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HEADER    HYDROLASE/HYDROLASE INHIBITOR           30-SEP-11   3U1J              
TITLE     APROTININ BOUND TO DENGUE VIRUS PROTEASE                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE PROTEASE SUBUNIT NS2B;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 1393-1438;                                    
COMPND   5 SYNONYM: FLAVIVIRIN PROTEASE NS2B REGULATORY SUBUNIT, NON-STRUCTURAL 
COMPND   6 PROTEIN 2B;                                                          
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: SERINE PROTEASE NS3;                                       
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 1474-1655;                                    
COMPND  12 SYNONYM: FLAVIVIRIN PROTEASE NS3 CATALYTIC SUBUNIT, NON-STRUCTURAL   
COMPND  13 PROTEIN 3;                                                           
COMPND  14 EC: 3.4.21.91, 3.6.1.15, 3.6.4.13;                                   
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MOL_ID: 3;                                                           
COMPND  17 MOLECULE: PANCREATIC TRYPSIN INHIBITOR;                              
COMPND  18 CHAIN: E;                                                            
COMPND  19 FRAGMENT: UNP RESIDUES 36-93;                                        
COMPND  20 SYNONYM: APROTININ, BASIC PROTEASE INHIBITOR, BPI, BPTI              
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DENGUE VIRUS 3;                                 
SOURCE   3 ORGANISM_COMMON: DENV-3;                                             
SOURCE   4 ORGANISM_TAXID: 408693;                                              
SOURCE   5 STRAIN: SINGAPORE/8120/1995;                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX6P1;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: DENGUE VIRUS 3;                                 
SOURCE  13 ORGANISM_COMMON: DENV-3;                                             
SOURCE  14 ORGANISM_TAXID: 408693;                                              
SOURCE  15 STRAIN: SINGAPORE/8120/1995;                                         
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PGEX6P1;                                  
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  23 ORGANISM_COMMON: BOVINE;                                             
SOURCE  24 ORGANISM_TAXID: 9913                                                 
KEYWDS    SERINE PROTEASE, BOVINE PANCREATIC TRYPSIN INHIBITOR, ER MEMBRANE,    
KEYWDS   2 HYDROLASE-HYDROLASE INHIBITOR COMPLEX                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.G.NOBLE                                                             
REVDAT   2   05-JUN-13 3U1J    1       JRNL                                     
REVDAT   1   09-NOV-11 3U1J    0                                                
JRNL        AUTH   C.G.NOBLE,C.C.SEH,A.T.CHAO,P.Y.SHI                           
JRNL        TITL   LIGAND-BOUND STRUCTURES OF THE DENGUE VIRUS PROTEASE REVEAL  
JRNL        TITL 2 THE ACTIVE CONFORMATION                                      
JRNL        REF    J.VIROL.                      V.  86   438 2012              
JRNL        REFN                   ISSN 0022-538X                               
JRNL        PMID   22031935                                                     
JRNL        DOI    10.1128/JVI.06225-11                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0110                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 24442                          
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) : 0.187                           
REMARK   3   R VALUE            (WORKING SET) : 0.186                           
REMARK   3   FREE R VALUE                     : 0.204                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1312                            
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1771                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.84                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2640                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 93                           
REMARK   3   BIN FREE R VALUE                    : 0.2870                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1856                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 193                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.15                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.76000                                              
REMARK   3    B22 (A**2) : 0.76000                                              
REMARK   3    B33 (A**2) : -1.15000                                             
REMARK   3    B12 (A**2) : 0.38000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.109         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.834         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.949                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1937 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2629 ; 1.263 ; 1.946       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   251 ; 6.076 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    87 ;29.086 ;24.368       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   327 ;16.813 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;12.271 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   279 ; 0.080 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1487 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  1207 ; 0.735 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1943 ; 1.370 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   730 ; 1.948 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   680 ; 3.388 ; 4.500       
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  : 3                                          
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    50        A    69                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.1894 -35.9263 -18.3130              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0273 T22:   0.0847                                     
REMARK   3      T33:   0.0900 T12:   0.0398                                     
REMARK   3      T13:  -0.0108 T23:  -0.0219                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4224 L22:   3.2029                                     
REMARK   3      L33:   5.5891 L12:   1.6665                                     
REMARK   3      L13:  -2.8256 L23:  -2.7968                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0583 S12:   0.2081 S13:  -0.5347                       
REMARK   3      S21:  -0.0785 S22:  -0.2758 S23:  -0.3397                       
REMARK   3      S31:   0.1609 S32:   0.3120 S33:   0.2174                       
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     6        B   171                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.4181 -29.4386 -12.1281              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0295 T22:   0.0491                                     
REMARK   3      T33:   0.0222 T12:   0.0254                                     
REMARK   3      T13:  -0.0074 T23:  -0.0056                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7698 L22:   0.2506                                     
REMARK   3      L33:   1.0470 L12:  -0.2567                                     
REMARK   3      L13:  -0.3534 L23:  -0.0100                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0082 S12:   0.0146 S13:  -0.0340                       
REMARK   3      S21:  -0.0051 S22:  -0.0199 S23:  -0.0361                       
REMARK   3      S31:  -0.0391 S32:   0.0576 S33:   0.0117                       
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 :   E     1        E    56                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.7126 -35.4404 -21.3030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0644 T22:   0.1549                                     
REMARK   3      T33:   0.0949 T12:   0.0579                                     
REMARK   3      T13:  -0.0703 T23:  -0.0534                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1616 L22:   2.7836                                     
REMARK   3      L33:   2.0048 L12:   2.9814                                     
REMARK   3      L13:   2.4210 L23:   0.4123                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0490 S12:  -0.0965 S13:   0.1089                       
REMARK   3      S21:  -0.1799 S22:  -0.0313 S23:   0.3580                       
REMARK   3      S31:  -0.0093 S32:  -0.3280 S33:  -0.0177                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3U1J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-OCT-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB068188.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-APR-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25786                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.100                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2IJO                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH 6.5, 30% PEG 4000, VAPOR     
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3860 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 217  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 261  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    45                                                      
REMARK 465     PRO A    46                                                      
REMARK 465     LEU A    47                                                      
REMARK 465     GLY A    48                                                      
REMARK 465     SER A    49                                                      
REMARK 465     VAL A    70                                                      
REMARK 465     SER A    71                                                      
REMARK 465     HIS A    72                                                      
REMARK 465     ASN A    73                                                      
REMARK 465     LEU A    74                                                      
REMARK 465     MET A    75                                                      
REMARK 465     ILE A    76                                                      
REMARK 465     THR A    77                                                      
REMARK 465     VAL A    78                                                      
REMARK 465     ASP A    79                                                      
REMARK 465     ASP A    80                                                      
REMARK 465     ASP A    81                                                      
REMARK 465     GLY A    82                                                      
REMARK 465     THR A    83                                                      
REMARK 465     MET A    84                                                      
REMARK 465     ARG A    85                                                      
REMARK 465     ILE A    86                                                      
REMARK 465     LYS A    87                                                      
REMARK 465     ASP A    88                                                      
REMARK 465     ASP A    89                                                      
REMARK 465     GLU A    90                                                      
REMARK 465     THR A    91                                                      
REMARK 465     GLU A    92                                                      
REMARK 465     ASN A    93                                                      
REMARK 465     ILE A    94                                                      
REMARK 465     LEU A    95                                                      
REMARK 465     GLY B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     GLY B    -6                                                      
REMARK 465     GLY B    -5                                                      
REMARK 465     SER B    -4                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     SER B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     VAL B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     TRP B     5                                                      
REMARK 465     PRO B   172                                                      
REMARK 465     ASP B   173                                                      
REMARK 465     GLY B   174                                                      
REMARK 465     PRO B   175                                                      
REMARK 465     THR B   176                                                      
REMARK 465     PRO B   177                                                      
REMARK 465     GLU B   178                                                      
REMARK 465     LEU B   179                                                      
REMARK 465     GLU B   180                                                      
REMARK 465     GLU B   181                                                      
REMARK 465     GLU B   182                                                      
REMARK 465     GLY E    57                                                      
REMARK 465     ALA E    58                                                      
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     ASP B   6    CG   OD1  OD2                                       
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    PHE B  31       -7.31     79.14                                   
REMARK 500    THR B 120      -73.83    -65.29                                   
REMARK 500    ASN E  44      107.50   -166.07                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3U1I   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 AUTHOR STATED THE SEQUENCE CONFLICT OF I115T (UNP RESIDUE NUMBER     
REMARK 999 1588) WAS A NATURALLY OCCURRING DIFFERENCE.                          
DBREF  3U1J A   50    95  UNP    Q5UB51   POLG_DEN3I    1393   1438             
DBREF  3U1J B    1   182  UNP    Q5UB51   POLG_DEN3I    1474   1655             
DBREF  3U1J E    1    58  UNP    P00974   BPT1_BOVIN      36     93             
SEQADV 3U1J GLY A   45  UNP  Q5UB51              EXPRESSION TAG                 
SEQADV 3U1J PRO A   46  UNP  Q5UB51              EXPRESSION TAG                 
SEQADV 3U1J LEU A   47  UNP  Q5UB51              EXPRESSION TAG                 
SEQADV 3U1J GLY A   48  UNP  Q5UB51              EXPRESSION TAG                 
SEQADV 3U1J SER A   49  UNP  Q5UB51              EXPRESSION TAG                 
SEQADV 3U1J GLY B   -8  UNP  Q5UB51              EXPRESSION TAG                 
SEQADV 3U1J GLY B   -7  UNP  Q5UB51              EXPRESSION TAG                 
SEQADV 3U1J GLY B   -6  UNP  Q5UB51              EXPRESSION TAG                 
SEQADV 3U1J GLY B   -5  UNP  Q5UB51              EXPRESSION TAG                 
SEQADV 3U1J SER B   -4  UNP  Q5UB51              EXPRESSION TAG                 
SEQADV 3U1J GLY B   -3  UNP  Q5UB51              EXPRESSION TAG                 
SEQADV 3U1J GLY B   -2  UNP  Q5UB51              EXPRESSION TAG                 
SEQADV 3U1J GLY B   -1  UNP  Q5UB51              EXPRESSION TAG                 
SEQADV 3U1J GLY B    0  UNP  Q5UB51              EXPRESSION TAG                 
SEQADV 3U1J THR B  115  UNP  Q5UB51    ILE  1588 SEE REMARK 999                 
SEQRES   1 A   51  GLY PRO LEU GLY SER ASP LEU THR VAL GLU LYS ALA ALA          
SEQRES   2 A   51  ASP VAL THR TRP GLU GLU GLU ALA GLU GLN THR GLY VAL          
SEQRES   3 A   51  SER HIS ASN LEU MET ILE THR VAL ASP ASP ASP GLY THR          
SEQRES   4 A   51  MET ARG ILE LYS ASP ASP GLU THR GLU ASN ILE LEU              
SEQRES   1 B  191  GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLY VAL LEU          
SEQRES   2 B  191  TRP ASP VAL PRO SER PRO PRO GLU THR GLN LYS ALA GLU          
SEQRES   3 B  191  LEU GLU GLU GLY VAL TYR ARG ILE LYS GLN GLN GLY ILE          
SEQRES   4 B  191  PHE GLY LYS THR GLN VAL GLY VAL GLY VAL GLN LYS GLU          
SEQRES   5 B  191  GLY VAL PHE HIS THR MET TRP HIS VAL THR ARG GLY ALA          
SEQRES   6 B  191  VAL LEU THR HIS ASN GLY LYS ARG LEU GLU PRO ASN TRP          
SEQRES   7 B  191  ALA SER VAL LYS LYS ASP LEU ILE SER TYR GLY GLY GLY          
SEQRES   8 B  191  TRP ARG LEU SER ALA GLN TRP GLN LYS GLY GLU GLU VAL          
SEQRES   9 B  191  GLN VAL ILE ALA VAL GLU PRO GLY LYS ASN PRO LYS ASN          
SEQRES  10 B  191  PHE GLN THR MET PRO GLY THR PHE GLN THR THR THR GLY          
SEQRES  11 B  191  GLU ILE GLY ALA ILE ALA LEU ASP PHE LYS PRO GLY THR          
SEQRES  12 B  191  SER GLY SER PRO ILE ILE ASN ARG GLU GLY LYS VAL VAL          
SEQRES  13 B  191  GLY LEU TYR GLY ASN GLY VAL VAL THR LYS ASN GLY GLY          
SEQRES  14 B  191  TYR VAL SER GLY ILE ALA GLN THR ASN ALA GLU PRO ASP          
SEQRES  15 B  191  GLY PRO THR PRO GLU LEU GLU GLU GLU                          
SEQRES   1 E   58  ARG PRO ASP PHE CYS LEU GLU PRO PRO TYR THR GLY PRO          
SEQRES   2 E   58  CYS LYS ALA ARG ILE ILE ARG TYR PHE TYR ASN ALA LYS          
SEQRES   3 E   58  ALA GLY LEU CYS GLN THR PHE VAL TYR GLY GLY CYS ARG          
SEQRES   4 E   58  ALA LYS ARG ASN ASN PHE LYS SER ALA GLU ASP CYS MET          
SEQRES   5 E   58  ARG THR CYS GLY GLY ALA                                      
FORMUL   4  HOH   *193(H2 O)                                                    
HELIX    1   1 TRP B   50  ARG B   54  1                                   5    
HELIX    2   2 PRO E    2  GLU E    7  5                                   6    
HELIX    3   3 SER E   47  GLY E   56  1                                  10    
SHEET    1   A 6 LEU A  51  ALA A  57  0                                        
SHEET    2   A 6 GLY B  21  GLY B  29 -1  O  VAL B  22   N  ALA A  57           
SHEET    3   A 6 GLY B  32  LYS B  42 -1  O  GLN B  41   N  GLY B  21           
SHEET    4   A 6 VAL B  45  MET B  49 -1  O  HIS B  47   N  VAL B  40           
SHEET    5   A 6 LEU B  76  TYR B  79 -1  O  TYR B  79   N  PHE B  46           
SHEET    6   A 6 PRO B  67  SER B  71 -1  N  TRP B  69   O  SER B  78           
SHEET    1   B 5 GLU A  66  GLY A  69  0                                        
SHEET    2   B 5 LYS B 107  THR B 111  1  O  GLN B 110   N  GLU A  66           
SHEET    3   B 5 VAL B  95  ALA B  99 -1  N  VAL B  97   O  PHE B 109           
SHEET    4   B 5 PRO B 138  ILE B 140 -1  O  ILE B 140   N  GLN B  96           
SHEET    5   B 5 VAL B 146  LEU B 149 -1  O  GLY B 148   N  ILE B 139           
SHEET    1   C 2 LEU B  58  HIS B  60  0                                        
SHEET    2   C 2 LYS B  63  LEU B  65 -1  O  LEU B  65   N  LEU B  58           
SHEET    1   D 4 GLY B 114  GLN B 117  0                                        
SHEET    2   D 4 GLU B 122  ILE B 126 -1  O  ILE B 123   N  PHE B 116           
SHEET    3   D 4 TYR B 161  GLY B 164 -1  O  SER B 163   N  ILE B 126           
SHEET    4   D 4 GLY B 153  VAL B 155 -1  N  VAL B 154   O  VAL B 162           
SHEET    1   E 2 ILE E  18  ASN E  24  0                                        
SHEET    2   E 2 LEU E  29  TYR E  35 -1  O  TYR E  35   N  ILE E  18           
SSBOND   1 CYS E    5    CYS E   55                          1555   1555  2.04  
SSBOND   2 CYS E   14    CYS E   38                          1555   1555  2.04  
