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HEADER    CHAPERONE/RNA                           05-MAR-12   4ALP              
TITLE     THE LIN28B COLD SHOCK DOMAIN IN COMPLEX WITH HEXAURIDINE              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LIN28 ISOFORM B;                                           
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: COLD SHOCK DOMAIN, RESIDUES 27-114;                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: HEXA URIDINE;                                              
COMPND   8 CHAIN: E;                                                            
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: XENOPUS TROPICALIS;                             
SOURCE   3 ORGANISM_TAXID: 8364;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 SYNTHETIC: YES;                                                      
SOURCE   8 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE   9 ORGANISM_TAXID: 32630                                                
KEYWDS    CHAPERONE-RNA COMPLEX, TRANSCRIPTION, LIN-28, RNA, LET-7, MIRNA       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.MAYR,A.SCHUETZ,N.DOEGE,U.HEINEMANN                                  
REVDAT   3   04-APR-18 4ALP    1       REMARK                                   
REVDAT   2   03-OCT-12 4ALP    1       REMARK                                   
REVDAT   1   05-SEP-12 4ALP    0                                                
JRNL        AUTH   F.MAYR,A.SCHUTZ,N.DOGE,U.HEINEMANN                           
JRNL        TITL   THE LIN28 COLD-SHOCK DOMAIN REMODELS PRE-LET-7 MICRORNA.     
JRNL        REF    NUCLEIC ACIDS RES.            V.  40  7492 2012              
JRNL        REFN                   ISSN 0305-1048                               
JRNL        PMID   22570413                                                     
JRNL        DOI    10.1093/NAR/GKS355                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.48 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.48                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.42                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 57423                          
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) : 0.170                           
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.188                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3023                            
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) : 1.48                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.52                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3863                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.75                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2020                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 205                          
REMARK   3   BIN FREE R VALUE                    : 0.2080                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2676                                    
REMARK   3   NUCLEIC ACID ATOMS       : 115                                     
REMARK   3   HETEROGEN ATOMS          : 12                                      
REMARK   3   SOLVENT ATOMS            : 656                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.92                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.56000                                             
REMARK   3    B22 (A**2) : 0.56000                                              
REMARK   3    B33 (A**2) : 0.01000                                              
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): 0.074         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.071         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.043         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.123         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.955                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3006 ; 0.013 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2196 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4069 ; 1.568 ; 1.941       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5318 ; 0.882 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   374 ; 5.944 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   134 ;33.998 ;22.687       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   512 ;11.712 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    25 ;16.425 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   409 ; 0.098 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3309 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   674 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  : 5                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    27        A   113                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.8561 -16.9259 -21.3675              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0386 T22:   0.0208                                     
REMARK   3      T33:   0.0099 T12:   0.0229                                     
REMARK   3      T13:  -0.0019 T23:  -0.0076                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7520 L22:   0.3736                                     
REMARK   3      L33:   0.5899 L12:   0.0431                                     
REMARK   3      L13:   0.3390 L23:  -0.3662                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0171 S12:   0.0418 S13:   0.0182                       
REMARK   3      S21:   0.0118 S22:  -0.0004 S23:   0.0213                       
REMARK   3      S31:   0.0332 S32:   0.0450 S33:  -0.0167                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    29        B   114                          
REMARK   3    ORIGIN FOR THE GROUP (A):  36.2539 -12.9261 -14.1948              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0336 T22:   0.0197                                     
REMARK   3      T33:   0.0133 T12:   0.0017                                     
REMARK   3      T13:  -0.0073 T23:  -0.0006                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3928 L22:   0.2545                                     
REMARK   3      L33:   0.3059 L12:  -0.1243                                     
REMARK   3      L13:  -0.0524 L23:   0.2724                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0058 S12:  -0.0375 S13:  -0.0407                       
REMARK   3      S21:  -0.0028 S22:  -0.0226 S23:   0.0098                       
REMARK   3      S31:  -0.0177 S32:  -0.0324 S33:   0.0168                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    29        C   114                          
REMARK   3    ORIGIN FOR THE GROUP (A):  37.0299 -16.2834 -46.3952              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0341 T22:   0.0048                                     
REMARK   3      T33:   0.0333 T12:  -0.0064                                     
REMARK   3      T13:  -0.0077 T23:   0.0079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4427 L22:   1.1878                                     
REMARK   3      L33:   0.3081 L12:  -0.1857                                     
REMARK   3      L13:   0.1034 L23:  -0.0841                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0070 S12:  -0.0226 S13:  -0.0159                       
REMARK   3      S21:  -0.0897 S22:   0.0618 S23:   0.0316                       
REMARK   3      S31:  -0.0274 S32:  -0.0141 S33:  -0.0548                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    30        D   113                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.3687 -14.0986 -51.7769              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0423 T22:   0.0414                                     
REMARK   3      T33:   0.0101 T12:  -0.0048                                     
REMARK   3      T13:   0.0129 T23:  -0.0095                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5440 L22:   0.3454                                     
REMARK   3      L33:   0.3762 L12:  -0.2124                                     
REMARK   3      L13:   0.0096 L23:   0.3166                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0312 S12:   0.1961 S13:   0.0201                       
REMARK   3      S21:   0.0085 S22:   0.0080 S23:  -0.0234                       
REMARK   3      S31:  -0.0342 S32:   0.0529 S33:  -0.0392                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     1        E     6                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.0887   1.0597 -34.7094              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0817 T22:   0.0503                                     
REMARK   3      T33:   0.0487 T12:  -0.0141                                     
REMARK   3      T13:  -0.0007 T23:   0.0091                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0429 L22:   0.1564                                     
REMARK   3      L33:   0.0953 L12:  -0.0803                                     
REMARK   3      L13:   0.0636 L23:  -0.1203                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0168 S12:   0.0019 S13:   0.0337                       
REMARK   3      S21:   0.0271 S22:  -0.0273 S23:  -0.0651                       
REMARK   3      S31:  -0.0097 S32:   0.0069 S33:   0.0440                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 4ALP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-MAR-12.                  
REMARK 100 THE DEPOSITION ID IS D_1290051559.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : BL14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91841                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 60327                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.480                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 32.400                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY                : 6.100                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 1.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       47.99100            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       30.58300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       47.99100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       30.58300            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DECAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11430 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 35590 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -69.3 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000      -47.99100            
REMARK 350   BIOMT2   1  0.000000 -1.000000  0.000000      -30.58300            
REMARK 350   BIOMT3   1  0.000000  0.000000 -1.000000      -63.21900            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       47.99100            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       30.58300            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -63.21900            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, E                               
REMARK 350   BIOMT1   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH E2010  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    25                                                      
REMARK 465     SER A    26                                                      
REMARK 465     GLU A   114                                                      
REMARK 465     GLY B    25                                                      
REMARK 465     SER B    26                                                      
REMARK 465     ASP B    27                                                      
REMARK 465     PRO B    28                                                      
REMARK 465     GLY C    25                                                      
REMARK 465     SER C    26                                                      
REMARK 465     ASP C    27                                                      
REMARK 465     PRO C    28                                                      
REMARK 465     GLY D    25                                                      
REMARK 465     SER D    26                                                      
REMARK 465     ASP D    27                                                      
REMARK 465     PRO D    28                                                      
REMARK 465     GLN D    29                                                      
REMARK 465     GLU D   114                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470       U E   3    C2   O2                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  2122     O    HOH A  2128              2.07            
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  64   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP B  64   CB  -  CG  -  OD2 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500      U E   3   O3' -  P   -  O5' ANGL. DEV. = -17.4 DEGREES          
REMARK 500      U E   3   O5' -  P   -  OP2 ANGL. DEV. =   8.8 DEGREES          
REMARK 500      U E   3   C3' -  O3' -  P   ANGL. DEV. =   7.5 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    ASN B 113       84.97   -163.93                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2051        DISTANCE =  6.17 ANGSTROMS                       
REMARK 525    HOH A2053        DISTANCE =  5.90 ANGSTROMS                       
REMARK 525    HOH A2056        DISTANCE =  7.19 ANGSTROMS                       
REMARK 525    HOH A2060        DISTANCE =  6.57 ANGSTROMS                       
REMARK 525    HOH A2112        DISTANCE =  6.82 ANGSTROMS                       
REMARK 525    HOH E2026        DISTANCE =  6.20 ANGSTROMS                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  5-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 700 THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  5-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 700 THE SHEETS PRESENTED AS "CA" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  5-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 700 THE SHEETS PRESENTED AS "DA" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  5-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1115                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 1114                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4A75   RELATED DB: PDB                                   
REMARK 900 THE LIN28 COLD SHOCK DOMAIN ACTS AS AN RNA CHAPERONE                 
REMARK 900 RELATED ID: 4A76   RELATED DB: PDB                                   
REMARK 900 THE LIN28 COLD SHOCK DOMAIN ACTS AS AN RNA CHAPERONE                 
DBREF  4ALP A   27   114  UNP    B4F6I0   B4F6I0_XENTR    27    114             
DBREF  4ALP B   27   114  UNP    B4F6I0   B4F6I0_XENTR    27    114             
DBREF  4ALP C   27   114  UNP    B4F6I0   B4F6I0_XENTR    27    114             
DBREF  4ALP D   27   114  UNP    B4F6I0   B4F6I0_XENTR    27    114             
DBREF  4ALP E    1     6  PDB    4ALP     4ALP             1      6             
SEQADV 4ALP GLY A   25  UNP  B4F6I0              EXPRESSION TAG                 
SEQADV 4ALP SER A   26  UNP  B4F6I0              EXPRESSION TAG                 
SEQADV 4ALP GLY B   25  UNP  B4F6I0              EXPRESSION TAG                 
SEQADV 4ALP SER B   26  UNP  B4F6I0              EXPRESSION TAG                 
SEQADV 4ALP GLY C   25  UNP  B4F6I0              EXPRESSION TAG                 
SEQADV 4ALP SER C   26  UNP  B4F6I0              EXPRESSION TAG                 
SEQADV 4ALP GLY D   25  UNP  B4F6I0              EXPRESSION TAG                 
SEQADV 4ALP SER D   26  UNP  B4F6I0              EXPRESSION TAG                 
SEQRES   1 A   90  GLY SER ASP PRO GLN VAL LEU ARG GLY SER GLY HIS CYS          
SEQRES   2 A   90  LYS TRP PHE ASN VAL ARG MET GLY PHE GLY PHE ILE SER          
SEQRES   3 A   90  MET THR SER ARG GLU GLY SER PRO LEU GLU ASN PRO VAL          
SEQRES   4 A   90  ASP VAL PHE VAL HIS GLN SER LYS LEU TYR MET GLU GLY          
SEQRES   5 A   90  PHE ARG SER LEU LYS GLU GLY GLU PRO VAL GLU PHE THR          
SEQRES   6 A   90  PHE LYS LYS SER SER LYS GLY PHE GLU SER LEU ARG VAL          
SEQRES   7 A   90  THR GLY PRO GLY GLY ASN PRO CYS LEU GLY ASN GLU              
SEQRES   1 B   90  GLY SER ASP PRO GLN VAL LEU ARG GLY SER GLY HIS CYS          
SEQRES   2 B   90  LYS TRP PHE ASN VAL ARG MET GLY PHE GLY PHE ILE SER          
SEQRES   3 B   90  MET THR SER ARG GLU GLY SER PRO LEU GLU ASN PRO VAL          
SEQRES   4 B   90  ASP VAL PHE VAL HIS GLN SER LYS LEU TYR MET GLU GLY          
SEQRES   5 B   90  PHE ARG SER LEU LYS GLU GLY GLU PRO VAL GLU PHE THR          
SEQRES   6 B   90  PHE LYS LYS SER SER LYS GLY PHE GLU SER LEU ARG VAL          
SEQRES   7 B   90  THR GLY PRO GLY GLY ASN PRO CYS LEU GLY ASN GLU              
SEQRES   1 C   90  GLY SER ASP PRO GLN VAL LEU ARG GLY SER GLY HIS CYS          
SEQRES   2 C   90  LYS TRP PHE ASN VAL ARG MET GLY PHE GLY PHE ILE SER          
SEQRES   3 C   90  MET THR SER ARG GLU GLY SER PRO LEU GLU ASN PRO VAL          
SEQRES   4 C   90  ASP VAL PHE VAL HIS GLN SER LYS LEU TYR MET GLU GLY          
SEQRES   5 C   90  PHE ARG SER LEU LYS GLU GLY GLU PRO VAL GLU PHE THR          
SEQRES   6 C   90  PHE LYS LYS SER SER LYS GLY PHE GLU SER LEU ARG VAL          
SEQRES   7 C   90  THR GLY PRO GLY GLY ASN PRO CYS LEU GLY ASN GLU              
SEQRES   1 D   90  GLY SER ASP PRO GLN VAL LEU ARG GLY SER GLY HIS CYS          
SEQRES   2 D   90  LYS TRP PHE ASN VAL ARG MET GLY PHE GLY PHE ILE SER          
SEQRES   3 D   90  MET THR SER ARG GLU GLY SER PRO LEU GLU ASN PRO VAL          
SEQRES   4 D   90  ASP VAL PHE VAL HIS GLN SER LYS LEU TYR MET GLU GLY          
SEQRES   5 D   90  PHE ARG SER LEU LYS GLU GLY GLU PRO VAL GLU PHE THR          
SEQRES   6 D   90  PHE LYS LYS SER SER LYS GLY PHE GLU SER LEU ARG VAL          
SEQRES   7 D   90  THR GLY PRO GLY GLY ASN PRO CYS LEU GLY ASN GLU              
SEQRES   1 E    6    U   U   U   U   U   U                                      
HET    GOL  B1115       6                                                       
HET    GOL  D1114       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   6  GOL    2(C3 H8 O3)                                                  
FORMUL   8  HOH   *656(H2 O)                                                    
HELIX    1   1 GLY A  104  ASN A  108  5                                   5    
HELIX    2   2 GLY B  104  ASN B  108  5                                   5    
HELIX    3   3 GLY C  104  ASN C  108  5                                   5    
HELIX    4   4 GLY D  104  ASN D  108  5                                   5    
SHEET    1  AA 6 LEU A  31  ASN A  41  0                                        
SHEET    2  AA 6 PRO A  85  SER A  93 -1  O  VAL A  86   N  GLY A  35           
SHEET    3  AA 6 GLY A  96  THR A 103 -1  O  GLY A  96   N  SER A  93           
SHEET    4  AA 6 SER A  57  HIS A  68  1  O  PHE A  66   N  SER A  99           
SHEET    5  AA 6 PHE A  46  ARG A  54 -1  O  GLY A  47   N  VAL A  67           
SHEET    6  AA 6 LEU A  31  ASN A  41 -1  O  SER A  34   N  SER A  53           
SHEET    1  BA 6 LEU B  31  ASN B  41  0                                        
SHEET    2  BA 6 PRO B  85  SER B  93 -1  O  VAL B  86   N  GLY B  35           
SHEET    3  BA 6 GLY B  96  THR B 103 -1  O  GLY B  96   N  SER B  93           
SHEET    4  BA 6 SER B  57  HIS B  68  1  O  PHE B  66   N  SER B  99           
SHEET    5  BA 6 PHE B  46  ARG B  54 -1  O  GLY B  47   N  VAL B  67           
SHEET    6  BA 6 LEU B  31  ASN B  41 -1  O  SER B  34   N  THR B  52           
SHEET    1  CA 6 LEU C  31  ASN C  41  0                                        
SHEET    2  CA 6 PRO C  85  SER C  93 -1  O  VAL C  86   N  GLY C  35           
SHEET    3  CA 6 GLY C  96  THR C 103 -1  O  GLY C  96   N  SER C  93           
SHEET    4  CA 6 SER C  57  HIS C  68  1  O  PHE C  66   N  SER C  99           
SHEET    5  CA 6 PHE C  46  ARG C  54 -1  O  GLY C  47   N  VAL C  67           
SHEET    6  CA 6 LEU C  31  ASN C  41 -1  O  SER C  34   N  THR C  52           
SHEET    1  DA 6 LEU D  31  ASN D  41  0                                        
SHEET    2  DA 6 PRO D  85  SER D  93 -1  O  VAL D  86   N  GLY D  35           
SHEET    3  DA 6 GLY D  96  THR D 103 -1  O  GLY D  96   N  SER D  93           
SHEET    4  DA 6 SER D  57  HIS D  68  1  O  PHE D  66   N  SER D  99           
SHEET    5  DA 6 PHE D  46  ARG D  54 -1  O  GLY D  47   N  VAL D  67           
SHEET    6  DA 6 LEU D  31  ASN D  41 -1  O  SER D  34   N  THR D  52           
SITE     1 AC1  7 ARG B  43  HOH B2027  HIS D  68  SER D  70                    
SITE     2 AC1  7 LYS D  71  HOH D2070  HOH E2002                               
SITE     1 AC2 12 PHE B  66  LYS B  95  GLU B  98  HOH B2119                    
SITE     2 AC2 12 HOH B2126  TRP D  39  ASN D  41  MET D  44                    
SITE     3 AC2 12 HOH D2019  HOH D2020  HOH D2126  HOH D2127                    
CRYST1   95.982   61.166   63.219  90.00  90.00  90.00 P 21 21 2    16          
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      0.010419  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016349  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015818        0.00000                         
ATOM      1  N   ASP A  27      23.012  -3.283  -7.085  1.00 48.30           N  
ANISOU    1  N   ASP A  27     6586   5834   5929   -134   -426   -183       N  
ATOM      2  CA  ASP A  27      21.864  -4.242  -7.072  1.00 37.74           C  
ANISOU    2  CA  ASP A  27     5242   4527   4572    -84   -358   -211       C  
ATOM      3  C   ASP A  27      22.390  -5.685  -7.093  1.00 26.21           C  
ANISOU    3  C   ASP A  27     3741   3131   3087    -83   -333   -171       C  
ATOM      4  O   ASP A  27      23.498  -5.928  -7.598  1.00 29.28           O  
ANISOU    4  O   ASP A  27     4093   3544   3487   -109   -357   -115       O  
ATOM      5  CB  ASP A  27      20.960  -4.019  -8.286  1.00 41.20           C  
ANISOU    5  CB  ASP A  27     5654   4948   5052    -52   -329   -206       C  
ATOM      6  CG  ASP A  27      20.499  -2.567  -8.435  1.00 41.95           C  
ANISOU    6  CG  ASP A  27     5781   4974   5183    -51   -358   -236       C  
ATOM      7  OD1 ASP A  27      20.378  -1.844  -7.409  1.00 39.21           O  
ANISOU    7  OD1 ASP A  27     5489   4589   4821    -55   -381   -287       O  
ATOM      8  OD2 ASP A  27      20.246  -2.160  -9.595  1.00 41.33           O  
ANISOU    8  OD2 ASP A  27     5673   4880   5150    -46   -358   -208       O  
ATOM      9  N   PRO A  28      21.613  -6.642  -6.552  1.00 25.20           N  
ANISOU    9  N   PRO A  28     3618   3031   2926    -54   -288   -196       N  
ATOM     10  CA  PRO A  28      21.982  -8.050  -6.743  1.00 22.92           C  
ANISOU   10  CA  PRO A  28     3289   2793   2624    -47   -266   -157       C  
ATOM     11  C   PRO A  28      22.043  -8.403  -8.222  1.00 19.56           C  
ANISOU   11  C   PRO A  28     2815   2378   2235    -32   -250   -118       C  
ATOM     12  O   PRO A  28      21.358  -7.815  -9.055  1.00 17.48           O  
ANISOU   12  O   PRO A  28     2549   2091   2002    -15   -239   -127       O  
ATOM     13  CB  PRO A  28      20.826  -8.824  -6.093  1.00 26.26           C  
ANISOU   13  CB  PRO A  28     3726   3233   3017    -16   -221   -191       C  
ATOM     14  CG  PRO A  28      20.159  -7.830  -5.176  1.00 28.64           C  
ANISOU   14  CG  PRO A  28     4078   3504   3298    -12   -225   -249       C  
ATOM     15  CD  PRO A  28      20.343  -6.496  -5.814  1.00 31.34           C  
ANISOU   15  CD  PRO A  28     4432   3795   3680    -22   -257   -256       C  
ATOM     16  N   GLN A  29      22.837  -9.407  -8.547  1.00 13.73           N  
ANISOU   16  N   GLN A  29     2040   1681   1495    -33   -247    -75       N  
ATOM     17  CA  GLN A  29      22.867  -9.873  -9.910  1.00 12.64           C  
ANISOU   17  CA  GLN A  29     1860   1561   1382    -12   -228    -45       C  
ATOM     18  C   GLN A  29      21.519 -10.448 -10.288  1.00 12.12           C  
ANISOU   18  C   GLN A  29     1796   1490   1318     25   -185    -73       C  
ATOM     19  O   GLN A  29      20.821 -11.021  -9.475  1.00 13.53           O  
ANISOU   19  O   GLN A  29     1994   1671   1474     37   -165    -99       O  
ATOM     20  CB  GLN A  29      23.949 -10.930 -10.044  1.00 12.21           C  
ANISOU   20  CB  GLN A  29     1768   1549   1320    -12   -231     -2       C  
ATOM     21  CG  GLN A  29      25.317 -10.331  -9.780  1.00 12.63           C  
ANISOU   21  CG  GLN A  29     1810   1612   1374    -52   -276     35       C  
ATOM     22  CD  GLN A  29      26.442 -11.349  -9.744  1.00 12.99           C  
ANISOU   22  CD  GLN A  29     1818   1704   1412    -52   -280     81       C  
ATOM     23  OE1 GLN A  29      26.247 -12.513 -10.071  1.00 14.59           O  
ANISOU   23  OE1 GLN A  29     2002   1927   1613    -18   -249     82       O  
ATOM     24  NE2 GLN A  29      27.670 -10.878  -9.396  1.00 13.08           N  
ANISOU   24  NE2 GLN A  29     1816   1729   1423    -91   -321    121       N  
ATOM     25  N   VAL A  30      21.202 -10.353 -11.567  1.00 10.61           N  
ANISOU   25  N   VAL A  30     1580   1299   1152     42   -171    -60       N  
ATOM     26  CA  VAL A  30      19.930 -10.854 -12.083  1.00 11.25           C  
ANISOU   26  CA  VAL A  30     1660   1375   1239     74   -135    -80       C  
ATOM     27  C   VAL A  30      19.927 -12.372 -11.967  1.00 10.60           C  
ANISOU   27  C   VAL A  30     1566   1321   1140     92   -116    -73       C  
ATOM     28  O   VAL A  30      20.953 -13.037 -12.094  1.00 12.35           O  
ANISOU   28  O   VAL A  30     1766   1569   1357     90   -126    -45       O  
ATOM     29  CB  VAL A  30      19.646 -10.443 -13.535  1.00 12.27           C  
ANISOU   29  CB  VAL A  30     1763   1501   1395     84   -130    -64       C  
ATOM     30  CG1 VAL A  30      19.483  -8.930 -13.662  1.00 13.65           C  
ANISOU   30  CG1 VAL A  30     1950   1640   1595     67   -151    -69       C  
ATOM     31  CG2 VAL A  30      20.708 -11.029 -14.484  1.00 13.27           C  
ANISOU   31  CG2 VAL A  30     1851   1668   1523     86   -134    -23       C  
ATOM     32  N   LEU A  31      18.742 -12.917 -11.749  1.00  9.11           N  
ANISOU   32  N   LEU A  31     1389   1125    946    111    -91    -95       N  
ATOM     33  CA  LEU A  31      18.519 -14.369 -11.683  1.00  8.61           C  
ANISOU   33  CA  LEU A  31     1318   1080    874    128    -77    -88       C  
ATOM     34  C   LEU A  31      18.590 -14.984 -13.090  1.00  8.82           C  
ANISOU   34  C   LEU A  31     1317   1115    917    148    -70    -72       C  
ATOM     35  O   LEU A  31      18.291 -14.322 -14.086  1.00  8.30           O  
ANISOU   35  O   LEU A  31     1242   1043    867    153    -66    -72       O  
ATOM     36  CB  LEU A  31      17.142 -14.671 -11.091  1.00 11.12           C  
ANISOU   36  CB  LEU A  31     1651   1389   1182    138    -55   -110       C  
ATOM     37  CG  LEU A  31      16.945 -14.204  -9.638  1.00 13.42           C  
ANISOU   37  CG  LEU A  31     1970   1681   1447    124    -56   -130       C  
ATOM     38  CD1 LEU A  31      15.458 -14.290  -9.292  1.00 16.47           C  
ANISOU   38  CD1 LEU A  31     2364   2065   1826    139    -29   -148       C  
ATOM     39  CD2 LEU A  31      17.810 -14.957  -8.649  1.00 17.90           C  
ANISOU   39  CD2 LEU A  31     2540   2271   1991    107    -72   -115       C  
ATOM     40  N   ARG A  32      19.005 -16.234 -13.178  1.00  8.57           N  
ANISOU   40  N   ARG A  32     1275   1099    881    162    -71    -60       N  
ATOM     41  CA  ARG A  32      19.093 -16.945 -14.431  1.00  8.26           C  
ANISOU   41  CA  ARG A  32     1216   1068    851    187    -65    -53       C  
ATOM     42  C   ARG A  32      18.430 -18.302 -14.296  1.00  8.46           C  
ANISOU   42  C   ARG A  32     1251   1085    878    203    -60    -60       C  
ATOM     43  O   ARG A  32      18.373 -18.913 -13.203  1.00  9.43           O  
ANISOU   43  O   ARG A  32     1384   1204    993    195    -66    -57       O  
ATOM     44  CB  ARG A  32      20.568 -17.097 -14.879  1.00 11.26           C  
ANISOU   44  CB  ARG A  32     1570   1476   1229    193    -76    -29       C  
ATOM     45  CG  ARG A  32      21.310 -18.111 -14.022  1.00 13.32           C  
ANISOU   45  CG  ARG A  32     1830   1746   1484    196    -87    -17       C  
ATOM     46  CD  ARG A  32      22.799 -18.287 -14.380  1.00 17.31           C  
ANISOU   46  CD  ARG A  32     2303   2282   1988    206    -97     10       C  
ATOM     47  NE  ARG A  32      23.488 -19.108 -13.391  1.00 18.10           N  
ANISOU   47  NE  ARG A  32     2403   2388   2086    204   -110     26       N  
ATOM     48  CZ  ARG A  32      23.817 -20.389 -13.544  1.00 14.38           C  
ANISOU   48  CZ  ARG A  32     1922   1919   1622    235   -111     30       C  
ATOM     49  NH1 ARG A  32      23.544 -21.036 -14.665  1.00 18.01           N  
ANISOU   49  NH1 ARG A  32     2377   2376   2089    272    -99     15       N  
ATOM     50  NH2 ARG A  32      24.432 -21.027 -12.555  1.00 18.66           N  
ANISOU   50  NH2 ARG A  32     2461   2464   2165    228   -127     50       N  
ATOM     51  N   GLY A  33      17.973 -18.820 -15.406  1.00  7.93           N  
ANISOU   51  N   GLY A  33     1178   1014    819    224    -54    -66       N  
ATOM     52  CA  GLY A  33      17.388 -20.146 -15.435  1.00  7.61           C  
ANISOU   52  CA  GLY A  33     1147    960    784    238    -58    -70       C  
ATOM     53  C   GLY A  33      17.329 -20.681 -16.828  1.00  7.65           C  
ANISOU   53  C   GLY A  33     1147    965    794    264    -57    -79       C  
ATOM     54  O   GLY A  33      17.820 -20.064 -17.757  1.00  8.17           O  
ANISOU   54  O   GLY A  33     1197   1050    855    272    -51    -78       O  
ATOM     55  N   SER A  34      16.762 -21.882 -16.959  1.00  7.91           N  
ANISOU   55  N   SER A  34     1192    977    834    276    -67    -85       N  
ATOM     56  CA  SER A  34      16.565 -22.528 -18.246  1.00  8.30           C  
ANISOU   56  CA  SER A  34     1246   1022    886    301    -72   -100       C  
ATOM     57  C   SER A  34      15.268 -23.292 -18.248  1.00  7.69           C  
ANISOU   57  C   SER A  34     1188    913    820    294    -84   -104       C  
ATOM     58  O   SER A  34      14.717 -23.589 -17.206  1.00  7.58           O  
ANISOU   58  O   SER A  34     1181    885    814    274    -90    -91       O  
ATOM     59  CB  SER A  34      17.738 -23.392 -18.663  1.00  9.91           C  
ANISOU   59  CB  SER A  34     1444   1234   1086    336    -80   -107       C  
ATOM     60  OG  SER A  34      17.910 -24.468 -17.790  1.00 12.33           O  
ANISOU   60  OG  SER A  34     1761   1518   1406    340    -98   -101       O  
ATOM     61  N   GLY A  35      14.803 -23.648 -19.428  1.00  7.46           N  
ANISOU   61  N   GLY A  35     1166    876    791    307    -90   -120       N  
ATOM     62  CA  GLY A  35      13.556 -24.370 -19.514  1.00  9.04           C  
ANISOU   62  CA  GLY A  35     1384   1046   1004    295   -108   -119       C  
ATOM     63  C   GLY A  35      13.131 -24.496 -20.965  1.00  8.28           C  
ANISOU   63  C   GLY A  35     1295    948    900    307   -114   -137       C  
ATOM     64  O   GLY A  35      13.976 -24.638 -21.841  1.00  8.92           O  
ANISOU   64  O   GLY A  35     1376   1046    967    337   -112   -157       O  
ATOM     65  N   HIS A  36      11.823 -24.443 -21.190  1.00  7.84           N  
ANISOU   65  N   HIS A  36     1246    878    854    284   -121   -128       N  
ATOM     66  CA  HIS A  36      11.290 -24.509 -22.540  1.00  8.05           C  
ANISOU   66  CA  HIS A  36     1280    905    872    288   -130   -141       C  
ATOM     67  C   HIS A  36      10.073 -23.643 -22.699  1.00  7.53           C  
ANISOU   67  C   HIS A  36     1201    844    813    259   -121   -120       C  
ATOM     68  O   HIS A  36       9.464 -23.273 -21.722  1.00  7.89           O  
ANISOU   68  O   HIS A  36     1237    886    873    239   -112    -97       O  
ATOM     69  CB  HIS A  36      10.935 -25.966 -22.897  1.00  8.73           C  
ANISOU   69  CB  HIS A  36     1397    952    966    296   -169   -156       C  
ATOM     70  CG  HIS A  36       9.902 -26.547 -22.032  1.00  9.06           C  
ANISOU   70  CG  HIS A  36     1446    962   1034    266   -191   -129       C  
ATOM     71  ND1 HIS A  36      10.173 -27.200 -20.865  1.00 10.94           N  
ANISOU   71  ND1 HIS A  36     1687   1183   1287    262   -202   -115       N  
ATOM     72  CD2 HIS A  36       8.515 -26.517 -22.154  1.00 10.58           C  
ANISOU   72  CD2 HIS A  36     1638   1144   1239    234   -204   -105       C  
ATOM     73  CE1 HIS A  36       9.005 -27.581 -20.306  1.00 10.79           C  
ANISOU   73  CE1 HIS A  36     1667   1144   1287    229   -221    -83       C  
ATOM     74  NE2 HIS A  36       8.003 -27.150 -21.067  1.00 12.02           N  
ANISOU   74  NE2 HIS A  36     1819   1305   1441    212   -221    -76       N  
ATOM     75  N   CYS A  37       9.804 -23.232 -23.919  1.00  7.89           N  
ANISOU   75  N   CYS A  37     1243    905    846    260   -120   -126       N  
ATOM     76  CA  CYS A  37       8.599 -22.442 -24.190  1.00  7.87           C  
ANISOU   76  CA  CYS A  37     1227    906    855    234   -115   -102       C  
ATOM     77  C   CYS A  37       7.346 -23.263 -23.893  1.00  7.52           C  
ANISOU   77  C   CYS A  37     1194    832    830    211   -140    -84       C  
ATOM     78  O   CYS A  37       7.136 -24.332 -24.480  1.00  9.07           O  
ANISOU   78  O   CYS A  37     1415   1006   1024    212   -173    -96       O  
ATOM     79  CB  CYS A  37       8.631 -21.976 -25.643  1.00  7.65           C  
ANISOU   79  CB  CYS A  37     1194    904    809    237   -115   -109       C  
ATOM     80  SG  CYS A  37       7.158 -21.094 -26.163  1.00  8.52           S  
ANISOU   80  SG  CYS A  37     1283   1017    934    206   -114    -75       S  
ATOM     81  N   LYS A  38       6.503 -22.739 -23.044  1.00  7.41           N  
ANISOU   81  N   LYS A  38     1163    819    834    192   -127    -55       N  
ATOM     82  CA  LYS A  38       5.151 -23.244 -22.813  1.00  8.54           C  
ANISOU   82  CA  LYS A  38     1304    945    996    165   -146    -24       C  
ATOM     83  C   LYS A  38       4.223 -22.900 -23.964  1.00  7.86           C  
ANISOU   83  C   LYS A  38     1209    863    912    150   -156    -10       C  
ATOM     84  O   LYS A  38       3.623 -23.785 -24.565  1.00  9.49           O  
ANISOU   84  O   LYS A  38     1432   1051   1121    134   -193     -5       O  
ATOM     85  CB  LYS A  38       4.602 -22.757 -21.464  1.00  7.90           C  
ANISOU   85  CB  LYS A  38     1200    873    926    156   -121      3       C  
ATOM     86  CG  LYS A  38       3.306 -23.390 -21.089  1.00  8.79           C  
ANISOU   86  CG  LYS A  38     1305    978   1057    130   -140     42       C  
ATOM     87  CD  LYS A  38       2.765 -22.781 -19.811  1.00 10.51           C  
ANISOU   87  CD  LYS A  38     1496   1217   1279    127   -108     68       C  
ATOM     88  CE  LYS A  38       1.543 -23.501 -19.356  1.00 13.79           C  
ANISOU   88  CE  LYS A  38     1896   1633   1709    101   -127    115       C  
ATOM     89  NZ  LYS A  38       0.920 -22.789 -18.199  1.00 18.32           N  
ANISOU   89  NZ  LYS A  38     2439   2240   2281    104    -89    139       N  
ATOM     90  N   TRP A  39       4.120 -21.619 -24.292  1.00  7.68           N  
ANISOU   90  N   TRP A  39     1163    864    890    152   -128     -3       N  
ATOM     91  CA  TRP A  39       3.384 -21.131 -25.437  1.00  7.62           C  
ANISOU   91  CA  TRP A  39     1143    867    885    137   -136     12       C  
ATOM     92  C   TRP A  39       3.921 -19.793 -25.825  1.00  6.91           C  
ANISOU   92  C   TRP A  39     1032    800    790    148   -108      8       C  
ATOM     93  O   TRP A  39       4.526 -19.081 -25.025  1.00  6.90           O  
ANISOU   93  O   TRP A  39     1023    804    793    162    -82      2       O  
ATOM     94  CB  TRP A  39       1.885 -21.035 -25.150  1.00  7.08           C  
ANISOU   94  CB  TRP A  39     1053    794    841    113   -140     56       C  
ATOM     95  CG  TRP A  39       1.481 -20.117 -24.071  1.00  7.61           C  
ANISOU   95  CG  TRP A  39     1092    871    927    118   -104     76       C  
ATOM     96  CD1 TRP A  39       1.375 -20.398 -22.723  1.00  7.19           C  
ANISOU   96  CD1 TRP A  39     1035    816    878    122    -91     83       C  
ATOM     97  CD2 TRP A  39       1.051 -18.737 -24.228  1.00  7.07           C  
ANISOU   97  CD2 TRP A  39      993    816    874    123    -77     93       C  
ATOM     98  NE1 TRP A  39       0.939 -19.268 -22.035  1.00  7.38           N  
ANISOU   98  NE1 TRP A  39     1032    855    915    133    -55     96       N  
ATOM     99  CE2 TRP A  39       0.734 -18.252 -22.893  1.00  6.74           C  
ANISOU   99  CE2 TRP A  39      936    779    844    135    -46    101       C  
ATOM    100  CE3 TRP A  39       0.875 -17.886 -25.316  1.00  6.36           C  
ANISOU  100  CE3 TRP A  39      888    735    790    119    -78    103       C  
ATOM    101  CZ2 TRP A  39       0.256 -16.956 -22.668  1.00  7.55           C  
ANISOU  101  CZ2 TRP A  39     1012    889    967    147    -17    113       C  
ATOM    102  CZ3 TRP A  39       0.434 -16.584 -25.079  1.00  7.37           C  
ANISOU  102  CZ3 TRP A  39      987    868    943    127    -51    120       C  
ATOM    103  CH2 TRP A  39       0.133 -16.141 -23.798  1.00  6.47           C  
ANISOU  103  CH2 TRP A  39      862    753    843    143    -22    122       C  
ATOM    104  N   PHE A  40       3.712 -19.438 -27.075  1.00  7.36           N  
ANISOU  104  N   PHE A  40     1084    873    840    140   -118     15       N  
ATOM    105  CA  PHE A  40       4.061 -18.111 -27.542  1.00  7.77           C  
ANISOU  105  CA  PHE A  40     1111    947    893    143    -98     23       C  
ATOM    106  C   PHE A  40       3.145 -17.709 -28.675  1.00  7.71           C  
ANISOU  106  C   PHE A  40     1085    951    891    122   -112     53       C  
ATOM    107  O   PHE A  40       3.075 -18.401 -29.678  1.00  9.69           O  
ANISOU  107  O   PHE A  40     1351   1210   1117    113   -138     45       O  
ATOM    108  CB  PHE A  40       5.533 -18.074 -27.981  1.00  6.74           C  
ANISOU  108  CB  PHE A  40      989    839    733    163    -93     -5       C  
ATOM    109  CG  PHE A  40       6.059 -16.683 -28.183  1.00  7.23           C  
ANISOU  109  CG  PHE A  40     1024    921    802    164    -74      8       C  
ATOM    110  CD1 PHE A  40       5.858 -16.001 -29.376  1.00  7.84           C  
ANISOU  110  CD1 PHE A  40     1080   1023    873    151    -81     30       C  
ATOM    111  CD2 PHE A  40       6.632 -16.016 -27.127  1.00  8.20           C  
ANISOU  111  CD2 PHE A  40     1141   1034    939    173    -54      5       C  
ATOM    112  CE1 PHE A  40       6.302 -14.673 -29.500  1.00  8.67           C  
ANISOU  112  CE1 PHE A  40     1158   1142    993    148    -69     51       C  
ATOM    113  CE2 PHE A  40       7.056 -14.687 -27.259  1.00  7.76           C  
ANISOU  113  CE2 PHE A  40     1062    988    896    170    -44     21       C  
ATOM    114  CZ  PHE A  40       6.886 -14.035 -28.424  1.00  7.83           C  
ANISOU  114  CZ  PHE A  40     1049   1019    905    157    -53     45       C  
ATOM    115  N   ASN A  41       2.388 -16.650 -28.494  1.00  7.48           N  
ANISOU  115  N   ASN A  41     1026    921    893    114    -98     86       N  
ATOM    116  CA  ASN A  41       1.420 -16.204 -29.479  1.00  7.69           C  
ANISOU  116  CA  ASN A  41     1030    957    931     91   -112    122       C  
ATOM    117  C   ASN A  41       1.985 -15.007 -30.219  1.00  7.83           C  
ANISOU  117  C   ASN A  41     1026    997    949     92   -104    133       C  
ATOM    118  O   ASN A  41       2.237 -13.970 -29.643  1.00  7.41           O  
ANISOU  118  O   ASN A  41      956    936    921    102    -83    139       O  
ATOM    119  CB  ASN A  41       0.086 -15.863 -28.802  1.00  8.44           C  
ANISOU  119  CB  ASN A  41     1101   1037   1067     84   -103    159       C  
ATOM    120  CG  ASN A  41      -0.960 -15.446 -29.771  1.00  9.06           C  
ANISOU  120  CG  ASN A  41     1153   1126   1162     60   -120    204       C  
ATOM    121  OD1 ASN A  41      -0.814 -14.483 -30.511  1.00  9.03           O  
ANISOU  121  OD1 ASN A  41     1129   1136   1166     56   -118    220       O  
ATOM    122  ND2 ASN A  41      -2.061 -16.197 -29.793  1.00 12.86           N  
ANISOU  122  ND2 ASN A  41     1632   1602   1652     39   -140    230       N  
ATOM    123  N   VAL A  42       2.251 -15.179 -31.536  1.00  7.41           N  
ANISOU  123  N   VAL A  42      975    974    865     79   -124    135       N  
ATOM    124  CA  VAL A  42       2.899 -14.110 -32.283  1.00  9.18           C  
ANISOU  124  CA  VAL A  42     1175   1228   1085     76   -119    151       C  
ATOM    125  C   VAL A  42       2.025 -12.935 -32.642  1.00 10.42           C  
ANISOU  125  C   VAL A  42     1294   1382   1282     58   -121    201       C  
ATOM    126  O   VAL A  42       2.518 -11.850 -32.900  1.00 10.53           O  
ANISOU  126  O   VAL A  42     1284   1406   1309     57   -116    220       O  
ATOM    127  CB  VAL A  42       3.621 -14.644 -33.543  1.00 11.42           C  
ANISOU  127  CB  VAL A  42     1470   1555   1313     73   -136    135       C  
ATOM    128  CG1 VAL A  42       4.647 -15.690 -33.147  1.00 11.84           C  
ANISOU  128  CG1 VAL A  42     1557   1609   1331    101   -130     84       C  
ATOM    129  CG2 VAL A  42       2.643 -15.167 -34.540  1.00 15.67           C  
ANISOU  129  CG2 VAL A  42     2012   2105   1836     48   -164    151       C  
ATOM    130  N   ARG A  43       0.712 -13.099 -32.645  1.00  8.87           N  
ANISOU  130  N   ARG A  43     1088   1171   1110     43   -131    229       N  
ATOM    131  CA  ARG A  43      -0.146 -11.948 -32.797  1.00  8.53           C  
ANISOU  131  CA  ARG A  43     1006   1120   1115     33   -129    278       C  
ATOM    132  C   ARG A  43      -0.080 -11.074 -31.545  1.00  8.63           C  
ANISOU  132  C   ARG A  43     1010   1099   1171     59   -101    272       C  
ATOM    133  O   ARG A  43       0.009  -9.861 -31.642  1.00 11.10           O  
ANISOU  133  O   ARG A  43     1297   1402   1515     61    -97    294       O  
ATOM    134  CB  ARG A  43      -1.591 -12.345 -33.115  1.00  9.96           C  
ANISOU  134  CB  ARG A  43     1174   1298   1313     11   -147    315       C  
ATOM    135  CG  ARG A  43      -2.512 -11.157 -33.278  1.00 10.68           C  
ANISOU  135  CG  ARG A  43     1219   1380   1456      4   -145    369       C  
ATOM    136  CD  ARG A  43      -3.906 -11.581 -33.802  1.00 11.38           C  
ANISOU  136  CD  ARG A  43     1289   1475   1558    -22   -168    415       C  
ATOM    137  NE  ARG A  43      -4.759 -10.405 -33.696  1.00 11.03           N  
ANISOU  137  NE  ARG A  43     1199   1417   1573    -17   -158    465       N  
ATOM    138  CZ  ARG A  43      -4.816  -9.434 -34.572  1.00 11.97           C  
ANISOU  138  CZ  ARG A  43     1288   1548   1713    -32   -171    504       C  
ATOM    139  NH1 ARG A  43      -4.183  -9.514 -35.746  1.00 12.21           N  
ANISOU  139  NH1 ARG A  43     1324   1613   1702    -59   -196    507       N  
ATOM    140  NH2 ARG A  43      -5.579  -8.359 -34.295  1.00 12.91           N  
ANISOU  140  NH2 ARG A  43     1366   1644   1893    -19   -160    545       N  
ATOM    141  N   MET A  44      -0.073 -11.706 -30.385  1.00  7.69           N  
ANISOU  141  N   MET A  44      913    960   1049     78    -84    240       N  
ATOM    142  CA  MET A  44       0.002 -11.003 -29.102  1.00  7.30           C  
ANISOU  142  CA  MET A  44      861    882   1030    105    -56    226       C  
ATOM    143  C   MET A  44       1.411 -10.454 -28.926  1.00  7.30           C  
ANISOU  143  C   MET A  44      874    881   1018    115    -51    199       C  
ATOM    144  O   MET A  44       1.601  -9.371 -28.356  1.00  8.94           O  
ANISOU  144  O   MET A  44     1073   1065   1257    129    -40    198       O  
ATOM    145  CB  MET A  44      -0.301 -11.950 -27.927  1.00  7.75           C  
ANISOU  145  CB  MET A  44      937    928   1077    119    -42    203       C  
ATOM    146  CG  MET A  44      -1.772 -12.366 -27.886  1.00  8.58           C  
ANISOU  146  CG  MET A  44     1022   1034   1201    110    -45    239       C  
ATOM    147  SD  MET A  44      -2.076 -13.501 -26.537  1.00  9.52           S  
ANISOU  147  SD  MET A  44     1160   1149   1307    120    -32    222       S  
ATOM    148  CE  MET A  44      -3.734 -14.096 -26.969  1.00 10.70           C  
ANISOU  148  CE  MET A  44     1281   1309   1475     94    -51    280       C  
ATOM    149  N   GLY A  45       2.409 -11.212 -29.371  1.00  7.25           N  
ANISOU  149  N   GLY A  45      888    899    968    110    -61    176       N  
ATOM    150  CA  GLY A  45       3.808 -10.854 -29.192  1.00  7.69           C  
ANISOU  150  CA  GLY A  45      951    961   1006    118    -57    154       C  
ATOM    151  C   GLY A  45       4.389 -11.278 -27.838  1.00  6.99           C  
ANISOU  151  C   GLY A  45      890    854    910    139    -39    115       C  
ATOM    152  O   GLY A  45       5.403 -10.699 -27.393  1.00  7.14           O  
ANISOU  152  O   GLY A  45      912    869    929    146    -35    102       O  
ATOM    153  N   PHE A  46       3.802 -12.288 -27.216  1.00  6.75           N  
ANISOU  153  N   PHE A  46      876    815    872    145    -34    101       N  
ATOM    154  CA  PHE A  46       4.271 -12.737 -25.937  1.00  6.45           C  
ANISOU  154  CA  PHE A  46      860    764    824    161    -20     70       C  
ATOM    155  C   PHE A  46       3.819 -14.174 -25.639  1.00  7.06           C  
ANISOU  155  C   PHE A  46      955    841    883    160    -25     61       C  
ATOM    156  O   PHE A  46       2.996 -14.730 -26.392  1.00  6.83           O  
ANISOU  156  O   PHE A  46      922    819    853    145    -41     79       O  
ATOM    157  CB  PHE A  46       3.927 -11.771 -24.804  1.00  6.82           C  
ANISOU  157  CB  PHE A  46      902    785    902    175      0     67       C  
ATOM    158  CG  PHE A  46       2.463 -11.439 -24.680  1.00  7.05           C  
ANISOU  158  CG  PHE A  46      911    804    962    178      9     92       C  
ATOM    159  CD1 PHE A  46       1.545 -12.347 -24.195  1.00  7.46           C  
ANISOU  159  CD1 PHE A  46      962    860   1009    179     14     98       C  
ATOM    160  CD2 PHE A  46       2.017 -10.169 -25.044  1.00  8.16           C  
ANISOU  160  CD2 PHE A  46     1027    930   1140    181     10    113       C  
ATOM    161  CE1 PHE A  46       0.204 -12.030 -24.087  1.00  8.03           C  
ANISOU  161  CE1 PHE A  46     1009    930   1111    183     24    128       C  
ATOM    162  CE2 PHE A  46       0.683  -9.845 -24.940  1.00  8.42           C  
ANISOU  162  CE2 PHE A  46     1038    956   1205    189     20    139       C  
ATOM    163  CZ  PHE A  46      -0.218 -10.776 -24.479  1.00  8.07           C  
ANISOU  163  CZ  PHE A  46      990    922   1151    190     29    147       C  
ATOM    164  N   GLY A  47       4.306 -14.715 -24.542  1.00  6.76           N  
ANISOU  164  N   GLY A  47      937    797    835    171    -16     37       N  
ATOM    165  CA  GLY A  47       3.987 -16.062 -24.090  1.00  7.12           C  
ANISOU  165  CA  GLY A  47      999    838    867    169    -25     31       C  
ATOM    166  C   GLY A  47       4.592 -16.320 -22.754  1.00  6.56           C  
ANISOU  166  C   GLY A  47      943    761    787    181    -12     10       C  
ATOM    167  O   GLY A  47       4.905 -15.407 -22.021  1.00  6.15           O  
ANISOU  167  O   GLY A  47      887    705    742    191      5      2       O  
ATOM    168  N   PHE A  48       4.710 -17.593 -22.423  1.00  6.11           N  
ANISOU  168  N   PHE A  48      904    701    716    179    -26      3       N  
ATOM    169  CA  PHE A  48       5.351 -18.051 -21.191  1.00  6.95           C  
ANISOU  169  CA  PHE A  48     1024    804    811    187    -19    -11       C  
ATOM    170  C   PHE A  48       6.359 -19.144 -21.436  1.00  6.59           C  
ANISOU  170  C   PHE A  48     1000    756    747    192    -40    -30       C  
ATOM    171  O   PHE A  48       6.182 -19.971 -22.335  1.00  7.04           O  
ANISOU  171  O   PHE A  48     1066    806    799    188    -63    -31       O  
ATOM    172  CB  PHE A  48       4.318 -18.538 -20.184  1.00  6.98           C  
ANISOU  172  CB  PHE A  48     1021    806    822    179    -14      8       C  
ATOM    173  CG  PHE A  48       3.661 -17.417 -19.443  1.00  7.00           C  
ANISOU  173  CG  PHE A  48     1006    817    836    187     15     16       C  
ATOM    174  CD1 PHE A  48       2.609 -16.672 -20.010  1.00  6.95           C  
ANISOU  174  CD1 PHE A  48      976    811    851    187     23     38       C  
ATOM    175  CD2 PHE A  48       4.136 -17.025 -18.206  1.00  7.41           C  
ANISOU  175  CD2 PHE A  48     1064    874    877    199     34      0       C  
ATOM    176  CE1 PHE A  48       2.055 -15.596 -19.342  1.00  7.76           C  
ANISOU  176  CE1 PHE A  48     1063    918    967    202     52     39       C  
ATOM    177  CE2 PHE A  48       3.561 -15.946 -17.562  1.00  7.99           C  
ANISOU  177  CE2 PHE A  48     1125    952    957    212     62     -1       C  
ATOM    178  CZ  PHE A  48       2.532 -15.228 -18.127  1.00  8.35           C  
ANISOU  178  CZ  PHE A  48     1148    996   1028    217     72     16       C  
ATOM    179  N   ILE A  49       7.412 -19.108 -20.643  1.00  6.19           N  
ANISOU  179  N   ILE A  49      957    708    686    202    -32    -46       N  
ATOM    180  CA  ILE A  49       8.400 -20.136 -20.506  1.00  6.26           C  
ANISOU  180  CA  ILE A  49      982    713    681    211    -47    -61       C  
ATOM    181  C   ILE A  49       8.143 -20.985 -19.272  1.00  7.02           C  
ANISOU  181  C   ILE A  49     1086    799    779    204    -53    -52       C  
ATOM    182  O   ILE A  49       7.820 -20.444 -18.236  1.00  7.74           O  
ANISOU  182  O   ILE A  49     1169    898    871    199    -35    -43       O  
ATOM    183  CB  ILE A  49       9.803 -19.511 -20.400  1.00  7.05           C  
ANISOU  183  CB  ILE A  49     1081    829    769    223    -37    -76       C  
ATOM    184  CG1 ILE A  49      10.130 -18.810 -21.727  1.00  6.92           C  
ANISOU  184  CG1 ILE A  49     1052    828    748    228    -35    -78       C  
ATOM    185  CG2 ILE A  49      10.852 -20.542 -19.950  1.00  7.27           C  
ANISOU  185  CG2 ILE A  49     1121    854    786    236    -49    -87       C  
ATOM    186  CD1 ILE A  49      11.314 -17.871 -21.672  1.00  8.50           C  
ANISOU  186  CD1 ILE A  49     1240   1046    941    232    -26    -80       C  
ATOM    187  N   SER A  50       8.257 -22.308 -19.386  1.00  6.51           N  
ANISOU  187  N   SER A  50     1038    719    717    205    -80    -53       N  
ATOM    188  CA  SER A  50       8.260 -23.194 -18.213  1.00  7.27           C  
ANISOU  188  CA  SER A  50     1140    806    815    197    -92    -40       C  
ATOM    189  C   SER A  50       9.727 -23.327 -17.780  1.00  7.39           C  
ANISOU  189  C   SER A  50     1161    825    819    214    -90    -57       C  
ATOM    190  O   SER A  50      10.542 -23.937 -18.458  1.00  8.53           O  
ANISOU  190  O   SER A  50     1318    961    962    232   -106    -75       O  
ATOM    191  CB  SER A  50       7.660 -24.539 -18.523  1.00  8.03           C  
ANISOU  191  CB  SER A  50     1249    874    924    187   -129    -28       C  
ATOM    192  OG  SER A  50       7.696 -25.375 -17.367  1.00 10.45           O  
ANISOU  192  OG  SER A  50     1558   1173   1236    176   -143     -7       O  
ATOM    193  N   MET A  51      10.061 -22.713 -16.647  1.00  7.44           N  
ANISOU  193  N   MET A  51     1160    849    816    208    -72    -52       N  
ATOM    194  CA  MET A  51      11.417 -22.793 -16.089  1.00  7.08           C  
ANISOU  194  CA  MET A  51     1118    811    761    218    -73    -61       C  
ATOM    195  C   MET A  51      11.569 -24.121 -15.352  1.00  8.52           C  
ANISOU  195  C   MET A  51     1308    979    950    213    -98    -45       C  
ATOM    196  O   MET A  51      10.871 -24.370 -14.370  1.00  8.24           O  
ANISOU  196  O   MET A  51     1269    948    914    194    -99    -22       O  
ATOM    197  CB  MET A  51      11.672 -21.645 -15.115  1.00  7.16           C  
ANISOU  197  CB  MET A  51     1120    841    756    209    -49    -61       C  
ATOM    198  CG  MET A  51      13.040 -21.714 -14.442  1.00  7.26           C  
ANISOU  198  CG  MET A  51     1134    864    758    212    -55    -63       C  
ATOM    199  SD  MET A  51      13.536 -20.195 -13.607  1.00  8.26           S  
ANISOU  199  SD  MET A  51     1260   1010    868    201    -36    -72       S  
ATOM    200  CE  MET A  51      12.125 -19.814 -12.551  1.00  9.94           C  
ANISOU  200  CE  MET A  51     1475   1229   1070    188    -17    -68       C  
ATOM    201  N   THR A  52      12.541 -24.923 -15.778  1.00  8.31           N  
ANISOU  201  N   THR A  52     1290    939    928    233   -117    -56       N  
ATOM    202  CA  THR A  52      12.814 -26.257 -15.186  1.00  8.39           C  
ANISOU  202  CA  THR A  52     1308    927    952    233   -147    -42       C  
ATOM    203  C   THR A  52      14.179 -26.327 -14.457  1.00  8.80           C  
ANISOU  203  C   THR A  52     1353    991    997    242   -147    -39       C  
ATOM    204  O   THR A  52      14.455 -27.295 -13.756  1.00  8.94           O  
ANISOU  204  O   THR A  52     1373    995   1027    238   -171    -20       O  
ATOM    205  CB  THR A  52      12.680 -27.324 -16.283  1.00  9.40           C  
ANISOU  205  CB  THR A  52     1454   1019   1098    252   -177    -57       C  
ATOM    206  OG1 THR A  52      13.571 -27.040 -17.351  1.00 10.18           O  
ANISOU  206  OG1 THR A  52     1553   1126   1186    284   -166    -88       O  
ATOM    207  CG2 THR A  52      11.230 -27.448 -16.781  1.00 10.91           C  
ANISOU  207  CG2 THR A  52     1651   1195   1298    232   -187    -48       C  
ATOM    208  N   SER A  53      14.968 -25.262 -14.564  1.00  8.63           N  
ANISOU  208  N   SER A  53     1322    997    960    249   -123    -50       N  
ATOM    209  CA ASER A  53      16.224 -25.133 -13.845  0.50  8.65           C  
ANISOU  209  CA ASER A  53     1314   1017    953    251   -123    -42       C  
ATOM    210  CA BSER A  53      16.236 -25.136 -13.859  0.50  8.83           C  
ANISOU  210  CA BSER A  53     1337   1040    977    252   -123    -42       C  
ATOM    211  C   SER A  53      16.410 -23.680 -13.479  1.00  8.91           C  
ANISOU  211  C   SER A  53     1338   1078    966    235    -99    -45       C  
ATOM    212  O   SER A  53      16.031 -22.780 -14.251  1.00  8.75           O  
ANISOU  212  O   SER A  53     1316   1063    942    237    -83    -59       O  
ATOM    213  CB ASER A  53      17.393 -25.589 -14.689  0.50 10.07           C  
ANISOU  213  CB ASER A  53     1488   1196   1139    287   -130    -54       C  
ATOM    214  CB BSER A  53      17.391 -25.575 -14.743  0.50 10.76           C  
ANISOU  214  CB BSER A  53     1576   1284   1227    288   -129    -55       C  
ATOM    215  OG ASER A  53      18.612 -25.339 -13.996  0.50 10.49           O  
ANISOU  215  OG ASER A  53     1526   1272   1185    286   -129    -39       O  
ATOM    216  OG BSER A  53      17.484 -26.986 -14.827  0.50 14.69           O  
ANISOU  216  OG BSER A  53     2083   1750   1745    307   -157    -54       O  
ATOM    217  N   ARG A  54      16.966 -23.410 -12.302  1.00  9.50           N  
ANISOU  217  N   ARG A  54     1411   1170   1029    217   -101    -31       N  
ATOM    218  CA  ARG A  54      17.139 -22.059 -11.843  1.00  8.71           C  
ANISOU  218  CA  ARG A  54     1310   1089    910    200    -85    -37       C  
ATOM    219  C   ARG A  54      18.482 -21.966 -11.157  1.00 10.08           C  
ANISOU  219  C   ARG A  54     1475   1281   1074    192    -97    -23       C  
ATOM    220  O   ARG A  54      18.793 -22.790 -10.301  1.00 10.46           O  
ANISOU  220  O   ARG A  54     1522   1330   1121    185   -112     -3       O  
ATOM    221  CB  ARG A  54      16.026 -21.697 -10.867  1.00 10.46           C  
ANISOU  221  CB  ARG A  54     1541   1315   1116    178    -74    -36       C  
ATOM    222  CG  ARG A  54      16.178 -20.299 -10.250  1.00  9.10           C  
ANISOU  222  CG  ARG A  54     1376   1158    924    163    -61    -50       C  
ATOM    223  CD  ARG A  54      15.018 -19.986  -9.349  1.00  9.61           C  
ANISOU  223  CD  ARG A  54     1449   1232    970    152    -45    -55       C  
ATOM    224  NE  ARG A  54      15.013 -20.899  -8.201  1.00 10.60           N  
ANISOU  224  NE  ARG A  54     1574   1373   1080    137    -56    -32       N  
ATOM    225  CZ  ARG A  54      13.944 -21.258  -7.511  1.00 10.82           C  
ANISOU  225  CZ  ARG A  54     1601   1415   1095    128    -47    -21       C  
ATOM    226  NH1 ARG A  54      12.750 -20.761  -7.822  1.00 13.60           N  
ANISOU  226  NH1 ARG A  54     1951   1766   1448    137    -25    -31       N  
ATOM    227  NH2 ARG A  54      14.067 -22.122  -6.511  1.00 11.67           N  
ANISOU  227  NH2 ARG A  54     1703   1540   1188    111    -61      7       N  
ATOM    228  N   GLU A  55      19.269 -20.980 -11.519  1.00  9.55           N  
ANISOU  228  N   GLU A  55     1399   1226   1001    191    -93    -26       N  
ATOM    229  CA  GLU A  55      20.605 -20.782 -10.910  1.00 11.62           C  
ANISOU  229  CA  GLU A  55     1651   1508   1255    180   -108     -7       C  
ATOM    230  C   GLU A  55      21.433 -22.046 -10.943  1.00 11.90           C  
ANISOU  230  C   GLU A  55     1671   1545   1303    199   -123     13       C  
ATOM    231  O   GLU A  55      22.185 -22.348  -9.984  1.00 14.16           O  
ANISOU  231  O   GLU A  55     1951   1843   1584    184   -139     36       O  
ATOM    232  CB  GLU A  55      20.437 -20.237  -9.486  1.00 13.90           C  
ANISOU  232  CB  GLU A  55     1956   1804   1520    146   -112     -6       C  
ATOM    233  CG  GLU A  55      19.800 -18.860  -9.440  1.00 14.65           C  
ANISOU  233  CG  GLU A  55     2066   1894   1603    132   -100    -31       C  
ATOM    234  CD  GLU A  55      20.788 -17.782  -9.794  1.00 16.18           C  
ANISOU  234  CD  GLU A  55     2252   2093   1799    122   -110    -27       C  
ATOM    235  OE1 GLU A  55      21.820 -17.701  -9.097  1.00 23.96           O  
ANISOU  235  OE1 GLU A  55     3234   3093   2773    102   -130     -8       O  
ATOM    236  OE2 GLU A  55      20.576 -17.019 -10.748  1.00 14.13           O  
ANISOU  236  OE2 GLU A  55     1990   1826   1553    129   -102    -37       O  
ATOM    237  N   GLY A  56      21.275 -22.775 -12.044  1.00 11.46           N  
ANISOU  237  N   GLY A  56     1610   1477   1265    233   -119      3       N  
ATOM    238  CA  GLY A  56      22.057 -23.982 -12.322  1.00 14.37           C  
ANISOU  238  CA  GLY A  56     1966   1841   1650    265   -132     14       C  
ATOM    239  C   GLY A  56      21.609 -25.255 -11.653  1.00 17.53           C  
ANISOU  239  C   GLY A  56     2378   2215   2066    264   -151     24       C  
ATOM    240  O   GLY A  56      22.331 -26.261 -11.769  1.00 23.43           O  
ANISOU  240  O   GLY A  56     3116   2954   2832    292   -167     35       O  
ATOM    241  N   SER A  57      20.475 -25.216 -10.959  1.00 13.99           N  
ANISOU  241  N   SER A  57     1948   1756   1611    236   -151     24       N  
ATOM    242  CA ASER A  57      19.936 -26.415 -10.306  0.50 15.84           C  
ANISOU  242  CA ASER A  57     2189   1967   1859    229   -173     42       C  
ATOM    243  CA BSER A  57      19.887 -26.360 -10.221  0.50 14.52           C  
ANISOU  243  CA BSER A  57     2023   1802   1691    226   -172     42       C  
ATOM    244  C   SER A  57      18.534 -26.754 -10.838  1.00 13.37           C  
ANISOU  244  C   SER A  57     1893   1629   1556    230   -171     27       C  
ATOM    245  O   SER A  57      17.680 -25.898 -11.011  1.00 12.22           O  
ANISOU  245  O   SER A  57     1753   1491   1396    217   -151     13       O  
ATOM    246  CB ASER A  57      19.935 -26.277  -8.785  0.50 21.82           C  
ANISOU  246  CB ASER A  57     2946   2746   2598    190   -181     70       C  
ATOM    247  CB BSER A  57      19.595 -25.956  -8.776  0.50 17.01           C  
ANISOU  247  CB BSER A  57     2340   2140   1981    184   -173     63       C  
ATOM    248  OG ASER A  57      18.767 -25.647  -8.290  0.50 21.97           O  
ANISOU  248  OG ASER A  57     2976   2775   2595    164   -165     62       O  
ATOM    249  OG BSER A  57      20.763 -25.838  -7.985  0.50 18.88           O  
ANISOU  249  OG BSER A  57     2565   2399   2209    172   -185     86       O  
ATOM    250  N   PRO A  58      18.293 -28.041 -11.115  1.00 12.64           N  
ANISOU  250  N   PRO A  58     1807   1501   1492    245   -197     33       N  
ATOM    251  CA  PRO A  58      16.970 -28.453 -11.550  1.00 12.06           C  
ANISOU  251  CA  PRO A  58     1749   1402   1430    238   -204     27       C  
ATOM    252  C   PRO A  58      15.911 -28.147 -10.505  1.00 11.15           C  
ANISOU  252  C   PRO A  58     1632   1304   1299    198   -198     52       C  
ATOM    253  O   PRO A  58      16.163 -28.245  -9.295  1.00 13.30           O  
ANISOU  253  O   PRO A  58     1896   1597   1560    174   -204     80       O  
ATOM    254  CB  PRO A  58      17.106 -29.970 -11.734  1.00 13.24           C  
ANISOU  254  CB  PRO A  58     1907   1506   1615    256   -244     37       C  
ATOM    255  CG  PRO A  58      18.538 -30.224 -11.844  1.00 17.68           C  
ANISOU  255  CG  PRO A  58     2459   2072   2185    288   -248     33       C  
ATOM    256  CD  PRO A  58      19.234 -29.176 -11.032  1.00 14.73           C  
ANISOU  256  CD  PRO A  58     2067   1745   1783    268   -225     47       C  
ATOM    257  N   LEU A  59      14.733 -27.759 -10.951  1.00 10.61           N  
ANISOU  257  N   LEU A  59     1569   1234   1227    190   -185     42       N  
ATOM    258  CA  LEU A  59      13.573 -27.509 -10.092  1.00 11.06           C  
ANISOU  258  CA  LEU A  59     1620   1312   1269    158   -176     66       C  
ATOM    259  C   LEU A  59      12.674 -28.714 -10.054  1.00 12.56           C  
ANISOU  259  C   LEU A  59     1811   1475   1483    143   -209     96       C  
ATOM    260  O   LEU A  59      12.355 -29.324 -11.099  1.00 14.57           O  
ANISOU  260  O   LEU A  59     2078   1691   1764    157   -229     85       O  
ATOM    261  CB  LEU A  59      12.752 -26.338 -10.606  1.00 10.36           C  
ANISOU  261  CB  LEU A  59     1532   1239   1165    159   -142     43       C  
ATOM    262  CG  LEU A  59      13.446 -24.984 -10.598  1.00  9.92           C  
ANISOU  262  CG  LEU A  59     1475   1207   1087    167   -113     16       C  
ATOM    263  CD1 LEU A  59      12.504 -23.960 -11.236  1.00 10.80           C  
ANISOU  263  CD1 LEU A  59     1586   1322   1194    170    -87     -1       C  
ATOM    264  CD2 LEU A  59      13.791 -24.590  -9.173  1.00 10.62           C  
ANISOU  264  CD2 LEU A  59     1560   1327   1147    146   -106     29       C  
ATOM    265  N   GLU A  60      12.274 -29.134  -8.862  1.00 11.05           N  
ANISOU  265  N   GLU A  60     1608   1304   1285    113   -219    138       N  
ATOM    266  CA  GLU A  60      11.242 -30.162  -8.785  1.00 12.00           C  
ANISOU  266  CA  GLU A  60     1725   1405   1429     91   -252    178       C  
ATOM    267  C   GLU A  60       9.938 -29.721  -9.388  1.00 12.87           C  
ANISOU  267  C   GLU A  60     1832   1518   1537     85   -236    175       C  
ATOM    268  O   GLU A  60       9.288 -30.490 -10.089  1.00 14.25           O  
ANISOU  268  O   GLU A  60     2014   1656   1742     80   -267    186       O  
ATOM    269  CB  GLU A  60      11.051 -30.608  -7.344  1.00 12.36           C  
ANISOU  269  CB  GLU A  60     1752   1483   1462     57   -264    231       C  
ATOM    270  CG  GLU A  60       9.866 -31.530  -7.133  1.00 12.20           C  
ANISOU  270  CG  GLU A  60     1719   1454   1461     26   -296    284       C  
ATOM    271  CD  GLU A  60       9.980 -32.476  -5.938  1.00 14.82           C  
ANISOU  271  CD  GLU A  60     2033   1798   1798     -6   -330    346       C  
ATOM    272  OE1 GLU A  60      10.987 -32.469  -5.229  1.00 15.48           O  
ANISOU  272  OE1 GLU A  60     2115   1897   1868     -5   -330    348       O  
ATOM    273  OE2 GLU A  60       9.029 -33.234  -5.800  1.00 15.34           O  
ANISOU  273  OE2 GLU A  60     2087   1858   1883    -35   -360    395       O  
ATOM    274  N   ASN A  61       9.557 -28.477  -9.125  1.00 11.91           N  
ANISOU  274  N   ASN A  61     1701   1440   1383     86   -190    160       N  
ATOM    275  CA  ASN A  61       8.328 -27.970  -9.656  1.00 12.02           C  
ANISOU  275  CA  ASN A  61     1708   1462   1397     83   -172    160       C  
ATOM    276  C   ASN A  61       8.607 -26.821 -10.594  1.00 11.14           C  
ANISOU  276  C   ASN A  61     1605   1347   1278    110   -141    111       C  
ATOM    277  O   ASN A  61       9.104 -25.816 -10.176  1.00 10.80           O  
ANISOU  277  O   ASN A  61     1562   1330   1210    119   -111     88       O  
ATOM    278  CB  ASN A  61       7.377 -27.583  -8.535  1.00 16.25           C  
ANISOU  278  CB  ASN A  61     2218   2051   1904     62   -148    195       C  
ATOM    279  CG  ASN A  61       6.856 -28.812  -7.794  1.00 20.23           C  
ANISOU  279  CG  ASN A  61     2706   2561   2420     29   -184    258       C  
ATOM    280  OD1 ASN A  61       7.154 -28.989  -6.635  1.00 28.46           O  
ANISOU  280  OD1 ASN A  61     3737   3638   3439     14   -183    283       O  
ATOM    281  ND2 ASN A  61       6.117 -29.665  -8.490  1.00 29.57           N  
ANISOU  281  ND2 ASN A  61     3888   3709   3637     15   -221    284       N  
ATOM    282  N   PRO A  62       8.270 -26.982 -11.863  1.00 10.41           N  
ANISOU  282  N   PRO A  62     1523   1224   1208    120   -154     96       N  
ATOM    283  CA  PRO A  62       8.563 -25.897 -12.831  1.00  9.64           C  
ANISOU  283  CA  PRO A  62     1431   1126   1104    143   -127     54       C  
ATOM    284  C   PRO A  62       7.780 -24.622 -12.475  1.00  9.99           C  
ANISOU  284  C   PRO A  62     1460   1205   1131    141    -86     53       C  
ATOM    285  O   PRO A  62       6.692 -24.678 -11.876  1.00 11.19           O  
ANISOU  285  O   PRO A  62     1595   1378   1279    125    -79     84       O  
ATOM    286  CB  PRO A  62       8.106 -26.467 -14.163  1.00 12.65           C  
ANISOU  286  CB  PRO A  62     1824   1473   1510    147   -153     48       C  
ATOM    287  CG  PRO A  62       8.022 -27.934 -13.976  1.00 15.56           C  
ANISOU  287  CG  PRO A  62     2202   1809   1900    134   -199     73       C  
ATOM    288  CD  PRO A  62       7.779 -28.199 -12.507  1.00 12.98           C  
ANISOU  288  CD  PRO A  62     1858   1509   1565    110   -198    114       C  
ATOM    289  N   VAL A  63       8.315 -23.504 -12.920  1.00  8.46           N  
ANISOU  289  N   VAL A  63     1270   1015    928    158    -63     20       N  
ATOM    290  CA  VAL A  63       7.761 -22.165 -12.639  1.00  9.39           C  
