552 2553                                                                
CONECT 2553 2552 2554                                                           
CONECT 2554 2553                                                                
CONECT 2555 2556                                                                
CONECT 2556 2555 2557                                                           
CONECT 2557 2556                                                                
CONECT 2558 2559 2560                                                           
CONECT 2559 2558                                                                
CONECT 2560 2558 2561 2562                                                      
CONECT 2561 2560                                                                
CONECT 2562 2560 2563                                                           
CONECT 2563 2562                                                                
CONECT 2564 2565                                                                
CONECT 2565 2564 2566                                                           
CONECT 2566 2565                                                                
CONECT 2567 2568 2569 2570 2571                                                 
CONECT 2568 2567                                                                
CONECT 2569 2567                                                                
CONECT 2570 2567                                                                
CONECT 2571 2567                                                                
CONECT 2572 2573                                                                
CONECT 2573 2572 2574                                                           
CONECT 2574 2573                                                                
CONECT 2575 2576                                                                
CONECT 2576 2575 2577                                                           
CONECT 2577 2576                                                                
CONECT 2578 2579 2580                                                           
CONECT 2579 2578                                                                
CONECT 2580 2578 2581 2582                                                      
CONECT 2581 2580                                                                
CONECT 2582 2580 2583                                                           
CONECT 2583 2582                                                                
MASTER      451    0   12   12   10    0   25    6 2956    2   46   28          
END