SSBOND   3 CYS E   30    CYS E   51                          1555   1555  2.04  
CISPEP   1 GLN A   67    THR A   68          0         3.99                     
CISPEP   2 ARG E    1    PRO E    2          0        18.48                     
CRYST1   84.789   84.789   66.031  90.00  90.00 120.00 P 3 2 1       6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011794  0.006809  0.000000        0.00000                         
SCALE2      0.000000  0.013618  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015144        0.00000                         
ATOM      1  N   ASP A  50     -18.811 -42.183  -4.296  1.00 38.25           N  
ANISOU    1  N   ASP A  50     4248   4777   5505   -603    425   1067       N  
ATOM      2  CA  ASP A  50     -17.362 -42.155  -3.915  1.00 36.50           C  
ANISOU    2  CA  ASP A  50     4269   4374   5225   -579    356    965       C  
ATOM      3  C   ASP A  50     -16.469 -42.310  -5.128  1.00 34.35           C  
ANISOU    3  C   ASP A  50     3995   4045   5009   -578    197    786       C  
ATOM      4  O   ASP A  50     -16.655 -43.199  -5.959  1.00 35.71           O  
ANISOU    4  O   ASP A  50     4065   4190   5310   -695     99    709       O  
ATOM      5  CB  ASP A  50     -17.026 -43.268  -2.925  1.00 37.86           C  
ANISOU    5  CB  ASP A  50     4518   4404   5462   -698    318   1059       C  
ATOM      6  CG  ASP A  50     -17.622 -43.041  -1.544  1.00 39.91           C  
ANISOU    6  CG  ASP A  50     4842   4717   5605   -703    482   1231       C  
ATOM      7  OD1 ASP A  50     -17.609 -44.006  -0.760  1.00 43.52           O  
ANISOU    7  OD1 ASP A  50     5315   5097   6121   -808    463   1358       O  
ATOM      8  OD2 ASP A  50     -18.089 -41.922  -1.236  1.00 41.01           O  
ANISOU    8  OD2 ASP A  50     5031   4956   5594   -595    658   1249       O  
ATOM      9  N   LEU A  51     -15.466 -41.459  -5.202  1.00 31.27           N  
ANISOU    9  N   LEU A  51     3743   3628   4508   -474    188    710       N  
ATOM     10  CA  LEU A  51     -14.597 -41.452  -6.347  1.00 28.35           C  
ANISOU   10  CA  LEU A  51     3369   3227   4174   -447     69    555       C  
ATOM     11  C   LEU A  51     -13.348 -42.263  -6.059  1.00 26.84           C  
ANISOU   11  C   LEU A  51     3269   2870   4056   -480    -24    547       C  
ATOM     12  O   LEU A  51     -12.962 -42.414  -4.909  1.00 27.05           O  
ANISOU   12  O   LEU A  51     3381   2857   4037   -504    -12    676       O  
ATOM     13  CB  LEU A  51     -14.259 -40.011  -6.684  1.00 27.34           C  
ANISOU   13  CB  LEU A  51     3310   3178   3898   -314    132    508       C  
ATOM     14  CG  LEU A  51     -15.537 -39.251  -7.046  1.00 28.76           C  
ANISOU   14  CG  LEU A  51     3358   3520   4048   -225    263    585       C  
ATOM     15  CD1 LEU A  51     -15.288 -37.791  -7.203  1.00 28.41           C  
ANISOU   15  CD1 LEU A  51     3422   3490   3880    -70    400    578       C  
ATOM     16  CD2 LEU A  51     -16.063 -39.795  -8.323  1.00 29.77           C  
ANISOU   16  CD2 LEU A  51     3271   3781   4260   -287    146    540       C  
ATOM     17  N   THR A  52     -12.740 -42.814  -7.101  1.00 24.74           N  
ANISOU   17  N   THR A  52     2976   2524   3900   -479   -100    421       N  
ATOM     18  CA  THR A  52     -11.420 -43.424  -6.951  1.00 23.79           C  
ANISOU   18  CA  THR A  52     2914   2255   3867   -439   -148    452       C  
ATOM     19  C   THR A  52     -10.435 -42.762  -7.898  1.00 22.73           C  
ANISOU   19  C   THR A  52     2789   2164   3680   -345   -190    331       C  
ATOM     20  O   THR A  52     -10.830 -42.004  -8.799  1.00 21.18           O  
ANISOU   20  O   THR A  52     2562   2084   3400   -324   -187    205       O  
ATOM     21  CB  THR A  52     -11.451 -44.943  -7.199  1.00 25.54           C  
ANISOU   21  CB  THR A  52     3128   2254   4320   -501   -123    442       C  
ATOM     22  OG1 THR A  52     -11.998 -45.199  -8.497  1.00 24.26           O  
ANISOU   22  OG1 THR A  52     2937   2084   4196   -582   -118    227       O  
ATOM     23  CG2 THR A  52     -12.294 -45.638  -6.137  1.00 26.48           C  
ANISOU   23  CG2 THR A  52     3241   2318   4502   -603    -77    604       C  
ATOM     24  N   VAL A  53      -9.147 -43.020  -7.682  1.00 22.70           N  
ANISOU   24  N   VAL A  53     2802   2096   3724   -281   -225    413       N  
ATOM     25  CA  VAL A  53      -8.118 -42.432  -8.522  1.00 22.59           C  
ANISOU   25  CA  VAL A  53     2777   2134   3669   -196   -257    331       C  
ATOM     26  C   VAL A  53      -7.117 -43.469  -8.996  1.00 24.39           C  
ANISOU   26  C   VAL A  53     2967   2199   4098   -104   -228    358       C  
ATOM     27  O   VAL A  53      -6.918 -44.513  -8.350  1.00 25.50           O  
ANISOU   27  O   VAL A  53     3095   2192   4399    -83   -190    520       O  
ATOM     28  CB  VAL A  53      -7.367 -41.229  -7.850  1.00 21.94           C  
ANISOU   28  CB  VAL A  53     2737   2216   3384   -210   -310    424       C  
ATOM     29  CG1 VAL A  53      -8.338 -40.058  -7.572  1.00 20.94           C  
ANISOU   29  CG1 VAL A  53     2700   2187   3070   -262   -252    361       C  
ATOM     30  CG2 VAL A  53      -6.629 -41.669  -6.574  1.00 23.73           C  
ANISOU   30  CG2 VAL A  53     2947   2470   3597   -259   -368    673       C  
ATOM     31  N   GLU A  54      -6.504 -43.187 -10.138  1.00 24.15           N  
ANISOU   31  N   GLU A  54     2923   2184   4067    -29   -212    219       N  
ATOM     32  CA  GLU A  54      -5.434 -44.050 -10.640  1.00 26.57           C  
ANISOU   32  CA  GLU A  54     3200   2332   4563    101   -127    254       C  
ATOM     33  C   GLU A  54      -4.387 -43.213 -11.361  1.00 24.59           C  
ANISOU   33  C   GLU A  54     2892   2222   4226    190   -151    225       C  
ATOM     34  O   GLU A  54      -4.714 -42.394 -12.226  1.00 22.47           O  
ANISOU   34  O   GLU A  54     2652   2066   3816    155   -171     38       O  
ATOM     35  CB  GLU A  54      -5.983 -45.192 -11.510  1.00 28.70           C  
ANISOU   35  CB  GLU A  54     3558   2351   4993     73     12     53       C  
ATOM     36  CG  GLU A  54      -6.495 -44.813 -12.894  1.00 33.10           C  
ANISOU   36  CG  GLU A  54     4166   2983   5425     -8     22   -246       C  
ATOM     37  CD  GLU A  54      -6.835 -46.029 -13.753  1.00 40.51           C  
ANISOU   37  CD  GLU A  54     5236   3668   6486    -97    179   -466       C  
ATOM     38  OE1 GLU A  54      -6.103 -46.281 -14.745  1.00 44.30           O  
ANISOU   38  OE1 GLU A  54     5780   4051   6998    -21    306   -609       O  
ATOM     39  OE2 GLU A  54      -7.821 -46.744 -13.432  1.00 44.11           O  
ANISOU   39  OE2 GLU A  54     5750   4011   6998   -265    197   -504       O  
ATOM     40  N   LYS A  55      -3.126 -43.421 -10.993  1.00 25.73           N  
ANISOU   40  N   LYS A  55     2929   2386   4459    305   -146    453       N  
ATOM     41  CA  LYS A  55      -2.055 -42.606 -11.545  1.00 24.56           C  
ANISOU   41  CA  LYS A  55     2695   2407   4229    367   -177    477       C  
ATOM     42  C   LYS A  55      -1.924 -42.855 -13.042  1.00 25.05           C  
ANISOU   42  C   LYS A  55     2799   2359   4357    466    -37    240       C  
ATOM     43  O   LYS A  55      -2.041 -43.999 -13.509  1.00 25.83           O  
ANISOU   43  O   LYS A  55     2963   2208   4641    543    129    155       O  
ATOM     44  CB  LYS A  55      -0.720 -42.845 -10.834  1.00 27.21           C  
ANISOU   44  CB  LYS A  55     2844   2845   4647    456   -209    830       C  
ATOM     45  CG  LYS A  55       0.349 -41.860 -11.290  1.00 27.25           C  
ANISOU   45  CG  LYS A  55     2737   3083   4532    457   -270    878       C  
ATOM     46  CD  LYS A  55       1.486 -41.708 -10.316  1.00 32.48           C  
ANISOU   46  CD  LYS A  55     3188   3993   5157    417   -393   1259       C  
ATOM     47  CE  LYS A  55       2.551 -40.819 -10.943  1.00 32.17           C  
ANISOU   47  CE  LYS A  55     3025   4173   5025    402   -431   1295       C  
ATOM     48  NZ  LYS A  55       3.741 -40.742 -10.080  1.00 37.91           N  
ANISOU   48  NZ  LYS A  55     3489   5201   5710    334   -564   1705       N  
ATOM     49  N   ALA A  56      -1.697 -41.775 -13.781  1.00 22.95           N  
ANISOU   49  N   ALA A  56     2526   2269   3923    442    -83    128       N  
ATOM     50  CA  ALA A  56      -1.593 -41.848 -15.235  1.00 24.11           C  
ANISOU   50  CA  ALA A  56     2718   2376   4064    506     35    -98       C  
ATOM     51  C   ALA A  56      -0.302 -41.258 -15.784  1.00 24.46           C  
ANISOU   51  C   ALA A  56     2647   2560   4085    613     62    -10       C  
ATOM     52  O   ALA A  56       0.186 -41.711 -16.809  1.00 25.90           O  
ANISOU   52  O   ALA A  56     2840   2661   4337    731    225   -115       O  
ATOM     53  CB  ALA A  56      -2.792 -41.180 -15.882  1.00 22.37           C  
ANISOU   53  CB  ALA A  56     2592   2254   3652    370    -23   -326       C  
ATOM     54  N   ALA A  57       0.241 -40.242 -15.114  1.00 23.81           N  
ANISOU   54  N   ALA A  57     2470   2687   3888    545    -79    170       N  
ATOM     55  CA  ALA A  57       1.420 -39.522 -15.610  1.00 24.86           C  
ANISOU   55  CA  ALA A  57     2478   2995   3971    589    -77    266       C  
ATOM     56  C   ALA A  57       2.142 -38.770 -14.502  1.00 25.11           C  
ANISOU   56  C   ALA A  57     2395   3237   3908    453   -238    528       C  
ATOM     57  O   ALA A  57       1.596 -38.564 -13.410  1.00 24.29           O  
ANISOU   57  O   ALA A  57     2358   3153   3715    300   -351    583       O  
ATOM     58  CB  ALA A  57       1.036 -38.544 -16.731  1.00 23.61           C  
ANISOU   58  CB  ALA A  57     2411   2922   3637    544    -65     45       C  
ATOM     59  N   ASP A  58       3.390 -38.401 -14.782  1.00 26.41           N  
ANISOU   59  N   ASP A  58     2383   3575   4074    482   -238    696       N  
ATOM     60  CA  ASP A  58       4.116 -37.455 -13.949  1.00 26.77           C  
ANISOU   60  CA  ASP A  58     2335   3878   3958    260   -406    903       C  
ATOM     61  C   ASP A  58       4.081 -36.096 -14.608  1.00 24.84           C  
ANISOU   61  C   ASP A  58     2204   3710   3522    124   -415    738       C  
ATOM     62  O   ASP A  58       3.780 -35.976 -15.797  1.00 24.33           O  
ANISOU   62  O   ASP A  58     2207   3562   3475    252   -297    544       O  
ATOM     63  CB  ASP A  58       5.554 -37.919 -13.702  1.00 30.45           C  
ANISOU   63  CB  ASP A  58     2479   4543   4546    339   -420   1271       C  
ATOM     64  CG  ASP A  58       5.622 -39.035 -12.684  1.00 34.58           C  
ANISOU   64  CG  ASP A  58     2875   5042   5218    421   -446   1539       C  
ATOM     65  OD1 ASP A  58       5.103 -38.871 -11.548  1.00 36.95           O  
ANISOU   65  OD1 ASP A  58     3262   5396   5379    212   -597   1584       O  
ATOM     66  OD2 ASP A  58       6.183 -40.091 -13.018  1.00 40.70           O  
ANISOU   66  OD2 ASP A  58     3478   5730   6255    706   -284   1715       O  
ATOM     67  N   VAL A  59       4.336 -35.057 -13.827  1.00 23.87           N  
ANISOU   67  N   VAL A  59     2131   3738   3198   -159   -541    812       N  
ATOM     68  CA  VAL A  59       4.268 -33.702 -14.363  1.00 22.60           C  
ANISOU   68  CA  VAL A  59     2122   3593   2869   -301   -511    669       C  
ATOM     69  C   VAL A  59       5.623 -33.329 -14.971  1.00 23.65           C  
ANISOU   69  C   VAL A  59     2043   3933   3007   -328   -514    827       C  
ATOM     70  O   VAL A  59       6.616 -33.165 -14.253  1.00 25.14           O  
ANISOU   70  O   VAL A  59     2064   4355   3130   -533   -638   1068       O  
ATOM     71  CB  VAL A  59       3.834 -32.688 -13.283  1.00 22.66           C  
ANISOU   71  CB  VAL A  59     2366   3594   2648   -621   -576    623       C  
ATOM     72  CG1 VAL A  59       3.846 -31.251 -13.840  1.00 22.98           C  
ANISOU   72  CG1 VAL A  59     2589   3596   2544   -760   -489    502       C  
ATOM     73  CG2 VAL A  59       2.444 -33.072 -12.736  1.00 21.44           C  
ANISOU   73  CG2 VAL A  59     2397   3242   2504   -556   -537    486       C  
ATOM     74  N   THR A  60       5.648 -33.218 -16.303  1.00 23.06           N  
ANISOU   74  N   THR A  60     1958   3808   2992   -138   -380    710       N  
ATOM     75  CA  THR A  60       6.869 -32.897 -17.032  1.00 25.52           C  
ANISOU   75  CA  THR A  60     2065   4307   3322   -126   -342    852       C  
ATOM     76  C   THR A  60       6.544 -32.128 -18.294  1.00 23.64           C  
ANISOU   76  C   THR A  60     1958   4005   3018    -57   -216    666       C  
ATOM     77  O   THR A  60       5.584 -32.444 -18.976  1.00 21.81           O  
ANISOU   77  O   THR A  60     1857   3621   2808    117   -127    465       O  
ATOM     78  CB  THR A  60       7.636 -34.157 -17.503  1.00 27.14           C  
ANISOU   78  CB  THR A  60     1995   4560   3756    168   -243   1010       C  
ATOM     79  OG1 THR A  60       7.408 -35.244 -16.586  1.00 30.99           O  
ANISOU   79  OG1 THR A  60     2425   4978   4370    248   -287   1119       O  
ATOM     80  CG2 THR A  60       9.136 -33.839 -17.631  1.00 30.53           C  
ANISOU   80  CG2 THR A  60     2115   5284   4200    106   -261   1310       C  
ATOM     81  N   TRP A  61       7.363 -31.126 -18.583  1.00 24.67           N  
ANISOU   81  N   TRP A  61     2037   4282   3054   -224   -218    761       N  
ATOM     82  CA  TRP A  61       7.385 -30.478 -19.884  1.00 25.01           C  
ANISOU   82  CA  TRP A  61     2126   4323   3053   -134    -85    673       C  
ATOM     83  C   TRP A  61       8.133 -31.382 -20.865  1.00 27.20           C  
ANISOU   83  C   TRP A  61     2166   4700   3468    136     35    737       C  
ATOM     84  O   TRP A  61       9.253 -31.820 -20.579  1.00 28.20           O  
ANISOU   84  O   TRP A  61     2022   4997   3695    148     18    974       O  
ATOM     85  CB  TRP A  61       8.082 -29.125 -19.769  1.00 25.87           C  
ANISOU   85  CB  TRP A  61     2266   4535   3026   -435   -110    775       C  
ATOM     86  CG  TRP A  61       8.198 -28.350 -21.053  1.00 26.54           C  
ANISOU   86  CG  TRP A  61     2388   4631   3063   -364     30    738       C  
ATOM     87  CD1 TRP A  61       9.137 -28.515 -22.038  1.00 28.39           C  
ANISOU   87  CD1 TRP A  61     2397   5040   3347   -239    117    847       C  
ATOM     88  CD2 TRP A  61       7.368 -27.265 -21.468  1.00 25.08           C  
ANISOU   88  CD2 TRP A  61     2471   4285   2772   -403    124    622       C  
ATOM     89  NE1 TRP A  61       8.929 -27.601 -23.050  1.00 27.78           N  
ANISOU   89  NE1 TRP A  61     2440   4936   3179   -221    237    793       N  
ATOM     90  CE2 TRP A  61       7.849 -26.823 -22.723  1.00 26.54           C  
ANISOU   90  CE2 TRP A  61     2577   4572   2935   -311    243    674       C  
ATOM     91  CE3 TRP A  61       6.252 -26.625 -20.904  1.00 24.66           C  
ANISOU   91  CE3 TRP A  61     2711   4007   2650   -480    150    509       C  
ATOM     92  CZ2 TRP A  61       7.258 -25.758 -23.423  1.00 26.68           C  
ANISOU   92  CZ2 TRP A  61     2786   4484   2865   -298    367    642       C  
ATOM     93  CZ3 TRP A  61       5.674 -25.559 -21.596  1.00 25.16           C  
ANISOU   93  CZ3 TRP A  61     2961   3948   2651   -442    301    486       C  
ATOM     94  CH2 TRP A  61       6.170 -25.147 -22.843  1.00 25.11           C  
ANISOU   94  CH2 TRP A  61     2857   4056   2625   -351    398    563       C  
ATOM     95  N   GLU A  62       7.504 -31.664 -22.004  1.00 27.87           N  
ANISOU   95  N   GLU A  62     2349   4695   3545    347    172    543       N  
ATOM     96  CA  GLU A  62       8.091 -32.533 -23.026  1.00 31.23           C  
ANISOU   96  CA  GLU A  62     2632   5166   4067    599    350    537       C  
ATOM     97  C   GLU A  62       8.658 -31.673 -24.157  1.00 33.01           C  
ANISOU   97  C   GLU A  62     2816   5542   4184    596    455    567       C  
ATOM     98  O   GLU A  62       7.925 -30.906 -24.773  1.00 31.59           O  
ANISOU   98  O   GLU A  62     2811   5339   3852    549    463    440       O  
ATOM     99  CB  GLU A  62       7.036 -33.516 -23.570  1.00 30.98           C  
ANISOU   99  CB  GLU A  62     2766   4955   4049    772    443    273       C  
ATOM    100  CG  GLU A  62       6.467 -34.525 -22.543  1.00 33.12           C  
ANISOU  100  CG  GLU A  62     3078   5051   4452    796    377    244       C  
ATOM    101  CD  GLU A  62       7.373 -35.736 -22.287  1.00 38.78           C  
ANISOU  101  CD  GLU A  62     3609   5724   5400    989    503    401       C  
ATOM    102  OE1 GLU A  62       8.450 -35.843 -22.914  1.00 42.37           O  
ANISOU  102  OE1 GLU A  62     3888   6287   5923   1126    660    531       O  
ATOM    103  OE2 GLU A  62       7.006 -36.594 -21.450  1.00 40.91           O  
ANISOU  103  OE2 GLU A  62     3898   5846   5799   1025    470    423       O  
ATOM    104  N   GLU A  63       9.959 -31.787 -24.429  1.00 36.89           N  
ANISOU  104  N   GLU A  63     3052   6204   4758    656    545    776       N  
ATOM    105  CA  GLU A  63      10.578 -30.981 -25.488  1.00 40.23           C  
ANISOU  105  CA  GLU A  63     3415   6787   5082    645    658    833       C  
ATOM    106  C   GLU A  63      10.035 -31.269 -26.889  1.00 41.30           C  
ANISOU  106  C   GLU A  63     3694   6885   5112    838    845    604       C  
ATOM    107  O   GLU A  63      10.089 -30.406 -27.771  1.00 41.83           O  
ANISOU  107  O   GLU A  63     3801   7061   5031    795    902    605       O  
ATOM    108  CB  GLU A  63      12.112 -31.067 -25.470  1.00 43.33           C  
ANISOU  108  CB  GLU A  63     3459   7411   5592    667    726   1145       C  
ATOM    109  CG  GLU A  63      12.739 -30.229 -24.360  1.00 46.08           C  
ANISOU  109  CG  GLU A  63     3671   7916   5919    326    509   1394       C  
ATOM    110  CD  GLU A  63      13.924 -29.393 -24.825  1.00 51.80           C  
ANISOU  110  CD  GLU A  63     4169   8906   6605    182    552   1635       C  
ATOM    111  OE1 GLU A  63      15.016 -29.959 -25.063  1.00 53.74           O  
ANISOU  111  OE1 GLU A  63     4071   9360   6986    338    665   1887       O  
ATOM    112  OE2 GLU A  63      13.763 -28.154 -24.932  1.00 53.26           O  
ANISOU  112  OE2 GLU A  63     4518   9082   6636    -86    496   1596       O  
ATOM    113  N   GLU A  64       9.523 -32.480 -27.096  1.00 42.80           N  
ANISOU  113  N   GLU A  64     3971   6931   5360   1021    945    413       N  
ATOM    114  CA  GLU A  64       8.840 -32.792 -28.351  1.00 44.51           C  
ANISOU  114  CA  GLU A  64     4371   7129   5410   1116   1092    150       C  
ATOM    115  C   GLU A  64       7.357 -33.113 -28.144  1.00 43.10           C  
ANISOU  115  C   GLU A  64     4421   6807   5146   1048    970    -85       C  
ATOM    116  O   GLU A  64       6.838 -34.114 -28.637  1.00 44.23           O  
ANISOU  116  O   GLU A  64     4695   6853   5255   1120   1082   -316       O  
ATOM    117  CB  GLU A  64       9.593 -33.837 -29.201  1.00 47.84           C  
ANISOU  117  CB  GLU A  64     4740   7539   5897   1347   1400     88       C  
ATOM    118  CG  GLU A  64      10.174 -35.031 -28.449  1.00 51.39           C  
ANISOU  118  CG  GLU A  64     5069   7823   6633   1525   1516    184       C  