ANISOU  290  CA  VAL A  63     1377   1155   1033    163    -26     10       C  
ATOM    291  C   VAL A  63       7.542 -21.461 -13.975  1.00  8.49           C  
ANISOU  291  C   VAL A  63     1263   1026    934    175    -20     -6       C  
ATOM    292  O   VAL A  63       8.419 -21.419 -14.812  1.00  7.87           O  
ANISOU  292  O   VAL A  63     1194    935    861    185    -30    -26       O  
ATOM    293  CB  VAL A  63       8.732 -21.369 -11.776  1.00  8.66           C  
ANISOU  293  CB  VAL A  63     1292   1079    917    168    -10    -11       C  
ATOM    294  CG1 VAL A  63       8.286 -19.904 -11.626  1.00 11.05           C  
ANISOU  294  CG1 VAL A  63     1592   1394   1211    178     21    -31       C  
ATOM    295  CG2 VAL A  63       8.933 -22.035 -10.396  1.00 10.00           C  
ANISOU  295  CG2 VAL A  63     1462   1272   1066    153    -16      9       C  
ATOM    296  N   ASP A  64       6.352 -20.894 -14.158  1.00  8.55           N  
ANISOU  296  N   ASP A  64     1255   1042    949    174     -3      4       N  
ATOM    297  CA  ASP A  64       6.095 -20.131 -15.402  1.00  8.28           C  
ANISOU  297  CA  ASP A  64     1217    996    931    182      1     -6       C  
ATOM    298  C   ASP A  64       6.723 -18.742 -15.327  1.00  7.06           C  
ANISOU  298  C   ASP A  64     1065    845    771    196     23    -33       C  
ATOM    299  O   ASP A  64       6.654 -18.088 -14.290  1.00  9.33           O  
ANISOU  299  O   ASP A  64     1352   1145   1045    200     43    -41       O  
ATOM    300  CB  ASP A  64       4.592 -20.046 -15.652  1.00  9.43           C  
ANISOU  300  CB  ASP A  64     1343   1148   1091    176      8     21       C  
ATOM    301  CG  ASP A  64       4.012 -21.377 -16.204  1.00 11.62           C  
ANISOU  301  CG  ASP A  64     1620   1411   1382    157    -26     49       C  
ATOM    302  OD1 ASP A  64       4.784 -22.288 -16.590  1.00 15.22           O  
ANISOU  302  OD1 ASP A  64     2096   1847   1838    155    -55     38       O  
ATOM    303  OD2 ASP A  64       2.764 -21.490 -16.343  1.00 14.27           O  
ANISOU  303  OD2 ASP A  64     1937   1755   1730    145    -27     81       O  
ATOM    304  N   VAL A  65       7.351 -18.320 -16.415  1.00  7.37           N  
ANISOU  304  N   VAL A  65     1107    872    818    201     15    -47       N  
ATOM    305  CA  VAL A  65       8.041 -17.028 -16.547  1.00  6.73           C  
ANISOU  305  CA  VAL A  65     1027    790    738    208     26    -66       C  
ATOM    306  C   VAL A  65       7.565 -16.344 -17.816  1.00  6.88           C  
ANISOU  306  C   VAL A  65     1034    803    777    210     26    -59       C  
ATOM    307  O   VAL A  65       7.600 -16.923 -18.913  1.00  6.76           O  
ANISOU  307  O   VAL A  65     1016    787    764    207     10    -53       O  
ATOM    308  CB  VAL A  65       9.567 -17.247 -16.611  1.00  6.25           C  
ANISOU  308  CB  VAL A  65      977    732    665    209     12    -78       C  
ATOM    309  CG1 VAL A  65      10.310 -15.920 -16.763  1.00  7.98           C  
ANISOU  309  CG1 VAL A  65     1195    949    887    210     16    -89       C  
ATOM    310  CG2 VAL A  65      10.058 -18.036 -15.396  1.00  8.47           C  
ANISOU  310  CG2 VAL A  65     1268   1019    928    205      8    -78       C  
ATOM    311  N   PHE A  66       7.052 -15.131 -17.697  1.00  6.39           N  
ANISOU  311  N   PHE A  66      964    735    729    215     42    -61       N  
ATOM    312  CA  PHE A  66       6.592 -14.380 -18.845  1.00  6.10           C  
ANISOU  312  CA  PHE A  66      910    691    714    215     40    -50       C  
ATOM    313  C   PHE A  66       7.711 -14.058 -19.803  1.00  6.26           C  
ANISOU  313  C   PHE A  66      931    714    733    210     25    -52       C  
ATOM    314  O   PHE A  66       8.864 -13.821 -19.395  1.00  6.70           O  
ANISOU  314  O   PHE A  66      995    771    777    209     20    -65       O  
ATOM    315  CB  PHE A  66       5.950 -13.085 -18.349  1.00  6.04           C  
ANISOU  315  CB  PHE A  66      896    671    726    226     58    -54       C  
ATOM    316  CG  PHE A  66       5.444 -12.191 -19.462  1.00  6.49           C  
ANISOU  316  CG  PHE A  66      934    717    813    225     55    -37       C  
ATOM    317  CD1 PHE A  66       4.330 -12.563 -20.204  1.00  6.22           C  
ANISOU  317  CD1 PHE A  66      881    689    793    220     54    -10       C  
ATOM    318  CD2 PHE A  66       6.069 -10.974 -19.765  1.00  6.95           C  
ANISOU  318  CD2 PHE A  66      992    760    889    225     47    -42       C  
ATOM    319  CE1 PHE A  66       3.882 -11.746 -21.219  1.00  6.81           C  
ANISOU  319  CE1 PHE A  66      935    756    894    217     48     10       C  
ATOM    320  CE2 PHE A  66       5.577 -10.143 -20.766  1.00  8.64           C  
ANISOU  320  CE2 PHE A  66     1185    963   1133    221     41    -20       C  
ATOM    321  CZ  PHE A  66       4.476 -10.536 -21.482  1.00  7.81           C  
ANISOU  321  CZ  PHE A  66     1059    866   1038    219     42      5       C  
ATOM    322  N   VAL A  67       7.398 -14.105 -21.110  1.00  6.09           N  
ANISOU  322  N   VAL A  67      895    697    719    204     15    -36       N  
ATOM    323  CA  VAL A  67       8.392 -13.718 -22.109  1.00  6.66           C  
ANISOU  323  CA  VAL A  67      960    783    786    200      2    -32       C  
ATOM    324  C   VAL A  67       7.706 -12.860 -23.180  1.00  6.61           C  
ANISOU  324  C   VAL A  67      932    776    801    192      0     -9       C  
ATOM    325  O   VAL A  67       6.694 -13.253 -23.802  1.00  7.58           O  
ANISOU  325  O   VAL A  67     1048    901    930    187     -3      5       O  
ATOM    326  CB  VAL A  67       9.108 -14.929 -22.740  1.00  6.46           C  
ANISOU  326  CB  VAL A  67      943    778    734    203     -9    -39       C  
ATOM    327  CG1 VAL A  67       8.132 -15.999 -23.269  1.00  6.74           C  
ANISOU  327  CG1 VAL A  67      984    811    766    201    -18    -35       C  
ATOM    328  CG2 VAL A  67      10.053 -14.477 -23.841  1.00  7.83           C  
ANISOU  328  CG2 VAL A  67     1102    977    896    202    -17    -31       C  
ATOM    329  N   HIS A  68       8.244 -11.649 -23.371  1.00  6.64           N  
ANISOU  329  N   HIS A  68      926    776    821    187     -4      0       N  
ATOM    330  CA  HIS A  68       7.832 -10.763 -24.455  1.00  6.43           C  
ANISOU  330  CA  HIS A  68      874    751    816    176    -13     27       C  
ATOM    331  C   HIS A  68       8.763 -10.875 -25.615  1.00  6.74           C  
ANISOU  331  C   HIS A  68      900    826    833    166    -27     42       C  
ATOM    332  O   HIS A  68       9.966 -11.087 -25.459  1.00  6.84           O  
ANISOU  332  O   HIS A  68      917    856    824    168    -30     33       O  
ATOM    333  CB  HIS A  68       7.844  -9.314 -23.909  1.00  6.14           C  
ANISOU  333  CB  HIS A  68      833    683    814    176    -15     30       C  
ATOM    334  CG  HIS A  68       7.178  -8.350 -24.814  1.00  7.50           C  
ANISOU  334  CG  HIS A  68      981    847   1021    166    -24     63       C  
ATOM    335  ND1 HIS A  68       7.858  -7.500 -25.634  1.00  8.60           N  
ANISOU  335  ND1 HIS A  68     1101    994   1171    149    -45     90       N  
ATOM    336  CD2 HIS A  68       5.844  -8.133 -25.037  1.00  8.85           C  
ANISOU  336  CD2 HIS A  68     1138   1004   1218    171    -18     79       C  
ATOM    337  CE1 HIS A  68       6.991  -6.804 -26.349  1.00  8.85           C  
ANISOU  337  CE1 HIS A  68     1110   1016   1236    142    -52    121       C  
ATOM    338  NE2 HIS A  68       5.754  -7.196 -26.027  1.00 10.10           N  
ANISOU  338  NE2 HIS A  68     1271   1162   1404    156    -36    114       N  
ATOM    339  N   GLN A  69       8.219 -10.657 -26.824  1.00  7.23           N  
ANISOU  339  N   GLN A  69      942    904    899    154    -36     69       N  
ATOM    340  CA  GLN A  69       9.005 -10.757 -28.041  1.00  7.38           C  
ANISOU  340  CA  GLN A  69      945    969    891    146    -48     85       C  
ATOM    341  C   GLN A  69      10.276  -9.904 -28.055  1.00  7.37           C  
ANISOU  341  C   GLN A  69      928    982    890    138    -55    101       C  
ATOM    342  O   GLN A  69      11.291 -10.254 -28.653  1.00  7.66           O  
ANISOU  342  O   GLN A  69      954   1063    892    140    -58    105       O  
ATOM    343  CB  GLN A  69       8.147 -10.454 -29.281  1.00  8.12           C  
ANISOU  343  CB  GLN A  69     1016   1078    991    129    -59    118       C  
ATOM    344  CG  GLN A  69       7.465  -9.088 -29.303  1.00  7.55           C  
ANISOU  344  CG  GLN A  69      922    978    969    116    -66    151       C  
ATOM    345  CD  GLN A  69       8.266  -7.959 -29.914  1.00  7.20           C  
ANISOU  345  CD  GLN A  69      849    949    935     98    -82    187       C  
ATOM    346  OE1 GLN A  69       9.415  -8.137 -30.335  1.00  8.37           O  
ANISOU  346  OE1 GLN A  69      990   1138   1050     95    -86    191       O  
ATOM    347  NE2 GLN A  69       7.625  -6.781 -30.011  1.00  8.62           N  
ANISOU  347  NE2 GLN A  69     1010   1098   1165     86    -93    218       N  
ATOM    348  N   SER A  70      10.200  -8.762 -27.357  1.00  7.69           N  
ANISOU  348  N   SER A  70      966    984    970    131    -61    109       N  
ATOM    349  CA  SER A  70      11.297  -7.795 -27.401  1.00  8.19           C  
ANISOU  349  CA  SER A  70     1014   1054   1044    115    -77    132       C  
ATOM    350  C   SER A  70      12.515  -8.350 -26.684  1.00  8.57           C  
ANISOU  350  C   SER A  70     1075   1117   1064    124    -73    111       C  
ATOM    351  O   SER A  70      13.627  -7.810 -26.894  1.00  9.06           O  
ANISOU  351  O   SER A  70     1118   1201   1122    110    -88    137       O  
ATOM    352  CB  SER A  70      10.890  -6.464 -26.724  1.00  8.99           C  
ANISOU  352  CB  SER A  70     1117   1098   1197    107    -90    139       C  
ATOM    353  OG  SER A  70      10.534  -6.697 -25.365  1.00  9.17           O  
ANISOU  353  OG  SER A  70     1173   1082   1226    126    -75     97       O  
ATOM    354  N   LYS A  71      12.359  -9.416 -25.884  1.00  7.55           N  
ANISOU  354  N   LYS A  71      973    978    915    144    -56     73       N  
ATOM    355  CA  LYS A  71      13.456  -9.971 -25.101  1.00  7.22           C  
ANISOU  355  CA  LYS A  71      945    946    852    152    -54     54       C  
ATOM    356  C   LYS A  71      14.135 -11.180 -25.738  1.00  7.50           C  
ANISOU  356  C   LYS A  71      975   1030    845    169    -46     48       C  
ATOM    357  O   LYS A  71      15.099 -11.742 -25.168  1.00  8.16           O  
ANISOU  357  O   LYS A  71     1064   1125    910    179    -44     37       O  
ATOM    358  CB  LYS A  71      13.009 -10.269 -23.669  1.00  8.40           C  
ANISOU  358  CB  LYS A  71     1127   1055   1009    162    -43     20       C  
ATOM    359  CG  LYS A  71      12.353  -9.053 -22.972  1.00  9.68           C  
ANISOU  359  CG  LYS A  71     1297   1170   1209    155    -48     18       C  
ATOM    360  CD  LYS A  71      13.166  -7.773 -23.071  1.00 10.32           C  
ANISOU  360  CD  LYS A  71     1365   1241   1311    133    -73     42       C  
ATOM    361  CE  LYS A  71      12.628  -6.609 -22.235  1.00 11.55           C  
ANISOU  361  CE  LYS A  71     1540   1342   1506    131    -82     28       C  
ATOM    362  NZ  LYS A  71      11.205  -6.331 -22.595  1.00 13.33           N  
ANISOU  362  NZ  LYS A  71     1760   1545   1758    143    -70     30       N  
ATOM    363  N   LEU A  72      13.643 -11.605 -26.885  1.00  7.70           N  
ANISOU  363  N   LEU A  72      990   1081    853    173    -44     54       N  
ATOM    364  CA  LEU A  72      14.194 -12.784 -27.544  1.00  8.13           C  
ANISOU  364  CA  LEU A  72     1045   1177    866    195    -37     39       C  
ATOM    365  C   LEU A  72      15.427 -12.404 -28.357  1.00  8.17           C  
ANISOU  365  C   LEU A  72     1014   1240    846    194    -40     68       C  
ATOM    366  O   LEU A  72      15.370 -11.574 -29.273  1.00  8.90           O  
ANISOU  366  O   LEU A  72     1079   1361    941    176    -48    104       O  
ATOM    367  CB  LEU A  72      13.124 -13.396 -28.482  1.00  8.07           C  
ANISOU  367  CB  LEU A  72     1045   1174    846    199    -38     31       C  
ATOM    368  CG  LEU A  72      11.766 -13.805 -27.824  1.00  7.67           C  
ANISOU  368  CG  LEU A  72     1021   1073    819    196    -37     13       C  
ATOM    369  CD1 LEU A  72      10.807 -14.320 -28.896  1.00  8.03           C  
ANISOU  369  CD1 LEU A  72     1069   1128    852    193    -44     14       C  
ATOM    370  CD2 LEU A  72      12.043 -14.869 -26.773  1.00  7.64           C  
ANISOU  370  CD2 LEU A  72     1044   1047    809    215    -32    -18       C  
ATOM    371  N   TYR A  73      16.529 -13.103 -28.104  1.00  8.49           N  
ANISOU  371  N   TYR A  73     1054   1308    862    216    -33     57       N  
ATOM    372  CA  TYR A  73      17.776 -12.918 -28.858  1.00  8.69           C  
ANISOU  372  CA  TYR A  73     1042   1401    859    222    -31     86       C  
ATOM    373  C   TYR A  73      17.703 -13.721 -30.123  1.00  9.99           C  
ANISOU  373  C   TYR A  73     1201   1616    979    248    -21     73       C  
ATOM    374  O   TYR A  73      17.808 -14.930 -30.087  1.00 10.58           O  
ANISOU  374  O   TYR A  73     1298   1690   1030    282    -12     34       O  
ATOM    375  CB  TYR A  73      18.956 -13.360 -27.974  1.00 10.76           C  
ANISOU  375  CB  TYR A  73     1303   1669   1114    238    -28     80       C  
ATOM    376  CG  TYR A  73      20.271 -13.372 -28.675  1.00  9.94           C  
ANISOU  376  CG  TYR A  73     1158   1641    978    252    -22    110       C  
ATOM    377  CD1 TYR A  73      20.746 -12.227 -29.318  1.00 12.24           C  
ANISOU  377  CD1 TYR A  73     1405   1975   1270    224    -33    165       C  
ATOM    378  CD2 TYR A  73      21.015 -14.526 -28.737  1.00 11.01           C  
ANISOU  378  CD2 TYR A  73     1294   1807   1082    295     -7     86       C  
ATOM    379  CE1 TYR A  73      21.977 -12.233 -29.975  1.00 12.86           C  
ANISOU  379  CE1 TYR A  73     1436   2133   1314    237    -26    201       C  
ATOM    380  CE2 TYR A  73      22.247 -14.558 -29.388  1.00 11.69           C  
ANISOU  380  CE2 TYR A  73     1335   1970   1134    315      2    115       C  
ATOM    381  CZ  TYR A  73      22.696 -13.414 -30.001  1.00 13.17           C  
ANISOU  381  CZ  TYR A  73     1476   2206   1319    285     -5    173       C  
ATOM    382  OH  TYR A  73      23.891 -13.361 -30.690  1.00 15.77           O  
ANISOU  382  OH  TYR A  73     1753   2623   1613    301      4    212       O  
ATOM    383  N   MET A  74      17.504 -13.015 -31.231  1.00  9.65           N  
ANISOU  383  N   MET A  74     1129   1613    924    230    -26    107       N  
ATOM    384  CA  MET A  74      17.491 -13.613 -32.576  1.00 10.97           C  
ANISOU  384  CA  MET A  74     1287   1841   1040    251    -17     99       C  
ATOM    385  C   MET A  74      17.315 -12.466 -33.542  1.00 11.59           C  
ANISOU  385  C   MET A  74     1326   1960   1118    217    -28    153       C  
ATOM    386  O   MET A  74      16.838 -11.363 -33.183  1.00 11.76           O  
ANISOU  386  O   MET A  74     1338   1942   1186    179    -44    186       O  
ATOM    387  CB  MET A  74      16.369 -14.636 -32.770  1.00 12.27           C  
ANISOU  387  CB  MET A  74     1495   1970   1196    266    -19     50       C  
ATOM    388  CG  MET A  74      14.972 -14.044 -32.574  1.00 11.11           C  
ANISOU  388  CG  MET A  74     1362   1768   1092    231    -33     61       C  
ATOM    389  SD  MET A  74      13.732 -15.260 -32.075  1.00 11.29           S  
ANISOU  389  SD  MET A  74     1439   1725   1126    242    -38     10       S  
ATOM    390  CE  MET A  74      13.639 -16.192 -33.524  1.00 11.02           C  
ANISOU  390  CE  MET A  74     1414   1740   1032    263    -42    -14       C  
ATOM    391  N   GLU A  75      17.680 -12.712 -34.784  1.00 11.42           N  
ANISOU  391  N   GLU A  75     1279   2017   1042    231    -20    163       N  
ATOM    392  CA  GLU A  75      17.484 -11.760 -35.857  1.00 12.49           C  
ANISOU  392  CA  GLU A  75     1374   2202   1167    198    -31    217       C  
ATOM    393  C   GLU A  75      16.124 -11.947 -36.497  1.00 13.77           C  
ANISOU  393  C   GLU A  75     1560   2343   1328    186    -40    202       C  
ATOM    394  O   GLU A  75      15.540 -13.018 -36.397  1.00 13.54           O  
ANISOU  394  O   GLU A  75     1574   2284   1285    210    -35    146       O  
ATOM    395  CB  GLU A  75      18.569 -11.913 -36.924  1.00 16.82           C  
ANISOU  395  CB  GLU A  75     1879   2860   1649    219    -15    240       C  
ATOM    396  CG  GLU A  75      19.946 -11.487 -36.433  1.00 18.69           C  
ANISOU  396  CG  GLU A  75     2077   3132   1892    221    -11    278       C  
ATOM    397  CD  GLU A  75      20.023 -10.002 -36.169  1.00 24.68           C  
ANISOU  397  CD  GLU A  75     2800   3873   2702    165    -38    349       C  
ATOM    398  OE1 GLU A  75      19.726  -9.217 -37.093  1.00 40.19           O  
ANISOU  398  OE1 GLU A  75     4731   5876   4662    133    -52    400       O  
ATOM    399  OE2 GLU A  75      20.338  -9.610 -35.033  1.00 35.39           O  
ANISOU  399  OE2 GLU A  75     4166   5173   4106    152    -49    354       O  
ATOM    400  N   GLY A  76      15.661 -10.936 -37.215  1.00 13.67           N  
ANISOU  400  N   GLY A  76     1515   2350   1327    147    -56    256       N  
ATOM    401  CA  GLY A  76      14.404 -11.023 -37.953  1.00 14.25           C  
ANISOU  401  CA  GLY A  76     1601   2414   1396    130    -68    253       C  
ATOM    402  C   GLY A  76      13.200 -11.028 -37.016  1.00 12.77           C  
ANISOU  402  C   GLY A  76     1452   2129   1270    119    -78    231       C  
ATOM    403  O   GLY A  76      13.277 -10.556 -35.890  1.00 13.58           O  
ANISOU  403  O   GLY A  76     1560   2173   1423    114    -78    233       O  
ATOM    404  N   PHE A  77      12.080 -11.561 -37.457  1.00 11.42           N  
ANISOU  404  N   PHE A  77     1305   1941   1091    115    -85    212       N  
ATOM    405  CA  PHE A  77      10.891 -11.623 -36.639  1.00 10.42           C  
ANISOU  405  CA  PHE A  77     1207   1732   1017    106    -93    197       C  
ATOM    406  C   PHE A  77      11.169 -12.528 -35.443  1.00  9.45           C  
ANISOU  406  C   PHE A  77     1124   1562    902    137    -79    143       C  
ATOM    407  O   PHE A  77      11.700 -13.639 -35.606  1.00 10.75           O  
ANISOU  407  O   PHE A  77     1311   1750   1022    168    -71    100       O  
ATOM    408  CB  PHE A  77       9.727 -12.139 -37.443  1.00 10.75           C  
ANISOU  408  CB  PHE A  77     1264   1775   1042     94   -107    191       C  
ATOM    409  CG  PHE A  77       8.401 -11.999 -36.742  1.00  9.60           C  
ANISOU  409  CG  PHE A  77     1134   1557    955     79   -116    194       C  
ATOM    410  CD1 PHE A  77       7.684 -10.840 -36.808  1.00 10.48           C  
ANISOU  410  CD1 PHE A  77     1216   1648   1116     49   -127    246       C  
ATOM    411  CD2 PHE A  77       7.958 -12.994 -35.907  1.00 10.63           C  
ANISOU  411  CD2 PHE A  77     1305   1637   1093     97   -112    149       C  
ATOM    412  CE1 PHE A  77       6.442 -10.710 -36.164  1.00  9.86           C  
ANISOU  412  CE1 PHE A  77     1147   1508   1090     41   -131    250       C  
ATOM    413  CE2 PHE A  77       6.738 -12.880 -35.257  1.00 10.35           C  
ANISOU  413  CE2 PHE A  77     1277   1545   1107     84   -118    158       C  
ATOM    414  CZ  PHE A  77       5.993 -11.723 -35.366  1.00  9.08           C  
ANISOU  414  CZ  PHE A  77     1086   1370    993     58   -125    207       C  
ATOM    415  N   ARG A  78      10.825 -12.054 -34.246  1.00  8.79           N  
ANISOU  415  N   ARG A  78     1048   1414    875    131    -78    144       N  
ATOM    416  CA  ARG A  78      11.117 -12.771 -32.987  1.00  8.19           C  
ANISOU  416  CA  ARG A  78     1005   1296    809    155    -66    102       C  
ATOM    417  C   ARG A  78       9.961 -13.620 -32.516  1.00  8.24           C  
ANISOU  417  C   ARG A  78     1045   1253    829    159    -70     73       C  
ATOM    418  O   ARG A  78       8.821 -13.131 -32.401  1.00  9.04           O  
ANISOU  418  O   ARG A  78     1142   1323    967    139    -76     93       O  
ATOM    419  CB  ARG A  78      11.502 -11.728 -31.941  1.00  8.62           C  
ANISOU  419  CB  ARG A  78     1048   1318    909    145    -64    121       C  
ATOM    420  CG  ARG A  78      12.786 -10.984 -32.291  1.00  8.66           C  
ANISOU  420  CG  ARG A  78     1018   1369    901    139    -66    153       C  
ATOM    421  CD  ARG A  78      13.113  -9.902 -31.280  1.00  9.07           C  
ANISOU  421  CD  ARG A  78     1063   1380   1001    124    -72    171       C  
ATOM    422  NE  ARG A  78      12.166  -8.815 -31.273  1.00  9.44           N  
ANISOU  422  NE  ARG A  78     1101   1388   1098    100    -86    199       N  
ATOM    423  CZ  ARG A  78      12.252  -7.743 -32.034  1.00 11.76           C  
ANISOU  423  CZ  ARG A  78     1359   1701   1408     73   -104    251       C  
ATOM    424  NH1 ARG A  78      13.236  -7.630 -32.913  1.00 12.16           N  
ANISOU  424  NH1 ARG A  78     1376   1818   1423     65   -109    283       N  
ATOM    425  NH2 ARG A  78      11.369  -6.762 -31.916  1.00 12.30           N  
ANISOU  425  NH2 ARG A  78     1421   1723   1529     56   -118    274       N  
ATOM    426  N   SER A  79      10.250 -14.883 -32.216  1.00  8.44           N  
ANISOU  426  N   SER A  79     1103   1272    830    184    -67     30       N  
ATOM    427  CA  SER A  79       9.231 -15.767 -31.732  1.00  7.88           C  
ANISOU  427  CA  SER A  79     1063   1156    773    184    -75      8       C  
ATOM    428  C   SER A  79       9.901 -16.957 -31.044  1.00  7.79           C  
ANISOU  428  C   SER A  79     1083   1130    747    213    -72    -33       C  
ATOM    429  O   SER A  79      11.085 -17.166 -31.153  1.00  8.17           O  
ANISOU  429  O   SER A  79     1127   1208    768    237    -63    -48       O  
ATOM    430  CB  SER A  79       8.331 -16.316 -32.877  1.00  8.97           C  
ANISOU  430  CB  SER A  79     1211   1307    889    172    -96      7       C  
ATOM    431  OG  SER A  79       9.015 -17.234 -33.712  1.00 10.22           O  
ANISOU  431  OG  SER A  79     1387   1501    994    195   -101    -25       O  
ATOM    432  N   LEU A  80       9.100 -17.728 -30.312  1.00  8.24           N  
ANISOU  432  N   LEU A  80     1166   1141    823    211    -81    -48       N  
ATOM    433  CA  LEU A  80       9.478 -19.017 -29.788  1.00  8.71           C  
ANISOU  433  CA  LEU A  80     1257   1178    872    234    -88    -84       C  
ATOM    434  C   LEU A  80       8.487 -20.036 -30.317  1.00  9.19           C  
ANISOU  434  C   LEU A  80     1346   1217    926    226   -116    -97       C  
ATOM    435  O   LEU A  80       7.302 -19.715 -30.474  1.00  9.85           O  
ANISOU  435  O   LEU A  80     1422   1288   1030    198   -126    -71       O  
ATOM    436  CB  LEU A  80       9.456 -19.035 -28.257  1.00  8.04           C  
ANISOU  436  CB  LEU A  80     1178   1057    820    233    -79    -82       C  
ATOM    437  CG  LEU A  80      10.545 -18.240 -27.577  1.00  8.26           C  
ANISOU  437  CG  LEU A  80     1186   1098    851    241    -59    -76       C  
ATOM    438  CD1 LEU A  80      10.319 -18.242 -26.060  1.00  8.41           C  
ANISOU  438  CD1 LEU A  80     1213   1082    898    236    -52    -74       C  
ATOM    439  CD2 LEU A  80      11.954 -18.727 -27.922  1.00  9.81           C  
ANISOU  439  CD2 LEU A  80     1382   1327   1016    270    -55    -96       C  
ATOM    440  N   LYS A  81       8.940 -21.270 -30.515  1.00 10.92           N  
ANISOU  440  N   LYS A  81     1596   1428   1122    251   -131   -135       N  
ATOM    441  CA  LYS A  81       8.095 -22.403 -30.833  1.00 12.62           C  
ANISOU  441  CA  LYS A  81     1847   1609   1336    243   -166   -152       C  
ATOM    442  C   LYS A  81       7.741 -23.112 -29.537  1.00 10.91           C  
ANISOU  442  C   LYS A  81     1647   1342   1155    238   -177   -149       C  
ATOM    443  O   LYS A  81       8.580 -23.207 -28.645  1.00 10.69           O  
ANISOU  443  O   LYS A  81     1617   1309   1135    257   -161   -157       O  
ATOM    444  CB  LYS A  81       8.868 -23.352 -31.756  1.00 14.76           C  
ANISOU  444  CB  LYS A  81     2148   1896   1564    279   -180   -200       C  
ATOM    445  CG  LYS A  81       8.044 -24.522 -32.272  1.00 18.94           C  
ANISOU  445  CG  LYS A  81     2721   2388   2088    270   -224   -224       C  
ATOM    446  CD  LYS A  81       8.899 -25.458 -33.111  1.00 25.60           C  
ANISOU  446  CD  LYS A  81     3597   3243   2886    315   -236   -281       C  
ATOM    447  CE  LYS A  81       8.009 -26.391 -33.910  1.00 36.98           C  
ANISOU  447  CE  LYS A  81     5083   4652   4314    301   -286   -305       C  
ATOM    448  NZ  LYS A  81       7.280 -25.684 -34.998  1.00 42.47           N  
ANISOU  448  NZ  LYS A  81     5764   5387   4983    269   -291   -284       N  
ATOM    449  N   GLU A  82       6.508 -23.624 -29.402  1.00 11.15           N  
ANISOU  449  N   GLU A  82     1690   1338   1208    209   -205   -133       N  
ATOM    450  CA  GLU A  82       6.176 -24.462 -28.243  1.00 10.48           C  
ANISOU  450  CA  GLU A  82     1620   1208   1152    202   -221   -126       C  
ATOM    451  C   GLU A  82       7.191 -25.540 -28.076  1.00 11.21           C  
ANISOU  451  C   GLU A  82     1742   1281   1233    236   -234   -166       C  
ATOM    452  O   GLU A  82       7.494 -26.249 -29.033  1.00 11.98           O  
ANISOU  452  O   GLU A  82     1869   1376   1306    255   -257   -203       O  
ATOM    453  CB  GLU A  82       4.772 -25.114 -28.309  1.00 13.14           C  
ANISOU  453  CB  GLU A  82     1969   1512   1509    166   -261   -101       C  
ATOM    454  CG  GLU A  82       3.695 -24.102 -28.102  1.00 16.06           C  
ANISOU  454  CG  GLU A  82     2303   1898   1902    135   -244    -52       C  
ATOM    455  CD  GLU A  82       2.260 -24.624 -28.093  1.00 16.03           C  
ANISOU  455  CD  GLU A  82     2299   1869   1920     96   -280    -14       C  
ATOM    456  OE1 GLU A  82       2.003 -25.860 -28.145  1.00 19.18           O  
ANISOU  456  OE1 GLU A  82     2730   2232   2323     86   -325    -22       O  
ATOM    457  OE2 GLU A  82       1.364 -23.737 -28.099  1.00 15.09           O  
ANISOU  457  OE2 GLU A  82     2146   1769   1818     75   -264     26       O  
ATOM    458  N   GLY A  83       7.660 -25.724 -26.852  1.00 10.52           N  
ANISOU  458  N   GLY A  83     1651   1179   1166    243   -223   -160       N  
ATOM    459  CA  GLY A  83       8.597 -26.734 -26.510  1.00 11.24           C  
ANISOU  459  CA  GLY A  83     1765   1248   1256    274   -236   -190       C  
ATOM    460  C   GLY A  83      10.042 -26.420 -26.762  1.00  9.32           C  
ANISOU  460  C   GLY A  83     1513   1040    987    316   -208   -217       C  
ATOM    461  O   GLY A  83      10.905 -27.170 -26.374  1.00 13.25           O  
ANISOU  461  O   GLY A  83     2023   1522   1486    345   -214   -238       O  
ATOM    462  N   GLU A  84      10.320 -25.291 -27.417  1.00  9.76           N  
ANISOU  462  N   GLU A  84     1542   1145   1020    317   -178   -212       N  
ATOM    463  CA  GLU A  84      11.721 -24.996 -27.741  1.00 10.99           C  
ANISOU  463  CA  GLU A  84     1684   1343   1150    355   -152   -231       C  
ATOM    464  C   GLU A  84      12.516 -24.721 -26.462  1.00  9.57           C  
ANISOU  464  C   GLU A  84     1486   1163    988    359   -133   -215       C  
ATOM    465  O   GLU A  84      12.054 -24.015 -25.572  1.00  9.25           O  
ANISOU  465  O   GLU A  84     1428   1115    968    330   -122   -184       O  
ATOM    466  CB  GLU A  84      11.815 -23.874 -28.771  1.00 17.73           C  
ANISOU  466  CB  GLU A  84     2509   2250   1975    350   -131   -220       C  
ATOM    467  CG  GLU A  84      12.468 -22.571 -28.431  1.00 22.43           C  
ANISOU  467  CG  GLU A  84     3065   2884   2572    343    -98   -191       C  
ATOM    468  CD  GLU A  84      12.792 -21.766 -29.678  1.00 12.50           C  
ANISOU  468  CD  GLU A  84     1782   1684   1281    346    -85   -184       C  
ATOM    469  OE1 GLU A  84      11.842 -21.399 -30.380  1.00 12.95           O  
ANISOU  469  OE1 GLU A  84     1839   1745   1336    321    -94   -172       O  
ATOM    470  OE2 GLU A  84      13.985 -21.461 -29.933  1.00 13.39           O  
ANISOU  470  OE2 GLU A  84     1873   1843   1371    370    -66   -184       O  
ATOM    471  N   PRO A  85      13.731 -25.272 -26.373  1.00  9.86           N  
ANISOU  471  N   PRO A  85     1523   1207   1013    398   -129   -235       N  
ATOM    472  CA  PRO A  85      14.566 -25.074 -25.189  1.00  9.46           C  
ANISOU  472  CA  PRO A  85     1455   1159    978    401   -115   -218       C  
ATOM    473  C   PRO A  85      15.146 -23.671 -25.145  1.00  9.55           C  
ANISOU  473  C   PRO A  85     1429   1218    980    390    -84   -193       C  
ATOM    474  O   PRO A  85      15.516 -23.117 -26.199  1.00  9.94           O  
ANISOU  474  O   PRO A  85     1461   1311   1002    401    -71   -195       O  
ATOM    475  CB  PRO A  85      15.694 -26.077 -25.328  1.00 11.70           C  
ANISOU  475  CB  PRO A  85     1748   1443   1253    450   -121   -246       C  
ATOM    476  CG  PRO A  85      15.762 -26.367 -26.780  1.00 14.00           C  
ANISOU  476  CG  PRO A  85     2051   1757   1511    480   -123   -279       C  
ATOM    477  CD  PRO A  85      14.351 -26.234 -27.303  1.00 11.51           C  
ANISOU  477  CD  PRO A  85     1754   1422   1198    444   -140   -277       C  
ATOM    478  N   VAL A  86      15.131 -23.089 -23.950  1.00  7.97           N  
ANISOU  478  N   VAL A  86     1217   1009    799    365    -76   -168       N  
ATOM    479  CA  VAL A  86      15.639 -21.732 -23.792  1.00  9.11           C  
ANISOU  479  CA  VAL A  86     1332   1187    940    349    -55   -145       C  
ATOM    480  C   VAL A  86      16.483 -21.582 -22.517  1.00  7.94           C  
ANISOU  480  C   VAL A  86     1175   1038    802    345    -51   -131       C  
ATOM    481  O   VAL A  86      16.372 -22.370 -21.567  1.00  8.15           O  
ANISOU  481  O   VAL A  86     1219   1035    843    344    -63   -133       O  
ATOM    482  CB  VAL A  86      14.460 -20.720 -23.730  1.00  8.29           C  
ANISOU  482  CB  VAL A  86     1224   1073    850    313    -51   -127       C  
ATOM    483  CG1 VAL A  86      13.779 -20.585 -25.085  1.00  8.53           C  
ANISOU  483  CG1 VAL A  86     1254   1117    869    312    -54   -131       C  
ATOM    484  CG2 VAL A  86      13.482 -21.085 -22.640  1.00  8.64           C  
ANISOU  484  CG2 VAL A  86     1286   1078    917    294    -58   -123       C  
ATOM    485  N   GLU A  87      17.306 -20.543 -22.513  1.00  7.95           N  
ANISOU  485  N   GLU A  87     1151   1073    797    338    -39   -112       N  
ATOM    486  CA  GLU A  87      18.024 -20.082 -21.366  1.00  7.99           C  
ANISOU  486  CA  GLU A  87     1146   1078    809    324    -38    -94       C  
ATOM    487  C   GLU A  87      17.692 -18.612 -21.212  1.00  7.20           C  
ANISOU  487  C   GLU A  87     1036    982    718    291    -33    -77       C  
ATOM    488  O   GLU A  87      17.450 -17.918 -22.193  1.00  8.14           O  
ANISOU  488  O   GLU A  87     1142   1118    833    287    -28    -70       O  
ATOM    489  CB  GLU A  87      19.546 -20.196 -21.591  1.00  9.12           C  
ANISOU  489  CB  GLU A  87     1263   1261    938    347    -35    -83       C  
ATOM    490  CG  GLU A  87      20.063 -21.581 -21.741  1.00 11.00           C  
ANISOU  490  CG  GLU A  87     1509   1498   1172    387    -40   -101       C  
ATOM    491  CD  GLU A  87      21.567 -21.629 -22.035  1.00 13.25           C  
ANISOU  491  CD  GLU A  87     1760   1829   1442    416    -33    -86       C  
ATOM    492  OE1 GLU A  87      22.203 -20.550 -22.209  1.00 15.22           O  
ANISOU  492  OE1 GLU A  87     1979   2118   1684    399    -26    -56       O  
ATOM    493  OE2 GLU A  87      22.083 -22.777 -22.090  1.00 16.80           O  
ANISOU  493  OE2 GLU A  87     2215   2277   1892    455    -37   -101       O  
ATOM    494  N   PHE A  88      17.640 -18.106 -19.991  1.00  7.23           N  
ANISOU  494  N   PHE A  88     1047    967    732    268    -35    -70       N  
ATOM    495  CA  PHE A  88      17.234 -16.729 -19.791  1.00  7.50           C  
ANISOU  495  CA  PHE A  88     1078    994    777    241    -33    -61       C  
ATOM    496  C   PHE A  88      17.687 -16.148 -18.472  1.00  7.22           C  
ANISOU  496  C   PHE A  88     1049    948    744    221    -40    -56       C  
ATOM    497  O   PHE A  88      17.934 -16.882 -17.511  1.00  8.35           O  
ANISOU  497  O   PHE A  88     1205   1085    882    223    -43    -61       O  
ATOM    498  CB  PHE A  88      15.678 -16.648 -19.879  1.00  7.37           C  
ANISOU  498  CB  PHE A  88     1076    949    772    235    -27    -72       C  
ATOM    499  CG  PHE A  88      14.988 -17.689 -19.020  1.00  6.80           C  
ANISOU  499  CG  PHE A  88     1026    856    702    238    -27    -84       C  
ATOM    500  CD1 PHE A  88      14.732 -18.918 -19.512  1.00  7.56           C  
ANISOU  500  CD1 PHE A  88     1129    947    794    255    -34    -92       C  
ATOM    501  CD2 PHE A  88      14.684 -17.440 -17.691  1.00  8.31           C  
ANISOU  501  CD2 PHE A  88     1229   1033    895    224    -24    -86       C  
ATOM    502  CE1 PHE A  88      14.167 -19.906 -18.738  1.00  7.95           C  
ANISOU  502  CE1 PHE A  88     1195    977    849    253    -41    -95       C  
ATOM    503  CE2 PHE A  88      14.153 -18.428 -16.902  1.00  7.76           C  
ANISOU  503  CE2 PHE A  88     1173    952    823    225    -27    -88       C  
ATOM    504  CZ  PHE A  88      13.898 -19.668 -17.434  1.00  8.25           C  
ANISOU  504  CZ  PHE A  88     1238   1006    887    237    -36    -89       C  
ATOM    505  N   THR A  89      17.727 -14.834 -18.407  1.00  6.75           N  
ANISOU  505  N   THR A  89      986    883    695    200    -44    -47       N  
ATOM    506  CA  THR A  89      17.757 -14.110 -17.150  1.00  7.38           C  
ANISOU  506  CA  THR A  89     1082    942    777    179    -52    -53       C  
ATOM    507  C   THR A  89      16.316 -13.631 -16.889  1.00  7.08           C  
ANISOU  507  C   THR A  89     1063    875    752    178    -40    -72       C  
ATOM    508  O   THR A  89      15.518 -13.487 -17.824  1.00  8.05           O  
ANISOU  508  O   THR A  89     1178    994    887    185    -32    -71       O  
ATOM    509  CB  THR A  89      18.686 -12.906 -17.242  1.00  6.89           C  
ANISOU  509  CB  THR A  89     1008    886    723    158    -71    -33       C  
ATOM    510  OG1 THR A  89      18.309 -12.157 -18.397  1.00  8.26           O  
ANISOU  510  OG1 THR A  89     1164   1060    912    156    -70    -20       O  
ATOM    511  CG2 THR A  89      20.149 -13.398 -17.366  1.00  8.34           C  
ANISOU  511  CG2 THR A  89     1169   1106    894    159    -81     -7       C  
ATOM    512  N   PHE A  90      15.981 -13.418 -15.615  1.00  7.35           N  
ANISOU  512  N   PHE A  90     1120    892    780    171    -38    -89       N  
ATOM    513  CA  PHE A  90      14.631 -13.070 -15.215  1.00  7.10           C  
ANISOU  513  CA  PHE A  90     1102    839    755    176    -22   -108       C  
ATOM    514  C   PHE A  90      14.627 -12.326 -13.884  1.00  8.03           C  
ANISOU  514  C   PHE A  90     1243    943    863    167    -24   -128       C  
ATOM    515  O   PHE A  90      15.661 -12.247 -13.197  1.00  8.72           O  
ANISOU  515  O   PHE A  90     1339   1037    936    152    -41   -127       O  
ATOM    516  CB  PHE A  90      13.732 -14.312 -15.189  1.00  7.43           C  
ANISOU  516  CB  PHE A  90     1144    888    790    189     -8   -108       C  
ATOM    517  CG  PHE A  90      13.994 -15.265 -14.048  1.00  7.33           C  
ANISOU  517  CG  PHE A  90     1142    885    756    187     -9   -110       C  
ATOM    518  CD1 PHE A  90      15.040 -16.163 -14.090  1.00  6.77           C  
ANISOU  518  CD1 PHE A  90     1065    828    676    187    -22    -98       C  
ATOM    519  CD2 PHE A  90      13.211 -15.225 -12.899  1.00  9.44           C  
ANISOU  519  CD2 PHE A  90     1423   1152   1010    185      3   -121       C  
ATOM    520  CE1 PHE A  90      15.282 -17.034 -13.039  1.00  8.79           C  
ANISOU  520  CE1 PHE A  90     1330   1092    917    182    -27    -94       C  
ATOM    521  CE2 PHE A  90      13.421 -16.108 -11.867  1.00  9.09           C  
ANISOU  521  CE2 PHE A  90     1385   1122    944    179      0   -116       C  
ATOM    522  CZ  PHE A  90      14.482 -17.004 -11.931  1.00  9.12           C  
ANISOU  522  CZ  PHE A  90     1384   1135    945    175    -17   -101       C  
ATOM    523  N   LYS A  91      13.457 -11.779 -13.592  1.00  8.97           N  
ANISOU  523  N   LYS A  91     1372   1045    989    178     -8   -146       N  
ATOM    524  CA  LYS A  91      13.241 -11.124 -12.310  1.00  8.78           C  
ANISOU  524  CA  LYS A  91     1374   1010    950    178     -4   -174       C  
ATOM    525  C   LYS A  91      11.842 -11.385 -11.809  1.00 10.12           C  
ANISOU  525  C   LYS A  91     1547   1186   1113    198     24   -187       C  
ATOM    526  O   LYS A  91      10.939 -11.678 -12.571  1.00  9.35           O  
ANISOU  526  O   LYS A  91     1430   1089   1032    210     38   -174       O  
ATOM    527  CB  LYS A  91      13.402  -9.615 -12.435  1.00 10.02           C  
ANISOU  527  CB  LYS A  91     1544   1134   1129    174    -20   -189       C  
ATOM    528  CG  LYS A  91      12.415  -8.945 -13.377  1.00 12.01           C  
ANISOU  528  CG  LYS A  91     1782   1364   1417    189    -10   -185       C  
ATOM    529  CD  LYS A  91      12.653  -7.439 -13.420  1.00 12.78           C  
ANISOU  529  CD  LYS A  91     1893   1420   1540    183    -33   -197       C  
ATOM    530  CE  LYS A  91      11.577  -6.732 -14.164  1.00 15.27           C  
ANISOU  530  CE  LYS A  91     2196   1710   1893    201    -23   -195       C  
ATOM    531  NZ  LYS A  91      11.743  -5.244 -14.140  1.00 20.19           N  
ANISOU  531  NZ  LYS A  91     2836   2284   2549    197    -50   -208       N  
ATOM    532  N   LYS A  92      11.669 -11.179 -10.502  1.00 10.64           N  
ANISOU  532  N   LYS A  92     1634   1258   1150    202     33   -212       N  
ATOM    533  CA  LYS A  92      10.344 -11.143  -9.909  1.00 10.75           C  
ANISOU  533  CA  LYS A  92     1648   1282   1153    225     64   -226       C  
ATOM    534  C   LYS A  92       9.616  -9.879 -10.329  1.00 11.81           C  
ANISOU  534  C   LYS A  92     1784   1384   1317    246     72   -245       C  
ATOM    535  O   LYS A  92      10.203  -8.828 -10.502  1.00 13.79           O  
ANISOU  535  O   LYS A  92     2051   1601   1585    241     51   -261       O  
ATOM    536  CB  LYS A  92      10.447 -11.235  -8.368  1.00 13.18           C  
ANISOU  536  CB  LYS A  92     1979   1614   1413    224     71   -249       C  
ATOM    537  CG  LYS A  92      11.038 -10.035  -7.673  1.00 22.73           C  
ANISOU  537  CG  LYS A  92     3224   2801   2612    223     56   -289       C  
ATOM    538  CD  LYS A  92      10.913 -10.185  -6.157  1.00 25.36           C  
ANISOU  538  CD  LYS A  92     3578   3166   2889    226     69   -315       C  
ATOM    539  CE  LYS A  92      11.772  -9.160  -5.428  1.00 35.48           C  
ANISOU  539  CE  LYS A  92     4901   4424   4153    215     42   -354       C  
ATOM    540  NZ  LYS A  92      11.679  -7.789  -6.014  1.00 38.89           N  
ANISOU  540  NZ  LYS A  92     5349   4802   4625    228     29   -381       N  
ATOM    541  N   SER A  93       8.287  -9.979 -10.487  1.00 13.79           N  
ANISOU  541  N   SER A  93     2017   1644   1578    270    101   -239       N  
ATOM    542  CA  SER A  93       7.459  -8.809 -10.720  1.00 18.28           C  
ANISOU  542  CA  SER A  93     2586   2184   2175    297    114   -257       C  
ATOM    543  C   SER A  93       6.041  -9.106 -10.219  1.00 21.99           C  
ANISOU  543  C   SER A  93     3037   2683   2632    327    153   -255       C  
ATOM    544  O   SER A  93       5.800 -10.167  -9.597  1.00 21.36           O  
ANISOU  544  O   SER A  93     2949   2647   2520    321    167   -240       O  
ATOM    545  CB  SER A  93       7.432  -8.432 -12.189  1.00 16.15           C  
ANISOU  545  CB  SER A  93     2295   1887   1953    290     98   -231       C  
ATOM    546  OG  SER A  93       6.760  -9.445 -12.976  1.00 18.32           O  
ANISOU  546  OG  SER A  93     2538   2185   2235    286    108   -193       O  
ATOM    547  N   SER A  94       5.126  -8.166 -10.490  1.00 28.99           N  
ANISOU  547  N   SER A  94     3915   3548   3548    357    169   -265       N  
ATOM    548  CA ASER A  94       3.699  -8.378 -10.197  0.50 25.84           C  
ANISOU  548  CA ASER A  94     3490   3181   3146    389    208   -254       C  
ATOM    549  CA BSER A  94       3.693  -8.362 -10.209  0.50 25.65           C  
ANISOU  549  CA BSER A  94     3465   3156   3122    389    208   -254       C  
ATOM    550  C   SER A  94       3.127  -9.510 -11.053  1.00 27.48           C  
ANISOU  550  C   SER A  94     3660   3414   3367    369    209   -198       C  
ATOM    551  O   SER A  94       2.130 -10.164 -10.678  1.00 30.85           O  
ANISOU  551  O   SER A  94     4060   3881   3779    380    234   -174       O  
ATOM    552  CB ASER A  94       2.915  -7.084 -10.443  0.50 27.37           C  
ANISOU  552  CB ASER A  94     3680   3340   3377    428    221   -274       C  
ATOM    553  CB BSER A  94       2.912  -7.064 -10.491  0.50 26.11           C  
ANISOU  553  CB BSER A  94     3520   3180   3220    428    220   -273       C  
ATOM    554  OG ASER A  94       3.264  -6.112  -9.478  0.50 25.38           O  
ANISOU  554  OG ASER A  94     3467   3067   3107    452    222   -332       O  
ATOM    555  OG BSER A  94       3.044  -6.646 -11.838  0.50 22.23           O  
ANISOU  555  OG BSER A  94     3016   2649   2782    413    195   -248       O  
ATOM    556  N   LYS A  95       3.738  -9.754 -12.214  1.00 26.06           N  
ANISOU  556  N   LYS A  95     3475   3211   3213    341    179   -176       N  
ATOM    557  CA  LYS A  95       3.306 -10.875 -13.063  1.00 24.02           C  
ANISOU  557  CA  LYS A  95     3189   2971   2964    321    172   -130       C  
ATOM    558  C   LYS A  95       3.658 -12.202 -12.448  1.00 21.84           C  
ANISOU  558  C   LYS A  95     2916   2727   2651    300    167   -117       C  
ATOM    559  O   LYS A  95       3.137 -13.249 -12.871  1.00 29.25           O  
ANISOU  559  O   LYS A  95     3835   3683   3594    286    162    -81       O  
ATOM    560  CB  LYS A  95       3.925 -10.838 -14.450  1.00 22.06           C  
ANISOU  560  CB  LYS A  95     2938   2697   2745    298    142   -114       C  
ATOM    561  CG  LYS A  95       3.620  -9.643 -15.308  1.00 19.77           C  
ANISOU  561  CG  LYS A  95     2638   2375   2497    309    138   -112       C  
ATOM    562  CD  LYS A  95       4.161  -9.846 -16.732  1.00 23.65           C  
ANISOU  562  CD  LYS A  95     3119   2857   3006    282    109    -87       C  
ATOM    563  CE  LYS A  95       3.949  -8.619 -17.592  1.00 26.11           C  
ANISOU  563  CE  LYS A  95     3420   3140   3361    287    100    -78       C  
ATOM    564  NZ  LYS A  95       4.543  -7.382 -16.993  1.00 30.84           N  
ANISOU  564  NZ  LYS A  95     4042   3705   3971    299     94   -111       N  
ATOM    565  N  AGLY A  96       4.515 -12.131 -11.433  0.50 20.26           N  
ANISOU  565  N  AGLY A  96     2744   2534   2420    298    166   -146       N  
ATOM    566  N  CGLY A  96       4.502 -12.260 -11.422  0.50 18.64           N  
ANISOU  566  N  CGLY A  96     2537   2331   2212    297    165   -143       N  
ATOM    567  CA AGLY A  96       5.180 -13.310 -10.936  0.38 16.83           C  
ANISOU  567  CA AGLY A  96     2316   2122   1956    275    152   -134       C  
ATOM    568  CA CGLY A  96       5.040 -13.547 -11.022  0.62 14.79           C  
ANISOU  568  CA CGLY A  96     2053   1867   1699    272    152   -126       C  
ATOM    569  C  AGLY A  96       6.657 -13.255 -11.289  0.50 13.80           C  
ANISOU  569  C  AGLY A  96     1954   1715   1574    256    122   -147       C  
ATOM    570  C  CGLY A  96       6.544 -13.374 -11.264  0.50 12.80           C  
ANISOU  570  C  CGLY A  96     1825   1592   1446    256    124   -144       C  
ATOM    571  O  AGLY A  96       7.473 -12.729 -10.512  0.50 16.57           O  
ANISOU  571  O  AGLY A  96     2328   2062   1904    254    117   -175       O  
ATOM    572  O  CGLY A  96       7.254 -12.818 -10.411  0.50 14.50           O  
ANISOU  572  O  CGLY A  96     2064   1806   1640    257    122   -173       O  
ATOM    573  N   PHE A  97       7.006 -13.846 -12.427  1.00 10.11           N  
ANISOU  573  N   PHE A  97     1477   1237   1127    242    102   -126       N  
ATOM    574  CA  PHE A  97       8.363 -13.738 -12.913  1.00  8.99           C  
ANISOU  574  CA  PHE A  97     1347   1080    989    228     77   -133       C  
ATOM    575  C   PHE A  97       8.350 -13.392 -14.386  1.00  8.25           C  
ANISOU  575  C   PHE A  97     1240    968    926    227     67   -121       C  
ATOM    576  O   PHE A  97       7.422 -13.820 -15.112  1.00  9.01           O  
ANISOU  576  O   PHE A  97     1318   1067   1037    229     71   -101       O  
ATOM    577  CB  PHE A  97       9.102 -15.048 -12.717  1.00  8.43           C  
ANISOU  577  CB  PHE A  97     1278   1023    900    214     61   -119       C  
ATOM    578  CG  PHE A  97       9.259 -15.421 -11.300  1.00  9.78           C  
ANISOU  578  CG  PHE A  97     1461   1216   1039    209     66   -124       C  
ATOM    579  CD1 PHE A  97      10.232 -14.807 -10.526  1.00 10.07           C  
ANISOU  579  CD1 PHE A  97     1517   1252   1056    203     59   -146       C  
ATOM    580  CD2 PHE A  97       8.385 -16.331 -10.707  1.00 11.65           C  
ANISOU  580  CD2 PHE A  97     1686   1476   1263    207     76   -103       C  
ATOM    581  CE1 PHE A  97      10.342 -15.107  -9.156  1.00 10.29           C  
ANISOU  581  CE1 PHE A  97     1556   1305   1048    197     63   -151       C  
ATOM    582  CE2 PHE A  97       8.486 -16.604  -9.344  1.00 12.94           C  
ANISOU  582  CE2 PHE A  97     1856   1666   1391    201     82   -105       C  
ATOM    583  CZ  PHE A  97       9.469 -16.023  -8.594  1.00 11.31           C  
ANISOU  583  CZ  PHE A  97     1671   1461   1161    196     76   -129       C  
ATOM    584  N   GLU A  98       9.287 -12.554 -14.804  1.00  7.69           N  
ANISOU  584  N   GLU A  98     1174    882    864    222     52   -130       N  
ATOM    585  CA  GLU A  98       9.370 -12.185 -16.199  1.00  7.90           C  
ANISOU  585  CA  GLU A  98     1184    899    916    218     41   -114       C  
ATOM    586  C   GLU A  98      10.820 -12.197 -16.672  1.00  7.66           C  
ANISOU  586  C   GLU A  98     1154    875    879    205     19   -109       C  
ATOM    587  O   GLU A  98      11.735 -11.807 -15.946  1.00  8.39           O  
ANISOU  587  O   GLU A  98     1261    965    962    197      9   -120       O  
ATOM    588  CB  GLU A  98       8.727 -10.841 -16.492  1.00 10.61           C  
ANISOU  588  CB  GLU A  98     1522   1218   1288    226     45   -117       C  
ATOM    589  CG  GLU A  98       9.364  -9.685 -15.827  1.00 11.05           C  
ANISOU  589  CG  GLU A  98     1597   1251   1349    225     36   -139       C  
ATOM    590  CD  GLU A  98       8.582  -8.399 -16.147  1.00 13.52           C  
ANISOU  590  CD  GLU A  98     1905   1533   1699    238     38   -142       C  
ATOM    591  OE1 GLU A  98       7.517  -8.213 -15.526  1.00 18.90           O  
ANISOU  591  OE1 GLU A  98     2588   2209   2382    261     62   -156       O  
ATOM    592  OE2 GLU A  98       9.016  -7.671 -17.073  1.00 18.59           O  
ANISOU  592  OE2 GLU A  98     2537   2159   2368    225     17   -125       O  
ATOM    593  N   SER A  99      10.995 -12.598 -17.926  1.00  7.42           N  
ANISOU  593  N   SER A  99     1108    856    855    202     11    -90       N  
ATOM    594  CA  SER A  99      12.301 -12.738 -18.488  1.00  7.03           C  
ANISOU  594  CA  SER A  99     1051    824    796    196     -4    -81       C  
ATOM    595  C   SER A  99      12.856 -11.371 -18.926  1.00  7.45           C  
ANISOU  595  C   SER A  99     1094    868    866    183    -18    -70       C  
ATOM    596  O   SER A  99      12.114 -10.475 -19.334  1.00  8.35           O  
ANISOU  596  O   SER A  99     1201    964   1006    182    -17    -64       O  
ATOM    597  CB  SER A  99      12.295 -13.694 -19.678  1.00  9.48           C  
ANISOU  597  CB  SER A  99     1348   1154   1098    202     -7    -69       C  
ATOM    598  OG  SER A  99      11.417 -13.302 -20.648  1.00 11.49           O  
ANISOU  598  OG  SER A  99     1590   1406   1369    201     -5    -58       O  
ATOM    599  N   LEU A 100      14.175 -11.254 -18.806  1.00  7.09           N  
ANISOU  599  N   LEU A 100     1046    837    811    173    -33    -62       N  
ATOM    600  CA  LEU A 100      14.928 -10.039 -19.218  1.00  8.36           C  
ANISOU  600  CA  LEU A 100     1193    994    989    154    -54    -42       C  
ATOM    601  C   LEU A 100      15.632 -10.204 -20.561  1.00  7.32           C  
ANISOU  601  C   LEU A 100     1030    901    851    151    -61    -10       C  
ATOM    602  O   LEU A 100      15.680  -9.289 -21.353  1.00  8.54           O  
ANISOU  602  O   LEU A 100     1164   1055   1023    138    -74     14       O  
ATOM    603  CB  LEU A 100      15.922  -9.690 -18.143  1.00  8.24           C  
ANISOU  603  CB  LEU A 100     1193    971    966    140    -71    -48       C  
ATOM    604  CG  LEU A 100      15.360  -9.364 -16.778  1.00  9.26           C  
ANISOU  604  CG  LEU A 100     1356   1068   1094    142    -66    -81       C  
ATOM    605  CD1 LEU A 100      16.422  -9.351 -15.692  1.00 11.60           C  
ANISOU  605  CD1 LEU A 100     1669   1366   1371    127    -84    -88       C  
ATOM    606  CD2 LEU A 100      14.546  -8.081 -16.793  1.00 10.78           C  
ANISOU  606  CD2 LEU A 100     1558   1220   1317    143    -71    -92       C  
ATOM    607  N   ARG A 101      16.123 -11.402 -20.811  1.00  7.63           N  
ANISOU  607  N   ARG A 101     1063    972    863    166    -53    -11       N  
ATOM    608  CA  ARG A 101      16.774 -11.737 -22.090  1.00  7.06           C  
ANISOU  608  CA  ARG A 101      961    946    776    172    -53     11       C  
ATOM    609  C   ARG A 101      16.674 -13.232 -22.238  1.00  7.04           C  
ANISOU  609  C   ARG A 101      967    958    749    199    -39     -9       C  
ATOM    610  O   ARG A 101      16.934 -13.978 -21.271  1.00  8.25           O  
ANISOU  610  O   ARG A 101     1138   1101    894    207    -37    -25       O  
ATOM    611  CB  ARG A 101      18.245 -11.299 -22.076  1.00  8.81           C  
ANISOU  611  CB  ARG A 101     1159   1196    990    159    -69     40       C  
ATOM    612  CG  ARG A 101      18.978 -11.605 -23.372  1.00  8.84           C  
ANISOU  612  CG  ARG A 101     1127   1258    971    170    -66     67       C  
ATOM    613  CD  ARG A 101      20.298 -10.840 -23.486  1.00  9.13           C  
ANISOU  613  CD  ARG A 101     1131   1329   1009    149    -85    110       C  
ATOM    614  NE  ARG A 101      21.022 -11.303 -24.697  1.00 10.17           N  
ANISOU  614  NE  ARG A 101     1224   1529   1110    168    -74    135       N  
ATOM    615  CZ  ARG A 101      21.808 -12.388 -24.713  1.00 10.27           C  
ANISOU  615  CZ  ARG A 101     1228   1578   1094    199    -60    126       C  
ATOM    616  NH1 ARG A 101      22.044 -13.103 -23.625  1.00  9.96           N  
ANISOU  616  NH1 ARG A 101     1213   1515   1057    210    -59    102       N  
ATOM    617  NH2 ARG A 101      22.334 -12.778 -25.860  1.00 10.14           N  
ANISOU  617  NH2 ARG A 101     1178   1625   1047    222    -47    142       N  
ATOM    618  N   VAL A 102      16.323 -13.693 -23.426  1.00  7.30           N  
ANISOU  618  N   VAL A 102      989   1013    769    212    -34     -7       N  
ATOM    619  CA  VAL A 102      16.084 -15.114 -23.661  1.00  6.61           C  
ANISOU  619  CA  VAL A 102      917    931    664    237    -27    -31       C  
ATOM    620  C   VAL A 102      16.858 -15.579 -24.884  1.00  6.73           C  
ANISOU  620  C   VAL A 102      910    995    649    258    -24    -26       C  
ATOM    621  O   VAL A 102      16.808 -14.926 -25.920  1.00  8.24           O  
ANISOU  621  O   VAL A 102     1079   1215    834    250    -25     -5       O  
ATOM    622  CB  VAL A 102      14.562 -15.393 -23.901  1.00  6.91           C  
ANISOU  622  CB  VAL A 102      972    941    712    235    -24    -44       C  
ATOM    623  CG1 VAL A 102      14.288 -16.878 -24.164  1.00  8.19           C  
ANISOU  623  CG1 VAL A 102     1152   1100    858    257    -26    -67       C  
ATOM    624  CG2 VAL A 102      13.687 -14.852 -22.778  1.00  7.45           C  
ANISOU  624  CG2 VAL A 102     1055    969    806    219    -21    -47       C  
ATOM    625  N   THR A 103      17.580 -16.671 -24.737  1.00  8.19           N  
ANISOU  625  N   THR A 103     1102   1193    816    286    -21    -42       N  
ATOM    626  CA  THR A 103      18.371 -17.281 -25.808  1.00  8.40           C  
ANISOU  626  CA  THR A 103     1111   1269    810    318    -15    -45       C  
ATOM    627  C   THR A 103      17.987 -18.743 -25.910  1.00  8.24           C  
ANISOU  627  C   THR A 103     1121   1227    779    349    -17    -84       C  
ATOM    628  O   THR A 103      17.224 -19.267 -25.097  1.00  8.44           O  
ANISOU  628  O   THR A 103     1176   1204    825    341    -25   -100       O  
ATOM    629  CB  THR A 103      19.895 -17.186 -25.541  1.00  8.64           C  
ANISOU  629  CB  THR A 103     1113   1339    830    329    -12    -24       C  
ATOM    630  OG1 THR A 103      20.245 -18.169 -24.560  1.00  9.96           O  
ANISOU  630  OG1 THR A 103     1300   1481   1004    348    -14    -43       O  
ATOM    631  CG2 THR A 103      20.255 -15.778 -25.097  1.00 12.66           C  
ANISOU  631  CG2 THR A 103     1599   1851   1358    290    -20     14       C  
ATOM    632  N   GLY A 104      18.558 -19.403 -26.903  1.00  9.60           N  
ANISOU  632  N   GLY A 104     1286   1440    921    385    -11    -99       N  
ATOM    633  CA  GLY A 104      18.566 -20.851 -26.938  1.00 10.15           C  
ANISOU  633  CA  GLY A 104     1384   1488    981    422    -17   -138       C  
ATOM    634  C   GLY A 104      19.648 -21.440 -26.039  1.00 11.86           C  
ANISOU  634  C   GLY A 104     1596   1702   1206    446    -16   -138       C  
ATOM    635  O   GLY A 104      20.375 -20.706 -25.358  1.00 10.84           O  
ANISOU  635  O   GLY A 104     1442   1589   1087    429    -11   -106       O  
ATOM    636  N   PRO A 105      19.793 -22.775 -26.042  1.00 10.67           N  
ANISOU  636  N   PRO A 105     1470   1529   1053    484    -25   -171       N  
ATOM    637  CA  PRO A 105      20.891 -23.405 -25.339  1.00 12.05           C  
ANISOU  637  CA  PRO A 105     1636   1706   1236    513    -24   -169       C  
ATOM    638  C   PRO A 105      22.239 -22.828 -25.759  1.00 11.72           C  
ANISOU  638  C   PRO A 105     1546   1735   1170    533     -3   -143       C  
ATOM    639  O   PRO A 105      22.455 -22.473 -26.933  1.00 13.31           O  
ANISOU  639  O   PRO A 105     1727   1991   1339    549     10   -143       O  
ATOM    640  CB  PRO A 105      20.771 -24.871 -25.765  1.00 13.09           C  
ANISOU  640  CB  PRO A 105     1801   1807   1363    560    -37   -215       C  
ATOM    641  CG  PRO A 105      19.359 -25.063 -26.157  1.00 14.25           C  
ANISOU  641  CG  PRO A 105     1983   1914   1514    537    -54   -235       C  
ATOM    642  CD  PRO A 105      18.956 -23.756 -26.757  1.00 11.72           C  
ANISOU  642  CD  PRO A 105     1641   1633   1178    503    -39   -212       C  
ATOM    643  N   GLY A 106      23.117 -22.682 -24.770  1.00 13.47           N  
ANISOU  643  N   GLY A 106     1748   1961   1408    527     -4   -114       N  
ATOM    644  CA  GLY A 106      24.481 -22.245 -25.067  1.00 12.76           C  
ANISOU  644  CA  GLY A 106     1608   1940   1300    546     11    -81       C  
ATOM    645  C   GLY A 106      24.588 -20.785 -25.426  1.00 13.11           C  
ANISOU  645  C   GLY A 106     1618   2026   1335    504     17    -40       C  
ATOM    646  O   GLY A 106      25.599 -20.345 -25.944  1.00 15.22           O  
ANISOU  646  O   GLY A 106     1839   2361   1582    517     29     -7       O  
ATOM    647  N   GLY A 107      23.518 -20.010 -25.186  1.00 11.24           N  
ANISOU  647  N   GLY A 107     1403   1753   1115    456      7    -37       N  
ATOM    648  CA  GLY A 107      23.474 -18.613 -25.600  1.00 10.55           C  
ANISOU  648  CA  GLY A 107     1288   1696   1025    417      7      0       C  
ATOM    649  C   GLY A 107      23.265 -18.383 -27.099  1.00 10.29           C  
ANISOU  649  C   GLY A 107     1237   1713    960    430     19      0       C  
ATOM    650  O   GLY A 107      23.353 -17.278 -27.552  1.00 11.32           O  
ANISOU  650  O   GLY A 107     1337   1875   1087    400     17     37       O  
ATOM    651  N   ASN A 108      22.918 -19.444 -27.820  1.00 11.98           N  
ANISOU  651  N   ASN A 108     1473   1928   1151    473     27    -44       N  
ATOM    652  CA  ASN A 108      22.630 -19.360 -29.242  1.00 12.56           C  
ANISOU  652  CA  ASN A 108     1536   2049   1186    487     37    -52       C  
ATOM    653  C   ASN A 108      21.364 -18.590 -29.470  1.00 11.61           C  
ANISOU  653  C   ASN A 108     1432   1898   1081    441     25    -46       C  
ATOM    654  O   ASN A 108      20.531 -18.534 -28.579  1.00 11.09           O  
ANISOU  654  O   ASN A 108     1396   1765   1051    413     12    -54       O  
ATOM    655  CB  ASN A 108      22.428 -20.782 -29.826  1.00 14.54           C  
ANISOU  655  CB  ASN A 108     1820   2291   1411    543     41   -111       C  
ATOM    656  CG  ASN A 108      23.738 -21.526 -30.065  1.00 18.14           C  
ANISOU  656  CG  ASN A 108     2253   2798   1840    605     58   -120       C  
ATOM    657  OD1 ASN A 108      24.349 -21.350 -31.104  1.00 24.02           O  
ANISOU  657  OD1 ASN A 108     2963   3622   2541    632     78   -110       O  
ATOM    658  ND2 ASN A 108      24.135 -22.364 -29.159  1.00 21.16           N  
ANISOU  658  ND2 ASN A 108     2651   3140   2247    628     52   -136       N  
ATOM    659  N   PRO A 109      21.182 -17.979 -30.650  1.00 11.64           N  
ANISOU  659  N   PRO A 109     1412   1953   1057    432     30    -27       N  
ATOM    660  CA  PRO A 109      19.887 -17.339 -30.923  1.00 10.80           C  
ANISOU  660  CA  PRO A 109     1320   1813    967    391     17    -22       C  
ATOM    661  C   PRO A 109      18.737 -18.308 -30.770  1.00 11.37           C  
ANISOU  661  C   PRO A 109     1446   1824   1049    399      7    -71       C  
ATOM    662  O   PRO A 109      18.868 -19.531 -31.086  1.00 13.77           O  
ANISOU  662  O   PRO A 109     1774   2128   1328    441      9   -115       O  
ATOM    663  CB  PRO A 109      20.026 -16.911 -32.396  1.00 10.72           C  
ANISOU  663  CB  PRO A 109     1278   1881    913    393     25     -1       C  
ATOM    664  CG  PRO A 109      21.501 -16.722 -32.585  1.00 13.55           C  
ANISOU  664  CG  PRO A 109     1587   2314   1245    415     41     30       C  
ATOM    665  CD  PRO A 109      22.110 -17.809 -31.785  1.00 13.60           C  
ANISOU  665  CD  PRO A 109     1615   2295   1257    457     47     -5       C  
ATOM    666  N   CYS A 110      17.590 -17.768 -30.394  1.00  9.42           N  
ANISOU  666  N   CYS A 110     1214   1527    836    359     -4    -62       N  
ATOM    667  CA  CYS A 110      16.391 -18.583 -30.394  1.00  9.44           C  
ANISOU  667  CA  CYS A 110     1259   1479    846    359    -17    -96       C  
ATOM    668  C   CYS A 110      16.065 -18.954 -31.845  1.00 11.60           C  
ANISOU  668  C   CYS A 110     1537   1793   1078    373    -20   -113       C  
ATOM    669  O   CYS A 110      16.437 -18.261 -32.780  1.00 12.72           O  
ANISOU  669  O   CYS A 110     1644   1995   1190    368    -12    -87       O  
ATOM    670  CB  CYS A 110      15.229 -17.786 -29.786  1.00  9.50           C  
ANISOU  670  CB  CYS A 110     1272   1438    896    315    -26    -75       C  
ATOM    671  SG  CYS A 110      15.451 -17.136 -28.118  1.00 10.02           S  
ANISOU  671  SG  CYS A 110     1337   1462   1007    295    -24    -59       S  
ATOM    672  N   LEU A 111      15.342 -20.037 -31.991  1.00 13.54           N  
ANISOU  672  N   LEU A 111     1823   2000   1318    385    -35   -153       N  
ATOM    673  CA  LEU A 111      14.966 -20.486 -33.341  1.00 13.83           C  
ANISOU  673  CA  LEU A 111     1874   2069   1311    397    -43   -176       C  
ATOM    674  C   LEU A 111      13.609 -19.944 -33.799  1.00 13.01           C  
ANISOU  674  C   LEU A 111     1773   1949   1220    352    -60   -154       C  
ATOM    675  O   LEU A 111      13.461 -19.518 -34.946  1.00 13.21           O  
ANISOU  675  O   LEU A 111     1782   2025   1211    343    -61   -141       O  
ATOM    676  CB  LEU A 111      14.977 -22.014 -33.417  1.00 17.29           C  
ANISOU  676  CB  LEU A 111     2359   2476   1733    438    -58   -234       C  
ATOM    677  CG  LEU A 111      16.361 -22.627 -33.106  1.00 21.42           C  
ANISOU  677  CG  LEU A 111     2876   3020   2242    491    -41   -257       C  
ATOM    678  CD1 LEU A 111      16.354 -24.154 -33.198  1.00 26.82           C  
ANISOU  678  CD1 LEU A 111     3610   3663   2915    535    -60   -317       C  
ATOM    679  CD2 LEU A 111      17.492 -22.040 -33.945  1.00 24.57           C  
ANISOU  679  CD2 LEU A 111     3229   3511   2593    516    -13   -240       C  
ATOM    680  N   GLY A 112      12.635 -19.937 -32.904  1.00 12.63           N  
ANISOU  680  N   GLY A 112     1742   1837   1219    324    -73   -146       N  
ATOM    681  CA  GLY A 112      11.295 -19.505 -33.245  1.00 11.28           C  
ANISOU  681  CA  GLY A 112     1572   1647   1066    284    -89   -123       C  
ATOM    682  C   GLY A 112      10.539 -20.489 -34.117  1.00 12.60           C  
ANISOU  682  C   GLY A 112     1775   1805   1207    286   -116   -152       C  
ATOM    683  O   GLY A 112      10.926 -21.660 -34.314  1.00 16.89           O  
ANISOU  683  O   GLY A 112     2352   2340   1724    319   -126   -200       O  
ATOM    684  N   ASN A 113       9.422 -20.025 -34.604  1.00 15.11           N  
ANISOU  684  N   ASN A 113     2086   2119   1535    249   -131   -125       N  
ATOM    685  CA  ASN A 113       8.632 -20.830 -35.559  1.00 17.96           C  
ANISOU  685  CA  ASN A 113     2479   2476   1867    241   -162   -146       C  
ATOM    686  C   ASN A 113       9.246 -21.194 -36.888  1.00 25.07           C  
ANISOU  686  C   ASN A 113     3389   3437   2700    266   -165   -177       C  
ATOM    687  O   ASN A 113       9.157 -22.379 -37.271  1.00 28.78           O  
ANISOU  687  O   ASN A 113     3904   3887   3143    286   -189   -227       O  
ATOM    688  CB  ASN A 113       7.374 -20.076 -35.791  1.00 20.44           C  
ANISOU  688  CB  ASN A 113     2774   2783   2209    193   -175    -99       C  
ATOM    689  CG  ASN A 113       6.557 -20.033 -34.541  1.00 18.40           C  
ANISOU  689  CG  ASN A 113     2516   2463   2011    174   -177    -78       C  
ATOM    690  OD1 ASN A 113       6.391 -21.059 -33.906  1.00 21.65           O  
ANISOU  690  OD1 ASN A 113     2961   2831   2434    183   -192   -103       O  
ATOM    691  ND2 ASN A 113       6.066 -18.859 -34.160  1.00 19.08           N  
ANISOU  691  ND2 ASN A 113     2565   2548   2135    150   -163    -31       N  
TER     692      ASN A 113                                                      
ATOM    693  N   GLN B  29      27.786 -21.745  -0.415  1.00 33.60           N  
ANISOU  693  N   GLN B  29     4036   4655   4075   -150    173    579       N  
ATOM    694  CA  GLN B  29      27.042 -20.768  -1.267  1.00 33.62           C  
ANISOU  694  CA  GLN B  29     4052   4643   4079   -150    159    467       C  
ATOM    695  C   GLN B  29      28.052 -19.968  -2.105  1.00 32.35           C  
ANISOU  695  C   GLN B  29     3929   4447   3915   -125    121    403       C  
ATOM    696  O   GLN B  29      29.081 -19.515  -1.596  1.00 27.14           O  
ANISOU  696  O   GLN B  29     3278   3829   3205   -106    105    413       O  
ATOM    697  CB  GLN B  29      26.176 -19.835  -0.388  1.00 38.00           C  
ANISOU  697  CB  GLN B  29     4583   5303   4552   -152    168    430       C  
ATOM    698  CG  GLN B  29      25.415 -18.733  -1.144  1.00 49.07           C  
ANISOU  698  CG  GLN B  29     5995   6695   5952   -147    150    317       C  
ATOM    699  CD  GLN B  29      24.523 -17.877  -0.242  1.00 48.05           C  
ANISOU  699  CD  GLN B  29     5834   6669   5752   -149    159    276       C  
ATOM    700  OE1 GLN B  29      24.614 -16.648  -0.243  1.00 47.53           O  
ANISOU  700  OE1 GLN B  29     5774   6636   5647   -130    135    199       O  
ATOM    701  NE2 GLN B  29      23.653 -18.528   0.527  1.00 61.67           N  
ANISOU  701  NE2 GLN B  29     7522   8441   7466   -173    195    325       N  
ATOM    702  N   VAL B  30      27.760 -19.797  -3.393  1.00 29.68           N  
ANISOU  702  N   VAL B  30     3610   4037   3629   -124    109    337       N  
ATOM    703  CA  VAL B  30      28.633 -18.998  -4.268  1.00 22.35           C  
ANISOU  703  CA  VAL B  30     2716   3078   2698   -102     77    280       C  
ATOM    704  C   VAL B  30      28.768 -17.550  -3.761  1.00 21.59           C  
ANISOU  704  C   VAL B  30     2625   3051   2527    -86     60    229       C  
ATOM    705  O   VAL B  30      27.811 -16.946  -3.281  1.00 23.72           O  
ANISOU  705  O   VAL B  30     2875   3373   2763    -90     67    196       O  
ATOM    706  CB  VAL B  30      28.126 -18.960  -5.731  1.00 23.86           C  
ANISOU  706  CB  VAL B  30     2920   3199   2944   -101     67    217       C  
ATOM    707  CG1 VAL B  30      28.072 -20.360  -6.328  1.00 28.02           C  
ANISOU  707  CG1 VAL B  30     3435   3654   3555   -116     81    249       C  
ATOM    708  CG2 VAL B  30      26.768 -18.268  -5.817  1.00 25.53           C  
ANISOU  708  CG2 VAL B  30     3120   3440   3140   -105     71    160       C  
ATOM    709  N   LEU B  31      29.960 -16.986  -3.886  1.00 16.40           N  
ANISOU  709  N   LEU B  31     1988   2391   1852    -68     39    215       N  
ATOM    710  CA  LEU B  31      30.166 -15.591  -3.590  1.00 13.75           C  
ANISOU  710  CA  LEU B  31     1655   2101   1468    -53     22    156       C  
ATOM    711  C   LEU B  31      29.878 -14.800  -4.878  1.00 13.11           C  
ANISOU  711  C   LEU B  31     1598   1961   1419    -45      6     89       C  
ATOM    712  O   LEU B  31      29.955 -15.347  -5.981  1.00 13.13           O  
ANISOU  712  O   LEU B  31     1619   1898   1471    -46      3     93       O  
ATOM    713  CB  LEU B  31      31.615 -15.383  -3.173  1.00 17.02           C  
ANISOU  713  CB  LEU B  31     2076   2535   1856    -40      8    171       C  
ATOM    714  CG  LEU B  31      32.157 -16.331  -2.100  1.00 17.75           C  
ANISOU  714  CG  LEU B  31     2148   2674   1920    -42     19    251       C  
ATOM    715  CD1 LEU B  31      33.638 -16.086  -1.856  1.00 19.64           C  
ANISOU  715  CD1 LEU B  31     2394   2928   2138    -25      0    255       C  
ATOM    716  CD2 LEU B  31      31.350 -16.151  -0.835  1.00 21.24           C  
ANISOU  716  CD2 LEU B  31     2553   3217   2301    -47     35    261       C  
ATOM    717  N   ARG B  32      29.516 -13.534  -4.713  1.00 13.59           N  
ANISOU  717  N   ARG B  32     1654   2053   1456    -35     -4     29       N  
ATOM    718  CA  ARG B  32      29.172 -12.652  -5.824  1.00 13.29           C  
ANISOU  718  CA  ARG B  32     1634   1966   1445    -22    -19    -25       C  
ATOM    719  C   ARG B  32      30.040 -11.443  -5.837  1.00 13.41           C  
ANISOU  719  C   ARG B  32     1660   1980   1453     -7    -36    -62       C  
ATOM    720  O   ARG B  32      30.327 -10.847  -4.794  1.00 14.18           O  
ANISOU  720  O   ARG B  32     1736   2133   1516     -4    -37    -82       O  
ATOM    721  CB  ARG B  32      27.739 -12.149  -5.701  1.00 15.01           C  
ANISOU  721  CB  ARG B  32     1832   2210   1659    -22    -16    -68       C  
ATOM    722  CG  ARG B  32      26.713 -13.239  -5.601  1.00 15.49           C  
ANISOU  722  CG  ARG B  32     1876   2278   1731    -40      4    -41       C  
ATOM    723  CD  ARG B  32      26.330 -13.750  -6.964  1.00 19.66           C  
ANISOU  723  CD  ARG B  32     2420   2740   2309    -39      0    -47       C  
ATOM    724  NE  ARG B  32      25.302 -14.792  -6.838  1.00 19.30           N  
ANISOU  724  NE  ARG B  32     2349   2697   2284    -59     22    -30       N  
ATOM    725  CZ  ARG B  32      24.462 -15.138  -7.806  1.00 14.87           C  
ANISOU  725  CZ  ARG B  32     1785   2102   1762    -60     22    -58       C  
ATOM    726  NH1 ARG B  32      24.528 -14.551  -9.013  1.00 13.84           N  
ANISOU  726  NH1 ARG B  32     1674   1937   1644    -38      0    -97       N  
ATOM    727  NH2 ARG B  32      23.581 -16.103  -7.575  1.00 16.75           N  
ANISOU  727  NH2 ARG B  32     1995   2343   2026    -82     45    -43       N  
ATOM    728  N   GLY B  33      30.458 -11.048  -7.037  1.00 10.86           N  
ANISOU  728  N   GLY B  33     1365   1596   1163      2    -48    -74       N  
ATOM    729  CA  GLY B  33      31.239  -9.846  -7.188  1.00 11.54           C  
ANISOU  729  CA  GLY B  33     1460   1667   1255     15    -61   -107       C  
ATOM    730  C   GLY B  33      31.087  -9.232  -8.556  1.00  9.40           C  
ANISOU  730  C   GLY B  33     1213   1337   1019     27    -72   -121       C  
ATOM    731  O   GLY B  33      30.492  -9.823  -9.458  1.00 10.35           O  
ANISOU  731  O   GLY B  33     1344   1434   1153     28    -71   -108       O  
ATOM    732  N   SER B  34      31.638  -8.046  -8.695  1.00 10.11           N  
ANISOU  732  N   SER B  34     1307   1407   1125     38    -80   -148       N  
ATOM    733  CA  SER B  34      31.741  -7.401 -10.005  1.00  9.44           C  
ANISOU  733  CA  SER B  34     1246   1267   1072     51    -88   -147       C  
ATOM    734  C   SER B  34      33.070  -6.669 -10.095  1.00 10.29           C  
ANISOU  734  C   SER B  34     1362   1348   1199     51    -89   -148       C  
ATOM    735  O   SER B  34      33.753  -6.452  -9.109  1.00 10.88           O  
ANISOU  735  O   SER B  34     1420   1448   1264     44    -87   -166       O  
ATOM    736  CB  SER B  34      30.550  -6.478 -10.269  1.00 11.60           C  
ANISOU  736  CB  SER B  34     1510   1531   1364     68    -97   -179       C  
ATOM    737  OG  SER B  34      30.476  -5.440  -9.330  1.00 15.82           O  
ANISOU  737  OG  SER B  34     2020   2081   1910     72   -101   -224       O  
ATOM    738  N   GLY B  35      33.452  -6.308 -11.313  1.00  8.56           N  
ANISOU  738  N   GLY B  35     1166   1083   1003     58    -91   -129       N  
ATOM    739  CA  GLY B  35      34.682  -5.577 -11.552  1.00  8.80           C  
ANISOU  739  CA  GLY B  35     1203   1081   1057     56    -88   -126       C  
ATOM    740  C   GLY B  35      34.955  -5.499 -13.037  1.00  8.84           C  
ANISOU  740  C   GLY B  35     1233   1049   1075     63    -87    -90       C  
ATOM    741  O   GLY B  35      34.039  -5.302 -13.821  1.00  9.23           O  
ANISOU  741  O   GLY B  35     1289   1090   1127     79    -93    -81       O  
ATOM    742  N   HIS B  36      36.219  -5.665 -13.397  1.00  8.68           N  
ANISOU  742  N   HIS B  36     1224   1015   1058     53    -79    -72       N  
ATOM    743  CA  HIS B  36      36.614  -5.564 -14.807  1.00  8.36           C  
ANISOU  743  CA  HIS B  36     1202    949   1022     58    -75    -37       C  
ATOM    744  C   HIS B  36      37.728  -6.521 -15.090  1.00  7.89           C  
ANISOU  744  C   HIS B  36     1151    900    946     43    -68    -22       C  
ATOM    745  O   HIS B  36      38.403  -6.987 -14.174  1.00  8.22           O  
ANISOU  745  O   HIS B  36     1184    957    983     31    -67    -36       O  
ATOM    746  CB  HIS B  36      36.986  -4.127 -15.134  1.00  9.29           C  
ANISOU  746  CB  HIS B  36     1321   1024   1183     63    -70    -31       C  
ATOM    747  CG  HIS B  36      38.161  -3.617 -14.369  1.00 11.16           C  
ANISOU  747  CG  HIS B  36     1546   1246   1448     47    -61    -53       C  
ATOM    748  ND1 HIS B  36      38.016  -2.914 -13.205  1.00 12.67           N  
ANISOU  748  ND1 HIS B  36     1713   1436   1664     46    -64   -100       N  
ATOM    749  CD2 HIS B  36      39.519  -3.697 -14.619  1.00 10.50           C  
ANISOU  749  CD2 HIS B  36     1466   1152   1370     32    -48    -43       C  
ATOM    750  CE1 HIS B  36      39.241  -2.585 -12.736  1.00 12.52           C  
ANISOU  750  CE1 HIS B  36     1681   1408   1667     31    -55   -120       C  
ATOM    751  NE2 HIS B  36      40.168  -3.065 -13.593  1.00 12.66           N  
ANISOU  751  NE2 HIS B  36     1717   1418   1674     22    -45    -83       N  
ATOM    752  N   CYS B  37      37.925  -6.878 -16.337  1.00  7.24           N  
ANISOU  752  N   CYS B  37     1080    818    852     47    -65      3       N  
ATOM    753  CA  CYS B  37      39.016  -7.769 -16.709  1.00  7.26           C  
ANISOU  753  CA  CYS B  37     1085    829    844     35    -59     10       C  
ATOM    754  C   CYS B  37      40.349  -7.027 -16.445  1.00  6.94           C  
ANISOU  754  C   CYS B  37     1044    767    825     22    -48      9       C  
ATOM    755  O   CYS B  37      40.563  -5.939 -16.962  1.00  9.10           O  
ANISOU  755  O   CYS B  37     1322   1015   1120     24    -39     24       O  
ATOM    756  CB  CYS B  37      38.900  -8.149 -18.181  1.00  8.10           C  
ANISOU  756  CB  CYS B  37     1196    948    930     43    -58     29       C  
ATOM    757  SG  CYS B  37      40.306  -9.034 -18.804  1.00  8.45           S  
ANISOU  757  SG  CYS B  37     1238   1004    966     29    -49     31       S  
ATOM    758  N   LYS B  38      41.220  -7.669 -15.702  1.00  7.72           N  
ANISOU  758  N   LYS B  38     1134    876    921     10    -48     -4       N  
ATOM    759  CA  LYS B  38      42.571  -7.181 -15.470  1.00  7.78           C  
ANISOU  759  CA  LYS B  38     1137    871    948     -2    -38    -13       C  
ATOM    760  C   LYS B  38      43.421  -7.525 -16.700  1.00  7.11           C  
ANISOU  760  C   LYS B  38     1059    785    857     -9    -28      5       C  
ATOM    761  O   LYS B  38      44.036  -6.645 -17.281  1.00  8.54           O  
ANISOU  761  O   LYS B  38     1242    946   1056    -15    -13     18       O  
ATOM    762  CB  LYS B  38      43.160  -7.835 -14.229  1.00  7.63           C  
ANISOU  762  CB  LYS B  38     1102    874    921     -8    -46    -36       C  
ATOM    763  CG  LYS B  38      44.439  -7.187 -13.686  1.00  8.63           C  
ANISOU  763  CG  LYS B  38     1215    995   1069    -19    -39    -60       C  
ATOM    764  CD  LYS B  38      44.966  -8.027 -12.536  1.00  9.17           C  
ANISOU  764  CD  LYS B  38     1267   1099   1118    -18    -50    -75       C  
ATOM    765  CE  LYS B  38      46.203  -7.403 -11.930  1.00  9.72           C  
ANISOU  765  CE  LYS B  38     1315   1172   1204    -26    -46   -109       C  
ATOM    766  NZ  LYS B  38      46.750  -8.315 -10.887  1.00 10.51           N  
ANISOU  766  NZ  LYS B  38     1397   1316   1277    -20    -60   -117       N  
ATOM    767  N   TRP B  39      43.448  -8.792 -17.097  1.00  7.26           N  
ANISOU  767  N   TRP B  39     1077    826    855     -7    -34      7       N  
ATOM    768  CA  TRP B  39      44.076  -9.230 -18.305  1.00  7.51           C  
ANISOU  768  CA  TRP B  39     1108    868    875    -11    -26     15       C  
ATOM    769  C   TRP B  39      43.513 -10.576 -18.693  1.00  6.92           C  
ANISOU  769  C   TRP B  39     1027    815    785     -3    -37      7       C  
ATOM    770  O   TRP B  39      42.930 -11.268 -17.872  1.00  6.47           O  
ANISOU  770  O   TRP B  39      965    757    733      0    -48      0       O  
ATOM    771  CB  TRP B  39      45.592  -9.377 -18.125  1.00  6.91           C  
ANISOU  771  CB  TRP B  39     1023    791    812    -25    -19      2       C  
ATOM    772  CG  TRP B  39      46.042 -10.363 -17.098  1.00  6.83           C  
ANISOU  772  CG  TRP B  39     1001    787    806    -27    -31    -16       C  
ATOM    773  CD1 TRP B  39      46.291 -10.107 -15.765  1.00  6.93           C  
ANISOU  773  CD1 TRP B  39     1007    798    827    -28    -37    -29       C  
ATOM    774  CD2 TRP B  39      46.430 -11.751 -17.309  1.00  6.56           C  
ANISOU  774  CD2 TRP B  39      956    764    772    -25    -39    -25       C  
ATOM    775  NE1 TRP B  39      46.759 -11.236 -15.128  1.00  7.26           N  
ANISOU  775  NE1 TRP B  39     1037    854    868    -25    -49    -35       N  
ATOM    776  CE2 TRP B  39      46.836 -12.272 -16.027  1.00  6.68           C  
ANISOU  776  CE2 TRP B  39      961    781    796    -24    -51    -31       C  
ATOM    777  CE3 TRP B  39      46.432 -12.605 -18.436  1.00  7.01           C  
ANISOU  777  CE3 TRP B  39     1006    833    824    -23    -39    -32       C  
ATOM    778  CZ2 TRP B  39      47.287 -13.568 -15.874  1.00  6.87           C  
ANISOU  778  CZ2 TRP B  39      971    807    832    -20    -61    -35       C  
ATOM    779  CZ3 TRP B  39      46.876 -13.912 -18.254  1.00  6.98           C  
ANISOU  779  CZ3 TRP B  39      984    829    837    -22    -49    -47       C  
ATOM    780  CH2 TRP B  39      47.278 -14.371 -16.994  1.00  7.44           C  
ANISOU  780  CH2 TRP B  39     1036    878    911    -20    -60    -44       C  
ATOM    781  N   PHE B  40      43.649 -10.923 -19.950  1.00  6.64           N  
ANISOU  781  N   PHE B  40      986    801    734     -1    -33      8       N  
ATOM    782  CA  PHE B  40      43.202 -12.233 -20.445  1.00  7.37           C  
ANISOU  782  CA  PHE B  40     1063    913    822      5    -42    -12       C  
ATOM    783  C   PHE B  40      44.077 -12.636 -21.622  1.00  7.82           C  
ANISOU  783  C   PHE B  40     1106    999    866      1    -34    -26       C  
ATOM    784  O   PHE B  40      44.277 -11.854 -22.513  1.00  9.75           O  
ANISOU  784  O   PHE B  40     1354   1264   1085      3    -23     -8       O  
ATOM    785  CB  PHE B  40      41.717 -12.208 -20.831  1.00  7.30           C  
ANISOU  785  CB  PHE B  40     1056    919    799     20    -50    -11       C  
ATOM    786  CG  PHE B  40      41.129 -13.593 -20.955  1.00  7.18           C  
ANISOU  786  CG  PHE B  40     1019    912    796     23    -59    -41       C  
ATOM    787  CD1 PHE B  40      41.205 -14.316 -22.126  1.00  7.64           C  
ANISOU  787  CD1 PHE B  40     1055   1003    845     28    -60    -70       C  
ATOM    788  CD2 PHE B  40      40.546 -14.185 -19.862  1.00  7.37           C  
ANISOU  788  CD2 PHE B  40     1041    913    846     20    -66    -43       C  
ATOM    789  CE1 PHE B  40      40.689 -15.593 -22.184  1.00  8.09           C  
ANISOU  789  CE1 PHE B  40     1086   1058    930     29    -68   -105       C  
ATOM    790  CE2 PHE B  40      40.022 -15.459 -19.928  1.00  7.90           C  
ANISOU  790  CE2 PHE B  40     1084    977    938     20    -72    -67       C  
ATOM    791  CZ  PHE B  40      40.087 -16.158 -21.113  1.00  8.88           C  
ANISOU  791  CZ  PHE B  40     1185   1124   1064     24    -73   -102       C  
ATOM    792  N   ASN B  41      44.640 -13.835 -21.595  1.00  8.29           N  
ANISOU  792  N   ASN B  41     1144   1059    944     -2    -40    -56       N  
ATOM    793  CA  ASN B  41      45.533 -14.333 -22.625  1.00  7.40           C  
ANISOU  793  CA  ASN B  41     1009    976    823     -5    -34    -82       C  
ATOM    794  C   ASN B  41      44.849 -15.516 -23.311  1.00  7.18           C  
ANISOU  794  C   ASN B  41      953    971    802      4    -45   -122       C  
ATOM    795  O   ASN B  41      44.572 -16.535 -22.663  1.00  8.06           O  
ANISOU  795  O   ASN B  41     1052   1052    955      4    -56   -140       O  
ATOM    796  CB  ASN B  41      46.868 -14.701 -22.024  1.00  8.09           C  
ANISOU  796  CB  ASN B  41     1090   1044    938    -17    -34    -94       C  
ATOM    797  CG  ASN B  41      47.844 -15.188 -23.054  1.00  9.04           C  
ANISOU  797  CG  ASN B  41     1184   1197   1052    -22    -27   -127       C  
ATOM    798  OD1 ASN B  41      47.564 -16.166 -23.776  1.00  8.73           O  
ANISOU  798  OD1 ASN B  41     1117   1181   1019    -15    -34   -165       O  
ATOM    799  ND2 ASN B  41      48.997 -14.560 -23.132  1.00  9.02           N  
ANISOU  799  ND2 ASN B  41     1183   1199   1043    -34    -13   -121       N  
ATOM    800  N   VAL B  42      44.552 -15.367 -24.603  1.00  8.52           N  
ANISOU  800  N   VAL B  42     1109   1195    933     12    -40   -135       N  
ATOM    801  CA  VAL B  42      43.787 -16.363 -25.337  1.00  8.31           C  
ANISOU  801  CA  VAL B  42     1048   1199    910     24    -51   -184       C  
ATOM    802  C   VAL B  42      44.567 -17.617 -25.694  1.00  9.25           C  
ANISOU  802  C   VAL B  42     1126   1323   1063     19    -55   -243       C  
ATOM    803  O   VAL B  42      43.961 -18.628 -26.003  1.00 10.99           O  
ANISOU  803  O   VAL B  42     1314   1549   1313     26    -64   -292       O  
ATOM    804  CB  VAL B  42      43.032 -15.789 -26.552  1.00  9.48           C  
ANISOU  804  CB  VAL B  42     1188   1414    997     41    -48   -181       C  
ATOM    805  CG1 VAL B  42      42.073 -14.674 -26.112  1.00  9.44           C  
ANISOU  805  CG1 VAL B  42     1219   1392    973     50    -49   -127       C  
ATOM    806  CG2 VAL B  42      43.989 -15.249 -27.606  1.00 10.54           C  
ANISOU  806  CG2 VAL B  42     1314   1608   1082     39    -33   -172       C  
ATOM    807  N   ARG B  43      45.891 -17.554 -25.749  1.00  8.63           N  
ANISOU  807  N   ARG B  43     1045   1246    986      9    -46   -245       N  
ATOM    808  CA  ARG B  43      46.660 -18.763 -25.881  1.00  9.03           C  
ANISOU  808  CA  ARG B  43     1057   1290   1084      5    -53   -302       C  
ATOM    809  C   ARG B  43      46.617 -19.597 -24.605  1.00  9.00           C  
ANISOU  809  C   ARG B  43     1056   1210   1153      3    -66   -296       C  
ATOM    810  O   ARG B  43      46.391 -20.827 -24.655  1.00 10.35           O  
ANISOU  810  O   ARG B  43     1190   1359   1381      7    -76   -341       O  
ATOM    811  CB  ARG B  43      48.100 -18.496 -26.333  1.00  9.19           C  
ANISOU  811  CB  ARG B  43     1067   1338   1085     -4    -41   -312       C  
ATOM    812  CG  ARG B  43      48.912 -19.756 -26.515  1.00  9.92           C  
ANISOU  812  CG  ARG B  43     1114   1424   1230     -4    -50   -378       C  
ATOM    813  CD  ARG B  43      50.372 -19.478 -26.928  1.00 10.48           C  
ANISOU  813  CD  ARG B  43     1172   1525   1282    -15    -37   -392       C  
ATOM    814  NE  ARG B  43      51.055 -20.772 -27.021  1.00 11.02           N  
ANISOU  814  NE  ARG B  43     1193   1580   1412    -12    -50   -462       N  
ATOM    815  CZ  ARG B  43      50.937 -21.602 -28.037  1.00 12.38           C  
ANISOU  815  CZ  ARG B  43     1313   1797   1594     -5    -54   -537       C  
ATOM    816  NH1 ARG B  43      50.358 -21.247 -29.176  1.00 12.33           N  
ANISOU  816  NH1 ARG B  43     1290   1872   1522      0    -45   -555       N  
ATOM    817  NH2 ARG B  43      51.460 -22.819 -27.971  1.00 13.36           N  
ANISOU  817  NH2 ARG B  43     1392   1890   1793     -1    -68   -600       N  
ATOM    818  N   MET B  44      46.769 -18.936 -23.478  1.00  8.17           N  
ANISOU  818  N   MET B  44      988   1067   1046     -2    -64   -241       N  
ATOM    819  CA  MET B  44      46.659 -19.585 -22.175  1.00  8.50           C  
ANISOU  819  CA  MET B  44     1036   1051   1142     -2    -75   -220       C  
ATOM    820  C   MET B  44      45.247 -20.089 -21.921  1.00  8.04           C  
ANISOU  820  C   MET B  44      974    973   1108      2    -80   -217       C  
ATOM    821  O   MET B  44      45.071 -21.143 -21.292  1.00  9.52           O  
ANISOU  821  O   MET B  44     1142   1116   1356      3    -88   -218       O  
ATOM    822  CB  MET B  44      47.033 -18.608 -21.064  1.00  8.08           C  
ANISOU  822  CB  MET B  44     1019    981   1067     -7    -71   -167       C  
ATOM    823  CG  MET B  44      48.501 -18.216 -21.014  1.00  9.03           C  
ANISOU  823  CG  MET B  44     1141   1109   1181    -14    -67   -170       C  
ATOM    824  SD  MET B  44      48.862 -17.066 -19.692  1.00  9.01           S  
ANISOU  824  SD  MET B  44     1171   1091   1159    -19    -64   -124       S  
ATOM    825  CE  MET B  44      50.459 -16.437 -20.251  1.00 12.15           C  
ANISOU  825  CE  MET B  44     1562   1511   1543    -31    -50   -145       C  
ATOM    826  N   GLY B  45      44.264 -19.303 -22.341  1.00  7.90           N  
ANISOU  826  N   GLY B  45      972    985   1044      6    -76   -207       N  
ATOM    827  CA  GLY B  45      42.885 -19.599 -22.067  1.00  7.52           C  
ANISOU  827  CA  GLY B  45      922    924   1012     10    -79   -204       C  
ATOM    828  C   GLY B  45      42.399 -19.139 -20.702  1.00  7.49           C  
ANISOU  828  C   GLY B  45      949    888   1008      6    -79   -150       C  
ATOM    829  O   GLY B  45      41.413 -19.664 -20.203  1.00  8.17           O  
ANISOU  829  O   GLY B  45     1028    953   1123      6    -80   -145       O  
ATOM    830  N   PHE B  46      43.070 -18.166 -20.128  1.00  7.17           N  
ANISOU  830  N   PHE B  46      937    849    936      3    -75   -116       N  
ATOM    831  CA  PHE B  46      42.696 -17.653 -18.815  1.00  7.12           C  
ANISOU  831  CA  PHE B  46      954    826    924      1    -75    -74       C  
ATOM    832  C   PHE B  46      43.227 -16.268 -18.629  1.00  7.21           C  
ANISOU  832  C   PHE B  46      992    851    896      0    -70    -55       C  
ATOM    833  O   PHE B  46      44.049 -15.793 -19.430  1.00  7.16           O  
ANISOU  833  O   PHE B  46      987    860    872     -2    -64    -65       O  
ATOM    834  CB  PHE B  46      43.078 -18.610 -17.693  1.00  6.74           C  
ANISOU  834  CB  PHE B  46      895    746    918     -1    -81    -54       C  
ATOM    835  CG  PHE B  46      44.531 -18.985 -17.657  1.00  7.51           C  
ANISOU  835  CG  PHE B  46      982    836   1033     -1    -85    -60       C  
ATOM    836  CD1 PHE B  46      45.489 -18.119 -17.153  1.00  7.86           C  
ANISOU  836  CD1 PHE B  46     1043    892   1049     -3    -84    -47       C  
ATOM    837  CD2 PHE B  46      44.931 -20.265 -18.100  1.00  7.78           C  
ANISOU  837  CD2 PHE B  46      985    848   1122      0    -90    -86       C  
ATOM    838  CE1 PHE B  46      46.823 -18.469 -17.118  1.00  8.48           C  
ANISOU  838  CE1 PHE B  46     1110    967   1145     -3    -88    -57       C  
ATOM    839  CE2 PHE B  46      46.274 -20.626 -18.023  1.00  8.75           C  
ANISOU  839  CE2 PHE B  46     1095    963   1264      2    -96    -95       C  
ATOM    840  CZ  PHE B  46      47.189 -19.730 -17.544  1.00  8.76           C  
ANISOU  840  CZ  PHE B  46     1116    983   1230      0    -95    -79       C  
ATOM    841  N   GLY B  47      42.863 -15.654 -17.516  1.00  6.99           N  
ANISOU  841  N   GLY B  47      980    817    858     -1    -70    -29       N  
ATOM    842  CA  GLY B  47      43.354 -14.367 -17.069  1.00  7.76           C  
ANISOU  842  CA  GLY B  47     1094    918    932     -4    -65    -17       C  
ATOM    843  C   GLY B  47      42.939 -14.128 -15.648  1.00  7.28           C  
ANISOU  843  C   GLY B  47     1037    858    869     -3    -69     -1       C  
ATOM    844  O   GLY B  47      42.625 -15.067 -14.892  1.00  7.09           O  
ANISOU  844  O   GLY B  47     1003    832    859     -2    -74     10       O  
ATOM    845  N   PHE B  48      42.871 -12.852 -15.291  1.00  6.15           N  
ANISOU  845  N   PHE B  48      906    719    711     -3    -66     -1       N  
ATOM    846  CA  PHE B  48      42.373 -12.411 -13.999  1.00  6.61           C  
ANISOU  846  CA  PHE B  48      962    789    760     -2    -69      1       C  
ATOM    847  C   PHE B  48      41.375 -11.270 -14.163  1.00  6.75           C  
ANISOU  847  C   PHE B  48      988    805    770      2    -66     -4       C  
ATOM    848  O   PHE B  48      41.469 -10.443 -15.090  1.00  6.45           O  
ANISOU  848  O   PHE B  48      961    753    735      3    -60     -5       O  
ATOM    849  CB  PHE B  48      43.490 -11.959 -13.088  1.00  7.87           C  
ANISOU  849  CB  PHE B  48     1113    959    917     -5    -70     -6       C  
ATOM    850  CG  PHE B  48      44.178 -13.097 -12.421  1.00  7.24           C  
ANISOU  850  CG  PHE B  48     1019    891    839     -3    -77      6       C  
ATOM    851  CD1 PHE B  48      45.192 -13.815 -13.077  1.00  7.86           C  
ANISOU  851  CD1 PHE B  48     1094    955    935     -5    -79      4       C  
ATOM    852  CD2 PHE B  48      43.793 -13.514 -11.166  1.00  8.22           C  
ANISOU  852  CD2 PHE B  48     1130   1042    948      1    -83     23       C  
ATOM    853  CE1 PHE B  48      45.813 -14.888 -12.479  1.00  8.01           C  
ANISOU  853  CE1 PHE B  48     1098    979    965      0    -88     20       C  
ATOM    854  CE2 PHE B  48      44.400 -14.580 -10.553  1.00  9.62           C  
ANISOU  854  CE2 PHE B  48     1294   1230   1131      7    -91     48       C  
ATOM    855  CZ  PHE B  48      45.407 -15.271 -11.206  1.00  8.56           C  
ANISOU  855  CZ  PHE B  48     1157   1073   1022      7    -94     47       C  
ATOM    856  N   ILE B  49      40.400 -11.280 -13.274  1.00  6.92           N  
ANISOU  856  N   ILE B  49     1004    841    783      5    -70     -4       N  
ATOM    857  CA  ILE B  49      39.466 -10.197 -13.053  1.00  7.04           C  
ANISOU  857  CA  ILE B  49     1021    859    796     11    -70    -17       C  
ATOM    858  C   ILE B  49      39.974  -9.365 -11.875  1.00  7.69           C  
ANISOU  858  C   ILE B  49     1089    956    876      9    -71    -38       C  
ATOM    859  O   ILE B  49      40.459  -9.911 -10.879  1.00  8.54           O  
ANISOU  859  O   ILE B  49     1182   1092    968      6    -73    -37       O  
ATOM    860  CB  ILE B  49      38.059 -10.742 -12.773  1.00  7.64           C  
ANISOU  860  CB  ILE B  49     1090    949    863     15    -73    -14       C  
ATOM    861  CG1 ILE B  49      37.467 -11.347 -14.038  1.00  7.15           C  
ANISOU  861  CG1 ILE B  49     1034    874    806     19    -73     -9       C  
ATOM    862  CG2 ILE B  49      37.118  -9.657 -12.191  1.00  7.80           C  
ANISOU  862  CG2 ILE B  49     1103    979    878     21    -75    -36       C  
ATOM    863  CD1 ILE B  49      36.252 -12.244 -13.729  1.00  8.35           C  
ANISOU  863  CD1 ILE B  49     1174   1039    959     18    -73     -8       C  
ATOM    864  N   SER B  50      39.844  -8.045 -11.984  1.00  8.41           N  
ANISOU  864  N   SER B  50     1180   1029    984     12    -69    -59       N  
ATOM    865  CA  SER B  50      40.014  -7.162 -10.837  1.00  8.70           C  
ANISOU  865  CA  SER B  50     1195   1083   1026     12    -70    -95       C  
ATOM    866  C   SER B  50      38.634  -6.932 -10.279  1.00  8.13           C  
ANISOU  866  C   SER B  50     1111   1031    943     20    -75   -110       C  
ATOM    867  O   SER B  50      37.811  -6.204 -10.854  1.00  8.45           O  
ANISOU  867  O   SER B  50     1158   1046   1005     28    -76   -116       O  
ATOM    868  CB  SER B  50      40.620  -5.841 -11.264  1.00  9.21           C  
ANISOU  868  CB  SER B  50     1258   1107   1131     10    -63   -114       C  
ATOM    869  OG  SER B  50      41.998  -5.991 -11.573  1.00  9.92           O  
ANISOU  869  OG  SER B  50     1350   1186   1229      0    -57   -109       O  
ATOM    870  N   MET B  51      38.358  -7.552  -9.129  1.00  9.29           N  
ANISOU  870  N   MET B  51     1239   1230   1058     18    -78   -115       N  
ATOM    871  CA  MET B  51      37.089  -7.363  -8.444  1.00  9.15           C  
ANISOU  871  CA  MET B  51     1205   1245   1026     23    -80   -134       C  
ATOM    872  C   MET B  51      37.114  -6.017  -7.701  1.00 10.90           C  
ANISOU  872  C   MET B  51     1399   1478   1264     28    -83   -192       C  
ATOM    873  O   MET B  51      38.016  -5.770  -6.919  1.00 11.17           O  
ANISOU  873  O   MET B  51     1411   1540   1291     26    -84   -219       O  
ATOM    874  CB  MET B  51      36.851  -8.505  -7.445  1.00  9.37           C  
ANISOU  874  CB  MET B  51     1218   1331   1011     19    -79   -111       C  
ATOM    875  CG  MET B  51      35.587  -8.326  -6.619  1.00 10.10           C  
ANISOU  875  CG  MET B  51     1286   1469   1080     21    -77   -132       C  
ATOM    876  SD  MET B  51      35.128  -9.842  -5.737  1.00 11.61           S  
ANISOU  876  SD  MET B  51     1464   1719   1228     13    -69    -81       S  
ATOM    877  CE  MET B  51      36.631 -10.212  -4.791  1.00 11.72           C  
ANISOU  877  CE  MET B  51     1462   1778   1211     15    -72    -64       C  
ATOM    878  N   THR B  52      36.157  -5.156  -8.024  1.00 10.52           N  
ANISOU  878  N   THR B  52     1349   1405   1243     37    -86   -216       N  
ATOM    879  CA  THR B  52      36.058  -3.822  -7.419  1.00 11.49           C  
ANISOU  879  CA  THR B  52     1439   1526   1398     43    -89   -279       C  
ATOM    880  C   THR B  52      34.800  -3.645  -6.583  1.00 13.23           C  
ANISOU  880  C   THR B  52     1631   1795   1600     49    -94   -317       C  
ATOM    881  O   THR B  52      34.667  -2.610  -5.958  1.00 14.50           O  
ANISOU  881  O   THR B  52     1757   1964   1788     55    -98   -380       O  
ATOM    882  CB  THR B  52      36.117  -2.743  -8.504  1.00 12.07           C  
ANISOU  882  CB  THR B  52     1528   1520   1538     49    -89   -278       C  
ATOM    883  OG1 THR B  52      35.047  -2.934  -9.412  1.00 13.01           O  
ANISOU  883  OG1 THR B  52     1669   1615   1656     60    -92   -245       O  
ATOM    884  CG2 THR B  52      37.389  -2.829  -9.298  1.00 11.46           C  
ANISOU  884  CG2 THR B  52     1474   1403   1477     40    -80   -243       C  
ATOM    885  N   SER B  53      33.942  -4.659  -6.554  1.00 12.34           N  
ANISOU  885  N   SER B  53     1527   1714   1447     47    -92   -284       N  
ATOM    886  CA ASER B  53      32.757  -4.727  -5.692  0.50 14.57           C  
ANISOU  886  CA ASER B  53     1779   2055   1700     49    -92   -313       C  
ATOM    887  CA BSER B  53      32.793  -4.716  -5.663  0.50 14.58           C  
ANISOU  887  CA BSER B  53     1779   2057   1700     49    -92   -314       C  
ATOM    888  C   SER B  53      32.569  -6.183  -5.268  1.00 14.42           C  
ANISOU  888  C   SER B  53     1764   2088   1626     38    -83   -262       C  
ATOM    889  O   SER B  53      32.694  -7.085  -6.088  1.00 12.72           O  
ANISOU  889  O   SER B  53     1580   1838   1413     33    -79   -208       O  
ATOM    890  CB ASER B  53      31.502  -4.269  -6.433  0.50 18.99           C  
ANISOU  890  CB ASER B  53     2347   2578   2291     61    -97   -323       C  
ATOM    891  CB BSER B  53      31.556  -4.121  -6.332  0.50 18.71           C  
ANISOU  891  CB BSER B  53     2307   2544   2258     62    -98   -331       C  
ATOM    892  OG ASER B  53      30.325  -4.654  -5.726  0.50 19.30           O  
ANISOU  892  OG ASER B  53     2361   2675   2295     59    -94   -340       O  
ATOM    893  OG BSER B  53      31.678  -2.713  -6.458  0.50 17.56           O  
ANISOU  893  OG BSER B  53     2146   2355   2169     74   -106   -380       O  
ATOM    894  N   ARG B  54      32.268  -6.438  -3.985  1.00 16.14           N  
ANISOU  894  N   ARG B  54     1946   2390   1796     34    -78   -277       N  
ATOM    895  CA AARG B  54      32.052  -7.791  -3.482  0.50 16.03           C  
ANISOU  895  CA AARG B  54     1931   2425   1735     22    -66   -219       C  
ATOM    896  CA BARG B  54      32.059  -7.803  -3.474  0.50 16.96           C  
ANISOU  896  CA BARG B  54     2047   2543   1851     22    -66   -219       C  
ATOM    897  C   ARG B  54      30.762  -7.809  -2.676  1.00 18.27           C  
ANISOU  897  C   ARG B  54     2180   2775   1986     19    -58   -241       C  
ATOM    898  O   ARG B  54      30.602  -7.023  -1.742  1.00 17.27           O  
ANISOU  898  O   ARG B  54     2012   2710   1837     25    -61   -301       O  
ATOM    899  CB AARG B  54      33.217  -8.212  -2.602  0.50 15.48           C  
ANISOU  899  CB AARG B  54     1845   2409   1625     21    -65   -199       C  
ATOM    900  CB BARG B  54      33.235  -8.238  -2.590  0.50 18.05           C  
ANISOU  900  CB BARG B  54     2171   2735   1950     21    -65   -197       C  
ATOM    901  CG AARG B  54      33.116  -9.626  -2.064  0.50 15.82           C  
ANISOU  901  CG AARG B  54     1886   2497   1627     12    -52   -124       C  
ATOM    902  CG BARG B  54      33.232  -9.697  -2.120  0.50 19.91           C  
ANISOU  902  CG BARG B  54     2407   3010   2146     12    -53   -119       C  
ATOM    903  CD AARG B  54      34.384 -10.018  -1.334  0.50 16.18           C  
ANISOU  903  CD AARG B  54     1920   2589   1637     16    -56    -97       C  
ATOM    904  CD BARG B  54      34.618 -10.093  -1.615  0.50 25.62           C  
ANISOU  904  CD BARG B  54     3126   3762   2845     16    -58    -91       C  
ATOM    905  NE AARG B  54      34.776  -9.028  -0.336  0.50 17.06           N  
ANISOU  905  NE AARG B  54     1990   2776   1715     26    -64   -165       N  
ATOM    906  NE BARG B  54      34.685 -11.256  -0.718  0.50 26.87           N  
ANISOU  906  NE BARG B  54     3268   3986   2955     14    -48    -20       N  
ATOM    907  CZ AARG B  54      36.032  -8.668  -0.071  0.50 18.25           C  
ANISOU  907  CZ AARG B  54     2131   2941   1861     35    -75   -188       C  
ATOM    908  CZ BARG B  54      33.654 -11.999  -0.327  0.50 30.82           C  
ANISOU  908  CZ BARG B  54     3756   4518   3435      4    -31     22       C  
ATOM    909  NH1AARG B  54      37.051  -9.187  -0.747  0.50 21.33           N  
ANISOU  909  NH1AARG B  54     2553   3273   2277     35    -79   -147       N  
ATOM    910  NH1BARG B  54      32.427 -11.745  -0.755  0.50 34.13           N  
ANISOU  910  NH1BARG B  54     4177   4912   3875     -4    -24     -3       N  
ATOM    911  NH2AARG B  54      36.265  -7.763   0.863  0.50 18.50           N  
ANISOU  911  NH2AARG B  54     2115   3047   1864     44    -82   -262       N  
ATOM    912  NH2BARG B  54      33.856 -13.012   0.500  0.50 31.00           N  
ANISOU  912  NH2BARG B  54     3761   4598   3418      3    -21     96       N  
ATOM    913  N   GLU B  55      29.832  -8.680  -3.054  1.00 18.27           N  
ANISOU  913  N   GLU B  55     2191   2763   1988     10    -47   -202       N  
ATOM    914  CA  GLU B  55      28.501  -8.777  -2.440  1.00 24.01           C  
ANISOU  914  CA  GLU B  55     2886   3545   2689      4    -36   -219       C  
ATOM    915  C   GLU B  55      27.822  -7.408  -2.385  1.00 22.47           C  
ANISOU  915  C   GLU B  55     2668   3355   2514     18    -49   -306       C  
ATOM    916  O   GLU B  55      27.125  -7.080  -1.408  1.00 33.87           O  
ANISOU  916  O   GLU B  55     4067   4875   3924     17    -43   -349       O  
ATOM    917  CB  GLU B  55      28.570  -9.442  -1.056  1.00 23.36           C  
ANISOU  917  CB  GLU B  55     2768   3566   2541     -6    -20   -188       C  
ATOM    918  CG  GLU B  55      29.341 -10.739  -1.028  1.00 23.73           C  
ANISOU  918  CG  GLU B  55     2834   3605   2577    -15    -10    -99       C  
ATOM    919  CD  GLU B  55      28.657 -11.907  -1.748  1.00 27.10           C  
ANISOU  919  CD  GLU B  55     3281   3978   3038    -30      4    -41       C  
ATOM    920  OE1 GLU B  55      27.474 -11.808  -2.130  1.00 33.10           O  
ANISOU  920  OE1 GLU B  55     4035   4722   3817    -35      9    -67       O  
ATOM    921  OE2 GLU B  55      29.330 -12.946  -1.906  1.00 33.38           O  
ANISOU  921  OE2 GLU B  55     4092   4745   3844    -36     10     27       O  
ATOM    922  N   GLY B  56      28.018  -6.628  -3.444  1.00 20.68           N  
ANISOU  922  N   GLY B  56     2468   3046   2343     31    -64   -329       N  
ATOM    923  CA  GLY B  56      27.376  -5.319  -3.634  1.00 23.99           C  
ANISOU  923  CA  GLY B  56     2870   3443   2801     49    -78   -401       C  
ATOM    924  C   GLY B  56      28.061  -4.142  -2.948  1.00 34.35           C  
ANISOU  924  C   GLY B  56     4151   4773   4127     58    -88   -468       C  
ATOM    925  O   GLY B  56      27.592  -3.012  -3.082  1.00 37.90           O  
ANISOU  925  O   GLY B  56     4582   5195   4623     73   -100   -530       O  
ATOM    926  N   SER B  57      29.167  -4.370  -2.233  1.00 25.63           N  
ANISOU  926  N   SER B  57     3037   3711   2990     51    -84   -459       N  
ATOM    927  CA  SER B  57      29.852  -3.246  -1.577  1.00 25.66           C  
ANISOU  927  CA  SER B  57     3003   3734   3011     59    -93   -535       C  
ATOM    928  C   SER B  57      31.173  -2.942  -2.277  1.00 19.77           C  
ANISOU  928  C   SER B  57     2287   2914   2309     61    -98   -516       C  
ATOM    929  O   SER B  57      31.926  -3.868  -2.554  1.00 19.01           O  
ANISOU  929  O   SER B  57     2222   2810   2188     52    -93   -449       O  
ATOM    930  CB  SER B  57      30.029  -3.466  -0.067  1.00 34.44           C  
ANISOU  930  CB  SER B  57     4062   4973   4050     55    -87   -566       C  
ATOM    931  OG  SER B  57      30.543  -4.739   0.244  1.00 46.70           O  
ANISOU  931  OG  SER B  57     5631   6570   5541     43    -76   -486       O  
ATOM    932  N   PRO B  58      31.463  -1.642  -2.527  1.00 23.46           N  
ANISOU  932  N   PRO B  58     2740   3326   2846     71   -108   -577       N  
ATOM    933  CA  PRO B  58      32.651  -1.189  -3.254  1.00 21.72           C  
ANISOU  933  CA  PRO B  58     2544   3027   2679     71   -110   -563       C  
ATOM    934  C   PRO B  58      33.946  -1.425  -2.485  1.00 21.45           C  
ANISOU  934  C   PRO B  58     2491   3045   2613     63   -107   -575       C  
ATOM    935  O   PRO B  58      33.991  -1.229  -1.248  1.00 22.82           O  
ANISOU  935  O   PRO B  58     2611   3308   2749     65   -109   -637       O  
ATOM    936  CB  PRO B  58      32.399   0.311  -3.432  1.00 24.41           C  
ANISOU  936  CB  PRO B  58     2858   3308   3109     84   -118   -635       C  
ATOM    937  CG  PRO B  58      31.590   0.690  -2.224  1.00 30.13           C  
ANISOU  937  CG  PRO B  58     3520   4116   3810     89   -122   -720       C  
ATOM    938  CD  PRO B  58      30.681  -0.486  -2.008  1.00 28.56           C  
ANISOU  938  CD  PRO B  58     3336   3985   3531     83   -116   -671       C  
ATOM    939  N   LEU B  59      34.988  -1.795  -3.210  1.00 18.11           N  
ANISOU  939  N   LEU B  59     2106   2571   2202     56   -103   -521       N  
ATOM    940  CA  LEU B  59      36.323  -1.957  -2.692  1.00 15.61           C  
ANISOU  940  CA  LEU B  59     1776   2287   1867     51   -103   -531       C  
ATOM    941  C   LEU B  59      37.247  -0.828  -3.170  1.00 18.29           C  
ANISOU  941  C   LEU B  59     2109   2550   2289     49   -102   -572       C  
ATOM    942  O   LEU B  59      37.212  -0.429  -4.352  1.00 20.46           O  
ANISOU  942  O   LEU B  59     2418   2729   2623     49    -99   -539       O  
ATOM    943  CB  LEU B  59      36.888  -3.312  -3.141  1.00 14.11           C  
ANISOU  943  CB  LEU B  59     1630   2097   1633     43    -98   -440       C  
ATOM    944  CG  LEU B  59      36.047  -4.566  -2.908  1.00 16.10           C  
ANISOU  944  CG  LEU B  59     1896   2399   1822     41    -94   -380       C  
ATOM    945  CD1 LEU B  59      36.700  -5.806  -3.498  1.00 18.35           C  
ANISOU  945  CD1 LEU B  59     2220   2660   2089     34    -90   -298       C  
ATOM    946  CD2 LEU B  59      35.780  -4.748  -1.401  1.00 17.92           C  
ANISOU  946  CD2 LEU B  59     2074   2748   1984     44    -94   -412       C  
ATOM    947  N   GLU B  60      38.074  -0.312  -2.278  1.00 17.02           N  
ANISOU  947  N   GLU B  60     1900   2434   2132     49   -105   -643       N  
ATOM    948  CA  GLU B  60      39.085   0.676  -2.636  1.00 21.46           C  
ANISOU  948  CA  GLU B  60     2449   2927   2776     44   -101   -685       C  
ATOM    949  C   GLU B  60      40.223   0.068  -3.451  1.00 23.48           C  
ANISOU  949  C   GLU B  60     2749   3140   3031     33    -94   -616       C  
ATOM    950  O   GLU B  60      40.715   0.682  -4.406  1.00 27.53           O  
ANISOU  950  O   GLU B  60     3282   3560   3617     25    -84   -602       O  
ATOM    951  CB  GLU B  60      39.632   1.346  -1.374  1.00 25.09           C  
ANISOU  951  CB  GLU B  60     2834   3458   3238     47   -107   -794       C  
ATOM    952  CG  GLU B  60      40.870   2.188  -1.611  1.00 35.55           C  
ANISOU  952  CG  GLU B  60     4139   4723   4644     38   -101   -841       C  
ATOM    953  CD  GLU B  60      41.030   3.262  -0.557  1.00 38.64           C  
ANISOU  953  CD  GLU B  60     4446   5155   5077     42   -106   -974       C  
ATOM    954  OE1 GLU B  60      40.408   4.334  -0.696  1.00 39.95           O  
ANISOU  954  OE1 GLU B  60     4587   5260   5332     45   -105  -1029       O  
ATOM    955  OE2 GLU B  60      41.768   3.019   0.404  1.00 43.76           O  
ANISOU  955  OE2 GLU B  60     5051   5900   5672     45   -113  -1025       O  
ATOM    956  N   ASN B  61      40.667  -1.124  -3.069  1.00 17.49           N  
ANISOU  956  N   ASN B  61     2003   2449   2193     32    -97   -573       N  
ATOM    957  CA  ASN B  61      41.755  -1.780  -3.755  1.00 18.43           C  
ANISOU  957  CA  ASN B  61     2157   2537   2309     24    -92   -517       C  
ATOM    958  C   ASN B  61      41.221  -3.020  -4.435  1.00 17.30           C  
ANISOU  958  C   ASN B  61     2066   2385   2122     23    -90   -423       C  
ATOM    959  O   ASN B  61      40.576  -3.849  -3.809  1.00 18.55           O  
ANISOU  959  O   ASN B  61     2220   2608   2217     29    -95   -400       O  
ATOM    960  CB  ASN B  61      42.874  -2.165  -2.821  1.00 20.13           C  
ANISOU  960  CB  ASN B  61     2339   2828   2479     26    -98   -545       C  
ATOM    961  CG  ASN B  61      43.602  -0.947  -2.267  1.00 28.19           C  
ANISOU  961  CG  ASN B  61     3304   3852   3554     24    -98   -647       C  
ATOM    962  OD1 ASN B  61      43.827   0.038  -2.975  1.00 32.75           O  
ANISOU  962  OD1 ASN B  61     3883   4339   4221     14    -87   -671       O  
ATOM    963  ND2 ASN B  61      43.960  -1.011  -0.997  1.00 31.69           N  
ANISOU  963  ND2 ASN B  61     3694   4401   3946     34   -109   -706       N  
ATOM    964  N   PRO B  62      41.469  -3.136  -5.725  1.00 14.69           N  
ANISOU  964  N   PRO B  62     1778   1976   1826     16    -83   -373       N  
ATOM    965  CA  PRO B  62      40.947  -4.310  -6.418  1.00 12.93           C  
ANISOU  965  CA  PRO B  62     1597   1745   1568     17    -82   -297       C  
ATOM    966  C   PRO B  62      41.541  -5.631  -5.930  1.00 13.33           C  
ANISOU  966  C   PRO B  62     1650   1850   1562     17    -86   -260       C  
ATOM    967  O   PRO B  62      42.673  -5.680  -5.436  1.00 14.77           O  
ANISOU  967  O   PRO B  62     1813   2059   1736     16    -89   -279       O  
ATOM    968  CB  PRO B  62      41.292  -4.032  -7.878  1.00 15.03           C  
ANISOU  968  CB  PRO B  62     1899   1929   1882     10    -73   -263       C  
ATOM    969  CG  PRO B  62      41.502  -2.571  -7.969  1.00 22.50           C  
ANISOU  969  CG  PRO B  62     2825   2829   2894      8    -67   -310       C  
ATOM    970  CD  PRO B  62      42.074  -2.176  -6.652  1.00 17.31           C  
ANISOU  970  CD  PRO B  62     2119   2225   2232      8    -72   -381       C  
ATOM    971  N   VAL B  63      40.747  -6.684  -6.067  1.00 11.13           N  
ANISOU  971  N   VAL B  63     1390   1584   1252     18    -87   -208       N  
ATOM    972  CA  VAL B  63      41.128  -8.034  -5.635  1.00 11.50           C  
ANISOU  972  CA  VAL B  63     1439   1672   1256     20    -90   -160       C  
ATOM    973  C   VAL B  63      41.172  -8.966  -6.838  1.00  9.89           C  
ANISOU  973  C   VAL B  63     1272   1413   1071     15    -86   -106       C  
ATOM    974  O   VAL B  63      40.228  -9.020  -7.619  1.00 10.07           O  
ANISOU  974  O   VAL B  63     1314   1401   1108     13    -82    -91       O  
ATOM    975  CB  VAL B  63      40.128  -8.584  -4.620  1.00 11.03           C  
ANISOU  975  CB  VAL B  63     1359   1680   1149     24    -90   -145       C  
ATOM    976  CG1 VAL B  63      40.401 -10.048  -4.288  1.00 12.30           C  
ANISOU  976  CG1 VAL B  63     1524   1869   1278     26    -91    -78       C  
ATOM    977  CG2 VAL B  63      40.186  -7.736  -3.344  1.00 12.82           C  
ANISOU  977  CG2 VAL B  63     1540   1983   1348     31    -95   -206       C  
ATOM    978  N   ASP B  64      42.278  -9.670  -6.989  1.00 10.10           N  
ANISOU  978  N   ASP B  64     1304   1435   1098     14    -88    -83       N  
ATOM    979  CA  ASP B  64      42.421 -10.620  -8.080  1.00  8.83           C  
ANISOU  979  CA  ASP B  64     1169   1228    956     10    -86    -42       C  
ATOM    980  C   ASP B  64      41.508 -11.804  -7.973  1.00 10.08           C  
ANISOU  980  C   ASP B  64     1330   1393   1104     11    -85      1       C  
ATOM    981  O   ASP B  64      41.444 -12.452  -6.944  1.00 10.56           O  
ANISOU  981  O   ASP B  64     1373   1499   1138     15    -87     26       O  
ATOM    982  CB  ASP B  64      43.853 -11.206  -8.112  1.00 11.84           C  
ANISOU  982  CB  ASP B  64     1547   1609   1342     11    -90    -33       C  
ATOM    983  CG  ASP B  64      44.892 -10.271  -8.655  1.00 15.40           C  
ANISOU  983  CG  ASP B  64     1999   2033   1817      5    -87    -70       C  
ATOM    984  OD1 ASP B  64      44.628  -9.177  -9.226  1.00 12.40           O  
ANISOU  984  OD1 ASP B  64     1626   1622   1460     -1    -78    -95       O  
ATOM    985  OD2 ASP B  64      46.066 -10.708  -8.514  1.00 18.73           O  
ANISOU  985  OD2 ASP B  64     2411   2464   2239      6    -92    -70       O  
ATOM    986  N   VAL B  65      40.828 -12.125  -9.070  1.00  7.57           N  
ANISOU  986  N   VAL B  65     1032   1033    810      6    -80     12       N  
ATOM    987  CA  VAL B  65      40.000 -13.328  -9.170  1.00  7.82           C  
ANISOU  987  CA  VAL B  65     1064   1059    848      4    -77     48       C  
ATOM    988  C   VAL B  65      40.368 -14.035 -10.445  1.00  7.74           C  
ANISOU  988  C   VAL B  65     1067   1003    872      2    -76     54       C  
ATOM    989  O   VAL B  65      40.243 -13.469 -11.524  1.00  7.80           O  
ANISOU  989  O   VAL B  65     1088    985    889      1    -75     33       O  
ATOM    990  CB  VAL B  65      38.504 -12.984  -9.141  1.00  7.59           C  
ANISOU  990  CB  VAL B  65     1033   1037    812      3    -72     38       C  
ATOM    991  CG1 VAL B  65      37.660 -14.230  -9.265  1.00  9.44           C  
ANISOU  991  CG1 VAL B  65     1261   1261   1061     -1    -65     70       C  
ATOM    992  CG2 VAL B  65      38.177 -12.211  -7.866  1.00  9.71           C  
ANISOU  992  CG2 VAL B  65     1282   1360   1046      6    -72     20       C  
ATOM    993  N   PHE B  66      40.822 -15.275 -10.363  1.00  8.05           N  
ANISOU  993  N   PHE B  66     1097   1031    930      1    -78     84       N  
ATOM    994  CA  PHE B  66      41.186 -16.055 -11.565  1.00  9.16           C  
ANISOU  994  CA  PHE B  66     1241   1131   1108      0    -78     79       C  
ATOM    995  C   PHE B  66      39.980 -16.303 -12.418  1.00  7.78           C  
ANISOU  995  C   PHE B  66     1067    938    949     -3    -73     68       C  
ATOM    996  O   PHE B  66      38.888 -16.496 -11.896  1.00  7.65           O  
ANISOU  996  O   PHE B  66     1044    932    930     -6    -68     80       O  
ATOM    997  CB  PHE B  66      41.774 -17.375 -11.131  1.00  7.87           C  
ANISOU  997  CB  PHE B  66     1061    956    973      1    -81    113       C  
ATOM    998  CG  PHE B  66      42.195 -18.262 -12.286  1.00  8.13           C  
ANISOU  998  CG  PHE B  66     1087    947   1052      0    -83     98       C  
ATOM    999  CD1 PHE B  66      43.326 -17.978 -13.009  1.00  8.42           C  
ANISOU  999  CD1 PHE B  66     1128    978   1090      2    -87     70       C  
ATOM   1000  CD2 PHE B  66      41.448 -19.380 -12.637  1.00  8.34           C  
ANISOU 1000  CD2 PHE B  66     1099    944   1126     -3    -79    105       C  
ATOM   1001  CE1 PHE B  66      43.676 -18.809 -14.084  1.00  9.19           C  
ANISOU 1001  CE1 PHE B  66     1214   1048   1229      1    -89     48       C  
ATOM   1002  CE2 PHE B  66      41.815 -20.201 -13.693  1.00  9.78           C  
ANISOU 1002  CE2 PHE B  66     1266   1092   1355     -3    -81     78       C  
ATOM   1003  CZ  PHE B  66      42.942 -19.910 -14.409  1.00  9.84           C  
ANISOU 1003  CZ  PHE B  66     1278   1102   1357      0    -87     48       C  
ATOM   1004  N   VAL B  67      40.162 -16.272 -13.736  1.00  6.90           N  
ANISOU 1004  N   VAL B  67      962    809    850     -2    -74     41       N  
ATOM   1005  CA  VAL B  67      39.081 -16.553 -14.645  1.00  6.87           C  
ANISOU 1005  CA  VAL B  67      953    797    858     -2    -71     22       C  
ATOM   1006  C   VAL B  67      39.571 -17.425 -15.813  1.00  7.36           C  
ANISOU 1006  C   VAL B  67     1001    841    951     -1    -73      0       C  
ATOM   1007  O   VAL B  67      40.517 -17.061 -16.531  1.00  7.47           O  
ANISOU 1007  O   VAL B  67     1021    860    954      0    -75    -15       O  
ATOM   1008  CB  VAL B  67      38.352 -15.304 -15.209  1.00  6.60           C  
ANISOU 1008  CB  VAL B  67      935    779    794      4    -71      4       C  
ATOM   1009  CG1 VAL B  67      39.338 -14.309 -15.816  1.00  7.16           C  
ANISOU 1009  CG1 VAL B  67     1021    851    846      7    -72     -1       C  
ATOM   1010  CG2 VAL B  67      37.235 -15.692 -16.204  1.00  8.05           C  
ANISOU 1010  CG2 VAL B  67     1108    964    986      9    -72    -18       C  
ATOM   1011  N   HIS B  68      38.927 -18.575 -15.990  1.00  7.19           N  
ANISOU 1011  N   HIS B  68      957    801    972     -4    -71     -7       N  
ATOM   1012  CA  HIS B  68      39.225 -19.499 -17.075  1.00  8.15           C  
ANISOU 1012  CA  HIS B  68     1055    909   1133     -4    -73    -44       C  
ATOM   1013  C   HIS B  68      38.247 -19.272 -18.180  1.00  7.43           C  
ANISOU 1013  C   HIS B  68      955    838   1027      1    -74    -84       C  
ATOM   1014  O   HIS B  68      37.047 -18.991 -17.937  1.00  7.52           O  
ANISOU 1014  O   HIS B  68      970    859   1029      2    -72    -82       O  
ATOM   1015  CB  HIS B  68      39.189 -20.940 -16.599  1.00  8.00           C  
ANISOU 1015  CB  HIS B  68     1007    849   1184    -10    -71    -32       C  
ATOM   1016  CG  HIS B  68      39.787 -21.897 -17.582  1.00  8.52           C  
ANISOU 1016  CG  HIS B  68     1042    894   1300     -9    -75    -76       C  
ATOM   1017  ND1 HIS B  68      39.039 -22.655 -18.396  1.00 13.13           N  
ANISOU 1017  ND1 HIS B  68     1593   1468   1928    -10    -74   -123       N  
ATOM   1018  CD2 HIS B  68      41.107 -22.143 -17.902  1.00  9.51           C  
ANISOU 1018  CD2 HIS B  68     1161   1014   1438     -5    -82    -88       C  
ATOM   1019  CE1 HIS B  68      39.856 -23.379 -19.195  1.00 12.08           C  
ANISOU 1019  CE1 HIS B  68     1431   1324   1834     -7    -79   -167       C  
ATOM   1020  NE2 HIS B  68      41.118 -23.070 -18.888  1.00 10.09           N  
ANISOU 1020  NE2 HIS B  68     1196   1073   1562     -4    -84   -144       N  
ATOM   1021  N   GLN B  69      38.684 -19.451 -19.429  1.00  8.20           N  
ANISOU 1021  N   GLN B  69     1038    952   1123      7    -77   -125       N  
ATOM   1022  CA  GLN B  69      37.808 -19.282 -20.592  1.00  8.36           C  
ANISOU 1022  CA  GLN B  69     1044   1008   1123     17    -80   -168       C  
ATOM   1023  C   GLN B  69      36.516 -20.112 -20.528  1.00  7.79           C  
ANISOU 1023  C   GLN B  69      943    923   1093     14    -79   -194       C  
ATOM   1024  O   GLN B  69      35.490 -19.666 -20.993  1.00  8.95           O  
ANISOU 1024  O   GLN B  69     1088   1100   1213     24    -82   -212       O  
ATOM   1025  CB  GLN B  69      38.538 -19.649 -21.913  1.00  8.29           C  
ANISOU 1025  CB  GLN B  69     1009   1028   1110     23    -83   -216       C  
ATOM   1026  CG  GLN B  69      39.128 -21.061 -22.040  1.00  9.16           C  
ANISOU 1026  CG  GLN B  69     1081   1108   1292     16    -85   -253       C  
ATOM   1027  CD  GLN B  69      38.208 -22.094 -22.623  1.00 11.72           C  
ANISOU 1027  CD  GLN B  69     1356   1428   1666     18    -87   -314       C  
ATOM   1028  OE1 GLN B  69      37.039 -21.818 -22.922  1.00 11.35           O  
ANISOU 1028  OE1 GLN B  69     1305   1407   1598     24    -87   -330       O  
ATOM   1029  NE2 GLN B  69      38.719 -23.325 -22.729  1.00 13.18           N  
ANISOU 1029  NE2 GLN B  69     1502   1578   1928     12    -87   -350       N  
ATOM   1030  N   SER B  70      36.617 -21.289 -19.898  1.00  9.14           N  
ANISOU 1030  N   SER B  70     1091   1046   1335      2    -74   -190       N  
ATOM   1031  CA  SER B  70      35.468 -22.195 -19.816  1.00  9.32           C  
ANISOU 1031  CA  SER B  70     1080   1046   1415     -4    -68   -214       C  
ATOM   1032  C   SER B  70      34.330 -21.623 -18.963  1.00 11.07           C  
ANISOU 1032  C   SER B  70     1319   1273   1613     -8    -62   -181       C  
ATOM   1033  O   SER B  70      33.182 -22.100 -19.045  1.00 12.32           O  
ANISOU 1033  O   SER B  70     1451   1426   1803    -13    -57   -208       O  
ATOM   1034  CB  SER B  70      35.921 -23.566 -19.280  1.00  9.60           C  
ANISOU 1034  CB  SER B  70     1085   1019   1542    -18    -62   -205       C  
ATOM   1035  OG  SER B  70      36.322 -23.442 -17.953  1.00 13.75           O  
ANISOU 1035  OG  SER B  70     1637   1522   2065    -24    -57   -130       O  
ATOM   1036  N   LYS B  71      34.594 -20.580 -18.191  1.00  9.07           N  
ANISOU 1036  N   LYS B  71     1106   1033   1304     -6    -63   -132       N  
ATOM   1037  CA  LYS B  71      33.587 -19.975 -17.318  1.00  8.74           C  
ANISOU 1037  CA  LYS B  71     1078   1003   1238     -9    -57   -105       C  
ATOM   1038  C   LYS B  71      32.928 -18.741 -17.883  1.00  9.62           C  
ANISOU 1038  C   LYS B  71     1207   1156   1291      6    -66   -124       C  
ATOM   1039  O   LYS B  71      32.064 -18.124 -17.218  1.00  9.61           O  
ANISOU 1039  O   LYS B  71     1215   1166   1267      6    -63   -111       O  
ATOM   1040  CB  LYS B  71      34.226 -19.610 -15.972  1.00 10.34           C  
ANISOU 1040  CB  LYS B  71     1305   1200   1422    -16    -53    -45       C  
ATOM   1041  CG  LYS B  71      35.090 -20.671 -15.325  1.00 14.31           C  
ANISOU 1041  CG  LYS B  71     1795   1667   1973    -26    -48    -11       C  
ATOM   1042  CD  LYS B  71      34.393 -21.979 -15.146  1.00 18.09           C  
ANISOU 1042  CD  LYS B  71     2239   2108   2526    -39    -35     -8       C  
ATOM   1043  CE  LYS B  71      35.301 -22.952 -14.398  1.00 27.49           C  
ANISOU 1043  CE  LYS B  71     3417   3259   3765    -45    -31     40       C  
ATOM   1044  NZ  LYS B  71      34.580 -24.228 -14.146  1.00 30.22           N  
ANISOU 1044  NZ  LYS B  71     3725   3559   4197    -59    -15     54       N  
ATOM   1045  N   LEU B  72      33.323 -18.344 -19.081  1.00  7.81           N  
ANISOU 1045  N   LEU B  72      980    951   1034     21    -75   -152       N  
ATOM   1046  CA  LEU B  72      32.821 -17.111 -19.653  1.00  8.00           C  
ANISOU 1046  CA  LEU B  72     1021   1013   1003     40    -84   -156       C  
ATOM   1047  C   LEU B  72      31.507 -17.347 -20.371  1.00  7.63           C  
ANISOU 1047  C   LEU B  72      946    992    958     51    -90   -202       C  
ATOM   1048  O   LEU B  72      31.428 -18.194 -21.278  1.00 10.10           O  
ANISOU 1048  O   LEU B  72     1226   1318   1292     54    -92   -249       O  
ATOM   1049  CB  LEU B  72      33.830 -16.554 -20.607  1.00  7.15           C  
ANISOU 1049  CB  LEU B  72      927    928    862     51    -89   -155       C  
ATOM   1050  CG  LEU B  72      35.197 -16.155 -20.041  1.00  7.45           C  
ANISOU 1050  CG  LEU B  72      990    945    894     42    -85   -117       C  
ATOM   1051  CD1 LEU B  72      36.141 -15.590 -21.123  1.00  8.60           C  
ANISOU 1051  CD1 LEU B  72     1144   1116   1006     51    -86   -116       C  
ATOM   1052  CD2 LEU B  72      35.045 -15.126 -18.937  1.00  7.49           C  
ANISOU 1052  CD2 LEU B  72     1022    938    883     40    -83    -81       C  
ATOM   1053  N   TYR B  73      30.503 -16.540 -20.057  1.00  8.77           N  
ANISOU 1053  N   TYR B  73     1100   1151   1078     61    -93   -196       N  
ATOM   1054  CA  TYR B  73      29.205 -16.557 -20.740  1.00  8.99           C  
ANISOU 1054  CA  TYR B  73     1103   1211   1099     77   -102   -240       C  
ATOM   1055  C   TYR B  73      29.246 -15.687 -21.993  1.00  9.22           C  
ANISOU 1055  C   TYR B  73     1138   1289   1074    108   -117   -247       C  
ATOM   1056  O   TYR B  73      29.252 -14.435 -21.904  1.00 10.62           O  
ANISOU 1056  O   TYR B  73     1344   1472   1215    123   -124   -210       O  
ATOM   1057  CB  TYR B  73      28.109 -16.095 -19.782  1.00  9.94           C  
ANISOU 1057  CB  TYR B  73     1227   1327   1221     74    -99   -232       C  
ATOM   1058  CG  TYR B  73      26.749 -15.949 -20.469  1.00 10.20           C  
ANISOU 1058  CG  TYR B  73     1235   1397   1243     94   -110   -278       C  
ATOM   1059  CD1 TYR B  73      26.046 -17.053 -20.891  1.00 10.74           C  
ANISOU 1059  CD1 TYR B  73     1259   1471   1348     87   -107   -332       C  
ATOM   1060  CD2 TYR B  73      26.209 -14.686 -20.710  1.00  9.90           C  
ANISOU 1060  CD2 TYR B  73     1213   1386   1162    121   -125   -269       C  
ATOM   1061  CE1 TYR B  73      24.825 -16.913 -21.521  1.00 11.61           C  
ANISOU 1061  CE1 TYR B  73     1341   1622   1447    108   -119   -381       C  
ATOM   1062  CE2 TYR B  73      24.973 -14.521 -21.361  1.00 10.78           C  
ANISOU 1062  CE2 TYR B  73     1299   1536   1259    145   -139   -311       C  
ATOM   1063  CZ  TYR B  73      24.310 -15.653 -21.757  1.00 12.27           C  
ANISOU 1063  CZ  TYR B  73     1444   1738   1480    138   -136   -369       C  
ATOM   1064  OH  TYR B  73      23.099 -15.532 -22.389  1.00 13.51           O  
ANISOU 1064  OH  TYR B  73     1570   1939   1623    162   -150   -417       O  
ATOM   1065  N   MET B  74      29.348 -16.358 -23.144  1.00  9.79           N  
ANISOU 1065  N   MET B  74     1179   1396   1144    117   -123   -291       N  
ATOM   1066  CA  MET B  74      29.303 -15.760 -24.478  1.00  9.61           C  
ANISOU 1066  CA  MET B  74     1149   1437   1062    149   -137   -301       C  
ATOM   1067  C   MET B  74      29.307 -16.877 -25.499  1.00 12.13           C  
ANISOU 1067  C   MET B  74     1418   1796   1393    152   -140   -371       C  
ATOM   1068  O   MET B  74      29.719 -18.011 -25.205  1.00 12.43           O  
ANISOU 1068  O   MET B  74     1435   1799   1490    128   -130   -401       O  
ATOM   1069  CB  MET B  74      30.508 -14.841 -24.707  1.00 10.31           C  
ANISOU 1069  CB  MET B  74     1274   1528   1113    154   -135   -244       C  
ATOM   1070  CG  MET B  74      31.841 -15.537 -24.534  1.00 11.16           C  
ANISOU 1070  CG  MET B  74     1384   1608   1247    130   -122   -242       C  
ATOM   1071  SD  MET B  74      33.228 -14.457 -24.163  1.00 11.37           S  
ANISOU 1071  SD  MET B  74     1458   1609   1253    122   -113   -171       S  
ATOM   1072  CE  MET B  74      33.242 -13.441 -25.543  1.00  9.91           C  
ANISOU 1072  CE  MET B  74     1275   1490   1001    153   -120   -149       C  
ATOM   1073  N   GLU B  75      28.928 -16.527 -26.714  1.00 11.58           N  
ANISOU 1073  N   GLU B  75     1327   1803   1268    184   -155   -396       N  
ATOM   1074  CA  GLU B  75      28.972 -17.424 -27.849  1.00 13.60           C  
ANISOU 1074  CA  GLU B  75     1528   2119   1519    194   -161   -470       C  
ATOM   1075  C   GLU B  75      30.361 -17.434 -28.481  1.00 14.00           C  
ANISOU 1075  C   GLU B  75     1583   2193   1541    192   -156   -456       C  
ATOM   1076  O   GLU B  75      31.125 -16.502 -28.327  1.00 15.43           O  
ANISOU 1076  O   GLU B  75     1809   2364   1688    192   -151   -384       O  
ATOM   1077  CB  GLU B  75      27.993 -16.988 -28.925  1.00 13.65           C  
ANISOU 1077  CB  GLU B  75     1505   2217   1463    234   -181   -502       C  
ATOM   1078  CG  GLU B  75      26.535 -17.083 -28.600  1.00 13.76           C  
ANISOU 1078  CG  GLU B  75     1499   2229   1499    242   -189   -539       C  
ATOM   1079  CD  GLU B  75      25.696 -16.540 -29.751  1.00 16.00           C  
ANISOU 1079  CD  GLU B  75     1753   2614   1709    289   -212   -564       C  
ATOM   1080  OE1 GLU B  75      25.522 -15.300 -29.815  1.00 15.79           O  
ANISOU 1080  OE1 GLU B  75     1763   2604   1629    315   -222   -495       O  
ATOM   1081  OE2 GLU B  75      25.312 -17.360 -30.606  1.00 17.62           O  
ANISOU 1081  OE2 GLU B  75     1897   2885   1913    300   -221   -652       O  
ATOM   1082  N   GLY B  76      30.636 -18.479 -29.239  1.00 13.03           N  
ANISOU 1082  N   GLY B  76     1407   2107   1436    190   -157   -532       N  
ATOM   1083  CA  GLY B  76      31.851 -18.530 -30.018  1.00 14.28           C  
ANISOU 1083  CA  GLY B  76     1557   2307   1559    192   -153   -534       C  
ATOM   1084  C   GLY B  76      33.081 -18.672 -29.139  1.00 14.21           C  
ANISOU 1084  C   GLY B  76     1584   2218   1595    161   -138   -489       C  
ATOM   1085  O   GLY B  76      33.062 -19.249 -28.067  1.00 13.85           O  
ANISOU 1085  O   GLY B  76     1548   2089   1623    136   -130   -485       O  
ATOM   1086  N   PHE B  77      34.168 -18.129 -29.636  1.00 14.93           N  
ANISOU 1086  N   PHE B  77     1692   2341   1637    164   -132   -454       N  
ATOM   1087  CA  PHE B  77      35.442 -18.175 -28.929  1.00 13.40           C  
ANISOU 1087  CA  PHE B  77     1528   2084   1476    138   -119   -415       C  
ATOM   1088  C   PHE B  77      35.310 -17.303 -27.683  1.00 11.29           C  
ANISOU 1088  C   PHE B  77     1320   1746   1221    127   -114   -336       C  
ATOM   1089  O   PHE B  77      34.850 -16.155 -27.793  1.00 12.62           O  
ANISOU 1089  O   PHE B  77     1517   1936   1341    144   -116   -286       O  
ATOM   1090  CB  PHE B  77      36.564 -17.673 -29.819  1.00 16.21           C  
ANISOU 1090  CB  PHE B  77     1886   2501   1771    144   -112   -396       C  
ATOM   1091  CG  PHE B  77      37.937 -17.923 -29.240  1.00 12.73           C  
ANISOU 1091  CG  PHE B  77     1462   2005   1369    118   -100   -378       C  
ATOM   1092  CD1 PHE B  77      38.599 -19.115 -29.453  1.00 13.64           C  
ANISOU 1092  CD1 PHE B  77     1534   2115   1531    106   -100   -446       C  
ATOM   1093  CD2 PHE B  77      38.543 -16.974 -28.441  1.00 12.14           C  
ANISOU 1093  CD2 PHE B  77     1442   1881   1289    106    -90   -299       C  
ATOM   1094  CE1 PHE B  77      39.843 -19.342 -28.912  1.00 12.81           C  
ANISOU 1094  CE1 PHE B  77     1443   1962   1462     86    -91   -431       C  
ATOM   1095  CE2 PHE B  77      39.790 -17.201 -27.896  1.00 12.31           C  
ANISOU 1095  CE2 PHE B  77     1475   1858   1344     85    -80   -288       C  
ATOM   1096  CZ  PHE B  77      40.440 -18.391 -28.122  1.00 12.13           C  
ANISOU 1096  CZ  PHE B  77     1412   1833   1363     76    -82   -351       C  
ATOM   1097  N   ARG B  78      35.686 -17.833 -26.529  1.00 10.00           N  
ANISOU 1097  N   ARG B  78     1171   1504   1122    102   -107   -325       N  
ATOM   1098  CA  ARG B  78      35.524 -17.141 -25.264  1.00  9.19           C  
ANISOU 1098  CA  ARG B  78     1114   1343   1033     92   -102   -263       C  
ATOM   1099  C   ARG B  78      36.778 -16.377 -24.861  1.00  8.56           C  
ANISOU 1099  C   ARG B  78     1071   1241    937     82    -93   -209       C  
ATOM   1100  O   ARG B  78      37.875 -16.949 -24.763  1.00  9.46           O  
ANISOU 1100  O   ARG B  78     1178   1338   1076     68    -88   -218       O  
ATOM   1101  CB  ARG B  78      35.148 -18.125 -24.180  1.00  9.92           C  
ANISOU 1101  CB  ARG B  78     1196   1373   1197     73   -100   -276       C  
ATOM   1102  CG  ARG B  78      33.776 -18.773 -24.453  1.00 10.89           C  
ANISOU 1102  CG  ARG B  78     1282   1510   1344     79   -105   -328       C  
ATOM   1103  CD  ARG B  78      33.408 -19.875 -23.486  1.00 10.74           C  
ANISOU 1103  CD  ARG B  78     1245   1429   1406     58    -98   -339       C  
ATOM   1104  NE  ARG B  78      34.286 -21.026 -23.602  1.00 10.10           N  
ANISOU 1104  NE  ARG B  78     1134   1317   1383     45    -94   -369       N  
ATOM   1105  CZ  ARG B  78      34.096 -22.051 -24.421  1.00 13.20           C  
ANISOU 1105  CZ  ARG B  78     1472   1722   1820     47    -97   -444       C  
ATOM   1106  NH1 ARG B  78      33.009 -22.119 -25.189  1.00 15.55           N  
ANISOU 1106  NH1 ARG B  78     1736   2066   2106     60   -103   -501       N  
ATOM   1107  NH2 ARG B  78      34.977 -23.033 -24.438  1.00 17.04           N  
ANISOU 1107  NH2 ARG B  78     1931   2172   2368     36    -94   -468       N  
ATOM   1108  N   SER B  79      36.635 -15.089 -24.597  1.00  9.24           N  
ANISOU 1108  N   SER B  79     1194   1325    992     89    -92   -156       N  
ATOM   1109  CA  SER B  79      37.721 -14.304 -24.078  1.00  8.80           C  
ANISOU 1109  CA  SER B  79     1169   1241    933     77    -82   -110       C  
ATOM   1110  C   SER B  79      37.148 -13.082 -23.365  1.00  8.92           C  
ANISOU 1110  C   SER B  79     1215   1231    941     83    -82    -67       C  
ATOM   1111  O   SER B  79      35.951 -12.816 -23.453  1.00  7.96           O  
ANISOU 1111  O   SER B  79     1092   1122    810     99    -91    -71       O  
ATOM   1112  CB  SER B  79      38.669 -13.888 -25.215  1.00  9.71           C  
ANISOU 1112  CB  SER B  79     1280   1400   1007     82    -74   -100       C  
ATOM   1113  OG  SER B  79      38.079 -12.930 -26.016  1.00 10.86           O  
ANISOU 1113  OG  SER B  79     1432   1588   1106    104    -75    -71       O  
ATOM   1114  N   LEU B  80      38.024 -12.355 -22.667  1.00  8.39           N  
ANISOU 1114  N   LEU B  80     1173   1131    885     70    -73    -33       N  
ATOM   1115  CA  LEU B  80      37.693 -11.066 -22.124  1.00  7.69           C  
ANISOU 1115  CA  LEU B  80     1107   1018    796     76    -72      0       C  
ATOM   1116  C   LEU B  80      38.643 -10.035 -22.706  1.00  8.26           C  
ANISOU 1116  C   LEU B  80     1192   1090    854     75    -60     37       C  
ATOM   1117  O   LEU B  80      39.829 -10.355 -22.992  1.00  9.28           O  
ANISOU 1117  O   LEU B  80     1317   1225    982     61    -49     35       O  
ATOM   1118  CB  LEU B  80      37.805 -11.037 -20.607  1.00  7.83           C  
ANISOU 1118  CB  LEU B  80     1134    994    845     60    -71      0       C  
ATOM   1119  CG  LEU B  80      36.809 -11.854 -19.812  1.00  7.51           C  
ANISOU 1119  CG  LEU B  80     1083    950    821     58    -79    -22       C  
ATOM   1120  CD1 LEU B  80      37.138 -11.840 -18.319  1.00  8.28           C  
ANISOU 1120  CD1 LEU B  80     1185   1022    937     43    -76    -16       C  
ATOM   1121  CD2 LEU B  80      35.388 -11.356 -20.061  1.00  8.44           C  
ANISOU 1121  CD2 LEU B  80     1198   1081    926     77    -87    -26       C  
ATOM   1122  N   LYS B  81      38.165  -8.805 -22.835  1.00  9.29           N  
ANISOU 1122  N   LYS B  81     1336   1211    982     89    -59     72       N  
ATOM   1123  CA  LYS B  81      39.001  -7.666 -23.221  1.00 10.83           C  
ANISOU 1123  CA  LYS B  81     1542   1390   1180     86    -43    116       C  
ATOM   1124  C   LYS B  81      39.405  -6.932 -21.972  1.00 12.06           C  
ANISOU 1124  C   LYS B  81     1709   1489   1383     71    -38    117       C  
ATOM   1125  O   LYS B  81      38.600  -6.749 -21.054  1.00 10.27           O  
ANISOU 1125  O   LYS B  81     1484   1242   1175     75    -49    100       O  
ATOM   1126  CB  LYS B  81      38.206  -6.724 -24.128  1.00 13.51           C  
ANISOU 1126  CB  LYS B  81     1885   1748   1500    114    -46    160       C  
ATOM   1127  CG  LYS B  81      38.849  -5.416 -24.564  1.00 17.73           C  
ANISOU 1127  CG  LYS B  81     2428   2258   2048    115    -28    221       C  
ATOM   1128  CD  LYS B  81      37.846  -4.630 -25.432  1.00 23.17           C  
ANISOU 1128  CD  LYS B  81     3117   2967   2716    149    -36    269       C  
ATOM   1129  CE  LYS B  81      38.310  -3.198 -25.698  1.00 36.54           C  
ANISOU 1129  CE  LYS B  81     4820   4618   4445    151    -18    340       C  
ATOM   1130  NZ  LYS B  81      39.083  -3.100 -26.963  1.00 43.36           N  
ANISOU 1130  NZ  LYS B  81     5677   5530   5264    152      1    393       N  
ATOM   1131  N   GLU B  82      40.669  -6.497 -21.904  1.00 11.41           N  
ANISOU 1131  N   GLU B  82     1630   1386   1319     53    -21    130       N  
ATOM   1132  CA  GLU B  82      41.136  -5.688 -20.762  1.00 10.11           C  
ANISOU 1132  CA  GLU B  82     1467   1171   1200     39    -15    122       C  
ATOM   1133  C   GLU B  82      40.206  -4.546 -20.487  1.00  9.93           C  
ANISOU 1133  C   GLU B  82     1448   1116   1207     54    -20    136       C  
ATOM   1134  O   GLU B  82      39.859  -3.811 -21.430  1.00 12.10           O  
ANISOU 1134  O   GLU B  82     1728   1389   1480     70    -15    181       O  
ATOM   1135  CB  GLU B  82      42.576  -5.136 -20.964  1.00 12.68           C  
ANISOU 1135  CB  GLU B  82     1792   1477   1548     19      6    137       C  
ATOM   1136  CG  GLU B  82      43.626  -6.212 -20.939  1.00 13.71           C  