ATOM    119  CD  GLU A  64       9.260 -36.253 -28.448  1.00 53.92           C  
ANISOU  119  CD  GLU A  64     5630   7869   6986   1590   1609   -106       C  
ATOM    120  OE1 GLU A  64       9.768 -37.367 -28.186  1.00 57.59           O  
ANISOU  120  OE1 GLU A  64     6046   8151   7683   1796   1825    -57       O  
ATOM    121  OE2 GLU A  64       8.045 -36.114 -28.713  1.00 52.73           O  
ANISOU  121  OE2 GLU A  64     5708   7687   6640   1436   1485   -356       O  
ATOM    122  N   ALA A  65       6.679 -32.238 -27.406  1.00 41.23           N  
ANISOU  122  N   ALA A  65     4240   6555   4870    890    763    -23       N  
ATOM    123  CA  ALA A  65       5.233 -32.285 -27.301  1.00 40.14           C  
ANISOU  123  CA  ALA A  65     4274   6343   4631    827    653   -184       C  
ATOM    124  C   ALA A  65       4.616 -31.965 -28.655  1.00 41.34           C  
ANISOU  124  C   ALA A  65     4509   6662   4536    829    710   -293       C  
ATOM    125  O   ALA A  65       5.264 -31.375 -29.523  1.00 42.11           O  
ANISOU  125  O   ALA A  65     4550   6918   4531    856    809   -212       O  
ATOM    126  CB  ALA A  65       4.750 -31.288 -26.270  1.00 37.87           C  
ANISOU  126  CB  ALA A  65     4029   5998   4358    689    488    -59       C  
ATOM    127  N   GLU A  66       3.357 -32.345 -28.822  1.00 41.78           N  
ANISOU  127  N   GLU A  66     4676   6718   4480    780    639   -448       N  
ATOM    128  CA  GLU A  66       2.621 -32.003 -30.019  1.00 43.99           C  
ANISOU  128  CA  GLU A  66     5001   7228   4484    738    642   -502       C  
ATOM    129  C   GLU A  66       2.378 -30.493 -30.120  1.00 44.24           C  
ANISOU  129  C   GLU A  66     4989   7380   4438    728    581   -255       C  
ATOM    130  O   GLU A  66       1.801 -29.868 -29.222  1.00 41.65           O  
ANISOU  130  O   GLU A  66     4679   6940   4203    704    487   -134       O  
ATOM    131  CB  GLU A  66       1.303 -32.774 -30.074  1.00 44.39           C  
ANISOU  131  CB  GLU A  66     5139   7296   4430    640    550   -683       C  
ATOM    132  CG  GLU A  66       0.488 -32.493 -31.327  1.00 47.62           C  
ANISOU  132  CG  GLU A  66     5556   8031   4506    549    518   -708       C  
ATOM    133  CD  GLU A  66      -0.089 -33.747 -31.936  1.00 51.19           C  
ANISOU  133  CD  GLU A  66     6125   8540   4783    398    542  -1010       C  
ATOM    134  OE1 GLU A  66       0.698 -34.676 -32.247  1.00 54.06           O  
ANISOU  134  OE1 GLU A  66     6598   8761   5179    418    731  -1227       O  
ATOM    135  OE2 GLU A  66      -1.324 -33.795 -32.116  1.00 52.40           O  
ANISOU  135  OE2 GLU A  66     6263   8881   4763    249    393  -1018       O  
ATOM    136  N   GLN A  67       2.873 -29.914 -31.209  1.00 47.10           N  
ANISOU  136  N   GLN A  67     5312   7943   4638    755    677   -174       N  
ATOM    137  CA  GLN A  67       2.485 -28.578 -31.629  1.00 49.21           C  
ANISOU  137  CA  GLN A  67     5554   8350   4790    760    662     65       C  
ATOM    138  C   GLN A  67       1.307 -28.806 -32.596  1.00 51.76           C  
ANISOU  138  C   GLN A  67     5874   8955   4834    726    599     25       C  
ATOM    139  O   GLN A  67       1.256 -29.845 -33.251  1.00 54.01           O  
ANISOU  139  O   GLN A  67     6198   9357   4963    662    621   -210       O  
ATOM    140  CB  GLN A  67       3.657 -27.869 -32.333  1.00 50.40           C  
ANISOU  140  CB  GLN A  67     5647   8600   4901    791    799    204       C  
ATOM    141  CG  GLN A  67       5.069 -28.169 -31.773  1.00 50.74           C  
ANISOU  141  CG  GLN A  67     5628   8499   5151    796    877    191       C  
ATOM    142  CD  GLN A  67       5.324 -27.577 -30.390  1.00 49.86           C  
ANISOU  142  CD  GLN A  67     5524   8158   5260    713    797    315       C  
ATOM    143  OE1 GLN A  67       4.854 -26.486 -30.070  1.00 49.39           O  
ANISOU  143  OE1 GLN A  67     5539   8024   5201    659    772    462       O  
ATOM    144  NE2 GLN A  67       6.078 -28.300 -29.567  1.00 48.61           N  
ANISOU  144  NE2 GLN A  67     5297   7888   5282    698    779    269       N  
ATOM    145  N   THR A  68       0.354 -27.884 -32.710  1.00 53.29           N  
ANISOU  145  N   THR A  68     6024   9271   4950    751    537    261       N  
ATOM    146  CA  THR A  68       0.346 -26.593 -32.048  1.00 53.28           C  
ANISOU  146  CA  THR A  68     6034   9092   5116    829    583    534       C  
ATOM    147  C   THR A  68      -1.054 -26.255 -31.570  1.00 53.53           C  
ANISOU  147  C   THR A  68     6044   9121   5172    876    511    685       C  
ATOM    148  O   THR A  68      -2.050 -26.537 -32.255  1.00 55.49           O  
ANISOU  148  O   THR A  68     6189   9675   5220    864    422    736       O  
ATOM    149  CB  THR A  68       0.815 -25.450 -33.000  1.00 55.18           C  
ANISOU  149  CB  THR A  68     6235   9488   5241    888    703    793       C  
ATOM    150  OG1 THR A  68       0.266 -24.202 -32.560  1.00 55.69           O  
ANISOU  150  OG1 THR A  68     6332   9409   5417    975    770   1090       O  
ATOM    151  CG2 THR A  68       0.379 -25.701 -34.450  1.00 57.84           C  
ANISOU  151  CG2 THR A  68     6476  10262   5237    876    675    825       C  
ATOM    152  N   GLY A  69      -1.119 -25.654 -30.387  1.00 52.13           N  
ANISOU  152  N   GLY A  69     5959   8620   5225    911    560    765       N  
ATOM    153  CA  GLY A  69      -2.305 -24.927 -29.981  1.00 52.74           C  
ANISOU  153  CA  GLY A  69     6029   8651   5358   1019    597   1002       C  
ATOM    154  C   GLY A  69      -2.195 -23.471 -30.403  1.00 54.40           C  
ANISOU  154  C   GLY A  69     6267   8822   5580   1141    782   1334       C  
ATOM    155  O   GLY A  69      -1.101 -22.955 -30.668  1.00 54.80           O  
ANISOU  155  O   GLY A  69     6386   8789   5645   1096    877   1346       O  
TER     156      GLY A  69                                                      
ATOM    157  N   ASP B   6      -9.835 -18.025  11.132  1.00 29.31           N  
ANISOU  157  N   ASP B   6     3944   4179   3012    268   -252   -450       N  
ATOM    158  CA  ASP B   6      -8.979 -18.978  11.896  1.00 28.65           C  
ANISOU  158  CA  ASP B   6     3785   4202   2896    275   -282   -437       C  
ATOM    159  C   ASP B   6      -9.702 -19.399  13.160  1.00 27.79           C  
ANISOU  159  C   ASP B   6     3666   4161   2732    346   -286   -417       C  
ATOM    160  O   ASP B   6     -10.510 -18.634  13.703  1.00 28.88           O  
ANISOU  160  O   ASP B   6     3853   4277   2841    370   -276   -447       O  
ATOM    161  CB  ASP B   6      -7.624 -18.349  12.256  1.00 30.00           C  
ANISOU  161  CB  ASP B   6     3937   4416   3043    205   -309   -511       C  
ATOM    162  N   VAL B   7      -9.425 -20.623  13.607  1.00 26.00           N  
ANISOU  162  N   VAL B   7     3375   4012   2488    384   -296   -363       N  
ATOM    163  CA  VAL B   7     -10.058 -21.180  14.807  1.00 24.31           C  
ANISOU  163  CA  VAL B   7     3145   3870   2221    456   -296   -331       C  
ATOM    164  C   VAL B   7      -9.016 -21.903  15.661  1.00 24.42           C  
ANISOU  164  C   VAL B   7     3091   3999   2188    471   -323   -323       C  
ATOM    165  O   VAL B   7      -7.986 -22.322  15.143  1.00 24.54           O  
ANISOU  165  O   VAL B   7     3066   4032   2224    438   -335   -317       O  
ATOM    166  CB  VAL B   7     -11.199 -22.164  14.445  1.00 23.44           C  
ANISOU  166  CB  VAL B   7     3032   3729   2145    511   -265   -244       C  
ATOM    167  CG1 VAL B   7     -12.432 -21.415  13.898  1.00 21.86           C  
ANISOU  167  CG1 VAL B   7     2892   3443   1969    517   -240   -251       C  
ATOM    168  CG2 VAL B   7     -10.705 -23.241  13.455  1.00 21.96           C  
ANISOU  168  CG2 VAL B   7     2806   3522   2014    497   -259   -189       C  
ATOM    169  N   PRO B   8      -9.291 -22.081  16.971  1.00 24.48           N  
ANISOU  169  N   PRO B   8     3083   4091   2126    527   -330   -319       N  
ATOM    170  CA  PRO B   8      -8.282 -22.702  17.836  1.00 25.05           C  
ANISOU  170  CA  PRO B   8     3089   4285   2142    549   -356   -312       C  
ATOM    171  C   PRO B   8      -8.022 -24.195  17.582  1.00 25.17           C  
ANISOU  171  C   PRO B   8     3053   4327   2180    593   -342   -217       C  
ATOM    172  O   PRO B   8      -6.897 -24.654  17.779  1.00 24.89           O  
ANISOU  172  O   PRO B   8     2963   4372   2121    592   -363   -213       O  
ATOM    173  CB  PRO B   8      -8.815 -22.463  19.256  1.00 25.65           C  
ANISOU  173  CB  PRO B   8     3170   4439   2137    606   -361   -327       C  
ATOM    174  CG  PRO B   8     -10.247 -22.143  19.111  1.00 25.25           C  
ANISOU  174  CG  PRO B   8     3177   4307   2108    633   -330   -310       C  
ATOM    175  CD  PRO B   8     -10.496 -21.660  17.711  1.00 23.79           C  
ANISOU  175  CD  PRO B   8     3036   3998   2004    576   -314   -322       C  
ATOM    176  N   SER B   9      -9.032 -24.939  17.134  1.00 24.47           N  
ANISOU  176  N   SER B   9     2983   4175   2138    628   -307   -143       N  
ATOM    177  CA  SER B   9      -8.894 -26.389  16.989  1.00 24.43           C  
ANISOU  177  CA  SER B   9     2939   4186   2155    673   -286    -52       C  
ATOM    178  C   SER B   9      -9.433 -26.875  15.633  1.00 24.40           C  
ANISOU  178  C   SER B   9     2958   4072   2240    650   -257    -12       C  
ATOM    179  O   SER B   9     -10.443 -27.583  15.602  1.00 23.92           O  
ANISOU  179  O   SER B   9     2908   3976   2204    686   -224     48       O  
ATOM    180  CB  SER B   9      -9.624 -27.109  18.148  1.00 24.07           C  
ANISOU  180  CB  SER B   9     2882   4200   2062    756   -265     10       C  
ATOM    181  OG  SER B   9      -9.073 -26.785  19.420  1.00 24.04           O  
ANISOU  181  OG  SER B   9     2851   4314   1969    787   -293    -21       O  
ATOM    182  N   PRO B  10      -8.765 -26.503  14.514  1.00 25.07           N  
ANISOU  182  N   PRO B  10     3047   4106   2371    587   -268    -48       N  
ATOM    183  CA  PRO B  10      -9.282 -26.861  13.190  1.00 25.48           C  
ANISOU  183  CA  PRO B  10     3122   4059   2501    564   -244    -19       C  
ATOM    184  C   PRO B  10      -9.514 -28.358  13.056  1.00 25.71           C  
ANISOU  184  C   PRO B  10     3128   4081   2559    609   -214     65       C  
ATOM    185  O   PRO B  10      -8.678 -29.143  13.520  1.00 25.98           O  
ANISOU  185  O   PRO B  10     3123   4179   2570    642   -217     98       O  
ATOM    186  CB  PRO B  10      -8.174 -26.432  12.218  1.00 25.76           C  
ANISOU  186  CB  PRO B  10     3149   4073   2565    502   -262    -62       C  
ATOM    187  CG  PRO B  10      -7.100 -25.862  13.019  1.00 25.37           C  
ANISOU  187  CG  PRO B  10     3070   4110   2457    486   -296   -113       C  
ATOM    188  CD  PRO B  10      -7.512 -25.732  14.434  1.00 25.83           C  
ANISOU  188  CD  PRO B  10     3125   4241   2447    534   -303   -117       C  
ATOM    189  N   PRO B  11     -10.648 -28.745  12.436  1.00 25.36           N  
ANISOU  189  N   PRO B  11     3108   3962   2563    611   -183     98       N  
ATOM    190  CA  PRO B  11     -10.993 -30.134  12.188  1.00 25.29           C  
ANISOU  190  CA  PRO B  11     3088   3928   2593    641   -149    172       C  
ATOM    191  C   PRO B  11      -9.979 -30.774  11.240  1.00 25.70           C  
ANISOU  191  C   PRO B  11     3121   3958   2685    622   -150    181       C  
ATOM    192  O   PRO B  11      -9.174 -30.070  10.620  1.00 24.40           O  
ANISOU  192  O   PRO B  11     2954   3789   2525    578   -175    131       O  
ATOM    193  CB  PRO B  11     -12.384 -30.044  11.547  1.00 24.98           C  
ANISOU  193  CB  PRO B  11     3078   3815   2596    625   -125    178       C  
ATOM    194  CG  PRO B  11     -12.441 -28.675  10.961  1.00 24.10           C  
ANISOU  194  CG  PRO B  11     2996   3674   2486    581   -148    109       C  
ATOM    195  CD  PRO B  11     -11.703 -27.835  11.952  1.00 24.48           C  
ANISOU  195  CD  PRO B  11     3039   3790   2470    586   -178     65       C  
ATOM    196  N   GLU B  12     -10.043 -32.102  11.164  1.00 26.32           N  
ANISOU  196  N   GLU B  12     3189   4020   2792    655   -118    247       N  
ATOM    197  CA AGLU B  12      -9.047 -32.914  10.489  0.50 26.45           C  
ANISOU  197  CA AGLU B  12     3186   4025   2836    657   -112    267       C  
ATOM    198  CA BGLU B  12      -9.038 -32.903  10.450  0.50 26.85           C  
ANISOU  198  CA BGLU B  12     3237   4074   2888    655   -113    266       C  
ATOM    199  C   GLU B  12      -9.706 -33.848   9.465  1.00 26.28           C  
ANISOU  199  C   GLU B  12     3183   3913   2886    644    -76    299       C  
ATOM    200  O   GLU B  12     -10.731 -34.474   9.770  1.00 26.47           O  
ANISOU  200  O   GLU B  12     3220   3908   2926    662    -43    340       O  
ATOM    201  CB AGLU B  12      -8.261 -33.705  11.555  0.50 27.18           C  
ANISOU  201  CB AGLU B  12     3246   4198   2882    723   -107    318       C  
ATOM    202  CB BGLU B  12      -8.191 -33.740  11.426  0.50 27.77           C  
ANISOU  202  CB BGLU B  12     3321   4268   2962    720   -107    317       C  
ATOM    203  CG AGLU B  12      -9.079 -34.721  12.413  0.50 26.30           C  
ANISOU  203  CG AGLU B  12     3141   4086   2766    782    -64    393       C  
ATOM    204  CG BGLU B  12      -7.730 -33.029  12.704  0.50 29.37           C  
ANISOU  204  CG BGLU B  12     3498   4577   3083    745   -138    294       C  
ATOM    205  CD AGLU B  12      -9.834 -34.147  13.650  0.50 25.24           C  
ANISOU  205  CD AGLU B  12     3009   4007   2575    807    -69    393       C  
ATOM    206  CD BGLU B  12      -7.717 -33.949  13.917  0.50 30.78           C  
ANISOU  206  CD BGLU B  12     3657   4820   3216    826   -115    365       C  
ATOM    207  OE1AGLU B  12      -9.814 -32.929  13.948  0.50 20.83           O  
ANISOU  207  OE1AGLU B  12     2451   3485   1976    782   -106    330       O  
ATOM    208  OE1BGLU B  12      -8.434 -34.975  13.910  0.50 31.63           O  
ANISOU  208  OE1BGLU B  12     3782   4875   3358    857    -69    431       O  
ATOM    209  OE2AGLU B  12     -10.459 -34.971  14.351  0.50 27.15           O  
ANISOU  209  OE2AGLU B  12     3252   4251   2810    855    -31    459       O  
ATOM    210  OE2BGLU B  12      -6.993 -33.641  14.885  0.50 32.55           O  
ANISOU  210  OE2BGLU B  12     3849   5150   3368    859   -141    355       O  
ATOM    211  N   THR B  13      -9.132 -33.935   8.263  1.00 25.92           N  
ANISOU  211  N   THR B  13     3139   3826   2881    611    -80    278       N  
ATOM    212  CA  THR B  13      -9.551 -34.925   7.274  1.00 25.72           C  
ANISOU  212  CA  THR B  13     3129   3723   2919    601    -47    303       C  
ATOM    213  C   THR B  13      -8.431 -35.957   7.144  1.00 26.91           C  
ANISOU  213  C   THR B  13     3262   3883   3076    637    -33    339       C  
ATOM    214  O   THR B  13      -7.311 -35.752   7.636  1.00 25.65           O  
ANISOU  214  O   THR B  13     3074   3795   2873    661    -55    337       O  
ATOM    215  CB  THR B  13      -9.790 -34.319   5.857  1.00 25.00           C  
ANISOU  215  CB  THR B  13     3053   3575   2868    543    -59    252       C  
ATOM    216  OG1 THR B  13      -8.539 -33.861   5.308  1.00 24.43           O  
ANISOU  216  OG1 THR B  13     2967   3527   2788    526    -85    221       O  
ATOM    217  CG2 THR B  13     -10.805 -33.172   5.895  1.00 24.05           C  
ANISOU  217  CG2 THR B  13     2951   3448   2736    514    -74    215       C  
ATOM    218  N   GLN B  14      -8.733 -37.059   6.461  1.00 28.48           N  
ANISOU  218  N   GLN B  14     3479   4013   3329    640      4    368       N  
ATOM    219  CA  GLN B  14      -7.711 -38.050   6.147  1.00 30.52           C  
ANISOU  219  CA  GLN B  14     3729   4265   3600    675     23    399       C  
ATOM    220  C   GLN B  14      -6.702 -37.425   5.186  1.00 31.16           C  
ANISOU  220  C   GLN B  14     3793   4362   3681    645     -9    351       C  
ATOM    221  O   GLN B  14      -7.044 -36.533   4.394  1.00 29.75           O  
ANISOU  221  O   GLN B  14     3623   4160   3517    589    -31    299       O  
ATOM    222  CB  GLN B  14      -8.343 -39.303   5.537  1.00 31.06           C  
ANISOU  222  CB  GLN B  14     3828   4242   3731    676     73    430       C  
ATOM    223  CG  GLN B  14      -9.167 -40.130   6.526  1.00 33.98           C  
ANISOU  223  CG  GLN B  14     4212   4594   4104    710    117    491       C  
ATOM    224  CD  GLN B  14      -8.362 -41.221   7.222  1.00 38.41           C  
ANISOU  224  CD  GLN B  14     4771   5171   4650    787    152    560       C  
ATOM    225  OE1 GLN B  14      -7.126 -41.178   7.275  1.00 40.75           O  
ANISOU  225  OE1 GLN B  14     5044   5523   4913    825    133    564       O  
ATOM    226  NE2 GLN B  14      -9.064 -42.214   7.758  1.00 40.54           N  
ANISOU  226  NE2 GLN B  14     5065   5394   4943    813    206    619       N  
ATOM    227  N   LYS B  15      -5.455 -37.876   5.283  1.00 32.94           N  
ANISOU  227  N   LYS B  15     3994   4634   3887    687    -10    372       N  
ATOM    228  CA  LYS B  15      -4.399 -37.400   4.396  1.00 34.13           C  
ANISOU  228  CA  LYS B  15     4123   4808   4036    662    -36    334       C  
ATOM    229  C   LYS B  15      -4.513 -38.042   3.016  1.00 33.59           C  
ANISOU  229  C   LYS B  15     4079   4656   4026    644    -12    326       C  
ATOM    230  O   LYS B  15      -4.880 -39.216   2.901  1.00 34.65           O  
ANISOU  230  O   LYS B  15     4237   4731   4194    674     29    364       O  
ATOM    231  CB  LYS B  15      -3.021 -37.683   5.009  1.00 35.48           C  
ANISOU  231  CB  LYS B  15     4250   5070   4159    718    -45    361       C  
ATOM    232  CG  LYS B  15      -2.442 -36.505   5.798  1.00 38.52           C  
ANISOU  232  CG  LYS B  15     4597   5557   4483    700    -91    326       C  
ATOM    233  CD  LYS B  15      -3.079 -36.352   7.180  1.00 42.70           C  
ANISOU  233  CD  LYS B  15     5127   6126   4970    727    -94    345       C  
ATOM    234  CE  LYS B  15      -3.315 -34.877   7.529  1.00 44.12           C  
ANISOU  234  CE  LYS B  15     5303   6340   5120    670   -135    281       C  
ATOM    235  NZ  LYS B  15      -2.089 -34.033   7.379  1.00 45.71           N  
ANISOU  235  NZ  LYS B  15     5461   6616   5287    637   -174    233       N  
ATOM    236  N   ALA B  16      -4.219 -37.267   1.974  1.00 32.85           N  
ANISOU  236  N   ALA B  16     3980   4555   3944    594    -36    276       N  
ATOM    237  CA  ALA B  16      -4.159 -37.806   0.619  1.00 32.12           C  
ANISOU  237  CA  ALA B  16     3905   4401   3898    581    -17    263       C  
ATOM    238  C   ALA B  16      -2.823 -38.528   0.453  1.00 32.17           C  
ANISOU  238  C   ALA B  16     3887   4443   3893    630     -7    289       C  
ATOM    239  O   ALA B  16      -1.805 -37.917   0.108  1.00 31.94           O  
ANISOU  239  O   ALA B  16     3824   4470   3841    619    -32    268       O  
ATOM    240  CB  ALA B  16      -4.330 -36.687  -0.436  1.00 31.61           C  
ANISOU  240  CB  ALA B  16     3843   4322   3843    517    -44    207       C  