ANISOU 1136  CG  GLU B  82     1914   1632   1662      2      9    111       C  
ATOM   1137  CD  GLU B  82      45.069  -5.740 -20.834  1.00 12.11           C  
ANISOU 1137  CD  GLU B  82     1705   1409   1485    -20     30    110       C  
ATOM   1138  OE1 GLU B  82      45.352  -4.505 -20.847  1.00 17.07           O  
ANISOU 1138  OE1 GLU B  82     2333   1999   2151    -26     46    134       O  
ATOM   1139  OE2 GLU B  82      45.930  -6.648 -20.823  1.00 14.60           O  
ANISOU 1139  OE2 GLU B  82     2012   1746   1788    -31     30     86       O  
ATOM   1140  N   GLY B  83      39.846  -4.364 -19.220  1.00 10.33           N  
ANISOU 1140  N   GLY B  83     1493   1145   1284     51    -29    101       N  
ATOM   1141  CA  GLY B  83      38.955  -3.315 -18.787  1.00 10.35           C  
ANISOU 1141  CA  GLY B  83     1492   1116   1322     65    -35     99       C  
ATOM   1142  C   GLY B  83      37.490  -3.543 -18.938  1.00 11.07           C  
ANISOU 1142  C   GLY B  83     1584   1229   1392     89    -53     95       C  
ATOM   1143  O   GLY B  83      36.727  -2.697 -18.488  1.00 12.22           O  
ANISOU 1143  O   GLY B  83     1724   1350   1570    101    -61     86       O  
ATOM   1144  N   GLU B  84      37.079  -4.618 -19.623  1.00 10.42           N  
ANISOU 1144  N   GLU B  84     1505   1192   1261     96    -60     98       N  
ATOM   1145  CA  GLU B  84      35.623  -4.763 -19.827  1.00 10.39           C  
ANISOU 1145  CA  GLU B  84     1496   1209   1240    119    -77     90       C  
ATOM   1146  C   GLU B  84      34.972  -5.094 -18.492  1.00 10.03           C  
ANISOU 1146  C   GLU B  84     1441   1162   1205    112    -86     44       C  
ATOM   1147  O   GLU B  84      35.523  -5.850 -17.683  1.00  9.22           O  
ANISOU 1147  O   GLU B  84     1335   1068   1099     91    -82     22       O  
ATOM   1148  CB  GLU B  84      35.233  -5.769 -20.901  1.00 10.86           C  
ANISOU 1148  CB  GLU B  84     1553   1320   1252    130    -83     94       C  
ATOM   1149  CG  GLU B  84      35.328  -7.239 -20.515  1.00 10.70           C  
ANISOU 1149  CG  GLU B  84     1524   1324   1216    113    -85     56       C  
ATOM   1150  CD  GLU B  84      34.677  -8.080 -21.621  1.00  9.12           C  
ANISOU 1150  CD  GLU B  84     1311   1172    979    129    -94     46       C  
ATOM   1151  OE1 GLU B  84      33.417  -8.205 -21.643  1.00 11.38           O  
ANISOU 1151  OE1 GLU B  84     1588   1475   1260    145   -107     27       O  
ATOM   1152  OE2 GLU B  84      35.379  -8.634 -22.495  1.00  9.60           O  
ANISOU 1152  OE2 GLU B  84     1368   1262   1018    125    -88     49       O  
ATOM   1153  N   PRO B  85      33.767  -4.535 -18.243  1.00 10.05           N  
ANISOU 1153  N   PRO B  85     1436   1161   1220    131    -98     32       N  
ATOM   1154  CA  PRO B  85      33.093  -4.783 -16.986  1.00  8.49           C  
ANISOU 1154  CA  PRO B  85     1224    972   1028    124   -104    -11       C  
ATOM   1155  C   PRO B  85      32.465  -6.151 -16.937  1.00  9.19           C  
ANISOU 1155  C   PRO B  85     1307   1100   1083    118   -107    -28       C  
ATOM   1156  O   PRO B  85      31.905  -6.647 -17.920  1.00  9.37           O  
ANISOU 1156  O   PRO B  85     1330   1145   1085    131   -113    -21       O  
ATOM   1157  CB  PRO B  85      31.999  -3.668 -16.937  1.00  9.90           C  
ANISOU 1157  CB  PRO B  85     1394   1133   1234    148   -116    -20       C  
ATOM   1158  CG  PRO B  85      31.775  -3.318 -18.374  1.00 11.34           C  
ANISOU 1158  CG  PRO B  85     1587   1314   1408    174   -121     24       C  
ATOM   1159  CD  PRO B  85      33.094  -3.493 -19.054  1.00 10.82           C  
ANISOU 1159  CD  PRO B  85     1534   1242   1331    160   -106     61       C  
ATOM   1160  N   VAL B  86      32.548  -6.782 -15.785  1.00  8.27           N  
ANISOU 1160  N   VAL B  86     1181    996    964     99   -103    -51       N  
ATOM   1161  CA  VAL B  86      32.023  -8.123 -15.607  1.00 10.12           C  
ANISOU 1161  CA  VAL B  86     1405   1258   1179     89   -102    -61       C  
ATOM   1162  C   VAL B  86      31.304  -8.254 -14.283  1.00  9.08           C  
ANISOU 1162  C   VAL B  86     1256   1145   1047     80   -100    -86       C  
ATOM   1163  O   VAL B  86      31.563  -7.516 -13.328  1.00  9.31           O  
ANISOU 1163  O   VAL B  86     1278   1173   1083     77    -99    -99       O  
ATOM   1164  CB  VAL B  86      33.140  -9.210 -15.666  1.00  8.16           C  
ANISOU 1164  CB  VAL B  86     1162   1012    927     70    -93    -46       C  
ATOM   1165  CG1 VAL B  86      33.681  -9.365 -17.082  1.00  9.03           C  
ANISOU 1165  CG1 VAL B  86     1282   1119   1029     78    -93    -30       C  
ATOM   1166  CG2 VAL B  86      34.256  -8.931 -14.680  1.00 10.07           C  
ANISOU 1166  CG2 VAL B  86     1405   1245   1174     56    -86    -43       C  
ATOM   1167  N   GLU B  87      30.386  -9.212 -14.237  1.00  9.01           N  
ANISOU 1167  N   GLU B  87     1234   1157   1031     76    -99    -95       N  
ATOM   1168  CA  GLU B  87      29.750  -9.671 -13.003  1.00  9.07           C  
ANISOU 1168  CA  GLU B  87     1221   1191   1032     62    -91   -108       C  
ATOM   1169  C   GLU B  87      30.048 -11.146 -12.907  1.00  8.70           C  
ANISOU 1169  C   GLU B  87     1169   1148    987     43    -80    -87       C  
ATOM   1170  O   GLU B  87      30.130 -11.821 -13.931  1.00  9.96           O  
ANISOU 1170  O   GLU B  87     1333   1294   1157     45    -82    -83       O  
ATOM   1171  CB  GLU B  87      28.211  -9.490 -13.091  1.00 11.44           C  
ANISOU 1171  CB  GLU B  87     1504   1508   1333     73    -97   -137       C  
ATOM   1172  CG  GLU B  87      27.755  -8.042 -13.143  1.00 12.22           C  
ANISOU 1172  CG  GLU B  87     1602   1599   1441     95   -110   -160       C  
ATOM   1173  CD  GLU B  87      26.235  -7.900 -13.332  1.00 13.01           C  
ANISOU 1173  CD  GLU B  87     1683   1716   1543    110   -119   -191       C  
ATOM   1174  OE1 GLU B  87      25.516  -8.922 -13.397  1.00 14.89           O  
ANISOU 1174  OE1 GLU B  87     1907   1974   1774    100   -112   -199       O  
ATOM   1175  OE2 GLU B  87      25.778  -6.734 -13.467  1.00 17.41           O  
ANISOU 1175  OE2 GLU B  87     2237   2262   2114    133   -132   -210       O  
ATOM   1176  N   PHE B  88      30.153 -11.683 -11.721  1.00  8.11           N  
ANISOU 1176  N   PHE B  88     1082   1094    905     26    -69    -75       N  
ATOM   1177  CA  PHE B  88      30.519 -13.074 -11.584  1.00  9.10           C  
ANISOU 1177  CA  PHE B  88     1200   1213   1043      9    -58    -45       C  
ATOM   1178  C   PHE B  88      30.117 -13.699 -10.268  1.00  9.53           C  
ANISOU 1178  C   PHE B  88     1233   1299   1088     -6    -44    -25       C  
ATOM   1179  O   PHE B  88      29.936 -13.028  -9.252  1.00 10.31           O  
ANISOU 1179  O   PHE B  88     1321   1435   1158     -6    -42    -32       O  
ATOM   1180  CB  PHE B  88      32.057 -13.249 -11.814  1.00  8.70           C  
ANISOU 1180  CB  PHE B  88     1167   1143    996      8    -61    -23       C  
ATOM   1181  CG  PHE B  88      32.897 -12.287 -11.033  1.00  8.69           C  
ANISOU 1181  CG  PHE B  88     1172   1156    974     11    -64    -24       C  
ATOM   1182  CD1 PHE B  88      33.200 -11.026 -11.522  1.00  8.57           C  
ANISOU 1182  CD1 PHE B  88     1170   1127    959     23    -73    -45       C  
ATOM   1183  CD2 PHE B  88      33.309 -12.591  -9.757  1.00  9.74           C  
ANISOU 1183  CD2 PHE B  88     1291   1321   1089      2    -59     -5       C  
ATOM   1184  CE1 PHE B  88      33.885 -10.102 -10.766  1.00 10.26           C  
ANISOU 1184  CE1 PHE B  88     1380   1351   1164     25    -75    -57       C  
ATOM   1185  CE2 PHE B  88      34.017 -11.645  -8.990  1.00 11.48           C  
ANISOU 1185  CE2 PHE B  88     1508   1565   1289      7    -63    -20       C  
ATOM   1186  CZ  PHE B  88      34.314 -10.415  -9.492  1.00 10.43           C  
ANISOU 1186  CZ  PHE B  88     1386   1411   1165     16    -71    -51       C  
ATOM   1187  N   THR B  89      30.025 -15.013 -10.311  1.00 10.04           N  
ANISOU 1187  N   THR B  89     1286   1349   1180    -20    -32      1       N  
ATOM   1188  CA  THR B  89      30.053 -15.819  -9.114  1.00  9.72           C  
ANISOU 1188  CA  THR B  89     1226   1330   1135    -36    -15     46       C  
ATOM   1189  C   THR B  89      31.500 -16.346  -8.975  1.00 11.44           C  
ANISOU 1189  C   THR B  89     1454   1531   1360    -36    -18     84       C  
ATOM   1190  O   THR B  89      32.196 -16.580  -9.962  1.00 10.12           O  
ANISOU 1190  O   THR B  89     1301   1324   1219    -31    -27     76       O  
ATOM   1191  CB  THR B  89      29.080 -16.996  -9.207  1.00 11.92           C  
ANISOU 1191  CB  THR B  89     1481   1593   1454    -53      1     59       C  
ATOM   1192  OG1 THR B  89      29.324 -17.708 -10.420  1.00 13.16           O  
ANISOU 1192  OG1 THR B  89     1641   1698   1660    -52     -2     46       O  
ATOM   1193  CG2 THR B  89      27.586 -16.531  -9.210  1.00 13.81           C  
ANISOU 1193  CG2 THR B  89     1704   1856   1685    -54      6     18       C  
ATOM   1194  N   PHE B  90      31.924 -16.583  -7.754  1.00 11.01           N  
ANISOU 1194  N   PHE B  90     1388   1513   1280    -41    -11    126       N  
ATOM   1195  CA  PHE B  90      33.277 -17.007  -7.464  1.00 11.18           C  
ANISOU 1195  CA  PHE B  90     1416   1528   1303    -37    -16    163       C  
ATOM   1196  C   PHE B  90      33.333 -17.749  -6.135  1.00 13.11           C  
ANISOU 1196  C   PHE B  90     1637   1814   1529    -43     -3    227       C  
ATOM   1197  O   PHE B  90      32.361 -17.779  -5.374  1.00 13.18           O  
ANISOU 1197  O   PHE B  90     1626   1865   1516    -52     11    240       O  
ATOM   1198  CB  PHE B  90      34.272 -15.861  -7.510  1.00 11.56           C  
ANISOU 1198  CB  PHE B  90     1480   1590   1319    -23    -33    131       C  
ATOM   1199  CG  PHE B  90      34.208 -14.908  -6.353  1.00 13.41           C  
ANISOU 1199  CG  PHE B  90     1702   1892   1500    -18    -34    116       C  
ATOM   1200  CD1 PHE B  90      33.257 -13.903  -6.341  1.00 11.10           C  
ANISOU 1200  CD1 PHE B  90     1405   1618   1192    -16    -35     69       C  
ATOM   1201  CD2 PHE B  90      35.161 -14.925  -5.341  1.00 14.04           C  
ANISOU 1201  CD2 PHE B  90     1769   2017   1545    -12    -38    140       C  
ATOM   1202  CE1 PHE B  90      33.222 -12.953  -5.316  1.00 12.97           C  
ANISOU 1202  CE1 PHE B  90     1623   1917   1386    -10    -38     40       C  
ATOM   1203  CE2 PHE B  90      35.119 -13.997  -4.305  1.00 13.92           C  
ANISOU 1203  CE2 PHE B  90     1735   2073   1479     -6    -40    111       C  
ATOM   1204  CZ  PHE B  90      34.143 -13.013  -4.318  1.00 14.06           C  
ANISOU 1204  CZ  PHE B  90     1746   2105   1488     -6    -40     58       C  
ATOM   1205  N   LYS B  91      34.457 -18.377  -5.904  1.00 12.35           N  
ANISOU 1205  N   LYS B  91     1541   1707   1443    -38     -8    269       N  
ATOM   1206  CA  LYS B  91      34.655 -19.134  -4.677  1.00 13.02           C  
ANISOU 1206  CA  LYS B  91     1603   1832   1510    -38      2    344       C  
ATOM   1207  C   LYS B  91      36.079 -18.923  -4.214  1.00 14.27           C  
ANISOU 1207  C   LYS B  91     1765   2018   1638    -21    -14    357       C  
ATOM   1208  O   LYS B  91      36.978 -18.594  -4.980  1.00 15.66           O  
ANISOU 1208  O   LYS B  91     1960   2159   1830    -13    -29    320       O  
ATOM   1209  CB  LYS B  91      34.437 -20.635  -4.879  1.00 15.54           C  
ANISOU 1209  CB  LYS B  91     1908   2093   1901    -50     17    404       C  
ATOM   1210  CG  LYS B  91      35.416 -21.299  -5.819  1.00 16.56           C  
ANISOU 1210  CG  LYS B  91     2048   2148   2094    -44      5    401       C  
ATOM   1211  CD  LYS B  91      35.099 -22.770  -5.920  1.00 20.13           C  
ANISOU 1211  CD  LYS B  91     2478   2540   2630    -56     22    455       C  
ATOM   1212  CE  LYS B  91      36.028 -23.478  -6.874  1.00 24.95           C  
ANISOU 1212  CE  LYS B  91     3090   3076   3311    -49      9    441       C  
ATOM   1213  NZ  LYS B  91      35.817 -24.956  -6.826  1.00 33.78           N  
ANISOU 1213  NZ  LYS B  91     4180   4130   4525    -59     25    498       N  
ATOM   1214  N   LYS B  92      36.297 -19.215  -2.928  1.00 15.35           N  
ANISOU 1214  N   LYS B  92     1879   2223   1730    -14     -9    416       N  
ATOM   1215  CA  LYS B  92      37.649 -19.281  -2.407  1.00 17.92           C  
ANISOU 1215  CA  LYS B  92     2200   2578   2030      4    -25    440       C  
ATOM   1216  C   LYS B  92      38.337 -20.542  -2.927  1.00 19.24           C  
ANISOU 1216  C   LYS B  92     2371   2669   2269      7    -28    492       C  
ATOM   1217  O   LYS B  92      37.728 -21.613  -3.048  1.00 20.50           O  
ANISOU 1217  O   LYS B  92     2520   2782   2485     -4    -11    545       O  
ATOM   1218  CB  LYS B  92      37.595 -19.326  -0.873  1.00 22.48           C  
ANISOU 1218  CB  LYS B  92     2746   3262   2533     13    -19    494       C  
ATOM   1219  CG  LYS B  92      38.935 -19.037  -0.208  1.00 30.54           C  
ANISOU 1219  CG  LYS B  92     3755   4341   3505     38    -40    497       C  
ATOM   1220  CD  LYS B  92      38.809 -19.203   1.306  1.00 41.96           C  
ANISOU 1220  CD  LYS B  92     5164   5907   4871     50    -34    557       C  
ATOM   1221  CE  LYS B  92      40.003 -18.622   2.049  1.00 50.97           C  
ANISOU 1221  CE  LYS B  92     6286   7133   5946     77    -57    533       C  
ATOM   1222  NZ  LYS B  92      39.782 -18.660   3.528  1.00 50.59           N  
ANISOU 1222  NZ  LYS B  92     6195   7222   5805     91    -51    582       N  
ATOM   1223  N   SER B  93      39.616 -20.401  -3.236  1.00 19.35           N  
ANISOU 1223  N   SER B  93     2395   2669   2289     22    -48    472       N  
ATOM   1224  CA  SER B  93      40.428 -21.464  -3.732  1.00 19.34           C  
ANISOU 1224  CA  SER B  93     2393   2601   2354     28    -54    506       C  
ATOM   1225  C   SER B  93      41.694 -21.389  -2.886  1.00 18.47           C  
ANISOU 1225  C   SER B  93     2270   2547   2199     53    -73    532       C  
ATOM   1226  O   SER B  93      41.874 -20.438  -2.105  1.00 19.36           O  
ANISOU 1226  O   SER B  93     2376   2745   2234     62    -79    507       O  
ATOM   1227  CB  SER B  93      40.696 -21.299  -5.228  1.00 22.99           C  
ANISOU 1227  CB  SER B  93     2877   2986   2870     21    -61    436       C  
ATOM   1228  OG  SER B  93      41.314 -20.033  -5.484  1.00 24.38           O  
ANISOU 1228  OG  SER B  93     3069   3191   3001     26    -74    367       O  
ATOM   1229  N   SER B  94      42.541 -22.389  -3.032  1.00 21.79           N  
ANISOU 1229  N   SER B  94     2683   2921   2672     66    -82    576       N  
ATOM   1230  CA  SER B  94      43.736 -22.523  -2.187  1.00 22.81           C  
ANISOU 1230  CA  SER B  94     2796   3105   2765     94   -101    613       C  
ATOM   1231  C   SER B  94      44.658 -21.288  -2.231  1.00 25.95           C  
ANISOU 1231  C   SER B  94     3201   3550   3107    103   -119    530       C  
ATOM   1232  O   SER B  94      45.222 -20.858  -1.224  1.00 24.89           O  
ANISOU 1232  O   SER B  94     3048   3505   2904    122   -131    536       O  
ATOM   1233  CB  SER B  94      44.504 -23.758  -2.605  1.00 29.37           C  
ANISOU 1233  CB  SER B  94     3618   3858   3680    106   -110    658       C  
ATOM   1234  OG  SER B  94      45.673 -23.880  -1.831  1.00 41.16           O  
ANISOU 1234  OG  SER B  94     5095   5404   5139    136   -132    691       O  
ATOM   1235  N   LYS B  95      44.787 -20.693  -3.414  1.00 24.82           N  
ANISOU 1235  N   LYS B  95     3082   3352   2995     88   -120    450       N  
ATOM   1236  CA  LYS B  95      45.721 -19.586  -3.599  1.00 22.27           C  
ANISOU 1236  CA  LYS B  95     2765   3056   2640     92   -134    375       C  
ATOM   1237  C   LYS B  95      45.052 -18.238  -3.841  1.00 21.89           C  
ANISOU 1237  C   LYS B  95     2730   3026   2559     76   -125    305       C  
ATOM   1238  O   LYS B  95      45.719 -17.204  -4.050  1.00 27.41           O  
ANISOU 1238  O   LYS B  95     3433   3739   3242     76   -131    239       O  
ATOM   1239  CB  LYS B  95      46.685 -19.932  -4.727  1.00 22.19           C  
ANISOU 1239  CB  LYS B  95     2765   2973   2690     92   -142    344       C  
ATOM   1240  CG  LYS B  95      47.438 -21.227  -4.544  1.00 28.16           C  
ANISOU 1240  CG  LYS B  95     3505   3703   3491    111   -154    403       C  
ATOM   1241  CD  LYS B  95      48.279 -21.264  -3.262  1.00 24.71           C  
ANISOU 1241  CD  LYS B  95     3040   3346   2999    140   -172    442       C  
ATOM   1242  CE  LYS B  95      48.986 -22.607  -3.077  1.00 34.25           C  
ANISOU 1242  CE  LYS B  95     4230   4523   4260    163   -185    512       C  
ATOM   1243  NZ  LYS B  95      49.805 -22.682  -1.827  1.00 37.42           N  
ANISOU 1243  NZ  LYS B  95     4602   5011   4602    197   -205    556       N  
ATOM   1244  N   GLY B  96      43.729 -18.225  -3.851  1.00 19.65           N  
ANISOU 1244  N   GLY B  96     2452   2738   2274     62   -109    316       N  
ATOM   1245  CA  GLY B  96      42.999 -16.985  -3.918  1.00 18.15           C  
ANISOU 1245  CA  GLY B  96     2270   2571   2054     51   -102    257       C  
ATOM   1246  C   GLY B  96      41.506 -17.137  -4.127  1.00 18.87           C  
ANISOU 1246  C   GLY B  96     2368   2645   2157     36    -85    269       C  
ATOM   1247  O   GLY B  96      40.760 -17.630  -3.263  1.00 19.31           O  
ANISOU 1247  O   GLY B  96     2405   2741   2188     35    -76    319       O  
ATOM   1248  N   PHE B  97      41.054 -16.653  -5.261  1.00 15.36           N  
ANISOU 1248  N   PHE B  97     1946   2146   1744     24    -81    223       N  
ATOM   1249  CA  PHE B  97      39.680 -16.755  -5.683  1.00 15.17           C  
ANISOU 1249  CA  PHE B  97     1928   2098   1737     11    -68    222       C  
ATOM   1250  C   PHE B  97      39.614 -17.203  -7.117  1.00 12.37           C  
ANISOU 1250  C   PHE B  97     1592   1666   1441      3    -67    207       C  
ATOM   1251  O   PHE B  97      40.509 -16.857  -7.932  1.00 12.48           O  
ANISOU 1251  O   PHE B  97     1620   1652   1470      6    -75    175       O  
ATOM   1252  CB  PHE B  97      38.925 -15.437  -5.543  1.00 16.72           C  
ANISOU 1252  CB  PHE B  97     2125   2325   1900      8    -66    168       C  
ATOM   1253  CG  PHE B  97      38.849 -14.938  -4.128  1.00 19.07           C  
ANISOU 1253  CG  PHE B  97     2396   2710   2137     15    -67    167       C  
ATOM   1254  CD1 PHE B  97      38.021 -15.567  -3.214  1.00 17.65           C  
ANISOU 1254  CD1 PHE B  97     2195   2579   1930     12    -55    215       C  
ATOM   1255  CD2 PHE B  97      39.574 -13.833  -3.720  1.00 20.21           C  
ANISOU 1255  CD2 PHE B  97     2531   2893   2253     23    -77    115       C  
ATOM   1256  CE1 PHE B  97      37.929 -15.119  -1.910  1.00 24.86           C  
ANISOU 1256  CE1 PHE B  97     3076   3589   2778     20    -55    212       C  
ATOM   1257  CE2 PHE B  97      39.514 -13.387  -2.407  1.00 27.89           C  
ANISOU 1257  CE2 PHE B  97     3470   3958   3168     32    -79    103       C  
ATOM   1258  CZ  PHE B  97      38.689 -14.040  -1.496  1.00 23.17           C  
ANISOU 1258  CZ  PHE B  97     2850   3419   2532     31    -68    152       C  
ATOM   1259  N   GLU B  98      38.594 -17.994  -7.414  1.00 11.54           N  
ANISOU 1259  N   GLU B  98     1482   1532   1368     -5    -55    228       N  
ATOM   1260  CA AGLU B  98      38.405 -18.423  -8.785  0.50 12.67           C  
ANISOU 1260  CA AGLU B  98     1635   1614   1565    -11    -55    203       C  
ATOM   1261  CA BGLU B  98      38.372 -18.570  -8.739  0.50 11.55           C  
ANISOU 1261  CA BGLU B  98     1491   1470   1427    -11    -54    208       C  
ATOM   1262  C   GLU B  98      36.946 -18.253  -9.186  1.00 11.99           C  
ANISOU 1262  C   GLU B  98     1548   1523   1484    -20    -45    181       C  
ATOM   1263  O   GLU B  98      35.998 -18.551  -8.449  1.00 11.12           O  
ANISOU 1263  O   GLU B  98     1422   1433   1367    -27    -33    207       O  
ATOM   1264  CB AGLU B  98      38.975 -19.824  -9.053  0.50 19.10           C  
ANISOU 1264  CB AGLU B  98     2436   2382   2439    -11    -55    236       C  
ATOM   1265  CB BGLU B  98      38.523 -20.104  -8.674  0.50 13.44           C  
ANISOU 1265  CB BGLU B  98     1711   1670   1725    -14    -48    257       C  
ATOM   1266  CG AGLU B  98      38.236 -21.009  -8.474  0.50 24.31           C  
ANISOU 1266  CG AGLU B  98     3072   3025   3138    -19    -41    292       C  
ATOM   1267  CG BGLU B  98      39.961 -20.601  -8.654  0.50 16.78           C  
ANISOU 1267  CG BGLU B  98     2131   2077   2167     -3    -61    275       C  
ATOM   1268  CD AGLU B  98      39.050 -22.285  -8.650  0.50 35.22           C  
ANISOU 1268  CD AGLU B  98     4438   4355   4588    -15    -44    326       C  
ATOM   1269  CD BGLU B  98      40.071 -22.099  -8.436  0.50 21.96           C  
ANISOU 1269  CD BGLU B  98     2764   2689   2890     -3    -56    330       C  
ATOM   1270  OE1AGLU B  98      40.293 -22.175  -8.731  0.50 29.83           O  
ANISOU 1270  OE1AGLU B  98     3761   3673   3899     -2    -59    319       O  
ATOM   1271  OE1BGLU B  98      39.090 -22.717  -7.974  0.50 24.73           O  
ANISOU 1271  OE1BGLU B  98     3098   3033   3263    -13    -40    371       O  
ATOM   1272  OE2AGLU B  98      38.461 -23.388  -8.717  0.50 50.56           O  
ANISOU 1272  OE2AGLU B  98     6360   6253   6598    -24    -32    354       O  
ATOM   1273  OE2BGLU B  98      41.150 -22.663  -8.699  0.50 26.89           O  
ANISOU 1273  OE2BGLU B  98     3381   3283   3549      5    -67    335       O  
ATOM   1274  N   SER B  99      36.773 -17.679 -10.376  1.00  9.11           N  
ANISOU 1274  N   SER B  99     1198   1137   1125    -18    -50    132       N  
ATOM   1275  CA ASER B  99      35.433 -17.456 -10.837  0.50  9.84           C  
ANISOU 1275  CA ASER B  99     1288   1229   1221    -22    -44    106       C  
ATOM   1276  CA BSER B  99      35.473 -17.477 -10.990  0.50  9.93           C  
ANISOU 1276  CA BSER B  99     1301   1236   1236    -21    -45    103       C  
ATOM   1277  C   SER B  99      34.761 -18.772 -11.305  1.00  9.55           C  
ANISOU 1277  C   SER B  99     1231   1156   1242    -32    -35    112       C  
ATOM   1278  O   SER B  99      35.401 -19.712 -11.802  1.00 10.49           O  
ANISOU 1278  O   SER B  99     1340   1237   1407    -33    -36    117       O  
ATOM   1279  CB ASER B  99      35.399 -16.354 -11.910  0.50  9.24           C  
ANISOU 1279  CB ASER B  99     1232   1151   1128    -12    -54     59       C  
ATOM   1280  CB BSER B  99      35.648 -16.782 -12.345  0.50  8.90           C  
ANISOU 1280  CB BSER B  99     1186   1090   1102    -13    -55     58       C  
ATOM   1281  OG ASER B  99      36.237 -16.697 -12.975  0.50  8.61           O  
ANISOU 1281  OG ASER B  99     1157   1044   1070     -9    -59     46       O  
ATOM   1282  OG BSER B  99      36.325 -15.571 -12.196  0.50  8.43           O  
ANISOU 1282  OG BSER B  99     1145   1049   1009     -5    -61     48       O  
ATOM   1283  N   LEU B 100      33.449 -18.824 -11.091  1.00 10.80           N  
ANISOU 1283  N   LEU B 100     1376   1324   1402    -39    -25    107       N  
ATOM   1284  CA  LEU B 100      32.613 -19.951 -11.457  1.00 11.30           C  
ANISOU 1284  CA  LEU B 100     1414   1355   1524    -51    -12    104       C  
ATOM   1285  C   LEU B 100      31.789 -19.671 -12.726  1.00 10.13           C  
ANISOU 1285  C   LEU B 100     1262   1202   1384    -46    -18     41       C  
ATOM   1286  O   LEU B 100      31.564 -20.568 -13.521  1.00 10.65           O  
ANISOU 1286  O   LEU B 100     1306   1235   1503    -50    -16     15       O  
ATOM   1287  CB  LEU B 100      31.704 -20.310 -10.281  1.00 12.97           C  
ANISOU 1287  CB  LEU B 100     1605   1586   1734    -66      6    145       C  
ATOM   1288  CG  LEU B 100      32.466 -20.737  -9.027  1.00 14.31           C  
ANISOU 1288  CG  LEU B 100     1771   1772   1893    -68     13    218       C  
ATOM   1289  CD1 LEU B 100      31.540 -20.619  -7.807  1.00 19.23           C  
ANISOU 1289  CD1 LEU B 100     2378   2446   2482    -79     31    253       C  
ATOM   1290  CD2 LEU B 100      32.998 -22.161  -9.159  1.00 23.29           C  
ANISOU 1290  CD2 LEU B 100     2890   2852   3107    -75     20    257       C  
ATOM   1291  N   ARG B 101      31.334 -18.433 -12.864  1.00  8.99           N  
ANISOU 1291  N   ARG B 101     1135   1091   1188    -34    -27     15       N  
ATOM   1292  CA  ARG B 101      30.541 -18.008 -14.028  1.00  9.53           C  
ANISOU 1292  CA  ARG B 101     1201   1166   1253    -23    -36    -38       C  
ATOM   1293  C   ARG B 101      30.739 -16.528 -14.163  1.00  8.35           C  
ANISOU 1293  C   ARG B 101     1079   1042   1050     -5    -50    -47       C  
ATOM   1294  O   ARG B 101      30.658 -15.806 -13.165  1.00  9.14           O  
ANISOU 1294  O   ARG B 101     1187   1162   1121     -6    -48    -31       O  
ATOM   1295  CB  ARG B 101      29.063 -18.360 -13.841  1.00 11.11           C  
ANISOU 1295  CB  ARG B 101     1374   1373   1471    -31    -25    -57       C  
ATOM   1296  CG  ARG B 101      28.187 -18.080 -15.050  1.00 14.68           C  
ANISOU 1296  CG  ARG B 101     1817   1838   1923    -16    -37   -115       C  
ATOM   1297  CD  ARG B 101      26.941 -19.007 -15.134  1.00 18.77           C  
ANISOU 1297  CD  ARG B 101     2295   2348   2488    -30    -23   -145       C  
ATOM   1298  NE  ARG B 101      26.106 -18.790 -16.333  1.00 18.49           N  
ANISOU 1298  NE  ARG B 101     2243   2333   2448    -12    -37   -208       N  
ATOM   1299  CZ  ARG B 101      25.441 -17.666 -16.504  1.00 12.71           C  
ANISOU 1299  CZ  ARG B 101     1523   1636   1669      7    -50   -226       C  
ATOM   1300  NH1 ARG B 101      25.502 -16.752 -15.574  1.00 13.59           N  
ANISOU 1300  NH1 ARG B 101     1657   1759   1744      8    -50   -194       N  
ATOM   1301  NH2 ARG B 101      24.722 -17.447 -17.604  1.00 15.67           N  
ANISOU 1301  NH2 ARG B 101     1882   2037   2034     29    -65   -278       N  
ATOM   1302  N   VAL B 102      31.012 -16.071 -15.374  1.00  7.51           N  
ANISOU 1302  N   VAL B 102      983    936    933     10    -62    -73       N  
ATOM   1303  CA  VAL B 102      31.293 -14.675 -15.632  1.00  7.54           C  
ANISOU 1303  CA  VAL B 102     1011    953    898     27    -73    -73       C  
ATOM   1304  C   VAL B 102      30.439 -14.160 -16.768  1.00  7.59           C  
ANISOU 1304  C   VAL B 102     1015    977    892     47    -84   -104       C  
ATOM   1305  O   VAL B 102      30.429 -14.728 -17.840  1.00  8.90           O  
ANISOU 1305  O   VAL B 102     1168   1148   1064     54    -88   -125       O  
ATOM   1306  CB  VAL B 102      32.804 -14.471 -15.997  1.00  6.98           C  
ANISOU 1306  CB  VAL B 102      959    870    820     28    -76    -57       C  
ATOM   1307  CG1 VAL B 102      33.189 -13.005 -16.201  1.00  7.93           C  
ANISOU 1307  CG1 VAL B 102     1102    995    913     41    -82    -51       C  
ATOM   1308  CG2 VAL B 102      33.707 -15.080 -14.915  1.00  7.64           C  
ANISOU 1308  CG2 VAL B 102     1042    942    918     12    -68    -27       C  
ATOM   1309  N   THR B 103      29.812 -13.024 -16.545  1.00  7.89           N  
ANISOU 1309  N   THR B 103     1061   1026    908     61    -91   -107       N  
ATOM   1310  CA  THR B 103      28.985 -12.358 -17.554  1.00  8.40           C  
ANISOU 1310  CA  THR B 103     1123   1109    957     87   -105   -127       C  
ATOM   1311  C   THR B 103      29.386 -10.890 -17.602  1.00  8.94           C  
ANISOU 1311  C   THR B 103     1215   1170   1010    104   -112   -106       C  
ATOM   1312  O   THR B 103      30.199 -10.433 -16.774  1.00  8.19           O  
ANISOU 1312  O   THR B 103     1133   1057    919     92   -106    -88       O  
ATOM   1313  CB  THR B 103      27.461 -12.424 -17.249  1.00  8.18           C  
ANISOU 1313  CB  THR B 103     1073   1098    935     91   -107   -158       C  
ATOM   1314  OG1 THR B 103      27.125 -11.519 -16.198  1.00  9.70           O  
ANISOU 1314  OG1 THR B 103     1271   1290   1122     91   -107   -154       O  
ATOM   1315  CG2 THR B 103      27.017 -13.821 -16.835  1.00  9.41           C  
ANISOU 1315  CG2 THR B 103     1203   1252   1121     67    -93   -173       C  
ATOM   1316  N   GLY B 104      28.802 -10.165 -18.568  1.00  9.12           N  
ANISOU 1316  N   GLY B 104     1238   1207   1018    132   -126   -110       N  
ATOM   1317  CA  GLY B 104      28.850  -8.730 -18.561  1.00  9.30           C  
ANISOU 1317  CA  GLY B 104     1276   1215   1041    150   -133    -90       C  
ATOM   1318  C   GLY B 104      27.786  -8.167 -17.639  1.00  9.19           C  
ANISOU 1318  C   GLY B 104     1251   1199   1040    155   -138   -114       C  
ATOM   1319  O   GLY B 104      27.096  -8.898 -16.942  1.00 10.42           O  
ANISOU 1319  O   GLY B 104     1389   1370   1200    141   -133   -140       O  
ATOM   1320  N   PRO B 105      27.652  -6.843 -17.616  1.00 10.17           N  
ANISOU 1320  N   PRO B 105     1381   1304   1177    175   -147   -104       N  
ATOM   1321  CA  PRO B 105      26.627  -6.210 -16.782  1.00 12.09           C  
ANISOU 1321  CA  PRO B 105     1608   1547   1437    183   -154   -136       C  
ATOM   1322  C   PRO B 105      25.246  -6.773 -17.101  1.00 11.69           C  
ANISOU 1322  C   PRO B 105     1536   1531   1375    195   -163   -168       C  
ATOM   1323  O   PRO B 105      24.919  -7.068 -18.277  1.00 11.25           O  
ANISOU 1323  O   PRO B 105     1478   1495   1301    215   -173   -163       O  
ATOM   1324  CB  PRO B 105      26.728  -4.748 -17.181  1.00 11.83           C  
ANISOU 1324  CB  PRO B 105     1583   1481   1428    210   -165   -115       C  
ATOM   1325  CG  PRO B 105      28.179  -4.604 -17.576  1.00 13.75           C  
ANISOU 1325  CG  PRO B 105     1848   1700   1674    199   -154    -74       C  
ATOM   1326  CD  PRO B 105      28.445  -5.838 -18.336  1.00 11.01           C  
ANISOU 1326  CD  PRO B 105     1506   1385   1291    190   -149    -64       C  
ATOM   1327  N   GLY B 106      24.451  -7.000 -16.070  1.00 10.55           N  
ANISOU 1327  N   GLY B 106     1371   1401   1236    182   -158   -204       N  
ATOM   1328  CA  GLY B 106      23.057  -7.390 -16.284  1.00 10.17           C  
ANISOU 1328  CA  GLY B 106     1298   1383   1184    193   -166   -241       C  
ATOM   1329  C   GLY B 106      22.894  -8.813 -16.755  1.00 10.05           C  
ANISOU 1329  C   GLY B 106     1270   1388   1157    177   -157   -250       C  
ATOM   1330  O   GLY B 106      21.834  -9.174 -17.232  1.00 11.91           O  
ANISOU 1330  O   GLY B 106     1483   1649   1391    189   -164   -283       O  
ATOM   1331  N   GLY B 107      23.954  -9.624 -16.670  1.00 11.01           N  
ANISOU 1331  N   GLY B 107     1404   1498   1278    152   -142   -225       N  
ATOM   1332  CA  GLY B 107      23.923 -10.985 -17.155  1.00 10.11           C  
ANISOU 1332  CA  GLY B 107     1276   1394   1169    137   -133   -236       C  
ATOM   1333  C   GLY B 107      24.023 -11.136 -18.671  1.00  9.62           C  
ANISOU 1333  C   GLY B 107     1213   1349   1092    161   -147   -240       C  
ATOM   1334  O   GLY B 107      23.804 -12.208 -19.213  1.00 10.36           O  
ANISOU 1334  O   GLY B 107     1285   1457   1194    154   -143   -267       O  
ATOM   1335  N   ASN B 108      24.382 -10.053 -19.350  1.00 10.42           N  
ANISOU 1335  N   ASN B 108     1333   1450   1173    189   -162   -214       N  
ATOM   1336  CA  ASN B 108      24.602 -10.117 -20.791  1.00 11.31           C  
ANISOU 1336  CA  ASN B 108     1445   1592   1260    214   -174   -209       C  
ATOM   1337  C   ASN B 108      25.909 -10.816 -21.146  1.00 10.37           C  
ANISOU 1337  C   ASN B 108     1336   1465   1138    195   -161   -190       C  
ATOM   1338  O   ASN B 108      26.774 -11.027 -20.271  1.00 10.47           O  
ANISOU 1338  O   ASN B 108     1364   1443   1169    167   -146   -171       O  
ATOM   1339  CB  ASN B 108      24.633  -8.704 -21.363  1.00 11.71           C  
ANISOU 1339  CB  ASN B 108     1512   1642   1292    250   -190   -171       C  
ATOM   1340  CG  ASN B 108      23.248  -8.074 -21.394  1.00 14.71           C  
ANISOU 1340  CG  ASN B 108     1874   2039   1673    281   -209   -195       C  
ATOM   1341  OD1 ASN B 108      22.405  -8.509 -22.131  1.00 17.10           O  
ANISOU 1341  OD1 ASN B 108     2151   2386   1958    301   -221   -228       O  
ATOM   1342  ND2 ASN B 108      22.992  -7.137 -20.476  1.00 15.51           N  
ANISOU 1342  ND2 ASN B 108     1984   2107   1801    282   -210   -190       N  
ATOM   1343  N   PRO B 109      26.078 -11.212 -22.413  1.00 10.61           N  
ANISOU 1343  N   PRO B 109     1352   1534   1142    211   -169   -200       N  
ATOM   1344  CA  PRO B 109      27.322 -11.854 -22.799  1.00  9.57           C  
ANISOU 1344  CA  PRO B 109     1226   1400   1009    195   -158   -189       C  
ATOM   1345  C   PRO B 109      28.532 -10.985 -22.563  1.00 10.06           C  
ANISOU 1345  C   PRO B 109     1324   1432   1066    189   -150   -133       C  
ATOM   1346  O   PRO B 109      28.483  -9.766 -22.735  1.00 10.22           O  
ANISOU 1346  O   PRO B 109     1362   1448   1073    210   -157    -97       O  
ATOM   1347  CB  PRO B 109      27.138 -12.131 -24.299  1.00 10.66           C  
ANISOU 1347  CB  PRO B 109     1338   1603   1109    222   -170   -213       C  
ATOM   1348  CG  PRO B 109      25.627 -12.179 -24.467  1.00 11.99           C  
ANISOU 1348  CG  PRO B 109     1477   1803   1274    243   -185   -257       C  
ATOM   1349  CD  PRO B 109      25.111 -11.143 -23.537  1.00 11.86           C  
ANISOU 1349  CD  PRO B 109     1484   1750   1270    247   -188   -228       C  
ATOM   1350  N   CYS B 110      29.631 -11.640 -22.196  1.00  9.58           N  
ANISOU 1350  N   CYS B 110     1270   1347   1022    161   -136   -127       N  
ATOM   1351  CA  CYS B 110      30.934 -10.947 -22.205  1.00  8.99           C  
ANISOU 1351  CA  CYS B 110     1222   1251    940    155   -128    -82       C  
ATOM   1352  C   CYS B 110      31.238 -10.502 -23.641  1.00  9.68           C  
ANISOU 1352  C   CYS B 110     1307   1382    985    180   -133    -62       C  
ATOM   1353  O   CYS B 110      30.738 -11.088 -24.593  1.00 10.96           O  
ANISOU 1353  O   CYS B 110     1443   1596   1123    196   -142    -93       O  
ATOM   1354  CB  CYS B 110      32.039 -11.870 -21.690  1.00  9.40           C  
ANISOU 1354  CB  CYS B 110     1275   1279   1015    125   -115    -87       C  
ATOM   1355  SG  CYS B 110      31.768 -12.521 -20.057  1.00  9.60           S  
ANISOU 1355  SG  CYS B 110     1298   1268   1081     98   -107    -97       S  
ATOM   1356  N   LEU B 111      32.086  -9.481 -23.792  1.00 10.90           N  
ANISOU 1356  N   LEU B 111     1486   1521   1134    183   -126    -12       N  
ATOM   1357  CA  LEU B 111      32.419  -8.959 -25.120  1.00 11.64           C  
ANISOU 1357  CA  LEU B 111     1578   1659   1184    206   -127     22       C  
ATOM   1358  C   LEU B 111      33.631  -9.679 -25.786  1.00  9.95           C  
ANISOU 1358  C   LEU B 111     1355   1473    951    190   -115     16       C  
ATOM   1359  O   LEU B 111      33.580 -10.088 -26.931  1.00 12.29           O  
ANISOU 1359  O   LEU B 111     1628   1836   1205    206   -119      2       O  
ATOM   1360  CB  LEU B 111      32.682  -7.476 -25.055  1.00 12.93           C  
ANISOU 1360  CB  LEU B 111     1766   1789   1357    216   -123     85       C  
ATOM   1361  CG  LEU B 111      31.498  -6.604 -24.634  1.00 22.20           C  
ANISOU 1361  CG  LEU B 111     2943   2941   2551    239   -137     93       C  
ATOM   1362  CD1 LEU B 111      31.825  -5.121 -24.782  1.00 24.74           C  
ANISOU 1362  CD1 LEU B 111     3283   3225   2892    253   -132    159       C  
ATOM   1363  CD2 LEU B 111      30.220  -6.953 -25.414  1.00 27.89           C  
ANISOU 1363  CD2 LEU B 111     3639   3721   3234    272   -158     68       C  
ATOM   1364  N   GLY B 112      34.738  -9.788 -25.050  1.00 10.68           N  
ANISOU 1364  N   GLY B 112     1463   1520   1074    160   -100     23       N  
ATOM   1365  CA  GLY B 112      35.920 -10.456 -25.574  1.00 10.53           C  
ANISOU 1365  CA  GLY B 112     1434   1522   1043    145    -89     12       C  
ATOM   1366  C   GLY B 112      36.818  -9.627 -26.488  1.00 12.04           C  
ANISOU 1366  C   GLY B 112     1632   1739   1201    150    -76     63       C  
ATOM   1367  O   GLY B 112      36.481  -8.499 -26.815  1.00 15.41           O  
ANISOU 1367  O   GLY B 112     2072   2167   1615    169    -75    115       O  
ATOM   1368  N   ASN B 113      37.978 -10.208 -26.806  1.00 13.79           N  
ANISOU 1368  N   ASN B 113     1844   1976   1418    132    -64     49       N  
ATOM   1369  CA  ASN B 113      39.030  -9.622 -27.657  1.00 16.71           C  
ANISOU 1369  CA  ASN B 113     2214   2375   1756    129    -46     91       C  
ATOM   1370  C   ASN B 113      39.958 -10.784 -28.066  1.00 18.91           C  
ANISOU 1370  C   ASN B 113     2467   2689   2028    113    -40     40       C  
ATOM   1371  O   ASN B 113      40.975 -11.077 -27.380  1.00 17.62           O  
ANISOU 1371  O   ASN B 113     2310   2482   1901     87    -31     28       O  
ATOM   1372  CB  ASN B 113      39.830  -8.546 -26.893  1.00 16.24           C  
ANISOU 1372  CB  ASN B 113     2185   2247   1736    110    -29    140       C  
ATOM   1373  CG  ASN B 113      40.881  -7.861 -27.776  1.00 18.55           C  
ANISOU 1373  CG  ASN B 113     2477   2566   2004    105     -5    190       C  
ATOM   1374  OD1 ASN B 113      41.899  -7.369 -27.262  1.00 26.40           O  
ANISOU 1374  OD1 ASN B 113     3483   3512   3033     81     12    208       O  
ATOM   1375  ND2 ASN B 113      40.682  -7.895 -29.090  1.00 22.36           N  
ANISOU 1375  ND2 ASN B 113     2940   3130   2425    125     -4    209       N  
ATOM   1376  N   GLU B 114      39.587 -11.496 -29.133  1.00 20.68           N  
ANISOU 1376  N   GLU B 114     2656   2992   2209    130    -48      1       N  
ATOM   1377  CA  GLU B 114      40.364 -12.685 -29.572  1.00 24.06           C  
ANISOU 1377  CA  GLU B 114     3048   3455   2636    118    -46    -62       C  
ATOM   1378  C   GLU B 114      41.568 -12.254 -30.439  1.00 31.36           C  
ANISOU 1378  C   GLU B 114     3966   4430   3519    111    -25    -33       C  
ATOM   1379  O   GLU B 114      42.639 -12.888 -30.372  1.00 32.06           O  
ANISOU 1379  O   GLU B 114     4040   4514   3627     90    -17    -68       O  
ATOM   1380  CB  GLU B 114      39.481 -13.676 -30.367  1.00 27.12           C  
ANISOU 1380  CB  GLU B 114     3390   3912   3001    138    -63   -133       C  
ATOM   1381  CG  GLU B 114      40.230 -14.942 -30.812  1.00 30.70           C  
ANISOU 1381  CG  GLU B 114     3798   4396   3467    127    -63   -212       C  
ATOM   1382  CD  GLU B 114      39.498 -15.796 -31.836  1.00 39.40           C  
ANISOU 1382  CD  GLU B 114     4843   5585   4541    148    -77   -290       C  
ATOM   1383  OE1 GLU B 114      38.308 -15.487 -32.151  1.00 29.50           O  
ANISOU 1383  OE1 GLU B 114     3584   4366   3256    173    -90   -286       O  
ATOM   1384  OE2 GLU B 114      40.129 -16.787 -32.303  1.00 33.16           O  
ANISOU 1384  OE2 GLU B 114     4008   4826   3764    141    -76   -362       O  
TER    1385      GLU B 114                                                      
ATOM   1386  N   GLN C  29      27.642  -1.131 -38.170  1.00 43.51           N  
ANISOU 1386  N   GLN C  29     5611   5240   5678    347    120     86       N  
ATOM   1387  CA  GLN C  29      27.675  -1.817 -39.494  1.00 33.74           C  
ANISOU 1387  CA  GLN C  29     4349   4001   4468    300     80    113       C  
ATOM   1388  C   GLN C  29      28.759  -2.887 -39.493  1.00 26.96           C  
ANISOU 1388  C   GLN C  29     3501   3167   3574    265     69    103       C  
ATOM   1389  O   GLN C  29      29.864  -2.676 -38.973  1.00 32.35           O  
ANISOU 1389  O   GLN C  29     4219   3853   4218    260     67     67       O  
ATOM   1390  CB  GLN C  29      27.939  -0.807 -40.613  1.00 41.36           C  
ANISOU 1390  CB  GLN C  29     5337   4931   5447    279     41    104       C  
ATOM   1391  CG  GLN C  29      28.414  -1.413 -41.941  1.00 49.99           C  
ANISOU 1391  CG  GLN C  29     6430   6020   6541    229      1    118       C  
ATOM   1392  CD  GLN C  29      29.036  -0.376 -42.864  1.00 39.85           C  
ANISOU 1392  CD  GLN C  29     5185   4701   5252    206    -26    105       C  
ATOM   1393  OE1 GLN C  29      28.850   0.828 -42.678  1.00 44.66           O  
ANISOU 1393  OE1 GLN C  29     5812   5284   5873    228    -24     92       O  
ATOM   1394  NE2 GLN C  29      29.786  -0.839 -43.855  1.00 36.46           N  
ANISOU 1394  NE2 GLN C  29     4773   4270   4809    164    -49    108       N  
ATOM   1395  N   VAL C  30      28.422  -4.052 -40.028  1.00 25.71           N  
ANISOU 1395  N   VAL C  30     3309   3023   3434    243     59    135       N  
ATOM   1396  CA  VAL C  30      29.402  -5.106 -40.200  1.00 20.35           C  
ANISOU 1396  CA  VAL C  30     2638   2363   2730    209     45    128       C  
ATOM   1397  C   VAL C  30      29.702  -5.201 -41.697  1.00 16.99           C  
ANISOU 1397  C   VAL C  30     2218   1919   2317    168      3    134       C  
ATOM   1398  O   VAL C  30      28.753  -5.298 -42.492  1.00 22.39           O  
ANISOU 1398  O   VAL C  30     2880   2590   3037    164    -15    164       O  
ATOM   1399  CB  VAL C  30      28.898  -6.478 -39.682  1.00 22.79           C  
ANISOU 1399  CB  VAL C  30     2912   2699   3048    214     64    158       C  
ATOM   1400  CG1 VAL C  30      29.995  -7.529 -39.806  1.00 17.86           C  
ANISOU 1400  CG1 VAL C  30     2298   2090   2396    182     48    147       C  
ATOM   1401  CG2 VAL C  30      28.444  -6.422 -38.213  1.00 24.53           C  
ANISOU 1401  CG2 VAL C  30     3131   2936   3253    260    115    160       C  
ATOM   1402  N   LEU C  31      30.989  -5.259 -42.054  1.00 15.50           N  
ANISOU 1402  N   LEU C  31     2058   1729   2100    138     -9    109       N  
ATOM   1403  CA  LEU C  31      31.377  -5.348 -43.471  1.00 14.13           C  
ANISOU 1403  CA  LEU C  31     1901   1538   1929    101    -38    113       C  
ATOM   1404  C   LEU C  31      31.102  -6.720 -44.078  1.00 12.66           C  
ANISOU 1404  C   LEU C  31     1695   1363   1750     82    -54    137       C  
ATOM   1405  O   LEU C  31      31.360  -7.768 -43.454  1.00 12.21           O  
ANISOU 1405  O   LEU C  31     1621   1330   1687     81    -42    137       O  
ATOM   1406  CB  LEU C  31      32.837  -4.919 -43.737  1.00 13.97           C  
ANISOU 1406  CB  LEU C  31     1914   1508   1886     76    -38     81       C  
ATOM   1407  CG  LEU C  31      33.275  -3.543 -43.280  1.00 16.00           C  
ANISOU 1407  CG  LEU C  31     2193   1744   2139     88    -31     55       C  
ATOM   1408  CD1 LEU C  31      34.796  -3.485 -43.265  1.00 14.88           C  
ANISOU 1408  CD1 LEU C  31     2067   1598   1986     62    -29     24       C  
ATOM   1409  CD2 LEU C  31      32.664  -2.429 -44.148  1.00 19.15           C  
ANISOU 1409  CD2 LEU C  31     2609   2109   2555     89    -44     68       C  
ATOM   1410  N   ARG C  32      30.601  -6.730 -45.303  1.00 12.86           N  
ANISOU 1410  N   ARG C  32     1729   1368   1789     66    -85    156       N  
ATOM   1411  CA  ARG C  32      30.165  -7.924 -45.985  1.00 13.77           C  
ANISOU 1411  CA  ARG C  32     1830   1485   1916     49   -111    177       C  
ATOM   1412  C   ARG C  32      30.807  -7.945 -47.348  1.00 12.83           C  
ANISOU 1412  C   ARG C  32     1756   1346   1771     19   -135    170       C  
ATOM   1413  O   ARG C  32      30.991  -6.895 -47.993  1.00 13.24           O  
ANISOU 1413  O   ARG C  32     1843   1374   1812     16   -141    166       O  
ATOM   1414  CB  ARG C  32      28.649  -7.855 -46.170  1.00 19.51           C  
ANISOU 1414  CB  ARG C  32     2523   2199   2689     66   -135    211       C  
ATOM   1415  CG  ARG C  32      28.040  -9.017 -46.885  1.00 22.50           C  
ANISOU 1415  CG  ARG C  32     2885   2572   3092     49   -173    234       C  
ATOM   1416  CD  ARG C  32      26.516  -8.942 -46.805  1.00 26.65           C  
ANISOU 1416  CD  ARG C  32     3360   3084   3680     69   -193    268       C  
ATOM   1417  NE  ARG C  32      26.034  -9.017 -45.422  1.00 29.24           N  
ANISOU 1417  NE  ARG C  32     3640   3435   4036     98   -144    279       N  
ATOM   1418  CZ  ARG C  32      26.021 -10.136 -44.678  1.00 37.52           C  
ANISOU 1418  CZ  ARG C  32     4657   4505   5093     97   -120    289       C  
ATOM   1419  NH1 ARG C  32      26.448 -11.307 -45.150  1.00 33.27           N  
ANISOU 1419  NH1 ARG C  32     4126   3970   4546     69   -144    289       N  
ATOM   1420  NH2 ARG C  32      25.562 -10.084 -43.438  1.00 35.47           N  
ANISOU 1420  NH2 ARG C  32     4362   4262   4850    127    -70    301       N  
ATOM   1421  N   GLY C  33      31.202  -9.123 -47.777  1.00 10.56           N  
ANISOU 1421  N   GLY C  33     1473   1066   1473      0   -145    169       N  
ATOM   1422  CA  GLY C  33      31.720  -9.330 -49.114  1.00 11.13           C  
ANISOU 1422  CA  GLY C  33     1593   1118   1517    -25   -164    164       C  
ATOM   1423  C   GLY C  33      31.514 -10.714 -49.650  1.00 11.02           C  
ANISOU 1423  C   GLY C  33     1578   1104   1504    -38   -191    172       C  
ATOM   1424  O   GLY C  33      30.997 -11.582 -48.960  1.00 12.11           O  
ANISOU 1424  O   GLY C  33     1672   1258   1671    -32   -195    183       O  
ATOM   1425  N   SER C  34      31.906 -10.937 -50.888  1.00 11.47           N  
ANISOU 1425  N   SER C  34     1687   1141   1529    -56   -209    167       N  
ATOM   1426  CA  SER C  34      31.887 -12.268 -51.452  1.00 13.39           C  
ANISOU 1426  CA  SER C  34     1940   1381   1767    -69   -234    166       C  
ATOM   1427  C   SER C  34      33.056 -12.460 -52.387  1.00 10.85           C  
ANISOU 1427  C   SER C  34     1677   1049   1396    -86   -214    144       C  
ATOM   1428  O   SER C  34      33.759 -11.511 -52.744  1.00 11.69           O  
ANISOU 1428  O   SER C  34     1818   1146   1476    -90   -184    135       O  
ATOM   1429  CB  SER C  34      30.536 -12.561 -52.090  1.00 12.82           C  
ANISOU 1429  CB  SER C  34     1865   1286   1719    -67   -299    191       C  
ATOM   1430  OG  SER C  34      30.289 -11.710 -53.175  1.00 16.95           O  
ANISOU 1430  OG  SER C  34     2442   1779   2215    -68   -328    197       O  
ATOM   1431  N   GLY C  35      33.316 -13.701 -52.747  1.00 11.83           N  
ANISOU 1431  N   GLY C  35     1811   1171   1510    -95   -224    135       N  
ATOM   1432  CA  GLY C  35      34.459 -14.041 -53.564  1.00 11.61           C  
ANISOU 1432  CA  GLY C  35     1835   1134   1439   -107   -195    113       C  
ATOM   1433  C   GLY C  35      34.693 -15.534 -53.593  1.00 11.06           C  
ANISOU 1433  C   GLY C  35     1759   1067   1374   -112   -204    102       C  
ATOM   1434  O   GLY C  35      33.752 -16.296 -53.622  1.00 11.81           O  
ANISOU 1434  O   GLY C  35     1839   1156   1491   -111   -254    114       O  
ATOM   1435  N   HIS C  36      35.954 -15.941 -53.682  1.00 11.81           N  
ANISOU 1435  N   HIS C  36     1867   1167   1451   -118   -158     78       N  
ATOM   1436  CA  HIS C  36      36.316 -17.336 -53.699  1.00 11.78           C  
ANISOU 1436  CA  HIS C  36     1859   1164   1453   -120   -161     64       C  
ATOM   1437  C   HIS C  36      37.598 -17.567 -52.950  1.00 10.65           C  
ANISOU 1437  C   HIS C  36     1682   1041   1324   -120   -106     44       C  
ATOM   1438  O   HIS C  36      38.390 -16.659 -52.782  1.00 10.75           O  
ANISOU 1438  O   HIS C  36     1692   1059   1333   -121    -64     36       O  
ATOM   1439  CB  HIS C  36      36.476 -17.800 -55.141  1.00 13.43           C  
ANISOU 1439  CB  HIS C  36     2146   1342   1613   -124   -172     51       C  
ATOM   1440  CG  HIS C  36      37.555 -17.070 -55.884  1.00 14.18           C  
ANISOU 1440  CG  HIS C  36     2293   1428   1666   -127   -114     37       C  
ATOM   1441  ND1 HIS C  36      37.311 -15.929 -56.567  1.00 18.75           N  
ANISOU 1441  ND1 HIS C  36     2918   1991   2212   -128   -113     50       N  
ATOM   1442  CD2 HIS C  36      38.904 -17.357 -56.058  1.00 17.48           C  
ANISOU 1442  CD2 HIS C  36     2720   1846   2074   -129    -50     14       C  
ATOM   1443  CE1 HIS C  36      38.462 -15.504 -57.129  1.00 20.29           C  
ANISOU 1443  CE1 HIS C  36     3153   2178   2378   -132    -47     37       C  
ATOM   1444  NE2 HIS C  36      39.425 -16.387 -56.834  1.00 17.44           N  
ANISOU 1444  NE2 HIS C  36     2766   1827   2033   -132     -8     15       N  
ATOM   1445  N   CYS C  37      37.786 -18.772 -52.425  1.00 10.29           N  
ANISOU 1445  N   CYS C  37     1604   1002   1300   -118   -112     38       N  
ATOM   1446  CA  CYS C  37      39.042 -19.111 -51.787  1.00 10.41           C  
ANISOU 1446  CA  CYS C  37     1590   1032   1333   -116    -69     18       C  
ATOM   1447  C   CYS C  37      40.217 -18.980 -52.730  1.00 10.53           C  
ANISOU 1447  C   CYS C  37     1646   1030   1322   -120    -21     -4       C  
ATOM   1448  O   CYS C  37      40.226 -19.604 -53.813  1.00 11.19           O  
ANISOU 1448  O   CYS C  37     1782   1091   1375   -121    -24    -14       O  
ATOM   1449  CB  CYS C  37      38.967 -20.504 -51.204  1.00 10.66           C  
ANISOU 1449  CB  CYS C  37     1589   1068   1391   -112    -89     19       C  
ATOM   1450  SG  CYS C  37      40.482 -21.067 -50.427  1.00  9.97           S  
ANISOU 1450  SG  CYS C  37     1463    993   1329   -106    -48     -3       S  
ATOM   1451  N   LYS C  38      41.182 -18.184 -52.358  1.00 10.70           N  
ANISOU 1451  N   LYS C  38     1647   1060   1357   -123     23    -14       N  
ATOM   1452  CA  LYS C  38      42.415 -18.015 -53.112  1.00 11.77           C  
ANISOU 1452  CA  LYS C  38     1807   1180   1483   -127     81    -33       C  
ATOM   1453  C   LYS C  38      43.324 -19.223 -52.896  1.00 10.39           C  
ANISOU 1453  C   LYS C  38     1606   1005   1334   -121    100    -54       C  
ATOM   1454  O   LYS C  38      43.754 -19.868 -53.871  1.00 12.02           O  
ANISOU 1454  O   LYS C  38     1855   1192   1519   -119    125    -68       O  
ATOM   1455  CB  LYS C  38      43.102 -16.715 -52.710  1.00 12.85           C  
ANISOU 1455  CB  LYS C  38     1920   1321   1640   -134    117    -33       C  
ATOM   1456  CG  LYS C  38      44.296 -16.322 -53.557  1.00 13.78           C  
ANISOU 1456  CG  LYS C  38     2061   1418   1755   -142    184    -46       C  
ATOM   1457  CD  LYS C  38      45.068 -15.183 -52.942  1.00 15.85           C  
ANISOU 1457  CD  LYS C  38     2282   1681   2057   -151    213    -48       C  
ATOM   1458  CE  LYS C  38      45.841 -14.428 -53.994  1.00 19.24           C  
ANISOU 1458  CE  LYS C  38     2748   2084   2476   -163    279    -46       C  
ATOM   1459  NZ  LYS C  38      46.747 -13.462 -53.324  1.00 22.76           N  
ANISOU 1459  NZ  LYS C  38     3141   2527   2980   -174    305    -52       N  
ATOM   1460  N   TRP C  39      43.639 -19.534 -51.632  1.00 10.18           N  
ANISOU 1460  N   TRP C  39     1516    999   1351   -116     88    -56       N  
ATOM   1461  CA  TRP C  39      44.282 -20.746 -51.240  1.00 11.31           C  
ANISOU 1461  CA  TRP C  39     1629   1142   1523   -108     89    -70       C  
ATOM   1462  C   TRP C  39      44.017 -20.978 -49.778  1.00  9.34           C  
ANISOU 1462  C   TRP C  39     1326    917   1306   -101     52    -60       C  
ATOM   1463  O   TRP C  39      43.628 -20.068 -49.043  1.00  9.26           O  
ANISOU 1463  O   TRP C  39     1298    922   1297   -101     39    -48       O  
ATOM   1464  CB  TRP C  39      45.806 -20.713 -51.517  1.00 12.28           C  
ANISOU 1464  CB  TRP C  39     1737   1253   1676   -108    148    -94       C  
ATOM   1465  CG  TRP C  39      46.589 -19.589 -50.911  1.00 11.14           C  
ANISOU 1465  CG  TRP C  39     1551   1115   1565   -115    172    -97       C  
ATOM   1466  CD1 TRP C  39      46.970 -18.420 -51.541  1.00 13.55           C  
ANISOU 1466  CD1 TRP C  39     1876   1408   1864   -127    215    -96       C  
ATOM   1467  CD2 TRP C  39      47.174 -19.522 -49.596  1.00  9.91           C  
ANISOU 1467  CD2 TRP C  39     1331    973   1458   -111    153   -103       C  
ATOM   1468  NE1 TRP C  39      47.693 -17.629 -50.713  1.00 14.06           N  
ANISOU 1468  NE1 TRP C  39     1889   1476   1975   -132    221   -102       N  
ATOM   1469  CE2 TRP C  39      47.859 -18.215 -49.515  1.00 11.35           C  
ANISOU 1469  CE2 TRP C  39     1496   1149   1665   -122    182   -108       C  
ATOM   1470  CE3 TRP C  39      47.184 -20.349 -48.494  1.00 10.39           C  
ANISOU 1470  CE3 TRP C  39     1355   1049   1544    -98    113   -103       C  
ATOM   1471  CZ2 TRP C  39      48.545 -17.840 -48.388  1.00 11.40           C  
ANISOU 1471  CZ2 TRP C  39     1449   1162   1720   -121    164   -117       C  
ATOM   1472  CZ3 TRP C  39      47.860 -19.945 -47.339  1.00 11.83           C  
ANISOU 1472  CZ3 TRP C  39     1487   1239   1766    -95     97   -111       C  
ATOM   1473  CH2 TRP C  39      48.544 -18.718 -47.305  1.00 11.06           C  
ANISOU 1473  CH2 TRP C  39     1374   1134   1694   -106    119   -120       C  
ATOM   1474  N   PHE C  40      44.206 -22.212 -49.329  1.00  9.11           N  
ANISOU 1474  N   PHE C  40     1275    888   1298    -92     35    -63       N  
ATOM   1475  CA  PHE C  40      43.979 -22.573 -47.935  1.00  8.36           C  
ANISOU 1475  CA  PHE C  40     1135    813   1226    -83      2    -50       C  
ATOM   1476  C   PHE C  40      44.882 -23.703 -47.545  1.00  9.23           C  
ANISOU 1476  C   PHE C  40     1218    917   1371    -73      2    -63       C  
ATOM   1477  O   PHE C  40      44.882 -24.746 -48.211  1.00 11.00           O  
ANISOU 1477  O   PHE C  40     1460   1123   1595    -71      2    -70       O  
ATOM   1478  CB  PHE C  40      42.494 -22.924 -47.717  1.00  8.03           C  
ANISOU 1478  CB  PHE C  40     1103    777   1168    -83    -37    -21       C  
ATOM   1479  CG  PHE C  40      42.082 -22.909 -46.274  1.00  7.74           C  
ANISOU 1479  CG  PHE C  40     1031    764   1144    -72    -59      0       C  
ATOM   1480  CD1 PHE C  40      42.315 -23.985 -45.473  1.00  8.45           C  
ANISOU 1480  CD1 PHE C  40     1096    856   1256    -62    -75      5       C  
ATOM   1481  CD2 PHE C  40      41.457 -21.783 -45.740  1.00  8.33           C  
ANISOU 1481  CD2 PHE C  40     1102    855   1206    -69    -62     12       C  
ATOM   1482  CE1 PHE C  40      41.973 -23.910 -44.136  1.00  8.16           C  
ANISOU 1482  CE1 PHE C  40     1037    840   1221    -49    -90     25       C  
ATOM   1483  CE2 PHE C  40      41.079 -21.719 -44.415  1.00  7.71           C  
ANISOU 1483  CE2 PHE C  40     1001    797   1131    -55    -74     30       C  
ATOM   1484  CZ  PHE C  40      41.355 -22.789 -43.607  1.00  7.66           C  
ANISOU 1484  CZ  PHE C  40      975    795   1140    -45    -88     37       C  
ATOM   1485  N   ASN C  41      45.694 -23.469 -46.505  1.00  9.64           N  
ANISOU 1485  N   ASN C  41     1229    980   1453    -65      0    -70       N  
ATOM   1486  CA  ASN C  41      46.575 -24.441 -45.943  1.00  9.55           C  
ANISOU 1486  CA  ASN C  41     1185    963   1480    -53     -7    -80       C  
ATOM   1487  C   ASN C  41      45.827 -25.231 -44.877  1.00  8.92           C  
ANISOU 1487  C   ASN C  41     1095    895   1396    -42    -51    -54       C  
ATOM   1488  O   ASN C  41      45.582 -24.753 -43.750  1.00  9.23           O  
ANISOU 1488  O   ASN C  41     1122    955   1430    -35    -72    -41       O  
ATOM   1489  CB  ASN C  41      47.847 -23.834 -45.397  1.00 12.48           C  
ANISOU 1489  CB  ASN C  41     1517   1333   1890    -50      2   -100       C  
ATOM   1490  CG  ASN C  41      48.830 -24.903 -45.029  1.00 16.71           C  
ANISOU 1490  CG  ASN C  41     2018   1856   2473    -36     -6   -113       C  
ATOM   1491  OD1 ASN C  41      48.659 -25.538 -44.040  1.00 15.56           O  
ANISOU 1491  OD1 ASN C  41     1860   1719   2332    -24    -45   -100       O  
ATOM   1492  ND2 ASN C  41      49.797 -25.181 -45.910  1.00 22.55           N  
ANISOU 1492  ND2 ASN C  41     2748   2573   3245    -37     35   -136       N  
ATOM   1493  N   VAL C  42      45.498 -26.458 -45.228  1.00  9.36           N  
ANISOU 1493  N   VAL C  42     1162    937   1457    -40    -62    -48       N  
ATOM   1494  CA AVAL C  42      44.689 -27.306 -44.378  0.50 10.83           C  
ANISOU 1494  CA AVAL C  42     1342   1129   1643    -33    -98    -18       C  
ATOM   1495  CA BVAL C  42      44.686 -27.288 -44.376  0.50  9.51           C  
ANISOU 1495  CA BVAL C  42     1175    963   1476    -33    -98    -18       C  
ATOM   1496  C   VAL C  42      45.424 -27.643 -43.075  1.00  9.65           C  
ANISOU 1496  C   VAL C  42     1161    988   1517    -15   -118    -14       C  
ATOM   1497  O   VAL C  42      44.833 -27.628 -42.006  1.00 11.18           O  
ANISOU 1497  O   VAL C  42     1352   1198   1696     -7   -139     12       O  
ATOM   1498  CB AVAL C  42      44.230 -28.586 -45.122  0.50 13.09           C  
ANISOU 1498  CB AVAL C  42     1646   1391   1937    -37   -109    -14       C  
ATOM   1499  CB BVAL C  42      44.201 -28.539 -45.134  0.50  9.42           C  
ANISOU 1499  CB BVAL C  42     1181    926   1470    -37   -109    -14       C  
ATOM   1500  CG1AVAL C  42      43.297 -28.224 -46.275  0.50 12.20           C  
ANISOU 1500  CG1AVAL C  42     1571   1269   1795    -52   -105    -13       C  
ATOM   1501  CG1BVAL C  42      43.250 -29.332 -44.251  0.50  8.12           C  
ANISOU 1501  CG1BVAL C  42     1007    765   1311    -33   -142     24       C  
ATOM   1502  CG2AVAL C  42      45.417 -29.396 -45.622  0.50 20.79           C  
ANISOU 1502  CG2AVAL C  42     2615   2341   2941    -28    -94    -44       C  
ATOM   1503  CG2BVAL C  42      43.506 -28.126 -46.430  0.50  9.76           C  
ANISOU 1503  CG2BVAL C  42     1263    958   1485    -52    -98    -20       C  
ATOM   1504  N   ARG C  43      46.720 -27.933 -43.142  1.00  9.84           N  
ANISOU 1504  N   ARG C  43     1164    999   1576     -8   -111    -41       N  
ATOM   1505  CA  ARG C  43      47.482 -28.275 -41.945  1.00 10.62           C  
ANISOU 1505  CA  ARG C  43     1233   1099   1700      9   -140    -40       C  
ATOM   1506  C   ARG C  43      47.513 -27.116 -40.908  1.00 10.21           C  
ANISOU 1506  C   ARG C  43     1177   1071   1629     14   -155    -36       C  
ATOM   1507  O   ARG C  43      47.368 -27.354 -39.717  1.00 12.87           O  
ANISOU 1507  O   ARG C  43     1515   1418   1955     30   -188    -17       O  
ATOM   1508  CB  ARG C  43      48.910 -28.693 -42.345  1.00 12.86           C  
ANISOU 1508  CB  ARG C  43     1487   1360   2037     16   -129    -72       C  
ATOM   1509  CG  ARG C  43      49.739 -29.077 -41.156  1.00 13.24           C  
ANISOU 1509  CG  ARG C  43     1505   1405   2118     36   -169    -71       C  
ATOM   1510  CD  ARG C  43      50.989 -29.824 -41.606  1.00 16.00           C  
ANISOU 1510  CD  ARG C  43     1821   1726   2531     45   -160    -98       C  
ATOM   1511  NE  ARG C  43      51.927 -28.959 -42.303  1.00 14.27           N  
ANISOU 1511  NE  ARG C  43     1576   1499   2346     37   -120   -130       N  
ATOM   1512  CZ  ARG C  43      52.857 -28.243 -41.684  1.00 17.60           C  
ANISOU 1512  CZ  ARG C  43     1960   1921   2806     40   -137   -144       C  
ATOM   1513  NH1 ARG C  43      52.930 -28.276 -40.368  1.00 16.04           N  
ANISOU 1513  NH1 ARG C  43     1755   1731   2606     54   -197   -132       N  
ATOM   1514  NH2 ARG C  43      53.711 -27.493 -42.369  1.00 22.39           N  
ANISOU 1514  NH2 ARG C  43     2537   2514   3453     29    -96   -170       N  
ATOM   1515  N   MET C  44      47.679 -25.914 -41.406  1.00 10.05           N  
ANISOU 1515  N   MET C  44     1159   1056   1603      2   -131    -54       N  
ATOM   1516  CA AMET C  44      47.800 -24.776 -40.513  0.50 10.36           C  
ANISOU 1516  CA AMET C  44     1196   1110   1629      7   -147    -58       C  
ATOM   1517  CA BMET C  44      47.852 -24.682 -40.612  0.50 11.36           C  
ANISOU 1517  CA BMET C  44     1322   1236   1757      5   -144    -60       C  
ATOM   1518  C   MET C  44      46.479 -24.085 -40.241  1.00  9.72           C  
ANISOU 1518  C   MET C  44     1145   1050   1496      5   -144    -34       C  
ATOM   1519  O   MET C  44      46.406 -23.194 -39.386  1.00  9.48           O  
ANISOU 1519  O   MET C  44     1122   1033   1447     14   -158    -35       O  
ATOM   1520  CB AMET C  44      48.761 -23.789 -41.091  0.50 11.40           C  
ANISOU 1520  CB AMET C  44     1309   1231   1792     -5   -124    -89       C  
ATOM   1521  CB BMET C  44      48.621 -23.569 -41.383  0.50 14.44           C  
ANISOU 1521  CB BMET C  44     1699   1616   2171    -10   -113    -90       C  
ATOM   1522  CG AMET C  44      50.148 -24.356 -41.198  0.50 13.12           C  
ANISOU 1522  CG AMET C  44     1485   1426   2072      0   -127   -113       C  
ATOM   1523  CG BMET C  44      50.021 -23.833 -41.972  0.50 16.86           C  
ANISOU 1523  CG BMET C  44     1967   1897   2539    -14    -94   -118       C  
ATOM   1524  SD AMET C  44      51.018 -23.811 -39.756  0.50 14.61           S  
ANISOU 1524  SD AMET C  44     1648   1616   2286     14   -183   -125       S  
ATOM   1525  SD BMET C  44      51.448 -23.625 -40.887  0.50 14.49           S  
ANISOU 1525  SD BMET C  44     1617   1586   2300     -1   -136   -140       S  
ATOM   1526  CE AMET C  44      52.611 -24.568 -40.114  0.50 14.93           C  
ANISOU 1526  CE AMET C  44     1630   1625   2418     18   -181   -151       C  
ATOM   1527  CE BMET C  44      50.982 -25.009 -39.821  0.50 13.88           C  
ANISOU 1527  CE BMET C  44     1554   1518   2201     23   -187   -115       C  
ATOM   1528  N   GLY C  45      45.414 -24.515 -40.898  1.00  8.61           N  
ANISOU 1528  N   GLY C  45     1023    911   1338     -2   -129    -12       N  
ATOM   1529  CA  GLY C  45      44.074 -24.020 -40.622  1.00  8.63           C  
ANISOU 1529  CA  GLY C  45     1045    930   1302     -2   -126     14       C  
ATOM   1530  C   GLY C  45      43.812 -22.587 -41.026  1.00  7.65           C  
ANISOU 1530  C   GLY C  45      932    811   1161    -11   -108      3       C  
ATOM   1531  O   GLY C  45      43.014 -21.896 -40.378  1.00  8.54           O  
ANISOU 1531  O   GLY C  45     1056    940   1247     -2   -109     19       O  
ATOM   1532  N   PHE C  46      44.438 -22.098 -42.083  1.00  7.92           N  
ANISOU 1532  N   PHE C  46      967    833   1210    -27    -87    -20       N  
ATOM   1533  CA  PHE C  46      44.138 -20.740 -42.546  1.00  8.01           C  
ANISOU 1533  CA  PHE C  46      993    845   1205    -37    -69    -26       C  
ATOM   1534  C   PHE C  46      44.396 -20.622 -44.018  1.00  8.13           C  
ANISOU 1534  C   PHE C  46     1021    841   1225    -56    -40    -39       C  
ATOM   1535  O   PHE C  46      45.084 -21.468 -44.640  1.00  8.40           O  
ANISOU 1535  O   PHE C  46     1050    860   1279    -60    -28    -52       O  
ATOM   1536  CB  PHE C  46      44.951 -19.695 -41.811  1.00  8.80           C  
ANISOU 1536  CB  PHE C  46     1080    946   1314    -32    -75    -48       C  
ATOM   1537  CG  PHE C  46      46.339 -19.536 -42.354  1.00  7.28           C  
ANISOU 1537  CG  PHE C  46      867    735   1164    -44    -60    -77       C  
ATOM   1538  CD1 PHE C  46      47.342 -20.466 -42.071  1.00  8.88           C  
ANISOU 1538  CD1 PHE C  46     1041    929   1403    -38    -72    -89       C  
ATOM   1539  CD2 PHE C  46      46.613 -18.523 -43.265  1.00  9.39           C  
ANISOU 1539  CD2 PHE C  46     1140    988   1437    -62    -29    -89       C  
ATOM   1540  CE1 PHE C  46      48.592 -20.316 -42.617  1.00 11.01           C  
ANISOU 1540  CE1 PHE C  46     1283   1178   1722    -48    -51   -114       C  
ATOM   1541  CE2 PHE C  46      47.878 -18.381 -43.843  1.00 12.25           C  
ANISOU 1541  CE2 PHE C  46     1479   1330   1845    -74     -3   -112       C  
ATOM   1542  CZ  PHE C  46      48.841 -19.295 -43.517  1.00 11.19           C  
ANISOU 1542  CZ  PHE C  46     1310   1187   1751    -67    -13   -124       C  
ATOM   1543  N   GLY C  47      43.915 -19.542 -44.578  1.00  7.61           N  
ANISOU 1543  N   GLY C  47      976    774   1140    -65    -26    -37       N  
ATOM   1544  CA  GLY C  47      44.156 -19.195 -45.965  1.00  7.92           C  
ANISOU 1544  CA  GLY C  47     1039    794   1175    -82      4    -47       C  
ATOM   1545  C   GLY C  47      43.745 -17.757 -46.250  1.00  7.46           C  
ANISOU 1545  C   GLY C  47     1000    734   1098    -89     14    -43       C  
ATOM   1546  O   GLY C  47      43.594 -16.944 -45.330  1.00  7.77           O  
ANISOU 1546  O   GLY C  47     1028    784   1139    -81      1    -42       O  
ATOM   1547  N   PHE C  48      43.499 -17.504 -47.514  1.00  8.05           N  
ANISOU 1547  N   PHE C  48     1111    793   1154   -101     34    -40       N  
ATOM   1548  CA  PHE C  48      43.027 -16.226 -47.993  1.00  7.78           C  
ANISOU 1548  CA  PHE C  48     1103    752   1100   -108     42    -32       C  
ATOM   1549  C   PHE C  48      41.861 -16.454 -48.951  1.00  8.23           C  
ANISOU 1549  C   PHE C  48     1202    801   1123   -110     27    -13       C  
ATOM   1550  O   PHE C  48      41.811 -17.433 -49.708  1.00  8.96           O  
ANISOU 1550  O   PHE C  48     1315    884   1204   -113     25    -15       O  
ATOM   1551  CB  PHE C  48      44.101 -15.401 -48.671  1.00  9.79           C  
ANISOU 1551  CB  PHE C  48     1366    987   1367   -122     85    -48       C  
ATOM   1552  CG  PHE C  48      45.090 -14.834 -47.711  1.00  8.60           C  
ANISOU 1552  CG  PHE C  48     1173    838   1257   -122     89    -65       C  
ATOM   1553  CD1 PHE C  48      46.149 -15.601 -47.278  1.00 10.17           C  
ANISOU 1553  CD1 PHE C  48     1334   1036   1494   -120     94    -83       C  
ATOM   1554  CD2 PHE C  48      44.892 -13.578 -47.122  1.00  8.99           C  
ANISOU 1554  CD2 PHE C  48     1217    886   1309   -122     78    -65       C  
ATOM   1555  CE1 PHE C  48      47.057 -15.108 -46.347  1.00 10.54           C  
ANISOU 1555  CE1 PHE C  48     1339   1080   1583   -120     84   -100       C  
ATOM   1556  CE2 PHE C  48      45.803 -13.085 -46.203  1.00 11.07           C  
ANISOU 1556  CE2 PHE C  48     1445   1147   1612   -122     71    -85       C  
ATOM   1557  CZ  PHE C  48      46.882 -13.864 -45.800  1.00 10.23           C  
ANISOU 1557  CZ  PHE C  48     1300   1040   1545   -121     70   -102       C  
ATOM   1558  N   ILE C  49      40.930 -15.526 -48.890  1.00  8.15           N  
ANISOU 1558  N   ILE C  49     1203    792   1100   -108     11      2       N  
ATOM   1559  CA  ILE C  49      39.821 -15.366 -49.807  1.00  8.30           C  
ANISOU 1559  CA  ILE C  49     1261    799   1093   -110     -9     21       C  
ATOM   1560  C   ILE C  49      40.169 -14.205 -50.724  1.00  9.65           C  
ANISOU 1560  C   ILE C  49     1472    950   1245   -121     16     19       C  
ATOM   1561  O   ILE C  49      40.704 -13.202 -50.301  1.00  9.65           O  
ANISOU 1561  O   ILE C  49     1458    949   1258   -123     37     12       O  
ATOM   1562  CB  ILE C  49      38.509 -15.052 -49.055  1.00  8.72           C  
ANISOU 1562  CB  ILE C  49     1293    865   1154    -98    -43     44       C  
ATOM   1563  CG1 ILE C  49      38.036 -16.254 -48.236  1.00  8.93           C  
ANISOU 1563  CG1 ILE C  49     1284    908   1199    -88    -64     54       C  
ATOM   1564  CG2 ILE C  49      37.437 -14.497 -49.978  1.00 10.12           C  
ANISOU 1564  CG2 ILE C  49     1505   1025   1313    -99    -67     63       C  
ATOM   1565  CD1 ILE C  49      37.071 -15.877 -47.092  1.00 10.42           C  
ANISOU 1565  CD1 ILE C  49     1440   1115   1403    -71    -76     74       C  
ATOM   1566  N   SER C  50      39.921 -14.402 -52.009  1.00 11.25           N  
ANISOU 1566  N   SER C  50     1728   1132   1414   -127     15     24       N  
ATOM   1567  CA ASER C  50      39.972 -13.340 -52.972  0.50  9.83           C  
ANISOU 1567  CA ASER C  50     1599    930   1207   -134     33     31       C  
ATOM   1568  CA BSER C  50      39.958 -13.338 -52.969  0.50  9.75           C  
ANISOU 1568  CA BSER C  50     1588    919   1196   -134     32     31       C  
ATOM   1569  C   SER C  50      38.573 -12.731 -53.003  1.00  9.90           C  
ANISOU 1569  C   SER C  50     1618    935   1207   -127    -15     54       C  
ATOM   1570  O   SER C  50      37.625 -13.318 -53.556  1.00 11.25           O  
ANISOU 1570  O   SER C  50     1813   1098   1362   -124    -58     66       O  
ATOM   1571  CB ASER C  50      40.355 -13.902 -54.344  0.50 11.07           C  
ANISOU 1571  CB ASER C  50     1820   1064   1323   -140     53     25       C  
ATOM   1572  CB BSER C  50      40.300 -13.889 -54.345  0.50 10.76           C  
ANISOU 1572  CB BSER C  50     1781   1025   1283   -140     51     26       C  
ATOM   1573  OG ASER C  50      40.565 -12.872 -55.304  0.50 13.59           O  
ANISOU 1573  OG ASER C  50     2195   1359   1610   -147     81     34       O  
ATOM   1574  OG BSER C  50      41.679 -14.157 -54.431  0.50 11.94           O  
ANISOU 1574  OG BSER C  50     1921   1171   1444   -146    109      6       O  
ATOM   1575  N   MET C  51      38.441 -11.563 -52.409  1.00 10.01           N  
ANISOU 1575  N   MET C  51     1613    951   1237   -124    -10     60       N  
ATOM   1576  CA  MET C  51      37.197 -10.818 -52.384  1.00 11.00           C  
ANISOU 1576  CA  MET C  51     1743   1070   1364   -114    -49     82       C  
ATOM   1577  C   MET C  51      36.983 -10.078 -53.709  1.00 10.62           C  
ANISOU 1577  C   MET C  51     1764    991   1279   -120    -54     95       C  
ATOM   1578  O   MET C  51      37.802  -9.264 -54.098  1.00 11.62           O  
ANISOU 1578  O   MET C  51     1917   1102   1395   -130    -13     92       O  
ATOM   1579  CB  MET C  51      37.211  -9.789 -51.238  1.00  9.93           C  
ANISOU 1579  CB  MET C  51     1567    945   1258   -104    -39     79       C  
ATOM   1580  CG  MET C  51      35.921  -8.974 -51.130  1.00 10.60           C  
ANISOU 1580  CG  MET C  51     1651   1023   1351    -89    -73    100       C  
ATOM   1581  SD  MET C  51      35.731  -8.103 -49.588  1.00 11.44           S  
ANISOU 1581  SD  MET C  51     1709   1145   1490    -69    -65     94       S  
ATOM   1582  CE  MET C  51      37.299  -7.287 -49.504  1.00 11.68           C  
ANISOU 1582  CE  MET C  51     1750   1164   1521    -86    -22     68       C  
ATOM   1583  N   THR C  52      35.850 -10.354 -54.355  1.00 12.49           N  
ANISOU 1583  N   THR C  52     2028   1215   1501   -114   -106    113       N  
ATOM   1584  CA  THR C  52      35.545  -9.769 -55.668  1.00 13.23           C  
ANISOU 1584  CA  THR C  52     2198   1276   1553   -117   -123    128       C  
ATOM   1585  C   THR C  52      34.278  -8.923 -55.655  1.00 14.27           C  
ANISOU 1585  C   THR C  52     2327   1394   1700   -104   -175    153       C  
ATOM   1586  O   THR C  52      33.960  -8.270 -56.659  1.00 14.50           O  
ANISOU 1586  O   THR C  52     2418   1393   1696   -104   -196    168       O  
ATOM   1587  CB  THR C  52      35.431 -10.879 -56.717  1.00 15.03           C  
ANISOU 1587  CB  THR C  52     2480   1490   1739   -120   -149    125       C  
ATOM   1588  OG1 THR C  52      34.438 -11.828 -56.304  1.00 16.65           O  
ANISOU 1588  OG1 THR C  52     2645   1705   1975   -113   -206    129       O  
ATOM   1589  CG2 THR C  52      36.791 -11.569 -56.902  1.00 16.55           C  
ANISOU 1589  CG2 THR C  52     2685   1689   1914   -130    -87    101       C  
ATOM   1590  N   SER C  53      33.641  -8.831 -54.484  1.00 12.83           N  
ANISOU 1590  N   SER C  53     2074   1233   1568    -92   -188    156       N  
ATOM   1591  CA ASER C  53      32.479  -7.987 -54.256  0.50 12.43           C  
ANISOU 1591  CA ASER C  53     2004   1172   1546    -75   -227    178       C  
ATOM   1592  CA BSER C  53      32.503  -7.966 -54.260  0.50 13.62           C  
ANISOU 1592  CA BSER C  53     2155   1322   1695    -75   -225    177       C  
ATOM   1593  C   SER C  53      32.551  -7.553 -52.809  1.00 12.72           C  
ANISOU 1593  C   SER C  53     1975   1234   1624    -63   -196    169       C  
ATOM   1594  O   SER C  53      32.827  -8.394 -51.951  1.00 12.97           O  
ANISOU 1594  O   SER C  53     1963   1293   1671    -62   -178    157       O  
ATOM   1595  CB ASER C  53      31.181  -8.761 -54.477  0.50 12.55           C  
ANISOU 1595  CB ASER C  53     2002   1181   1584    -67   -293    195       C  
ATOM   1596  CB BSER C  53      31.202  -8.703 -54.536  0.50 16.00           C  
ANISOU 1596  CB BSER C  53     2443   1616   2018    -68   -293    196       C  
ATOM   1597  OG ASER C  53      30.041  -7.965 -54.173  0.50 12.68           O  
ANISOU 1597  OG ASER C  53     1987   1187   1641    -49   -327    217       O  
ATOM   1598  OG BSER C  53      31.214  -9.253 -55.837  0.50 25.29           O  
ANISOU 1598  OG BSER C  53     3688   2769   3150    -78   -327    197       O  
ATOM   1599  N  AARG C  54      32.352  -6.263 -52.544  0.50 12.23           N  
ANISOU 1599  N  AARG C  54     1912   1159   1574    -52   -189    175       N  
ATOM   1600  N  BARG C  54      32.293  -6.273 -52.541  0.50 12.41           N  
ANISOU 1600  N  BARG C  54     1933   1181   1598    -51   -191    176       N  
ATOM   1601  CA AARG C  54      32.319  -5.732 -51.185  0.50 12.02           C  
ANISOU 1601  CA AARG C  54     1833   1150   1580    -35   -164    165       C  
ATOM   1602  CA BARG C  54      32.335  -5.709 -51.195  0.50 12.15           C  
ANISOU 1602  CA BARG C  54     1851   1167   1597    -35   -164    165       C  
ATOM   1603  C  AARG C  54      31.148  -4.800 -51.052  0.50 13.59           C  
ANISOU 1603  C  AARG C  54     2020   1333   1809    -11   -192    184       C  
ATOM   1604  C  BARG C  54      31.173  -4.763 -51.031  0.50 13.77           C  
ANISOU 1604  C  BARG C  54     2042   1355   1832    -11   -190    183       C  
ATOM   1605  O  AARG C  54      30.916  -3.965 -51.923  0.50 13.32           O  
ANISOU 1605  O  AARG C  54     2027   1267   1764    -13   -212    197       O  
ATOM   1606  O  BARG C  54      30.973  -3.875 -51.858  0.50 13.26           O  
ANISOU 1606  O  BARG C  54     2019   1259   1757    -12   -209    196       O  
ATOM   1607  CB AARG C  54      33.604  -4.975 -50.861  0.50 10.84           C  
ANISOU 1607  CB AARG C  54     1697   1000   1421    -45   -118    141       C  
ATOM   1608  CB BARG C  54      33.646  -4.949 -50.987  0.50 11.27           C  
ANISOU 1608  CB BARG C  54     1756   1051   1472    -47   -118    142       C  
ATOM   1609  CG AARG C  54      33.557  -4.249 -49.534  0.50 11.00           C  
ANISOU 1609  CG AARG C  54     1679   1031   1469    -25   -101    128       C  
ATOM   1610  CG BARG C  54      33.832  -4.369 -49.601  0.50 11.59           C  
ANISOU 1610  CG BARG C  54     1757   1106   1538    -31    -95    124       C  
ATOM   1611  CD AARG C  54      34.889  -3.574 -49.203  0.50 10.43           C  
ANISOU 1611  CD AARG C  54     1617    952   1394    -39    -65    101       C  
ATOM   1612  CD BARG C  54      35.289  -3.960 -49.391  0.50 12.75           C  
ANISOU 1612  CD BARG C  54     1913   1249   1680    -49    -58     98       C  
ATOM   1613  NE AARG C  54      34.725  -2.636 -48.105  0.50 13.20           N  
ANISOU 1613  NE AARG C  54     1947   1301   1766    -17    -60     87       N  
ATOM   1614  NE BARG C  54      35.725  -2.827 -50.197  0.50 15.03           N  
ANISOU 1614  NE BARG C  54     2245   1502   1963    -63    -47    102       N  
ATOM   1615  CZ AARG C  54      35.691  -2.190 -47.301  0.50 14.19           C  
ANISOU 1615  CZ AARG C  54     2064   1426   1900    -20    -40     59       C  
ATOM   1616  CZ BARG C  54      36.986  -2.584 -50.555  0.50 15.58           C  
ANISOU 1616  CZ BARG C  54     2331   1558   2030    -87    -13     90       C  
ATOM   1617  NH1AARG C  54      36.938  -2.605 -47.426  0.50 15.05           N  
ANISOU 1617  NH1AARG C  54     2173   1538   2006    -45    -21     42       N  
ATOM   1618  NH1BARG C  54      38.001  -3.382 -50.162  0.50 11.50           N  
ANISOU 1618  NH1BARG C  54     1790   1060   1518   -100     10     69       N  
ATOM   1619  NH2AARG C  54      35.398  -1.303 -46.365  0.50 15.00           N  
ANISOU 1619  NH2AARG C  54     2158   1522   2016      3    -42     45       N  
ATOM   1620  NH2BARG C  54      37.226  -1.496 -51.276  0.50 12.42           N  
ANISOU 1620  NH2BARG C  54     1970   1121   1627    -99     -2    101       N  
ATOM   1621  N   GLU C  55      30.420  -4.923 -49.952  1.00 14.53           N  
ANISOU 1621  N   GLU C  55     2082   1471   1965     11   -189    187       N  
ATOM   1622  CA  GLU C  55      29.350  -4.000 -49.620  1.00 15.09           C  
ANISOU 1622  CA  GLU C  55     2131   1527   2073     39   -203    202       C  
ATOM   1623  C   GLU C  55      28.371  -3.837 -50.769  1.00 15.98           C  
ANISOU 1623  C   GLU C  55     2264   1608   2198     40   -260    231       C  
ATOM   1624  O   GLU C  55      27.837  -2.750 -50.963  1.00 17.58           O  
ANISOU 1624  O   GLU C  55     2475   1784   2418     56   -276    241       O  
ATOM   1625  CB  GLU C  55      29.941  -2.652 -49.173  1.00 16.73           C  
ANISOU 1625  CB  GLU C  55     2357   1722   2275     47   -173    184       C  
ATOM   1626  CG  GLU C  55      30.637  -2.742 -47.827  1.00 20.84           C  
ANISOU 1626  CG  GLU C  55     2853   2271   2794     56   -129    155       C  
ATOM   1627  CD  GLU C  55      31.236  -1.432 -47.410  1.00 31.49           C  
ANISOU 1627  CD  GLU C  55     4222   3602   4140     62   -109    133       C  
ATOM   1628  OE1 GLU C  55      32.403  -1.163 -47.798  1.00 32.71           O  
ANISOU 1628  OE1 GLU C  55     4408   3746   4274     36    -96    117       O  
ATOM   1629  OE2 GLU C  55      30.523  -0.677 -46.712  1.00 34.45           O  
ANISOU 1629  OE2 GLU C  55     4580   3970   4539     94   -105    133       O  
ATOM   1630  N   GLY C  56      28.121  -4.923 -51.499  1.00 13.85           N  
ANISOU 1630  N   GLY C  56     2002   1339   1922     24   -296    242       N  
ATOM   1631  CA  GLY C  56      27.142  -4.923 -52.565  1.00 17.32           C  
ANISOU 1631  CA  GLY C  56     2459   1746   2373     26   -364    267       C  
ATOM   1632  C   GLY C  56      27.645  -4.554 -53.931  1.00 20.47           C  
ANISOU 1632  C   GLY C  56     2944   2115   2716      8   -388    269       C  
ATOM   1633  O   GLY C  56      26.882  -4.635 -54.905  1.00 22.08           O  
ANISOU 1633  O   GLY C  56     3177   2290   2922      9   -454    289       O  
ATOM   1634  N   SER C  57      28.905  -4.114 -54.034  1.00 16.86           N  
ANISOU 1634  N   SER C  57     2531   1661   2213     -6   -338    251       N  
ATOM   1635  CA  SER C  57      29.448  -3.642 -55.320  1.00 15.66           C  
ANISOU 1635  CA  SER C  57     2466   1478   2006    -21   -346    256       C  
ATOM   1636  C   SER C  57      30.626  -4.467 -55.779  1.00 18.08           C  
ANISOU 1636  C   SER C  57     2812   1796   2261    -46   -309    238       C  
ATOM   1637  O   SER C  57      31.440  -4.857 -54.986  1.00 14.89           O  
ANISOU 1637  O   SER C  57     2373   1420   1862    -54   -259    216       O  
ATOM   1638  CB  SER C  57      29.919  -2.203 -55.170  1.00 20.45           C  
ANISOU 1638  CB  SER C  57     3092   2066   2611    -18   -311    256       C  
ATOM   1639  OG  SER C  57      28.819  -1.331 -54.975  1.00 25.77           O  
ANISOU 1639  OG  SER C  57     3744   2720   3328      7   -349    274       O  
ATOM   1640  N   PRO C  58      30.752  -4.709 -57.089  1.00 17.56           N  
ANISOU 1640  N   PRO C  58     2824   1705   2141    -57   -334    247       N  
ATOM   1641  CA  PRO C  58      31.897  -5.452 -57.602  1.00 16.36           C  
ANISOU 1641  CA  PRO C  58     2716   1560   1938    -77   -291    229       C  
ATOM   1642  C   PRO C  58      33.211  -4.717 -57.514  1.00 17.08           C  
ANISOU 1642  C   PRO C  58     2824   1650   2012    -91   -213    219       C  
ATOM   1643  O   PRO C  58      33.271  -3.487 -57.745  1.00 20.72           O  
ANISOU 1643  O   PRO C  58     3313   2086   2470    -89   -203    233       O  
ATOM   1644  CB  PRO C  58      31.550  -5.647 -59.083  1.00 22.68           C  
ANISOU 1644  CB  PRO C  58     3609   2326   2679    -78   -340    245       C  
ATOM   1645  CG  PRO C  58      30.755  -4.439 -59.409  1.00 24.32           C  
ANISOU 1645  CG  PRO C  58     3840   2503   2897    -65   -381    272       C  
ATOM   1646  CD  PRO C  58      29.985  -4.068 -58.175  1.00 22.97           C  
ANISOU 1646  CD  PRO C  58     3573   2349   2805    -49   -394    274       C  
ATOM   1647  N   LEU C  59      34.257  -5.482 -57.230  1.00 14.80           N  
ANISOU 1647  N   LEU C  59     2520   1385   1717   -104   -161    195       N  
ATOM   1648  CA  LEU C  59      35.614  -4.982 -57.212  1.00 14.85           C  
ANISOU 1648  CA  LEU C  59     2537   1388   1716   -120    -86    184       C  
ATOM   1649  C   LEU C  59      36.318  -5.381 -58.491  1.00 21.01           C  
ANISOU 1649  C   LEU C  59     3398   2149   2435   -132    -55    187       C  
ATOM   1650  O   LEU C  59      36.315  -6.548 -58.876  1.00 22.15           O  
ANISOU 1650  O   LEU C  59     3559   2302   2553   -132    -67    177       O  
ATOM   1651  CB  LEU C  59      36.366  -5.528 -55.993  1.00 15.66           C  
ANISOU 1651  CB  LEU C  59     2563   1526   1860   -125    -49    156       C  
ATOM   1652  CG  LEU C  59      35.804  -5.124 -54.635  1.00 13.70           C  
ANISOU 1652  CG  LEU C  59     2243   1297   1665   -110    -68    151       C  
ATOM   1653  CD1 LEU C  59      36.617  -5.840 -53.569  1.00 17.30           C  
ANISOU 1653  CD1 LEU C  59     2640   1785   2147   -113    -37    124       C  
ATOM   1654  CD2 LEU C  59      35.875  -3.608 -54.443  1.00 16.95           C  
ANISOU 1654  CD2 LEU C  59     2660   1686   2094   -108    -56    158       C  
ATOM   1655  N   GLU C  60      36.910  -4.409 -59.158  1.00 17.32           N  
ANISOU 1655  N   GLU C  60     2985   1653   1944   -142    -14    202       N  
ATOM   1656  CA  GLU C  60      37.691  -4.707 -60.358  1.00 19.98           C  
ANISOU 1656  CA  GLU C  60     3403   1969   2218   -152     33    206       C  
ATOM   1657  C   GLU C  60      38.944  -5.534 -59.992  1.00 19.34           C  
ANISOU 1657  C   GLU C  60     3281   1910   2154   -164    102    178       C  
ATOM   1658  O   GLU C  60      39.265  -6.522 -60.667  1.00 24.00           O  
ANISOU 1658  O   GLU C  60     3914   2502   2704   -163    119    169       O  
ATOM   1659  CB  GLU C  60      38.049  -3.397 -61.068  1.00 19.81           C  
ANISOU 1659  CB  GLU C  60     3442   1909   2174   -159     70    234       C  
ATOM   1660  CG  GLU C  60      39.040  -3.577 -62.181  1.00 21.01           C  
ANISOU 1660  CG  GLU C  60     3674   2040   2269   -170    144    241       C  
ATOM   1661  CD  GLU C  60      39.108  -2.396 -63.116  1.00 20.99           C  
ANISOU 1661  CD  GLU C  60     3755   1993   2226   -174    168    278       C  
ATOM   1662  OE1 GLU C  60      38.317  -1.434 -62.956  1.00 20.15           O  
ANISOU 1662  OE1 GLU C  60     3649   1869   2135   -167    117    298       O  
ATOM   1663  OE2 GLU C  60      39.987  -2.456 -64.000  1.00 23.67           O  
ANISOU 1663  OE2 GLU C  60     4160   2313   2519   -182    243    288       O  
ATOM   1664  N   ASN C  61      39.643  -5.132 -58.933  1.00 15.89           N  
ANISOU 1664  N   ASN C  61     2767   1489   1781   -173    138    164       N  
ATOM   1665  CA  ASN C  61      40.889  -5.745 -58.479  1.00 16.63           C  
ANISOU 1665  CA  ASN C  61     2812   1598   1907   -185    200    139       C  
ATOM   1666  C   ASN C  61      40.599  -6.554 -57.202  1.00 19.22           C  
ANISOU 1666  C   ASN C  61     3057   1965   2280   -176    160    115       C  
ATOM   1667  O   ASN C  61      40.225  -5.989 -56.212  1.00 18.70           O  
ANISOU 1667  O   ASN C  61     2939   1910   2254   -172    133    112       O  
ATOM   1668  CB  ASN C  61      41.946  -4.686 -58.222  1.00 19.21           C  
ANISOU 1668  CB  ASN C  61     3113   1907   2277   -203    262    142       C  
ATOM   1669  CG  ASN C  61      42.249  -3.849 -59.472  1.00 26.54           C  
ANISOU 1669  CG  ASN C  61     4126   2794   3163   -213    309    172       C  
ATOM   1670  OD1 ASN C  61      42.217  -2.615 -59.437  1.00 38.96           O  
ANISOU 1670  OD1 ASN C  61     5705   4342   4755   -221    314    191       O  
ATOM   1671  ND2 ASN C  61      42.507  -4.526 -60.582  1.00 27.32           N  
ANISOU 1671  ND2 ASN C  61     4295   2883   3201   -211    344    178       N  
ATOM   1672  N   PRO C  62      40.768  -7.880 -57.228  1.00 15.82           N  
ANISOU 1672  N   PRO C  62     2617   1553   1839   -172    159     98       N  
ATOM   1673  CA  PRO C  62      40.441  -8.627 -56.011  1.00 14.77           C  
ANISOU 1673  CA  PRO C  62     2410   1454   1747   -164    122     81       C  
ATOM   1674  C   PRO C  62      41.299  -8.251 -54.818  1.00 13.36           C  
ANISOU 1674  C   PRO C  62     2158   1290   1627   -170    149     63       C  
ATOM   1675  O   PRO C  62      42.435  -7.811 -54.962  1.00 18.89           O  
ANISOU 1675  O   PRO C  62     2853   1976   2348   -184    205     57       O  
ATOM   1676  CB  PRO C  62      40.665 -10.103 -56.415  1.00 17.94           C  
ANISOU 1676  CB  PRO C  62     2824   1864   2126   -161    125     67       C  
ATOM   1677  CG  PRO C  62      40.698 -10.118 -57.897  1.00 24.89           C  
ANISOU 1677  CG  PRO C  62     3797   2715   2943   -162    143     78       C  
ATOM   1678  CD  PRO C  62      41.195  -8.769 -58.332  1.00 18.35           C  
ANISOU 1678  CD  PRO C  62     2999   1863   2110   -173    189     94       C  
ATOM   1679  N   VAL C  63      40.713  -8.403 -53.630  1.00 12.60           N  
ANISOU 1679  N   VAL C  63     2007   1219   1560   -158    108     57       N  
ATOM   1680  CA  VAL C  63      41.324  -8.001 -52.397  1.00 13.40           C  
ANISOU 1680  CA  VAL C  63     2048   1332   1710   -158    116     39       C  
ATOM   1681  C   VAL C  63      41.453  -9.259 -51.527  1.00 10.62           C  
ANISOU 1681  C   VAL C  63     1649   1011   1375   -149    101     23       C  
ATOM   1682  O   VAL C  63      40.472 -10.001 -51.329  1.00 11.47           O  
ANISOU 1682  O   VAL C  63     1753   1135   1470   -136     62     31       O  
ATOM   1683  CB  VAL C  63      40.435  -6.965 -51.704  1.00 10.69           C  
ANISOU 1683  CB  VAL C  63     1693    988   1378   -146     82     47       C  
ATOM   1684  CG1 VAL C  63      40.912  -6.643 -50.282  1.00 11.21           C  
ANISOU 1684  CG1 VAL C  63     1703   1068   1485   -140     79     25       C  
ATOM   1685  CG2 VAL C  63      40.417  -5.678 -52.519  1.00 13.25           C  
ANISOU 1685  CG2 VAL C  63     2063   1278   1692   -155     97     64       C  
ATOM   1686  N   ASP C  64      42.654  -9.491 -51.048  1.00 11.04           N  
ANISOU 1686  N   ASP C  64     1665   1067   1462   -157    130      2       N  
ATOM   1687  CA  ASP C  64      42.915 -10.615 -50.114  1.00  9.87           C  
ANISOU 1687  CA  ASP C  64     1471    944   1333   -147    114    -13       C  
ATOM   1688  C   ASP C  64      42.280 -10.398 -48.761  1.00 10.89           C  
ANISOU 1688  C   ASP C  64     1567   1095   1474   -130     75    -15       C  
ATOM   1689  O   ASP C  64      42.382  -9.323 -48.150  1.00 11.28           O  
ANISOU 1689  O   ASP C  64     1606   1138   1540   -128     71    -21       O  
ATOM   1690  CB  ASP C  64      44.406 -10.787 -49.869  1.00 14.42           C  
ANISOU 1690  CB  ASP C  64     2011   1514   1952   -158    148    -35       C  
ATOM   1691  CG  ASP C  64      45.177 -11.217 -51.082  1.00 17.52           C  
ANISOU 1691  CG  ASP C  64     2428   1888   2338   -171    199    -36       C  
ATOM   1692  OD1 ASP C  64      44.625 -11.780 -52.035  1.00 18.28           O  
ANISOU 1692  OD1 ASP C  64     2573   1981   2390   -168    202    -25       O  
ATOM   1693  OD2 ASP C  64      46.405 -10.961 -51.054  1.00 27.01           O  
ANISOU 1693  OD2 ASP C  64     3601   3076   3585   -183    238    -49       O  
ATOM   1694  N   VAL C  65      41.585 -11.419 -48.266  1.00  8.63           N  
ANISOU 1694  N   VAL C  65     1268    832   1180   -116     47     -8       N  
ATOM   1695  CA  VAL C  65      40.986 -11.383 -46.937  1.00  7.61           C  
ANISOU 1695  CA  VAL C  65     1110    724   1057    -96     19     -7       C  
ATOM   1696  C   VAL C  65      41.460 -12.658 -46.237  1.00  7.71           C  
ANISOU 1696  C   VAL C  65     1093    755   1081    -89     12    -16       C  
ATOM   1697  O   VAL C  65      41.205 -13.783 -46.696  1.00  8.67           O  
ANISOU 1697  O   VAL C  65     1218    880   1194    -91      7     -7       O  
ATOM   1698  CB  VAL C  65      39.445 -11.359 -46.996  1.00  8.29           C  
ANISOU 1698  CB  VAL C  65     1207    816   1124    -82     -5     18       C  
ATOM   1699  CG1 VAL C  65      38.820 -11.293 -45.618  1.00  9.00           C  
ANISOU 1699  CG1 VAL C  65     1271    927   1220    -58    -20     22       C  
ATOM   1700  CG2 VAL C  65      38.975 -10.176 -47.837  1.00 10.21           C  
ANISOU 1700  CG2 VAL C  65     1484   1037   1357    -87     -3     29       C  
ATOM   1701  N   PHE C  66      42.171 -12.486 -45.148  1.00  7.63           N  
ANISOU 1701  N   PHE C  66     1056    752   1089    -82      6    -34       N  
ATOM   1702  CA  PHE C  66      42.607 -13.633 -44.335  1.00  7.83           C  
ANISOU 1702  CA  PHE C  66     1055    793   1125    -72     -7    -40       C  
ATOM   1703  C   PHE C  66      41.399 -14.402 -43.822  1.00  7.55           C  
ANISOU 1703  C   PHE C  66     1019    778   1069    -55    -25    -15       C  
ATOM   1704  O   PHE C  66      40.375 -13.819 -43.441  1.00  7.62           O  
ANISOU 1704  O   PHE C  66     1037    794   1064    -41    -31      0       O  
ATOM   1705  CB  PHE C  66      43.390 -13.097 -43.142  1.00  7.60           C  
ANISOU 1705  CB  PHE C  66     1007    766   1113    -62    -22    -63       C  
ATOM   1706  CG  PHE C  66      43.844 -14.146 -42.182  1.00  7.97           C  
ANISOU 1706  CG  PHE C  66     1032    827   1167    -49    -43    -68       C  
ATOM   1707  CD1 PHE C  66      45.036 -14.856 -42.376  1.00  8.43           C  
ANISOU 1707  CD1 PHE C  66     1066    876   1259    -58    -41    -84       C  
ATOM   1708  CD2 PHE C  66      43.100 -14.414 -41.049  1.00  8.40           C  
ANISOU 1708  CD2 PHE C  66     1092    902   1196    -24    -64    -56       C  
ATOM   1709  CE1 PHE C  66      45.447 -15.804 -41.431  1.00  8.88           C  
ANISOU 1709  CE1 PHE C  66     1105    944   1324    -43    -67    -88       C  
ATOM   1710  CE2 PHE C  66      43.525 -15.359 -40.128  1.00  7.90           C  
ANISOU 1710  CE2 PHE C  66     1017    850   1135     -9    -85    -57       C  
ATOM   1711  CZ  PHE C  66      44.693 -16.056 -40.342  1.00  7.98           C  
ANISOU 1711  CZ  PHE C  66     1003    850   1178    -20    -91    -73       C  
ATOM   1712  N   VAL C  67      41.525 -15.728 -43.756  1.00  6.87           N  
ANISOU 1712  N   VAL C  67      921    699    989    -53    -32    -10       N  
ATOM   1713  CA  VAL C  67      40.466 -16.568 -43.184  1.00  6.63           C  
ANISOU 1713  CA  VAL C  67      885    685    949    -39    -47     16       C  
ATOM   1714  C   VAL C  67      41.049 -17.712 -42.337  1.00  7.53           C  
ANISOU 1714  C   VAL C  67      979    807   1072    -29    -58     14       C  
ATOM   1715  O   VAL C  67      41.928 -18.430 -42.790  1.00  7.68           O  
ANISOU 1715  O   VAL C  67      991    817   1108    -39    -56      0       O  
ATOM   1716  CB  VAL C  67      39.551 -17.143 -44.270  1.00  7.08           C  
ANISOU 1716  CB  VAL C  67      954    732   1003    -50    -51     37       C  
ATOM   1717  CG1 VAL C  67      40.336 -17.851 -45.350  1.00  8.94           C  
ANISOU 1717  CG1 VAL C  67     1200    951   1244    -67    -43     22       C  
ATOM   1718  CG2 VAL C  67      38.500 -18.058 -43.629  1.00  8.30           C  
ANISOU 1718  CG2 VAL C  67     1092    899   1163    -38    -66     67       C  
ATOM   1719  N   HIS C  68      40.596 -17.796 -41.101  1.00  7.43           N  
ANISOU 1719  N   HIS C  68      962    812   1047     -7    -68     28       N  
ATOM   1720  CA  HIS C  68      40.968 -18.850 -40.179  1.00  7.14           C  
ANISOU 1720  CA  HIS C  68      914    784   1013      5    -81     34       C  
ATOM   1721  C   HIS C  68      39.899 -19.899 -40.150  1.00  7.17           C  
ANISOU 1721  C   HIS C  68      912    792   1018      8    -81     71       C  
ATOM   1722  O   HIS C  68      38.716 -19.582 -40.269  1.00  7.29           O  
ANISOU 1722  O   HIS C  68      929    810   1027     10    -72     94       O  
ATOM   1723  CB  HIS C  68      41.186 -18.268 -38.771  1.00  7.47           C  
ANISOU 1723  CB  HIS C  68      966    839   1033     30    -92     27       C  
ATOM   1724  CG  HIS C  68      41.864 -19.237 -37.850  1.00  8.53           C  
ANISOU 1724  CG  HIS C  68     1095    977   1168     44   -113     27       C  
ATOM   1725  ND1 HIS C  68      41.189 -19.864 -36.875  1.00 10.87           N  
ANISOU 1725  ND1 HIS C  68     1401   1286   1441     65   -113     58       N  
ATOM   1726  CD2 HIS C  68      43.141 -19.704 -37.822  1.00  8.70           C  
ANISOU 1726  CD2 HIS C  68     1103    988   1214     39   -134      4       C  
ATOM   1727  CE1 HIS C  68      42.021 -20.700 -36.230  1.00 10.53           C  
ANISOU 1727  CE1 HIS C  68     1356   1241   1401     74   -138     54       C  
ATOM   1728  NE2 HIS C  68      43.226 -20.608 -36.801  1.00  8.59           N  
ANISOU 1728  NE2 HIS C  68     1093    981   1188     59   -154     20       N  
ATOM   1729  N   GLN C  69      40.313 -21.168 -39.993  1.00  7.50           N  
ANISOU 1729  N   GLN C  69      945    831   1074      7    -93     77       N  
ATOM   1730  CA  GLN C  69      39.370 -22.298 -39.933  1.00  7.66           C  
ANISOU 1730  CA  GLN C  69      956    850   1104      7    -95    113       C  
ATOM   1731  C   GLN C  69      38.231 -22.085 -38.930  1.00  8.02           C  
ANISOU 1731  C   GLN C  69     1001    911   1134     27    -82    149       C  
ATOM   1732  O   GLN C  69      37.122 -22.536 -39.165  1.00  8.21           O  
ANISOU 1732  O   GLN C  69     1012    930   1174     22    -77    182       O  
ATOM   1733  CB  GLN C  69      40.093 -23.647 -39.663  1.00  8.46           C  
ANISOU 1733  CB  GLN C  69     1048    942   1221      9   -111    114       C  
ATOM   1734  CG  GLN C  69      40.847 -23.701 -38.359  1.00 10.06           C  
ANISOU 1734  CG  GLN C  69     1255   1156   1409     32   -122    110       C  
ATOM   1735  CD  GLN C  69      40.035 -24.137 -37.137  1.00 10.53           C  
ANISOU 1735  CD  GLN C  69     1322   1229   1449     53   -117    151       C  
ATOM   1736  OE1 GLN C  69      38.856 -24.480 -37.259  1.00 10.25           O  
ANISOU 1736  OE1 GLN C  69     1279   1193   1421     49   -102    187       O  
ATOM   1737  NE2 GLN C  69      40.653 -24.089 -35.940  1.00 14.69           N  
ANISOU 1737  NE2 GLN C  69     1866   1765   1951     77   -131    148       N  
ATOM   1738  N   SER C  70      38.498 -21.430 -37.792  1.00  8.14           N  
ANISOU 1738  N   SER C  70     1031    942   1120     51    -76    143       N  
ATOM   1739  CA  SER C  70      37.526 -21.228 -36.751  1.00  9.62           C  
ANISOU 1739  CA  SER C  70     1225   1143   1285     75    -55    175       C  
ATOM   1740  C   SER C  70      36.340 -20.359 -37.147  1.00  9.50           C  
ANISOU 1740  C   SER C  70     1203   1129   1276     75    -32    190       C  
ATOM   1741  O   SER C  70      35.273 -20.367 -36.466  1.00 12.24           O  
ANISOU 1741  O   SER C  70     1545   1484   1619     93     -5    225       O  
ATOM   1742  CB  SER C  70      38.193 -20.633 -35.498  1.00 10.55           C  
ANISOU 1742  CB  SER C  70     1373   1274   1361    103    -59    158       C  
ATOM   1743  OG  SER C  70      38.659 -19.345 -35.714  1.00 13.84           O  
ANISOU 1743  OG  SER C  70     1801   1688   1768    103    -64    120       O  
ATOM   1744  N   LYS C  71      36.467 -19.670 -38.283  1.00  7.96           N  
ANISOU 1744  N   LYS C  71     1006    923   1093     55    -41    166       N  
ATOM   1745  CA  LYS C  71      35.459 -18.733 -38.774  1.00  8.31           C  
ANISOU 1745  CA  LYS C  71     1045    964   1146     55    -29    175       C  
ATOM   1746  C   LYS C  71      34.590 -19.319 -39.873  1.00  9.16           C  
ANISOU 1746  C   LYS C  71     1132   1056   1291     33    -40    198       C  
ATOM   1747  O   LYS C  71      33.726 -18.606 -40.423  1.00 10.82           O  
ANISOU 1747  O   LYS C  71     1336   1260   1516     31    -39    206       O  
ATOM   1748  CB  LYS C  71      36.102 -17.438 -39.257  1.00 10.76           C  
ANISOU 1748  CB  LYS C  71     1375   1270   1443     49    -34    137       C  
ATOM   1749  CG  LYS C  71      36.957 -16.752 -38.211  1.00 12.74           C  
ANISOU 1749  CG  LYS C  71     1647   1530   1663     69    -32    110       C  
ATOM   1750  CD  LYS C  71      36.376 -16.660 -36.828  1.00 15.28           C  
ANISOU 1750  CD  LYS C  71     1980   1867   1957    104    -13    128       C  
ATOM   1751  CE  LYS C  71      37.185 -15.733 -35.935  1.00 23.53           C  
ANISOU 1751  CE  LYS C  71     3057   2915   2968    125    -21     93       C  
ATOM   1752  NZ  LYS C  71      36.471 -15.621 -34.650  1.00 25.74           N  
ANISOU 1752  NZ  LYS C  71     3357   3208   3212    163      3    113       N  
ATOM   1753  N   LEU C  72      34.768 -20.604 -40.206  1.00  8.24           N  
ANISOU 1753  N   LEU C  72     1005    930   1194     17    -57    207       N  
ATOM   1754  CA  LEU C  72      34.056 -21.265 -41.309  1.00  7.29           C  
ANISOU 1754  CA  LEU C  72      871    789   1110     -4    -79    222       C  
ATOM   1755  C   LEU C  72      32.789 -21.953 -40.838  1.00  8.72           C  
ANISOU 1755  C   LEU C  72     1019    967   1328      0    -73    271       C  
ATOM   1756  O   LEU C  72      32.827 -22.702 -39.869  1.00  9.51           O  
ANISOU 1756  O   LEU C  72     1110   1075   1429     10    -57    292       O  
ATOM   1757  CB  LEU C  72      34.973 -22.296 -41.953  1.00  7.99           C  
ANISOU 1757  CB  LEU C  72      969    863   1201    -22   -101    202       C  
ATOM   1758  CG  LEU C  72      36.299 -21.764 -42.447  1.00  8.38           C  
ANISOU 1758  CG  LEU C  72     1044    912   1225    -27   -100    158       C  
ATOM   1759  CD1 LEU C  72      37.115 -22.916 -43.037  1.00  9.54           C  
ANISOU 1759  CD1 LEU C  72     1197   1043   1382    -40   -114    142       C  
ATOM   1760  CD2 LEU C  72      36.099 -20.637 -43.459  1.00  8.22           C  
ANISOU 1760  CD2 LEU C  72     1043    884   1195    -37   -101    143       C  
ATOM   1761  N   TYR C  73      31.690 -21.611 -41.456  1.00  9.70           N  
ANISOU 1761  N   TYR C  73     1125   1078   1483     -6    -84    288       N  
ATOM   1762  CA  TYR C  73      30.415 -22.269 -41.240  1.00 10.34           C  
ANISOU 1762  CA  TYR C  73     1163   1147   1618     -8    -82    336       C  
ATOM   1763  C   TYR C  73      30.348 -23.598 -42.026  1.00 10.99           C  
ANISOU 1763  C   TYR C  73     1236   1201   1736    -35   -124    342       C  
ATOM   1764  O   TYR C  73      30.243 -23.591 -43.268  1.00 11.90           O  
ANISOU 1764  O   TYR C  73     1365   1294   1862    -55   -167    324       O  
ATOM   1765  CB  TYR C  73      29.290 -21.345 -41.672  1.00 11.64           C  
ANISOU 1765  CB  TYR C  73     1307   1302   1812     -5    -86    350       C  
ATOM   1766  CG  TYR C  73      27.912 -21.953 -41.555  1.00 14.33           C  
ANISOU 1766  CG  TYR C  73     1593   1625   2225     -9    -88    399       C  
ATOM   1767  CD1 TYR C  73      27.381 -22.254 -40.311  1.00 16.14           C  
ANISOU 1767  CD1 TYR C  73     1792   1868   2473     10    -37    439       C  
ATOM   1768  CD2 TYR C  73      27.144 -22.174 -42.688  1.00 14.38           C  
ANISOU 1768  CD2 TYR C  73     1580   1600   2282    -31   -141    407       C  
ATOM   1769  CE1 TYR C  73      26.092 -22.789 -40.192  1.00 18.32           C  
ANISOU 1769  CE1 TYR C  73     2009   2124   2827      6    -31    490       C  
ATOM   1770  CE2 TYR C  73      25.844 -22.667 -42.581  1.00 17.41           C  
ANISOU 1770  CE2 TYR C  73     1904   1963   2746    -36   -147    453       C  
ATOM   1771  CZ  TYR C  73      25.365 -22.997 -41.336  1.00 16.81           C  
ANISOU 1771  CZ  TYR C  73     1790   1899   2696    -18    -89    495       C  
ATOM   1772  OH  TYR C  73      24.089 -23.518 -41.223  1.00 23.51           O  
ANISOU 1772  OH  TYR C  73     2573   2725   3635    -25    -88    545       O  
ATOM   1773  N   MET C  74      30.460 -24.689 -41.296  1.00 13.10           N  
ANISOU 1773  N   MET C  74     1491   1469   2018    -34   -113    365       N  
ATOM   1774  CA  MET C  74      30.344 -26.055 -41.831  1.00 12.84           C  
ANISOU 1774  CA  MET C  74     1446   1406   2025    -57   -149    375       C  
ATOM   1775  C   MET C  74      30.416 -26.981 -40.661  1.00 12.33           C  
ANISOU 1775  C   MET C  74     1366   1347   1970    -47   -120    409       C  
ATOM   1776  O   MET C  74      30.905 -26.612 -39.592  1.00 13.50           O  
ANISOU 1776  O   MET C  74     1528   1523   2076    -23    -81    411       O  
ATOM   1777  CB  MET C  74      31.439 -26.382 -42.835  1.00 11.70           C  
ANISOU 1777  CB  MET C  74     1343   1249   1852    -71   -183    327       C  
ATOM   1778  CG  MET C  74      32.837 -26.203 -42.257  1.00 12.48           C  
ANISOU 1778  CG  MET C  74     1470   1373   1899    -56   -158    297       C  
ATOM   1779  SD  MET C  74      34.146 -25.829 -43.434  1.00 10.88           S  
ANISOU 1779  SD  MET C  74     1312   1163   1655    -66   -174    237       S  
ATOM   1780  CE  MET C  74      34.109 -27.266 -44.514  1.00 11.98           C  
ANISOU 1780  CE  MET C  74     1461   1262   1825    -87   -218    230       C  
ATOM   1781  N   GLU C  75      29.868 -28.178 -40.852  1.00 14.33           N  
ANISOU 1781  N   GLU C  75     1593   1571   2280    -65   -143    438       N  
ATOM   1782  CA  GLU C  75      29.931 -29.219 -39.855  1.00 14.71           C  
ANISOU 1782  CA  GLU C  75     1628   1616   2343    -60   -120    474       C  
ATOM   1783  C   GLU C  75      31.200 -30.010 -40.059  1.00 14.16           C  
ANISOU 1783  C   GLU C  75     1593   1540   2245    -64   -145    441       C  
ATOM   1784  O   GLU C  75      31.781 -30.015 -41.158  1.00 16.33           O  
ANISOU 1784  O   GLU C  75     1891   1802   2509    -77   -182    396       O  
ATOM   1785  CB  GLU C  75      28.721 -30.165 -39.942  1.00 14.77           C  
ANISOU 1785  CB  GLU C  75     1586   1589   2436    -80   -133    525       C  
ATOM   1786  CG  GLU C  75      27.430 -29.514 -39.430  1.00 22.52           C  
ANISOU 1786  CG  GLU C  75     2521   2576   3458    -70    -93    571       C  
ATOM   1787  CD  GLU C  75      26.171 -30.329 -39.686  1.00 32.64           C  
ANISOU 1787  CD  GLU C  75     3742   3817   4842    -95   -111    620       C  
ATOM   1788  OE1 GLU C  75      26.245 -31.579 -39.754  1.00 46.30           O  
ANISOU 1788  OE1 GLU C  75     5463   5517   6610   -114   -136    636       O  
ATOM   1789  OE2 GLU C  75      25.093 -29.701 -39.812  1.00 50.25           O  
ANISOU 1789  OE2 GLU C  75     5928   6042   7120    -94   -103    643       O  
ATOM   1790  N   GLY C  76      31.649 -30.633 -38.986  1.00 14.48           N  
ANISOU 1790  N   GLY C  76     1639   1590   2273    -49   -120    463       N  
ATOM   1791  CA  GLY C  76      32.850 -31.459 -39.057  1.00 12.59           C  
ANISOU 1791  CA  GLY C  76     1426   1341   2015    -49   -143    436       C  
ATOM   1792  C   GLY C  76      34.106 -30.635 -39.166  1.00 12.67           C  
ANISOU 1792  C   GLY C  76     1471   1376   1966    -35   -143    382       C  
ATOM   1793  O   GLY C  76      34.199 -29.529 -38.588  1.00 13.61           O  
ANISOU 1793  O   GLY C  76     1600   1525   2044    -17   -115    376       O  
ATOM   1794  N   PHE C  77      35.113 -31.200 -39.826  1.00 11.19           N  
ANISOU 1794  N   PHE C  77     1300   1172   1776    -43   -172    344       N  
ATOM   1795  CA  PHE C  77      36.422 -30.545 -39.938  1.00  9.43           C  
ANISOU 1795  CA  PHE C  77     1103    968   1511    -31   -170    294       C  
ATOM   1796  C   PHE C  77      36.336 -29.329 -40.846  1.00 11.24           C  
ANISOU 1796  C   PHE C  77     1342   1205   1721    -39   -167    262       C  
ATOM   1797  O   PHE C  77      35.781 -29.396 -41.933  1.00 12.26           O  
ANISOU 1797  O   PHE C  77     1473   1315   1870    -58   -186    256       O  
ATOM   1798  CB  PHE C  77      37.431 -31.533 -40.507  1.00 10.75           C  
ANISOU 1798  CB  PHE C  77     1280   1110   1693    -36   -195    265       C  
ATOM   1799  CG  PHE C  77      38.835 -30.997 -40.550  1.00 10.52           C  
ANISOU 1799  CG  PHE C  77     1266   1095   1636    -24   -190    218       C  
ATOM   1800  CD1 PHE C  77      39.602 -30.982 -39.436  1.00 11.49           C  
ANISOU 1800  CD1 PHE C  77     1390   1233   1741     -3   -186    221       C  
ATOM   1801  CD2 PHE C  77      39.351 -30.497 -41.725  1.00 10.68           C  
ANISOU 1801  CD2 PHE C  77     1300   1108   1648    -34   -190    175       C  
ATOM   1802  CE1 PHE C  77      40.888 -30.472 -39.476  1.00 10.78           C  
ANISOU 1802  CE1 PHE C  77     1305   1151   1638      6   -187    179       C  
ATOM   1803  CE2 PHE C  77      40.630 -30.013 -41.767  1.00 10.47           C  
ANISOU 1803  CE2 PHE C  77     1279   1090   1607    -25   -181    136       C  
ATOM   1804  CZ  PHE C  77      41.376 -30.002 -40.645  1.00 10.63           C  
ANISOU 1804  CZ  PHE C  77     1292   1125   1623     -6   -181    138       C  
ATOM   1805  N   ARG C  78      36.879 -28.222 -40.363  1.00  9.20           N  
ANISOU 1805  N   ARG C  78     1094    974   1424    -24   -147    244       N  
ATOM   1806  CA  ARG C  78      36.776 -26.933 -41.057  1.00  8.77           C  
ANISOU 1806  CA  ARG C  78     1051    929   1350    -29   -140    219       C  
ATOM   1807  C   ARG C  78      38.008 -26.622 -41.857  1.00  8.09           C  
ANISOU 1807  C   ARG C  78      985    839   1250    -34   -143    170       C  
ATOM   1808  O   ARG C  78      39.141 -26.639 -41.368  1.00  9.49           O  
ANISOU 1808  O   ARG C  78     1164   1023   1418    -23   -140    149       O  
ATOM   1809  CB  ARG C  78      36.533 -25.826 -40.036  1.00  8.59           C  
ANISOU 1809  CB  ARG C  78     1029    935   1299     -8   -113    229       C  
ATOM   1810  CG  ARG C  78      35.224 -25.978 -39.284  1.00  8.95           C  
ANISOU 1810  CG  ARG C  78     1055    986   1359      0    -95    280       C  
ATOM   1811  CD  ARG C  78      34.977 -24.880 -38.243  1.00 10.13           C  
ANISOU 1811  CD  ARG C  78     1212   1162   1474     25    -63    287       C  
ATOM   1812  NE  ARG C  78      35.981 -24.913 -37.241  1.00 10.81           N  
ANISOU 1812  NE  ARG C  78     1320   1261   1523     45    -61    274       N  
ATOM   1813  CZ  ARG C  78      35.982 -25.718 -36.199  1.00 14.86           C  
ANISOU 1813  CZ  ARG C  78     1838   1778   2029     61    -53    304       C  
ATOM   1814  NH1 ARG C  78      34.954 -26.540 -36.015  1.00 18.44           N  
ANISOU 1814  NH1 ARG C  78     2270   2221   2513     57    -38    353       N  
ATOM   1815  NH2 ARG C  78      37.008 -25.711 -35.339  1.00 17.14           N  
ANISOU 1815  NH2 ARG C  78     2153   2076   2282     81    -63    287       N  
ATOM   1816  N   SER C  79      37.784 -26.333 -43.143  1.00  8.34           N  
ANISOU 1816  N   SER C  79     1031    855   1282    -51   -151    152       N  
ATOM   1817  CA  SER C  79      38.812 -25.850 -44.067  1.00  8.28           C  
ANISOU 1817  CA  SER C  79     1046    841   1258    -57   -143    109       C  
ATOM   1818  C   SER C  79      38.089 -25.296 -45.295  1.00  9.21           C  
ANISOU 1818  C   SER C  79     1187    945   1366    -72   -151    105       C  
ATOM   1819  O   SER C  79      36.878 -25.422 -45.388  1.00  7.97           O  
ANISOU 1819  O   SER C  79     1023    782   1224    -77   -171    133       O  
ATOM   1820  CB  SER C  79      39.777 -26.987 -44.471  1.00  9.14           C  
ANISOU 1820  CB  SER C  79     1159    929   1382    -58   -149     87       C  
ATOM   1821  OG  SER C  79      39.130 -27.956 -45.293  1.00  9.34           O  
ANISOU 1821  OG  SER C  79     1197    927   1423    -70   -173     94       O  
ATOM   1822  N   LEU C  80      38.844 -24.672 -46.215  1.00  8.14           N  
ANISOU 1822  N   LEU C  80     1080    803   1209    -77   -136     73       N  
ATOM   1823  CA  LEU C  80      38.357 -24.300 -47.540  1.00  8.27           C  
ANISOU 1823  CA  LEU C  80     1133    800   1208    -90   -146     65       C  
ATOM   1824  C   LEU C  80      39.199 -24.973 -48.599  1.00  8.71           C  
ANISOU 1824  C   LEU C  80     1223    832   1253    -94   -140     35       C  
ATOM   1825  O   LEU C  80      40.346 -25.343 -48.363  1.00  8.86           O  
ANISOU 1825  O   LEU C  80     1233    853   1280    -88   -116     14       O  
ATOM   1826  CB  LEU C  80      38.427 -22.774 -47.734  1.00  8.45           C  
ANISOU 1826  CB  LEU C  80     1170    834   1206    -90   -126     59       C  
ATOM   1827  CG  LEU C  80      37.533 -21.925 -46.867  1.00  8.49           C  
ANISOU 1827  CG  LEU C  80     1150    859   1216    -82   -129     85       C  
ATOM   1828  CD1 LEU C  80      37.820 -20.452 -47.176  1.00  8.16           C  
ANISOU 1828  CD1 LEU C  80     1127    821   1151    -83   -108     72       C  
ATOM   1829  CD2 LEU C  80      36.051 -22.263 -47.061  1.00  9.11           C  
ANISOU 1829  CD2 LEU C  80     1220    927   1314    -86   -163    116       C  
ATOM   1830  N   LYS C  81      38.605 -25.149 -49.771  1.00 10.10           N  
ANISOU 1830  N   LYS C  81     1440    983   1413   -103   -164     31       N  
ATOM   1831  CA  LYS C  81      39.274 -25.638 -50.958  1.00 11.32           C  
ANISOU 1831  CA  LYS C  81     1645   1112   1545   -105   -154      0       C  
ATOM   1832  C   LYS C  81      39.468 -24.502 -51.939  1.00 11.19           C  
ANISOU 1832  C   LYS C  81     1676   1090   1484   -108   -131    -12       C  
ATOM   1833  O   LYS C  81      38.595 -23.665 -52.086  1.00 11.14           O  
ANISOU 1833  O   LYS C  81     1678   1087   1467   -113   -151      5       O  
ATOM   1834  CB  LYS C  81      38.439 -26.730 -51.595  1.00 15.65           C  
ANISOU 1834  CB  LYS C  81     2217   1628   2098   -111   -205      3       C  
ATOM   1835  CG  LYS C  81      39.127 -27.454 -52.731  1.00 16.93           C  
ANISOU 1835  CG  LYS C  81     2436   1760   2236   -107   -197    -31       C  
ATOM   1836  CD  LYS C  81      38.210 -28.525 -53.278  1.00 23.98           C  
ANISOU 1836  CD  LYS C  81     3353   2617   3138   -113   -260    -29       C  
ATOM   1837  CE  LYS C  81      38.868 -29.429 -54.298  1.00 39.21           C  
ANISOU 1837  CE  LYS C  81     5343   4512   5043   -105   -256    -67       C  
ATOM   1838  NZ  LYS C  81      38.209 -30.769 -54.262  1.00 41.92           N  
ANISOU 1838  NZ  LYS C  81     5681   4824   5422   -110   -315    -63       N  
ATOM   1839  N   GLU C  82      40.657 -24.433 -52.505  1.00 11.19           N  
ANISOU 1839  N   GLU C  82     1701   1083   1466   -104    -83    -40       N  
ATOM   1840  CA  GLU C  82      40.998 -23.435 -53.510  1.00 12.38           C  
ANISOU 1840  CA  GLU C  82     1903   1224   1574   -107    -49    -50       C  
ATOM   1841  C   GLU C  82      39.878 -23.328 -54.541  1.00 12.20           C  
ANISOU 1841  C   GLU C  82     1943   1180   1513   -112    -95    -42       C  
ATOM   1842  O   GLU C  82      39.436 -24.337 -55.098  1.00 13.44           O  
ANISOU 1842  O   GLU C  82     2131   1312   1662   -111   -134    -49       O  
ATOM   1843  CB  GLU C  82      42.347 -23.770 -54.188  1.00 15.96           C  
ANISOU 1843  CB  GLU C  82     2383   1663   2017   -101     10    -81       C  
ATOM   1844  CG  GLU C  82      42.794 -22.746 -55.207  1.00 17.76           C  
ANISOU 1844  CG  GLU C  82     2665   1879   2201   -103     58    -88       C  
ATOM   1845  CD  GLU C  82      44.001 -23.159 -56.054  1.00 32.68           C  
ANISOU 1845  CD  GLU C  82     4590   3748   4077    -94    124   -116       C  
ATOM   1846  OE1 GLU C  82      44.800 -24.020 -55.616  1.00 36.65           O  
ANISOU 1846  OE1 GLU C  82     5054   4251   4620    -85    144   -133       O  
ATOM   1847  OE2 GLU C  82      44.158 -22.597 -57.171  1.00 39.03           O  
ANISOU 1847  OE2 GLU C  82     5464   4535   4831    -94    160   -120       O  
ATOM   1848  N   GLY C  83      39.427 -22.105 -54.769  1.00 11.83           N  
ANISOU 1848  N   GLY C  83     1912   1137   1444   -117    -96    -27       N  
ATOM   1849  CA  GLY C  83      38.422 -21.811 -55.770  1.00 12.52           C  
ANISOU 1849  CA  GLY C  83     2060   1201   1493   -120   -142    -18       C  
ATOM   1850  C   GLY C  83      36.984 -21.847 -55.322  1.00 11.83           C  
ANISOU 1850  C   GLY C  83     1940   1115   1437   -124   -212      9       C  
ATOM   1851  O   GLY C  83      36.085 -21.370 -56.033  1.00 15.28           O  
ANISOU 1851  O   GLY C  83     2416   1534   1852   -126   -257     21       O  
ATOM   1852  N   GLU C  84      36.711 -22.412 -54.156  1.00 11.39           N  
ANISOU 1852  N   GLU C  84     1812   1078   1434   -124   -224     23       N  
ATOM   1853  CA  GLU C  84      35.322 -22.520 -53.744  1.00 11.31           C  
ANISOU 1853  CA  GLU C  84     1767   1067   1463   -127   -282     53       C  
ATOM   1854  C   GLU C  84      34.705 -21.141 -53.460  1.00 11.32           C  
ANISOU 1854  C   GLU C  84     1752   1082   1466   -125   -282     75       C  
ATOM   1855  O   GLU C  84      35.357 -20.263 -52.868  1.00 10.87           O  
ANISOU 1855  O   GLU C  84     1676   1048   1404   -120   -232     72       O  
ATOM   1856  CB  GLU C  84      35.153 -23.491 -52.581  1.00 11.77           C  
ANISOU 1856  CB  GLU C  84     1758   1138   1574   -127   -287     66       C  
ATOM   1857  CG  GLU C  84      35.449 -23.000 -51.174  1.00 11.16           C  
ANISOU 1857  CG  GLU C  84     1619   1098   1522   -119   -246     80       C  
ATOM   1858  CD  GLU C  84      34.969 -23.983 -50.160  1.00 11.06           C  
ANISOU 1858  CD  GLU C  84     1552   1092   1557   -118   -261    103       C  
ATOM   1859  OE1 GLU C  84      33.755 -24.014 -49.868  1.00 10.67           O  
ANISOU 1859  OE1 GLU C  84     1471   1038   1542   -120   -293    134       O  
ATOM   1860  OE2 GLU C  84      35.808 -24.747 -49.676  1.00 11.85           O  
ANISOU 1860  OE2 GLU C  84     1639   1198   1664   -114   -240     91       O  
ATOM   1861  N   PRO C  85      33.460 -20.909 -53.901  1.00 10.67           N  
ANISOU 1861  N   PRO C  85     1676    980   1395   -128   -340     95       N  
ATOM   1862  CA  PRO C  85      32.819 -19.629 -53.740  1.00 11.65           C  
ANISOU 1862  CA  PRO C  85     1789   1112   1525   -123   -344    115       C  
ATOM   1863  C   PRO C  85      32.360 -19.400 -52.287  1.00 12.14           C  
ANISOU 1863  C   PRO C  85     1769   1203   1640   -115   -325    139       C  
ATOM   1864  O   PRO C  85      31.866 -20.324 -51.638  1.00 11.21           O  
ANISOU 1864  O   PRO C  85     1603   1088   1566   -116   -341    154       O  
ATOM   1865  CB  PRO C  85      31.638 -19.708 -54.699  1.00 13.88           C  
ANISOU 1865  CB  PRO C  85     2101   1359   1811   -127   -422    128       C  
ATOM   1866  CG  PRO C  85      31.347 -21.139 -54.809  1.00 13.20           C  
ANISOU 1866  CG  PRO C  85     2007   1255   1753   -135   -463    125       C  
ATOM   1867  CD  PRO C  85      32.650 -21.823 -54.739  1.00 14.01           C  
ANISOU 1867  CD  PRO C  85     2128   1367   1825   -135   -412     96       C  
ATOM   1868  N   VAL C  86      32.505 -18.178 -51.805  1.00 10.14           N  
ANISOU 1868  N   VAL C  86     1504    969   1380   -106   -291    143       N  
ATOM   1869  CA  VAL C  86      32.243 -17.870 -50.421  1.00 10.58           C  
ANISOU 1869  CA  VAL C  86     1496   1051   1470    -94   -263    160       C  
ATOM   1870  C   VAL C  86      31.553 -16.519 -50.294  1.00  9.98           C  
ANISOU 1870  C   VAL C  86     1413    976   1402    -83   -264    175       C  
ATOM   1871  O   VAL C  86      31.743 -15.630 -51.152  1.00 11.64           O  
ANISOU 1871  O   VAL C  86     1670   1171   1579    -85   -269    166       O  
ATOM   1872  CB  VAL C  86      33.533 -17.899 -49.533  1.00 10.42           C  
ANISOU 1872  CB  VAL C  86     1465   1059   1435    -90   -207    139       C  
ATOM   1873  CG1 VAL C  86      34.097 -19.302 -49.406  1.00 11.87           C  
ANISOU 1873  CG1 VAL C  86     1641   1243   1625    -96   -207    129       C  
ATOM   1874  CG2 VAL C  86      34.586 -16.929 -50.066  1.00 11.01           C  
ANISOU 1874  CG2 VAL C  86     1581   1130   1469    -93   -175    114       C  
ATOM   1875  N   GLU C  87      30.763 -16.371 -49.220  1.00  9.76           N  
ANISOU 1875  N   GLU C  87     1328    963   1416    -68   -255    198       N  
ATOM   1876  CA  GLU C  87      30.203 -15.124 -48.775  1.00 11.30           C  
ANISOU 1876  CA  GLU C  87     1507   1164   1623    -51   -243    210       C  
ATOM   1877  C   GLU C  87      30.682 -14.950 -47.349  1.00 10.40           C  
ANISOU 1877  C   GLU C  87     1361   1080   1508    -35   -190    206       C  
ATOM   1878  O   GLU C  87      30.750 -15.924 -46.612  1.00 10.54           O  
ANISOU 1878  O   GLU C  87     1351   1113   1540    -34   -178    213       O  
ATOM   1879  CB  GLU C  87      28.665 -15.169 -48.735  1.00 13.65           C  
ANISOU 1879  CB  GLU C  87     1760   1447   1979    -43   -279    245       C  
ATOM   1880  CG  GLU C  87      27.987 -15.343 -50.058  1.00 19.48           C  
ANISOU 1880  CG  GLU C  87     2524   2149   2727    -56   -347    253       C  
ATOM   1881  CD  GLU C  87      26.451 -15.366 -49.971  1.00 18.02           C  
ANISOU 1881  CD  GLU C  87     2283   1947   2616    -48   -387    289       C  
ATOM   1882  OE1 GLU C  87      25.845 -15.286 -48.875  1.00 22.37           O  
ANISOU 1882  OE1 GLU C  87     2771   2513   3213    -31   -354    311       O  
ATOM   1883  OE2 GLU C  87      25.866 -15.536 -51.018  1.00 20.98           O  
ANISOU 1883  OE2 GLU C  87     2677   2288   3003    -58   -454    295       O  
ATOM   1884  N   PHE C  88      30.957 -13.737 -46.887  1.00  9.20           N  
ANISOU 1884  N   PHE C  88     1217    937   1341    -21   -161    195       N  
ATOM   1885  CA  PHE C  88      31.503 -13.568 -45.568  1.00  9.31           C  
ANISOU 1885  CA  PHE C  88     1215    977   1346     -4   -119    185       C  
ATOM   1886  C   PHE C  88      31.313 -12.183 -45.024  1.00  8.73           C  
ANISOU 1886  C   PHE C  88     1142    905   1268     16    -99    180       C  
ATOM   1887  O   PHE C  88      31.122 -11.232 -45.777  1.00  9.65           O  
ANISOU 1887  O   PHE C  88     1281   1001   1381     13   -113    178       O  
ATOM   1888  CB  PHE C  88      33.041 -13.855 -45.594  1.00  8.83           C  
ANISOU 1888  CB  PHE C  88     1180    923   1250    -18   -103    152       C  
ATOM   1889  CG  PHE C  88      33.735 -13.162 -46.725  1.00  8.71           C  
ANISOU 1889  CG  PHE C  88     1208    890   1211    -35   -108    133       C  
ATOM   1890  CD1 PHE C  88      33.772 -13.735 -47.995  1.00  9.42           C  
ANISOU 1890  CD1 PHE C  88     1327    960   1291    -55   -132    133       C  
ATOM   1891  CD2 PHE C  88      34.259 -11.884 -46.558  1.00 11.71           C  
ANISOU 1891  CD2 PHE C  88     1604   1266   1578    -31    -88    116       C  
ATOM   1892  CE1 PHE C  88      34.319 -13.062 -49.067  1.00 10.39           C  
ANISOU 1892  CE1 PHE C  88     1497   1063   1386    -67   -129    120       C  
ATOM   1893  CE2 PHE C  88      34.810 -11.208 -47.635  1.00 12.62           C  
ANISOU 1893  CE2 PHE C  88     1760   1359   1675    -47    -88    105       C  
ATOM   1894  CZ  PHE C  88      34.842 -11.806 -48.884  1.00 11.85           C  
ANISOU 1894  CZ  PHE C  88     1693   1245   1562    -64   -105    108       C  
ATOM   1895  N   THR C  89      31.374 -12.088 -43.707  1.00  9.29           N  
ANISOU 1895  N   THR C  89     1195    996   1335     39    -66    179       N  
ATOM   1896  CA  THR C  89      31.561 -10.825 -43.030  1.00  9.21           C  
ANISOU 1896  CA  THR C  89     1198    989   1310     60    -44    161       C  
ATOM   1897  C   THR C  89      33.058 -10.703 -42.694  1.00  8.57           C  
ANISOU 1897  C   THR C  89     1144    915   1196     51    -35    125       C  
ATOM   1898  O   THR C  89      33.738 -11.734 -42.524  1.00  8.88           O  
ANISOU 1898  O   THR C  89     1179    966   1227     40    -35    120       O  
ATOM   1899  CB  THR C  89      30.746 -10.748 -41.755  1.00 10.73           C  
ANISOU 1899  CB  THR C  89     1365   1197   1513     95    -13    178       C  
ATOM   1900  OG1 THR C  89      31.023 -11.931 -40.987  1.00 12.48           O  
ANISOU 1900  OG1 THR C  89     1574   1440   1727     96      0    186       O  
ATOM   1901  CG2 THR C  89      29.252 -10.632 -42.127  1.00 12.60           C  
ANISOU 1901  CG2 THR C  89     1568   1420   1798    105    -20    214       C  
ATOM   1902  N   PHE C  90      33.566  -9.472 -42.511  1.00  9.55           N  
ANISOU 1902  N   PHE C  90     1290   1030   1307     58    -28    100       N  
ATOM   1903  CA  PHE C  90      34.996  -9.256 -42.305  1.00  9.71           C  
ANISOU 1903  CA  PHE C  90     1329   1049   1310     45    -25     66       C  
ATOM   1904  C   PHE C  90      35.239  -7.918 -41.654  1.00 10.86           C  
ANISOU 1904  C   PHE C  90     1492   1185   1448     63    -19     42       C  
ATOM   1905  O   PHE C  90      34.311  -7.122 -41.522  1.00 10.73           O  
ANISOU 1905  O   PHE C  90     1477   1161   1438     84    -13     52       O  
ATOM   1906  CB  PHE C  90      35.758  -9.369 -43.647  1.00 10.43           C  
ANISOU 1906  CB  PHE C  90     1436   1123   1402     11    -35     59       C  
ATOM   1907  CG  PHE C  90      35.517  -8.249 -44.603  1.00 10.28           C  
ANISOU 1907  CG  PHE C  90     1441   1078   1387      2    -39     61       C  
ATOM   1908  CD1 PHE C  90      34.421  -8.243 -45.452  1.00 12.50           C  
ANISOU 1908  CD1 PHE C  90     1726   1347   1675      2    -56     89       C  
ATOM   1909  CD2 PHE C  90      36.413  -7.207 -44.687  1.00 10.52           C  
ANISOU 1909  CD2 PHE C  90     1490   1090   1416     -6    -31     38       C  
ATOM   1910  CE1 PHE C  90      34.232  -7.193 -46.369  1.00 11.18           C  
ANISOU 1910  CE1 PHE C  90     1587   1152   1507     -4    -64     93       C  
ATOM   1911  CE2 PHE C  90      36.223  -6.172 -45.581  1.00 12.34           C  
ANISOU 1911  CE2 PHE C  90     1746   1292   1649    -14    -33     44       C  
ATOM   1912  CZ  PHE C  90      35.117  -6.166 -46.402  1.00 12.68           C  
ANISOU 1912  CZ  PHE C  90     1798   1325   1692    -12    -50     72       C  
ATOM   1913  N   LYS C  91      36.470  -7.677 -41.249  1.00  8.92           N  
ANISOU 1913  N   LYS C  91     1257    936   1194     55    -22     11       N  
ATOM   1914  CA  LYS C  91      36.892  -6.420 -40.649  1.00  9.93           C  
ANISOU 1914  CA  LYS C  91     1404   1048   1318     67    -24    -17       C  
ATOM   1915  C   LYS C  91      38.313  -6.090 -41.045  1.00 10.41           C  
ANISOU 1915  C   LYS C  91     1470   1089   1393     38    -34    -45       C  
ATOM   1916  O   LYS C  91      39.090  -6.960 -41.436  1.00  9.16           O  
ANISOU 1916  O   LYS C  91     1299    937   1243     16    -35    -47       O  
ATOM   1917  CB  LYS C  91      36.844  -6.485 -39.121  1.00 11.24           C  
ANISOU 1917  CB  LYS C  91     1578   1231   1461    102    -23    -31       C  
ATOM   1918  CG  LYS C  91      37.743  -7.533 -38.493  1.00 12.09           C  
ANISOU 1918  CG  LYS C  91     1678   1356   1557     98    -34    -42       C  
ATOM   1919  CD  LYS C  91      37.754  -7.505 -36.942  1.00 15.83           C  
ANISOU 1919  CD  LYS C  91     2174   1842   1996    136    -38    -57       C  
ATOM   1920  CE  LYS C  91      38.766  -8.490 -36.367  1.00 17.85           C  
ANISOU 1920  CE  LYS C  91     2426   2110   2243    131    -59    -69       C  
ATOM   1921  NZ  LYS C  91      38.849  -8.558 -34.869  1.00 23.53           N  
ANISOU 1921  NZ  LYS C  91     3178   2841   2920    169    -69    -83       N  
ATOM   1922  N   LYS C  92      38.672  -4.813 -40.961  1.00 11.02           N  
ANISOU 1922  N   LYS C  92     1564   1140   1481     37    -39    -67       N  
ATOM   1923  CA ALYS C  92      40.049  -4.377 -41.136  0.50 11.34           C  
ANISOU 1923  CA ALYS C  92     1602   1158   1546     11    -48    -94       C  
ATOM   1924  CA BLYS C  92      40.044  -4.333 -41.078  0.50 11.93           C  
ANISOU 1924  CA BLYS C  92     1678   1232   1620     12    -49    -95       C  
ATOM   1925  C   LYS C  92      40.862  -4.773 -39.858  1.00 11.05           C  
ANISOU 1925  C   LYS C  92     1560   1132   1505     24    -71   -124       C  
ATOM   1926  O   LYS C  92      40.367  -4.792 -38.718  1.00 13.15           O  
ANISOU 1926  O   LYS C  92     1840   1413   1742     58    -80   -131       O  
ATOM   1927  CB ALYS C  92      40.102  -2.852 -41.396  0.50 12.59           C  
ANISOU 1927  CB ALYS C  92     1781   1279   1723      6    -50   -106       C  
ATOM   1928  CB BLYS C  92      40.048  -2.804 -41.067  0.50 12.75           C  
ANISOU 1928  CB BLYS C  92     1803   1301   1739     14    -54   -111       C  
ATOM   1929  CG ALYS C  92      41.328  -2.358 -42.180  0.50 13.76           C  
ANISOU 1929  CG ALYS C  92     1923   1394   1909    -32    -45   -117       C  
ATOM   1930  CG BLYS C  92      41.383  -2.165 -41.450  0.50 17.01           C  
ANISOU 1930  CG BLYS C  92     2337   1807   2318    -18    -59   -133       C  
ATOM   1931  CD ALYS C  92      41.262  -0.856 -42.432  0.50 16.38           C  
ANISOU 1931  CD ALYS C  92     2276   1685   2260    -36    -47   -123       C  
ATOM   1932  CD BLYS C  92      41.312  -0.655 -41.298  0.50 23.85           C  
ANISOU 1932  CD BLYS C  92     3225   2635   3200    -13    -69   -149       C  
ATOM   1933  CE ALYS C  92      42.662  -0.259 -42.539  0.50 22.23           C  
ANISOU 1933  CE ALYS C  92     3005   2391   3050    -67    -51   -147       C  
ATOM   1934  CE BLYS C  92      39.888  -0.164 -41.518  0.50 23.24           C  
ANISOU 1934  CE BLYS C  92     3169   2559   3100     11    -59   -126       C  
ATOM   1935  NZ ALYS C  92      42.791   0.999 -41.755  0.50 27.14           N  
ANISOU 1935  NZ ALYS C  92     3641   2980   3690    -56    -78   -177       N  
ATOM   1936  NZ BLYS C  92      39.234   0.344 -40.266  0.50 22.67           N  
ANISOU 1936  NZ BLYS C  92     3115   2491   3008     55    -73   -146       N  
ATOM   1937  N   SER C  93      42.130  -5.141 -40.066  1.00 10.28           N  
ANISOU 1937  N   SER C  93     1442   1026   1436     -2    -79   -140       N  
ATOM   1938  CA  SER C  93      43.061  -5.463 -38.976  1.00 11.52           C  
ANISOU 1938  CA  SER C  93     1592   1186   1599      6   -112   -169       C  
ATOM   1939  C   SER C  93      44.483  -5.299 -39.496  1.00 10.39           C  
ANISOU 1939  C   SER C  93     1419   1015   1512    -29   -118   -188       C  
ATOM   1940  O   SER C  93      44.705  -5.044 -40.681  1.00 11.36           O  
ANISOU 1940  O   SER C  93     1532   1120   1661    -58    -88   -175       O  
ATOM   1941  CB  SER C  93      42.848  -6.865 -38.413  1.00 11.97           C  
ANISOU 1941  CB  SER C  93     1641   1278   1629     23   -116   -156       C  
ATOM   1942  OG  SER C  93      43.295  -7.802 -39.357  1.00 12.40           O  
ANISOU 1942  OG  SER C  93     1667   1337   1705     -3    -99   -141       O  
ATOM   1943  N   SER C  94      45.446  -5.582 -38.634  1.00 11.88           N  
ANISOU 1943  N   SER C  94     1594   1200   1720    -26   -155   -215       N  
ATOM   1944  CA  SER C  94      46.836  -5.595 -39.085  1.00 11.99           C  
ANISOU 1944  CA  SER C  94     1568   1187   1800    -59   -160   -230       C  
ATOM   1945  C   SER C  94      47.125  -6.712 -40.107  1.00 10.86           C  
ANISOU 1945  C   SER C  94     1396   1057   1671    -79   -122   -207       C  
ATOM   1946  O   SER C  94      48.135  -6.668 -40.791  1.00 12.83           O  
ANISOU 1946  O   SER C  94     1612   1283   1976   -107   -104   -212       O  
ATOM   1947  CB  SER C  94      47.796  -5.716 -37.923  1.00 13.81           C  
ANISOU 1947  CB  SER C  94     1785   1408   2053    -49   -218   -265       C  
ATOM   1948  OG  SER C  94      47.537  -6.886 -37.135  1.00 12.93           O  
ANISOU 1948  OG  SER C  94     1682   1330   1899    -21   -237   -259       O  
ATOM   1949  N   LYS C  95      46.214  -7.658 -40.258  1.00 10.91           N  
ANISOU 1949  N   LYS C  95     1416   1098   1631    -64   -105   -181       N  
ATOM   1950  CA  LYS C  95      46.333  -8.642 -41.322  1.00  9.59           C  
ANISOU 1950  CA  LYS C  95     1233    938   1471    -81    -69   -160       C  
ATOM   1951  C   LYS C  95      45.982  -8.074 -42.716  1.00 11.07           C  
ANISOU 1951  C   LYS C  95     1436   1110   1658   -103    -24   -141       C  
ATOM   1952  O   LYS C  95      46.193  -8.779 -43.719  1.00 12.44           O  
ANISOU 1952  O   LYS C  95     1606   1285   1836   -118      8   -127       O  
ATOM   1953  CB  LYS C  95      45.485  -9.867 -41.016  1.00  9.16           C  
ANISOU 1953  CB  LYS C  95     1188    919   1373    -59    -72   -140       C  
ATOM   1954  CG  LYS C  95      45.711 -10.488 -39.646  1.00 10.05           C  
ANISOU 1954  CG  LYS C  95     1295   1047   1474    -34   -113   -152       C  
ATOM   1955  CD  LYS C  95      44.998 -11.838 -39.511  1.00 10.40           C  
ANISOU 1955  CD  LYS C  95     1343   1121   1487    -19   -108   -126       C  
ATOM   1956  CE  LYS C  95      45.075 -12.385 -38.084  1.00 10.45           C  
ANISOU 1956  CE  LYS C  95     1356   1143   1471      9   -146   -132       C  
ATOM   1957  NZ  LYS C  95      44.607 -11.401 -37.046  1.00 12.03           N  
ANISOU 1957  NZ  LYS C  95     1589   1344   1637     34   -165   -143       N  
ATOM   1958  N   GLY C  96      45.378  -6.887 -42.751  1.00 10.97           N  
ANISOU 1958  N   GLY C  96     1449   1084   1634   -100    -25   -138       N  
ATOM   1959  CA  GLY C  96      44.825  -6.310 -43.965  1.00 11.98           C  
ANISOU 1959  CA  GLY C  96     1603   1197   1750   -114      7   -115       C  
ATOM   1960  C   GLY C  96      43.323  -6.304 -43.737  1.00  9.78           C  
ANISOU 1960  C   GLY C  96     1352    940   1423    -88     -3    -96       C  
ATOM   1961  O   GLY C  96      42.752  -5.401 -43.092  1.00 12.14           O  
ANISOU 1961  O   GLY C  96     1665   1234   1713    -71    -20   -102       O  
ATOM   1962  N   PHE C  97      42.679  -7.382 -44.164  1.00  9.60           N  
ANISOU 1962  N   PHE C  97     1333    940   1375    -84      3    -74       N  
ATOM   1963  CA  PHE C  97      41.303  -7.680 -43.851  1.00  9.27           C  
ANISOU 1963  CA  PHE C  97     1302    920   1300    -59     -8    -54       C  
ATOM   1964  C   PHE C  97      41.243  -9.118 -43.370  1.00  8.46           C  
ANISOU 1964  C   PHE C  97     1180    845   1187    -50    -17    -49       C  
ATOM   1965  O   PHE C  97      42.032  -9.957 -43.823  1.00  9.36           O  
ANISOU 1965  O   PHE C  97     1282    959   1315    -65     -8    -53       O  
ATOM   1966  CB  PHE C  97      40.426  -7.514 -45.089  1.00 10.45           C  
ANISOU 1966  CB  PHE C  97     1476   1060   1434    -67      1    -26       C  
ATOM   1967  CG  PHE C  97      40.345  -6.084 -45.572  1.00 10.01           C  
ANISOU 1967  CG  PHE C  97     1444    974   1385    -74      8    -25       C  
ATOM   1968  CD1 PHE C  97      39.613  -5.121 -44.873  1.00 12.92           C  
ANISOU 1968  CD1 PHE C  97     1818   1338   1752    -52     -5    -27       C  
ATOM   1969  CD2 PHE C  97      41.110  -5.675 -46.652  1.00 13.45           C  
ANISOU 1969  CD2 PHE C  97     1895   1382   1831   -101     32    -24       C  
ATOM   1970  CE1 PHE C  97      39.586  -3.785 -45.267  1.00 15.27           C  
ANISOU 1970  CE1 PHE C  97     2137   1604   2059    -57     -2    -28       C  
ATOM   1971  CE2 PHE C  97      41.094  -4.354 -47.061  1.00 16.56           C  
ANISOU 1971  CE2 PHE C  97     2311   1745   2233   -109     39    -21       C  
ATOM   1972  CZ  PHE C  97      40.342  -3.405 -46.366  1.00 16.54           C  
ANISOU 1972  CZ  PHE C  97     2314   1737   2232    -88     18    -23       C  
ATOM   1973  N   GLU C  98      40.323  -9.416 -42.453  1.00  8.49           N  
ANISOU 1973  N   GLU C  98     1181    870   1171    -23    -29    -38       N  
ATOM   1974  CA  GLU C  98      40.197 -10.763 -41.944  1.00  8.48           C  
ANISOU 1974  CA  GLU C  98     1165    893   1163    -13    -36    -28       C  
ATOM   1975  C   GLU C  98      38.730 -11.106 -41.741  1.00  8.58           C  
ANISOU 1975  C   GLU C  98     1178    921   1160      5    -34      3       C  
ATOM   1976  O   GLU C  98      37.908 -10.260 -41.369  1.00 10.19           O  
ANISOU 1976  O   GLU C  98     1390   1123   1356     24    -31      9       O  
ATOM   1977  CB  GLU C  98      40.966 -10.955 -40.651  1.00 10.69           C  
ANISOU 1977  CB  GLU C  98     1437   1182   1442      1    -52    -49       C  
ATOM   1978  CG  GLU C  98      40.511 -10.139 -39.469  1.00 11.55           C  
ANISOU 1978  CG  GLU C  98     1563   1296   1529     31    -61    -58       C  
ATOM   1979  CD  GLU C  98      41.299 -10.514 -38.244  1.00 13.18           C  
ANISOU 1979  CD  GLU C  98     1770   1509   1726     47    -86    -78       C  
ATOM   1980  OE1 GLU C  98      42.389  -9.970 -38.072  1.00 11.10           O  
ANISOU 1980  OE1 GLU C  98     1504   1228   1483     38   -107   -110       O  
ATOM   1981  OE2 GLU C  98      40.887 -11.430 -37.509  1.00 15.29           O  
ANISOU 1981  OE2 GLU C  98     2039   1798   1971     67    -88    -61       O  
ATOM   1982  N   SER C  99      38.419 -12.376 -41.958  1.00  7.19           N  
ANISOU 1982  N   SER C  99      989    756    986      1    -36     22       N  