ATOM    241  N   GLU B  17      -2.837 -39.829   0.736  1.00 31.99           N  
ANISOU  241  N   GLU B  17     3881   4387   3886    687     33    338       N  
ATOM    242  CA  GLU B  17      -1.643 -40.670   0.643  1.00 32.46           C  
ANISOU  242  CA  GLU B  17     3923   4475   3934    751     51    372       C  
ATOM    243  C   GLU B  17      -1.469 -41.208  -0.777  1.00 31.06           C  
ANISOU  243  C   GLU B  17     3767   4234   3800    742     71    351       C  
ATOM    244  O   GLU B  17      -1.758 -42.374  -1.075  1.00 31.70           O  
ANISOU  244  O   GLU B  17     3885   4239   3917    772    116    374       O  
ATOM    245  CB  GLU B  17      -1.709 -41.793   1.683  1.00 33.85           C  
ANISOU  245  CB  GLU B  17     4112   4645   4102    827     91    441       C  
ATOM    246  CG  GLU B  17      -1.602 -41.277   3.113  1.00 37.18           C  
ANISOU  246  CG  GLU B  17     4503   5157   4466    851     69    465       C  
ATOM    247  CD  GLU B  17      -2.242 -42.200   4.146  1.00 43.73           C  
ANISOU  247  CD  GLU B  17     5360   5959   5297    906    111    529       C  
ATOM    248  OE1 GLU B  17      -2.583 -43.360   3.800  1.00 46.24           O  
ANISOU  248  OE1 GLU B  17     5720   6187   5661    932    164    562       O  
ATOM    249  OE2 GLU B  17      -2.393 -41.759   5.312  1.00 45.33           O  
ANISOU  249  OE2 GLU B  17     5541   6228   5452    922     94    546       O  
ATOM    250  N   LEU B  18      -1.008 -40.318  -1.650  1.00 28.96           N  
ANISOU  250  N   LEU B  18     3479   3996   3528    697     40    305       N  
ATOM    251  CA  LEU B  18      -0.845 -40.592  -3.073  1.00 27.01           C  
ANISOU  251  CA  LEU B  18     3247   3702   3314    681     51    276       C  
ATOM    252  C   LEU B  18       0.521 -40.082  -3.491  1.00 26.05           C  
ANISOU  252  C   LEU B  18     3077   3660   3159    689     29    267       C  
ATOM    253  O   LEU B  18       0.955 -39.030  -3.036  1.00 25.62           O  
ANISOU  253  O   LEU B  18     2984   3679   3070    661     -5    253       O  
ATOM    254  CB  LEU B  18      -1.919 -39.842  -3.871  1.00 26.49           C  
ANISOU  254  CB  LEU B  18     3203   3586   3275    607     36    225       C  
ATOM    255  CG  LEU B  18      -3.385 -40.245  -3.684  1.00 27.10           C  
ANISOU  255  CG  LEU B  18     3321   3588   3386    585     55    223       C  
ATOM    256  CD1 LEU B  18      -4.305 -39.168  -4.216  1.00 27.92           C  
ANISOU  256  CD1 LEU B  18     3430   3680   3495    519     29    177       C  
ATOM    257  CD2 LEU B  18      -3.630 -41.542  -4.416  1.00 28.49           C  
ANISOU  257  CD2 LEU B  18     3532   3685   3605    604     98    226       C  
ATOM    258  N   GLU B  19       1.209 -40.821  -4.354  1.00 25.60           N  
ANISOU  258  N   GLU B  19     3021   3589   3114    725     52    272       N  
ATOM    259  CA  GLU B  19       2.455 -40.316  -4.918  1.00 25.49           C  
ANISOU  259  CA  GLU B  19     2959   3651   3072    726     34    260       C  
ATOM    260  C   GLU B  19       2.131 -39.095  -5.778  1.00 24.36           C  
ANISOU  260  C   GLU B  19     2814   3504   2938    644      5    208       C  
ATOM    261  O   GLU B  19       1.030 -39.003  -6.359  1.00 22.45           O  
ANISOU  261  O   GLU B  19     2613   3187   2730    606     10    181       O  
ATOM    262  CB  GLU B  19       3.176 -41.386  -5.745  1.00 26.23           C  
ANISOU  262  CB  GLU B  19     3060   3728   3177    786     68    275       C  
ATOM    263  CG  GLU B  19       3.346 -42.744  -5.037  1.00 29.69           C  
ANISOU  263  CG  GLU B  19     3519   4144   3616    875    109    331       C  
ATOM    264  CD  GLU B  19       4.423 -42.765  -3.941  1.00 33.97           C  
ANISOU  264  CD  GLU B  19     4006   4797   4103    937    100    378       C  
ATOM    265  OE1 GLU B  19       5.268 -41.839  -3.866  1.00 35.55           O  
ANISOU  265  OE1 GLU B  19     4144   5100   4263    913     63    364       O  
ATOM    266  OE2 GLU B  19       4.422 -43.736  -3.152  1.00 34.78           O  
ANISOU  266  OE2 GLU B  19     4128   4886   4201   1010    133    430       O  
ATOM    267  N   GLU B  20       3.064 -38.149  -5.841  1.00 23.57           N  
ANISOU  267  N   GLU B  20     2664   3485   2807    618    -21    195       N  
ATOM    268  CA  GLU B  20       2.887 -36.978  -6.705  1.00 23.13           C  
ANISOU  268  CA  GLU B  20     2608   3422   2758    546    -41    153       C  
ATOM    269  C   GLU B  20       2.680 -37.394  -8.159  1.00 22.06           C  
ANISOU  269  C   GLU B  20     2499   3229   2651    547    -20    135       C  
ATOM    270  O   GLU B  20       3.255 -38.396  -8.631  1.00 22.08           O  
ANISOU  270  O   GLU B  20     2500   3230   2659    601      4    151       O  
ATOM    271  CB  GLU B  20       4.075 -36.012  -6.618  1.00 23.90           C  
ANISOU  271  CB  GLU B  20     2646   3614   2821    516    -65    144       C  
ATOM    272  CG  GLU B  20       4.208 -35.316  -5.272  1.00 28.35           C  
ANISOU  272  CG  GLU B  20     3182   4238   3351    495    -92    144       C  
ATOM    273  CD  GLU B  20       5.015 -34.029  -5.352  1.00 32.86           C  
ANISOU  273  CD  GLU B  20     3709   4876   3899    431   -117    114       C  
ATOM    274  OE1 GLU B  20       5.919 -33.915  -6.229  1.00 35.33           O  
ANISOU  274  OE1 GLU B  20     3990   5224   4210    422   -112    111       O  
ATOM    275  OE2 GLU B  20       4.744 -33.130  -4.533  1.00 32.09           O  
ANISOU  275  OE2 GLU B  20     3610   4795   3786    386   -140     93       O  
ATOM    276  N   GLY B  21       1.850 -36.630  -8.861  1.00 19.69           N  
ANISOU  276  N   GLY B  21     2225   2887   2369    492    -28    102       N  
ATOM    277  CA  GLY B  21       1.627 -36.869 -10.279  1.00 19.06           C  
ANISOU  277  CA  GLY B  21     2166   2766   2309    489    -13     80       C  
ATOM    278  C   GLY B  21       0.208 -36.606 -10.730  1.00 17.77           C  
ANISOU  278  C   GLY B  21     2045   2536   2168    453    -14     52       C  
ATOM    279  O   GLY B  21      -0.583 -35.990 -10.002  1.00 17.40           O  
ANISOU  279  O   GLY B  21     2011   2478   2122    423    -29     48       O  
ATOM    280  N   VAL B  22      -0.105 -37.060 -11.939  1.00 16.91           N  
ANISOU  280  N   VAL B  22     1957   2391   2075    459      0     30       N  
ATOM    281  CA  VAL B  22      -1.408 -36.819 -12.548  1.00 16.44           C  
ANISOU  281  CA  VAL B  22     1929   2284   2031    427     -1      0       C  
ATOM    282  C   VAL B  22      -2.251 -38.092 -12.503  1.00 16.84           C  
ANISOU  282  C   VAL B  22     2012   2273   2111    447     19     -8       C  
ATOM    283  O   VAL B  22      -1.785 -39.171 -12.878  1.00 16.71           O  
ANISOU  283  O   VAL B  22     2004   2239   2106    484     43     -7       O  
ATOM    284  CB  VAL B  22      -1.292 -36.315 -14.016  1.00 15.96           C  
ANISOU  284  CB  VAL B  22     1866   2234   1962    414     -1    -25       C  
ATOM    285  CG1 VAL B  22      -2.654 -35.846 -14.532  1.00 15.99           C  
ANISOU  285  CG1 VAL B  22     1895   2207   1971    383     -8    -53       C  
ATOM    286  CG2 VAL B  22      -0.222 -35.181 -14.155  1.00 15.65           C  
ANISOU  286  CG2 VAL B  22     1794   2254   1898    395    -12    -12       C  
ATOM    287  N   TYR B  23      -3.499 -37.946 -12.056  1.00 16.33           N  
ANISOU  287  N   TYR B  23     1968   2177   2060    419     13    -17       N  
ATOM    288  CA  TYR B  23      -4.399 -39.081 -11.797  1.00 16.35           C  
ANISOU  288  CA  TYR B  23     1998   2119   2092    425     35    -23       C  
ATOM    289  C   TYR B  23      -5.676 -39.014 -12.611  1.00 15.92           C  
ANISOU  289  C   TYR B  23     1959   2037   2049    389     33    -65       C  
ATOM    290  O   TYR B  23      -6.255 -37.942 -12.769  1.00 15.20           O  
ANISOU  290  O   TYR B  23     1861   1971   1942    361     11    -76       O  
ATOM    291  CB  TYR B  23      -4.800 -39.082 -10.311  1.00 16.43           C  
ANISOU  291  CB  TYR B  23     2010   2125   2105    426     34      9       C  
ATOM    292  CG  TYR B  23      -3.669 -39.560  -9.435  1.00 18.08           C  
ANISOU  292  CG  TYR B  23     2206   2359   2304    473     44     52       C  
ATOM    293  CD1 TYR B  23      -2.594 -38.723  -9.126  1.00 17.56           C  
ANISOU  293  CD1 TYR B  23     2105   2360   2204    479     22     68       C  
ATOM    294  CD2 TYR B  23      -3.665 -40.861  -8.939  1.00 19.51           C  
ANISOU  294  CD2 TYR B  23     2407   2496   2506    511     77     77       C  
ATOM    295  CE1 TYR B  23      -1.542 -39.173  -8.323  1.00 19.21           C  
ANISOU  295  CE1 TYR B  23     2293   2608   2397    526     29    106       C  
ATOM    296  CE2 TYR B  23      -2.618 -41.329  -8.157  1.00 21.64           C  
ANISOU  296  CE2 TYR B  23     2663   2796   2761    566     89    122       C  
ATOM    297  CZ  TYR B  23      -1.560 -40.478  -7.851  1.00 20.17           C  
ANISOU  297  CZ  TYR B  23     2434   2691   2535    574     62    135       C  
ATOM    298  OH  TYR B  23      -0.530 -40.941  -7.072  1.00 19.50           O  
ANISOU  298  OH  TYR B  23     2328   2650   2428    632     71    178       O  
ATOM    299  N   ARG B  24      -6.138 -40.160 -13.104  1.00 15.54           N  
ANISOU  299  N   ARG B  24     1933   1941   2030    391     57    -90       N  
ATOM    300  CA  ARG B  24      -7.519 -40.266 -13.570  1.00 15.60           C  
ANISOU  300  CA  ARG B  24     1950   1925   2050    352     55   -130       C  
ATOM    301  C   ARG B  24      -8.424 -40.352 -12.354  1.00 15.70           C  
ANISOU  301  C   ARG B  24     1969   1918   2078    334     59   -108       C  
ATOM    302  O   ARG B  24      -8.115 -41.063 -11.393  1.00 16.07           O  
ANISOU  302  O   ARG B  24     2027   1936   2142    356     80    -72       O  
ATOM    303  CB  ARG B  24      -7.707 -41.535 -14.421  1.00 16.62           C  
ANISOU  303  CB  ARG B  24     2102   2006   2206    352     83   -170       C  
ATOM    304  CG  ARG B  24      -6.751 -41.637 -15.599  1.00 16.60           C  
ANISOU  304  CG  ARG B  24     2097   2022   2187    379     85   -192       C  
ATOM    305  CD  ARG B  24      -6.921 -42.993 -16.343  1.00 20.33           C  
ANISOU  305  CD  ARG B  24     2599   2438   2687    381    116   -237       C  
ATOM    306  NE  ARG B  24      -5.815 -43.196 -17.271  1.00 20.29           N  
ANISOU  306  NE  ARG B  24     2593   2450   2665    422    124   -247       N  
ATOM    307  CZ  ARG B  24      -5.774 -42.735 -18.519  1.00 21.63           C  
ANISOU  307  CZ  ARG B  24     2749   2662   2807    418    108   -285       C  
ATOM    308  NH1 ARG B  24      -6.793 -42.067 -19.033  1.00 19.84           N  
ANISOU  308  NH1 ARG B  24     2508   2464   2564    379     85   -317       N  
ATOM    309  NH2 ARG B  24      -4.707 -42.969 -19.278  1.00 23.41           N  
ANISOU  309  NH2 ARG B  24     2973   2904   3015    460    119   -289       N  
ATOM    310  N   ILE B  25      -9.551 -39.643 -12.397  1.00 14.75           N  
ANISOU  310  N   ILE B  25     1840   1816   1949    300     41   -125       N  
ATOM    311  CA  ILE B  25     -10.565 -39.730 -11.347  1.00 15.35           C  
ANISOU  311  CA  ILE B  25     1917   1877   2036    281     46   -108       C  
ATOM    312  C   ILE B  25     -11.713 -40.543 -11.930  1.00 16.12           C  
ANISOU  312  C   ILE B  25     2020   1944   2161    244     61   -151       C  
ATOM    313  O   ILE B  25     -12.209 -40.220 -13.009  1.00 16.03           O  
ANISOU  313  O   ILE B  25     1996   1957   2135    225     47   -195       O  
ATOM    314  CB  ILE B  25     -11.088 -38.323 -10.929  1.00 14.70           C  
ANISOU  314  CB  ILE B  25     1819   1842   1922    271     16    -97       C  
ATOM    315  CG1 ILE B  25      -9.926 -37.489 -10.390  1.00 14.51           C  
ANISOU  315  CG1 ILE B  25     1790   1849   1874    297      1    -64       C  
ATOM    316  CG2 ILE B  25     -12.246 -38.440  -9.889  1.00 14.41           C  
ANISOU  316  CG2 ILE B  25     1781   1797   1896    254     23    -82       C  
ATOM    317  CD1 ILE B  25     -10.228 -35.966 -10.242  1.00 14.35           C  
ANISOU  317  CD1 ILE B  25     1762   1868   1820    287    -24    -63       C  
ATOM    318  N   LYS B  26     -12.104 -41.603 -11.235  1.00 16.79           N  
ANISOU  318  N   LYS B  26     2120   1975   2281    234     93   -139       N  
ATOM    319  CA  LYS B  26     -13.135 -42.512 -11.731  1.00 18.43           C  
ANISOU  319  CA  LYS B  26     2333   2146   2520    190    114   -183       C  
ATOM    320  C   LYS B  26     -14.370 -42.529 -10.844  1.00 18.64           C  
ANISOU  320  C   LYS B  26     2349   2171   2559    156    121   -169       C  
ATOM    321  O   LYS B  26     -14.280 -42.436  -9.616  1.00 18.47           O  
ANISOU  321  O   LYS B  26     2332   2145   2539    175    130   -116       O  
ATOM    322  CB  LYS B  26     -12.548 -43.917 -11.901  1.00 19.62           C  
ANISOU  322  CB  LYS B  26     2520   2222   2711    200    156   -190       C  
ATOM    323  CG  LYS B  26     -11.381 -43.910 -12.890  1.00 22.41           C  
ANISOU  323  CG  LYS B  26     2879   2584   3048    236    149   -208       C  
ATOM    324  CD  LYS B  26     -11.146 -45.271 -13.452  1.00 30.77           C  
ANISOU  324  CD  LYS B  26     3974   3572   4144    235    188   -240       C  
ATOM    325  CE  LYS B  26     -10.431 -45.168 -14.784  1.00 33.38           C  
ANISOU  325  CE  LYS B  26     4303   3927   4452    255    176   -283       C  
ATOM    326  NZ  LYS B  26     -10.160 -46.523 -15.319  1.00 35.42           N  
ANISOU  326  NZ  LYS B  26     4601   4110   4745    260    218   -318       N  
ATOM    327  N   GLN B  27     -15.533 -42.619 -11.476  1.00 19.10           N  
ANISOU  327  N   GLN B  27     2389   2245   2622    107    117   -218       N  
ATOM    328  CA  GLN B  27     -16.782 -42.615 -10.748  1.00 20.77           C  
ANISOU  328  CA  GLN B  27     2581   2466   2842     72    124   -210       C  
ATOM    329  C   GLN B  27     -17.621 -43.803 -11.149  1.00 21.38           C  
ANISOU  329  C   GLN B  27     2661   2499   2962     12    156   -256       C  
ATOM    330  O   GLN B  27     -17.645 -44.186 -12.318  1.00 20.24           O  
ANISOU  330  O   GLN B  27     2515   2351   2821    -10    153   -318       O  
ATOM    331  CB  GLN B  27     -17.559 -41.348 -11.068  1.00 21.28           C  
ANISOU  331  CB  GLN B  27     2609   2615   2861     67     85   -224       C  
ATOM    332  CG  GLN B  27     -18.739 -41.087 -10.138  1.00 25.28           C  
ANISOU  332  CG  GLN B  27     3091   3147   3364     47     88   -202       C  
ATOM    333  CD  GLN B  27     -19.000 -39.608 -10.000  1.00 27.49           C  
ANISOU  333  CD  GLN B  27     3351   3499   3592     77     52   -185       C  
ATOM    334  OE1 GLN B  27     -19.087 -39.076  -8.883  1.00 31.33           O  
ANISOU  334  OE1 GLN B  27     3840   3997   4067     99     51   -139       O  
ATOM    335  NE2 GLN B  27     -19.089 -38.924 -11.134  1.00 26.60           N  
ANISOU  335  NE2 GLN B  27     3223   3435   3448     82     25   -222       N  
ATOM    336  N   GLN B  28     -18.324 -44.358 -10.174  1.00 22.26           N  
ANISOU  336  N   GLN B  28     2774   2579   3104    -14    187   -228       N  
ATOM    337  CA  GLN B  28     -19.335 -45.374 -10.418  1.00 25.01           C  
ANISOU  337  CA  GLN B  28     3117   2890   3494    -85    219   -272       C  
ATOM    338  C   GLN B  28     -20.577 -44.648 -10.966  1.00 25.76           C  
ANISOU  338  C   GLN B  28     3156   3075   3557   -126    185   -316       C  
ATOM    339  O   GLN B  28     -21.093 -43.718 -10.342  1.00 26.24           O  
ANISOU  339  O   GLN B  28     3188   3197   3585   -109    163   -282       O  
ATOM    340  CB  GLN B  28     -19.617 -46.126  -9.108  1.00 25.30           C  
ANISOU  340  CB  GLN B  28     3174   2866   3571    -96    267   -215       C  
ATOM    341  CG  GLN B  28     -20.327 -47.467  -9.244  1.00 29.53           C  
ANISOU  341  CG  GLN B  28     3724   3327   4167   -168    319   -250       C  
ATOM    342  CD  GLN B  28     -19.509 -48.510 -10.007  1.00 32.25           C  
ANISOU  342  CD  GLN B  28     4119   3586   4548   -169    349   -287       C  
ATOM    343  OE1 GLN B  28     -19.972 -49.049 -10.996  1.00 35.33           O  
ANISOU  343  OE1 GLN B  28     4505   3961   4957   -228    354   -365       O  
ATOM    344  NE2 GLN B  28     -18.296 -48.797  -9.537  1.00 32.53           N  
ANISOU  344  NE2 GLN B  28     4200   3568   4589   -100    369   -233       N  
ATOM    345  N   GLY B  29     -21.025 -45.032 -12.157  1.00 26.48           N  
ANISOU  345  N   GLY B  29     3229   3180   3650   -172    178   -394       N  
ATOM    346  CA  GLY B  29     -22.172 -44.365 -12.775  1.00 26.18           C  
ANISOU  346  CA  GLY B  29     3132   3241   3574   -204    144   -439       C  
ATOM    347  C   GLY B  29     -22.944 -45.319 -13.665  1.00 26.42           C  
ANISOU  347  C   GLY B  29     3143   3266   3630   -283    158   -524       C  
ATOM    348  O   GLY B  29     -22.942 -46.529 -13.454  1.00 26.45           O  
ANISOU  348  O   GLY B  29     3176   3180   3691   -330    204   -540       O  
ATOM    349  N   ILE B  30     -23.592 -44.764 -14.676  1.00 26.77           N  
ANISOU  349  N   ILE B  30     3136   3405   3627   -297    120   -581       N  
ATOM    350  CA  ILE B  30     -24.232 -45.586 -15.676  1.00 27.52           C  
ANISOU  350  CA  ILE B  30     3208   3513   3736   -370    125   -675       C  
ATOM    351  C   ILE B  30     -23.102 -46.358 -16.362  1.00 27.92           C  
ANISOU  351  C   ILE B  30     3315   3479   3811   -358    142   -708       C  
ATOM    352  O   ILE B  30     -22.016 -45.807 -16.614  1.00 27.94           O  
ANISOU  352  O   ILE B  30     3346   3480   3789   -286    125   -678       O  
ATOM    353  CB  ILE B  30     -25.076 -44.742 -16.658  1.00 27.76           C  
ANISOU  353  CB  ILE B  30     3168   3680   3698   -371     77   -725       C  
ATOM    354  CG1 ILE B  30     -26.109 -43.914 -15.871  1.00 27.78           C  
ANISOU  354  CG1 ILE B  30     3119   3764   3672   -366     63   -680       C  
ATOM    355  CG2 ILE B  30     -25.780 -45.652 -17.671  1.00 28.39           C  
ANISOU  355  CG2 ILE B  30     3216   3781   3787   -455     80   -831       C  
ATOM    356  CD1 ILE B  30     -26.646 -42.715 -16.615  1.00 27.05           C  
ANISOU  356  CD1 ILE B  30     2971   3806   3499   -323     15   -692       C  
ATOM    357  N   PHE B  31     -23.349 -47.645 -16.566  1.00 28.35           N  
ANISOU  357  N   PHE B  31     3390   3459   3920   -430    182   -765       N  
ATOM    358  CA  PHE B  31     -22.431 -48.585 -17.223  1.00 28.21           C  
ANISOU  358  CA  PHE B  31     3430   3352   3934   -429    208   -808       C  
ATOM    359  C   PHE B  31     -21.295 -49.105 -16.339  1.00 27.62           C  
ANISOU  359  C   PHE B  31     3429   3158   3904   -379    251   -735       C  
ATOM    360  O   PHE B  31     -20.560 -49.993 -16.756  1.00 28.60           O  
ANISOU  360  O   PHE B  31     3607   3197   4060   -375    282   -764       O  
ATOM    361  CB  PHE B  31     -21.856 -48.036 -18.542  1.00 28.11           C  
ANISOU  361  CB  PHE B  31     3408   3407   3864   -383    165   -855       C  
ATOM    362  CG  PHE B  31     -22.894 -47.738 -19.583  1.00 28.91           C  
ANISOU  362  CG  PHE B  31     3441   3623   3918   -429    127   -939       C  