ATOM   1983  CA  SER C  99      37.072 -12.893 -41.925  1.00  7.40           C  
ANISOU 1983  CA  SER C  99     1006    792   1012     13    -36     56       C  
ATOM   1984  C   SER C  99      36.545 -13.043 -40.519  1.00  8.11           C  
ANISOU 1984  C   SER C  99     1089    902   1090     44    -28     67       C  
ATOM   1985  O   SER C  99      37.245 -13.472 -39.647  1.00  9.32           O  
ANISOU 1985  O   SER C  99     1243   1065   1231     53    -31     55       O  
ATOM   1986  CB  SER C  99      37.059 -14.291 -42.592  1.00  8.68           C  
ANISOU 1986  CB  SER C  99     1158    955   1185     -3    -45     70       C  
ATOM   1987  OG  SER C  99      37.493 -14.219 -43.934  1.00 12.14           O  
ANISOU 1987  OG  SER C  99     1613   1373   1625    -28    -47     60       O  
ATOM   1988  N   LEU C 100      35.253 -12.780 -40.370  1.00  8.60           N  
ANISOU 1988  N   LEU C 100     1142    966   1157     60    -18     94       N  
ATOM   1989  CA  LEU C 100      34.546 -12.978 -39.121  1.00  8.72           C  
ANISOU 1989  CA  LEU C 100     1150    998   1162     92      1    113       C  
ATOM   1990  C   LEU C 100      33.688 -14.228 -39.157  1.00  9.07           C  
ANISOU 1990  C   LEU C 100     1167   1050   1229     90      7    153       C  
ATOM   1991  O   LEU C 100      33.673 -14.977 -38.197  1.00  9.74           O  
ANISOU 1991  O   LEU C 100     1248   1148   1302    105     20    167       O  
ATOM   1992  CB  LEU C 100      33.681 -11.759 -38.789  1.00 10.48           C  
ANISOU 1992  CB  LEU C 100     1380   1217   1384    118     20    116       C  
ATOM   1993  CG  LEU C 100      34.445 -10.432 -38.523  1.00 11.29           C  
ANISOU 1993  CG  LEU C 100     1514   1309   1466    125     15     76       C  
ATOM   1994  CD1 LEU C 100      33.468  -9.255 -38.578  1.00 16.99           C  
ANISOU 1994  CD1 LEU C 100     2239   2019   2197    146     29     82       C  
ATOM   1995  CD2 LEU C 100      35.157 -10.490 -37.167  1.00 13.55           C  
ANISOU 1995  CD2 LEU C 100     1823   1608   1716    149     17     54       C  
ATOM   1996  N   ARG C 101      32.978 -14.416 -40.258  1.00  9.26           N  
ANISOU 1996  N   ARG C 101     1174   1060   1285     71     -6    171       N  
ATOM   1997  CA  ARG C 101      32.164 -15.593 -40.500  1.00  9.74           C  
ANISOU 1997  CA  ARG C 101     1203   1117   1377     62    -12    207       C  
ATOM   1998  C   ARG C 101      32.080 -15.840 -41.990  1.00  8.97           C  
ANISOU 1998  C   ARG C 101     1107    998   1300     32    -48    205       C  
ATOM   1999  O   ARG C 101      31.795 -14.919 -42.736  1.00 11.52           O  
ANISOU 1999  O   ARG C 101     1441   1308   1626     28    -59    199       O  
ATOM   2000  CB  ARG C 101      30.775 -15.480 -39.921  1.00 10.87           C  
ANISOU 2000  CB  ARG C 101     1316   1264   1550     85     11    245       C  
ATOM   2001  CG  ARG C 101      29.914 -16.689 -40.196  1.00 11.68           C  
ANISOU 2001  CG  ARG C 101     1379   1358   1699     72      2    284       C  
ATOM   2002  CD  ARG C 101      28.601 -16.580 -39.411  1.00 13.08           C  
ANISOU 2002  CD  ARG C 101     1519   1538   1912     98     40    326       C  
ATOM   2003  NE  ARG C 101      27.736 -17.735 -39.642  1.00 16.34           N  
ANISOU 2003  NE  ARG C 101     1886   1937   2383     83     30    367       N  
ATOM   2004  CZ  ARG C 101      26.876 -17.852 -40.646  1.00 15.61           C  
ANISOU 2004  CZ  ARG C 101     1763   1821   2348     65     -6    384       C  
ATOM   2005  NH1 ARG C 101      26.695 -16.880 -41.525  1.00 18.64           N  
ANISOU 2005  NH1 ARG C 101     2156   2190   2734     61    -35    366       N  
ATOM   2006  NH2 ARG C 101      26.164 -18.971 -40.725  1.00 17.66           N  
ANISOU 2006  NH2 ARG C 101     1979   2065   2664     50    -16    421       N  
ATOM   2007  N   VAL C 102      32.341 -17.060 -42.433  1.00  8.08           N  
ANISOU 2007  N   VAL C 102      989    880   1198     13    -67    209       N  
ATOM   2008  CA  VAL C 102      32.386 -17.405 -43.830  1.00  8.30           C  
ANISOU 2008  CA  VAL C 102     1031    886   1234    -13   -102    202       C  
ATOM   2009  C   VAL C 102      31.456 -18.582 -44.158  1.00  9.66           C  
ANISOU 2009  C   VAL C 102     1176   1044   1449    -24   -128    233       C  
ATOM   2010  O   VAL C 102      31.472 -19.591 -43.458  1.00  9.56           O  
ANISOU 2010  O   VAL C 102     1143   1039   1450    -21   -119    249       O  
ATOM   2011  CB  VAL C 102      33.822 -17.829 -44.236  1.00  6.63           C  
ANISOU 2011  CB  VAL C 102      848    673    995    -28   -103    168       C  
ATOM   2012  CG1 VAL C 102      33.899 -18.088 -45.765  1.00  7.92           C  
ANISOU 2012  CG1 VAL C 102     1040    811   1156    -51   -132    158       C  
ATOM   2013  CG2 VAL C 102      34.869 -16.820 -43.806  1.00  8.35           C  
ANISOU 2013  CG2 VAL C 102     1084    901   1184    -20    -80    138       C  
ATOM   2014  N   THR C 103      30.666 -18.424 -45.216  1.00  9.21           N  
ANISOU 2014  N   THR C 103     1122    963   1414    -35   -164    242       N  
ATOM   2015  CA  THR C 103      29.754 -19.470 -45.696  1.00  9.08           C  
ANISOU 2015  CA  THR C 103     1081    925   1445    -49   -203    268       C  
ATOM   2016  C   THR C 103      30.011 -19.637 -47.199  1.00  9.61           C  
ANISOU 2016  C   THR C 103     1192    964   1493    -70   -251    245       C  
ATOM   2017  O   THR C 103      30.782 -18.881 -47.829  1.00 10.07           O  
ANISOU 2017  O   THR C 103     1297   1022   1506    -73   -245    217       O  
ATOM   2018  CB  THR C 103      28.239 -19.096 -45.496  1.00 10.53           C  
ANISOU 2018  CB  THR C 103     1216   1098   1685    -39   -212    306       C  
ATOM   2019  OG1 THR C 103      27.856 -18.133 -46.454  1.00 11.53           O  
ANISOU 2019  OG1 THR C 103     1364   1207   1809    -41   -244    299       O  
ATOM   2020  CG2 THR C 103      27.954 -18.578 -44.079  1.00 11.57           C  
ANISOU 2020  CG2 THR C 103     1315   1256   1822    -11   -153    325       C  
ATOM   2021  N   GLY C 104      29.341 -20.636 -47.770  1.00 11.82           N  
ANISOU 2021  N   GLY C 104     1461   1217   1810    -85   -297    260       N  
ATOM   2022  CA  GLY C 104      29.192 -20.725 -49.211  1.00 12.74           C  
ANISOU 2022  CA  GLY C 104     1622   1301   1915   -101   -354    245       C  
ATOM   2023  C   GLY C 104      28.103 -19.788 -49.736  1.00 14.43           C  
ANISOU 2023  C   GLY C 104     1830   1497   2152    -97   -391    262       C  
ATOM   2024  O   GLY C 104      27.526 -18.961 -49.003  1.00 15.06           O  
ANISOU 2024  O   GLY C 104     1871   1592   2258    -80   -365    283       O  
ATOM   2025  N   PRO C 105      27.814 -19.909 -51.031  1.00 14.39           N  
ANISOU 2025  N   PRO C 105     1870   1458   2138   -109   -454    253       N  
ATOM   2026  CA  PRO C 105      26.751 -19.091 -51.596  1.00 16.91           C  
ANISOU 2026  CA  PRO C 105     2185   1755   2484   -105   -501    271       C  
ATOM   2027  C   PRO C 105      25.422 -19.272 -50.860  1.00 15.40           C  
ANISOU 2027  C   PRO C 105     1907   1559   2385   -100   -515    312       C  
ATOM   2028  O   PRO C 105      25.047 -20.406 -50.495  1.00 16.52           O  
ANISOU 2028  O   PRO C 105     2007   1693   2578   -110   -527    329       O  
ATOM   2029  CB  PRO C 105      26.639 -19.635 -53.026  1.00 19.15           C  
ANISOU 2029  CB  PRO C 105     2531   1998   2745   -120   -578    254       C  
ATOM   2030  CG  PRO C 105      27.976 -20.241 -53.330  1.00 18.76           C  
ANISOU 2030  CG  PRO C 105     2540   1957   2630   -127   -547    219       C  
ATOM   2031  CD  PRO C 105      28.465 -20.770 -52.036  1.00 15.23           C  
ANISOU 2031  CD  PRO C 105     2037   1543   2204   -124   -485    224       C  
ATOM   2032  N   GLY C 106      24.750 -18.160 -50.614  1.00 15.32           N  
ANISOU 2032  N   GLY C 106     1870   1552   2399    -83   -507    330       N  
ATOM   2033  CA  GLY C 106      23.412 -18.205 -50.032  1.00 18.66           C  
ANISOU 2033  CA  GLY C 106     2207   1963   2916    -75   -517    371       C  
ATOM   2034  C   GLY C 106      23.390 -18.653 -48.574  1.00 15.54           C  
ANISOU 2034  C   GLY C 106     1751   1600   2554    -64   -443    393       C  
ATOM   2035  O   GLY C 106      22.343 -18.882 -47.987  1.00 16.31           O  
ANISOU 2035  O   GLY C 106     1774   1689   2733    -58   -436    432       O  
ATOM   2036  N   GLY C 107      24.568 -18.731 -47.952  1.00 14.83           N  
ANISOU 2036  N   GLY C 107     1693   1544   2399    -60   -383    371       N  
ATOM   2037  CA  GLY C 107      24.626 -19.197 -46.563  1.00 12.97           C  
ANISOU 2037  CA  GLY C 107     1412   1336   2180    -48   -316    391       C  
ATOM   2038  C   GLY C 107      24.845 -20.672 -46.405  1.00 12.68           C  
ANISOU 2038  C   GLY C 107     1363   1293   2161    -67   -324    398       C  
ATOM   2039  O   GLY C 107      24.833 -21.160 -45.295  1.00 15.71           O  
ANISOU 2039  O   GLY C 107     1712   1695   2561    -58   -274    421       O  
ATOM   2040  N   ASN C 108      25.023 -21.370 -47.530  1.00 13.26           N  
ANISOU 2040  N   ASN C 108     1470   1337   2230    -91   -390    380       N  
ATOM   2041  CA  ASN C 108      25.346 -22.816 -47.509  1.00 15.77           C  
ANISOU 2041  CA  ASN C 108     1786   1643   2561   -109   -405    381       C  
ATOM   2042  C   ASN C 108      26.614 -23.096 -46.714  1.00 12.73           C  
ANISOU 2042  C   ASN C 108     1426   1292   2117   -101   -345    362       C  
ATOM   2043  O   ASN C 108      27.479 -22.231 -46.612  1.00 12.26           O  
ANISOU 2043  O   ASN C 108     1405   1258   1994    -89   -311    334       O  
ATOM   2044  CB  ASN C 108      25.585 -23.341 -48.925  1.00 16.32           C  
ANISOU 2044  CB  ASN C 108     1911   1677   2611   -131   -480    351       C  
ATOM   2045  CG  ASN C 108      24.311 -23.771 -49.619  1.00 23.32           C  
ANISOU 2045  CG  ASN C 108     2766   2518   3577   -146   -560    374       C  
ATOM   2046  OD1 ASN C 108      24.000 -23.307 -50.721  1.00 28.64           O  
ANISOU 2046  OD1 ASN C 108     3477   3166   4239   -151   -623    359       O  
ATOM   2047  ND2 ASN C 108      23.578 -24.637 -48.977  1.00 22.98           N  
ANISOU 2047  ND2 ASN C 108     2653   2461   3614   -155   -560    411       N  
ATOM   2048  N   PRO C 109      26.716 -24.280 -46.110  1.00 15.04           N  
ANISOU 2048  N   PRO C 109     1694   1582   2435   -108   -333    379       N  
ATOM   2049  CA  PRO C 109      28.004 -24.635 -45.539  1.00 14.65           C  
ANISOU 2049  CA  PRO C 109     1676   1559   2331   -101   -292    356       C  
ATOM   2050  C   PRO C 109      29.107 -24.590 -46.588  1.00 11.87           C  
ANISOU 2050  C   PRO C 109     1390   1201   1919   -110   -316    306       C  
ATOM   2051  O   PRO C 109      28.903 -24.929 -47.740  1.00 12.77           O  
ANISOU 2051  O   PRO C 109     1531   1283   2038   -126   -371    291       O  
ATOM   2052  CB  PRO C 109      27.782 -26.054 -45.016  1.00 14.73           C  
ANISOU 2052  CB  PRO C 109     1652   1554   2389   -112   -295    385       C  
ATOM   2053  CG  PRO C 109      26.313 -26.259 -44.987  1.00 21.59           C  
ANISOU 2053  CG  PRO C 109     2460   2398   3343   -120   -316    430       C  
ATOM   2054  CD  PRO C 109      25.734 -25.372 -46.030  1.00 16.27           C  
ANISOU 2054  CD  PRO C 109     1796   1707   2675   -124   -363    417       C  
ATOM   2055  N   CYS C 110      30.291 -24.205 -46.141  1.00 11.18           N  
ANISOU 2055  N   CYS C 110     1329   1141   1775    -98   -273    280       N  
ATOM   2056  CA  CYS C 110      31.517 -24.327 -46.928  1.00 12.39           C  
ANISOU 2056  CA  CYS C 110     1537   1291   1879   -104   -278    235       C  
ATOM   2057  C   CYS C 110      31.773 -25.780 -47.233  1.00 11.87           C  
ANISOU 2057  C   CYS C 110     1477   1201   1832   -117   -305    230       C  
ATOM   2058  O   CYS C 110      31.305 -26.654 -46.488  1.00 12.20           O  
ANISOU 2058  O   CYS C 110     1478   1238   1917   -119   -305    261       O  
ATOM   2059  CB  CYS C 110      32.693 -23.736 -46.155  1.00 11.20           C  
ANISOU 2059  CB  CYS C 110     1396   1172   1684    -89   -227    215       C  
ATOM   2060  SG  CYS C 110      32.550 -21.997 -45.674  1.00 11.17           S  
ANISOU 2060  SG  CYS C 110     1390   1194   1657    -72   -193    215       S  
ATOM   2061  N   LEU C 111      32.562 -26.029 -48.280  1.00 11.77           N  
ANISOU 2061  N   LEU C 111     1516   1171   1784   -124   -320    192       N  
ATOM   2062  CA  LEU C 111      32.837 -27.390 -48.750  1.00 12.33           C  
ANISOU 2062  CA  LEU C 111     1602   1212   1868   -134   -349    179       C  
ATOM   2063  C   LEU C 111      34.124 -27.980 -48.148  1.00 11.66           C  
ANISOU 2063  C   LEU C 111     1519   1143   1769   -125   -311    161       C  
ATOM   2064  O   LEU C 111      34.106 -29.077 -47.571  1.00 12.32           O  
ANISOU 2064  O   LEU C 111     1577   1216   1886   -126   -318    177       O  
ATOM   2065  CB  LEU C 111      32.901 -27.410 -50.279  1.00 15.79           C  
ANISOU 2065  CB  LEU C 111     2104   1619   2276   -143   -389    147       C  
ATOM   2066  CG  LEU C 111      31.603 -27.084 -51.016  1.00 30.01           C  
ANISOU 2066  CG  LEU C 111     3909   3393   4098   -153   -448    163       C  
ATOM   2067  CD1 LEU C 111      31.816 -27.498 -52.464  1.00 28.25           C  
ANISOU 2067  CD1 LEU C 111     3762   3133   3839   -160   -493    128       C  
ATOM   2068  CD2 LEU C 111      30.353 -27.744 -50.424  1.00 30.09           C  
ANISOU 2068  CD2 LEU C 111     3856   3389   4188   -163   -484    206       C  
ATOM   2069  N   GLY C 112      35.198 -27.231 -48.216  1.00 10.32           N  
ANISOU 2069  N   GLY C 112     1372    993   1555   -115   -273    132       N  
ATOM   2070  CA  GLY C 112      36.438 -27.656 -47.638  1.00 10.28           C  
ANISOU 2070  CA  GLY C 112     1362   1000   1543   -105   -241    115       C  
ATOM   2071  C   GLY C 112      37.265 -28.650 -48.400  1.00 11.14           C  
ANISOU 2071  C   GLY C 112     1501   1082   1647   -106   -247     83       C  
ATOM   2072  O   GLY C 112      36.861 -29.124 -49.434  1.00 11.53           O  
ANISOU 2072  O   GLY C 112     1585   1100   1695   -116   -280     72       O  
ATOM   2073  N   ASN C 113      38.453 -28.908 -47.866  1.00  9.65           N  
ANISOU 2073  N   ASN C 113     1302    905   1459    -95   -217     66       N  
ATOM   2074  CA  ASN C 113      39.443 -29.780 -48.458  1.00 10.35           C  
ANISOU 2074  CA  ASN C 113     1412    970   1547    -90   -210     33       C  
ATOM   2075  C   ASN C 113      40.015 -30.722 -47.382  1.00 10.47           C  
ANISOU 2075  C   ASN C 113     1391    989   1597    -79   -208     43       C  
ATOM   2076  O   ASN C 113      41.231 -30.894 -47.294  1.00 11.01           O  
ANISOU 2076  O   ASN C 113     1457   1058   1668    -67   -183     18       O  
ATOM   2077  CB  ASN C 113      40.531 -28.912 -49.096  1.00 11.76           C  
ANISOU 2077  CB  ASN C 113     1618   1156   1694    -85   -166     -1       C  
ATOM   2078  CG  ASN C 113      41.553 -29.695 -49.910  1.00 12.04           C  
ANISOU 2078  CG  ASN C 113     1681   1165   1727    -78   -148    -38       C  
ATOM   2079  OD1 ASN C 113      42.741 -29.297 -49.985  1.00 15.24           O  
ANISOU 2079  OD1 ASN C 113     2083   1577   2130    -69   -102    -62       O  
ATOM   2080  ND2 ASN C 113      41.131 -30.796 -50.505  1.00 13.58           N  
ANISOU 2080  ND2 ASN C 113     1902   1327   1929    -80   -180    -44       N  
ATOM   2081  N  AGLU C 114      39.142 -31.348 -46.586  0.50 10.96           N  
ANISOU 2081  N  AGLU C 114     1425   1049   1688    -82   -234     82       N  
ATOM   2082  N  BGLU C 114      39.148 -31.405 -46.633  0.50 11.04           N  
ANISOU 2082  N  BGLU C 114     1436   1057   1699    -83   -235     81       N  
ATOM   2083  CA AGLU C 114      39.583 -32.220 -45.498  0.50 11.87           C  
ANISOU 2083  CA AGLU C 114     1511   1166   1831    -71   -235     99       C  
ATOM   2084  CA BGLU C 114      39.601 -32.298 -45.567  0.50 11.80           C  
ANISOU 2084  CA BGLU C 114     1504   1154   1823    -71   -236     97       C  
ATOM   2085  C  AGLU C 114      40.389 -33.384 -46.043  0.50 15.20           C  
ANISOU 2085  C  AGLU C 114     1948   1554   2272    -66   -243     71       C  
ATOM   2086  C  BGLU C 114      40.408 -33.499 -46.089  0.50 15.79           C  
ANISOU 2086  C  BGLU C 114     2024   1626   2349    -66   -245     70       C  
ATOM   2087  O  AGLU C 114      40.007 -33.954 -47.052  0.50 10.89           O  
ANISOU 2087  O  AGLU C 114     1430    976   1730    -76   -266     57       O  
ATOM   2088  O  BGLU C 114      41.376 -33.936 -45.443  0.50 13.32           O  
ANISOU 2088  O  BGLU C 114     1693   1315   2050    -50   -235     63       O  
ATOM   2089  CB AGLU C 114      38.385 -32.746 -44.684  0.50 12.08           C  
ANISOU 2089  CB AGLU C 114     1511   1190   1887    -77   -256    151       C  
ATOM   2090  CB BGLU C 114      38.410 -32.768 -44.707  0.50 12.17           C  
ANISOU 2090  CB BGLU C 114     1523   1200   1899    -77   -256    150       C  
ATOM   2091  CG AGLU C 114      38.822 -33.661 -43.532  0.50 12.94           C  
ANISOU 2091  CG AGLU C 114     1598   1298   2019    -64   -256    174       C  
ATOM   2092  CG BGLU C 114      38.844 -33.668 -43.543  0.50 12.95           C  
ANISOU 2092  CG BGLU C 114     1600   1299   2021    -64   -256    173       C  
ATOM   2093  CD AGLU C 114      37.651 -34.235 -42.743  0.50 13.48           C  
ANISOU 2093  CD AGLU C 114     1641   1360   2119    -70   -267    230       C  
ATOM   2094  CD BGLU C 114      37.673 -34.257 -42.765  0.50 13.58           C  
ANISOU 2094  CD BGLU C 114     1654   1372   2132    -70   -267    229       C  
ATOM   2095  OE1AGLU C 114      36.513 -34.190 -43.232  0.50 13.31           O  
ANISOU 2095  OE1AGLU C 114     1613   1325   2117    -88   -282    249       O  
ATOM   2096  OE1BGLU C 114      36.526 -34.166 -43.226  0.50 13.28           O  
ANISOU 2096  OE1BGLU C 114     1610   1322   2113    -88   -282    248       O  
ATOM   2097  OE2AGLU C 114      37.891 -34.708 -41.616  0.50 16.39           O  
ANISOU 2097  OE2AGLU C 114     1997   1736   2495    -57   -259    258       O  
ATOM   2098  OE2BGLU C 114      37.920 -34.791 -41.673  0.50 16.64           O  
ANISOU 2098  OE2BGLU C 114     2028   1764   2528    -57   -261    257       O  
TER    2099      GLU C 114                                                      
ATOM   2100  N   VAL D  30      18.350 -27.175 -44.350  1.00 29.22           N  
ANISOU 2100  N   VAL D  30     3803   3420   3876    188   -157   -252       N  
ATOM   2101  CA  VAL D  30      17.655 -25.926 -44.827  1.00 24.48           C  
ANISOU 2101  CA  VAL D  30     3216   2867   3216    152   -123   -258       C  
ATOM   2102  C   VAL D  30      17.599 -25.822 -46.350  1.00 21.54           C  
ANISOU 2102  C   VAL D  30     2802   2530   2853    134   -115   -328       C  
ATOM   2103  O   VAL D  30      18.630 -26.007 -47.005  1.00 31.30           O  
ANISOU 2103  O   VAL D  30     3999   3795   4095    145   -135   -387       O  
ATOM   2104  CB  VAL D  30      18.368 -24.669 -44.304  1.00 26.07           C  
ANISOU 2104  CB  VAL D  30     3437   3126   3343    146   -120   -252       C  
ATOM   2105  CG1 VAL D  30      17.476 -23.439 -44.519  1.00 26.24           C  
ANISOU 2105  CG1 VAL D  30     3476   3175   3318    112    -85   -238       C  
ATOM   2106  CG2 VAL D  30      18.734 -24.813 -42.831  1.00 33.93           C  
ANISOU 2106  CG2 VAL D  30     4461   4111   4320    174   -137   -200       C  
ATOM   2107  N   LEU D  31      16.436 -25.502 -46.931  1.00 19.64           N  
ANISOU 2107  N   LEU D  31     2562   2294   2606    111    -88   -326       N  
ATOM   2108  CA  LEU D  31      16.336 -25.362 -48.406  1.00 14.25           C  
ANISOU 2108  CA  LEU D  31     1834   1661   1918     99    -81   -391       C  
ATOM   2109  C   LEU D  31      16.679 -23.950 -48.850  1.00 13.53           C  
ANISOU 2109  C   LEU D  31     1748   1641   1751     79    -63   -389       C  
ATOM   2110  O   LEU D  31      16.279 -22.965 -48.221  1.00 11.47           O  
ANISOU 2110  O   LEU D  31     1525   1380   1450     64    -44   -339       O  
ATOM   2111  CB  LEU D  31      14.975 -25.790 -48.957  1.00 18.91           C  
ANISOU 2111  CB  LEU D  31     2412   2231   2542     89    -65   -400       C  
ATOM   2112  CG  LEU D  31      14.467 -27.138 -48.480  1.00 24.53           C  
ANISOU 2112  CG  LEU D  31     3117   2858   3343    102    -76   -393       C  
ATOM   2113  CD1 LEU D  31      12.976 -27.225 -48.770  1.00 29.14           C  
ANISOU 2113  CD1 LEU D  31     3699   3424   3948     85    -52   -388       C  
ATOM   2114  CD2 LEU D  31      15.236 -28.254 -49.157  1.00 24.47           C  
ANISOU 2114  CD2 LEU D  31     3054   2839   3404    125   -107   -468       C  
ATOM   2115  N   ARG D  32      17.434 -23.851 -49.948  1.00 13.63           N  
ANISOU 2115  N   ARG D  32     1716   1715   1748     78    -67   -445       N  
ATOM   2116  CA AARG D  32      17.842 -22.572 -50.492  0.50 12.73           C  
ANISOU 2116  CA AARG D  32     1597   1667   1571     58    -47   -439       C  
ATOM   2117  CA BARG D  32      17.829 -22.566 -50.486  0.50 12.60           C  
ANISOU 2117  CA BARG D  32     1581   1651   1555     58    -46   -438       C  
ATOM   2118  C   ARG D  32      17.567 -22.482 -51.983  1.00 12.95           C  
ANISOU 2118  C   ARG D  32     1578   1765   1575     51    -34   -478       C  
ATOM   2119  O   ARG D  32      17.652 -23.486 -52.720  1.00 14.42           O  
ANISOU 2119  O   ARG D  32     1718   1969   1791     68    -51   -542       O  
ATOM   2120  CB AARG D  32      19.348 -22.327 -50.248  0.50 12.86           C  
ANISOU 2120  CB AARG D  32     1602   1708   1577     62    -60   -459       C  
ATOM   2121  CB BARG D  32      19.325 -22.285 -50.207  0.50 12.48           C  
ANISOU 2121  CB BARG D  32     1556   1658   1527     61    -59   -456       C  
ATOM   2122  CG AARG D  32      19.666 -21.833 -48.857  0.50 13.93           C  
ANISOU 2122  CG AARG D  32     1781   1805   1705     64    -65   -416       C  
ATOM   2123  CG BARG D  32      19.713 -22.424 -48.749  0.50 12.81           C  
ANISOU 2123  CG BARG D  32     1635   1647   1584     76    -77   -426       C  
ATOM   2124  CD AARG D  32      21.165 -21.764 -48.569  0.50 15.16           C  
ANISOU 2124  CD AARG D  32     1918   1983   1859     73    -84   -448       C  
ATOM   2125  CD BARG D  32      21.169 -22.033 -48.488  0.50 14.30           C  
ANISOU 2125  CD BARG D  32     1809   1866   1759     80    -90   -451       C  
ATOM   2126  NE AARG D  32      21.355 -21.372 -47.186  0.50 13.32           N  
ANISOU 2126  NE AARG D  32     1722   1720   1616     81    -92   -413       N  
ATOM   2127  NE BARG D  32      21.649 -22.662 -47.270  0.50 15.06           N  
ANISOU 2127  NE BARG D  32     1924   1919   1877    109   -121   -441       N  
ATOM   2128  CZ AARG D  32      21.562 -22.230 -46.203  0.50 15.24           C  
ANISOU 2128  CZ AARG D  32     1981   1925   1882    112   -121   -403       C  
ATOM   2129  CZ BARG D  32      21.633 -22.113 -46.068  0.50 15.54           C  
ANISOU 2129  CZ BARG D  32     2022   1964   1916    112   -121   -400       C  
ATOM   2130  NH1AARG D  32      21.682 -23.519 -46.458  0.50 16.41           N  
ANISOU 2130  NH1AARG D  32     2109   2046   2077    137   -145   -426       N  
ATOM   2131  NH1BARG D  32      21.219 -20.875 -45.895  0.50 17.11           N  
ANISOU 2131  NH1BARG D  32     2241   2179   2080     85    -94   -374       N  
ATOM   2132  NH2AARG D  32      21.682 -21.787 -44.971  0.50 16.97           N  
ANISOU 2132  NH2AARG D  32     2231   2136   2080    121   -127   -371       N  
ATOM   2133  NH2BARG D  32      22.078 -22.813 -45.040  0.50 15.63           N  
ANISOU 2133  NH2BARG D  32     2045   1949   1942    145   -152   -389       N  
ATOM   2134  N   GLY D  33      17.286 -21.276 -52.445  1.00 11.63           N  
ANISOU 2134  N   GLY D  33     1419   1644   1356     31     -7   -442       N  
ATOM   2135  CA  GLY D  33      17.078 -20.998 -53.820  1.00 14.41           C  
ANISOU 2135  CA  GLY D  33     1727   2078   1667     27      7   -462       C  
ATOM   2136  C   GLY D  33      17.408 -19.573 -54.179  1.00 12.31           C  
ANISOU 2136  C   GLY D  33     1467   1861   1349      4     36   -412       C  
ATOM   2137  O   GLY D  33      17.781 -18.755 -53.330  1.00 12.55           O  
ANISOU 2137  O   GLY D  33     1532   1853   1383    -10     44   -369       O  
ATOM   2138  N   SER D  34      17.309 -19.247 -55.463  1.00 12.96           N  
ANISOU 2138  N   SER D  34     1508   2031   1385      2     52   -417       N  
ATOM   2139  CA  SER D  34      17.481 -17.889 -55.906  1.00 13.79           C  
ANISOU 2139  CA  SER D  34     1615   2179   1446    -18     83   -354       C  
ATOM   2140  C   SER D  34      16.497 -17.571 -57.031  1.00 15.54           C  
ANISOU 2140  C   SER D  34     1814   2470   1620    -12     98   -332       C  
ATOM   2141  O   SER D  34      15.873 -18.476 -57.587  1.00 14.50           O  
ANISOU 2141  O   SER D  34     1654   2370   1485      9     83   -384       O  
ATOM   2142  CB  SER D  34      18.938 -17.567 -56.290  1.00 22.53           C  
ANISOU 2142  CB  SER D  34     2686   3339   2534    -31     93   -367       C  
ATOM   2143  OG  SER D  34      19.345 -18.390 -57.355  1.00 22.62           O  
ANISOU 2143  OG  SER D  34     2637   3439   2519    -15     84   -434       O  
ATOM   2144  N   GLY D  35      16.327 -16.289 -57.315  1.00 14.01           N  
ANISOU 2144  N   GLY D  35     1631   2294   1396    -28    127   -254       N  
ATOM   2145  CA  GLY D  35      15.315 -15.857 -58.264  1.00 15.11           C  
ANISOU 2145  CA  GLY D  35     1756   2495   1490    -17    140   -217       C  
ATOM   2146  C   GLY D  35      15.165 -14.371 -58.303  1.00 14.22           C  
ANISOU 2146  C   GLY D  35     1664   2371   1366    -36    170   -119       C  
ATOM   2147  O   GLY D  35      16.131 -13.651 -58.095  1.00 16.77           O  
ANISOU 2147  O   GLY D  35     1988   2681   1701    -60    188    -85       O  
ATOM   2148  N   HIS D  36      13.959 -13.889 -58.568  1.00 13.83           N  
ANISOU 2148  N   HIS D  36     1628   2324   1303    -25    175    -73       N  
ATOM   2149  CA  HIS D  36      13.683 -12.481 -58.587  1.00 13.60           C  
ANISOU 2149  CA  HIS D  36     1619   2271   1277    -38    200     21       C  
ATOM   2150  C   HIS D  36      12.287 -12.239 -58.101  1.00 15.71           C  
ANISOU 2150  C   HIS D  36     1921   2479   1566    -26    191     41       C  
ATOM   2151  O   HIS D  36      11.461 -13.149 -58.111  1.00 14.29           O  
ANISOU 2151  O   HIS D  36     1740   2307   1382     -6    170    -12       O  
ATOM   2152  CB  HIS D  36      13.874 -11.924 -60.009  1.00 16.50           C  
ANISOU 2152  CB  HIS D  36     1939   2754   1576    -32    223     79       C  
ATOM   2153  CG  HIS D  36      13.005 -12.604 -61.043  1.00 19.56           C  
ANISOU 2153  CG  HIS D  36     2289   3243   1897      4    209     47       C  
ATOM   2154  ND1 HIS D  36      13.389 -13.722 -61.692  1.00 21.63           N  
ANISOU 2154  ND1 HIS D  36     2504   3593   2121     20    194    -37       N  
ATOM   2155  CD2 HIS D  36      11.708 -12.338 -61.449  1.00 20.07           C  
ANISOU 2155  CD2 HIS D  36     2357   3329   1938     29    204     78       C  
ATOM   2156  CE1 HIS D  36      12.404 -14.113 -62.532  1.00 23.30           C  
ANISOU 2156  CE1 HIS D  36     2684   3886   2281     54    182    -60       C  
ATOM   2157  NE2 HIS D  36      11.377 -13.257 -62.396  1.00 22.09           N  
ANISOU 2157  NE2 HIS D  36     2563   3696   2135     60    188     12       N  
ATOM   2158  N   CYS D  37      12.024 -11.010 -57.669  1.00 14.24           N  
ANISOU 2158  N   CYS D  37     1763   2232   1414    -40    207    113       N  
ATOM   2159  CA  CYS D  37      10.667 -10.668 -57.225  1.00 14.97           C  
ANISOU 2159  CA  CYS D  37     1886   2271   1529    -27    199    132       C  
ATOM   2160  C   CYS D  37       9.688 -10.722 -58.379  1.00 17.77           C  
ANISOU 2160  C   CYS D  37     2214   2710   1828      2    196    152       C  
ATOM   2161  O   CYS D  37       9.870  -9.989 -59.377  1.00 19.28           O  
ANISOU 2161  O   CYS D  37     2378   2968   1979      8    214    221       O  
ATOM   2162  CB  CYS D  37      10.641  -9.280 -56.606  1.00 15.62           C  
ANISOU 2162  CB  CYS D  37     1995   2273   1666    -46    215    199       C  
ATOM   2163  SG  CYS D  37       8.984  -8.705 -56.193  1.00 16.72           S  
ANISOU 2163  SG  CYS D  37     2162   2358   1833    -28    207    223       S  
ATOM   2164  N   LYS D  38       8.670 -11.559 -58.230  1.00 14.84           N  
ANISOU 2164  N   LYS D  38     1845   2337   1454     22    175     95       N  
ATOM   2165  CA  LYS D  38       7.552 -11.652 -59.183  1.00 15.28           C  
ANISOU 2165  CA  LYS D  38     1874   2467   1462     55    167     98       C  
ATOM   2166  C   LYS D  38       6.621 -10.454 -59.040  1.00 17.72           C  
ANISOU 2166  C   LYS D  38     2207   2735   1791     62    173    174       C  
ATOM   2167  O   LYS D  38       6.420  -9.722 -60.008  1.00 20.17           O  
ANISOU 2167  O   LYS D  38     2493   3110   2058     81    182    243       O  
ATOM   2168  CB  LYS D  38       6.802 -12.970 -58.988  1.00 13.64           C  
ANISOU 2168  CB  LYS D  38     1658   2261   1264     69    144      3       C  
ATOM   2169  CG  LYS D  38       5.856 -13.356 -60.136  1.00 17.81           C  
ANISOU 2169  CG  LYS D  38     2139   2891   1736    106    131    -25       C  
ATOM   2170  CD  LYS D  38       4.965 -14.515 -59.721  1.00 16.79           C  
ANISOU 2170  CD  LYS D  38     2004   2730   1642    113    112   -116       C  
ATOM   2171  CE  LYS D  38       4.244 -15.129 -60.933  1.00 21.96           C  
ANISOU 2171  CE  LYS D  38     2598   3501   2246    150     96   -174       C  
ATOM   2172  NZ  LYS D  38       3.398 -16.272 -60.483  1.00 20.33           N  
ANISOU 2172  NZ  LYS D  38     2381   3249   2093    152     80   -268       N  
ATOM   2173  N   TRP D  39       6.043 -10.267 -57.847  1.00 16.82           N  
ANISOU 2173  N   TRP D  39     2133   2517   1738     51    169    161       N  
ATOM   2174  CA  TRP D  39       5.351  -9.060 -57.483  1.00 16.28           C  
ANISOU 2174  CA  TRP D  39     2088   2388   1707     53    175    223       C  
ATOM   2175  C   TRP D  39       5.323  -8.884 -55.970  1.00 14.24           C  
ANISOU 2175  C   TRP D  39     1871   2019   1520     28    175    198       C  
ATOM   2176  O   TRP D  39       5.628  -9.853 -55.239  1.00 13.23           O  
ANISOU 2176  O   TRP D  39     1756   1868   1402     15    168    133       O  
ATOM   2177  CB  TRP D  39       3.934  -9.060 -58.053  1.00 16.91           C  
ANISOU 2177  CB  TRP D  39     2154   2510   1762     88    161    224       C  
ATOM   2178  CG  TRP D  39       3.078 -10.243 -57.728  1.00 16.23           C  
ANISOU 2178  CG  TRP D  39     2065   2426   1676     96    144    134       C  
ATOM   2179  CD1 TRP D  39       2.911 -11.407 -58.465  1.00 17.32           C  
ANISOU 2179  CD1 TRP D  39     2165   2644   1770    114    131     68       C  
ATOM   2180  CD2 TRP D  39       2.232 -10.412 -56.551  1.00 14.95           C  
ANISOU 2180  CD2 TRP D  39     1934   2179   1567     87    139     96       C  
ATOM   2181  NE1 TRP D  39       2.037 -12.247 -57.853  1.00 18.67           N  
ANISOU 2181  NE1 TRP D  39     2341   2777   1972    113    120     -1       N  
ATOM   2182  CE2 TRP D  39       1.604 -11.708 -56.679  1.00 18.27           C  
ANISOU 2182  CE2 TRP D  39     2333   2630   1976     96    127     15       C  
ATOM   2183  CE3 TRP D  39       1.989  -9.658 -55.418  1.00 15.38           C  
ANISOU 2183  CE3 TRP D  39     2024   2142   1678     70    145    114       C  
ATOM   2184  CZ2 TRP D  39       0.722 -12.187 -55.736  1.00 15.19           C  
ANISOU 2184  CZ2 TRP D  39     1961   2181   1628     88    124    -29       C  
ATOM   2185  CZ3 TRP D  39       1.078 -10.137 -54.478  1.00 15.85           C  
ANISOU 2185  CZ3 TRP D  39     2100   2154   1768     66    141     63       C  
ATOM   2186  CH2 TRP D  39       0.480 -11.376 -54.625  1.00 14.88           C  
ANISOU 2186  CH2 TRP D  39     1960   2061   1632     72    133     -1       C  
ATOM   2187  N   PHE D  40       5.018  -7.669 -55.504  1.00 14.22           N  
ANISOU 2187  N   PHE D  40     1885   1950   1566     23    182    247       N  
ATOM   2188  CA  PHE D  40       4.939  -7.358 -54.071  1.00 14.22           C  
ANISOU 2188  CA  PHE D  40     1917   1856   1629      4    181    218       C  
ATOM   2189  C   PHE D  40       3.841  -6.357 -53.770  1.00 15.71           C  
ANISOU 2189  C   PHE D  40     2113   1995   1860     17    179    245       C  
ATOM   2190  O   PHE D  40       3.717  -5.331 -54.470  1.00 18.01           O  
ANISOU 2190  O   PHE D  40     2390   2286   2165     28    185    316       O  
ATOM   2191  CB  PHE D  40       6.257  -6.812 -53.537  1.00 12.82           C  
ANISOU 2191  CB  PHE D  40     1744   1634   1490    -24    194    230       C  
ATOM   2192  CG  PHE D  40       6.428  -7.029 -52.049  1.00 11.88           C  
ANISOU 2192  CG  PHE D  40     1651   1453   1409    -40    188    172       C  
ATOM   2193  CD1 PHE D  40       6.859  -8.265 -51.557  1.00 12.21           C  
ANISOU 2193  CD1 PHE D  40     1702   1511   1424    -46    179    115       C  
ATOM   2194  CD2 PHE D  40       6.092  -6.021 -51.156  1.00 13.52           C  
ANISOU 2194  CD2 PHE D  40     1868   1589   1677    -47    190    172       C  
ATOM   2195  CE1 PHE D  40       6.944  -8.473 -50.194  1.00 12.33           C  
ANISOU 2195  CE1 PHE D  40     1739   1480   1463    -55    174     71       C  
ATOM   2196  CE2 PHE D  40       6.181  -6.235 -49.791  1.00 13.40           C  
ANISOU 2196  CE2 PHE D  40     1871   1535   1683    -57    184    115       C  
ATOM   2197  CZ  PHE D  40       6.616  -7.451 -49.317  1.00 11.90           C  
ANISOU 2197  CZ  PHE D  40     1693   1370   1457    -61    177     70       C  
ATOM   2198  N   ASN D  41       3.061  -6.637 -52.734  1.00 13.09           N  
ANISOU 2198  N   ASN D  41     1799   1620   1551     16    171    191       N  
ATOM   2199  CA  ASN D  41       1.872  -5.872 -52.330  1.00 12.25           C  
ANISOU 2199  CA  ASN D  41     1698   1472   1484     30    166    195       C  
ATOM   2200  C   ASN D  41       2.157  -5.214 -50.996  1.00 13.92           C  
ANISOU 2200  C   ASN D  41     1925   1606   1758      9    170    169       C  
ATOM   2201  O   ASN D  41       2.183  -5.885 -49.989  1.00 12.55           O  
ANISOU 2201  O   ASN D  41     1766   1422   1579     -2    168    113       O  
ATOM   2202  CB  ASN D  41       0.649  -6.797 -52.246  1.00 14.41           C  
ANISOU 2202  CB  ASN D  41     1970   1774   1728     45    156    144       C  
ATOM   2203  CG  ASN D  41      -0.638  -6.061 -51.941  1.00 19.26           C  
ANISOU 2203  CG  ASN D  41     2583   2356   2377     63    149    142       C  
ATOM   2204  OD1 ASN D  41      -0.725  -5.300 -50.973  1.00 14.99           O  
ANISOU 2204  OD1 ASN D  41     2052   1753   1890     53    152    131       O  
ATOM   2205  ND2 ASN D  41      -1.639  -6.263 -52.790  1.00 24.25           N  
ANISOU 2205  ND2 ASN D  41     3196   3037   2980     91    139    146       N  
ATOM   2206  N   VAL D  42       2.428  -3.907 -50.982  1.00 15.05           N  
ANISOU 2206  N   VAL D  42     2058   1696   1961      6    175    211       N  
ATOM   2207  CA  VAL D  42       2.782  -3.207 -49.729  1.00 14.17           C  
ANISOU 2207  CA  VAL D  42     1952   1515   1916    -11    177    173       C  
ATOM   2208  C   VAL D  42       1.582  -2.893 -48.816  1.00 14.83           C  
ANISOU 2208  C   VAL D  42     2037   1565   2030      0    168    125       C  
ATOM   2209  O   VAL D  42       1.782  -2.658 -47.613  1.00 18.66           O  
ANISOU 2209  O   VAL D  42     2523   2016   2548    -12    167     70       O  
ATOM   2210  CB  VAL D  42       3.591  -1.908 -49.985  1.00 16.13           C  
ANISOU 2210  CB  VAL D  42     2181   1708   2237    -22    187    224       C  
ATOM   2211  CG1 VAL D  42       4.980  -2.225 -50.564  1.00 20.50           C  
ANISOU 2211  CG1 VAL D  42     2730   2293   2766    -43    200    255       C  
ATOM   2212  CG2 VAL D  42       2.811  -0.977 -50.882  1.00 20.64           C  
ANISOU 2212  CG2 VAL D  42     2737   2262   2843      0    185    297       C  
ATOM   2213  N   ARG D  43       0.353  -2.919 -49.336  1.00 14.15           N  
ANISOU 2213  N   ARG D  43     1946   1497   1930     24    160    137       N  
ATOM   2214  CA AARG D  43      -0.824  -2.796 -48.480  0.50 14.03           C  
ANISOU 2214  CA AARG D  43     1930   1463   1936     34    153     83       C  
ATOM   2215  CA BARG D  43      -0.860  -2.815 -48.493  0.50 14.18           C  
ANISOU 2215  CA BARG D  43     1949   1483   1953     35    153     83       C  
ATOM   2216  C   ARG D  43      -0.938  -4.015 -47.560  1.00 11.96           C  
ANISOU 2216  C   ARG D  43     1685   1233   1623     20    157     20       C  
ATOM   2217  O   ARG D  43      -1.181  -3.863 -46.388  1.00 14.72           O  
ANISOU 2217  O   ARG D  43     2036   1564   1992     13    159    -31       O  
ATOM   2218  CB AARG D  43      -2.097  -2.649 -49.313  0.50 15.30           C  
ANISOU 2218  CB AARG D  43     2079   1645   2089     66    143    108       C  
ATOM   2219  CB BARG D  43      -2.158  -2.726 -49.335  0.50 15.63           C  
ANISOU 2219  CB BARG D  43     2121   1690   2125     67    143    106       C  
ATOM   2220  CG AARG D  43      -3.398  -2.447 -48.527  0.50 15.55           C  
ANISOU 2220  CG AARG D  43     2104   1659   2145     78    136     51       C  
ATOM   2221  CG BARG D  43      -3.464  -3.305 -48.722  0.50 15.59           C  
ANISOU 2221  CG BARG D  43     2115   1704   2102     75    139     42       C  
ATOM   2222  CD AARG D  43      -4.578  -2.287 -49.477  0.50 17.86           C  
ANISOU 2222  CD AARG D  43     2380   1977   2429    114    123     77       C  
ATOM   2223  CD BARG D  43      -4.317  -2.281 -47.983  0.50 17.32           C  
ANISOU 2223  CD BARG D  43     2320   1874   2387     87    132      9       C  
ATOM   2224  NE AARG D  43      -5.859  -2.621 -48.852  0.50 15.88           N  
ANISOU 2224  NE AARG D  43     2121   1736   2174    122    120     11       N  
ATOM   2225  NE BARG D  43      -5.006  -2.861 -46.835  0.50 17.81           N  
ANISOU 2225  NE BARG D  43     2384   1948   2432     76    138    -66       N  
ATOM   2226  CZ AARG D  43      -7.045  -2.368 -49.403  0.50 15.77           C  
ANISOU 2226  CZ AARG D  43     2088   1737   2165    154    106     13       C  
ATOM   2227  CZ BARG D  43      -6.265  -3.277 -46.799  0.50 19.89           C  
ANISOU 2227  CZ BARG D  43     2638   2240   2677     89    137    -99       C  
ATOM   2228  NH1AARG D  43      -7.120  -1.774 -50.592  0.50 18.77           N  
ANISOU 2228  NH1AARG D  43     2456   2125   2550    185     92     83       N  
ATOM   2229  NH1BARG D  43      -7.057  -3.148 -47.853  0.50 25.20           N  
ANISOU 2229  NH1BARG D  43     3297   2931   3347    118    124    -71       N  
ATOM   2230  NH2AARG D  43      -8.148  -2.707 -48.774  0.50 13.26           N  
ANISOU 2230  NH2AARG D  43     1761   1431   1845    156    106    -52       N  
ATOM   2231  NH2BARG D  43      -6.720  -3.802 -45.681  0.50 13.01           N  
ANISOU 2231  NH2BARG D  43     1768   1383   1791     73    149   -160       N  
ATOM   2232  N   MET D  44      -0.738  -5.206 -48.123  1.00 11.21           N  
ANISOU 2232  N   MET D  44     1599   1191   1468     18    160     27       N  
ATOM   2233  CA  MET D  44      -0.866  -6.425 -47.364  1.00 10.06           C  
ANISOU 2233  CA  MET D  44     1468   1070   1285      5    165    -18       C  
ATOM   2234  C   MET D  44       0.483  -6.922 -46.850  1.00  8.66           C  
ANISOU 2234  C   MET D  44     1304    892   1092    -14    169    -25       C  
ATOM   2235  O   MET D  44       0.496  -7.824 -46.028  1.00 10.97           O  
ANISOU 2235  O   MET D  44     1609   1198   1361    -23    173    -56       O  
ATOM   2236  CB  MET D  44      -1.522  -7.536 -48.226  1.00  9.38           C  
ANISOU 2236  CB  MET D  44     1376   1031   1155     16    164    -19       C  
ATOM   2237  CG  MET D  44      -2.951  -7.223 -48.674  1.00 11.26           C  
ANISOU 2237  CG  MET D  44     1596   1278   1401     38    158    -25       C  
ATOM   2238  SD  MET D  44      -4.051  -6.972 -47.299  1.00 12.13           S  
ANISOU 2238  SD  MET D  44     1707   1361   1539     33    165    -78       S  
ATOM   2239  CE  MET D  44      -5.585  -6.609 -48.190  1.00 11.14           C  
ANISOU 2239  CE  MET D  44     1555   1254   1422     66    153    -79       C  
ATOM   2240  N   GLY D  45       1.587  -6.371 -47.294  1.00  9.76           N  
ANISOU 2240  N   GLY D  45     1439   1021   1246    -20    168      5       N  
ATOM   2241  CA  GLY D  45       2.906  -6.797 -46.796  1.00  8.95           C  
ANISOU 2241  CA  GLY D  45     1345    921   1132    -37    170     -7       C  
ATOM   2242  C   GLY D  45       3.376  -8.137 -47.253  1.00  7.94           C  
ANISOU 2242  C   GLY D  45     1224    834    956    -39    168     -7       C  
ATOM   2243  O   GLY D  45       4.062  -8.831 -46.498  1.00  9.78           O  
ANISOU 2243  O   GLY D  45     1468   1071   1174    -48    167    -31       O  
ATOM   2244  N   PHE D  46       3.044  -8.549 -48.479  1.00  8.45           N  
ANISOU 2244  N   PHE D  46     1278    934    997    -28    167     15       N  
ATOM   2245  CA  PHE D  46       3.554  -9.803 -49.003  1.00  7.69           C  
ANISOU 2245  CA  PHE D  46     1179    877    864    -28    163      4       C  
ATOM   2246  C   PHE D  46       3.611  -9.800 -50.514  1.00  9.34           C  
ANISOU 2246  C   PHE D  46     1364   1134   1048    -16    161     33       C  
ATOM   2247  O   PHE D  46       3.009  -8.931 -51.157  1.00  8.79           O  
ANISOU 2247  O   PHE D  46     1283   1071    984     -3    162     67       O  
ATOM   2248  CB  PHE D  46       2.713 -10.994 -48.531  1.00  7.42           C  
ANISOU 2248  CB  PHE D  46     1152    848    820    -26    163    -31       C  
ATOM   2249  CG  PHE D  46       1.459 -11.217 -49.345  1.00  6.66           C  
ANISOU 2249  CG  PHE D  46     1037    776    715    -11    161    -36       C  
ATOM   2250  CD1 PHE D  46       0.307 -10.506 -49.036  1.00  8.66           C  
ANISOU 2250  CD1 PHE D  46     1291   1012    986     -4    164    -36       C  
ATOM   2251  CD2 PHE D  46       1.429 -12.141 -50.398  1.00  7.90           C  
ANISOU 2251  CD2 PHE D  46     1171    979    849     -1    155    -50       C  
ATOM   2252  CE1 PHE D  46      -0.860 -10.687 -49.779  1.00  8.46           C  
ANISOU 2252  CE1 PHE D  46     1245   1014    954     12    161    -46       C  
ATOM   2253  CE2 PHE D  46       0.257 -12.335 -51.115  1.00  8.40           C  
ANISOU 2253  CE2 PHE D  46     1213   1072    906     15    152    -66       C  
ATOM   2254  CZ  PHE D  46      -0.872 -11.622 -50.792  1.00 10.09           C  
ANISOU 2254  CZ  PHE D  46     1429   1268   1136     22    154    -62       C  
ATOM   2255  N   GLY D  47       4.299 -10.794 -51.069  1.00  8.50           N  
ANISOU 2255  N   GLY D  47     1247   1068    913    -16    157     16       N  
ATOM   2256  CA  GLY D  47       4.371 -10.996 -52.503  1.00 10.12           C  
ANISOU 2256  CA  GLY D  47     1421   1340   1081     -1    154     30       C  
ATOM   2257  C   GLY D  47       4.844 -12.376 -52.840  1.00  9.03           C  
ANISOU 2257  C   GLY D  47     1267   1239    922      0    146    -16       C  
ATOM   2258  O   GLY D  47       4.755 -13.278 -52.028  1.00  8.43           O  
ANISOU 2258  O   GLY D  47     1205   1130    866     -6    142    -54       O  
ATOM   2259  N   PHE D  48       5.315 -12.531 -54.080  1.00 10.58           N  
ANISOU 2259  N   PHE D  48     1430   1506   1080     11    144    -11       N  
ATOM   2260  CA  PHE D  48       5.873 -13.781 -54.563  1.00 10.84           C  
ANISOU 2260  CA  PHE D  48     1437   1582   1097     15    134    -64       C  
ATOM   2261  C   PHE D  48       7.224 -13.536 -55.170  1.00 10.05           C  
ANISOU 2261  C   PHE D  48     1320   1527    971      9    139    -46       C  
ATOM   2262  O   PHE D  48       7.446 -12.484 -55.809  1.00 10.35           O  
ANISOU 2262  O   PHE D  48     1349   1597    986     10    152     11       O  
ATOM   2263  CB  PHE D  48       4.903 -14.471 -55.551  1.00 12.54           C  
ANISOU 2263  CB  PHE D  48     1615   1862   1288     39    124   -104       C  
ATOM   2264  CG  PHE D  48       3.853 -15.258 -54.827  1.00 12.06           C  
ANISOU 2264  CG  PHE D  48     1564   1750   1267     38    119   -148       C  
ATOM   2265  CD1 PHE D  48       4.084 -16.575 -54.469  1.00 14.99           C  
ANISOU 2265  CD1 PHE D  48     1926   2096   1670     32    112   -205       C  
ATOM   2266  CD2 PHE D  48       2.669 -14.657 -54.454  1.00 11.99           C  
ANISOU 2266  CD2 PHE D  48     1571   1713   1270     41    124   -128       C  
ATOM   2267  CE1 PHE D  48       3.143 -17.279 -53.770  1.00 19.07           C  
ANISOU 2267  CE1 PHE D  48     2451   2562   2232     27    113   -234       C  
ATOM   2268  CE2 PHE D  48       1.700 -15.353 -53.749  1.00 14.43           C  
ANISOU 2268  CE2 PHE D  48     1887   1978   1618     36    125   -165       C  
ATOM   2269  CZ  PHE D  48       1.955 -16.683 -53.401  1.00 15.38           C  
ANISOU 2269  CZ  PHE D  48     1998   2073   1770     27    121   -214       C  
ATOM   2270  N   ILE D  49       8.103 -14.509 -54.962  1.00 10.62           N  
ANISOU 2270  N   ILE D  49     1383   1597   1051      3    130    -94       N  
ATOM   2271  CA  ILE D  49       9.369 -14.650 -55.637  1.00 11.90           C  
ANISOU 2271  CA  ILE D  49     1518   1816   1188      0    132   -102       C  
ATOM   2272  C   ILE D  49       9.203 -15.700 -56.753  1.00 13.14           C  
ANISOU 2272  C   ILE D  49     1622   2055   1313     22    119   -163       C  
ATOM   2273  O   ILE D  49       8.572 -16.729 -56.530  1.00 13.01           O  
ANISOU 2273  O   ILE D  49     1600   2017   1325     32    104   -220       O  
ATOM   2274  CB  ILE D  49      10.455 -15.110 -54.641  1.00 11.23           C  
ANISOU 2274  CB  ILE D  49     1451   1676   1137    -14    125   -128       C  
ATOM   2275  CG1 ILE D  49      10.735 -13.941 -53.683  1.00 11.77           C  
ANISOU 2275  CG1 ILE D  49     1557   1683   1230    -33    138    -77       C  
ATOM   2276  CG2 ILE D  49      11.691 -15.615 -55.402  1.00 11.88           C  
ANISOU 2276  CG2 ILE D  49     1494   1823   1196    -12    121   -162       C  
ATOM   2277  CD1 ILE D  49      11.494 -14.382 -52.439  1.00 12.16           C  
ANISOU 2277  CD1 ILE D  49     1630   1675   1312    -42    127   -104       C  
ATOM   2278  N   SER D  50       9.736 -15.415 -57.938  1.00 13.00           N  
ANISOU 2278  N   SER D  50     1564   2135   1240     31    126   -152       N  
ATOM   2279  CA  SER D  50       9.890 -16.444 -58.977  1.00 14.13           C  
ANISOU 2279  CA  SER D  50     1646   2370   1349     52    112   -226       C  
ATOM   2280  C   SER D  50      11.238 -17.084 -58.744  1.00 12.96           C  
ANISOU 2280  C   SER D  50     1487   2216   1220     41    106   -270       C  
ATOM   2281  O   SER D  50      12.271 -16.443 -59.009  1.00 14.62           O  
ANISOU 2281  O   SER D  50     1690   2461   1403     28    121   -233       O  
ATOM   2282  CB  SER D  50       9.816 -15.825 -60.361  1.00 18.57           C  
ANISOU 2282  CB  SER D  50     2165   3057   1832     70    123   -191       C  
ATOM   2283  OG  SER D  50       8.493 -15.484 -60.656  1.00 18.61           O  
ANISOU 2283  OG  SER D  50     2171   3077   1820     89    121   -170       O  
ATOM   2284  N   MET D  51      11.234 -18.331 -58.236  1.00 13.71           N  
ANISOU 2284  N   MET D  51     1577   2262   1367     46     84   -345       N  
ATOM   2285  CA  MET D  51      12.458 -19.065 -57.982  1.00 12.76           C  
ANISOU 2285  CA  MET D  51     1444   2130   1274     42     72   -394       C  
ATOM   2286  C   MET D  51      12.949 -19.650 -59.300  1.00 17.02           C  
ANISOU 2286  C   MET D  51     1907   2786   1770     61     64   -463       C  
ATOM   2287  O   MET D  51      12.232 -20.412 -59.905  1.00 16.76           O  
ANISOU 2287  O   MET D  51     1834   2793   1739     82     50   -527       O  
ATOM   2288  CB  MET D  51      12.226 -20.157 -56.955  1.00 14.42           C  
ANISOU 2288  CB  MET D  51     1675   2241   1562     44     52   -436       C  
ATOM   2289  CG  MET D  51      13.408 -21.075 -56.745  1.00 15.66           C  
ANISOU 2289  CG  MET D  51     1810   2383   1754     48     33   -494       C  
ATOM   2290  SD  MET D  51      13.381 -22.106 -55.267  1.00 14.69           S  
ANISOU 2290  SD  MET D  51     1726   2129   1723     48     13   -504       S  
ATOM   2291  CE  MET D  51      11.821 -22.990 -55.425  1.00 15.16           C  
ANISOU 2291  CE  MET D  51     1770   2157   1831     59      8   -542       C  
ATOM   2292  N   THR D  52      14.166 -19.281 -59.707  1.00 14.83           N  
ANISOU 2292  N   THR D  52     1609   2568   1457     52     75   -454       N  
ATOM   2293  CA  THR D  52      14.720 -19.749 -61.014  1.00 16.81           C  
ANISOU 2293  CA  THR D  52     1781   2951   1653     70     71   -520       C  
ATOM   2294  C   THR D  52      15.877 -20.730 -60.837  1.00 19.98           C  
ANISOU 2294  C   THR D  52     2152   3343   2095     73     51   -604       C  
ATOM   2295  O   THR D  52      16.351 -21.315 -61.808  1.00 19.43           O  
ANISOU 2295  O   THR D  52     2012   3376   1994     90     43   -681       O  
ATOM   2296  CB  THR D  52      15.140 -18.560 -61.864  1.00 17.80           C  
ANISOU 2296  CB  THR D  52     1890   3178   1694     61    103   -444       C  
ATOM   2297  OG1 THR D  52      16.072 -17.755 -61.145  1.00 18.33           O  
ANISOU 2297  OG1 THR D  52     1997   3186   1781     30    122   -380       O  
ATOM   2298  CG2 THR D  52      13.920 -17.692 -62.252  1.00 18.99           C  
ANISOU 2298  CG2 THR D  52     2057   3354   1803     69    118   -368       C  
ATOM   2299  N   SER D  53      16.323 -20.916 -59.600  1.00 19.07           N  
ANISOU 2299  N   SER D  53     2086   3111   2046     59     41   -592       N  
ATOM   2300  CA ASER D  53      17.295 -21.933 -59.246  0.50 18.59           C  
ANISOU 2300  CA ASER D  53     2003   3020   2040     67     16   -667       C  
ATOM   2301  CA BSER D  53      17.313 -21.913 -59.241  0.50 18.17           C  
ANISOU 2301  CA BSER D  53     1951   2967   1986     67     16   -666       C  
ATOM   2302  C   SER D  53      16.993 -22.478 -57.864  1.00 18.93           C  
ANISOU 2302  C   SER D  53     2102   2923   2166     67     -2   -656       C  
ATOM   2303  O   SER D  53      16.660 -21.715 -56.938  1.00 18.52           O  
ANISOU 2303  O   SER D  53     2114   2803   2120     50     11   -576       O  
ATOM   2304  CB ASER D  53      18.716 -21.372 -59.260  0.50 23.29           C  
ANISOU 2304  CB ASER D  53     2590   3652   2607     51     28   -652       C  
ATOM   2305  CB BSER D  53      18.709 -21.286 -59.216  0.50 21.65           C  
ANISOU 2305  CB BSER D  53     2386   3440   2398     50     30   -645       C  
ATOM   2306  OG ASER D  53      19.625 -22.330 -58.737  0.50 26.21           O  
ANISOU 2306  OG ASER D  53     2945   3975   3036     62      0   -720       O  
ATOM   2307  OG BSER D  53      19.054 -20.716 -60.466  0.50 22.43           O  
ANISOU 2307  OG BSER D  53     2433   3673   2415     47     54   -640       O  
ATOM   2308  N   ARG D  54      17.038 -23.797 -57.720  1.00 20.55           N  
ANISOU 2308  N   ARG D  54     2279   3086   2440     87    -32   -734       N  
ATOM   2309  CA AARG D  54      16.735 -24.462 -56.454  0.50 19.75           C  
ANISOU 2309  CA AARG D  54     2224   2856   2421     90    -49   -718       C  
ATOM   2310  CA BARG D  54      16.766 -24.428 -56.452  0.50 19.96           C  
ANISOU 2310  CA BARG D  54     2251   2885   2446     89    -48   -717       C  
ATOM   2311  C   ARG D  54      17.975 -25.263 -56.078  1.00 22.60           C  
ANISOU 2311  C   ARG D  54     2565   3187   2831    103    -76   -768       C  
ATOM   2312  O   ARG D  54      18.479 -26.088 -56.876  1.00 21.76           O  
ANISOU 2312  O   ARG D  54     2392   3129   2747    122    -96   -861       O  
ATOM   2313  CB AARG D  54      15.473 -25.344 -56.555  0.50 21.10           C  
ANISOU 2313  CB AARG D  54     2380   2985   2649    101    -58   -754       C  
ATOM   2314  CB BARG D  54      15.505 -25.265 -56.521  0.50 21.08           C  
ANISOU 2314  CB BARG D  54     2381   2983   2642    100    -57   -749       C  
ATOM   2315  CG AARG D  54      15.159 -26.184 -55.314  0.50 20.11           C  
ANISOU 2315  CG AARG D  54     2294   2730   2617    104    -72   -735       C  
ATOM   2316  CG BARG D  54      14.979 -25.683 -55.168  0.50 20.83           C  
ANISOU 2316  CG BARG D  54     2406   2824   2681     96    -61   -700       C  
ATOM   2317  CD AARG D  54      13.748 -26.740 -55.264  0.50 18.37           C  
ANISOU 2317  CD AARG D  54     2071   2459   2448    104    -69   -743       C  
ATOM   2318  CD BARG D  54      13.862 -26.661 -55.333  0.50 20.48           C  
ANISOU 2318  CD BARG D  54     2337   2737   2708    104    -69   -744       C  
ATOM   2319  NE AARG D  54      13.429 -27.766 -56.281  0.50 19.23           N  
ANISOU 2319  NE AARG D  54     2100   2598   2605    122    -86   -852       N  
ATOM   2320  NE BARG D  54      13.782 -27.621 -54.247  0.50 25.52           N  
ANISOU 2320  NE BARG D  54     2997   3255   3441    109    -83   -728       N  
ATOM   2321  CZ AARG D  54      13.601 -29.083 -56.130  0.50 19.18           C  
ANISOU 2321  CZ AARG D  54     2057   2522   2706    138   -111   -917       C  
ATOM   2322  CZ BARG D  54      12.671 -27.859 -53.566  0.50 28.85           C  
ANISOU 2322  CZ BARG D  54     3451   3602   3908     99    -71   -686       C  
ATOM   2323  NH1AARG D  54      14.146 -29.571 -55.024  0.50 19.89           N  
ANISOU 2323  NH1AARG D  54     2183   2512   2859    140   -123   -875       N  
ATOM   2324  NH1BARG D  54      11.562 -27.201 -53.880  0.50 32.13           N  
ANISOU 2324  NH1BARG D  54     3875   4049   4281     86    -48   -667       N  
ATOM   2325  NH2AARG D  54      13.243 -29.928 -57.104  0.50 19.31           N  
ANISOU 2325  NH2AARG D  54     1994   2572   2770    154   -126  -1028       N  
ATOM   2326  NH2BARG D  54      12.663 -28.759 -52.592  0.50 26.12           N  
ANISOU 2326  NH2BARG D  54     3122   3151   3649    104    -81   -662       N  
ATOM   2327  N   GLU D  55      18.486 -25.020 -54.889  1.00 21.54           N  
ANISOU 2327  N   GLU D  55     2484   2983   2715     98    -80   -713       N  
ATOM   2328  CA  GLU D  55      19.726 -25.657 -54.455  1.00 23.64           C  
ANISOU 2328  CA  GLU D  55     2735   3224   3022    114   -108   -751       C  
ATOM   2329  C   GLU D  55      20.809 -25.708 -55.513  1.00 24.32           C  
ANISOU 2329  C   GLU D  55     2753   3408   3077    120   -113   -827       C  
ATOM   2330  O   GLU D  55      21.445 -26.749 -55.751  1.00 28.85           O  
ANISOU 2330  O   GLU D  55     3277   3979   3703    144   -143   -909       O  
ATOM   2331  CB  GLU D  55      19.411 -26.999 -53.816  1.00 25.53           C  
ANISOU 2331  CB  GLU D  55     2975   3364   3360    138   -138   -774       C  
ATOM   2332  CG  GLU D  55      18.808 -26.843 -52.413  1.00 35.90           C  
ANISOU 2332  CG  GLU D  55     4362   4583   4694    132   -132   -681       C  
ATOM   2333  CD  GLU D  55      19.743 -26.221 -51.352  1.00 33.52           C  
ANISOU 2333  CD  GLU D  55     4105   4267   4364    132   -137   -629       C  
ATOM   2334  OE1 GLU D  55      20.885 -25.751 -51.647  1.00 34.96           O  
ANISOU 2334  OE1 GLU D  55     4265   4507   4509    130   -140   -657       O  
ATOM   2335  OE2 GLU D  55      19.341 -26.204 -50.163  1.00 26.12           O  
ANISOU 2335  OE2 GLU D  55     3220   3263   3440    134   -136   -561       O  
ATOM   2336  N   GLY D  56      21.058 -24.554 -56.125  1.00 25.46           N  
ANISOU 2336  N   GLY D  56     2894   3641   3139     97    -82   -797       N  
ATOM   2337  CA  GLY D  56      22.143 -24.400 -57.084  1.00 30.03           C  
ANISOU 2337  CA  GLY D  56     3410   4324   3674     96    -77   -853       C  
ATOM   2338  C   GLY D  56      21.872 -24.991 -58.462  1.00 34.01           C  
ANISOU 2338  C   GLY D  56     3836   4927   4157    111    -80   -937       C  
ATOM   2339  O   GLY D  56      22.755 -24.984 -59.311  1.00 37.36           O  
ANISOU 2339  O   GLY D  56     4200   5452   4543    113    -77   -993       O  
ATOM   2340  N   SER D  57      20.664 -25.502 -58.684  1.00 27.13           N  
ANISOU 2340  N   SER D  57     2962   4034   3311    122    -86   -953       N  
ATOM   2341  CA  SER D  57      20.313 -26.156 -59.970  1.00 28.84           C  
ANISOU 2341  CA  SER D  57     3096   4347   3513    142    -94  -1050       C  
ATOM   2342  C   SER D  57      19.328 -25.231 -60.679  1.00 30.73           C  
ANISOU 2342  C   SER D  57     3342   4664   3667    131    -62   -994       C  
ATOM   2343  O   SER D  57      18.260 -24.946 -60.113  1.00 25.99           O  
ANISOU 2343  O   SER D  57     2798   3993   3084    122    -54   -930       O  
ATOM   2344  CB  SER D  57      19.640 -27.522 -59.722  1.00 38.33           C  
ANISOU 2344  CB  SER D  57     4278   5461   4822    166   -128  -1123       C  
ATOM   2345  OG  SER D  57      20.536 -28.478 -59.140  1.00 41.45           O  
ANISOU 2345  OG  SER D  57     4659   5782   5305    184   -162  -1176       O  
ATOM   2346  N   PRO D  58      19.668 -24.745 -61.901  1.00 29.35           N  
ANISOU 2346  N   PRO D  58     3110   4641   3400    131    -42  -1013       N  
ATOM   2347  CA  PRO D  58      18.772 -23.877 -62.688  1.00 29.93           C  
ANISOU 2347  CA  PRO D  58     3181   4803   3385    127    -14   -956       C  
ATOM   2348  C   PRO D  58      17.481 -24.593 -63.053  1.00 25.16           C  
ANISOU 2348  C   PRO D  58     2551   4199   2807    151    -32  -1014       C  
ATOM   2349  O   PRO D  58      17.508 -25.798 -63.299  1.00 24.62           O  
ANISOU 2349  O   PRO D  58     2426   4128   2800    174    -63  -1132       O  
ATOM   2350  CB  PRO D  58      19.587 -23.570 -63.944  1.00 40.18           C  
ANISOU 2350  CB  PRO D  58     4404   6272   4588    131      2   -988       C  
ATOM   2351  CG  PRO D  58      21.004 -23.649 -63.485  1.00 41.81           C  
ANISOU 2351  CG  PRO D  58     4610   6453   4822    119      0  -1005       C  
ATOM   2352  CD  PRO D  58      21.034 -24.765 -62.474  1.00 39.07           C  
ANISOU 2352  CD  PRO D  58     4284   5965   4594    132    -40  -1065       C  
ATOM   2353  N   LEU D  59      16.349 -23.875 -63.022  1.00 18.56           N  
ANISOU 2353  N   LEU D  59     1757   3355   1939    145    -14   -937       N  
ATOM   2354  CA  LEU D  59      15.030 -24.478 -63.294  1.00 18.12           C  
ANISOU 2354  CA  LEU D  59     1678   3293   1911    165    -29   -989       C  
ATOM   2355  C   LEU D  59      14.554 -24.016 -64.674  1.00 19.06           C  
ANISOU 2355  C   LEU D  59     1738   3582   1920    185    -18  -1001       C  
ATOM   2356  O   LEU D  59      14.707 -22.873 -65.045  1.00 18.05           O  
ANISOU 2356  O   LEU D  59     1628   3527   1702    175     10   -906       O  
ATOM   2357  CB  LEU D  59      14.010 -24.112 -62.219  1.00 19.08           C  
ANISOU 2357  CB  LEU D  59     1884   3283   2080    148    -22   -904       C  
ATOM   2358  CG  LEU D  59      14.353 -24.511 -60.778  1.00 17.63           C  
ANISOU 2358  CG  LEU D  59     1763   2941   1994    131    -32   -877       C  
ATOM   2359  CD1 LEU D  59      13.226 -24.003 -59.867  1.00 17.72           C  
ANISOU 2359  CD1 LEU D  59     1847   2855   2028    116    -19   -792       C  
ATOM   2360  CD2 LEU D  59      14.551 -26.012 -60.604  1.00 18.81           C  
ANISOU 2360  CD2 LEU D  59     1870   3030   2246    148    -65   -985       C  
ATOM   2361  N   GLU D  60      14.039 -24.940 -65.463  1.00 16.59           N  
ANISOU 2361  N   GLU D  60     1346   3339   1617    215    -41  -1122       N  
ATOM   2362  CA  GLU D  60      13.511 -24.561 -66.781  1.00 17.90           C  
ANISOU 2362  CA  GLU D  60     1448   3682   1671    241    -34  -1140       C  
ATOM   2363  C   GLU D  60      12.389 -23.531 -66.639  1.00 18.78           C  
ANISOU 2363  C   GLU D  60     1618   3779   1738    236    -14  -1025       C  
ATOM   2364  O   GLU D  60      12.276 -22.632 -67.466  1.00 17.31           O  
ANISOU 2364  O   GLU D  60     1415   3721   1438    247      5   -961       O  
ATOM   2365  CB  GLU D  60      12.981 -25.785 -67.516  1.00 18.99           C  
ANISOU 2365  CB  GLU D  60     1489   3881   1843    277    -67  -1304       C  
ATOM   2366  CG  GLU D  60      12.407 -25.458 -68.907  1.00 18.70           C  
ANISOU 2366  CG  GLU D  60     1376   4046   1681    312    -64  -1337       C  
ATOM   2367  CD  GLU D  60      12.119 -26.683 -69.745  1.00 17.93           C  
ANISOU 2367  CD  GLU D  60     1164   4037   1611    350    -99  -1524       C  
ATOM   2368  OE1 GLU D  60      13.008 -27.558 -69.821  1.00 20.77           O  
ANISOU 2368  OE1 GLU D  60     1470   4395   2026    354   -117  -1632       O  
ATOM   2369  OE2 GLU D  60      11.032 -26.750 -70.318  1.00 19.89           O  
ANISOU 2369  OE2 GLU D  60     1371   4355   1830    376   -109  -1567       O  
ATOM   2370  N   ASN D  61      11.502 -23.728 -65.671  1.00 16.23           N  
ANISOU 2370  N   ASN D  61     1352   3310   1503    225    -21  -1005       N  
ATOM   2371  CA  ASN D  61      10.410 -22.776 -65.409  1.00 17.77           C  
ANISOU 2371  CA  ASN D  61     1605   3476   1670    220     -5   -901       C  
ATOM   2372  C   ASN D  61      10.419 -22.325 -63.972  1.00 17.97           C  
ANISOU 2372  C   ASN D  61     1730   3332   1765    184      7   -806       C  
ATOM   2373  O   ASN D  61      10.754 -23.100 -63.109  1.00 15.82           O  
ANISOU 2373  O   ASN D  61     1477   2946   1585    171     -5   -842       O  
ATOM   2374  CB  ASN D  61       9.070 -23.384 -65.760  1.00 20.39           C  
ANISOU 2374  CB  ASN D  61     1895   3823   2026    245    -24   -980       C  
ATOM   2375  CG  ASN D  61       8.911 -23.499 -67.264  1.00 23.82           C  
ANISOU 2375  CG  ASN D  61     2232   4455   2361    286    -34  -1056       C  
ATOM   2376  OD1 ASN D  61       8.946 -24.576 -67.812  1.00 30.76           O  
ANISOU 2376  OD1 ASN D  61     3029   5387   3269    308    -59  -1197       O  
ATOM   2377  ND2 ASN D  61       8.863 -22.355 -67.932  1.00 25.78           N  
ANISOU 2377  ND2 ASN D  61     2485   4819   2490    297    -13   -959       N  
ATOM   2378  N   PRO D  62      10.092 -21.053 -63.744  1.00 17.01           N  
ANISOU 2378  N   PRO D  62     1665   3199   1597    172     31   -683       N  
ATOM   2379  CA  PRO D  62      10.134 -20.576 -62.365  1.00 18.89           C  
ANISOU 2379  CA  PRO D  62     1991   3288   1898    140     42   -601       C  
ATOM   2380  C   PRO D  62       9.085 -21.215 -61.487  1.00 18.70           C  
ANISOU 2380  C   PRO D  62     1996   3148   1960    136     30   -629       C  
ATOM   2381  O   PRO D  62       8.053 -21.671 -61.961  1.00 18.72           O  
ANISOU 2381  O   PRO D  62     1962   3182   1968    156     19   -685       O  
ATOM   2382  CB  PRO D  62       9.860 -19.081 -62.499  1.00 20.65           C  
ANISOU 2382  CB  PRO D  62     2252   3536   2056    133     68   -479       C  
ATOM   2383  CG  PRO D  62       9.116 -18.931 -63.756  1.00 24.74           C  
ANISOU 2383  CG  PRO D  62     2714   4189   2496    167     65   -494       C  
ATOM   2384  CD  PRO D  62       9.661 -19.999 -64.676  1.00 18.96           C  
ANISOU 2384  CD  PRO D  62     1897   3565   1740    188     47   -612       C  
ATOM   2385  N   VAL D  63       9.386 -21.241 -60.197  1.00 16.89           N  
ANISOU 2385  N   VAL D  63     1829   2790   1796    111     33   -590       N  
ATOM   2386  CA  VAL D  63       8.501 -21.756 -59.164  1.00 13.37           C  
ANISOU 2386  CA  VAL D  63     1421   2227   1432    102     29   -594       C  
ATOM   2387  C   VAL D  63       8.122 -20.614 -58.225  1.00 13.45           C  
ANISOU 2387  C   VAL D  63     1505   2169   1434     82     49   -489       C  
ATOM   2388  O   VAL D  63       8.983 -19.834 -57.751  1.00 13.55           O  
ANISOU 2388  O   VAL D  63     1556   2163   1430     65     61   -426       O  
ATOM   2389  CB  VAL D  63       9.201 -22.868 -58.371  1.00 15.88           C  
ANISOU 2389  CB  VAL D  63     1743   2456   1835     94     14   -639       C  
ATOM   2390  CG1 VAL D  63       8.449 -23.194 -57.088  1.00 21.40           C  
ANISOU 2390  CG1 VAL D  63     2492   3028   2608     79     18   -608       C  
ATOM   2391  CG2 VAL D  63       9.437 -24.112 -59.275  1.00 18.62           C  
ANISOU 2391  CG2 VAL D  63     2007   2856   2212    117     -8   -761       C  
ATOM   2392  N   ASP D  64       6.826 -20.513 -57.944  1.00 13.17           N  
ANISOU 2392  N   ASP D  64     1485   2099   1418     83     53   -478       N  
ATOM   2393  CA  ASP D  64       6.334 -19.469 -57.006  1.00 12.67           C  
ANISOU 2393  CA  ASP D  64     1487   1971   1355     66     70   -391       C  
ATOM   2394  C   ASP D  64       6.766 -19.751 -55.593  1.00 11.29           C  
ANISOU 2394  C   ASP D  64     1361   1689   1236     44     73   -369       C  
ATOM   2395  O   ASP D  64       6.617 -20.899 -55.118  1.00 12.47           O  
ANISOU 2395  O   ASP D  64     1504   1784   1449     43     64   -415       O  
ATOM   2396  CB  ASP D  64       4.794 -19.421 -56.969  1.00 12.63           C  
ANISOU 2396  CB  ASP D  64     1481   1952   1363     72     73   -397       C  
ATOM   2397  CG  ASP D  64       4.174 -18.763 -58.171  1.00 16.52           C  
ANISOU 2397  CG  ASP D  64     1938   2547   1789     97     72   -392       C  
ATOM   2398  OD1 ASP D  64       4.821 -18.045 -58.965  1.00 17.11           O  
ANISOU 2398  OD1 ASP D  64     1999   2701   1798    107     75   -355       O  
ATOM   2399  OD2 ASP D  64       2.923 -18.936 -58.305  1.00 19.75           O  
ANISOU 2399  OD2 ASP D  64     2332   2959   2211    108     68   -420       O  
ATOM   2400  N   VAL D  65       7.300 -18.712 -54.918  1.00 10.53           N  
ANISOU 2400  N   VAL D  65     1312   1565   1123     29     85   -300       N  
ATOM   2401  CA  VAL D  65       7.666 -18.794 -53.489  1.00  9.18           C  
ANISOU 2401  CA  VAL D  65     1188   1305    991     13     87   -274       C  
ATOM   2402  C   VAL D  65       7.046 -17.618 -52.769  1.00  8.62           C  
ANISOU 2402  C   VAL D  65     1160   1201    912      2    103   -213       C  
ATOM   2403  O   VAL D  65       7.325 -16.473 -53.100  1.00  8.57           O  
ANISOU 2403  O   VAL D  65     1160   1223    874      0    112   -172       O  
ATOM   2404  CB  VAL D  65       9.201 -18.833 -53.311  1.00  8.80           C  
ANISOU 2404  CB  VAL D  65     1142   1261    939      8     81   -274       C  
ATOM   2405  CG1 VAL D  65       9.542 -18.942 -51.805  1.00  8.86           C  
ANISOU 2405  CG1 VAL D  65     1196   1190    981     -1     79   -249       C  
ATOM   2406  CG2 VAL D  65       9.823 -19.990 -54.079  1.00 11.49           C  
ANISOU 2406  CG2 VAL D  65     1433   1639   1292     22     63   -344       C  
ATOM   2407  N   PHE D  66       6.179 -17.882 -51.793  1.00  7.33           N  
ANISOU 2407  N   PHE D  66     1024    979    782     -4    108   -207       N  
ATOM   2408  CA  PHE D  66       5.574 -16.831 -50.984  1.00  7.09           C  
ANISOU 2408  CA  PHE D  66     1029    917    747    -13    121   -162       C  
ATOM   2409  C   PHE D  66       6.635 -16.064 -50.199  1.00  7.15           C  
ANISOU 2409  C   PHE D  66     1064    903    749    -23    123   -130       C  
ATOM   2410  O   PHE D  66       7.566 -16.658 -49.685  1.00  7.36           O  
ANISOU 2410  O   PHE D  66     1096    913    785    -25    115   -142       O  
ATOM   2411  CB  PHE D  66       4.560 -17.454 -50.055  1.00  7.30           C  
ANISOU 2411  CB  PHE D  66     1070    893    808    -18    128   -169       C  
ATOM   2412  CG  PHE D  66       3.856 -16.481 -49.152  1.00  7.11           C  
ANISOU 2412  CG  PHE D  66     1077    843    781    -26    141   -135       C  
ATOM   2413  CD1 PHE D  66       4.360 -16.130 -47.914  1.00  7.35           C  
ANISOU 2413  CD1 PHE D  66     1139    841    811    -35    145   -113       C  
ATOM   2414  CD2 PHE D  66       2.619 -15.933 -49.541  1.00  7.95           C  
ANISOU 2414  CD2 PHE D  66     1175    961    883    -21    148   -135       C  
ATOM   2415  CE1 PHE D  66       3.709 -15.248 -47.059  1.00  7.70           C  
ANISOU 2415  CE1 PHE D  66     1203    868    853    -41    156    -95       C  
ATOM   2416  CE2 PHE D  66       1.975 -15.040 -48.697  1.00  7.59           C  
ANISOU 2416  CE2 PHE D  66     1152    891    840    -27    159   -113       C  
ATOM   2417  CZ  PHE D  66       2.486 -14.717 -47.454  1.00  8.02           C  
ANISOU 2417  CZ  PHE D  66     1235    915    896    -37    163    -96       C  
ATOM   2418  N   VAL D  67       6.455 -14.755 -50.091  1.00  7.53           N  
ANISOU 2418  N   VAL D  67     1124    948    786    -28    133    -95       N  
ATOM   2419  CA  VAL D  67       7.370 -13.929 -49.292  1.00  7.32           C  
ANISOU 2419  CA  VAL D  67     1118    898    765    -40    136    -76       C  
ATOM   2420  C   VAL D  67       6.624 -12.868 -48.507  1.00  7.46           C  
ANISOU 2420  C   VAL D  67     1155    882    796    -45    145    -56       C  
ATOM   2421  O   VAL D  67       5.950 -12.023 -49.054  1.00  7.00           O  
ANISOU 2421  O   VAL D  67     1089    828    739    -41    151    -34       O  
ATOM   2422  CB  VAL D  67       8.533 -13.321 -50.085  1.00  7.62           C  
ANISOU 2422  CB  VAL D  67     1137    967    790    -44    137    -62       C  
ATOM   2423  CG1 VAL D  67       8.019 -12.477 -51.256  1.00  8.94           C  
ANISOU 2423  CG1 VAL D  67     1285   1170    941    -39    147    -27       C  
ATOM   2424  CG2 VAL D  67       9.453 -12.510 -49.126  1.00 10.04           C  
ANISOU 2424  CG2 VAL D  67     1458   1241   1114    -58    139    -54       C  
ATOM   2425  N   HIS D  68       6.695 -12.931 -47.190  1.00  6.57           N  
ANISOU 2425  N   HIS D  68     1064    739    693    -49    144    -65       N  
ATOM   2426  CA  HIS D  68       6.157 -11.918 -46.299  1.00  6.20           C  
ANISOU 2426  CA  HIS D  68     1029    666    659    -53    151    -61       C  
ATOM   2427  C   HIS D  68       7.182 -10.827 -46.020  1.00  7.22           C  
ANISOU 2427  C   HIS D  68     1154    784    804    -61    151    -59       C  
ATOM   2428  O   HIS D  68       8.387 -11.077 -45.967  1.00  7.81           O  
ANISOU 2428  O   HIS D  68     1225    868    875    -65    144    -67       O  
ATOM   2429  CB  HIS D  68       5.739 -12.550 -44.975  1.00  7.08           C  
ANISOU 2429  CB  HIS D  68     1158    766    764    -52    153    -75       C  
ATOM   2430  CG  HIS D  68       4.958 -11.626 -44.129  1.00  6.96           C  
ANISOU 2430  CG  HIS D  68     1148    738    758    -53    161    -81       C  
ATOM   2431  ND1 HIS D  68       5.444 -11.078 -42.989  1.00  7.45           N  
ANISOU 2431  ND1 HIS D  68     1213    797    818    -54    158    -99       N  
ATOM   2432  CD2 HIS D  68       3.673 -11.107 -44.304  1.00  7.41           C  
ANISOU 2432  CD2 HIS D  68     1200    788    827    -51    169    -81       C  
ATOM   2433  CE1 HIS D  68       4.527 -10.259 -42.470  1.00  6.91           C  
ANISOU 2433  CE1 HIS D  68     1142    721    762    -54    165   -112       C  
ATOM   2434  NE2 HIS D  68       3.445 -10.255 -43.271  1.00  7.22           N  
ANISOU 2434  NE2 HIS D  68     1176    753    811    -52    172    -99       N  
ATOM   2435  N   GLN D  69       6.717  -9.603 -45.824  1.00  7.27           N  
ANISOU 2435  N   GLN D  69     1156    766    837    -64    157    -53       N  
ATOM   2436  CA  GLN D  69       7.656  -8.495 -45.549  1.00  7.86           C  
ANISOU 2436  CA  GLN D  69     1220    820    946    -74    158    -57       C  
ATOM   2437  C   GLN D  69       8.606  -8.723 -44.376  1.00  7.71           C  
ANISOU 2437  C   GLN D  69     1203    803    920    -76    149    -96       C  
ATOM   2438  O   GLN D  69       9.731  -8.266 -44.395  1.00  8.32           O  
ANISOU 2438  O   GLN D  69     1267    877   1017    -85    147   -105       O  
ATOM   2439  CB  GLN D  69       6.904  -7.176 -45.345  1.00  8.49           C  
ANISOU 2439  CB  GLN D  69     1290    863   1072    -75    164    -55       C  
ATOM   2440  CG  GLN D  69       5.883  -7.086 -44.224  1.00  8.46           C  
ANISOU 2440  CG  GLN D  69     1294    851   1069    -67    162    -89       C  
ATOM   2441  CD  GLN D  69       6.447  -6.746 -42.864  1.00  8.84           C  
ANISOU 2441  CD  GLN D  69     1337    897   1125    -69    157   -138       C  
ATOM   2442  OE1 GLN D  69       7.640  -6.512 -42.719  1.00  9.49           O  
ANISOU 2442  OE1 GLN D  69     1408    977   1220    -77    152   -152       O  
ATOM   2443  NE2 GLN D  69       5.580  -6.753 -41.866  1.00 11.69           N  
ANISOU 2443  NE2 GLN D  69     1700   1267   1473    -61    157   -169       N  
ATOM   2444  N   SER D  70       8.183  -9.524 -43.412  1.00  7.87           N  
ANISOU 2444  N   SER D  70     1240    838    911    -67    143   -114       N  
ATOM   2445  CA  SER D  70       8.987  -9.799 -42.230  1.00  7.94           C  
ANISOU 2445  CA  SER D  70     1251    863    901    -61    132   -146       C  
ATOM   2446  C   SER D  70      10.208 -10.611 -42.507  1.00  8.44           C  
ANISOU 2446  C   SER D  70     1314    944    948    -59    121   -145       C  
ATOM   2447  O   SER D  70      11.096 -10.675 -41.670  1.00  8.83           O  
ANISOU 2447  O   SER D  70     1359   1008    987    -53    109   -172       O  
ATOM   2448  CB  SER D  70       8.142 -10.443 -41.119  1.00  7.80           C  
ANISOU 2448  CB  SER D  70     1250    864    850    -50    133   -152       C  
ATOM   2449  OG  SER D  70       7.699 -11.719 -41.557  1.00  9.02           O  
ANISOU 2449  OG  SER D  70     1418   1022    984    -46    136   -122       O  
ATOM   2450  N   LYS D  71      10.259 -11.226 -43.684  1.00  7.59           N  
ANISOU 2450  N   LYS D  71     1205    840    838    -62    123   -120       N  
ATOM   2451  CA  LYS D  71      11.384 -12.071 -44.067  1.00  7.35           C  
ANISOU 2451  CA  LYS D  71     1169    827    796    -58    111   -126       C  
ATOM   2452  C   LYS D  71      12.499 -11.329 -44.771  1.00  7.80           C  
ANISOU 2452  C   LYS D  71     1201    888    872    -71    114   -131       C  
ATOM   2453  O   LYS D  71      13.542 -11.938 -45.067  1.00  8.87           O  
ANISOU 2453  O   LYS D  71     1326   1043    999    -69    104   -144       O  
ATOM   2454  CB  LYS D  71      10.934 -13.210 -44.969  1.00  8.43           C  
ANISOU 2454  CB  LYS D  71     1307    973    921    -53    111   -111       C  
ATOM   2455  CG  LYS D  71       9.730 -13.970 -44.519  1.00  7.73           C  
ANISOU 2455  CG  LYS D  71     1236    874    827    -45    114   -102       C  
ATOM   2456  CD  LYS D  71       9.815 -14.515 -43.107  1.00  7.53           C  
ANISOU 2456  CD  LYS D  71     1228    846    787    -34    107   -103       C  
ATOM   2457  CE  LYS D  71       8.763 -15.598 -42.924  1.00  8.69           C  
ANISOU 2457  CE  LYS D  71     1385    981    935    -30    114    -85       C  
ATOM   2458  NZ  LYS D  71       8.750 -16.077 -41.513  1.00  8.78           N  
ANISOU 2458  NZ  LYS D  71     1413    996    926    -19    112    -70       N  
ATOM   2459  N   LEU D  72      12.277 -10.078 -45.151  1.00  8.40           N  
ANISOU 2459  N   LEU D  72     1265    945    979    -86    129   -118       N  
ATOM   2460  CA  LEU D  72      13.203  -9.363 -46.016  1.00  9.32           C  
ANISOU 2460  CA  LEU D  72     1356   1064   1120   -103    139   -106       C  
ATOM   2461  C   LEU D  72      14.330  -8.735 -45.190  1.00  9.75           C  
ANISOU 2461  C   LEU D  72     1394   1107   1204   -111    134   -145       C  
ATOM   2462  O   LEU D  72      14.085  -7.940 -44.266  1.00 10.89           O  
ANISOU 2462  O   LEU D  72     1534   1224   1376   -112    133   -170       O  
ATOM   2463  CB  LEU D  72      12.478  -8.264 -46.788  1.00  9.04           C  
ANISOU 2463  CB  LEU D  72     1312   1006   1116   -113    158    -63       C  
ATOM   2464  CG  LEU D  72      11.273  -8.732 -47.621  1.00  8.81           C  
ANISOU 2464  CG  LEU D  72     1294    995   1058   -101    162    -29       C  
ATOM   2465  CD1 LEU D  72      10.544  -7.569 -48.295  1.00  9.33           C  
ANISOU 2465  CD1 LEU D  72     1349   1038   1154   -105    177     16       C  
ATOM   2466  CD2 LEU D  72      11.616  -9.751 -48.673  1.00  8.60           C  
ANISOU 2466  CD2 LEU D  72     1257   1018    990    -95    159    -23       C  
ATOM   2467  N   TYR D  73      15.556  -9.089 -45.538  1.00 10.44           N  
ANISOU 2467  N   TYR D  73     1463   1217   1285   -116    130   -160       N  
ATOM   2468  CA  TYR D  73      16.743  -8.512 -44.932  1.00 12.15           C  
ANISOU 2468  CA  TYR D  73     1655   1429   1533   -126    125   -202       C  
ATOM   2469  C   TYR D  73      17.079  -7.152 -45.545  1.00 13.12           C  
ANISOU 2469  C   TYR D  73     1747   1520   1718   -155    151   -183       C  
ATOM   2470  O   TYR D  73      17.520  -7.081 -46.693  1.00 14.84           O  
ANISOU 2470  O   TYR D  73     1946   1752   1937   -171    169   -146       O  
ATOM   2471  CB  TYR D  73      17.901  -9.459 -45.106  1.00 12.19           C  
ANISOU 2471  CB  TYR D  73     1649   1472   1510   -119    111   -227       C  
ATOM   2472  CG  TYR D  73      19.198  -8.930 -44.563  1.00 14.19           C  
ANISOU 2472  CG  TYR D  73     1870   1727   1794   -128    105   -277       C  
ATOM   2473  CD1 TYR D  73      19.317  -8.627 -43.206  1.00 16.20           C  
ANISOU 2473  CD1 TYR D  73     2123   1975   2055   -115     87   -327       C  
ATOM   2474  CD2 TYR D  73      20.285  -8.749 -45.380  1.00 14.42           C  
ANISOU 2474  CD2 TYR D  73     1866   1771   1841   -148    117   -281       C  
ATOM   2475  CE1 TYR D  73      20.530  -8.175 -42.676  1.00 20.78           C  
ANISOU 2475  CE1 TYR D  73     2667   2564   2664   -120     79   -386       C  
ATOM   2476  CE2 TYR D  73      21.483  -8.286 -44.856  1.00 18.72           C  
ANISOU 2476  CE2 TYR D  73     2376   2317   2419   -157    112   -335       C  
ATOM   2477  CZ  TYR D  73      21.591  -8.016 -43.515  1.00 18.23           C  
ANISOU 2477  CZ  TYR D  73     2312   2247   2366   -142     91   -390       C  
ATOM   2478  OH  TYR D  73      22.797  -7.535 -43.010  1.00 24.16           O  
ANISOU 2478  OH  TYR D  73     3022   3005   3152   -149     84   -454       O  
ATOM   2479  N   MET D  74      16.763  -6.102 -44.795  1.00 12.25           N  
ANISOU 2479  N   MET D  74     1627   1366   1659   -161    154   -204       N  
ATOM   2480  CA  MET D  74      16.993  -4.710 -45.194  1.00 14.42           C  
ANISOU 2480  CA  MET D  74     1869   1592   2015   -189    178   -186       C  
ATOM   2481  C   MET D  74      16.571  -3.836 -44.022  1.00 15.73           C  
ANISOU 2481  C   MET D  74     2026   1717   2234   -185    169   -238       C  
ATOM   2482  O   MET D  74      15.818  -4.270 -43.150  1.00 17.49           O  
ANISOU 2482  O   MET D  74     2271   1955   2417   -162    151   -267       O  
ATOM   2483  CB  MET D  74      16.209  -4.323 -46.447  1.00 15.98           C  
ANISOU 2483  CB  MET D  74     2073   1776   2223   -197    201   -102       C  
ATOM   2484  CG  MET D  74      14.682  -4.410 -46.266  1.00 17.77           C  
ANISOU 2484  CG  MET D  74     2331   1991   2429   -177    194    -82       C  
ATOM   2485  SD  MET D  74      13.782  -4.622 -47.817  1.00 15.19           S  
ANISOU 2485  SD  MET D  74     2016   1688   2066   -171    210      7       S  
ATOM   2486  CE  MET D  74      14.138  -3.123 -48.682  1.00 18.47           C  
ANISOU 2486  CE  MET D  74     2396   2056   2564   -197    241     74       C  
ATOM   2487  N   GLU D  75      17.132  -2.631 -43.965  1.00 18.24           N  
ANISOU 2487  N   GLU D  75     2302   1985   2644   -209    183   -258       N  
ATOM   2488  CA  GLU D  75      16.714  -1.631 -43.006  1.00 21.64           C  
ANISOU 2488  CA  GLU D  75     2709   2367   3142   -208    177   -313       C  
ATOM   2489  C   GLU D  75      15.516  -0.836 -43.505  1.00 18.21           C  
ANISOU 2489  C   GLU D  75     2282   1878   2758   -210    192   -257       C  
ATOM   2490  O   GLU D  75      15.287  -0.685 -44.719  1.00 19.61           O  
ANISOU 2490  O   GLU D  75     2466   2039   2943   -221    213   -169       O  
ATOM   2491  CB  GLU D  75      17.890  -0.668 -42.737  1.00 22.82           C  
ANISOU 2491  CB  GLU D  75     2802   2478   3388   -234    185   -368       C  
ATOM   2492  CG  GLU D  75      19.062  -1.375 -42.073  1.00 30.35           C  
ANISOU 2492  CG  GLU D  75     3743   3491   4296   -225    165   -440       C  
ATOM   2493  CD  GLU D  75      18.749  -1.806 -40.650  1.00 38.93           C  
ANISOU 2493  CD  GLU D  75     4838   4623   5328   -190    131   -520       C  
ATOM   2494  OE1 GLU D  75      18.606  -0.918 -39.779  1.00 56.33           O  
ANISOU 2494  OE1 GLU D  75     7006   6803   7592   -188    123   -593       O  
ATOM   2495  OE2 GLU D  75      18.633  -3.032 -40.401  1.00 46.30           O  
ANISOU 2495  OE2 GLU D  75     5810   5621   6161   -164    112   -510       O  
ATOM   2496  N   GLY D  76      14.781  -0.296 -42.548  1.00 19.74           N  
ANISOU 2496  N   GLY D  76     2468   2047   2985   -197    179   -312       N  
ATOM   2497  CA  GLY D  76      13.634   0.573 -42.846  1.00 19.84           C  
ANISOU 2497  CA  GLY D  76     2479   2000   3059   -195    188   -276       C  
ATOM   2498  C   GLY D  76      12.438  -0.233 -43.328  1.00 18.50           C  
ANISOU 2498  C   GLY D  76     2357   1865   2805   -174    186   -216       C  
ATOM   2499  O   GLY D  76      12.344  -1.421 -43.068  1.00 18.94           O  
ANISOU 2499  O   GLY D  76     2445   1986   2763   -159    174   -225       O  
ATOM   2500  N   PHE D  77      11.555   0.431 -44.069  1.00 19.71           N  
ANISOU 2500  N   PHE D  77     2511   1972   3003   -174    197   -154       N  
ATOM   2501  CA  PHE D  77      10.373  -0.198 -44.680  1.00 15.13           C  
ANISOU 2501  CA  PHE D  77     1968   1422   2356   -154    196    -96       C  
ATOM   2502  C   PHE D  77      10.782  -1.308 -45.628  1.00 15.74           C  
ANISOU 2502  C   PHE D  77     2070   1561   2346   -155    202    -42       C  
ATOM   2503  O   PHE D  77      11.622  -1.139 -46.525  1.00 16.09           O  
ANISOU 2503  O   PHE D  77     2101   1606   2405   -172    218      6       O  
ATOM   2504  CB  PHE D  77       9.527   0.838 -45.424  1.00 17.10           C  
ANISOU 2504  CB  PHE D  77     2207   1611   2679   -151    206    -33       C  
ATOM   2505  CG  PHE D  77       8.147   0.322 -45.795  1.00 15.53           C  
ANISOU 2505  CG  PHE D  77     2038   1442   2420   -125    199      0       C  
ATOM   2506  CD1 PHE D  77       7.103   0.401 -44.886  1.00 14.78           C  
ANISOU 2506  CD1 PHE D  77     1947   1341   2328   -107    185    -58       C  
ATOM   2507  CD2 PHE D  77       7.923  -0.223 -47.036  1.00 14.99           C  
ANISOU 2507  CD2 PHE D  77     1988   1414   2294   -118    207     79       C  
ATOM   2508  CE1 PHE D  77       5.850  -0.062 -45.212  1.00 13.98           C  
ANISOU 2508  CE1 PHE D  77     1867   1266   2176    -86    180    -34       C  
ATOM   2509  CE2 PHE D  77       6.679  -0.712 -47.380  1.00 14.74           C  
ANISOU 2509  CE2 PHE D  77     1977   1412   2210    -94    199     99       C  
ATOM   2510  CZ  PHE D  77       5.640  -0.590 -46.476  1.00 13.07           C  
ANISOU 2510  CZ  PHE D  77     1769   1185   2010    -79    187     44       C  
ATOM   2511  N   ARG D  78      10.190  -2.473 -45.388  1.00 12.82           N  
ANISOU 2511  N   ARG D  78     1733   1246   1890   -136    189    -56       N  
ATOM   2512  CA  ARG D  78      10.572  -3.700 -46.114  1.00 11.18           C  
ANISOU 2512  CA  ARG D  78     1544   1099   1602   -134    189    -27       C  
ATOM   2513  C   ARG D  78       9.651  -4.010 -47.282  1.00 13.15           C  
ANISOU 2513  C   ARG D  78     1807   1373   1816   -121    195     36       C  
ATOM   2514  O   ARG D  78       8.415  -4.163 -47.109  1.00 12.10           O  
ANISOU 2514  O   ARG D  78     1689   1239   1668   -104    189     34       O  
ATOM   2515  CB  ARG D  78      10.591  -4.867 -45.148  1.00 10.90           C  
ANISOU 2515  CB  ARG D  78     1531   1105   1503   -121    172    -81       C  
ATOM   2516  CG  ARG D  78      11.675  -4.764 -44.090  1.00 10.73           C  
ANISOU 2516  CG  ARG D  78     1495   1085   1496   -127    162   -144       C  
ATOM   2517  CD  ARG D  78      11.597  -5.906 -43.084  1.00 10.80           C  
ANISOU 2517  CD  ARG D  78     1525   1138   1438   -109    145   -183       C  
ATOM   2518  NE  ARG D  78      10.365  -5.808 -42.314  1.00 11.32           N  
ANISOU 2518  NE  ARG D  78     1602   1201   1495    -95    142   -200       N  
ATOM   2519  CZ  ARG D  78      10.209  -5.090 -41.207  1.00 14.40           C  
ANISOU 2519  CZ  ARG D  78     1976   1583   1911    -91    136   -255       C  
ATOM   2520  NH1 ARG D  78      11.230  -4.422 -40.685  1.00 17.73           N  
ANISOU 2520  NH1 ARG D  78     2367   1996   2372    -98    130   -305       N  
ATOM   2521  NH2 ARG D  78       9.033  -5.050 -40.602  1.00 13.77           N  
ANISOU 2521  NH2 ARG D  78     1904   1510   1818    -79    136   -270       N  
ATOM   2522  N   SER D  79      10.235  -4.037 -48.475  1.00 11.79           N  
ANISOU 2522  N   SER D  79     1622   1226   1631   -129    208     91       N  
ATOM   2523  CA  SER D  79       9.525  -4.409 -49.700  1.00 13.35           C  
ANISOU 2523  CA  SER D  79     1823   1467   1780   -114    212    148       C  
ATOM   2524  C   SER D  79      10.497  -4.955 -50.724  1.00 12.05           C  
ANISOU 2524  C   SER D  79     1644   1362   1572   -121    222    175       C  
ATOM   2525  O   SER D  79      11.700  -4.873 -50.514  1.00 12.58           O  
ANISOU 2525  O   SER D  79     1698   1425   1656   -141    228    158       O  
ATOM   2526  CB  SER D  79       8.762  -3.181 -50.267  1.00 16.43           C  
ANISOU 2526  CB  SER D  79     2202   1818   2223   -108    222    212       C  
ATOM   2527  OG  SER D  79       9.653  -2.246 -50.830  1.00 16.54           O  
ANISOU 2527  OG  SER D  79     2189   1806   2288   -127    243    266       O  
ATOM   2528  N   LEU D  80       9.973  -5.573 -51.783  1.00 12.73           N  
ANISOU 2528  N   LEU D  80     1727   1510   1597   -104    221    206       N  
ATOM   2529  CA  LEU D  80      10.756  -5.956 -52.949  1.00 12.81           C  
ANISOU 2529  CA  LEU D  80     1714   1591   1560   -107    232    236       C  
ATOM   2530  C   LEU D  80      10.247  -5.171 -54.168  1.00 15.38           C  
ANISOU 2530  C   LEU D  80     2021   1945   1877    -96    248    325       C  
ATOM   2531  O   LEU D  80       9.045  -4.929 -54.271  1.00 16.31           O  
ANISOU 2531  O   LEU D  80     2148   2052   1995    -74    240    344       O  
ATOM   2532  CB  LEU D  80      10.660  -7.450 -53.222  1.00 12.60           C  
ANISOU 2532  CB  LEU D  80     1691   1631   1465    -91    216    187       C  
ATOM   2533  CG  LEU D  80      11.282  -8.419 -52.196  1.00 12.30           C  
ANISOU 2533  CG  LEU D  80     1667   1577   1427    -97    200    112       C  
ATOM   2534  CD1 LEU D  80      11.014  -9.864 -52.572  1.00 13.09           C  
ANISOU 2534  CD1 LEU D  80     1765   1731   1476    -79    184     70       C  
ATOM   2535  CD2 LEU D  80      12.799  -8.228 -52.038  1.00 13.45           C  
ANISOU 2535  CD2 LEU D  80     1796   1722   1590   -119    208    100       C  
ATOM   2536  N   LYS D  81      11.167  -4.821 -55.064  1.00 18.22           N  
ANISOU 2536  N   LYS D  81     2352   2345   2225   -109    270    378       N  
ATOM   2537  CA  LYS D  81      10.827  -4.228 -56.359  1.00 20.21           C  
ANISOU 2537  CA  LYS D  81     2581   2649   2449    -96    288    473       C  
ATOM   2538  C   LYS D  81      10.672  -5.362 -57.373  1.00 22.41           C  
ANISOU 2538  C   LYS D  81     2842   3048   2624    -71    279    455       C  
ATOM   2539  O   LYS D  81      11.485  -6.263 -57.396  1.00 18.30           O  
ANISOU 2539  O   LYS D  81     2310   2571   2068    -80    275    399       O  
ATOM   2540  CB  LYS D  81      11.940  -3.253 -56.772  1.00 25.67           C  
ANISOU 2540  CB  LYS D  81     3244   3325   3184   -126    321    545       C  
ATOM   2541  CG  LYS D  81      11.722  -2.461 -58.050  1.00 31.76           C  
ANISOU 2541  CG  LYS D  81     3988   4142   3935   -115    346    667       C  
ATOM   2542  CD  LYS D  81      12.787  -1.369 -58.162  1.00 32.87           C  
ANISOU 2542  CD  LYS D  81     4104   4234   4152   -153    383    737       C  
ATOM   2543  CE  LYS D  81      12.862  -0.770 -59.563  1.00 40.55           C  
ANISOU 2543  CE  LYS D  81     5043   5278   5086   -145    415    870       C  
ATOM   2544  NZ  LYS D  81      11.797   0.254 -59.782  1.00 53.17           N  
ANISOU 2544  NZ  LYS D  81     6646   6822   6732   -122    414    963       N  
ATOM   2545  N   GLU D  82       9.624  -5.314 -58.208  1.00 24.13           N  
ANISOU 2545  N   GLU D  82     3051   3320   2795    -38    273    497       N  
ATOM   2546  CA  GLU D  82       9.456  -6.310 -59.277  1.00 22.71           C  
ANISOU 2546  CA  GLU D  82     2842   3267   2517    -12    264    474       C  
ATOM   2547  C   GLU D  82      10.771  -6.492 -60.047  1.00 22.26           C  
ANISOU 2547  C   GLU D  82     2749   3291   2416    -28    286    491       C  
ATOM   2548  O   GLU D  82      11.427  -5.521 -60.478  1.00 25.14           O  
ANISOU 2548  O   GLU D  82     3097   3656   2798    -46    316    579       O  
ATOM   2549  CB  GLU D  82       8.298  -5.950 -60.251  1.00 24.21           C  
ANISOU 2549  CB  GLU D  82     3017   3522   2660     28    259    536       C  
ATOM   2550  CG  GLU D  82       6.905  -6.166 -59.674  1.00 32.07           C  
ANISOU 2550  CG  GLU D  82     4037   4470   3675     50    232    492       C  
ATOM   2551  CD  GLU D  82       5.777  -5.907 -60.667  1.00 33.67           C  
ANISOU 2551  CD  GLU D  82     4219   4747   3825     95    222    541       C  
ATOM   2552  OE1 GLU D  82       6.064  -5.657 -61.857  1.00 35.16           O  
ANISOU 2552  OE1 GLU D  82     4372   5038   3949    113    234    609       O  
ATOM   2553  OE2 GLU D  82       4.591  -5.957 -60.263  1.00 32.70           O  
ANISOU 2553  OE2 GLU D  82     4111   4589   3722    115    202    510       O  
ATOM   2554  N   GLY D  83      11.145  -7.753 -60.198  1.00 19.99           N  
ANISOU 2554  N   GLY D  83     2447   3069   2080    -22    271    403       N  
ATOM   2555  CA  GLY D  83      12.352  -8.134 -60.916  1.00 21.36           C  
ANISOU 2555  CA  GLY D  83     2580   3331   2205    -34    287    394       C  
ATOM   2556  C   GLY D  83      13.666  -8.100 -60.156  1.00 22.19           C  
ANISOU 2556  C   GLY D  83     2690   3376   2363    -73    298    364       C  
ATOM   2557  O   GLY D  83      14.690  -8.575 -60.678  1.00 18.50           O  
ANISOU 2557  O   GLY D  83     2187   2983   1857    -82    307    338       O  
ATOM   2558  N   GLU D  84      13.696  -7.550 -58.938  1.00 18.88           N  
ANISOU 2558  N   GLU D  84     2310   2832   2029    -94    296    361       N  
ATOM   2559  CA  GLU D  84      15.005  -7.449 -58.255  1.00 19.03           C  
ANISOU 2559  CA  GLU D  84     2327   2804   2096   -129    306    330       C  
ATOM   2560  C   GLU D  84      15.492  -8.843 -57.902  1.00 17.20           C  
ANISOU 2560  C   GLU D  84     2094   2599   1840   -121    279    224       C  
ATOM   2561  O   GLU D  84      14.694  -9.678 -57.526  1.00 16.35           O  
ANISOU 2561  O   GLU D  84     2008   2481   1724    -99    251    170       O  
ATOM   2562  CB  GLU D  84      14.994  -6.525 -57.036  1.00 19.95           C  
ANISOU 2562  CB  GLU D  84     2476   2793   2309   -150    308    340       C  
ATOM   2563  CG  GLU D  84      14.368  -7.072 -55.750  1.00 19.68           C  
ANISOU 2563  CG  GLU D  84     2484   2688   2305   -140    276    265       C  
ATOM   2564  CD  GLU D  84      14.676  -6.176 -54.551  1.00 15.93           C  
ANISOU 2564  CD  GLU D  84     2026   2108   1918   -163    279    257       C  
ATOM   2565  OE1 GLU D  84      15.811  -6.278 -54.039  1.00 19.36           O  
ANISOU 2565  OE1 GLU D  84     2450   2528   2376   -183    281    215       O  
ATOM   2566  OE2 GLU D  84      13.817  -5.364 -54.146  1.00 18.87           O  
ANISOU 2566  OE2 GLU D  84     2415   2416   2336   -160    279    287       O  
ATOM   2567  N   PRO D  85      16.804  -9.102 -58.012  1.00 15.70           N  
ANISOU 2567  N   PRO D  85     1876   2441   1646   -140    288    193       N  
ATOM   2568  CA  PRO D  85      17.300 -10.434 -57.786  1.00 16.28           C  
ANISOU 2568  CA  PRO D  85     1941   2543   1699   -129    261     95       C  
ATOM   2569  C   PRO D  85      17.398 -10.754 -56.286  1.00 12.99           C  
ANISOU 2569  C   PRO D  85     1565   2025   1343   -132    236     39       C  
ATOM   2570  O   PRO D  85      17.797  -9.894 -55.496  1.00 15.37           O  
ANISOU 2570  O   PRO D  85     1883   2256   1700   -155    246     58       O  
ATOM   2571  CB  PRO D  85      18.684 -10.420 -58.439  1.00 20.23           C  
ANISOU 2571  CB  PRO D  85     2393   3114   2178   -148    282     89       C  
ATOM   2572  CG  PRO D  85      19.094  -8.992 -58.369  1.00 18.65           C  
ANISOU 2572  CG  PRO D  85     2192   2870   2023   -181    319    174       C  
ATOM   2573  CD  PRO D  85      17.845  -8.221 -58.593  1.00 18.38           C  
ANISOU 2573  CD  PRO D  85     2180   2811   1992   -170    327    254       C  
ATOM   2574  N   VAL D  86      16.989 -11.968 -55.918  1.00 12.80           N  
ANISOU 2574  N   VAL D  86     1555   1997   1310   -109    204    -27       N  
ATOM   2575  CA  VAL D  86      17.033 -12.366 -54.530  1.00 12.04           C  
ANISOU 2575  CA  VAL D  86     1495   1819   1259   -107    181    -70       C  
ATOM   2576  C   VAL D  86      17.609 -13.769 -54.379  1.00 12.69           C  
ANISOU 2576  C   VAL D  86     1565   1922   1335    -91    153   -149       C  
ATOM   2577  O   VAL D  86      17.599 -14.574 -55.292  1.00 14.48           O  
ANISOU 2577  O   VAL D  86     1758   2214   1527    -75    146   -181       O  
ATOM   2578  CB  VAL D  86      15.626 -12.348 -53.871  1.00 13.18           C  
ANISOU 2578  CB  VAL D  86     1682   1906   1420    -95    171    -57       C  
ATOM   2579  CG1 VAL D  86      15.106 -10.932 -53.784  1.00 12.73           C  
ANISOU 2579  CG1 VAL D  86     1639   1811   1386   -109    193     11       C  
ATOM   2580  CG2 VAL D  86      14.658 -13.250 -54.643  1.00 14.50           C  
ANISOU 2580  CG2 VAL D  86     1837   2120   1550    -70    160    -75       C  
ATOM   2581  N   GLU D  87      18.098 -14.010 -53.173  1.00 12.00           N  
ANISOU 2581  N   GLU D  87     1501   1774   1284    -91    135   -179       N  
ATOM   2582  CA AGLU D  87      18.695 -15.236 -52.675  0.50 12.95           C  
ANISOU 2582  CA AGLU D  87     1618   1887   1415    -73    105   -243       C  
ATOM   2583  CA BGLU D  87      18.568 -15.313 -52.726  0.50 11.63           C  
ANISOU 2583  CA BGLU D  87     1452   1721   1247    -71    104   -243       C  
ATOM   2584  C   GLU D  87      17.946 -15.530 -51.384  1.00 10.16           C  
ANISOU 2584  C   GLU D  87     1312   1460   1089    -61     88   -240       C  
ATOM   2585  O   GLU D  87      17.776 -14.603 -50.593  1.00 11.63           O  
ANISOU 2585  O   GLU D  87     1524   1604   1290    -74     97   -211       O  
ATOM   2586  CB AGLU D  87      20.153 -14.868 -52.346  0.50 15.24           C  
ANISOU 2586  CB AGLU D  87     1888   2181   1718    -87    106   -265       C  
ATOM   2587  CB BGLU D  87      20.095 -15.368 -52.585  0.50 11.75           C  
ANISOU 2587  CB BGLU D  87     1439   1754   1270    -78     99   -281       C  
ATOM   2588  CG AGLU D  87      21.184 -15.945 -52.112  0.50 21.38           C  
ANISOU 2588  CG AGLU D  87     2646   2972   2505    -70     78   -332       C  
ATOM   2589  CG BGLU D  87      20.845 -14.733 -53.741  0.50 15.33           C  
ANISOU 2589  CG BGLU D  87     1847   2280   1697    -98    127   -268       C  
ATOM   2590  CD AGLU D  87      22.591 -15.376 -52.277  0.50 19.46           C  
ANISOU 2590  CD AGLU D  87     2367   2761   2265    -89     89   -350       C  
ATOM   2591  CD BGLU D  87      21.526 -15.754 -54.635  0.50 24.79           C  
ANISOU 2591  CD BGLU D  87     2995   3553   2869    -84    116   -328       C  
ATOM   2592  OE1AGLU D  87      23.038 -15.314 -53.441  0.50 25.03           O  
ANISOU 2592  OE1AGLU D  87     3028   3538   2944    -99    108   -355       O  
ATOM   2593  OE1BGLU D  87      22.207 -16.664 -54.102  0.50 32.46           O  
ANISOU 2593  OE1BGLU D  87     3961   4508   3863    -68     86   -389       O  
ATOM   2594  OE2AGLU D  87      23.220 -14.940 -51.274  0.50 14.12           O  
ANISOU 2594  OE2AGLU D  87     1702   2046   1616    -95     82   -360       O  
ATOM   2595  OE2BGLU D  87      21.417 -15.629 -55.874  0.50 28.75           O  
ANISOU 2595  OE2BGLU D  87     3460   4136   3328    -87    135   -316       O  
ATOM   2596  N   PHE D  88      17.524 -16.754 -51.120  1.00 10.57           N  
ANISOU 2596  N   PHE D  88     1371   1494   1150    -39     65   -270       N  
ATOM   2597  CA  PHE D  88      16.656 -17.003 -49.987  1.00  9.31           C  
ANISOU 2597  CA  PHE D  88     1254   1272   1010    -30     56   -253       C  
ATOM   2598  C   PHE D  88      16.677 -18.404 -49.477  1.00  9.07           C  
ANISOU 2598  C   PHE D  88     1227   1214   1004     -7     29   -283       C  
ATOM   2599  O   PHE D  88      16.955 -19.336 -50.230  1.00 11.02           O  
ANISOU 2599  O   PHE D  88     1442   1484   1260      4     16   -324       O  
ATOM   2600  CB  PHE D  88      15.184 -16.639 -50.306  1.00  9.24           C  
ANISOU 2600  CB  PHE D  88     1260   1256    993    -35     72   -219       C  
ATOM   2601  CG  PHE D  88      14.695 -17.288 -51.545  1.00  9.47           C  
ANISOU 2601  CG  PHE D  88     1257   1331   1010    -26     72   -240       C  
ATOM   2602  CD1 PHE D  88      14.868 -16.660 -52.756  1.00  9.38           C  
ANISOU 2602  CD1 PHE D  88     1214   1384    964    -33     89   -229       C  
ATOM   2603  CD2 PHE D  88      14.112 -18.548 -51.523  1.00  9.29           C  
ANISOU 2603  CD2 PHE D  88     1229   1290   1011     -9     56   -273       C  
ATOM   2604  CE1 PHE D  88      14.497 -17.252 -53.959  1.00 10.12           C  
ANISOU 2604  CE1 PHE D  88     1268   1541   1034    -20     87   -258       C  
ATOM   2605  CE2 PHE D  88      13.750 -19.138 -52.723  1.00 11.55           C  
ANISOU 2605  CE2 PHE D  88     1473   1626   1287      0     54   -310       C  
ATOM   2606  CZ  PHE D  88      13.955 -18.487 -53.928  1.00 10.52           C  
ANISOU 2606  CZ  PHE D  88     1310   1576   1111     -2     67   -306       C  
ATOM   2607  N   THR D  89      16.387 -18.560 -48.183  1.00  8.69           N  
ANISOU 2607  N   THR D  89     1215   1116    969      0     20   -262       N  
ATOM   2608  CA  THR D  89      16.025 -19.851 -47.626  1.00  9.09           C  
ANISOU 2608  CA  THR D  89     1276   1128   1050     20      2   -266       C  
ATOM   2609  C   THR D  89      14.491 -19.963 -47.732  1.00  8.00           C  
ANISOU 2609  C   THR D  89     1153    967    919     14     18   -242       C  
ATOM   2610  O   THR D  89      13.775 -18.952 -47.766  1.00  8.41           O  
ANISOU 2610  O   THR D  89     1220   1027    949      0     39   -215       O  
ATOM   2611  CB  THR D  89      16.422 -19.958 -46.156  1.00  9.85           C  
ANISOU 2611  CB  THR D  89     1401   1194   1146     34    -11   -246       C  
ATOM   2612  OG1 THR D  89      15.917 -18.813 -45.483  1.00  9.31           O  
ANISOU 2612  OG1 THR D  89     1359   1125   1053     20      5   -215       O  
ATOM   2613  CG2 THR D  89      17.995 -19.930 -46.005  1.00 10.12           C  
ANISOU 2613  CG2 THR D  89     1415   1252   1176     45    -33   -279       C  
ATOM   2614  N   PHE D  90      14.017 -21.203 -47.781  1.00  9.06           N  
ANISOU 2614  N   PHE D  90     1279   1071   1092     27      8   -254       N  
ATOM   2615  CA  PHE D  90      12.578 -21.474 -47.829  1.00  8.61           C  
ANISOU 2615  CA  PHE D  90     1229    988   1052     21     23   -239       C  
ATOM   2616  C   PHE D  90      12.267 -22.826 -47.272  1.00 10.09           C  
ANISOU 2616  C   PHE D  90     1417   1118   1296     34     13   -235       C  
ATOM   2617  O   PHE D  90      13.159 -23.612 -47.020  1.00 10.38           O  
ANISOU 2617  O   PHE D  90     1445   1137   1362     51     -9   -248       O  
ATOM   2618  CB  PHE D  90      12.049 -21.320 -49.285  1.00  9.40           C  
ANISOU 2618  CB  PHE D  90     1293   1133   1143     15     32   -273       C  
ATOM   2619  CG  PHE D  90      12.475 -22.408 -50.253  1.00 11.16           C  
ANISOU 2619  CG  PHE D  90     1466   1374   1397     29     14   -337       C  
ATOM   2620  CD1 PHE D  90      13.692 -22.350 -50.892  1.00 12.60           C  
ANISOU 2620  CD1 PHE D  90     1619   1605   1561     35      2   -372       C  
ATOM   2621  CD2 PHE D  90      11.649 -23.482 -50.510  1.00 12.43           C  
ANISOU 2621  CD2 PHE D  90     1605   1505   1613     36      9   -367       C  
ATOM   2622  CE1 PHE D  90      14.052 -23.298 -51.828  1.00 14.71           C  
ANISOU 2622  CE1 PHE D  90     1834   1900   1856     49    -14   -441       C  
ATOM   2623  CE2 PHE D  90      12.008 -24.449 -51.434  1.00 13.70           C  
ANISOU 2623  CE2 PHE D  90     1710   1683   1809     50     -8   -439       C  
ATOM   2624  CZ  PHE D  90      13.229 -24.369 -52.079  1.00 13.58           C  
ANISOU 2624  CZ  PHE D  90     1665   1724   1769     58    -21   -479       C  
ATOM   2625  N   LYS D  91      10.983 -23.104 -47.114  1.00  9.51           N  
ANISOU 2625  N   LYS D  91     1351   1015   1246     26     29   -217       N  
ATOM   2626  CA  LYS D  91      10.497 -24.415 -46.666  1.00 10.31           C  
ANISOU 2626  CA  LYS D  91     1447   1053   1415     32     26   -208       C  
ATOM   2627  C   LYS D  91       9.185 -24.721 -47.398  1.00 10.86           C  
ANISOU 2627  C   LYS D  91     1492   1114   1518     21     42   -235       C  
ATOM   2628  O   LYS D  91       8.533 -23.809 -47.953  1.00  9.73           O  
ANISOU 2628  O   LYS D  91     1349   1014   1332      9     57   -242       O  
ATOM   2629  CB  LYS D  91      10.245 -24.450 -45.156  1.00 11.98           C  
ANISOU 2629  CB  LYS D  91     1702   1229   1620     33     36   -137       C  
ATOM   2630  CG  LYS D  91       9.135 -23.498 -44.707  1.00 13.27           C  
ANISOU 2630  CG  LYS D  91     1892   1408   1742     14     64   -104       C  
ATOM   2631  CD  LYS D  91       8.900 -23.569 -43.213  1.00 18.52           C  
ANISOU 2631  CD  LYS D  91     2590   2054   2391     17     75    -39       C  
ATOM   2632  CE  LYS D  91       7.730 -22.692 -42.799  1.00 20.14           C  
ANISOU 2632  CE  LYS D  91     2814   2277   2561      0    104    -18       C  
ATOM   2633  NZ  LYS D  91       7.297 -22.923 -41.383  1.00 24.67           N  
ANISOU 2633  NZ  LYS D  91     3413   2841   3120      1    120     43       N  
ATOM   2634  N   LYS D  92       8.830 -25.996 -47.427  1.00 10.64           N  
ANISOU 2634  N   LYS D  92     1440   1030   1572     25     38   -251       N  
ATOM   2635  CA  LYS D  92       7.470 -26.413 -47.819  1.00 11.46           C  
ANISOU 2635  CA  LYS D  92     1519   1110   1721     12     56   -272       C  
ATOM   2636  C   LYS D  92       6.541 -26.192 -46.625  1.00 11.07           C  
ANISOU 2636  C   LYS D  92     1511   1027   1666     -3     84   -199       C  
ATOM   2637  O   LYS D  92       6.873 -26.479 -45.484  1.00 13.46           O  
ANISOU 2637  O   LYS D  92     1844   1294   1974      0     86   -137       O  
ATOM   2638  CB  LYS D  92       7.499 -27.898 -48.227  1.00 13.81           C  
ANISOU 2638  CB  LYS D  92     1769   1350   2126     20     42   -321       C  
ATOM   2639  CG  LYS D  92       6.177 -28.477 -48.760  1.00 21.67           C  
ANISOU 2639  CG  LYS D  92     2724   2319   3188      7     57   -364       C  
ATOM   2640  CD  LYS D  92       6.332 -29.928 -49.240  1.00 29.02           C  
ANISOU 2640  CD  LYS D  92     3595   3189   4239     17     40   -429       C  
ATOM   2641  CE  LYS D  92       5.043 -30.508 -49.808  1.00 38.29           C  
ANISOU 2641  CE  LYS D  92     4719   4339   5488      4     54   -487       C  
ATOM   2642  NZ  LYS D  92       4.082 -30.978 -48.770  1.00 37.89           N  
ANISOU 2642  NZ  LYS D  92     4689   4203   5502    -18     86   -418       N  
ATOM   2643  N   SER D  93       5.395 -25.562 -46.865  1.00 10.14           N  
ANISOU 2643  N   SER D  93     1394    932   1525    -18    106   -204       N  
ATOM   2644  CA  SER D  93       4.388 -25.373 -45.825  1.00 10.26           C  
ANISOU 2644  CA  SER D  93     1438    922   1535    -35    135   -146       C  
ATOM   2645  C   SER D  93       3.010 -25.436 -46.464  1.00 10.27           C  
ANISOU 2645  C   SER D  93     1410    925   1567    -49    153   -185       C  
ATOM   2646  O   SER D  93       2.891 -25.624 -47.669  1.00 10.61           O  
ANISOU 2646  O   SER D  93     1410    991   1628    -43    140   -255       O  
ATOM   2647  CB  SER D  93       4.570 -24.027 -45.138  1.00 10.59           C  
ANISOU 2647  CB  SER D  93     1524   1010   1488    -36    142   -105       C  
ATOM   2648  OG  SER D  93       4.219 -22.982 -46.027  1.00  9.51           O  
ANISOU 2648  OG  SER D  93     1378    925   1308    -38    141   -141       O  
ATOM   2649  N   SER D  94       1.988 -25.136 -45.691  1.00 10.96           N  
ANISOU 2649  N   SER D  94     1516   1001   1645    -66    181   -146       N  
ATOM   2650  CA  SER D  94       0.660 -25.051 -46.266  1.00 11.24           C  
ANISOU 2650  CA  SER D  94     1523   1045   1702    -78    198   -186       C  
ATOM   2651  C   SER D  94       0.527 -23.866 -47.250  1.00 10.99           C  
ANISOU 2651  C   SER D  94     1486   1087   1602    -67    185   -226       C  
ATOM   2652  O   SER D  94      -0.411 -23.838 -48.045  1.00 10.41           O  
ANISOU 2652  O   SER D  94     1377   1034   1542    -68    188   -275       O  
ATOM   2653  CB  SER D  94      -0.392 -25.010 -45.167  1.00 11.09           C  
ANISOU 2653  CB  SER D  94     1522   1001   1688    -99    233   -135       C  
ATOM   2654  OG  SER D  94      -0.202 -23.913 -44.358  1.00 11.30           O  
ANISOU 2654  OG  SER D  94     1592   1065   1633    -97    239    -89       O  
ATOM   2655  N   LYS D  95       1.494 -22.952 -47.256  1.00  9.60           N  
ANISOU 2655  N   LYS D  95     1336    950   1359    -56    171   -207       N  
ATOM   2656  CA  LYS D  95       1.513 -21.888 -48.261  1.00  9.61           C  
ANISOU 2656  CA  LYS D  95     1329   1016   1305    -45    159   -233       C  
ATOM   2657  C   LYS D  95       2.004 -22.335 -49.640  1.00 10.44           C  
ANISOU 2657  C   LYS D  95     1388   1158   1418    -29    137   -294       C  
ATOM   2658  O   LYS D  95       1.891 -21.552 -50.599  1.00 10.60           O  
ANISOU 2658  O   LYS D  95     1393   1242   1392    -18    130   -312       O  
ATOM   2659  CB  LYS D  95       2.315 -20.680 -47.782  1.00  8.98           C  
ANISOU 2659  CB  LYS D  95     1289    960   1163    -42    156   -190       C  
ATOM   2660  CG  LYS D  95       1.906 -20.135 -46.457  1.00  8.70           C  
ANISOU 2660  CG  LYS D  95     1290    903   1110    -53    174   -143       C  
ATOM   2661  CD  LYS D  95       2.550 -18.791 -46.135  1.00  8.85           C  
ANISOU 2661  CD  LYS D  95     1335    948   1076    -50    169   -120       C  
ATOM   2662  CE  LYS D  95       2.231 -18.264 -44.787  1.00  7.94           C  
ANISOU 2662  CE  LYS D  95     1249    823    943    -57    184    -88       C  
ATOM   2663  NZ  LYS D  95       2.644 -19.099 -43.624  1.00  9.47           N  
ANISOU 2663  NZ  LYS D  95     1460    994   1144    -59    189    -57       N  
ATOM   2664  N   GLY D  96       2.587 -23.533 -49.740  1.00 10.58           N  
ANISOU 2664  N   GLY D  96     1383   1144   1492    -26    126   -322       N  
ATOM   2665  CA  GLY D  96       3.327 -23.995 -50.905  1.00 11.91           C  
ANISOU 2665  CA  GLY D  96     1506   1353   1666     -9    102   -385       C  
ATOM   2666  C   GLY D  96       4.792 -23.954 -50.546  1.00 12.36           C  
ANISOU 2666  C   GLY D  96     1585   1405   1704     -3     88   -360       C  
ATOM   2667  O   GLY D  96       5.249 -24.709 -49.649  1.00 15.97           O  
ANISOU 2667  O   GLY D  96     2059   1799   2208     -6     86   -335       O  
ATOM   2668  N   PHE D  97       5.539 -23.122 -51.236  1.00  9.53           N  
ANISOU 2668  N   PHE D  97     1225   1115   1281      5     79   -364       N  
ATOM   2669  CA  PHE D  97       6.920 -22.793 -50.844  1.00 10.14           C  
ANISOU 2669  CA  PHE D  97     1325   1195   1330      7     69   -336       C  
ATOM   2670  C   PHE D  97       6.896 -21.439 -50.214  1.00  9.55           C  
ANISOU 2670  C   PHE D  97     1297   1129   1200     -2     83   -274       C  
ATOM   2671  O   PHE D  97       6.295 -20.490 -50.754  1.00  9.11           O  
ANISOU 2671  O   PHE D  97     1241   1115   1106     -4     93   -265       O  
ATOM   2672  CB  PHE D  97       7.862 -22.849 -52.013  1.00 12.44           C  
ANISOU 2672  CB  PHE D  97     1576   1554   1597     20     52   -386       C  
ATOM   2673  CG  PHE D  97       7.960 -24.195 -52.604  1.00 14.21           C  
ANISOU 2673  CG  PHE D  97     1747   1769   1883     33     34   -461       C  
ATOM   2674  CD1 PHE D  97       8.472 -25.261 -51.859  1.00 17.54           C  
ANISOU 2674  CD1 PHE D  97     2170   2116   2375     36     22   -464       C  
ATOM   2675  CD2 PHE D  97       7.452 -24.422 -53.873  1.00 19.91           C  
ANISOU 2675  CD2 PHE D  97     2410   2555   2598     44     29   -529       C  
ATOM   2676  CE1 PHE D  97       8.532 -26.530 -52.426  1.00 21.85           C  
ANISOU 2676  CE1 PHE D  97     2661   2643   2998     48      5   -540       C  
ATOM   2677  CE2 PHE D  97       7.525 -25.687 -54.437  1.00 24.91           C  
ANISOU 2677  CE2 PHE D  97     2984   3180   3298     57     11   -615       C  
ATOM   2678  CZ  PHE D  97       8.058 -26.736 -53.706  1.00 29.42           C  
ANISOU 2678  CZ  PHE D  97     3557   3666   3953     57      0   -621       C  
ATOM   2679  N   GLU D  98       7.540 -21.364 -49.048  1.00  8.73           N  
ANISOU 2679  N   GLU D  98     1230    988   1097     -6     83   -235       N  
ATOM   2680  CA  GLU D  98       7.466 -20.181 -48.204  1.00  8.39           C  
ANISOU 2680  CA  GLU D  98     1227    943   1015    -15     95   -186       C  
ATOM   2681  C   GLU D  98       8.876 -19.730 -47.829  1.00  7.41           C  
ANISOU 2681  C   GLU D  98     1116    831    867    -12     84   -175       C  
ATOM   2682  O   GLU D  98       9.623 -20.494 -47.223  1.00  7.63           O  
ANISOU 2682  O   GLU D  98     1149    835    915     -4     70   -176       O  
ATOM   2683  CB  GLU D  98       6.682 -20.534 -46.953  1.00  8.19           C  
ANISOU 2683  CB  GLU D  98     1230    870   1011    -21    108   -153       C  
ATOM   2684  CG  GLU D  98       6.617 -19.437 -45.928  1.00  8.32           C  
ANISOU 2684  CG  GLU D  98     1281    889    990    -28    119   -115       C  
ATOM   2685  CD  GLU D  98       5.712 -19.762 -44.766  1.00  8.34           C  
ANISOU 2685  CD  GLU D  98     1304    862   1003    -34    136    -84       C  
ATOM   2686  OE1 GLU D  98       5.187 -20.898 -44.633  1.00 10.18           O  
ANISOU 2686  OE1 GLU D  98     1527   1061   1278    -35    142    -80       O  
ATOM   2687  OE2 GLU D  98       5.487 -18.867 -43.940  1.00  8.32           O  
ANISOU 2687  OE2 GLU D  98     1322    870    969    -38    145    -64       O  
ATOM   2688  N   SER D  99       9.198 -18.504 -48.160  1.00  7.95           N  
ANISOU 2688  N   SER D  99     1187    933    900    -19     90   -165       N  
ATOM   2689  CA  SER D  99      10.513 -18.000 -47.880  1.00  7.41           C  
ANISOU 2689  CA  SER D  99     1123    876    815    -19     82   -162       C  
ATOM   2690  C   SER D  99      10.685 -17.707 -46.377  1.00  7.55           C  
ANISOU 2690  C   SER D  99     1174    864    829    -20     81   -138       C  
ATOM   2691  O   SER D  99       9.753 -17.369 -45.668  1.00  7.95           O  
ANISOU 2691  O   SER D  99     1245    897    877    -24     93   -117       O  
ATOM   2692  CB  SER D  99      10.847 -16.834 -48.741  1.00 11.61           C  
ANISOU 2692  CB  SER D  99     1641   1447   1322    -28     91   -155       C  
ATOM   2693  OG  SER D  99      10.039 -15.723 -48.513  1.00 11.94           O  
ANISOU 2693  OG  SER D  99     1699   1479   1356    -37    107   -125       O  
ATOM   2694  N   LEU D 100      11.916 -17.883 -45.894  1.00  7.89           N  
ANISOU 2694  N   LEU D 100     1217    910    869    -12     65   -147       N  
ATOM   2695  CA  LEU D 100      12.209 -17.710 -44.453  1.00  8.19           C  
ANISOU 2695  CA  LEU D 100     1280    936    896     -5     60   -131       C  
ATOM   2696  C   LEU D 100      13.137 -16.507 -44.233  1.00  7.57           C  
ANISOU 2696  C   LEU D 100     1196    878    800    -12     58   -144       C  
ATOM   2697  O   LEU D 100      12.988 -15.781 -43.247  1.00  8.24           O  
ANISOU 2697  O   LEU D 100     1294    962    873    -13     62   -140       O  
ATOM   2698  CB  LEU D 100      12.833 -19.019 -43.937  1.00  8.92           C  
ANISOU 2698  CB  LEU D 100     1372   1012   1002     15     39   -131       C  
ATOM   2699  CG  LEU D 100      11.874 -20.199 -43.949  1.00 12.02           C  
ANISOU 2699  CG  LEU D 100     1767   1370   1428     19     43   -113       C  
ATOM   2700  CD1 LEU D 100      12.587 -21.519 -43.632  1.00 15.10           C  
ANISOU 2700  CD1 LEU D 100     2151   1735   1850     41     20   -111       C  
ATOM   2701  CD2 LEU D 100      10.692 -19.977 -42.980  1.00 12.59           C  
ANISOU 2701  CD2 LEU D 100     1866   1430   1488     13     64    -74       C  
ATOM   2702  N   ARG D 101      14.137 -16.313 -45.102  1.00  7.61           N  
ANISOU 2702  N   ARG D 101     1176    904    809    -17     54   -167       N  
ATOM   2703  CA  ARG D 101      15.039 -15.153 -45.022  1.00  8.53           C  
ANISOU 2703  CA  ARG D 101     1280   1034    924    -29     57   -180       C  
ATOM   2704  C   ARG D 101      15.469 -14.820 -46.438  1.00  9.16           C  
ANISOU 2704  C   ARG D 101     1331   1138   1008    -44     68   -184       C  
ATOM   2705  O   ARG D 101      15.966 -15.684 -47.161  1.00  9.78           O  
ANISOU 2705  O   ARG D 101     1390   1239   1085    -36     58   -203       O  
ATOM   2706  CB  ARG D 101      16.254 -15.474 -44.205  1.00  9.88           C  
ANISOU 2706  CB  ARG D 101     1447   1215   1091    -14     34   -207       C  
ATOM   2707  CG  ARG D 101      17.133 -14.244 -43.993  1.00 11.28           C  
ANISOU 2707  CG  ARG D 101     1606   1403   1276    -28     39   -230       C  
ATOM   2708  CD  ARG D 101      18.164 -14.468 -42.937  1.00 14.17           C  
ANISOU 2708  CD  ARG D 101     1966   1783   1632     -9     14   -262       C  
ATOM   2709  NE  ARG D 101      18.956 -13.263 -42.702  1.00 16.91           N  
ANISOU 2709  NE  ARG D 101     2288   2137   1996    -24     19   -296       N  
ATOM   2710  CZ  ARG D 101      20.046 -12.940 -43.398  1.00 16.91           C  
ANISOU 2710  CZ  ARG D 101     2256   2151   2016    -39     22   -321       C  
ATOM   2711  NH1 ARG D 101      20.483 -13.716 -44.369  1.00 16.74           N  
ANISOU 2711  NH1 ARG D 101     2223   2145   1991    -38     19   -320       N  
ATOM   2712  NH2 ARG D 101      20.717 -11.827 -43.070  1.00 20.61           N  
ANISOU 2712  NH2 ARG D 101     2699   2618   2512    -55     28   -354       N  
ATOM   2713  N   VAL D 102      15.225 -13.586 -46.845  1.00  7.73           N  
ANISOU 2713  N   VAL D 102     1144    957    835    -63     89   -165       N  
ATOM   2714  CA  VAL D 102      15.409 -13.153 -48.226  1.00  9.08           C  
ANISOU 2714  CA  VAL D 102     1289   1159   1003    -77    106   -149       C  
ATOM   2715  C   VAL D 102      16.415 -12.008 -48.239  1.00  9.50           C  
ANISOU 2715  C   VAL D 102     1322   1211   1077    -97    118   -148       C  
ATOM   2716  O   VAL D 102      16.255 -10.992 -47.535  1.00 10.16           O  
ANISOU 2716  O   VAL D 102     1413   1260   1188   -108    126   -141       O  
ATOM   2717  CB  VAL D 102      14.069 -12.688 -48.853  1.00  8.32           C  
ANISOU 2717  CB  VAL D 102     1199   1058    901    -79    122   -110       C  
ATOM   2718  CG1 VAL D 102      14.284 -12.209 -50.297  1.00  9.77           C  
ANISOU 2718  CG1 VAL D 102     1352   1287   1072    -89    140    -83       C  
ATOM   2719  CG2 VAL D 102      13.012 -13.763 -48.765  1.00  8.12           C  
ANISOU 2719  CG2 VAL D 102     1189   1028    865    -62    112   -118       C  
ATOM   2720  N   THR D 103      17.447 -12.178 -49.055  1.00 10.08           N  
ANISOU 2720  N   THR D 103     1363   1323   1142   -105    122   -159       N  
ATOM   2721  CA  THR D 103      18.464 -11.142 -49.249  1.00 10.44           C  
ANISOU 2721  CA  THR D 103     1381   1371   1213   -129    140   -155       C  
ATOM   2722  C   THR D 103      18.565 -10.849 -50.746  1.00 11.12           C  
ANISOU 2722  C   THR D 103     1437   1505   1282   -143    165   -116       C  
ATOM   2723  O   THR D 103      17.976 -11.522 -51.597  1.00 11.54           O  
ANISOU 2723  O   THR D 103     1487   1599   1298   -129    164   -106       O  
ATOM   2724  CB  THR D 103      19.877 -11.578 -48.730  1.00 12.19           C  
ANISOU 2724  CB  THR D 103     1583   1606   1440   -127    122   -211       C  
ATOM   2725  OG1 THR D 103      20.455 -12.530 -49.615  1.00 13.28           O  
ANISOU 2725  OG1 THR D 103     1697   1797   1551   -119    116   -231       O  
ATOM   2726  CG2 THR D 103      19.814 -12.146 -47.334  1.00 13.10           C  
ANISOU 2726  CG2 THR D 103     1725   1695   1555   -103     92   -246       C  
ATOM   2727  N   GLY D 104      19.394  -9.859 -51.055  1.00 13.50           N  
ANISOU 2727  N   GLY D 104     1709   1807   1611   -170    189    -97       N  
ATOM   2728  CA  GLY D 104      19.817  -9.684 -52.445  1.00 15.64           C  
ANISOU 2728  CA  GLY D 104     1943   2140   1856   -184    216    -61       C  
ATOM   2729  C   GLY D 104      21.007 -10.585 -52.753  1.00 16.58           C  
ANISOU 2729  C   GLY D 104     2031   2317   1951   -181    205   -117       C  
ATOM   2730  O   GLY D 104      21.413 -11.390 -51.916  1.00 14.87           O  
ANISOU 2730  O   GLY D 104     1825   2085   1738   -164    175   -178       O  
ATOM   2731  N   PRO D 105      21.576 -10.443 -53.956  1.00 17.28           N  
ANISOU 2731  N   PRO D 105     2077   2476   2012   -194    231    -93       N  
ATOM   2732  CA  PRO D 105      22.818 -11.154 -54.286  1.00 18.83           C  
ANISOU 2732  CA  PRO D 105     2234   2731   2189   -195    225   -151       C  
ATOM   2733  C   PRO D 105      23.901 -11.019 -53.208  1.00 16.72           C  
ANISOU 2733  C   PRO D 105     1963   2420   1970   -205    212   -205       C  
ATOM   2734  O   PRO D 105      24.093  -9.939 -52.621  1.00 17.60           O  
ANISOU 2734  O   PRO D 105     2077   2475   2133   -229    228   -185       O  
ATOM   2735  CB  PRO D 105      23.280 -10.463 -55.568  1.00 19.60           C  
ANISOU 2735  CB  PRO D 105     2285   2899   2264   -221    268    -97       C  
ATOM   2736  CG  PRO D 105      22.057  -9.847 -56.138  1.00 22.34           C  
ANISOU 2736  CG  PRO D 105     2649   3244   2593   -218    287    -13       C  
ATOM   2737  CD  PRO D 105      21.239  -9.432 -54.972  1.00 19.82           C  
ANISOU 2737  CD  PRO D 105     2381   2824   2326   -213    270     -7       C  
ATOM   2738  N   GLY D 106      24.610 -12.116 -52.952  1.00 18.12           N  
ANISOU 2738  N   GLY D 106     2128   2621   2134   -184    181   -279       N  
ATOM   2739  CA  GLY D 106      25.722 -12.099 -51.997  1.00 18.69           C  
ANISOU 2739  CA  GLY D 106     2190   2668   2243   -186    163   -337       C  
ATOM   2740  C   GLY D 106      25.394 -11.877 -50.537  1.00 17.73           C  
ANISOU 2740  C   GLY D 106     2108   2473   2154   -174    139   -351       C  
ATOM   2741  O   GLY D 106      26.277 -11.535 -49.743  1.00 20.89           O  
ANISOU 2741  O   GLY D 106     2493   2854   2587   -180    130   -394       O  
ATOM   2742  N   GLY D 107      24.119 -11.993 -50.163  1.00 15.73           N  
ANISOU 2742  N   GLY D 107     1900   2182   1892   -158    130   -319       N  
ATOM   2743  CA  GLY D 107      23.708 -11.803 -48.770  1.00 16.38           C  
ANISOU 2743  CA  GLY D 107     2019   2208   1996   -145    109   -331       C  
ATOM   2744  C   GLY D 107      23.525 -10.357 -48.371  1.00 14.34           C  
ANISOU 2744  C   GLY D 107     1758   1904   1783   -172    134   -307       C  
ATOM   2745  O   GLY D 107      23.303 -10.030 -47.188  1.00 15.57           O  
ANISOU 2745  O   GLY D 107     1933   2022   1960   -163    118   -329       O  
ATOM   2746  N   ASN D 108      23.568  -9.485 -49.363  1.00 14.00           N  
ANISOU 2746  N   ASN D 108     1691   1867   1759   -204    172   -259       N  
ATOM   2747  CA  ASN D 108      23.427  -8.072 -49.112  1.00 17.71           C  
ANISOU 2747  CA  ASN D 108     2153   2284   2292   -233    198   -231       C  
ATOM   2748  C   ASN D 108      21.952  -7.740 -48.981  1.00 16.47           C  
ANISOU 2748  C   ASN D 108     2034   2088   2133   -223    200   -183       C  
ATOM   2749  O   ASN D 108      21.074  -8.557 -49.308  1.00 14.24           O  
ANISOU 2749  O   ASN D 108     1781   1828   1801   -200    189   -163       O  
ATOM   2750  CB  ASN D 108      24.029  -7.260 -50.239  1.00 17.16           C  
ANISOU 2750  CB  ASN D 108     2040   2231   2247   -271    242   -184       C  
ATOM   2751  CG  ASN D 108      25.542  -7.425 -50.329  1.00 18.40           C  
ANISOU 2751  CG  ASN D 108     2151   2424   2415   -286    245   -238       C  
ATOM   2752  OD1 ASN D 108      26.037  -8.085 -51.243  1.00 20.90           O  
ANISOU 2752  OD1 ASN D 108     2445   2809   2687   -286    252   -237       O  
ATOM   2753  ND2 ASN D 108      26.266  -6.884 -49.359  1.00 17.57           N  
ANISOU 2753  ND2 ASN D 108     2026   2281   2368   -297    238   -295       N  
ATOM   2754  N   PRO D 109      21.660  -6.580 -48.425  1.00 16.23           N  
ANISOU 2754  N   PRO D 109     2002   1998   2166   -239    212   -175       N  
ATOM   2755  CA  PRO D 109      20.263  -6.222 -48.258  1.00 15.75           C  
ANISOU 2755  CA  PRO D 109     1973   1899   2109   -228    212   -136       C  
ATOM   2756  C   PRO D 109      19.478  -6.133 -49.556  1.00 16.49           C  
ANISOU 2756  C   PRO D 109     2073   2013   2178   -231    235    -53       C  
ATOM   2757  O   PRO D 109      19.994  -5.807 -50.634  1.00 16.69           O  
ANISOU 2757  O   PRO D 109     2068   2066   2204   -251    263     -7       O  
ATOM   2758  CB  PRO D 109      20.315  -4.856 -47.588  1.00 17.09           C  
ANISOU 2758  CB  PRO D 109     2124   2000   2368   -249    224   -148       C  
ATOM   2759  CG  PRO D 109      21.684  -4.743 -46.958  1.00 21.22           C  
ANISOU 2759  CG  PRO D 109     2612   2527   2924   -261    217   -220       C  
ATOM   2760  CD  PRO D 109      22.592  -5.667 -47.713  1.00 18.74           C  
ANISOU 2760  CD  PRO D 109     2284   2277   2556   -261    217   -222       C  
ATOM   2761  N   CYS D 110      18.185  -6.435 -49.445  1.00 13.46           N  
ANISOU 2761  N   CYS D 110     1725   1622   1767   -209    223    -34       N  
ATOM   2762  CA  CYS D 110      17.257  -6.222 -50.526  1.00 14.14           C  
ANISOU 2762  CA  CYS D 110     1814   1723   1832   -205    240     38       C  
ATOM   2763  C   CYS D 110      17.139  -4.725 -50.807  1.00 15.48           C  
ANISOU 2763  C   CYS D 110     1966   1840   2075   -228    268     97       C  
ATOM   2764  O   CYS D 110      17.356  -3.926 -49.915  1.00 17.35           O  
ANISOU 2764  O   CYS D 110     2195   2012   2383   -241    268     68       O  
ATOM   2765  CB  CYS D 110      15.858  -6.775 -50.145  1.00 12.91           C  
ANISOU 2765  CB  CYS D 110     1697   1561   1645   -177    219     33       C  
ATOM   2766  SG  CYS D 110      15.785  -8.522 -49.690  1.00 13.17           S  
ANISOU 2766  SG  CYS D 110     1754   1635   1615   -150    187    -26       S  
ATOM   2767  N   LEU D 111      16.742  -4.383 -52.019  1.00 17.57           N  
ANISOU 2767  N   LEU D 111     2220   2131   2323   -229    291    179       N  
ATOM   2768  CA  LEU D 111      16.610  -2.977 -52.406  1.00 18.17           C  
ANISOU 2768  CA  LEU D 111     2276   2153   2474   -248    320    254       C  
ATOM   2769  C   LEU D 111      15.246  -2.377 -52.091  1.00 18.13           C  
ANISOU 2769  C   LEU D 111     2294   2091   2502   -230    311    280       C  
ATOM   2770  O   LEU D 111      15.161  -1.292 -51.525  1.00 18.38           O  
ANISOU 2770  O   LEU D 111     2316   2040   2628   -244    318    282       O  
ATOM   2771  CB  LEU D 111      16.923  -2.784 -53.904  1.00 22.75           C  
ANISOU 2771  CB  LEU D 111     2827   2797   3019   -257    352    346       C  
ATOM   2772  CG  LEU D 111      18.326  -3.251 -54.338  1.00 35.30           C  
ANISOU 2772  CG  LEU D 111     4383   4448   4578   -279    368    325       C  
ATOM   2773  CD1 LEU D 111      18.564  -2.939 -55.813  1.00 39.60           C  
ANISOU 2773  CD1 LEU D 111     4894   5064   5085   -288    404    424       C  
ATOM   2774  CD2 LEU D 111      19.432  -2.654 -53.470  1.00 35.28           C  
ANISOU 2774  CD2 LEU D 111     4359   4381   4665   -312    376    276       C  
ATOM   2775  N   GLY D 112      14.193  -3.080 -52.483  1.00 17.34           N  
ANISOU 2775  N   GLY D 112     2219   2037   2332   -200    296    292       N  
ATOM   2776  CA  GLY D 112      12.837  -2.622 -52.291  1.00 20.46           C  
ANISOU 2776  CA  GLY D 112     2633   2392   2748   -180    286    313       C  
ATOM   2777  C   GLY D 112      12.444  -1.455 -53.152  1.00 23.35           C  
ANISOU 2777  C   GLY D 112     2981   2730   3161   -181    309    415       C  
ATOM   2778  O   GLY D 112      13.193  -1.080 -54.052  1.00 20.58           O  
ANISOU 2778  O   GLY D 112     2602   2405   2812   -198    336    482       O  
ATOM   2779  N   ASN D 113      11.261  -0.894 -52.886  1.00 24.03           N  
ANISOU 2779  N   ASN D 113     3079   2765   3283   -162    298    430       N  
ATOM   2780  CA  ASN D 113      10.822   0.349 -53.544  1.00 33.72           C  
ANISOU 2780  CA  ASN D 113     4289   3946   4576   -159    315    528       C  
ATOM   2781  C   ASN D 113      10.940   1.543 -52.599  1.00 39.26           C  
ANISOU 2781  C   ASN D 113     4976   4528   5411   -178    319    506       C  
ATOM   2782  O   ASN D 113      12.003   2.179 -52.536  1.00 47.86           O  
ANISOU 2782  O   ASN D 113     6037   5574   6573   -210    341    517       O  
ATOM   2783  CB  ASN D 113       9.389   0.223 -54.056  1.00 43.94           C  
ANISOU 2783  CB  ASN D 113     5599   5270   5825   -119    299    565       C  
ATOM   2784  CG  ASN D 113       9.326  -0.091 -55.540  1.00 44.16           C  
ANISOU 2784  CG  ASN D 113     5613   5397   5765   -101    311    652       C  
ATOM   2785  OD1 ASN D 113       8.774  -1.107 -55.939  1.00 45.87           O  
ANISOU 2785  OD1 ASN D 113     5841   5699   5887    -76    295    625       O  
ATOM   2786  ND2 ASN D 113       9.899   0.785 -56.362  1.00 43.23           N  
ANISOU 2786  ND2 ASN D 113     5467   5274   5681   -114    341    756       N  
TER    2787      ASN D 113                                                      
ATOM   2788  O5'   U E   1       4.745  -5.449 -33.696  1.00 13.04           O  
ANISOU 2788  O5'   U E   1     1895   1583   1473   -136     47     69       O  
ATOM   2789  C5'   U E   1       5.792  -4.574 -34.006  1.00 13.00           C  
ANISOU 2789  C5'   U E   1     1880   1571   1488   -136     40     82       C  
ATOM   2790  C4'   U E   1       7.033  -5.348 -34.387  1.00 10.72           C  
ANISOU 2790  C4'   U E   1     1583   1280   1210   -134     47     98       C  
ATOM   2791  O4'   U E   1       7.500  -6.144 -33.275  1.00  9.86           O  
ANISOU 2791  O4'   U E   1     1477   1168   1099   -137     41     97       O  
ATOM   2792  C3'   U E   1       6.878  -6.365 -35.498  1.00  9.99           C  
ANISOU 2792  C3'   U E   1     1492   1193   1109   -129     67    101       C  
ATOM   2793  O3'   U E   1       6.861  -5.747 -36.771  1.00 10.39           O  
ANISOU 2793  O3'   U E   1     1537   1245   1165   -124     75    108       O  
ATOM   2794  C2'   U E   1       8.097  -7.232 -35.284  1.00 10.46           C  
ANISOU 2794  C2'   U E   1     1547   1250   1178   -127     69    114       C  
ATOM   2795  O2'   U E   1       9.254  -6.573 -35.785  1.00 13.50           O  
ANISOU 2795  O2'   U E   1     1917   1629   1582   -125     68    133       O  
ATOM   2796  C1'   U E   1       8.133  -7.311 -33.766  1.00  9.50           C  
ANISOU 2796  C1'   U E   1     1429   1125   1054   -133     54    106       C  
ATOM   2797  N1    U E   1       7.452  -8.501 -33.235  1.00  8.18           N  
ANISOU 2797  N1    U E   1     1274    964    870   -134     60     95       N  
ATOM   2798  C2    U E   1       8.186  -9.664 -33.220  1.00  8.72           C  
ANISOU 2798  C2    U E   1     1341   1031    938   -131     68    103       C  
ATOM   2799  O2    U E   1       9.328  -9.724 -33.637  1.00 10.05           O  
ANISOU 2799  O2    U E   1     1501   1196   1121   -128     71    119       O  
ATOM   2800  N3    U E   1       7.551 -10.740 -32.660  1.00  7.77           N  
ANISOU 2800  N3    U E   1     1231    916    802   -133     71     93       N  
ATOM   2801  C4    U E   1       6.242 -10.792 -32.205  1.00  8.63           C  
ANISOU 2801  C4    U E   1     1351   1031    897   -135     69     77       C  
ATOM   2802  O4    U E   1       5.796 -11.837 -31.743  1.00  8.04           O  
ANISOU 2802  O4    U E   1     1284    960    810   -136     73     71       O  
ATOM   2803  C5    U E   1       5.546  -9.547 -32.263  1.00  8.95           C  
ANISOU 2803  C5    U E   1     1390   1071    937   -136     63     71       C  
ATOM   2804  C6    U E   1       6.160  -8.467 -32.758  1.00  9.24           C  
ANISOU 2804  C6    U E   1     1419   1103    989   -136     58     79       C  
ATOM   2805  P     U E   2       5.993  -6.414 -37.945  1.00 12.41           P  
ANISOU 2805  P     U E   2     1801   1507   1405   -119     92    103       P  
ATOM   2806  OP1   U E   2       4.575  -6.505 -37.534  1.00 13.17           O  
ANISOU 2806  OP1   U E   2     1908   1609   1485   -123     89     85       O  
ATOM   2807  OP2   U E   2       6.664  -7.645 -38.455  1.00 14.87           O  
ANISOU 2807  OP2   U E   2     2114   1819   1714   -113    105    112       O  
ATOM   2808  O5'   U E   2       6.180  -5.283 -39.048  1.00 12.25           O  
ANISOU 2808  O5'   U E   2     1771   1485   1395   -115     94    112       O  
ATOM   2809  C5'   U E   2       5.391  -4.085 -38.943  1.00 12.87           C  
ANISOU 2809  C5'   U E   2     1850   1564   1474   -119     85    102       C  
ATOM   2810  C4'   U E   2       6.050  -3.037 -39.774  1.00 12.85           C  
ANISOU 2810  C4'   U E   2     1836   1558   1488   -116     85    116       C  
ATOM   2811  O4'   U E   2       6.109  -3.529 -41.133  1.00 12.64           O  
ANISOU 2811  O4'   U E   2     1809   1534   1457   -108    103    123       O  
ATOM   2812  C3'   U E   2       5.316  -1.698 -39.842  1.00 15.09           C  
ANISOU 2812  C3'   U E   2     2118   1840   1773   -120     76    108       C  
ATOM   2813  O3'   U E   2       6.275  -0.679 -39.603  1.00 16.54           O  
ANISOU 2813  O3'   U E   2     2290   2017   1977   -122     63    120       O  
ATOM   2814  C2'   U E   2       4.858  -1.621 -41.297  1.00 15.80           C  
ANISOU 2814  C2'   U E   2     2208   1935   1858   -113     91    110       C  
ATOM   2815  O2'   U E   2       4.707  -0.321 -41.814  1.00 21.69           O  
ANISOU 2815  O2'   U E   2     2948   2679   2612   -114     86    112       O  
ATOM   2816  C1'   U E   2       5.960  -2.417 -41.984  1.00 12.48           C  
ANISOU 2816  C1'   U E   2     1782   1513   1444   -106    103    127       C  
ATOM   2817  N1    U E   2       5.679  -2.909 -43.328  1.00 11.58           N  
ANISOU 2817  N1    U E   2     1674   1404   1321    -97    121    130       N  
ATOM   2818  C2    U E   2       6.768  -3.144 -44.131  1.00 11.19           C  
ANISOU 2818  C2    U E   2     1617   1352   1281    -87    132    149       C  
ATOM   2819  O2    U E   2       7.908  -2.920 -43.768  1.00 12.70           O  
ANISOU 2819  O2    U E   2     1796   1540   1489    -87    127    164       O  
ATOM   2820  N3    U E   2       6.469  -3.639 -45.378  1.00 10.94           N  
ANISOU 2820  N3    U E   2     1593   1323   1238    -77    148    151       N  
ATOM   2821  C4    U E   2       5.212  -3.910 -45.882  1.00 10.70           C  
ANISOU 2821  C4    U E   2     1577   1297   1190    -77    151    135       C  
ATOM   2822  O4    U E   2       5.098  -4.320 -47.031  1.00 11.20           O  
ANISOU 2822  O4    U E   2     1648   1362   1245    -66    164    139       O  
ATOM   2823  C5    U E   2       4.134  -3.630 -44.982  1.00 11.61           C  
ANISOU 2823  C5    U E   2     1698   1415   1299    -88    139    117       C  
ATOM   2824  C6    U E   2       4.403  -3.190 -43.749  1.00 12.77           C  
ANISOU 2824  C6    U E   2     1837   1559   1454    -97    125    115       C  
ATOM   2825  P     U E   3       6.324  -0.049 -38.113  1.00 19.92           P  
ANISOU 2825  P     U E   3     2720   2438   2410   -130     41    113       P  
ATOM   2826  OP1   U E   3       7.296   1.062 -38.217  1.00 24.80           O  
ANISOU 2826  OP1   U E   3     3324   3047   3050   -132     28    128       O  
ATOM   2827  OP2   U E   3       6.453  -1.129 -37.105  1.00 25.22           O  
ANISOU 2827  OP2   U E   3     3398   3110   3073   -132     40    108       O  
ATOM   2828  O5'   U E   3       4.886   0.562 -38.428  1.00 37.22           O  
ANISOU 2828  O5'   U E   3     4919   4634   4586   -130     43     97       O  
ATOM   2829  C5'   U E   3       3.930   0.807 -37.442  1.00 36.19           C  