ATOM    363  CD1 PHE B  31     -23.831 -48.696 -19.955  1.00 31.41           C  
ANISOU  363  CD1 PHE B  31     3737   3932   4265   -527    146  -1027       C  
ATOM    364  CD2 PHE B  31     -22.923 -46.498 -20.207  1.00 30.19           C  
ANISOU  364  CD2 PHE B  31     3559   3906   4005   -373     75   -931       C  
ATOM    365  CE1 PHE B  31     -24.790 -48.416 -20.923  1.00 33.39           C  
ANISOU  365  CE1 PHE B  31     3916   4306   4465   -568    108  -1108       C  
ATOM    366  CE2 PHE B  31     -23.876 -46.213 -21.179  1.00 30.02           C  
ANISOU  366  CE2 PHE B  31     3471   4002   3931   -404     41  -1004       C  
ATOM    367  CZ  PHE B  31     -24.812 -47.170 -21.532  1.00 32.51           C  
ANISOU  367  CZ  PHE B  31     3758   4321   4271   -501     54  -1094       C  
ATOM    368  N   GLY B  32     -21.145 -48.567 -15.136  1.00 26.06           N  
ANISOU  368  N   GLY B  32     3234   2959   3706   -338    254   -642       N  
ATOM    369  CA  GLY B  32     -20.050 -48.996 -14.271  1.00 25.57           C  
ANISOU  369  CA  GLY B  32     3234   2802   3676   -282    291   -568       C  
ATOM    370  C   GLY B  32     -19.077 -47.871 -13.966  1.00 24.85           C  
ANISOU  370  C   GLY B  32     3143   2761   3538   -191    255   -501       C  
ATOM    371  O   GLY B  32     -19.470 -46.699 -13.889  1.00 23.88           O  
ANISOU  371  O   GLY B  32     2974   2731   3367   -175    211   -483       O  
ATOM    372  N   LYS B  33     -17.813 -48.241 -13.780  1.00 24.34           N  
ANISOU  372  N   LYS B  33     3127   2633   3486   -132    276   -464       N  
ATOM    373  CA ALYS B  33     -16.782 -47.283 -13.397  0.50 24.06           C  
ANISOU  373  CA ALYS B  33     3092   2638   3410    -52    247   -399       C  
ATOM    374  CA BLYS B  33     -16.747 -47.316 -13.401  0.50 24.43           C  
ANISOU  374  CA BLYS B  33     3140   2682   3458    -51    249   -399       C  
ATOM    375  C   LYS B  33     -16.147 -46.639 -14.626  1.00 24.25           C  
ANISOU  375  C   LYS B  33     3103   2720   3390    -21    208   -439       C  
ATOM    376  O   LYS B  33     -15.610 -47.322 -15.502  1.00 25.23           O  
ANISOU  376  O   LYS B  33     3253   2807   3525    -17    222   -485       O  
ATOM    377  CB ALYS B  33     -15.712 -47.960 -12.531  0.50 24.27           C  
ANISOU  377  CB ALYS B  33     3170   2585   3467      1    289   -334       C  
ATOM    378  CB BLYS B  33     -15.641 -48.096 -12.682  0.50 24.81           C  
ANISOU  378  CB BLYS B  33     3243   2645   3538      0    292   -342       C  
ATOM    379  CG ALYS B  33     -14.649 -47.018 -11.971  0.50 22.74           C  
ANISOU  379  CG ALYS B  33     2969   2438   3232     77    261   -267       C  
ATOM    380  CG BLYS B  33     -15.646 -47.996 -11.172  0.50 25.73           C  
ANISOU  380  CG BLYS B  33     3364   2748   3663     25    310   -257       C  
ATOM    381  CD ALYS B  33     -15.122 -46.323 -10.691  0.50 23.56           C  
ANISOU  381  CD ALYS B  33     3051   2578   3322     82    251   -205       C  
ATOM    382  CD BLYS B  33     -14.358 -47.360 -10.665  0.50 25.93           C  
ANISOU  382  CD BLYS B  33     3394   2803   3654    108    292   -193       C  
ATOM    383  CE ALYS B  33     -15.307 -47.322  -9.561  0.50 24.93           C  
ANISOU  383  CE ALYS B  33     3256   2676   3540     80    305   -155       C  
ATOM    384  CE BLYS B  33     -14.522 -46.846  -9.237  0.50 26.41           C  
ANISOU  384  CE BLYS B  33     3443   2890   3702    130    289   -119       C  
ATOM    385  NZ ALYS B  33     -14.292 -48.415  -9.621  0.50 26.55           N  
ANISOU  385  NZ ALYS B  33     3512   2798   3775    120    350   -140       N  
ATOM    386  NZ BLYS B  33     -15.181 -45.514  -9.185  0.50 28.12           N  
ANISOU  386  NZ BLYS B  33     3612   3196   3875    115    239   -125       N  
ATOM    387  N   THR B  34     -16.202 -45.314 -14.675  1.00 23.44           N  
ANISOU  387  N   THR B  34     2963   2706   3237      2    162   -419       N  
ATOM    388  CA  THR B  34     -15.653 -44.571 -15.799  1.00 24.17           C  
ANISOU  388  CA  THR B  34     3041   2858   3283     33    127   -447       C  
ATOM    389  C   THR B  34     -14.836 -43.356 -15.334  1.00 21.94           C  
ANISOU  389  C   THR B  34     2751   2621   2963     90    100   -383       C  
ATOM    390  O   THR B  34     -15.029 -42.842 -14.226  1.00 21.08           O  
ANISOU  390  O   THR B  34     2636   2519   2852     98     97   -330       O  
ATOM    391  CB  THR B  34     -16.777 -44.110 -16.752  1.00 24.96           C  
ANISOU  391  CB  THR B  34     3097   3035   3351     -6     97   -510       C  
ATOM    392  OG1 THR B  34     -16.194 -43.505 -17.911  1.00 30.20           O  
ANISOU  392  OG1 THR B  34     3751   3753   3970     27     70   -535       O  
ATOM    393  CG2 THR B  34     -17.677 -43.116 -16.090  1.00 25.32           C  
ANISOU  393  CG2 THR B  34     3105   3142   3371    -13     74   -477       C  
ATOM    394  N   GLN B  35     -13.930 -42.902 -16.189  1.00 20.95           N  
ANISOU  394  N   GLN B  35     2626   2525   2808    127     83   -391       N  
ATOM    395  CA  GLN B  35     -13.138 -41.720 -15.877  1.00 18.92           C  
ANISOU  395  CA  GLN B  35     2361   2310   2516    172     60   -340       C  
ATOM    396  C   GLN B  35     -14.007 -40.487 -16.053  1.00 18.02           C  
ANISOU  396  C   GLN B  35     2215   2268   2363    162     27   -342       C  
ATOM    397  O   GLN B  35     -14.488 -40.212 -17.166  1.00 19.25           O  
ANISOU  397  O   GLN B  35     2351   2470   2491    153     11   -387       O  
ATOM    398  CB  GLN B  35     -11.919 -41.616 -16.784  1.00 18.53           C  
ANISOU  398  CB  GLN B  35     2318   2273   2447    210     56   -346       C  
ATOM    399  CG  GLN B  35     -11.109 -40.329 -16.553  1.00 17.66           C  
ANISOU  399  CG  GLN B  35     2197   2210   2302    245     33   -298       C  
ATOM    400  CD  GLN B  35      -9.873 -40.247 -17.440  1.00 18.48           C  
ANISOU  400  CD  GLN B  35     2302   2329   2387    281     34   -301       C  
ATOM    401  OE1 GLN B  35      -9.272 -41.266 -17.763  1.00 18.07           O  
ANISOU  401  OE1 GLN B  35     2269   2241   2355    296     57   -317       O  
ATOM    402  NE2 GLN B  35      -9.482 -39.025 -17.822  1.00 15.70           N  
ANISOU  402  NE2 GLN B  35     1934   2032   1998    295     12   -283       N  
ATOM    403  N   VAL B  36     -14.203 -39.756 -14.962  1.00 16.61           N  
ANISOU  403  N   VAL B  36     2032   2100   2178    169     19   -293       N  
ATOM    404  CA AVAL B  36     -14.975 -38.515 -15.012  0.50 15.84           C  
ANISOU  404  CA AVAL B  36     1911   2066   2042    170     -7   -288       C  
ATOM    405  CA BVAL B  36     -14.984 -38.514 -14.980  0.50 15.64           C  
ANISOU  405  CA BVAL B  36     1885   2039   2017    170     -6   -287       C  
ATOM    406  C   VAL B  36     -14.100 -37.284 -15.214  1.00 15.11           C  
ANISOU  406  C   VAL B  36     1822   2004   1914    207    -25   -258       C  
ATOM    407  O   VAL B  36     -14.545 -36.278 -15.776  1.00 14.85           O  
ANISOU  407  O   VAL B  36     1775   2021   1844    217    -43   -263       O  
ATOM    408  CB AVAL B  36     -15.911 -38.333 -13.782  0.50 15.99           C  
ANISOU  408  CB AVAL B  36     1922   2085   2069    154     -4   -259       C  
ATOM    409  CB BVAL B  36     -15.875 -38.351 -13.694  0.50 15.69           C  
ANISOU  409  CB BVAL B  36     1885   2044   2033    155     -3   -256       C  
ATOM    410  CG1AVAL B  36     -17.046 -39.331 -13.841  0.50 16.40           C  
ANISOU  410  CG1AVAL B  36     1958   2124   2147    107     11   -296       C  
ATOM    411  CG1BVAL B  36     -15.047 -38.304 -12.409  0.50 15.11           C  
ANISOU  411  CG1BVAL B  36     1832   1935   1972    178      5   -200       C  
ATOM    412  CG2AVAL B  36     -15.155 -38.423 -12.449  0.50 15.49           C  
ANISOU  412  CG2AVAL B  36     1880   1982   2024    174      7   -204       C  
ATOM    413  CG2BVAL B  36     -16.779 -37.110 -13.797  0.50 14.45           C  
ANISOU  413  CG2BVAL B  36     1705   1951   1833    162    -27   -253       C  
ATOM    414  N   GLY B  37     -12.845 -37.371 -14.788  1.00 14.74           N  
ANISOU  414  N   GLY B  37     1791   1929   1877    229    -17   -227       N  
ATOM    415  CA  GLY B  37     -11.945 -36.234 -14.886  1.00 13.88           C  
ANISOU  415  CA  GLY B  37     1685   1847   1741    254    -31   -200       C  
ATOM    416  C   GLY B  37     -10.543 -36.626 -14.472  1.00 13.54           C  
ANISOU  416  C   GLY B  37     1652   1780   1712    273    -21   -174       C  
ATOM    417  O   GLY B  37     -10.204 -37.815 -14.442  1.00 13.90           O  
ANISOU  417  O   GLY B  37     1706   1789   1785    277     -1   -181       O  
ATOM    418  N   VAL B  38      -9.759 -35.610 -14.115  1.00 13.20           N  
ANISOU  418  N   VAL B  38     1606   1757   1649    285    -31   -143       N  
ATOM    419  CA  VAL B  38      -8.334 -35.723 -13.859  1.00 12.85           C  
ANISOU  419  CA  VAL B  38     1561   1714   1607    304    -27   -119       C  
ATOM    420  C   VAL B  38      -7.977 -34.824 -12.670  1.00 13.24           C  
ANISOU  420  C   VAL B  38     1608   1776   1644    302    -38    -85       C  
ATOM    421  O   VAL B  38      -8.643 -33.818 -12.416  1.00 12.45           O  
ANISOU  421  O   VAL B  38     1513   1688   1528    289    -50    -84       O  
ATOM    422  CB  VAL B  38      -7.525 -35.266 -15.103  1.00 13.14           C  
ANISOU  422  CB  VAL B  38     1590   1778   1623    314    -28   -130       C  
ATOM    423  CG1 VAL B  38      -5.990 -35.413 -14.892  1.00 13.57           C  
ANISOU  423  CG1 VAL B  38     1634   1844   1678    333    -22   -105       C  
ATOM    424  CG2 VAL B  38      -7.945 -36.070 -16.355  1.00 13.09           C  
ANISOU  424  CG2 VAL B  38     1586   1767   1621    317    -19   -171       C  
ATOM    425  N   GLY B  39      -6.935 -35.206 -11.938  1.00 13.19           N  
ANISOU  425  N   GLY B  39     1595   1773   1643    318    -34    -61       N  
ATOM    426  CA  GLY B  39      -6.458 -34.416 -10.810  1.00 12.64           C  
ANISOU  426  CA  GLY B  39     1517   1725   1557    314    -46    -35       C  
ATOM    427  C   GLY B  39      -4.947 -34.486 -10.700  1.00 13.37           C  
ANISOU  427  C   GLY B  39     1589   1848   1641    330    -46    -18       C  
ATOM    428  O   GLY B  39      -4.295 -35.313 -11.356  1.00 13.26           O  
ANISOU  428  O   GLY B  39     1569   1833   1636    352    -32    -19       O  
ATOM    429  N   VAL B  40      -4.402 -33.605  -9.873  1.00 13.64           N  
ANISOU  429  N   VAL B  40     1611   1914   1656    318    -61     -5       N  
ATOM    430  CA  VAL B  40      -2.961 -33.454  -9.740  1.00 14.24           C  
ANISOU  430  CA  VAL B  40     1657   2034   1717    324    -64      6       C  
ATOM    431  C   VAL B  40      -2.631 -33.547  -8.250  1.00 15.01           C  
ANISOU  431  C   VAL B  40     1741   2160   1802    334    -74     28       C  
ATOM    432  O   VAL B  40      -3.170 -32.778  -7.421  1.00 14.37           O  
ANISOU  432  O   VAL B  40     1669   2081   1709    314    -87     24       O  
ATOM    433  CB  VAL B  40      -2.451 -32.102 -10.310  1.00 14.02           C  
ANISOU  433  CB  VAL B  40     1623   2030   1674    287    -74     -4       C  
ATOM    434  CG1 VAL B  40      -0.921 -31.975 -10.072  1.00 15.26           C  
ANISOU  434  CG1 VAL B  40     1739   2243   1814    286    -77      6       C  
ATOM    435  CG2 VAL B  40      -2.782 -31.966 -11.803  1.00 14.85           C  
ANISOU  435  CG2 VAL B  40     1741   2115   1784    284    -63    -20       C  
ATOM    436  N   GLN B  41      -1.776 -34.511  -7.919  1.00 15.51           N  
ANISOU  436  N   GLN B  41     1782   2246   1863    373    -64     50       N  
ATOM    437  CA  GLN B  41      -1.272 -34.661  -6.555  1.00 16.13           C  
ANISOU  437  CA  GLN B  41     1839   2369   1920    394    -73     75       C  
ATOM    438  C   GLN B  41       0.052 -33.917  -6.459  1.00 17.46           C  
ANISOU  438  C   GLN B  41     1963   2609   2059    378    -89     71       C  
ATOM    439  O   GLN B  41       0.983 -34.196  -7.220  1.00 17.36           O  
ANISOU  439  O   GLN B  41     1927   2621   2045    390    -81     75       O  
ATOM    440  CB  GLN B  41      -1.106 -36.143  -6.171  1.00 16.60           C  
ANISOU  440  CB  GLN B  41     1900   2417   1990    453    -49    108       C  
ATOM    441  CG  GLN B  41      -0.469 -36.356  -4.788  1.00 16.86           C  
ANISOU  441  CG  GLN B  41     1905   2510   1992    488    -55    141       C  
ATOM    442  CD  GLN B  41      -1.469 -36.246  -3.656  1.00 18.86           C  
ANISOU  442  CD  GLN B  41     2176   2747   2240    486    -59    150       C  
ATOM    443  OE1 GLN B  41      -2.636 -35.948  -3.878  1.00 18.00           O  
ANISOU  443  OE1 GLN B  41     2100   2587   2152    455    -58    132       O  
ATOM    444  NE2 GLN B  41      -1.009 -36.484  -2.429  1.00 19.71           N  
ANISOU  444  NE2 GLN B  41     2262   2910   2318    523    -63    180       N  
ATOM    445  N   LYS B  42       0.121 -32.963  -5.531  1.00 18.86           N  
ANISOU  445  N   LYS B  42     2130   2822   2213    348   -111     62       N  
ATOM    446  CA  LYS B  42       1.343 -32.205  -5.295  1.00 21.46           C  
ANISOU  446  CA  LYS B  42     2414   3225   2513    321   -129     52       C  
ATOM    447  C   LYS B  42       1.432 -31.832  -3.824  1.00 22.51           C  
ANISOU  447  C   LYS B  42     2530   3409   2614    317   -150     50       C  
ATOM    448  O   LYS B  42       0.492 -31.246  -3.247  1.00 21.32           O  
ANISOU  448  O   LYS B  42     2411   3227   2463    297   -158     36       O  
ATOM    449  CB  LYS B  42       1.375 -30.929  -6.140  1.00 22.02           C  
ANISOU  449  CB  LYS B  42     2495   3278   2591    257   -132     20       C  
ATOM    450  CG  LYS B  42       2.694 -30.142  -5.970  1.00 26.45           C  
ANISOU  450  CG  LYS B  42     3006   3913   3127    217   -146      7       C  
ATOM    451  CD  LYS B  42       2.456 -28.636  -5.963  1.00 31.23           C  
ANISOU  451  CD  LYS B  42     3634   4497   3733    145   -153    -27       C  
ATOM    452  CE  LYS B  42       3.776 -27.858  -5.968  1.00 34.53           C  
ANISOU  452  CE  LYS B  42     4003   4981   4133     92   -161    -45       C  
ATOM    453  NZ  LYS B  42       3.543 -26.405  -6.226  1.00 37.09           N  
ANISOU  453  NZ  LYS B  42     4361   5263   4467     19   -157    -77       N  
ATOM    454  N   GLU B  43       2.570 -32.180  -3.226  1.00 23.88           N  
ANISOU  454  N   GLU B  43     2649   3666   2756    342   -158     65       N  
ATOM    455  CA  GLU B  43       2.855 -31.871  -1.825  1.00 25.65           C  
ANISOU  455  CA  GLU B  43     2845   3961   2939    344   -181     62       C  
ATOM    456  C   GLU B  43       1.786 -32.394  -0.880  1.00 24.98           C  
ANISOU  456  C   GLU B  43     2794   3845   2852    384   -177     83       C  
ATOM    457  O   GLU B  43       1.321 -31.689   0.026  1.00 26.08           O  
ANISOU  457  O   GLU B  43     2943   3996   2971    362   -194     63       O  
ATOM    458  CB  GLU B  43       3.080 -30.364  -1.656  1.00 26.90           C  
ANISOU  458  CB  GLU B  43     2996   4140   3083    264   -204     12       C  
ATOM    459  CG  GLU B  43       4.506 -29.950  -2.050  1.00 31.20           C  
ANISOU  459  CG  GLU B  43     3481   4762   3610    229   -213     -2       C  
ATOM    460  CD  GLU B  43       4.696 -28.452  -2.193  1.00 35.79           C  
ANISOU  460  CD  GLU B  43     4067   5339   4193    137   -224    -52       C  
ATOM    461  OE1 GLU B  43       5.757 -28.064  -2.720  1.00 39.81           O  
ANISOU  461  OE1 GLU B  43     4532   5896   4697     98   -225    -65       O  
ATOM    462  OE2 GLU B  43       3.809 -27.662  -1.792  1.00 36.59           O  
ANISOU  462  OE2 GLU B  43     4215   5387   4298    105   -229    -79       O  
ATOM    463  N   GLY B  44       1.391 -33.641  -1.104  1.00 23.78           N  
ANISOU  463  N   GLY B  44     2661   3650   2722    442   -150    122       N  
ATOM    464  CA  GLY B  44       0.407 -34.302  -0.264  1.00 22.35           C  
ANISOU  464  CA  GLY B  44     2511   3436   2545    482   -137    151       C  
ATOM    465  C   GLY B  44      -1.028 -33.840  -0.435  1.00 20.23           C  
ANISOU  465  C   GLY B  44     2294   3088   2304    447   -133    131       C  
ATOM    466  O   GLY B  44      -1.887 -34.212   0.350  1.00 20.86           O  
ANISOU  466  O   GLY B  44     2394   3148   2382    471   -125    151       O  
ATOM    467  N   VAL B  45      -1.298 -33.028  -1.457  1.00 18.28           N  
ANISOU  467  N   VAL B  45     2066   2799   2079    394   -138     95       N  
ATOM    468  CA  VAL B  45      -2.663 -32.518  -1.664  1.00 15.88           C  
ANISOU  468  CA  VAL B  45     1807   2430   1796    366   -135     77       C  
ATOM    469  C   VAL B  45      -3.108 -32.848  -3.078  1.00 15.44           C  
ANISOU  469  C   VAL B  45     1775   2311   1780    357   -117     71       C  
ATOM    470  O   VAL B  45      -2.340 -32.682  -4.034  1.00 15.11           O  
ANISOU  470  O   VAL B  45     1720   2277   1744    343   -117     60       O  
ATOM    471  CB  VAL B  45      -2.741 -30.995  -1.411  1.00 15.87           C  
ANISOU  471  CB  VAL B  45     1814   2441   1775    314   -158     38       C  
ATOM    472  CG1 VAL B  45      -4.101 -30.429  -1.839  1.00 14.23           C  
ANISOU  472  CG1 VAL B  45     1652   2167   1586    294   -151     22       C  
ATOM    473  CG2 VAL B  45      -2.476 -30.688   0.079  1.00 15.18           C  
ANISOU  473  CG2 VAL B  45     1706   2416   1643    323   -177     36       C  
ATOM    474  N   PHE B  46      -4.348 -33.322  -3.195  1.00 14.13           N  
ANISOU  474  N   PHE B  46     1640   2090   1638    365   -101     77       N  
ATOM    475  CA  PHE B  46      -4.922 -33.665  -4.487  1.00 13.65           C  
ANISOU  475  CA  PHE B  46     1600   1976   1610    355    -86     65       C  
ATOM    476  C   PHE B  46      -5.847 -32.550  -4.985  1.00 13.06           C  
ANISOU  476  C   PHE B  46     1548   1877   1535    318    -95     36       C  
ATOM    477  O   PHE B  46      -6.806 -32.163  -4.305  1.00 13.00           O  
ANISOU  477  O   PHE B  46     1556   1861   1520    315    -99     35       O  
ATOM    478  CB  PHE B  46      -5.678 -34.985  -4.373  1.00 13.20           C  
ANISOU  478  CB  PHE B  46     1558   1876   1580    383    -60     86       C  
ATOM    479  CG  PHE B  46      -6.117 -35.536  -5.691  1.00 14.70           C  
ANISOU  479  CG  PHE B  46     1763   2019   1801    374    -44     68       C  
ATOM    480  CD1 PHE B  46      -5.201 -36.129  -6.543  1.00 16.24           C  
ANISOU  480  CD1 PHE B  46     1949   2213   2006    390    -34     66       C  
ATOM    481  CD2 PHE B  46      -7.446 -35.463  -6.083  1.00 14.07           C  
ANISOU  481  CD2 PHE B  46     1702   1903   1737    352    -40     50       C  
ATOM    482  CE1 PHE B  46      -5.598 -36.641  -7.796  1.00 16.19           C  
ANISOU  482  CE1 PHE B  46     1958   2167   2025    382    -20     42       C  
ATOM    483  CE2 PHE B  46      -7.853 -35.979  -7.328  1.00 13.23           C  
ANISOU  483  CE2 PHE B  46     1606   1764   1656    342    -28     25       C  
ATOM    484  CZ  PHE B  46      -6.922 -36.589  -8.170  1.00 15.30           C  