ANISOU 2829  C5'   U E   3     4800   4506   4444   -132     33     80       C  
ATOM   2830  C4'   U E   3       3.676   2.293 -37.301  1.00 25.58           C  
ANISOU 2830  C4'   U E   3     3456   3157   3106   -134     19     77       C  
ATOM   2831  O4'   U E   3       2.596   2.346 -36.337  1.00 25.11           O  
ANISOU 2831  O4'   U E   3     3409   3101   3030   -134     13     60       O  
ATOM   2832  C3'   U E   3       4.799   3.063 -36.609  1.00 21.26           C  
ANISOU 2832  C3'   U E   3     2901   2597   2577   -138      0     86       C  
ATOM   2833  O3'   U E   3       4.591   4.481 -36.399  1.00 16.77           O  
ANISOU 2833  O3'   U E   3     2334   2022   2014   -139    -17     83       O  
ATOM   2834  C2'   U E   3       4.675   2.454 -35.225  1.00 22.50           C  
ANISOU 2834  C2'   U E   3     3069   2753   2724   -139     -9     77       C  
ATOM   2835  O2'   U E   3       5.354   3.099 -34.173  1.00 20.59           O  
ANISOU 2835  O2'   U E   3     2830   2500   2493   -142    -31     79       O  
ATOM   2836  C1'   U E   3       3.157   2.540 -35.042  1.00 24.74           C  
ANISOU 2836  C1'   U E   3     3366   3045   2987   -136     -4     59       C  
ATOM   2837  N1    U E   3       2.630   1.522 -34.129  1.00 24.99           N  
ANISOU 2837  N1    U E   3     3408   3082   3002   -135      0     49       N  
ATOM   2838  N3    U E   3       1.598   1.001 -32.160  1.00 30.34           N  
ANISOU 2838  N3    U E   3     4107   3765   3657   -132     -8     30       N  
ATOM   2839  C4    U E   3       1.680  -0.366 -32.355  1.00 25.97           C  
ANISOU 2839  C4    U E   3     3551   3217   3098   -133      5     33       C  
ATOM   2840  O4    U E   3       1.210  -1.128 -31.514  1.00 29.89           O  
ANISOU 2840  O4    U E   3     4055   3718   3582   -132      7     26       O  
ATOM   2841  C5    U E   3       2.306  -0.754 -33.575  1.00 31.31           C  
ANISOU 2841  C5    U E   3     4216   3893   3784   -135     16     44       C  
ATOM   2842  C6    U E   3       2.761   0.185 -34.398  1.00 25.70           C  
ANISOU 2842  C6    U E   3     3496   3178   3087   -135     13     52       C  
ATOM   2843  P     U E   4       5.385   5.686 -37.087  1.00 15.07           P  
ANISOU 2843  P     U E   4     2106   1798   1822   -141    -26     98       P  
ATOM   2844  OP1   U E   4       4.516   6.900 -36.956  1.00 13.85           O  
ANISOU 2844  OP1   U E   4     1959   1642   1662   -141    -37     86       O  
ATOM   2845  OP2   U E   4       5.789   5.232 -38.442  1.00 18.28           O  
ANISOU 2845  OP2   U E   4     2499   2210   2234   -138     -7    112       O  
ATOM   2846  O5'   U E   4       6.638   6.009 -36.164  1.00 17.86           O  
ANISOU 2846  O5'   U E   4     2453   2137   2193   -146    -49    109       O  
ATOM   2847  C5'   U E   4       7.738   5.093 -36.094  1.00 19.89           C  
ANISOU 2847  C5'   U E   4     2701   2392   2461   -148    -45    124       C  
ATOM   2848  C4'   U E   4       9.018   5.871 -35.946  1.00 18.84           C  
ANISOU 2848  C4'   U E   4     2555   2246   2355   -153    -64    143       C  
ATOM   2849  O4'   U E   4       9.256   6.656 -37.141  1.00 16.08           O  
ANISOU 2849  O4'   U E   4     2192   1897   2020   -152    -59    157       O  
ATOM   2850  C3'   U E   4       9.019   6.899 -34.836  1.00 16.26           C  
ANISOU 2850  C3'   U E   4     2238   1907   2033   -158    -94    136       C  
ATOM   2851  O3'   U E   4       9.299   6.288 -33.586  1.00 20.09           O  
ANISOU 2851  O3'   U E   4     2733   2387   2513   -159   -105    131       O  
ATOM   2852  C2'   U E   4      10.150   7.809 -35.267  1.00 17.14           C  
ANISOU 2852  C2'   U E   4     2332   2006   2173   -163   -108    159       C  
ATOM   2853  O2'   U E   4      11.441   7.236 -35.054  1.00 18.56           O  
ANISOU 2853  O2'   U E   4     2499   2181   2371   -166   -112    179       O  
ATOM   2854  C1'   U E   4       9.916   7.846 -36.775  1.00 14.88           C  
ANISOU 2854  C1'   U E   4     2034   1731   1888   -158    -85    167       C  
ATOM   2855  N1    U E   4       9.108   8.976 -37.254  1.00 13.10           N  
ANISOU 2855  N1    U E   4     1812   1505   1659   -157    -88    158       N  
ATOM   2856  C2    U E   4       9.766  10.175 -37.366  1.00 15.10           C  
ANISOU 2856  C2    U E   4     2055   1745   1934   -162   -108    172       C  
ATOM   2857  O2    U E   4      10.933  10.311 -37.060  1.00 13.61           O  
ANISOU 2857  O2    U E   4     1855   1546   1768   -168   -123    191       O  
ATOM   2858  N3    U E   4       9.014  11.196 -37.886  1.00 11.43           N  
ANISOU 2858  N3    U E   4     1594   1281   1466   -161   -110    164       N  
ATOM   2859  C4    U E   4       7.673  11.156 -38.221  1.00 11.76           C  
ANISOU 2859  C4    U E   4     1647   1334   1484   -156    -96    144       C  
ATOM   2860  O4    U E   4       7.138  12.160 -38.688  1.00 10.08           O  
ANISOU 2860  O4    U E   4     1436   1121   1272   -155   -100    140       O  
ATOM   2861  C5    U E   4       7.059   9.875 -38.071  1.00 12.80           C  
ANISOU 2861  C5    U E   4     1789   1479   1595   -151    -76    132       C  
ATOM   2862  C6    U E   4       7.779   8.851 -37.595  1.00 14.97           C  
ANISOU 2862  C6    U E   4     2061   1753   1872   -152    -73    139       C  
ATOM   2863  P     U E   5       8.721   6.888 -32.273  1.00 19.68           P  
ANISOU 2863  P     U E   5     2701   2327   2449   -159   -127    113       P  
ATOM   2864  OP1   U E   5       9.070   8.327 -32.108  1.00 29.06           O  
ANISOU 2864  OP1   U E   5     3888   3499   3652   -163   -154    118       O  
ATOM   2865  OP2   U E   5       9.055   5.937 -31.144  1.00 21.67           O  
ANISOU 2865  OP2   U E   5     2961   2576   2694   -160   -132    109       O  
ATOM   2866  O5'   U E   5       7.144   6.805 -32.489  1.00 20.66           O  
ANISOU 2866  O5'   U E   5     2838   2464   2545   -153   -111     92       O  
ATOM   2867  C5'   U E   5       6.519   5.514 -32.514  1.00 22.29           C  
ANISOU 2867  C5'   U E   5     3049   2684   2734   -149    -88     83       C  
ATOM   2868  C4'   U E   5       5.436   5.517 -31.473  1.00 18.40           C  
ANISOU 2868  C4'   U E   5     2577   2195   2219   -144    -93     63       C  
ATOM   2869  O4'   U E   5       4.487   6.548 -31.829  1.00 24.80           O  
ANISOU 2869  O4'   U E   5     3393   3007   3022   -141    -94     54       O  
ATOM   2870  C3'   U E   5       4.602   4.252 -31.312  1.00 21.31           C  
ANISOU 2870  C3'   U E   5     2952   2578   2567   -140    -73     53       C  
ATOM   2871  O3'   U E   5       5.267   3.315 -30.462  1.00 20.35           O  
ANISOU 2871  O3'   U E   5     2832   2453   2445   -142    -76     56       O  
ATOM   2872  C2'   U E   5       3.320   4.807 -30.701  1.00 22.69           C  
ANISOU 2872  C2'   U E   5     3143   2756   2721   -134    -76     35       C  
ATOM   2873  O2'   U E   5       3.471   4.988 -29.295  1.00 27.37           O  
ANISOU 2873  O2'   U E   5     3750   3339   3309   -132    -95     29       O  
ATOM   2874  C1'   U E   5       3.180   6.142 -31.441  1.00 20.99           C  
ANISOU 2874  C1'   U E   5     2924   2535   2515   -134    -83     37       C  
ATOM   2875  N1    U E   5       2.315   6.123 -32.630  1.00 19.40           N  
ANISOU 2875  N1    U E   5     2716   2346   2307   -133    -63     35       N  
ATOM   2876  C2    U E   5       0.947   6.163 -32.417  1.00 22.94           C  
ANISOU 2876  C2    U E   5     3176   2803   2734   -127    -55     21       C  
ATOM   2877  O2    U E   5       0.450   6.173 -31.302  1.00 27.55           O  
ANISOU 2877  O2    U E   5     3774   3387   3305   -122    -63     11       O  
ATOM   2878  N3    U E   5       0.185   6.181 -33.558  1.00 21.93           N  
ANISOU 2878  N3    U E   5     3042   2685   2602   -126    -38     20       N  
ATOM   2879  C4    U E   5       0.634   6.191 -34.863  1.00 22.62           C  
ANISOU 2879  C4    U E   5     3116   2775   2703   -130    -29     31       C  
ATOM   2880  O4    U E   5      -0.181   6.207 -35.784  1.00 20.68           O  
ANISOU 2880  O4    U E   5     2868   2538   2451   -128    -15     28       O  
ATOM   2881  C5    U E   5       2.059   6.183 -35.001  1.00 22.48           C  
ANISOU 2881  C5    U E   5     3087   2747   2706   -134    -36     46       C  
ATOM   2882  C6    U E   5       2.832   6.160 -33.906  1.00 22.62           C  
ANISOU 2882  C6    U E   5     3109   2755   2729   -136    -53     48       C  
ATOM   2883  P     U E   6       5.213   1.737 -30.655  1.00 24.05           P  
ANISOU 2883  P     U E   6     3298   2932   2905   -142    -55     57       P  
ATOM   2884  OP1   U E   6       5.061   1.470 -32.130  1.00 22.74           O  
ANISOU 2884  OP1   U E   6     3121   2775   2743   -141    -34     64       O  
ATOM   2885  OP2   U E   6       4.267   1.122 -29.675  1.00 25.31           O  
ANISOU 2885  OP2   U E   6     3473   3099   3044   -137    -52     42       O  
ATOM   2886  O5'   U E   6       6.689   1.294 -30.229  1.00 30.90           O  
ANISOU 2886  O5'   U E   6     4158   3791   3791   -146    -64     71       O  
ATOM   2887  C5'   U E   6       7.847   1.702 -30.991  1.00 26.65           C  
ANISOU 2887  C5'   U E   6     3603   3245   3277   -150    -68     90       C  
ATOM   2888  C4'   U E   6       9.096   1.621 -30.143  1.00 28.75           C  
ANISOU 2888  C4'   U E   6     3865   3499   3558   -155    -87    101       C  
ATOM   2889  O4'   U E   6       8.971   2.547 -29.034  1.00 27.06           O  
ANISOU 2889  O4'   U E   6     3664   3273   3342   -156   -112     92       O  
ATOM   2890  C3'   U E   6       9.398   0.251 -29.539  1.00 29.03           C  
ANISOU 2890  C3'   U E   6     3904   3538   3587   -155    -79    101       C  
ATOM   2891  O3'   U E   6      10.783  -0.071 -29.551  1.00 39.04           O  
ANISOU 2891  O3'   U E   6     5158   4799   4876   -159    -84    120       O  
ATOM   2892  C2'   U E   6       8.942   0.399 -28.095  1.00 28.96           C  
ANISOU 2892  C2'   U E   6     3914   3525   3565   -154    -96     86       C  
ATOM   2893  O2'   U E   6       9.618  -0.506 -27.234  1.00 30.71           O  
ANISOU 2893  O2'   U E   6     4137   3743   3788   -155   -100     89       O  
ATOM   2894  C1'   U E   6       9.233   1.881 -27.836  1.00 24.65           C  
ANISOU 2894  C1'   U E   6     3369   2964   3031   -156   -121     88       C  
ATOM   2895  N1    U E   6       8.351   2.454 -26.813  1.00 17.41           N  
ANISOU 2895  N1    U E   6     2472   2043   2096   -151   -135     69       N  
ATOM   2896  C2    U E   6       8.905   2.715 -25.583  1.00 14.23           C  
ANISOU 2896  C2    U E   6     2081   1627   1697   -152   -159     68       C  
ATOM   2897  O2    U E   6      10.086   2.556 -25.351  1.00 13.54           O  
ANISOU 2897  O2    U E   6     1986   1530   1628   -158   -172     82       O  
ATOM   2898  N3    U E   6       8.026   3.192 -24.647  1.00 13.13           N  
ANISOU 2898  N3    U E   6     1963   1487   1539   -145   -170     51       N  
ATOM   2899  C4    U E   6       6.671   3.393 -24.802  1.00 16.07           C  
ANISOU 2899  C4    U E   6     2345   1869   1890   -137   -157     36       C  
ATOM   2900  O4    U E   6       6.002   3.794 -23.851  1.00 13.75           O  
ANISOU 2900  O4    U E   6     2070   1572   1579   -129   -167     23       O  
ATOM   2901  C5    U E   6       6.171   3.084 -26.105  1.00 15.11           C  
ANISOU 2901  C5    U E   6     2209   1762   1768   -138   -132     39       C  
ATOM   2902  C6    U E   6       7.006   2.628 -27.040  1.00 18.65           C  
ANISOU 2902  C6    U E   6     2638   2211   2233   -145   -122     55       C  
TER    2903        U E   6                                                      
HETATM 2904  C1  GOL B1115      51.979 -17.097 -24.485  1.00 36.21           C  
HETATM 2905  O1  GOL B1115      51.083 -17.969 -23.730  1.00 31.33           O  
HETATM 2906  C2  GOL B1115      53.462 -17.446 -24.417  1.00 21.15           C  
HETATM 2907  O2  GOL B1115      53.483 -18.591 -23.595  1.00 23.18           O  
HETATM 2908  C3  GOL B1115      54.288 -16.274 -23.844  1.00 20.56           C  
HETATM 2909  O3  GOL B1115      55.554 -16.662 -23.211  1.00 14.90           O  
HETATM 2910  C1  GOL D1114      -2.629 -10.096 -53.706  1.00 29.80           C  
HETATM 2911  O1  GOL D1114      -2.473 -10.384 -55.109  1.00 32.49           O  
HETATM 2912  C2  GOL D1114      -3.818  -9.187 -53.439  1.00 27.48           C  
HETATM 2913  O2  GOL D1114      -5.036  -9.790 -53.884  1.00 28.32           O  
HETATM 2914  C3  GOL D1114      -3.926  -8.904 -51.946  1.00 27.00           C  
HETATM 2915  O3  GOL D1114      -4.894  -7.874 -51.732  1.00 29.88           O  
HETATM 2916  O   HOH A2001      24.016  -3.926  -4.860  1.00 34.95           O  
HETATM 2917  O   HOH A2002      25.764  -2.221  -5.794  1.00 40.40           O  
HETATM 2918  O   HOH A2003      23.975  -6.783  -4.188  1.00 33.12           O  
HETATM 2919  O   HOH A2004      18.682  -7.102  -9.363  1.00 24.43           O  
HETATM 2920  O   HOH A2005      21.927  -6.463 -11.475  1.00 26.18           O  
HETATM 2921  O   HOH A2006      24.320 -10.723  -6.571  1.00 21.88           O  
HETATM 2922  O   HOH A2007      18.176 -10.722  -8.643  1.00 22.11           O  
HETATM 2923  O   HOH A2008      21.354 -13.329  -8.010  1.00 24.79           O  
HETATM 2924  O   HOH A2009      27.179 -13.527 -12.339  1.00 15.65           O  
HETATM 2925  O   HOH A2010      27.581  -8.128  -8.558  1.00 22.60           O  
HETATM 2926  O   HOH A2011      22.883  -8.586 -13.138  1.00 12.28           O  
HETATM 2927  O   HOH A2012      22.031 -14.771 -10.248  1.00 18.57           O  
HETATM 2928  O   HOH A2013      23.337 -13.293 -13.517  1.00 18.06           O  
HETATM 2929  O   HOH A2014      16.563 -10.767 -11.062  1.00 14.52           O  
HETATM 2930  O   HOH A2015      24.073 -17.432 -11.146  1.00 24.83           O  
HETATM 2931  O   HOH A2016      24.262 -23.872 -15.140  1.00 22.72           O  
HETATM 2932  O   HOH A2017      21.678 -20.825 -16.762  1.00 31.15           O  
HETATM 2933  O   HOH A2018      25.880 -23.278 -12.050  1.00 26.01           O  
HETATM 2934  O   HOH A2019      27.976 -21.892 -12.461  1.00 21.91           O  
HETATM 2935  O   HOH A2020      25.389 -19.521 -10.101  1.00 21.73           O  
HETATM 2936  O   HOH A2021      20.459 -18.923 -18.010  1.00 12.12           O  
HETATM 2937  O   HOH A2022      17.480 -26.623 -19.057  1.00 27.77           O  
HETATM 2938  O   HOH A2023      16.181 -26.439 -21.360  1.00 22.76           O  
HETATM 2939  O   HOH A2024      12.752 -27.756 -19.940  1.00 13.41           O  
HETATM 2940  O   HOH A2025       5.285 -26.699 -20.651  1.00 26.24           O  
HETATM 2941  O   HOH A2026      16.638  -7.999 -11.388  1.00 21.52           O  
HETATM 2942  O   HOH A2027      19.897  -5.050 -12.604  1.00 33.07           O  
HETATM 2943  O   HOH A2028      28.394 -22.448  -8.922  1.00 27.10           O  
HETATM 2944  O   HOH A2029      29.916 -24.156 -10.924  1.00 34.98           O  
HETATM 2945  O   HOH A2030       3.906 -26.454 -24.402  1.00 21.91           O  
HETATM 2946  O   HOH A2031      -0.481 -24.951 -17.016  1.00 26.39           O  
HETATM 2947  O   HOH A2032       3.865 -26.201 -18.388  1.00 31.68           O  
HETATM 2948  O   HOH A2033       2.178 -21.282 -28.650  1.00 11.53           O  
HETATM 2949  O   HOH A2034      -0.159 -19.547 -28.419  1.00 16.17           O  
HETATM 2950  O   HOH A2035       2.883 -21.503 -31.253  1.00 23.80           O  
HETATM 2951  O   HOH A2036       4.760 -19.458 -31.540  1.00 13.04           O  
HETATM 2952  O   HOH A2037       0.594 -21.885 -32.329  1.00 30.91           O  
HETATM 2953  O   HOH A2038      -0.904 -15.796 -33.696  1.00 16.63           O  
HETATM 2954  O   HOH A2039      -3.668 -15.559 -32.290  1.00 26.78           O  
HETATM 2955  O   HOH A2040      -5.569 -16.612 -29.454  1.00 29.58           O  
HETATM 2956  O   HOH A2041      -3.600 -18.058 -28.569  1.00 27.37           O  
HETATM 2957  O   HOH A2042      -0.832 -19.167 -30.999  1.00 22.99           O  
HETATM 2958  O   HOH A2043      -4.760 -11.902 -29.917  1.00 29.74           O  
HETATM 2959  O   HOH A2044       1.293 -18.991 -34.758  1.00 28.96           O  
HETATM 2960  O   HOH A2045       1.001 -17.619 -32.648  1.00 16.86           O  
HETATM 2961  O   HOH A2046      -6.785  -9.924 -31.610  1.00 25.19           O  
HETATM 2962  O   HOH A2047       8.465 -30.349 -17.282  1.00 22.68           O  
HETATM 2963  O   HOH A2048      -0.426  -7.572 -27.969  1.00 15.15           O  
HETATM 2964  O   HOH A2049       3.205  -7.263 -27.318  1.00 15.83           O  
HETATM 2965  O   HOH A2050      13.058 -16.691  -7.306  1.00 18.34           O  
HETATM 2966  O   HOH A2051       6.708 -19.510  -8.027  1.00 20.10           O  
HETATM 2967  O   HOH A2052      10.769 -18.112  -5.827  1.00 22.68           O  
HETATM 2968  O   HOH A2053      13.235 -18.347  -2.059  1.00 44.28           O  
HETATM 2969  O   HOH A2054      17.442 -24.314  -3.789  1.00 25.61           O  
HETATM 2970  O   HOH A2055      19.566 -19.076  -5.448  1.00 38.84           O  
HETATM 2971  O   HOH A2056      11.695 -16.246  -2.332  1.00 38.47           O  
HETATM 2972  O   HOH A2057      12.706 -14.311  -6.456  1.00 29.70           O  
HETATM 2973  O   HOH A2058      22.953 -29.814 -10.943  1.00 44.06           O  
HETATM 2974  O   HOH A2059       5.232 -21.363  -9.502  1.00 27.34           O  
HETATM 2975  O   HOH A2060       2.832 -21.339  -7.731  1.00 32.70           O  
HETATM 2976  O   HOH A2061       4.816 -17.254 -10.143  1.00 30.16           O  
HETATM 2977  O   HOH A2062       1.620 -17.638 -14.761  1.00 25.78           O  
HETATM 2978  O   HOH A2063       6.159 -24.144 -15.412  1.00 21.61           O  
HETATM 2979  O   HOH A2064       7.340 -28.121 -17.492  1.00 19.86           O  
HETATM 2980  O   HOH A2065      11.387  -3.877 -29.136  1.00 29.74           O  
HETATM 2981  O   HOH A2066      16.245  -6.954 -30.563  1.00 38.09           O  
HETATM 2982  O   HOH A2067       7.195  -6.901 -21.063  1.00 19.21           O  
HETATM 2983  O   HOH A2068      14.180 -29.991 -14.227  1.00 25.08           O  
HETATM 2984  O   HOH A2069      16.015 -28.016 -17.104  1.00 23.55           O  
HETATM 2985  O   HOH A2070      21.374 -15.166 -36.092  1.00 25.57           O  
HETATM 2986  O   HOH A2071      24.288 -18.535 -34.646  1.00 34.70           O  
HETATM 2987  O   HOH A2072      25.288 -10.960 -28.142  1.00 17.11           O  
HETATM 2988  O   HOH A2073      20.980  -8.671 -28.898  1.00 26.21           O  
HETATM 2989  O   HOH A2074      16.459  -7.223 -35.057  1.00 29.34           O  
HETATM 2990  O   HOH A2075      20.076 -27.564 -14.381  1.00 25.29           O  
HETATM 2991  O   HOH A2076      19.783 -22.563 -14.538  1.00 13.29           O  
HETATM 2992  O   HOH A2077      17.319 -29.245 -15.230  1.00 32.54           O  
HETATM 2993  O   HOH A2078      15.337 -15.251 -39.671  1.00 24.72           O  
HETATM 2994  O   HOH A2079      21.912 -17.857 -36.293  1.00 24.77           O  
HETATM 2995  O   HOH A2080      17.586 -22.455  -7.675  1.00 21.62           O  
HETATM 2996  O   HOH A2081      10.369 -21.973  -6.946  1.00 13.33           O  
HETATM 2997  O   HOH A2082      11.958 -18.405  -9.300  1.00 13.84           O  
HETATM 2998  O   HOH A2083       9.475 -19.553  -7.842  1.00 14.66           O  
HETATM 2999  O   HOH A2084      12.330 -19.905  -4.263  1.00 19.20           O  
HETATM 3000  O   HOH A2085      16.300 -24.154  -6.315  1.00 15.92           O  
HETATM 3001  O   HOH A2086       4.305 -16.824 -37.491  1.00 24.63           O  
HETATM 3002  O   HOH A2087      11.940 -26.850 -30.654  1.00 33.31           O  
HETATM 3003  O   HOH A2088      15.521 -17.468  -6.513  1.00 23.51           O  
HETATM 3004  O   HOH A2089      21.836 -23.080  -7.457  1.00 35.93           O  
HETATM 3005  O   HOH A2090      22.107 -19.041  -6.597  1.00 29.00           O  
HETATM 3006  O   HOH A2091      16.378 -25.289 -29.989  1.00 25.49           O  
HETATM 3007  O   HOH A2092      14.624 -27.050 -30.898  1.00 35.33           O  
HETATM 3008  O   HOH A2093      22.034 -29.019 -13.572  1.00 34.43           O  
HETATM 3009  O   HOH A2094      22.990 -27.595  -8.813  1.00 42.67           O  
HETATM 3010  O   HOH A2095      14.472  -6.357 -10.189  1.00 34.30           O  
HETATM 3011  O   HOH A2096      14.082 -11.905  -6.619  1.00 21.77           O  
HETATM 3012  O   HOH A2097      16.235  -6.394 -13.529  1.00 28.13           O  
HETATM 3013  O   HOH A2098      18.387 -29.300  -7.842  1.00 22.10           O  
HETATM 3014  O   HOH A2099      -0.549 -12.794  -8.242  1.00 27.16           O  
HETATM 3015  O   HOH A2100      10.054 -13.948  -5.548  1.00 35.29           O  
HETATM 3016  O   HOH A2101      12.439 -30.979  -3.810  1.00 29.36           O  
HETATM 3017  O   HOH A2102       7.750 -34.035  -8.064  1.00 18.15           O  
HETATM 3018  O   HOH A2103       6.760 -31.491  -5.328  1.00 41.22           O  
HETATM 3019  O   HOH A2104      15.760  -4.150 -21.883  1.00 27.38           O  
HETATM 3020  O   HOH A2105      18.444  -6.653 -19.323  1.00 44.70           O  
HETATM 3021  O   HOH A2106      21.075 -27.894 -28.357  1.00 40.15           O  
HETATM 3022  O   HOH A2107       4.665 -26.558 -11.642  1.00 31.66           O  
HETATM 3023  O   HOH A2108       5.998 -23.897  -9.367  1.00 25.67           O  
HETATM 3024  O   HOH A2109      21.031 -23.177 -33.182  1.00 32.70           O  
HETATM 3025  O   HOH A2110      19.816 -19.298 -35.484  1.00 21.79           O  
HETATM 3026  O   HOH A2111      20.421 -23.892 -30.668  1.00 22.06           O  
HETATM 3027  O   HOH A2112      20.014 -24.422 -35.696  1.00 40.62           O  
HETATM 3028  O   HOH A2113       4.190 -21.154 -12.185  1.00 15.75           O  
HETATM 3029  O   HOH A2114       5.354 -16.370 -12.719  1.00 19.43           O  
HETATM 3030  O   HOH A2115       1.858 -22.232 -13.777  1.00 33.48           O  
HETATM 3031  O   HOH A2116       1.032 -19.371 -16.688  1.00 14.82           O  
HETATM 3032  O   HOH A2117      12.724 -18.736 -39.786  1.00 27.99           O  
HETATM 3033  O   HOH A2118       9.862 -10.734 -21.183  1.00 12.42           O  
HETATM 3034  O   HOH A2119       4.842  -4.421 -26.916  1.00 31.38           O  
HETATM 3035  O   HOH A2120       4.620  -6.760 -29.690  1.00 19.53           O  
HETATM 3036  O   HOH A2121       9.188  -4.455 -30.978  1.00 19.57           O  
HETATM 3037  O   HOH A2122      15.737  -8.786 -28.412  1.00 36.44           O  
HETATM 3038  O   HOH A2123      13.821  -5.838 -28.988  1.00 28.38           O  
HETATM 3039  O   HOH A2124      14.763  -5.486 -25.666  1.00 32.59           O  
HETATM 3040  O   HOH A2125      12.601  -4.244 -24.562  1.00 19.70           O  
HETATM 3041  O   HOH A2126      17.282  -9.860 -26.188  1.00 27.09           O  
HETATM 3042  O   HOH A2127       9.647  -7.987 -21.097  1.00 16.34           O  
HETATM 3043  O   HOH A2128      16.685  -9.506 -30.106  1.00 24.77           O  
HETATM 3044  O   HOH A2129      23.085 -13.608 -33.906  1.00 28.36           O  
HETATM 3045  O   HOH A2130      25.005 -15.878 -33.027  1.00 24.56           O  
HETATM 3046  O   HOH A2131      25.670 -13.612 -27.727  1.00 11.74           O  
HETATM 3047  O   HOH A2132      25.465 -10.636 -30.837  1.00 26.53           O  
HETATM 3048  O   HOH A2133      18.906  -9.827 -30.908  1.00 35.89           O  
HETATM 3049  O   HOH A2134      15.149  -9.423 -34.226  1.00 11.05           O  
HETATM 3050  O   HOH A2135      20.286 -10.616 -32.886  1.00 28.72           O  
HETATM 3051  O   HOH A2136      18.715 -15.284 -35.667  1.00 17.86           O  
HETATM 3052  O   HOH A2137      20.757 -13.269 -32.956  1.00 25.94           O  
HETATM 3053  O   HOH A2138      13.598 -14.731 -37.401  1.00 15.55           O  
HETATM 3054  O   HOH A2139      18.401  -9.096 -39.928  1.00 42.29           O  
HETATM 3055  O   HOH A2140      17.033  -8.398 -37.574  1.00 25.10           O  
HETATM 3056  O   HOH A2141      19.224  -6.988 -34.008  1.00 39.08           O  
HETATM 3057  O   HOH A2142      11.532  -8.111 -35.869  1.00 26.55           O  
HETATM 3058  O   HOH A2143      12.068 -12.788 -40.082  1.00 12.49           O  
HETATM 3059  O   HOH A2144      10.411 -16.065 -35.703  1.00 14.37           O  
HETATM 3060  O   HOH A2145      13.360  -5.348 -34.778  1.00 37.32           O  
HETATM 3061  O   HOH A2146      10.597  -4.665 -33.831  1.00 22.20           O  
HETATM 3062  O   HOH A2147       6.558 -16.662 -36.118  1.00 20.70           O  
HETATM 3063  O   HOH A2148       5.974 -23.248 -34.980  1.00 30.18           O  
HETATM 3064  O   HOH A2149       4.725 -23.209 -31.647  1.00 23.40           O  
HETATM 3065  O   HOH A2150       5.866 -27.572 -30.844  1.00 29.43           O  
HETATM 3066  O   HOH A2151       9.658 -27.670 -29.938  1.00 23.33           O  
HETATM 3067  O   HOH A2152      -0.645 -26.570 -28.385  1.00 25.98           O  
HETATM 3068  O   HOH A2153       2.484 -27.652 -26.361  1.00 33.59           O  
HETATM 3069  O   HOH A2154      -0.588 -23.646 -30.431  1.00 34.58           O  
HETATM 3070  O   HOH A2155      12.419 -28.616 -24.565  1.00 34.12           O  
HETATM 3071  O   HOH A2156      12.303 -24.042 -32.792  1.00 32.97           O  
HETATM 3072  O   HOH A2157      16.003 -22.929 -28.808  1.00 15.40           O  
HETATM 3073  O   HOH A2158      17.980 -24.840 -22.564  1.00 23.20           O  
HETATM 3074  O   HOH A2159      21.769 -17.865 -22.327  1.00 13.70           O  
HETATM 3075  O   HOH A2160      25.052 -20.359 -22.048  1.00 18.24           O  
HETATM 3076  O   HOH A2161      20.641 -24.979 -21.695  1.00 22.85           O  
HETATM 3077  O   HOH A2162      25.062 -23.614 -21.492  1.00 41.88           O  
HETATM 3078  O   HOH A2163      19.836 -14.655 -21.227  1.00 10.65           O  
HETATM 3079  O   HOH A2164      20.359 -10.387 -19.268  1.00 10.03           O  
HETATM 3080  O   HOH A2165      10.035  -4.941 -16.524  1.00 27.50           O  
HETATM 3081  O   HOH A2166      12.050  -4.362 -11.335  1.00 30.13           O  
HETATM 3082  O   HOH A2167      13.503  -4.687 -16.265  1.00 32.89           O  
HETATM 3083  O   HOH A2168      14.139 -10.615  -9.048  1.00 16.67           O  
HETATM 3084  O   HOH A2169      12.251  -7.540  -9.345  1.00 33.16           O  
HETATM 3085  O   HOH A2170       5.988  -5.458 -11.158  1.00 37.54           O  
HETATM 3086  O   HOH A2171       1.724 -12.686  -9.303  1.00 35.64           O  
HETATM 3087  O   HOH A2172       4.535  -6.169 -14.591  1.00 33.97           O  
HETATM 3088  O   HOH A2173       0.231  -9.046  -9.048  1.00 29.42           O  
HETATM 3089  O   HOH A2174       3.034 -15.517 -13.982  1.00 22.22           O  
HETATM 3090  O   HOH A2175       0.995 -15.444 -11.643  1.00 34.50           O  
HETATM 3091  O   HOH A2176       4.437 -13.811 -14.971  1.00 33.12           O  
HETATM 3092  O   HOH A2177       6.984  -6.150 -18.366  1.00 20.31           O  
HETATM 3093  O   HOH A2178       6.878 -13.413  -7.767  1.00 36.30           O  
HETATM 3094  O   HOH A2179       7.227  -5.686 -14.677  1.00 26.78           O  
HETATM 3095  O   HOH A2180      11.102  -7.929 -18.625  1.00 15.51           O  
HETATM 3096  O   HOH A2181      16.822  -8.388 -23.811  1.00 19.89           O  
HETATM 3097  O   HOH A2182      15.381  -6.533 -20.392  1.00 19.74           O  
HETATM 3098  O   HOH A2183      19.742  -9.843 -26.704  1.00 25.47           O  
HETATM 3099  O   HOH A2184      22.917  -9.936 -27.148  1.00 18.96           O  
HETATM 3100  O   HOH A2185      22.873  -8.350 -24.899  1.00 20.86           O  
HETATM 3101  O   HOH A2186      21.587 -12.427 -20.748  1.00 10.19           O  
HETATM 3102  O   HOH A2187      24.059 -15.121 -26.012  1.00 10.38           O  
HETATM 3103  O   HOH A2188      24.125 -25.216 -27.265  1.00 29.18           O  
HETATM 3104  O   HOH A2189      27.355 -21.843 -27.489  1.00 21.32           O  
HETATM 3105  O   HOH A2190      26.710 -18.780 -23.921  1.00 20.70           O  
HETATM 3106  O   HOH A2191      23.483 -21.099 -33.679  1.00 38.62           O  
HETATM 3107  O   HOH A2192      26.525 -19.542 -31.143  1.00 21.24           O  
HETATM 3108  O   HOH A2193      26.393 -24.115 -28.720  1.00 35.57           O  
HETATM 3109  O   HOH A2194      20.624 -20.591 -33.075  1.00 18.03           O  
HETATM 3110  O   HOH A2195      18.470 -22.036 -30.057  1.00 14.33           O  
HETATM 3111  O   HOH A2196      17.525 -17.532 -35.111  1.00 17.01           O  
HETATM 3112  O   HOH A2197      11.654 -18.295 -36.599  1.00 14.65           O  
HETATM 3113  O   HOH A2198      15.531 -18.514 -36.543  1.00 29.16           O  
HETATM 3114  O   HOH A2199      14.391 -22.164 -37.550  1.00 33.00           O  
HETATM 3115  O   HOH A2200       8.292 -20.630 -39.592  1.00 47.72           O  
HETATM 3116  O   HOH A2201       9.716 -22.568 -40.127  1.00 25.41           O  
HETATM 3117  O   HOH B2001      29.215 -18.694   0.940  1.00 22.82           O  
HETATM 3118  O   HOH B2002      31.068 -22.657   0.802  1.00 41.20           O  
HETATM 3119  O   HOH B2003      31.628 -20.042  -2.559  1.00 20.60           O  
HETATM 3120  O   HOH B2004      27.088 -14.891  -2.011  1.00 34.28           O  
HETATM 3121  O   HOH B2005      25.279 -21.203  -4.309  1.00 28.98           O  
HETATM 3122  O   HOH B2006      25.045 -15.979  -4.249  1.00 29.49           O  
HETATM 3123  O   HOH B2007      24.882 -15.456 -12.294  1.00 23.85           O  
HETATM 3124  O   HOH B2008      27.705  -4.458 -10.551  1.00 33.57           O  
HETATM 3125  O   HOH B2009      31.368  -3.171 -10.434  1.00 29.64           O  
HETATM 3126  O   HOH B2010      31.900  -3.562 -13.085  1.00 16.99           O  
HETATM 3127  O   HOH B2011      33.756  -1.785 -14.162  1.00 33.49           O  
HETATM 3128  O   HOH B2012      35.653  -2.110 -12.051  1.00 15.32           O  
HETATM 3129  O   HOH B2013      42.712  -3.516 -12.534  1.00 21.13           O  
HETATM 3130  O   HOH B2014      31.558 -18.413   2.320  1.00 23.75           O  
HETATM 3131  O   HOH B2015      29.056 -25.403   0.197  1.00 46.86           O  
HETATM 3132  O   HOH B2016      43.949  -3.967 -16.861  1.00 14.97           O  
HETATM 3133  O   HOH B2017      48.377  -9.529  -8.519  1.00 20.46           O  
HETATM 3134  O   HOH B2018      48.652  -6.455  -9.802  1.00 16.84           O  
HETATM 3135  O   HOH B2019      45.152  -9.036 -21.620  1.00 10.29           O  
HETATM 3136  O   HOH B2020      41.904 -11.091 -24.624  1.00 16.85           O  
HETATM 3137  O   HOH B2021      47.344 -10.785 -21.464  1.00 20.31           O  
HETATM 3138  O   HOH B2022      43.916  -9.103 -24.080  1.00 18.84           O  
HETATM 3139  O   HOH B2023      44.799 -12.537 -25.373  1.00 21.46           O  
HETATM 3140  O   HOH B2024      47.216 -11.518 -24.305  1.00 29.98           O  
HETATM 3141  O   HOH B2025      52.663 -13.075 -23.108  1.00 24.77           O  
HETATM 3142  O   HOH B2026      47.739 -14.999 -26.762  1.00 16.78           O  
HETATM 3143  O   HOH B2027      50.342 -15.740 -25.374  1.00 16.46           O  
HETATM 3144  O   HOH B2028      49.905 -12.279 -21.950  1.00 17.75           O  
HETATM 3145  O   HOH B2029      49.989 -21.419 -23.142  1.00 27.16           O  
HETATM 3146  O   HOH B2030      44.414 -25.810 -20.135  1.00 29.62           O  
HETATM 3147  O   HOH B2031      43.790 -22.436 -23.930  1.00 18.06           O  
HETATM 3148  O   HOH B2032      47.919 -23.281 -24.889  1.00 42.16           O  
HETATM 3149  O   HOH B2033      50.482 -22.577 -31.888  1.00 14.89           O  
HETATM 3150  O   HOH B2034      47.048 -23.016 -21.033  1.00 14.72           O  
HETATM 3151  O   HOH B2035      43.619 -23.292 -20.320  1.00 15.72           O  
HETATM 3152  O   HOH B2036      42.452 -10.822  -1.463  1.00 33.25           O  
HETATM 3153  O   HOH B2037      43.862  -8.536  -2.364  1.00 32.53           O  
HETATM 3154  O   HOH B2038      45.779 -11.632  -4.721  1.00 30.20           O  
HETATM 3155  O   HOH B2039      43.259  -6.911  -9.311  1.00 16.50           O  
HETATM 3156  O   HOH B2040      38.507 -22.128 -13.105  1.00 25.56           O  
HETATM 3157  O   HOH B2041      38.419 -26.096 -20.271  1.00 26.95           O  
HETATM 3158  O   HOH B2042      38.535 -24.368 -14.627  1.00 29.40           O  
HETATM 3159  O   HOH B2043      28.241 -20.042 -19.845  1.00 24.64           O  
HETATM 3160  O   HOH B2044      32.826  -1.774  -8.865  1.00 25.18           O  
HETATM 3161  O   HOH B2045      29.303  -7.062  -5.937  1.00 25.74           O  
HETATM 3162  O   HOH B2046      29.391 -13.683 -30.120  1.00 27.11           O  
HETATM 3163  O   HOH B2047      32.413 -12.420 -30.298  1.00 24.44           O  
HETATM 3164  O   HOH B2048      30.296 -22.272 -30.608  1.00 36.06           O  
HETATM 3165  O   HOH B2049      31.146  -7.246   0.790  1.00 27.16           O  
HETATM 3166  O   HOH B2050      33.942  -6.419   1.570  1.00 25.87           O  
HETATM 3167  O   HOH B2051      39.877 -10.057  -0.572  1.00 30.52           O  
HETATM 3168  O   HOH B2052      39.438  -7.078  -0.033  1.00 16.53           O  
HETATM 3169  O   HOH B2053      43.380  -4.670 -24.942  1.00 30.97           O  
HETATM 3170  O   HOH B2054      48.988  -2.980 -23.865  1.00 41.26           O  
HETATM 3171  O   HOH B2055      39.705  -0.685 -16.450  1.00 32.25           O  
HETATM 3172  O   HOH B2056      33.787   0.489 -17.928  1.00 25.71           O  
HETATM 3173  O   HOH B2057      37.402   0.413 -15.126  1.00 16.20           O  
HETATM 3174  O   HOH B2058      31.083  -4.170 -21.836  1.00 25.84           O  
HETATM 3175  O   HOH B2059      29.308  -2.133 -20.660  1.00 36.81           O  
HETATM 3176  O   HOH B2060      25.796  -9.163  -4.787  1.00 33.07           O  
HETATM 3177  O   HOH B2061      26.367  -1.953  -0.692  1.00 36.94           O  
HETATM 3178  O   HOH B2062      33.150  -3.241   1.006  1.00 33.74           O  
HETATM 3179  O   HOH B2063      34.049 -19.267   1.209  1.00 23.76           O  
HETATM 3180  O   HOH B2064      35.292   1.429  -0.347  1.00 31.41           O  
HETATM 3181  O   HOH B2065      38.579  -1.529  -6.428  1.00 30.54           O  
HETATM 3182  O   HOH B2066      36.539   2.943  -2.192  1.00 23.23           O  
HETATM 3183  O   HOH B2067      39.629   3.236  -5.405  1.00 47.84           O  
HETATM 3184  O   HOH B2068      42.035   5.179  -3.627  1.00 37.95           O  
HETATM 3185  O   HOH B2069      38.019   5.026  -0.877  1.00 19.63           O  
HETATM 3186  O   HOH B2070      42.148   1.706  -7.444  1.00 35.26           O  
HETATM 3187  O   HOH B2071      40.527  -4.893  -1.333  1.00 17.50           O  
HETATM 3188  O   HOH B2072      27.208  -5.510 -22.311  1.00 24.58           O  
HETATM 3189  O   HOH B2073      43.337  -5.987  -2.579  1.00 31.88           O  
HETATM 3190  O   HOH B2074      18.591  -5.814 -15.177  1.00 25.94           O  
HETATM 3191  O   HOH B2075      27.372  -9.573 -27.190  1.00 19.57           O  
HETATM 3192  O   HOH B2076      44.546  -9.377  -5.177  1.00 18.07           O  
HETATM 3193  O   HOH B2077      42.773 -15.132  -7.081  1.00 15.98           O  
HETATM 3194  O   HOH B2078      42.931 -12.948  -4.537  1.00 26.89           O  
HETATM 3195  O   HOH B2079      46.815  -7.145  -7.176  1.00 39.42           O  
HETATM 3196  O   HOH B2080      47.125 -12.504 -10.472  1.00 16.42           O  
HETATM 3197  O   HOH B2081      46.848 -12.884  -7.060  1.00 25.12           O  
HETATM 3198  O   HOH B2082      37.743 -19.575 -13.471  1.00 11.93           O  
HETATM 3199  O   HOH B2083      41.505 -23.955 -22.489  1.00 16.05           O  
HETATM 3200  O   HOH B2084      36.947 -25.569 -23.599  1.00 23.39           O  
HETATM 3201  O   HOH B2085      32.553 -23.700 -21.288  1.00 30.90           O  
HETATM 3202  O   HOH B2086      31.098 -23.803 -16.765  1.00 44.52           O  
HETATM 3203  O   HOH B2087      34.537 -25.044 -16.310  1.00 38.20           O  
HETATM 3204  O   HOH B2088      37.736 -25.955 -17.266  1.00 28.71           O  
HETATM 3205  O   HOH B2089      29.473 -19.215 -17.796  1.00 24.78           O  
HETATM 3206  O   HOH B2090      31.977 -23.242 -12.810  1.00 25.14           O  
HETATM 3207  O   HOH B2091      29.140 -19.634 -22.441  1.00 30.13           O  
HETATM 3208  O   HOH B2092      21.001 -16.639 -19.821  1.00 17.12           O  
HETATM 3209  O   HOH B2093      26.107 -16.060 -24.397  1.00 13.03           O  
HETATM 3210  O   HOH B2094      31.183 -20.045 -26.284  1.00 11.37           O  
HETATM 3211  O   HOH B2095      28.423 -13.720 -27.484  1.00 12.88           O  
HETATM 3212  O   HOH B2096      33.031 -14.863 -29.397  1.00 17.94           O  
HETATM 3213  O   HOH B2097      28.614 -20.541 -29.507  1.00 18.29           O  
HETATM 3214  O   HOH B2098      34.524 -21.491 -29.009  1.00 31.89           O  
HETATM 3215  O   HOH B2099      34.110 -16.710 -32.351  1.00 34.81           O  
HETATM 3216  O   HOH B2100      36.321 -13.853 -27.894  1.00 14.20           O  
HETATM 3217  O   HOH B2101      29.639 -22.438 -26.096  1.00 24.18           O  
HETATM 3218  O   HOH B2102      32.438 -24.966 -25.824  1.00 38.55           O  
HETATM 3219  O   HOH B2103      42.321  -6.908 -24.227  1.00 15.28           O  
HETATM 3220  O   HOH B2104      37.715  -2.152 -22.242  1.00 31.07           O  
HETATM 3221  O   HOH B2105      41.428  -2.810 -23.669  1.00 28.37           O  
HETATM 3222  O   HOH B2106      47.862  -3.720 -21.203  1.00 20.20           O  
HETATM 3223  O   HOH B2107      41.649  -2.213 -16.976  1.00 26.23           O  
HETATM 3224  O   HOH B2108      35.500  -1.114 -16.442  1.00 17.10           O  
HETATM 3225  O   HOH B2109      33.083  -0.024 -20.470  1.00 54.46           O  
HETATM 3226  O   HOH B2110      31.610  -6.562 -20.660  1.00 10.37           O  
HETATM 3227  O   HOH B2111      30.055  -4.800 -14.106  1.00 23.06           O  
HETATM 3228  O   HOH B2112      25.524 -11.720 -13.942  1.00 12.24           O  
HETATM 3229  O   HOH B2113      27.433  -4.651 -13.089  1.00 19.81           O  
HETATM 3230  O   HOH B2114      28.005 -20.158 -10.359  1.00 16.92           O  
HETATM 3231  O   HOH B2115      27.184 -16.137 -12.815  1.00 25.94           O  
HETATM 3232  O   HOH B2116      34.119 -19.899  -1.247  1.00 16.90           O  
HETATM 3233  O   HOH B2117      35.512 -22.583  -1.540  1.00 21.18           O  
HETATM 3234  O   HOH B2118      37.918 -24.043  -3.655  1.00 29.15           O  
HETATM 3235  O   HOH B2119      43.731 -21.082  -5.977  1.00 26.60           O  
HETATM 3236  O   HOH B2120      40.409 -23.144  -0.068  1.00 39.25           O  
HETATM 3237  O   HOH B2121      41.780 -24.722  -4.486  1.00 28.93           O  
HETATM 3238  O   HOH B2122      47.780 -24.317  -0.290  1.00 41.83           O  
HETATM 3239  O   HOH B2123      45.408 -15.187  -6.825  1.00 23.20           O  
HETATM 3240  O   HOH B2124      50.859 -18.865  -1.172  1.00 29.91           O  
HETATM 3241  O   HOH B2125      41.846 -17.067  -0.663  1.00 33.39           O  
HETATM 3242  O   HOH B2126      40.548 -22.819 -11.430  1.00 26.32           O  
HETATM 3243  O   HOH B2127      39.487 -24.467  -6.043  1.00 27.90           O  
HETATM 3244  O   HOH B2128      36.087 -22.287 -10.824  1.00 31.66           O  
HETATM 3245  O   HOH B2129      30.279 -21.274 -15.929  1.00 18.34           O  
HETATM 3246  O   HOH B2130      27.688 -21.605 -15.126  1.00 37.09           O  
HETATM 3247  O   HOH B2131      24.687 -19.904 -19.214  1.00 22.81           O  
HETATM 3248  O   HOH B2132      23.560 -14.921 -15.625  1.00 17.33           O  
HETATM 3249  O   HOH B2133      23.164 -15.037 -18.232  1.00 14.47           O  
HETATM 3250  O   HOH B2134      25.283  -4.908 -20.566  1.00 30.96           O  
HETATM 3251  O   HOH B2135      19.608  -7.391 -16.995  1.00 20.31           O  
HETATM 3252  O   HOH B2136      19.875  -8.329 -20.942  1.00 17.28           O  
HETATM 3253  O   HOH B2137      20.869  -5.224 -19.333  1.00 43.09           O  
HETATM 3254  O   HOH B2138      26.763  -8.365 -24.538  1.00 19.98           O  
HETATM 3255  O   HOH B2139      29.060  -7.349 -21.638  1.00 12.80           O  
HETATM 3256  O   HOH B2140      29.591 -11.346 -26.971  1.00 14.23           O  
HETATM 3257  O   HOH B2141      31.549 -10.120 -28.499  1.00 24.24           O  
HETATM 3258  O   HOH B2142      35.042 -11.534 -28.714  1.00 20.07           O  
HETATM 3259  O   HOH B2143      35.619  -6.437 -28.540  1.00 42.10           O  
HETATM 3260  O   HOH B2144      37.030 -10.332 -30.238  1.00 31.64           O  
HETATM 3261  O   HOH B2145      43.833 -11.394 -27.632  1.00 23.63           O  
HETATM 3262  O   HOH B2146      41.654  -8.178 -31.155  1.00 35.09           O  
HETATM 3263  O   HOH B2147      37.529 -18.025 -33.348  1.00 29.41           O  
HETATM 3264  O   HOH B2148      40.704 -16.738 -35.365  1.00 19.35           O  
HETATM 3265  O   HOH B2149      44.331 -11.101 -32.177  1.00 30.91           O  
HETATM 3266  O   HOH C2001      29.974  -1.983 -36.181  1.00 38.16           O  
HETATM 3267  O   HOH C2002      32.006  -1.386 -39.346  1.00 35.43           O  
HETATM 3268  O   HOH C2003      32.539  -0.788 -41.461  1.00 43.99           O  
HETATM 3269  O   HOH C2004      28.383  -4.475 -45.598  1.00 21.52           O  
HETATM 3270  O   HOH C2005      32.918  -5.491 -39.907  1.00 17.26           O  
HETATM 3271  O   HOH C2006      25.003  -6.360 -44.716  1.00 27.24           O  
HETATM 3272  O   HOH C2007      23.024 -11.960 -45.257  1.00 22.26           O  
HETATM 3273  O   HOH C2008      28.044 -11.629 -47.650  1.00 34.74           O  
HETATM 3274  O   HOH C2009      27.894 -13.777 -44.986  1.00 28.99           O  
HETATM 3275  O   HOH C2010      28.589 -10.066 -50.691  1.00 23.41           O  
HETATM 3276  O   HOH C2011      30.492 -12.996 -55.275  1.00 30.42           O  
HETATM 3277  O   HOH C2012      27.484 -13.342 -54.726  1.00 31.66           O  
HETATM 3278  O   HOH C2013      31.361 -15.553 -54.903  1.00 25.06           O  
HETATM 3279  O   HOH C2014      34.804 -14.560 -57.074  1.00 19.37           O  
HETATM 3280  O   HOH C2015      42.123 -16.405 -56.831  1.00 35.48           O  
HETATM 3281  O   HOH C2016      40.670 -19.803 -57.132  1.00 47.69           O  
HETATM 3282  O   HOH C2017      34.081  -3.286 -39.414  1.00 22.85           O  
HETATM 3283  O   HOH C2018      34.144  -2.310 -36.743  1.00 27.10           O  
HETATM 3284  O   HOH C2019      31.851  -6.108 -37.397  1.00 39.41           O  
HETATM 3285  O   HOH C2020      24.541 -13.484 -42.482  1.00 31.42           O  
HETATM 3286  O   HOH C2021      43.328 -19.198 -56.377  1.00 25.77           O  
HETATM 3287  O   HOH C2022      46.166 -19.827 -55.477  1.00 38.77           O  
HETATM 3288  O   HOH C2023      48.144 -12.588 -55.404  1.00 38.16           O  
HETATM 3289  O   HOH C2024      29.200 -16.944 -53.615  1.00 24.20           O  
HETATM 3290  O   HOH C2025      44.955 -24.170 -51.375  1.00 11.87           O  
HETATM 3291  O   HOH C2026      42.817 -26.359 -49.149  1.00 11.09           O  
HETATM 3292  O   HOH C2027      46.661 -27.525 -47.738  1.00 17.36           O  
HETATM 3293  O   HOH C2028      46.943 -25.855 -50.122  1.00 32.36           O  
HETATM 3294  O   HOH C2029      49.197 -23.552 -48.914  1.00 32.86           O  
HETATM 3295  O   HOH C2030      51.020 -28.446 -45.077  1.00 18.23           O  
HETATM 3296  O   HOH C2031      42.128 -26.572 -42.141  1.00 10.60           O  
HETATM 3297  O   HOH C2032      44.474 -27.999 -39.290  1.00 21.51           O  
HETATM 3298  O   HOH C2033      48.242 -29.019 -45.523  1.00 18.57           O  
HETATM 3299  O   HOH C2034      45.473 -26.231 -37.360  1.00 29.97           O  
HETATM 3300  O   HOH C2035      51.479 -30.259 -38.238  1.00 37.57           O  
HETATM 3301  O   HOH C2036      55.620 -25.962 -40.776  1.00 15.56           O  
HETATM 3302  O   HOH C2037      48.076 -25.250 -36.952  1.00 38.76           O  
HETATM 3303  O   HOH C2038      54.619 -27.021 -38.379  1.00 22.75           O  
HETATM 3304  O   HOH C2039      45.509 -22.274 -36.963  1.00 11.77           O  
HETATM 3305  O   HOH C2040      41.115  -0.618 -48.938  1.00 25.09           O  
HETATM 3306  O   HOH C2041      43.448  -3.678 -50.331  1.00 28.58           O  
HETATM 3307  O   HOH C2042      23.197  -6.222 -53.396  1.00 42.87           O  
HETATM 3308  O   HOH C2043      45.111  -5.828 -47.282  1.00 28.68           O  
HETATM 3309  O   HOH C2044      40.840 -13.398 -58.469  1.00 41.12           O  
HETATM 3310  O   HOH C2045      42.812 -11.747 -54.009  1.00 27.07           O  
HETATM 3311  O   HOH C2046      34.009  -8.457 -59.449  1.00 24.16           O  
HETATM 3312  O   HOH C2047      31.305  -9.207 -58.304  1.00 34.82           O  
HETATM 3313  O   HOH C2048      31.904 -11.486 -57.067  1.00 23.99           O  
HETATM 3314  O   HOH C2049      27.052  -9.331 -54.271  1.00 37.41           O  
HETATM 3315  O   HOH C2050      28.949  -7.245 -56.585  1.00 23.57           O  
HETATM 3316  O   HOH C2051      29.275  -7.594 -51.577  1.00 17.02           O  
HETATM 3317  O   HOH C2052      32.800  -2.119 -53.037  1.00 19.68           O  
HETATM 3318  O   HOH C2053      34.227  -0.912 -51.161  1.00 23.37           O  
HETATM 3319  O   HOH C2054      37.526  -0.915 -44.648  1.00 25.49           O  
HETATM 3320  O   HOH C2055      38.544  -0.179 -48.246  1.00 31.76           O  
HETATM 3321  O   HOH C2056      35.243   0.128 -43.652  1.00 38.90           O  
HETATM 3322  O   HOH C2057      40.932  -2.888 -50.320  1.00 20.81           O  
HETATM 3323  O   HOH C2058      39.567  -2.393 -52.741  1.00 28.07           O  
HETATM 3324  O   HOH C2059      36.464   1.245 -49.445  1.00 24.91           O  
HETATM 3325  O   HOH C2060      43.566 -28.144 -53.531  1.00 23.18           O  
HETATM 3326  O   HOH C2061      38.597 -23.042 -59.487  1.00 41.06           O  
HETATM 3327  O   HOH C2062      32.887 -25.631 -55.173  1.00 26.36           O  
HETATM 3328  O   HOH C2063      24.778  -3.251 -49.974  1.00 44.87           O  
HETATM 3329  O   HOH C2064      26.776  -1.522 -53.069  1.00 20.12           O  
HETATM 3330  O   HOH C2065      26.615  -0.997 -49.182  1.00 30.46           O  
HETATM 3331  O   HOH C2066      30.961 -24.732 -53.454  1.00 22.98           O  
HETATM 3332  O   HOH C2067      25.263  -7.191 -54.937  1.00 36.35           O  
HETATM 3333  O   HOH C2068      26.691 -10.191 -39.081  1.00 36.09           O  
HETATM 3334  O   HOH C2069      43.069  -3.463 -35.577  1.00 27.79           O  
HETATM 3335  O   HOH C2070      47.601  -3.716 -44.089  1.00 28.98           O  
HETATM 3336  O   HOH C2071      47.533   0.125 -41.839  0.50 25.26           O  
HETATM 3337  O   HOH C2072      33.326  -1.456 -55.671  1.00 27.18           O  
HETATM 3338  O   HOH C2073      37.678  -8.908 -58.707  1.00 45.17           O  
HETATM 3339  O   HOH C2074      43.013  -7.155 -61.439  1.00 37.15           O  
HETATM 3340  O   HOH C2075      28.373 -29.653 -47.734  1.00 36.37           O  
HETATM 3341  O   HOH C2076      27.420 -24.683 -51.931  1.00 23.28           O  
HETATM 3342  O   HOH C2077      44.999  -7.802 -51.402  1.00 20.94           O  
HETATM 3343  O   HOH C2078      44.247  -8.506 -46.514  1.00 26.98           O  
HETATM 3344  O   HOH C2079      47.557 -13.648 -49.719  1.00 39.97           O  
HETATM 3345  O   HOH C2080      47.265  -8.781 -49.764  1.00 25.17           O  
HETATM 3346  O   HOH C2081      39.642 -15.110 -39.982  1.00 11.78           O  
HETATM 3347  O   HOH C2082      43.443 -23.829 -35.407  1.00 24.58           O  
HETATM 3348  O   HOH C2083      44.674 -21.252 -33.553  1.00 24.68           O  
HETATM 3349  O   HOH C2084      32.616 -22.293 -37.235  1.00 29.32           O  
HETATM 3350  O   HOH C2085      31.605 -19.407 -38.157  1.00 28.22           O  
HETATM 3351  O   HOH C2086      34.260 -14.082 -35.687  1.00 20.23           O  
HETATM 3352  O   HOH C2087      37.584 -12.337 -34.851  1.00 29.45           O  
HETATM 3353  O   HOH C2088      22.578 -24.589 -43.264  1.00 35.59           O  
HETATM 3354  O   HOH C2089      23.141 -24.469 -39.003  1.00 34.56           O  
HETATM 3355  O   HOH C2090      27.211 -25.672 -41.032  1.00 25.60           O  
HETATM 3356  O   HOH C2091      29.689 -24.071 -38.054  1.00 32.68           O  
HETATM 3357  O   HOH C2092      27.485 -26.214 -38.383  1.00 39.94           O  
HETATM 3358  O   HOH C2093      32.656 -27.560 -37.581  1.00 14.82           O  
HETATM 3359  O   HOH C2094      28.797 -29.093 -43.336  1.00 19.16           O  
HETATM 3360  O   HOH C2095      29.871 -32.068 -43.083  1.00 35.83           O  
HETATM 3361  O   HOH C2096      33.578 -30.766 -42.998  1.00 12.34           O  
HETATM 3362  O   HOH C2097      23.381 -31.409 -41.599  1.00 37.48           O  
HETATM 3363  O   HOH C2098      24.817 -34.269 -40.173  1.00 33.98           O  
HETATM 3364  O   HOH C2099      26.125 -29.363 -42.985  1.00 23.31           O  
HETATM 3365  O   HOH C2100      29.991 -30.341 -36.661  1.00 29.84           O  
HETATM 3366  O   HOH C2101      34.690 -33.758 -41.140  1.00 11.20           O  
HETATM 3367  O   HOH C2102      37.065 -29.416 -44.310  1.00 10.65           O  
HETATM 3368  O   HOH C2103      35.861 -32.354 -52.183  1.00 36.85           O  
HETATM 3369  O   HOH C2104      42.905 -26.087 -51.844  1.00 12.37           O  
HETATM 3370  O   HOH C2105      40.537 -26.736 -56.121  1.00 26.97           O  
HETATM 3371  O   HOH C2106      36.971 -25.213 -56.207  1.00 26.80           O  
HETATM 3372  O   HOH C2107      46.546 -23.600 -53.553  1.00 21.63           O  
HETATM 3373  O   HOH C2108      37.064 -20.636 -58.651  1.00 32.91           O  
HETATM 3374  O   HOH C2109      31.694 -23.013 -51.342  1.00 12.88           O  
HETATM 3375  O   HOH C2110      23.352 -15.170 -47.522  1.00 21.00           O  
HETATM 3376  O   HOH C2111      26.487 -15.908 -45.718  1.00 21.17           O  
HETATM 3377  O   HOH C2112      26.963 -15.540 -53.167  1.00 28.26           O  
HETATM 3378  O   HOH C2113      29.770 -11.740 -38.585  1.00 19.40           O  
HETATM 3379  O   HOH C2114      41.227 -10.631 -34.912  1.00 27.89           O  
HETATM 3380  O   HOH C2115      34.321  -6.768 -35.710  1.00 38.02           O  
HETATM 3381  O   HOH C2116      36.636  -2.857 -40.051  1.00 11.85           O  
HETATM 3382  O   HOH C2117      38.333  -3.115 -37.844  1.00 19.90           O  
HETATM 3383  O   HOH C2118      40.650  -5.070 -36.019  1.00 23.51           O  
HETATM 3384  O   HOH C2119      37.043  -0.576 -41.619  1.00 25.57           O  
HETATM 3385  O   HOH C2120      39.318  -0.567 -37.272  1.00 32.11           O  
HETATM 3386  O   HOH C2121      41.723   2.395 -38.912  1.00 31.13           O  
HETATM 3387  O   HOH C2122      44.530   3.276 -41.128  1.00 28.77           O  
HETATM 3388  O   HOH C2123      44.419  -2.974 -42.940  1.00 27.71           O  
HETATM 3389  O   HOH C2124      44.897  -1.795 -40.373  1.00 39.39           O  
HETATM 3390  O   HOH C2125      44.982  -5.378 -35.730  1.00 17.53           O  
HETATM 3391  O   HOH C2126      48.939  -4.252 -41.680  1.00 20.93           O  
HETATM 3392  O   HOH C2127      46.248  -9.178 -36.352  1.00 14.89           O  
HETATM 3393  O   HOH C2128      47.994 -10.926 -43.848  1.00  9.72           O  
HETATM 3394  O   HOH C2129      46.892  -9.294 -46.995  1.00 20.26           O  
HETATM 3395  O   HOH C2130      41.217 -14.573 -37.763  1.00 22.22           O  
HETATM 3396  O   HOH C2131      38.348 -12.245 -37.374  1.00 16.63           O  
HETATM 3397  O   HOH C2132      32.397 -17.142 -37.018  1.00 21.83           O  
HETATM 3398  O   HOH C2133      28.625 -14.517 -42.694  1.00 29.19           O  
HETATM 3399  O   HOH C2134      28.959 -19.656 -38.137  1.00 34.08           O  
HETATM 3400  O   HOH C2135      24.781 -16.737 -43.681  1.00 28.82           O  
HETATM 3401  O   HOH C2136      24.346 -19.557 -43.107  1.00 18.43           O  
HETATM 3402  O   HOH C2137      25.496 -20.247 -38.061  1.00 29.61           O  
HETATM 3403  O   HOH C2138      20.061 -17.710 -49.037  1.00 17.14           O  
HETATM 3404  O   HOH C2139      22.642 -16.762 -45.411  1.00 33.29           O  
HETATM 3405  O   HOH C2140      21.836 -23.674 -52.962  1.00 36.79           O  
HETATM 3406  O   HOH C2141      27.192 -26.930 -48.760  1.00 40.71           O  
HETATM 3407  O   HOH C2142      29.246 -23.879 -50.327  1.00 14.32           O  
HETATM 3408  O   HOH C2143      30.067 -28.890 -45.726  1.00 15.71           O  
HETATM 3409  O   HOH C2144      36.056 -30.859 -46.499  1.00 11.83           O  
HETATM 3410  O   HOH C2145      32.544 -30.348 -45.704  1.00 17.61           O  
HETATM 3411  O   HOH C2146      35.907 -31.813 -49.814  1.00 37.96           O  
HETATM 3412  O   HOH C2147      43.781 -31.850 -47.464  1.00 17.63           O  
HETATM 3413  O   HOH C2148      41.858 -30.973 -53.075  1.00 34.85           O  
HETATM 3414  O   HOH C2149      45.250 -30.527 -51.353  1.00 28.33           O  
HETATM 3415  O   HOH C2150      45.745 -30.161 -48.551  1.00 22.22           O  
HETATM 3416  O   HOH C2151      39.018 -32.467 -50.928  1.00 34.76           O  
HETATM 3417  O   HOH C2152      34.809 -32.630 -44.800  1.00 18.04           O  
HETATM 3418  O   HOH C2153      35.088 -36.303 -44.411  1.00 18.34           O  
HETATM 3419  O   HOH D2001      21.794 -27.398 -44.941  1.00 50.31           O  
HETATM 3420  O   HOH D2002      14.233 -25.135 -45.026  1.00 17.84           O  
HETATM 3421  O   HOH D2003      20.103 -18.922 -51.658  1.00 17.51           O  
HETATM 3422  O   HOH D2004      21.531 -19.948 -57.164  1.00 44.82           O  
HETATM 3423  O   HOH D2005      19.375 -16.516 -59.532  1.00 35.94           O  
HETATM 3424  O   HOH D2006      18.686 -14.077 -58.893  1.00 26.01           O  
HETATM 3425  O   HOH D2007      17.641 -13.015 -61.214  1.00 34.46           O  
HETATM 3426  O   HOH D2008      15.751 -15.012 -61.777  1.00 23.82           O  
HETATM 3427  O   HOH D2009       8.622 -14.223 -63.024  1.00 31.85           O  
HETATM 3428  O   HOH D2010      13.025 -27.554 -44.957  1.00 20.78           O  
HETATM 3429  O   HOH D2011      14.772 -24.158 -42.540  1.00 27.68           O  
HETATM 3430  O   HOH D2012       7.323 -10.098 -62.568  1.00 27.49           O  
HETATM 3431  O   HOH D2013       1.688 -18.858 -60.749  1.00 28.16           O  
HETATM 3432  O   HOH D2014       1.544 -15.152 -58.647  1.00 20.37           O  
HETATM 3433  O   HOH D2015       4.566  -5.587 -57.463  1.00 25.00           O  
HETATM 3434  O   HOH D2016       2.832  -2.805 -53.696  1.00 28.27           O  
HETATM 3435  O   HOH D2017      -2.987  -2.429 -52.787  1.00 33.60           O  
HETATM 3436  O   HOH D2018      -0.371  -2.273 -52.285  1.00 29.87           O  
HETATM 3437  O   HOH D2019      -1.258  -7.667 -55.568  1.00 23.95           O  
HETATM 3438  O   HOH D2020      -4.464  -5.297 -52.009  1.00 22.87           O  
HETATM 3439  O   HOH D2021       1.224  -2.037 -43.325  1.00 36.77           O  
HETATM 3440  O   HOH D2022       1.116  -0.789 -45.901  1.00 31.36           O  
HETATM 3441  O   HOH D2023      -1.492  -5.357 -43.826  1.00 31.36           O  
HETATM 3442  O   HOH D2024      -2.181  -1.386 -45.048  1.00 25.24           O  
HETATM 3443  O   HOH D2025       1.116  -4.589 -43.847  1.00 42.39           O  
HETATM 3444  O   HOH D2026      -7.453  -5.171 -51.120  1.00 30.07           O  
HETATM 3445  O   HOH D2027      -6.935  -4.189 -42.686  1.00 19.82           O  
HETATM 3446  O   HOH D2028       5.692 -18.451 -62.816  1.00 30.45           O  
HETATM 3447  O   HOH D2029       1.261  -8.526 -43.481  1.00 11.16           O  
HETATM 3448  O   HOH D2030       8.609 -30.503 -52.678  1.00 22.67           O  
HETATM 3449  O   HOH D2031       2.803 -23.351 -57.389  1.00 22.90           O  
HETATM 3450  O   HOH D2032       3.077 -24.074 -54.684  1.00 19.98           O  
HETATM 3451  O   HOH D2033       7.057 -17.876 -60.576  1.00 17.99           O  
HETATM 3452  O   HOH D2034      15.131 -17.753 -40.814  1.00 24.31           O  
HETATM 3453  O   HOH D2035      18.572 -18.394 -61.488  1.00 33.26           O  
HETATM 3454  O   HOH D2036      20.023 -22.032 -55.465  1.00 22.62           O  
HETATM 3455  O   HOH D2037      10.370 -29.661 -54.594  1.00 33.07           O  
HETATM 3456  O   HOH D2038      11.390 -27.183 -58.052  1.00 35.40           O  
HETATM 3457  O   HOH D2039      10.822 -29.883 -50.942  1.00 27.92           O  
HETATM 3458  O   HOH D2040      18.769 -28.824 -50.051  1.00 34.01           O  
HETATM 3459  O   HOH D2041      22.044 -29.626 -56.482  1.00 52.81           O  
HETATM 3460  O   HOH D2042      19.653  -5.733 -56.740  1.00 27.03           O  
HETATM 3461  O   HOH D2043      28.200 -18.058 -56.343  1.00 32.31           O  
HETATM 3462  O   HOH D2044      15.851 -21.655 -41.722  1.00 29.40           O  
HETATM 3463  O   HOH D2045      19.211 -18.337 -42.673  1.00 30.14           O  
HETATM 3464  O   HOH D2046      20.873 -29.929 -61.496  1.00 48.82           O  
HETATM 3465  O   HOH D2047       2.510 -23.091 -41.379  1.00 31.29           O  
HETATM 3466  O   HOH D2048      17.098 -26.631 -66.055  1.00 32.99           O  
HETATM 3467  O   HOH D2049      18.898 -28.603 -63.261  1.00 27.30           O  
HETATM 3468  O   HOH D2050       0.354 -26.327 -51.826  1.00 24.46           O  
HETATM 3469  O   HOH D2051       0.012 -28.355 -47.761  1.00 30.09           O  
HETATM 3470  O   HOH D2052      13.100 -20.711 -64.087  1.00 24.22           O  
HETATM 3471  O   HOH D2053      11.406 -26.649 -64.421  1.00 22.31           O  
HETATM 3472  O   HOH D2054      14.159 -27.744 -64.736  1.00 24.17           O  
HETATM 3473  O   HOH D2055      15.683 -26.722 -70.005  1.00 17.12           O  
HETATM 3474  O   HOH D2056       8.700 -27.553 -68.683  1.00 27.91           O  
HETATM 3475  O   HOH D2057       9.682 -24.494 -71.053  1.00 10.94           O  
HETATM 3476  O   HOH D2058      14.010 -29.263 -67.911  1.00 24.18           O  
HETATM 3477  O   HOH D2059       6.943 -24.111 -70.176  1.00 23.68           O  
HETATM 3478  O   HOH D2060       6.460 -20.900 -64.119  1.00 38.11           O  
HETATM 3479  O   HOH D2061      20.726  -1.088 -49.948  1.00 37.08           O  
HETATM 3480  O   HOH D2062       4.858 -22.281 -59.079  1.00 20.18           O  
HETATM 3481  O   HOH D2063       4.511 -21.923 -53.695  1.00 14.86           O  
HETATM 3482  O   HOH D2064       1.406 -21.106 -57.174  1.00 22.88           O  
HETATM 3483  O   HOH D2065       1.385 -17.157 -56.731  1.00 20.68           O  
HETATM 3484  O   HOH D2066       7.372 -15.682 -46.284  1.00  8.07           O  
HETATM 3485  O   HOH D2067       2.849  -6.657 -42.282  1.00 19.35           O  
HETATM 3486  O   HOH D2068      11.802  -8.636 -39.953  1.00 18.97           O  
HETATM 3487  O   HOH D2069      15.346 -11.253 -42.364  1.00 26.24           O  
HETATM 3488  O   HOH D2070       5.651 -15.732 -41.486  1.00 17.17           O  
HETATM 3489  O   HOH D2071      11.610 -16.839 -41.085  1.00 13.82           O  
HETATM 3490  O   HOH D2072       7.277 -18.517 -41.848  1.00 17.20           O  
HETATM 3491  O   HOH D2073      11.053 -14.983 -39.275  1.00 25.47           O  
HETATM 3492  O   HOH D2074       8.677 -15.989 -37.985  1.00 17.49           O  
HETATM 3493  O   HOH D2075      14.259  -8.459 -41.625  1.00 25.89           O  
HETATM 3494  O   HOH D2076      22.970  -7.517 -40.322  1.00 32.53           O  
HETATM 3495  O   HOH D2077      16.855  -6.962 -41.301  1.00 34.23           O  
HETATM 3496  O   HOH D2078      19.662  -5.314 -43.492  1.00 30.61           O  
HETATM 3497  O   HOH D2079      13.631  -3.326 -41.722  1.00 13.00           O  
HETATM 3498  O   HOH D2080      18.708  -1.593 -46.118  1.00 18.74           O  
HETATM 3499  O   HOH D2081      13.741   0.582 -46.704  1.00 24.81           O  
HETATM 3500  O   HOH D2082      17.932   1.073 -45.784  1.00 26.91           O  
HETATM 3501  O   HOH D2083      15.557  -0.519 -39.753  1.00 28.10           O  
HETATM 3502  O   HOH D2084       9.567  -1.927 -41.499  1.00 27.76           O  
HETATM 3503  O   HOH D2085      11.799   3.326 -43.801  1.00 23.39           O  
HETATM 3504  O   HOH D2086      11.209  -0.854 -49.206  1.00 18.28           O  
HETATM 3505  O   HOH D2087       9.398  -4.410 -37.656  1.00 16.99           O  
HETATM 3506  O   HOH D2088      10.489  -1.631 -39.298  1.00 27.75           O  
HETATM 3507  O   HOH D2089      13.988  -2.984 -38.975  1.00 32.37           O  
HETATM 3508  O   HOH D2090       8.069  -2.835 -57.896  1.00 31.18           O  
HETATM 3509  O   HOH D2091      10.762  -3.150 -61.670  1.00 28.98           O  
HETATM 3510  O   HOH D2092      14.056  -4.586 -61.045  1.00 26.86           O  
HETATM 3511  O   HOH D2093      10.135  -9.706 -63.018  1.00 41.27           O  
HETATM 3512  O   HOH D2094      18.189  -7.224 -54.928  1.00 16.41           O  
HETATM 3513  O   HOH D2095      18.209  -4.662 -58.923  1.00 35.84           O  
HETATM 3514  O   HOH D2096      24.995 -17.118 -54.866  1.00 40.31           O  
HETATM 3515  O   HOH D2097      21.379 -15.007 -49.132  1.00 21.92           O  
HETATM 3516  O   HOH D2098      20.932 -12.928 -57.279  1.00 29.28           O  
HETATM 3517  O   HOH D2099      16.501 -18.962 -42.787  1.00 17.97           O  
HETATM 3518  O   HOH D2100       6.497 -26.227 -42.670  1.00 24.35           O  
HETATM 3519  O   HOH D2101       4.844 -21.679 -42.049  1.00 22.26           O  
HETATM 3520  O   HOH D2102      10.573 -27.941 -46.290  1.00 12.59           O  
HETATM 3521  O   HOH D2103       8.643 -29.363 -44.656  1.00 37.03           O  
HETATM 3522  O   HOH D2104       3.544 -27.485 -49.695  1.00 27.31           O  
HETATM 3523  O   HOH D2105       1.896 -31.293 -51.056  1.00 33.77           O  
HETATM 3524  O   HOH D2106       3.302 -28.689 -46.163  1.00 43.38           O  
HETATM 3525  O   HOH D2107       3.433 -33.803 -48.865  1.00 19.30           O  
HETATM 3526  O   HOH D2108       2.236 -25.592 -42.851  1.00 12.72           O  
HETATM 3527  O   HOH D2109      -0.969 -26.194 -49.382  1.00 16.75           O  
HETATM 3528  O   HOH D2110       1.289 -21.759 -43.382  1.00 15.03           O  
HETATM 3529  O   HOH D2111      -0.319 -19.863 -50.764  1.00 10.13           O  
HETATM 3530  O   HOH D2112       2.449 -20.377 -52.935  1.00 26.77           O  
HETATM 3531  O   HOH D2113       5.415 -16.143 -44.287  1.00  8.78           O  
HETATM 3532  O   HOH D2114      14.149 -13.786 -41.672  1.00 12.12           O  
HETATM 3533  O   HOH D2115      18.885 -16.250 -46.603  1.00 21.48           O  
HETATM 3534  O   HOH D2116      20.383 -11.105 -40.195  1.00 40.14           O  
HETATM 3535  O   HOH D2117      20.550 -13.824 -39.632  1.00 32.71           O  
HETATM 3536  O   HOH D2118      19.841 -16.629 -44.590  1.00 33.09           O  
HETATM 3537  O   HOH D2119      26.157  -4.943 -47.468  1.00 21.06           O  
HETATM 3538  O   HOH D2120      22.229  -4.145 -50.730  1.00 30.60           O  
HETATM 3539  O   HOH D2121      20.335  -6.424 -53.260  1.00 18.68           O  
HETATM 3540  O   HOH D2122      18.449  -1.831 -48.610  1.00 21.26           O  
HETATM 3541  O   HOH D2123      17.128   0.239 -50.104  1.00 32.79           O  
HETATM 3542  O   HOH D2124      13.207   0.281 -50.516  1.00 26.00           O  
HETATM 3543  O   HOH D2125      10.753   2.291 -49.553  1.00 36.00           O  
HETATM 3544  O   HOH D2126      -5.154 -11.880 -55.385  1.00 43.25           O  
HETATM 3545  O   HOH D2127      -2.671 -13.097 -54.985  1.00 24.50           O  
HETATM 3546  O   HOH E2001       9.474  -8.291 -38.492  1.00 23.34           O  
HETATM 3547  O   HOH E2002       4.590  -9.586 -38.805  1.00 14.50           O  
HETATM 3548  O   HOH E2003       5.684   1.991 -41.690  1.00 29.36           O  
HETATM 3549  O   HOH E2004       8.006   1.077 -41.662  1.00 36.30           O  
HETATM 3550  O   HOH E2005       6.778   3.341 -40.005  1.00 29.26           O  
HETATM 3551  O   HOH E2006       9.183   1.842 -36.652  1.00 30.64           O  
HETATM 3552  O   HOH E2007       5.100  -1.918 -35.338  1.00 31.27           O  
HETATM 3553  O   HOH E2008       8.645  -2.155 -36.554  1.00 43.93           O  
HETATM 3554  O   HOH E2009       0.104   2.530 -37.959  1.00 33.62           O  
HETATM 3555  O   HOH E2010       0.000   0.000 -36.164  0.50 26.32           O  
HETATM 3556  O   HOH E2011       8.342   2.091 -34.082  1.00 43.89           O  
HETATM 3557  O   HOH E2012       0.393   2.295 -29.878  1.00 30.83           O  
HETATM 3558  O   HOH E2013       2.240  -0.993 -29.043  1.00 31.72           O  
HETATM 3559  O   HOH E2014      12.448   5.466 -36.816  1.00 28.27           O  
HETATM 3560  O   HOH E2015      10.331   3.526 -32.348  1.00 47.95           O  
HETATM 3561  O   HOH E2016      12.393   5.197 -33.259  1.00 37.24           O  
HETATM 3562  O   HOH E2017      11.445   7.268 -29.522  1.00 42.30           O  
HETATM 3563  O   HOH E2018       2.603   2.760 -28.278  1.00 38.95           O  
HETATM 3564  O   HOH E2019      -1.390   4.407 -30.362  1.00 26.37           O  
HETATM 3565  O   HOH E2020      11.154   9.572 -31.114  1.00 24.75           O  
HETATM 3566  O   HOH E2021       5.243  -0.168 -27.227  1.00 28.68           O  
HETATM 3567  O   HOH E2022       5.860  -0.950 -32.987  1.00 28.29           O  
HETATM 3568  O   HOH E2023      12.573   2.714 -29.574  1.00 33.28           O  
HETATM 3569  O   HOH E2024      12.309  -0.056 -26.884  1.00 33.45           O  
HETATM 3570  O   HOH E2025      11.068  -2.830 -26.460  1.00 30.02           O  
HETATM 3571  O   HOH E2026      28.280 -22.397 -56.967  1.00 34.09           O  
CONECT 2904 2905 2906                                                           
CONECT 2905 2904                                                                
CONECT 2906 2904 2907 2908                                                      
CONECT 2907 2906                                                                
CONECT 2908 2906 2909                                                           
CONECT 2909 2908                                                                
CONECT 2910 2911 2912                                                           
CONECT 2911 2910                                                                
CONECT 2912 2910 2913 2914                                                      
CONECT 2913 2912                                                                
CONECT 2914 2912 2915                                                           
CONECT 2915 2914                                                                
MASTER      498    0    2    4   24    0    5    6 3459    5   12   29          
END

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Related entries of code: 4alp

Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code	Check Database	Protein Sequence Similarity
4a75	RCSB PDB PDBbind	90aa, >4A75_1\|Chains... *
4a76	RCSB PDB PDBbind	90aa, >4A76_1\|Chains... at 100%
Complexes with the same small molecule ligand
PDB Code	Check Database	Ligand Name
2kfy	RCSB PDB PDBbind	6-mer
2kg0	RCSB PDB PDBbind	6-mer
2kg1	RCSB PDB PDBbind	6-mer
2kh9	RCSB PDB PDBbind	6-mer
2rqc	RCSB PDB PDBbind	6-mer
4a75	RCSB PDB PDBbind	6-mer
6hyu	RCSB PDB PDBbind	6-mer
6gd3	RCSB PDB PDBbind	6-mer
6g2k	RCSB PDB PDBbind	6-mer
6a2h	RCSB PDB PDBbind	6-mer
6so9	RCSB PDB PDBbind	6-mer

Entry Information

PDB ID	4alp
Complex Type	Protein-Nucleic Acid
PDBbind Subset	general set
Protein Name	Lin28b Cold shock domain
Ligand Name	6-mer
EC.Number	E.C.-.-.-.-
Resolution	1.48(Å)
Affinity (Kd/Ki/IC50)	Kd=2760nM
Release Year	2012
Protein/NA Sequence	Check fasta file
Primary Reference	(2012) Nucleic Acids Res. Vol. 40: pp. 7492

Links to External Databases

RCSB PDB	The mother database
PDBsum	Enhanced annotations on PDB entries
Pubchem	Comprehensive collection of chemical and biological data
UniProtKB AC	UniProt accession number (AC): B4F6I0
Entrez Gene ID	NCBI Entrez Gene ID: 100216028
ASD	Information of known allosteric effects of PDB entries

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