ANISOU  484  CZ  PHE B  46     1864   2022   1927    357    -17     21       C  
ATOM    485  N   HIS B  47      -5.526 -32.038  -6.170  1.00 13.10           N  
ANISOU  485  N   HIS B  47     1555   1875   1545    298    -96     16       N  
ATOM    486  CA  HIS B  47      -6.157 -30.855  -6.741  1.00 13.10           C  
ANISOU  486  CA  HIS B  47     1577   1859   1540    269   -102     -5       C  
ATOM    487  C   HIS B  47      -6.957 -31.236  -7.983  1.00 12.54           C  
ANISOU  487  C   HIS B  47     1519   1757   1488    272    -90    -16       C  
ATOM    488  O   HIS B  47      -6.431 -31.897  -8.875  1.00 12.94           O  
ANISOU  488  O   HIS B  47     1559   1805   1551    280    -81    -18       O  
ATOM    489  CB  HIS B  47      -5.096 -29.861  -7.195  1.00 12.90           C  
ANISOU  489  CB  HIS B  47     1543   1854   1502    242   -109    -17       C  
ATOM    490  CG  HIS B  47      -4.120 -29.452  -6.127  1.00 13.73           C  
ANISOU  490  CG  HIS B  47     1627   2003   1587    230   -123    -16       C  
ATOM    491  ND1 HIS B  47      -3.045 -30.232  -5.751  1.00 14.15           N  
ANISOU  491  ND1 HIS B  47     1643   2099   1634    248   -125     -1       N  
ATOM    492  CD2 HIS B  47      -4.026 -28.308  -5.407  1.00 14.72           C  
ANISOU  492  CD2 HIS B  47     1761   2139   1692    201   -135    -33       C  
ATOM    493  CE1 HIS B  47      -2.346 -29.596  -4.822  1.00 14.13           C  
ANISOU  493  CE1 HIS B  47     1621   2142   1606    229   -142     -9       C  
ATOM    494  NE2 HIS B  47      -2.925 -28.430  -4.591  1.00 13.94           N  
ANISOU  494  NE2 HIS B  47     1625   2095   1574    197   -148    -32       N  
ATOM    495  N   THR B  48      -8.197 -30.769  -8.067  1.00 12.07           N  
ANISOU  495  N   THR B  48     1479   1679   1425    268    -90    -25       N  
ATOM    496  CA  THR B  48      -8.970 -30.944  -9.300  1.00 11.83           C  
ANISOU  496  CA  THR B  48     1455   1634   1403    269    -82    -40       C  
ATOM    497  C   THR B  48      -9.965 -29.780  -9.482  1.00 11.79           C  
ANISOU  497  C   THR B  48     1471   1628   1380    266    -86    -48       C  
ATOM    498  O   THR B  48      -9.926 -28.792  -8.739  1.00 11.73           O  
ANISOU  498  O   THR B  48     1478   1621   1355    260    -92    -44       O  
ATOM    499  CB  THR B  48      -9.614 -32.378  -9.364  1.00 12.18           C  
ANISOU  499  CB  THR B  48     1493   1662   1473    279    -71    -41       C  
ATOM    500  OG1 THR B  48     -10.164 -32.606 -10.666  1.00 13.16           O  
ANISOU  500  OG1 THR B  48     1616   1781   1601    276    -66    -65       O  
ATOM    501  CG2 THR B  48     -10.666 -32.576  -8.299  1.00 12.35           C  
ANISOU  501  CG2 THR B  48     1518   1677   1496    281    -69    -31       C  
ATOM    502  N   MET B  49     -10.791 -29.880 -10.514  1.00 11.78           N  
ANISOU  502  N   MET B  49     1471   1627   1378    272    -81    -61       N  
ATOM    503  CA  MET B  49     -11.847 -28.910 -10.763  1.00 12.19           C  
ANISOU  503  CA  MET B  49     1538   1684   1408    280    -82    -64       C  
ATOM    504  C   MET B  49     -13.117 -29.342 -10.047  1.00 11.32           C  
ANISOU  504  C   MET B  49     1422   1579   1298    287    -82    -64       C  
ATOM    505  O   MET B  49     -13.458 -30.538  -9.981  1.00 11.64           O  
ANISOU  505  O   MET B  49     1443   1617   1359    281    -78    -69       O  
ATOM    506  CB  MET B  49     -12.067 -28.751 -12.280  1.00 12.10           C  
ANISOU  506  CB  MET B  49     1524   1686   1385    290    -77    -76       C  
ATOM    507  CG  MET B  49     -10.775 -28.251 -12.971  1.00 14.37           C  
ANISOU  507  CG  MET B  49     1817   1970   1670    283    -71    -71       C  
ATOM    508  SD  MET B  49     -11.026 -27.412 -14.532  1.00 18.44           S  
ANISOU  508  SD  MET B  49     2343   2503   2159    303    -61    -71       S  
ATOM    509  CE  MET B  49     -11.698 -25.869 -13.924  1.00 15.46           C  
ANISOU  509  CE  MET B  49     2004   2110   1760    314    -54    -54       C  
ATOM    510  N   TRP B  50     -13.807 -28.364  -9.479  1.00 11.38           N  
ANISOU  510  N   TRP B  50     1447   1592   1285    299    -84    -57       N  
ATOM    511  CA  TRP B  50     -15.008 -28.635  -8.698  1.00 11.72           C  
ANISOU  511  CA  TRP B  50     1482   1647   1324    307    -83    -52       C  
ATOM    512  C   TRP B  50     -16.067 -29.396  -9.501  1.00 11.90           C  
ANISOU  512  C   TRP B  50     1478   1690   1350    307    -80    -67       C  
ATOM    513  O   TRP B  50     -16.633 -30.373  -8.988  1.00 11.98           O  
ANISOU  513  O   TRP B  50     1468   1702   1379    295    -75    -67       O  
ATOM    514  CB  TRP B  50     -15.588 -27.345  -8.083  1.00 11.15           C  
ANISOU  514  CB  TRP B  50     1436   1578   1221    328    -83    -44       C  
ATOM    515  CG  TRP B  50     -16.615 -27.641  -7.021  1.00 12.72           C  
ANISOU  515  CG  TRP B  50     1625   1793   1414    338    -82    -35       C  
ATOM    516  CD1 TRP B  50     -16.379 -27.763  -5.668  1.00 13.29           C  
ANISOU  516  CD1 TRP B  50     1701   1859   1486    337    -84    -23       C  
ATOM    517  CD2 TRP B  50     -18.019 -27.901  -7.209  1.00 14.23           C  
ANISOU  517  CD2 TRP B  50     1794   2015   1596    351    -78    -36       C  
ATOM    518  NE1 TRP B  50     -17.553 -28.085  -5.012  1.00 13.33           N  
ANISOU  518  NE1 TRP B  50     1691   1887   1484    350    -78    -14       N  
ATOM    519  CE2 TRP B  50     -18.568 -28.176  -5.932  1.00 13.55           C  
ANISOU  519  CE2 TRP B  50     1702   1938   1508    356    -74    -22       C  
ATOM    520  CE3 TRP B  50     -18.864 -27.918  -8.328  1.00 15.00           C  
ANISOU  520  CE3 TRP B  50     1872   2143   1682    360    -76    -49       C  
ATOM    521  CZ2 TRP B  50     -19.931 -28.442  -5.739  1.00 15.63           C  
ANISOU  521  CZ2 TRP B  50     1940   2237   1762    365    -68    -18       C  
ATOM    522  CZ3 TRP B  50     -20.227 -28.211  -8.140  1.00 15.45           C  
ANISOU  522  CZ3 TRP B  50     1900   2241   1728    368    -73    -49       C  
ATOM    523  CH2 TRP B  50     -20.742 -28.463  -6.852  1.00 16.94           C  
ANISOU  523  CH2 TRP B  50     2082   2434   1918    369    -68    -33       C  
ATOM    524  N   HIS B  51     -16.322 -28.984 -10.748  1.00 11.56           N  
ANISOU  524  N   HIS B  51     1433   1667   1291    317    -81    -80       N  
ATOM    525  CA  HIS B  51     -17.349 -29.668 -11.560  1.00 12.35           C  
ANISOU  525  CA  HIS B  51     1501   1801   1388    315    -81   -102       C  
ATOM    526  C   HIS B  51     -17.071 -31.158 -11.796  1.00 12.28           C  
ANISOU  526  C   HIS B  51     1471   1776   1415    283    -77   -122       C  
ATOM    527  O   HIS B  51     -17.982 -31.918 -12.136  1.00 13.47           O  
ANISOU  527  O   HIS B  51     1595   1948   1573    267    -75   -145       O  
ATOM    528  CB  HIS B  51     -17.602 -28.963 -12.895  1.00 12.01           C  
ANISOU  528  CB  HIS B  51     1457   1791   1313    338    -83   -112       C  
ATOM    529  CG  HIS B  51     -16.503 -29.131 -13.908  1.00 11.77           C  
ANISOU  529  CG  HIS B  51     1432   1749   1289    333    -82   -121       C  
ATOM    530  ND1 HIS B  51     -15.482 -28.216 -14.055  1.00 12.02           N  
ANISOU  530  ND1 HIS B  51     1494   1759   1314    342    -77   -102       N  
ATOM    531  CD2 HIS B  51     -16.287 -30.089 -14.845  1.00 13.51           C  
ANISOU  531  CD2 HIS B  51     1632   1979   1521    319    -83   -149       C  
ATOM    532  CE1 HIS B  51     -14.686 -28.597 -15.047  1.00 12.84           C  
ANISOU  532  CE1 HIS B  51     1591   1864   1423    338    -75   -113       C  
ATOM    533  NE2 HIS B  51     -15.151 -29.736 -15.539  1.00 14.04           N  
ANISOU  533  NE2 HIS B  51     1714   2034   1585    326    -79   -142       N  
ATOM    534  N   VAL B  52     -15.822 -31.569 -11.635  1.00 12.39           N  
ANISOU  534  N   VAL B  52     1498   1754   1452    275    -74   -115       N  
ATOM    535  CA  VAL B  52     -15.467 -32.992 -11.792  1.00 12.58           C  
ANISOU  535  CA  VAL B  52     1512   1754   1512    253    -64   -130       C  
ATOM    536  C   VAL B  52     -16.014 -33.868 -10.658  1.00 13.56           C  
ANISOU  536  C   VAL B  52     1631   1858   1663    238    -53   -119       C  
ATOM    537  O   VAL B  52     -16.599 -34.949 -10.913  1.00 13.83           O  
ANISOU  537  O   VAL B  52     1650   1883   1721    213    -41   -140       O  
ATOM    538  CB  VAL B  52     -13.935 -33.185 -11.938  1.00 12.87           C  
ANISOU  538  CB  VAL B  52     1562   1765   1562    258    -62   -122       C  
ATOM    539  CG1 VAL B  52     -13.566 -34.667 -11.915  1.00 12.30           C  
ANISOU  539  CG1 VAL B  52     1486   1659   1525    246    -46   -131       C  
ATOM    540  CG2 VAL B  52     -13.441 -32.531 -13.251  1.00 11.52           C  
ANISOU  540  CG2 VAL B  52     1393   1615   1368    269    -68   -135       C  
ATOM    541  N   THR B  53     -15.831 -33.423  -9.416  1.00 13.70           N  
ANISOU  541  N   THR B  53     1659   1869   1675    249    -53    -86       N  
ATOM    542  CA  THR B  53     -16.203 -34.243  -8.259  1.00 14.72           C  
ANISOU  542  CA  THR B  53     1784   1980   1825    241    -38    -66       C  
ATOM    543  C   THR B  53     -17.448 -33.760  -7.526  1.00 15.20           C  
ANISOU  543  C   THR B  53     1836   2070   1869    244    -39    -55       C  
ATOM    544  O   THR B  53     -18.055 -34.520  -6.754  1.00 15.67           O  
ANISOU  544  O   THR B  53     1886   2121   1946    233    -22    -41       O  
ATOM    545  CB  THR B  53     -15.062 -34.330  -7.194  1.00 15.03           C  
ANISOU  545  CB  THR B  53     1840   2001   1870    258    -36    -33       C  
ATOM    546  OG1 THR B  53     -14.901 -33.067  -6.551  1.00 15.45           O  
ANISOU  546  OG1 THR B  53     1903   2076   1889    275    -52    -20       O  
ATOM    547  CG2 THR B  53     -13.717 -34.822  -7.804  1.00 14.67           C  
ANISOU  547  CG2 THR B  53     1800   1935   1839    262    -33    -37       C  
ATOM    548  N   ARG B  54     -17.787 -32.489  -7.733  1.00 14.53           N  
ANISOU  548  N   ARG B  54     1756   2016   1747    264    -54    -58       N  
ATOM    549  CA  ARG B  54     -18.822 -31.782  -6.964  1.00 14.77           C  
ANISOU  549  CA  ARG B  54     1782   2076   1751    280    -55    -44       C  
ATOM    550  C   ARG B  54     -18.658 -31.966  -5.450  1.00 15.11           C  
ANISOU  550  C   ARG B  54     1834   2108   1798    288    -47    -12       C  
ATOM    551  O   ARG B  54     -19.645 -32.047  -4.720  1.00 15.47           O  
ANISOU  551  O   ARG B  54     1866   2174   1836    292    -38      0       O  
ATOM    552  CB  ARG B  54     -20.246 -32.167  -7.436  1.00 15.63           C  
ANISOU  552  CB  ARG B  54     1857   2223   1858    267    -49    -61       C  
ATOM    553  CG  ARG B  54     -20.469 -31.989  -8.956  1.00 15.13           C  
ANISOU  553  CG  ARG B  54     1779   2186   1782    265    -59    -94       C  
ATOM    554  CD  ARG B  54     -21.928 -32.204  -9.357  1.00 16.23           C  
ANISOU  554  CD  ARG B  54     1876   2381   1907    255    -58   -113       C  
ATOM    555  NE  ARG B  54     -22.790 -31.144  -8.836  1.00 15.93           N  
ANISOU  555  NE  ARG B  54     1835   2386   1828    292    -61    -93       N  
ATOM    556  CZ  ARG B  54     -23.025 -29.984  -9.451  1.00 17.77           C  
ANISOU  556  CZ  ARG B  54     2077   2655   2020    334    -70    -92       C  
ATOM    557  NH1 ARG B  54     -23.825 -29.100  -8.877  1.00 17.35           N  
ANISOU  557  NH1 ARG B  54     2026   2636   1931    373    -68    -72       N  
ATOM    558  NH2 ARG B  54     -22.493 -29.710 -10.645  1.00 16.02           N  
ANISOU  558  NH2 ARG B  54     1864   2434   1788    342    -78   -109       N  
ATOM    559  N   GLY B  55     -17.411 -32.058  -4.988  1.00 14.87           N  
ANISOU  559  N   GLY B  55     1821   2052   1774    292    -50      0       N  
ATOM    560  CA  GLY B  55     -17.126 -32.229  -3.571  1.00 15.54           C  
ANISOU  560  CA  GLY B  55     1911   2135   1855    305    -44     29       C  
ATOM    561  C   GLY B  55     -17.347 -33.623  -2.992  1.00 16.77           C  
ANISOU  561  C   GLY B  55     2053   2273   2042    296    -20     51       C  
ATOM    562  O   GLY B  55     -17.360 -33.781  -1.766  1.00 17.34           O  
ANISOU  562  O   GLY B  55     2127   2353   2105    312    -12     82       O  
ATOM    563  N   ALA B  56     -17.527 -34.626  -3.846  1.00 17.12           N  
ANISOU  563  N   ALA B  56     2087   2294   2121    270     -6     37       N  
ATOM    564  CA  ALA B  56     -17.700 -36.014  -3.388  1.00 18.65           C  
ANISOU  564  CA  ALA B  56     2276   2455   2352    256     24     58       C  
ATOM    565  C   ALA B  56     -16.431 -36.547  -2.717  1.00 18.92           C  
ANISOU  565  C   ALA B  56     2327   2467   2395    280     32     89       C  
ATOM    566  O   ALA B  56     -15.327 -36.084  -2.978  1.00 17.92           O  
ANISOU  566  O   ALA B  56     2208   2344   2254    295     14     82       O  
ATOM    567  CB  ALA B  56     -18.096 -36.925  -4.562  1.00 19.44           C  
ANISOU  567  CB  ALA B  56     2367   2530   2488    218     37     24       C  
ATOM    568  N   VAL B  57     -16.599 -37.537  -1.849  1.00 19.36           N  
ANISOU  568  N   VAL B  57     2385   2501   2470    286     63    125       N  
ATOM    569  CA  VAL B  57     -15.469 -38.115  -1.141  1.00 20.77           C  
ANISOU  569  CA  VAL B  57     2576   2664   2651    319     76    162       C  
ATOM    570  C   VAL B  57     -14.621 -38.944  -2.115  1.00 21.60           C  
ANISOU  570  C   VAL B  57     2692   2726   2788    314     87    147       C  
ATOM    571  O   VAL B  57     -15.156 -39.642  -2.959  1.00 22.32           O  
ANISOU  571  O   VAL B  57     2785   2779   2914    281    104    121       O  
ATOM    572  CB  VAL B  57     -15.981 -38.971   0.043  1.00 21.29           C  
ANISOU  572  CB  VAL B  57     2643   2717   2728    332    113    212       C  
ATOM    573  CG1 VAL B  57     -14.878 -39.813   0.637  1.00 22.52           C  
ANISOU  573  CG1 VAL B  57     2812   2852   2889    373    135    255       C  
ATOM    574  CG2 VAL B  57     -16.590 -38.054   1.102  1.00 22.07           C  
ANISOU  574  CG2 VAL B  57     2731   2870   2784    349     99    229       C  
ATOM    575  N   LEU B  58     -13.306 -38.835  -2.013  1.00 22.56           N  
ANISOU  575  N   LEU B  58     2818   2858   2894    347     76    158       N  
ATOM    576  CA  LEU B  58     -12.432 -39.743  -2.748  1.00 24.96           C  
ANISOU  576  CA  LEU B  58     3133   3123   3226    355     93    154       C  
ATOM    577  C   LEU B  58     -12.085 -40.895  -1.824  1.00 26.46           C  
ANISOU  577  C   LEU B  58     3337   3284   3432    391    133    208       C  
ATOM    578  O   LEU B  58     -11.927 -40.696  -0.617  1.00 27.10           O  
ANISOU  578  O   LEU B  58     3412   3398   3484    424    132    249       O  
ATOM    579  CB  LEU B  58     -11.157 -39.049  -3.182  1.00 24.65           C  
ANISOU  579  CB  LEU B  58     3087   3119   3161    374     63    141       C  
ATOM    580  CG  LEU B  58     -11.295 -37.726  -3.922  1.00 26.39           C  
ANISOU  580  CG  LEU B  58     3297   3372   3358    348     26    100       C  
ATOM    581  CD1 LEU B  58      -9.905 -37.218  -4.276  1.00 28.40           C  
ANISOU  581  CD1 LEU B  58     3543   3654   3591    363      6     95       C  
ATOM    582  CD2 LEU B  58     -12.147 -37.867  -5.179  1.00 28.22           C  
ANISOU  582  CD2 LEU B  58     3531   3577   3612    312     29     58       C  
ATOM    583  N   THR B  59     -11.993 -42.096  -2.381  1.00 27.74           N  
ANISOU  583  N   THR B  59     3520   3381   3636    388    169    207       N  
ATOM    584  CA  THR B  59     -11.566 -43.250  -1.600  1.00 29.41           C  
ANISOU  584  CA  THR B  59     3753   3556   3865    431    215    262       C  
ATOM    585  C   THR B  59     -10.276 -43.793  -2.182  1.00 29.62           C  
ANISOU  585  C   THR B  59     3792   3565   3896    470    223    264       C  
ATOM    586  O   THR B  59     -10.135 -43.905  -3.406  1.00 29.01           O  
ANISOU  586  O   THR B  59     3720   3462   3837    446    218    216       O  
ATOM    587  CB  THR B  59     -12.636 -44.360  -1.552  1.00 30.09           C  
ANISOU  587  CB  THR B  59     3863   3567   4003    398    267    270       C  
ATOM    588  OG1 THR B  59     -12.903 -44.818  -2.882  1.00 32.39           O  
ANISOU  588  OG1 THR B  59     4167   3807   4332    353    274    212       O  
ATOM    589  CG2 THR B  59     -13.919 -43.839  -0.946  1.00 30.93           C  
ANISOU  589  CG2 THR B  59     3950   3699   4100    363    260    273       C  
ATOM    590  N   HIS B  60      -9.325 -44.083  -1.300  1.00 30.25           N  
ANISOU  590  N   HIS B  60     3870   3670   3951    535    235    318       N  
ATOM    591  CA  HIS B  60      -8.028 -44.631  -1.692  1.00 31.41           C  
ANISOU  591  CA  HIS B  60     4024   3813   4096    586    246    330       C  
ATOM    592  C   HIS B  60      -7.363 -45.265  -0.472  1.00 32.62           C  
ANISOU  592  C   HIS B  60     4181   3984   4228    663    276    406       C  
ATOM    593  O   HIS B  60      -7.445 -44.725   0.634  1.00 32.49           O  
ANISOU  593  O   HIS B  60     4143   4028   4173    681    259    438       O  
ATOM    594  CB  HIS B  60      -7.124 -43.542  -2.284  1.00 30.77           C  
ANISOU  594  CB  HIS B  60     3908   3804   3976    584    193    296       C  
ATOM    595  CG  HIS B  60      -5.938 -44.081  -3.025  1.00 31.32           C  
ANISOU  595  CG  HIS B  60     3981   3868   4048    623    204    294       C  
ATOM    596  ND1 HIS B  60      -4.700 -44.235  -2.438  1.00 33.39           N  
ANISOU  596  ND1 HIS B  60     4225   4184   4276    692    205    338       N  
ATOM    597  CD2 HIS B  60      -5.802 -44.504  -4.304  1.00 31.89           C  
ANISOU  597  CD2 HIS B  60     4071   3894   4149    608    215    254       C  
ATOM    598  CE1 HIS B  60      -3.856 -44.744  -3.319  1.00 32.94           C  
ANISOU  598  CE1 HIS B  60     4174   4112   4227    719    218    327       C  
ATOM    599  NE2 HIS B  60      -4.499 -44.913  -4.462  1.00 34.50           N  
ANISOU  599  NE2 HIS B  60     4395   4247   4464    669    224    276       N  
ATOM    600  N   ASN B  61      -6.725 -46.418  -0.669  1.00 34.22           N  
ANISOU  600  N   ASN B  61     4414   4136   4453    713    321    435       N  
ATOM    601  CA  ASN B  61      -5.966 -47.075   0.410  1.00 35.66           C  
ANISOU  601  CA  ASN B  61     4599   4339   4609    802    354    513       C  
ATOM    602  C   ASN B  61      -6.832 -47.426   1.618  1.00 35.66           C  
ANISOU  602  C   ASN B  61     4613   4321   4612    811    387    568       C  
ATOM    603  O   ASN B  61      -6.340 -47.453   2.743  1.00 36.59           O  
ANISOU  603  O   ASN B  61     4716   4499   4687    877    391    629       O  
ATOM    604  CB  ASN B  61      -4.820 -46.164   0.886  1.00 36.18           C  
ANISOU  604  CB  ASN B  61     4612   4528   4606    845    303    524       C  
ATOM    605  CG  ASN B  61      -3.560 -46.291   0.053  1.00 38.44           C  
ANISOU  605  CG  ASN B  61     4885   4837   4881    880    295    510       C  
ATOM    606  OD1 ASN B  61      -3.426 -47.180  -0.789  1.00 41.32           O  
ANISOU  606  OD1 ASN B  61     5286   5127   5286    891    333    501       O  
ATOM    607  ND2 ASN B  61      -2.611 -45.394   0.303  1.00 41.96           N  
ANISOU  607  ND2 ASN B  61     5277   5393   5271    898    247    505       N  
ATOM    608  N   GLY B  62      -8.119 -47.674   1.389  1.00 35.16           N  
ANISOU  608  N   GLY B  62     4575   4185   4597    743    409    545       N  
ATOM    609  CA  GLY B  62      -9.071 -47.908   2.473  1.00 34.94           C  
ANISOU  609  CA  GLY B  62     4555   4144   4574    740    439    593       C  
ATOM    610  C   GLY B  62      -9.452 -46.671   3.282  1.00 34.34           C  
ANISOU  610  C   GLY B  62     4435   4164   4445    726    388    590       C  
ATOM    611  O   GLY B  62     -10.018 -46.786   4.372  1.00 34.62           O  
ANISOU  611  O   GLY B  62     4470   4213   4468    744    409    640       O  
ATOM    612  N   LYS B  63      -9.146 -45.487   2.754  1.00 33.09           N  
ANISOU  612  N   LYS B  63     4243   4071   4258    697    323    532       N  
ATOM    613  CA  LYS B  63      -9.429 -44.233   3.453  1.00 32.23           C  
ANISOU  613  CA  LYS B  63     4098   4048   4098    684    274    521       C  
ATOM    614  C   LYS B  63     -10.400 -43.376   2.652  1.00 30.99           C  
ANISOU  614  C   LYS B  63     3933   3882   3958    603    241    453       C  
ATOM    615  O   LYS B  63     -10.399 -43.426   1.425  1.00 29.96           O  
ANISOU  615  O   LYS B  63     3810   3711   3859    564    235    404       O  
ATOM    616  CB  LYS B  63      -8.130 -43.464   3.712  1.00 32.48           C  
ANISOU  616  CB  LYS B  63     4094   4175   4070    726    228    517       C  
ATOM    617  CG  LYS B  63      -7.288 -44.060   4.839  1.00 34.72           C  
ANISOU  617  CG  LYS B  63     4370   4505   4314    815    251    590       C  
ATOM    618  CD  LYS B  63      -5.819 -43.993   4.502  1.00 38.39           C  
ANISOU  618  CD  LYS B  63     4812   5025   4750    858    229    586       C  
ATOM    619  CE  LYS B  63      -4.994 -44.796   5.497  1.00 41.29           C  
ANISOU  619  CE  LYS B  63     5173   5434   5080    957    260    664       C  
ATOM    620  NZ  LYS B  63      -4.781 -44.028   6.757  1.00 43.96           N  
ANISOU  620  NZ  LYS B  63     5469   5886   5345    987    226    682       N  
ATOM    621  N   ARG B  64     -11.248 -42.636   3.365  1.00 30.33           N  
ANISOU  621  N   ARG B  64     3834   3837   3850    585    224    453       N  
ATOM    622  CA AARG B  64     -12.185 -41.720   2.733  0.50 29.63           C  
ANISOU  622  CA AARG B  64     3737   3754   3767    522    193    395       C  
ATOM    623  CA BARG B  64     -12.204 -41.714   2.766  0.50 29.65           C  
ANISOU  623  CA BARG B  64     3739   3757   3769    522    193    396       C  
ATOM    624  C   ARG B  64     -11.663 -40.291   2.862  1.00 28.86           C  
ANISOU  624  C   ARG B  64     3614   3733   3616    524    135    364       C  
ATOM    625  O   ARG B  64     -11.493 -39.772   3.970  1.00 28.42           O  
ANISOU  625  O   ARG B  64     3546   3738   3514    556    121    387       O  
ATOM    626  CB AARG B  64     -13.600 -41.861   3.316  0.50 30.24           C  
ANISOU  626  CB AARG B  64     3814   3817   3856    496    217    413       C  
ATOM    627  CB BARG B  64     -13.545 -41.796   3.495  0.50 30.28           C  
ANISOU  627  CB BARG B  64     3818   3831   3854    503    216    418       C  
ATOM    628  CG AARG B  64     -14.271 -43.216   3.043  0.50 31.76           C  
ANISOU  628  CG AARG B  64     4031   3924   4111    472    277    432       C  
ATOM    629  CG BARG B  64     -14.270 -43.121   3.354  0.50 31.87           C  
ANISOU  629  CG BARG B  64     4043   3952   4114    482    276    443       C  
ATOM    630  CD AARG B  64     -15.722 -43.043   2.580  0.50 32.70           C  
ANISOU  630  CD AARG B  64     4141   4027   4256    403    280    396       C  
ATOM    631  CD BARG B  64     -15.615 -43.049   4.040  0.50 33.17           C  
ANISOU  631  CD BARG B  64     4198   4125   4280    457    294    461       C  
ATOM    632  NE AARG B  64     -16.455 -42.085   3.403  0.50 33.52           N  
ANISOU  632  NE AARG B  64     4220   4197   4317    406    257    404       N  
ATOM    633  NE BARG B  64     -16.639 -43.770   3.294  0.50 35.66           N  
ANISOU  633  NE BARG B  64     4520   4374   4653    392    328    438       N  
ATOM    634  CZ AARG B  64     -17.547 -41.437   3.006  0.50 34.03           C  
ANISOU  634  CZ AARG B  64     4265   4282   4381    361    239    365       C  
ATOM    635  CZ BARG B  64     -17.365 -43.239   2.314  0.50 35.63           C  
ANISOU  635  CZ BARG B  64     4499   4375   4660    334    301    374       C  
ATOM    636  NH1AARG B  64     -18.147 -40.578   3.823  0.50 34.18           N  
ANISOU  636  NH1AARG B  64     4266   4361   4357    375    222    376       N  
ATOM    637  NH1BARG B  64     -18.280 -43.972   1.696  0.50 37.33           N  
ANISOU  637  NH1BARG B  64     4716   4539   4926    273    332    351       N  
ATOM    638  NH2AARG B  64     -18.037 -41.639   1.788  0.50 33.28           N  
ANISOU  638  NH2AARG B  64     4168   4154   4323    306    238    314       N  
ATOM    639  NH2BARG B  64     -17.183 -41.979   1.953  0.50 35.44           N  
ANISOU  639  NH2BARG B  64     4457   4411   4597    336    245    334       N  
ATOM    640  N   LEU B  65     -11.394 -39.677   1.708  1.00 27.36           N  
ANISOU  640  N   LEU B  65     3420   3539   3433    490    106    310       N  
ATOM    641  CA  LEU B  65     -10.800 -38.336   1.614  1.00 26.31           C  
ANISOU  641  CA  LEU B  65     3271   3464   3259    484     57    275       C  
ATOM    642  C   LEU B  65     -11.875 -37.280   1.345  1.00 24.64           C  
ANISOU  642  C   LEU B  65     3060   3259   3040    443     35    237       C  
ATOM    643  O   LEU B  65     -12.565 -37.315   0.330  1.00 23.15           O  
ANISOU  643  O   LEU B  65     2877   3035   2881    407     39    207       O  
ATOM    644  CB  LEU B  65      -9.742 -38.291   0.500  1.00 27.30           C  
ANISOU  644  CB  LEU B  65     3393   3584   3394    477     43    247       C  
ATOM    645  CG  LEU B  65      -8.371 -38.970   0.613  1.00 29.31           C  
ANISOU  645  CG  LEU B  65     3639   3854   3641    523     52    274       C  
ATOM    646  CD1 LEU B  65      -8.442 -40.374   1.146  1.00 33.45           C  
ANISOU  646  CD1 LEU B  65     4180   4340   4188    564    100    328       C  
ATOM    647  CD2 LEU B  65      -7.686 -38.972  -0.757  1.00 31.52           C  
ANISOU  647  CD2 LEU B  65     3918   4116   3940    505     45    239       C  
ATOM    648  N   GLU B  66     -12.029 -36.363   2.291  1.00 22.76           N  
ANISOU  648  N   GLU B  66     2816   3072   2760    454     15    239       N  
ATOM    649  CA  GLU B  66     -12.984 -35.266   2.159  1.00 21.07           C  
ANISOU  649  CA  GLU B  66     2605   2868   2531    429     -3    207       C  
ATOM    650  C   GLU B  66     -12.263 -34.055   1.616  1.00 18.60           C  
ANISOU  650  C   GLU B  66     2294   2576   2197    413    -38    164       C  
ATOM    651  O   GLU B  66     -11.068 -33.905   1.872  1.00 19.34           O  
ANISOU  651  O   GLU B  66     2378   2697   2271    425    -53    165       O  
ATOM    652  CB  GLU B  66     -13.578 -34.946   3.523  1.00 21.67           C  
ANISOU  652  CB  GLU B  66     2679   2983   2571    454     -1    231       C  
ATOM    653  CG  GLU B  66     -14.483 -36.049   4.038  1.00 23.60           C  
ANISOU  653  CG  GLU B  66     2921   3205   2838    463     38    275       C  
ATOM    654  CD  GLU B  66     -14.439 -36.184   5.534  1.00 22.44           C  
ANISOU  654  CD  GLU B  66     2769   3102   2653    508     48    320       C  
ATOM    655  OE1 GLU B  66     -13.343 -36.117   6.118  1.00 23.69           O  
ANISOU  655  OE1 GLU B  66     2920   3298   2780    541     34    331       O  
ATOM    656  OE2 GLU B  66     -15.512 -36.366   6.125  1.00 24.38           O  
ANISOU  656  OE2 GLU B  66     3012   3351   2897    512     70    344       O  
ATOM    657  N   PRO B  67     -12.965 -33.190   0.846  1.00 17.41           N  
ANISOU  657  N   PRO B  67     2153   2412   2047    386    -50    130       N  
ATOM    658  CA  PRO B  67     -12.285 -31.954   0.423  1.00 16.25           C  
ANISOU  658  CA  PRO B  67     2014   2279   1879    371    -77     94       C  
ATOM    659  C   PRO B  67     -11.895 -31.059   1.603  1.00 16.21           C  
ANISOU  659  C   PRO B  67     2012   2316   1830    383    -96     90       C  
ATOM    660  O   PRO B  67     -12.704 -30.846   2.523  1.00 15.65           O  
ANISOU  660  O   PRO B  67     1946   2263   1737    401    -92    100       O  
ATOM    661  CB  PRO B  67     -13.340 -31.224  -0.426  1.00 15.90           C  
ANISOU  661  CB  PRO B  67     1984   2216   1840    353    -79     69       C  
ATOM    662  CG  PRO B  67     -14.417 -32.236  -0.731  1.00 17.06           C  
ANISOU  662  CG  PRO B  67     2122   2344   2016    350    -56     83       C  
ATOM    663  CD  PRO B  67     -14.379 -33.215   0.421  1.00 16.96           C  
ANISOU  663  CD  PRO B  67     2099   2337   2005    371    -38    123       C  
ATOM    664  N   ASN B  68     -10.670 -30.538   1.581  1.00 15.22           N  
ANISOU  664  N   ASN B  68     1881   2212   1689    373   -115     71       N  
ATOM    665  CA  ASN B  68     -10.230 -29.567   2.586  1.00 14.35           C  
ANISOU  665  CA  ASN B  68     1773   2143   1535    374   -135     52       C  
ATOM    666  C   ASN B  68     -10.546 -28.129   2.229  1.00 13.68           C  
ANISOU  666  C   ASN B  68     1718   2039   1439    347   -146     11       C  
ATOM    667  O   ASN B  68     -10.645 -27.275   3.104  1.00 13.37           O  
ANISOU  667  O   ASN B  68     1693   2021   1365    349   -156     -8       O  
ATOM    668  CB  ASN B  68      -8.722 -29.687   2.873  1.00 15.60           C  
ANISOU  668  CB  ASN B  68     1904   2346   1677    371   -151     49       C  
ATOM    669  CG  ASN B  68      -8.407 -30.819   3.834  1.00 16.40           C  
ANISOU  669  CG  ASN B  68     1979   2487   1765    415   -142     92       C  
ATOM    670  OD1 ASN B  68      -7.852 -30.604   4.912  1.00 21.72           O  
ANISOU  670  OD1 ASN B  68     2635   3222   2395    432   -157     91       O  
ATOM    671  ND2 ASN B  68      -8.778 -32.024   3.456  1.00 17.92           N  
ANISOU  671  ND2 ASN B  68     2170   2647   1992    435   -116    130       N  
ATOM    672  N   TRP B  69     -10.642 -27.858   0.935  1.00 12.87           N  
ANISOU  672  N   TRP B  69     1629   1897   1364    325   -140     -1       N  
ATOM    673  CA  TRP B  69     -10.962 -26.532   0.462  1.00 12.35           C  
ANISOU  673  CA  TRP B  69     1596   1805   1290    306   -142    -32       C  
ATOM    674  C   TRP B  69     -11.777 -26.698  -0.827  1.00 12.44           C  
ANISOU  674  C   TRP B  69     1616   1780   1328    307   -128    -26       C  
ATOM    675  O   TRP B  69     -11.452 -27.526  -1.666  1.00 11.62           O  
ANISOU  675  O   TRP B  69     1494   1669   1252    301   -123    -16       O  
ATOM    676  CB  TRP B  69      -9.679 -25.691   0.238  1.00 12.74           C  
ANISOU  676  CB  TRP B  69     1650   1858   1334    268   -155    -62       C  
ATOM    677  CG  TRP B  69      -9.998 -24.379  -0.395  1.00 12.90           C  
ANISOU  677  CG  TRP B  69     1712   1836   1352    249   -148    -88       C  
ATOM    678  CD1 TRP B  69     -10.453 -23.255   0.226  1.00 14.56           C  
ANISOU  678  CD1 TRP B  69     1960   2032   1537    250   -147   -112       C  
ATOM    679  CD2 TRP B  69      -9.985 -24.087  -1.806  1.00 13.51           C  
ANISOU  679  CD2 TRP B  69     1802   1876   1453    235   -135    -88       C  
ATOM    680  NE1 TRP B  69     -10.709 -22.268  -0.712  1.00 15.92           N  
ANISOU  680  NE1 TRP B  69     2172   2156   1718    238   -132   -124       N  
ATOM    681  CE2 TRP B  69     -10.414 -22.754  -1.963  1.00 14.23           C  
ANISOU  681  CE2 TRP B  69     1941   1931   1532    230   -125   -108       C  
ATOM    682  CE3 TRP B  69      -9.618 -24.822  -2.945  1.00 14.52           C  
ANISOU  682  CE3 TRP B  69     1908   2000   1608    231   -130    -74       C  
ATOM    683  CZ2 TRP B  69     -10.513 -22.133  -3.228  1.00 14.99           C  
ANISOU  683  CZ2 TRP B  69     2063   1989   1642    223   -108   -107       C  
ATOM    684  CZ3 TRP B  69      -9.712 -24.210  -4.201  1.00 14.57           C  
ANISOU  684  CZ3 TRP B  69     1936   1974   1626    221   -117    -77       C  
ATOM    685  CH2 TRP B  69     -10.156 -22.881  -4.330  1.00 16.27           C  
ANISOU  685  CH2 TRP B  69     2197   2156   1828    219   -105    -91       C  
ATOM    686  N   ALA B  70     -12.851 -25.925  -0.970  1.00 12.68           N  
ANISOU  686  N   ALA B  70     1674   1794   1347    319   -121    -33       N  
ATOM    687  CA  ALA B  70     -13.642 -25.990  -2.197  1.00 11.50           C  
ANISOU  687  CA  ALA B  70     1529   1625   1215    324   -109    -29       C  
ATOM    688  C   ALA B  70     -14.219 -24.636  -2.559  1.00 12.05           C  
ANISOU  688  C   ALA B  70     1638   1675   1265    333   -103    -44       C  
ATOM    689  O   ALA B  70     -14.690 -23.912  -1.697  1.00 11.63           O  
ANISOU  689  O   ALA B  70     1608   1623   1186    350   -102    -50       O  
ATOM    690  CB  ALA B  70     -14.756 -27.015  -2.072  1.00 12.50           C  
ANISOU  690  CB  ALA B  70     1632   1766   1352    342   -100     -8       C  
ATOM    691  N   SER B  71     -14.199 -24.311  -3.852  1.00 12.00           N  
ANISOU  691  N   SER B  71     1640   1649   1268    328    -95    -47       N  
ATOM    692  CA  SER B  71     -14.853 -23.093  -4.328  1.00 12.93           C  
ANISOU  692  CA  SER B  71     1797   1747   1367    349    -82    -52       C  
ATOM    693  C   SER B  71     -15.581 -23.362  -5.641  1.00 12.88           C  
ANISOU  693  C   SER B  71     1778   1749   1366    367    -74    -42       C  
ATOM    694  O   SER B  71     -14.957 -23.613  -6.681  1.00 12.73           O  
ANISOU  694  O   SER B  71     1748   1724   1362    350    -73    -43       O  
ATOM    695  CB  SER B  71     -13.868 -21.940  -4.497  1.00 13.75           C  
ANISOU  695  CB  SER B  71     1940   1814   1468    325    -77    -69       C  
ATOM    696  OG  SER B  71     -14.525 -20.846  -5.144  1.00 15.01           O  
ANISOU  696  OG  SER B  71     2142   1946   1612    351    -56    -66       O  
ATOM    697  N   VAL B  72     -16.905 -23.322  -5.589  1.00 13.00           N  
ANISOU  697  N   VAL B  72     1789   1788   1363    402    -68    -33       N  
ATOM    698  CA  VAL B  72     -17.708 -23.473  -6.815  1.00 13.73           C  
ANISOU  698  CA  VAL B  72     1864   1902   1449    423    -62    -27       C  
ATOM    699  C   VAL B  72     -17.432 -22.293  -7.763  1.00 14.43           C  
ANISOU  699  C   VAL B  72     1992   1965   1523    440    -48    -25       C  
ATOM    700  O   VAL B  72     -17.367 -22.457  -8.994  1.00 15.14           O  
ANISOU  700  O   VAL B  72     2070   2067   1616    443    -45    -23       O  
ATOM    701  CB  VAL B  72     -19.216 -23.547  -6.465  1.00 13.38           C  
ANISOU  701  CB  VAL B  72     1802   1899   1382    460    -58    -18       C  
ATOM    702  CG1 VAL B  72     -20.109 -23.232  -7.671  1.00 14.94           C  
ANISOU  702  CG1 VAL B  72     1990   2129   1557    495    -51    -14       C  
ATOM    703  CG2 VAL B  72     -19.552 -24.936  -5.877  1.00 13.92           C  
ANISOU  703  CG2 VAL B  72     1823   1994   1471    438    -67    -17       C  
ATOM    704  N   LYS B  73     -17.265 -21.111  -7.182  1.00 15.91           N  
ANISOU  704  N   LYS B  73     2231   2117   1696    451    -36    -26       N  
ATOM    705  CA  LYS B  73     -17.021 -19.892  -7.956  1.00 17.72           C  
ANISOU  705  CA  LYS B  73     2510   2310   1913    467    -13    -20       C  
ATOM    706  C   LYS B  73     -15.722 -19.976  -8.768  1.00 16.90           C  
ANISOU  706  C   LYS B  73     2404   2182   1834    425    -12    -23       C  
ATOM    707  O   LYS B  73     -15.693 -19.628  -9.959  1.00 17.26           O  
ANISOU  707  O   LYS B  73     2458   2225   1873    441      2     -9       O  
ATOM    708  CB  LYS B  73     -17.016 -18.675  -7.018  1.00 18.85           C  
ANISOU  708  CB  LYS B  73     2712   2407   2040    478      1    -27       C  
ATOM    709  CG  LYS B  73     -17.120 -17.354  -7.745  1.00 24.65           C  
ANISOU  709  CG  LYS B  73     3508   3098   2759    510     34    -14       C  
ATOM    710  CD  LYS B  73     -17.353 -16.208  -6.761  1.00 31.59           C  
ANISOU  710  CD  LYS B  73     4451   3931   3620    529     53    -25       C  
ATOM    711  CE  LYS B  73     -16.031 -15.589  -6.326  1.00 36.28           C  
ANISOU  711  CE  LYS B  73     5084   4463   4236    467     59    -52       C  
ATOM    712  NZ  LYS B  73     -15.306 -15.063  -7.529  1.00 41.18           N  
ANISOU  712  NZ  LYS B  73     5729   5045   4873    449     83    -37       N  
ATOM    713  N   LYS B  74     -14.661 -20.460  -8.135  1.00 15.73           N  
ANISOU  713  N   LYS B  74     2240   2025   1709    376    -27    -38       N  
ATOM    714  CA  LYS B  74     -13.371 -20.676  -8.820  1.00 15.61           C  
ANISOU  714  CA  LYS B  74     2213   1999   1717    334    -28    -41       C  
ATOM    715  C   LYS B  74     -13.296 -21.979  -9.605  1.00 14.41           C  
ANISOU  715  C   LYS B  74     2008   1885   1580    332    -41    -38       C  
ATOM    716  O   LYS B  74     -12.333 -22.198 -10.373  1.00 13.73           O  
ANISOU  716  O   LYS B  74     1910   1797   1508    308    -39    -37       O  
ATOM    717  CB  LYS B  74     -12.232 -20.627  -7.806  1.00 15.71           C  
ANISOU  717  CB  LYS B  74     2226   1999   1744    286    -39    -60       C  
ATOM    718  CG  LYS B  74     -12.071 -19.239  -7.222  1.00 18.66           C  
ANISOU  718  CG  LYS B  74     2657   2326   2106    276    -23    -73       C  
ATOM    719  CD  LYS B  74     -10.985 -19.179  -6.188  1.00 23.61           C  
ANISOU  719  CD  LYS B  74     3277   2952   2740    225    -37   -100       C  
ATOM    720  CE  LYS B  74     -10.752 -17.718  -5.779  1.00 25.11           C  
ANISOU  720  CE  LYS B  74     3529   3087   2922    204    -16   -121       C  
ATOM    721  NZ  LYS B  74      -9.596 -17.609  -4.871  1.00 29.75           N  
ANISOU  721  NZ  LYS B  74     4104   3683   3514    146    -32   -155       N  
ATOM    722  N   ASP B  75     -14.311 -22.819  -9.406  1.00 13.40           N  
ANISOU  722  N   ASP B  75     1851   1790   1448    353    -52    -37       N  
ATOM    723  CA  ASP B  75     -14.372 -24.192  -9.957  1.00 12.77           C  
ANISOU  723  CA  ASP B  75     1724   1741   1385    346    -63    -41       C  
ATOM    724  C   ASP B  75     -13.146 -25.036  -9.613  1.00 11.93           C  
ANISOU  724  C   ASP B  75     1596   1628   1306    310    -73    -47       C  
ATOM    725  O   ASP B  75     -12.617 -25.736 -10.471  1.00 11.78           O  
ANISOU  725  O   ASP B  75     1555   1617   1301    301    -73    -51       O  
ATOM    726  CB  ASP B  75     -14.611 -24.163 -11.481  1.00 12.62           C  
ANISOU  726  CB  ASP B  75     1698   1741   1356    365    -55    -39       C  
ATOM    727  CG  ASP B  75     -15.101 -25.501 -12.022  1.00 13.84           C  
ANISOU  727  CG  ASP B  75     1806   1930   1520    362    -65    -53       C  
ATOM    728  OD1 ASP B  75     -15.519 -26.366 -11.216  1.00 12.26           O  
ANISOU  728  OD1 ASP B  75     1585   1737   1335    351    -74    -59       O  
ATOM    729  OD2 ASP B  75     -15.083 -25.679 -13.254  1.00 14.20           O  
ANISOU  729  OD2 ASP B  75     1839   1996   1559    371    -62    -59       O  
ATOM    730  N   LEU B  76     -12.718 -24.998  -8.345  1.00 11.39           N  
ANISOU  730  N   LEU B  76     1533   1553   1242    296    -80    -48       N  
ATOM    731  CA  LEU B  76     -11.513 -25.708  -7.925  1.00 11.12           C  
ANISOU  731  CA  LEU B  76     1476   1523   1226    270    -89    -50       C  
ATOM    732  C   LEU B  76     -11.752 -26.343  -6.574  1.00 10.90           C  
ANISOU  732  C   LEU B  76     1435   1507   1198    274    -98    -45       C  
ATOM    733  O   LEU B  76     -12.569 -25.854  -5.788  1.00 10.83           O  
ANISOU  733  O   LEU B  76     1443   1500   1173    289    -98    -44       O  
ATOM    734  CB  LEU B  76     -10.323 -24.746  -7.805  1.00 11.13           C  
ANISOU  734  CB  LEU B  76     1494   1510   1223    242    -88    -56       C  
ATOM    735  CG  LEU B  76      -9.854 -24.140  -9.142  1.00 12.76           C  
ANISOU  735  CG  LEU B  76     1712   1703   1431    234    -73    -55       C  
ATOM    736  CD1 LEU B  76      -8.773 -23.104  -8.854  1.00 12.63           C  
ANISOU  736  CD1 LEU B  76     1715   1670   1414    197    -68    -63       C  
ATOM    737  CD2 LEU B  76      -9.328 -25.240 -10.091  1.00 12.42           C  
ANISOU  737  CD2 LEU B  76     1633   1679   1404    234    -75    -51       C  
ATOM    738  N   ILE B  77     -11.018 -27.410  -6.289  1.00 11.04           N  
ANISOU  738  N   ILE B  77     1424   1536   1232    267   -103    -38       N  
ATOM    739  CA  ILE B  77     -11.234 -28.136  -5.050  1.00 11.83           C  
ANISOU  739  CA  ILE B  77     1511   1650   1333    278   -106    -26       C  
ATOM    740  C   ILE B  77      -9.970 -28.899  -4.706  1.00 12.46           C  
ANISOU  740  C   ILE B  77     1567   1745   1421    273   -111    -17       C  
ATOM    741  O   ILE B  77      -9.274 -29.399  -5.601  1.00 11.90           O  
ANISOU  741  O   ILE B  77     1483   1671   1367    268   -107    -17       O  
ATOM    742  CB  ILE B  77     -12.476 -29.093  -5.188  1.00 11.90           C  
ANISOU  742  CB  ILE B  77     1509   1657   1355    293    -96    -16       C  
ATOM    743  CG1 ILE B  77     -12.831 -29.762  -3.850  1.00 11.69           C  
ANISOU  743  CG1 ILE B  77     1472   1641   1326    306    -93      3       C  
ATOM    744  CG2 ILE B  77     -12.283 -30.123  -6.345  1.00 12.01           C  
ANISOU  744  CG2 ILE B  77     1506   1660   1397    286    -88    -21       C  
ATOM    745  CD1 ILE B  77     -14.213 -30.495  -3.906  1.00 12.07           C  
ANISOU  745  CD1 ILE B  77     1510   1687   1387    312    -80     10       C  
ATOM    746  N   SER B  78      -9.634 -28.947  -3.426  1.00 12.89           N  
ANISOU  746  N   SER B  78     1614   1822   1460    280   -118     -8       N  
ATOM    747  CA  SER B  78      -8.458 -29.720  -3.031  1.00 13.63           C  
ANISOU  747  CA  SER B  78     1680   1942   1555    286   -122      5       C  
ATOM    748  C   SER B  78      -8.784 -30.673  -1.873  1.00 14.07           C  
ANISOU  748  C   SER B  78     1724   2013   1607    316   -116     33       C  
ATOM    749  O   SER B  78      -9.594 -30.357  -1.008  1.00 14.82           O  
ANISOU  749  O   SER B  78     1830   2114   1685    325   -117     36       O  
ATOM    750  CB  SER B  78      -7.277 -28.799  -2.693  1.00 14.09           C  
ANISOU  750  CB  SER B  78     1730   2030   1591    263   -138    -12       C  
ATOM    751  OG  SER B  78      -7.588 -27.966  -1.588  1.00 15.03           O  
ANISOU  751  OG  SER B  78     1864   2165   1682    259   -149    -24       O  
ATOM    752  N   TYR B  79      -8.141 -31.840  -1.884  1.00 14.93           N  
ANISOU  752  N   TYR B  79     1813   2127   1730    336   -106     56       N  
ATOM    753  CA  TYR B  79      -8.345 -32.904  -0.893  1.00 15.17           C  
ANISOU  753  CA  TYR B  79     1835   2166   1761    371    -91     93       C  
ATOM    754  C   TYR B  79      -7.042 -33.150  -0.141  1.00 16.16           C  
ANISOU  754  C   TYR B  79     1934   2344   1861    394   -100    110       C  
ATOM    755  O   TYR B  79      -5.983 -33.257  -0.754  1.00 15.37           O  
ANISOU  755  O   TYR B  79     1817   2258   1764    392   -104    105       O  
ATOM    756  CB  TYR B  79      -8.742 -34.210  -1.591  1.00 15.29           C  
ANISOU  756  CB  TYR B  79     1856   2137   1817    380    -63    109       C  
ATOM    757  CG  TYR B  79     -10.084 -34.183  -2.298  1.00 15.12           C  
ANISOU  757  CG  TYR B  79     1850   2074   1817    358    -54     92       C  
ATOM    758  CD1 TYR B  79     -10.233 -33.562  -3.547  1.00 15.00           C  
ANISOU  758  CD1 TYR B  79     1842   2047   1810    332    -63     58       C  
ATOM    759  CD2 TYR B  79     -11.205 -34.795  -1.720  1.00 16.05           C  
ANISOU  759  CD2 TYR B  79     1974   2176   1947    364    -35    111       C  
ATOM    760  CE1 TYR B  79     -11.487 -33.547  -4.197  1.00 15.08           C  
ANISOU  760  CE1 TYR B  79     1860   2034   1833    316    -56     42       C  
ATOM    761  CE2 TYR B  79     -12.433 -34.798  -2.347  1.00 13.29           C  
ANISOU  761  CE2 TYR B  79     1630   1802   1614    341    -27     94       C  
ATOM    762  CZ  TYR B  79     -12.571 -34.175  -3.588  1.00 15.13           C  
ANISOU  762  CZ  TYR B  79     1867   2031   1851    319    -40     58       C  
ATOM    763  OH  TYR B  79     -13.805 -34.165  -4.177  1.00 15.63           O  
ANISOU  763  OH  TYR B  79     1928   2085   1923    301    -35     40       O  
ATOM    764  N   GLY B  80      -7.124 -33.257   1.185  1.00 17.14           N  
ANISOU  764  N   GLY B  80     2050   2505   1956    422   -102    132       N  
ATOM    765  CA  GLY B  80      -5.953 -33.555   2.011  1.00 18.53           C  
ANISOU  765  CA  GLY B  80     2194   2745   2099    453   -110    152       C  
ATOM    766  C   GLY B  80      -5.315 -32.311   2.605  1.00 19.54           C  
ANISOU  766  C   GLY B  80     2306   2934   2182    430   -144    117       C  
ATOM    767  O   GLY B  80      -4.523 -32.399   3.567  1.00 21.45           O  
ANISOU  767  O   GLY B  80     2516   3247   2383    455   -156    128       O  
ATOM    768  N   GLY B  81      -5.644 -31.152   2.040  1.00 18.67           N  
ANISOU  768  N   GLY B  81     2217   2798   2078    381   -157     74       N  
ATOM    769  CA  GLY B  81      -5.098 -29.872   2.510  1.00 18.85           C  
ANISOU  769  CA  GLY B  81     2233   2861   2065    347   -184     32       C  
ATOM    770  C   GLY B  81      -5.540 -28.719   1.615  1.00 18.73           C  
ANISOU  770  C   GLY B  81     2253   2794   2069    298   -185     -6       C  
ATOM    771  O   GLY B  81      -6.267 -28.930   0.638  1.00 17.20           O  
ANISOU  771  O   GLY B  81     2082   2543   1910    296   -169      0       O  
ATOM    772  N   GLY B  82      -5.080 -27.507   1.934  1.00 18.74           N  
ANISOU  772  N   GLY B  82     2259   2815   2046    259   -203    -48       N  
ATOM    773  CA  GLY B  82      -5.380 -26.331   1.115  1.00 18.96           C  
ANISOU  773  CA  GLY B  82     2323   2789   2089    215   -199    -82       C  
ATOM    774  C   GLY B  82      -4.605 -26.357  -0.202  1.00 18.90           C  
ANISOU  774  C   GLY B  82     2305   2765   2111    188   -192    -82       C  
ATOM    775  O   GLY B  82      -3.720 -27.196  -0.401  1.00 19.18           O  
ANISOU  775  O   GLY B  82     2300   2837   2149    200   -194    -64       O  
ATOM    776  N   TRP B  83      -4.927 -25.420  -1.080  1.00 18.60           N  
ANISOU  776  N   TRP B  83     2302   2674   2089    157   -182   -102       N  
ATOM    777  CA  TRP B  83      -4.361 -25.365  -2.436  1.00 18.60           C  
ANISOU  777  CA  TRP B  83     2297   2653   2114    135   -170    -99       C  
ATOM    778  C   TRP B  83      -2.845 -25.208  -2.392  1.00 19.30           C  
ANISOU  778  C   TRP B  83     2344   2795   2194     99   -180   -113       C  
ATOM    779  O   TRP B  83      -2.341 -24.317  -1.700  1.00 20.70           O  
ANISOU  779  O   TRP B  83     2520   2994   2350     59   -192   -146       O  
ATOM    780  CB  TRP B  83      -4.965 -24.173  -3.175  1.00 18.23           C  
ANISOU  780  CB  TRP B  83     2301   2546   2077    110   -155   -116       C  
ATOM    781  CG  TRP B  83      -4.845 -24.273  -4.671  1.00 16.97           C  
ANISOU  781  CG  TRP B  83     2145   2359   1944    107   -137   -103       C  
ATOM    782  CD1 TRP B  83      -3.985 -23.579  -5.477  1.00 17.28           C  
ANISOU  782  CD1 TRP B  83     2183   2390   1990     67   -127   -112       C  
ATOM    783  CD2 TRP B  83      -5.624 -25.108  -5.536  1.00 16.61           C  
ANISOU  783  CD2 TRP B  83     2100   2293   1914    144   -127    -80       C  
ATOM    784  NE1 TRP B  83      -4.183 -23.929  -6.796  1.00 15.63           N  
ANISOU  784  NE1 TRP B  83     1976   2160   1799     83   -111    -93       N  
ATOM    785  CE2 TRP B  83      -5.174 -24.877  -6.857  1.00 17.13           C  
ANISOU  785  CE2 TRP B  83     2167   2345   1995    130   -113    -76       C  
ATOM    786  CE3 TRP B  83      -6.656 -26.044  -5.320  1.00 16.30           C  
ANISOU  786  CE3 TRP B  83     2061   2251   1881    184   -127    -63       C  
ATOM    787  CZ2 TRP B  83      -5.716 -25.550  -7.966  1.00 17.61           C  
ANISOU  787  CZ2 TRP B  83     2228   2393   2069    157   -102    -62       C  
ATOM    788  CZ3 TRP B  83      -7.189 -26.718  -6.424  1.00 16.87           C  
ANISOU  788  CZ3 TRP B  83     2132   2306   1972    204   -116    -51       C  
ATOM    789  CH2 TRP B  83      -6.721 -26.464  -7.725  1.00 17.33           C  
ANISOU  789  CH2 TRP B  83     2191   2355   2039    192   -105    -53       C  
ATOM    790  N   ARG B  84      -2.119 -26.059  -3.119  1.00 19.30           N  
ANISOU  790  N   ARG B  84     2307   2816   2207    112   -176    -91       N  
ATOM    791  CA  ARG B  84      -0.647 -26.013  -3.130  1.00 20.84           C  
ANISOU  791  CA  ARG B  84     2452   3073   2391     83   -184    -99       C  
ATOM    792  C   ARG B  84      -0.018 -25.597  -4.464  1.00 20.95           C  
ANISOU  792  C   ARG B  84     2463   3070   2426     49   -168   -101       C  
ATOM    793  O   ARG B  84       1.200 -25.473  -4.546  1.00 20.96           O  
ANISOU  793  O   ARG B  84     2420   3126   2418     19   -173   -109       O  
ATOM    794  CB  ARG B  84      -0.041 -27.371  -2.707  1.00 21.19           C  
ANISOU  794  CB  ARG B  84     2447   3180   2424    134   -191    -68       C  
ATOM    795  CG  ARG B  84      -0.538 -27.914  -1.368  1.00 24.33           C  
ANISOU  795  CG  ARG B  84     2842   3604   2797    176   -203    -56       C  
ATOM    796  CD  ARG B  84      -0.015 -27.147  -0.177  1.00 31.92           C  
ANISOU  796  CD  ARG B  84     3782   4628   3718    147   -227    -87       C  
ATOM    797  NE  ARG B  84      -0.920 -27.299   0.973  1.00 39.19           N  
ANISOU  797  NE  ARG B  84     4722   5548   4617    181   -234    -82       N  
ATOM    798  CZ  ARG B  84      -0.749 -28.155   1.982  1.00 42.10           C  
ANISOU  798  CZ  ARG B  84     5060   5978   4956    232   -241    -55       C  
ATOM    799  NH1 ARG B  84       0.315 -28.955   2.024  1.00 44.08           N  
ANISOU  799  NH1 ARG B  84     5258   6297   5193    261   -244    -31       N  
ATOM    800  NH2 ARG B  84      -1.648 -28.200   2.964  1.00 43.89           N  
ANISOU  800  NH2 ARG B  84     5309   6202   5164    260   -243    -49       N  
ATOM    801  N   LEU B  85      -0.827 -25.405  -5.505  1.00 20.62           N  
ANISOU  801  N   LEU B  85     2463   2963   2408     55   -149    -93       N  
ATOM    802  CA  LEU B  85      -0.271 -25.069  -6.827  1.00 21.18           C  
ANISOU  802  CA  LEU B  85     2532   3020   2495     31   -130    -89       C  
ATOM    803  C   LEU B  85      -0.067 -23.561  -6.931  1.00 22.77           C  
ANISOU  803  C   LEU B  85     2761   3192   2697    -31   -120   -115       C  
ATOM    804  O   LEU B  85      -1.015 -22.812  -7.153  1.00 23.20           O  
ANISOU  804  O   LEU B  85     2871   3185   2758    -32   -107   -120       O  
ATOM    805  CB  LEU B  85      -1.157 -25.610  -7.969  1.00 20.23           C  
ANISOU  805  CB  LEU B  85     2438   2854   2394     71   -113    -68       C  
ATOM    806  CG  LEU B  85      -1.554 -27.093  -7.907  1.00 18.89           C  
ANISOU  806  CG  LEU B  85     2252   2692   2229    128   -117    -48       C  
ATOM    807  CD1 LEU B  85      -2.567 -27.425  -8.999  1.00 18.72           C  
ANISOU  807  CD1 LEU B  85     2261   2626   2225    154   -102    -41       C  
ATOM    808  CD2 LEU B  85      -0.340 -28.045  -7.987  1.00 20.48           C  
ANISOU  808  CD2 LEU B  85     2402   2951   2428    146   -119    -33       C  
ATOM    809  N   SER B  86       1.175 -23.132  -6.728  1.00 24.47           N  
ANISOU  809  N   SER B  86     2937   3454   2904    -82   -124   -132       N  
ATOM    810  CA  SER B  86       1.515 -21.715  -6.603  1.00 25.93           C  
ANISOU  810  CA  SER B  86     3146   3613   3090   -155   -114   -164       C  
ATOM    811  C   SER B  86       1.900 -21.008  -7.904  1.00 26.53           C  
ANISOU  811  C   SER B  86     3238   3653   3188   -190    -80   -153       C  
ATOM    812  O   SER B  86       1.864 -19.773  -7.955  1.00 27.53           O  
ANISOU  812  O   SER B  86     3408   3729   3323   -243    -60   -173       O  
ATOM    813  CB  SER B  86       2.635 -21.522  -5.566  1.00 26.83           C  
ANISOU  813  CB  SER B  86     3206   3803   3182   -204   -136   -196       C  
ATOM    814  OG  SER B  86       3.768 -22.305  -5.898  1.00 27.63           O  
ANISOU  814  OG  SER B  86     3236   3984   3278   -198   -142   -179       O  
ATOM    815  N   ALA B  87       2.260 -21.763  -8.943  1.00 25.81           N  
ANISOU  815  N   ALA B  87     3118   3584   3105   -160    -71   -122       N  
ATOM    816  CA  ALA B  87       2.701 -21.160 -10.206  1.00 26.67           C  
ANISOU  816  CA  ALA B  87     3234   3669   3228   -189    -37   -106       C  
ATOM    817  C   ALA B  87       1.588 -20.379 -10.918  1.00 26.97           C  
ANISOU  817  C   ALA B  87     3348   3619   3278   -175     -9    -95       C  
ATOM    818  O   ALA B  87       0.423 -20.763 -10.872  1.00 26.11           O  
ANISOU  818  O   ALA B  87     3271   3481   3165   -120    -16    -87       O  
ATOM    819  CB  ALA B  87       3.316 -22.213 -11.136  1.00 25.96           C  
ANISOU  819  CB  ALA B  87     3095   3629   3138   -151    -34    -77       C  
ATOM    820  N   GLN B  88       1.974 -19.272 -11.550  1.00 28.16           N  
ANISOU  820  N   GLN B  88     3525   3732   3440   -225     24    -92       N  
ATOM    821  CA  GLN B  88       1.066 -18.414 -12.309  1.00 29.13           C  
ANISOU  821  CA  GLN B  88     3721   3776   3571   -209     59    -74       C  
ATOM    822  C   GLN B  88       1.519 -18.328 -13.749  1.00 28.81           C  
ANISOU  822  C   GLN B  88     3672   3736   3536   -205     92    -38       C  
ATOM    823  O   GLN B  88       2.715 -18.175 -14.022  1.00 29.30           O  
ANISOU  823  O   GLN B  88     3694   3834   3605   -256    104    -36       O  
ATOM    824  CB  GLN B  88       1.074 -16.992 -11.743  1.00 30.58           C  
ANISOU  824  CB  GLN B  88     3957   3895   3763   -273     81   -100       C  
ATOM    825  CG  GLN B  88      -0.225 -16.543 -11.096  1.00 34.91           C  
ANISOU  825  CG  GLN B  88     4573   4385   4305   -239     78   -112       C  
ATOM    826  CD  GLN B  88      -0.490 -17.226  -9.782  1.00 39.55           C  
ANISOU  826  CD  GLN B  88     5135   5014   4878   -224     33   -141       C  
ATOM    827  OE1 GLN B  88       0.441 -17.599  -9.072  1.00 42.55           O  
ANISOU  827  OE1 GLN B  88     5459   5455   5253   -262      8   -165       O  
ATOM    828  NE2 GLN B  88      -1.769 -17.391  -9.440  1.00 41.83           N  
ANISOU  828  NE2 GLN B  88     5460   5276   5155   -165     24   -137       N  
ATOM    829  N   TRP B  89       0.564 -18.403 -14.669  1.00 27.63           N  
ANISOU  829  N   TRP B  89     3560   3557   3381   -143    108     -9       N  
ATOM    830  CA  TRP B  89       0.859 -18.197 -16.072  1.00 27.84           C  
ANISOU  830  CA  TRP B  89     3587   3581   3406   -131    144     26       C  
ATOM    831  C   TRP B  89       1.226 -16.739 -16.328  1.00 28.98           C  
ANISOU  831  C   TRP B  89     3779   3666   3566   -189    192     37       C  
ATOM    832  O   TRP B  89       0.569 -15.823 -15.819  1.00 28.19           O  
ANISOU  832  O   TRP B  89     3742   3497   3470   -200    206     27       O  
ATOM    833  CB  TRP B  89      -0.325 -18.590 -16.953  1.00 27.14           C  
ANISOU  833  CB  TRP B  89     3526   3483   3301    -49    147     50       C  
ATOM    834  CG  TRP B  89      -0.105 -18.280 -18.400  1.00 27.17           C  
ANISOU  834  CG  TRP B  89     3536   3488   3297    -29    186     89       C  
ATOM    835  CD1 TRP B  89       0.801 -18.869 -19.239  1.00 28.46           C  
ANISOU  835  CD1 TRP B  89     3649   3707   3456    -28    193    104       C  
ATOM    836  CD2 TRP B  89      -0.793 -17.295 -19.177  1.00 28.18           C  
ANISOU  836  CD2 TRP B  89     3726   3565   3416     -2    228    122       C  
ATOM    837  NE1 TRP B  89       0.712 -18.314 -20.500  1.00 28.06           N  
ANISOU  837  NE1 TRP B  89     3623   3643   3392     -3    234    144       N  
ATOM    838  CE2 TRP B  89      -0.263 -17.349 -20.487  1.00 28.58           C  
ANISOU  838  CE2 TRP B  89     3758   3644   3455     14    257    157       C  
ATOM    839  CE3 TRP B  89      -1.819 -16.377 -18.898  1.00 27.34           C  
ANISOU  839  CE3 TRP B  89     3689   3393   3305     16    245    127       C  
ATOM    840  CZ2 TRP B  89      -0.717 -16.512 -21.514  1.00 29.14           C  
ANISOU  840  CZ2 TRP B  89     3877   3684   3511     49    303    200       C  
ATOM    841  CZ3 TRP B  89      -2.274 -15.545 -19.933  1.00 27.42           C  
ANISOU  841  CZ3 TRP B  89     3749   3369   3301     55    292    171       C  
ATOM    842  CH2 TRP B  89      -1.729 -15.622 -21.213  1.00 28.62           C  
ANISOU  842  CH2 TRP B  89     3880   3553   3441     71    321    208       C  
ATOM    843  N   GLN B  90       2.279 -16.553 -17.118  1.00 30.56           N  
ANISOU  843  N   GLN B  90     3948   3889   3771   -225    220     58       N  
ATOM    844  CA  GLN B  90       2.767 -15.228 -17.493  1.00 33.00           C  
ANISOU  844  CA  GLN B  90     4298   4141   4098   -287    274     73       C  
ATOM    845  C   GLN B  90       2.387 -14.994 -18.947  1.00 33.32           C  
ANISOU  845  C   GLN B  90     4368   4163   4127   -231    317    128       C  
ATOM    846  O   GLN B  90       2.735 -15.790 -19.821  1.00 33.21           O  
ANISOU  846  O   GLN B  90     4307   4212   4099   -194    313    150       O  
ATOM    847  CB  GLN B  90       4.296 -15.135 -17.319  1.00 33.76           C  
ANISOU  847  CB  GLN B  90     4331   4285   4209   -375    280     60       C  
ATOM    848  CG  GLN B  90       4.832 -15.566 -15.942  1.00 35.93           C  
ANISOU  848  CG  GLN B  90     4555   4611   4485   -422    231      6       C  
ATOM    849  CD  GLN B  90       4.262 -14.749 -14.788  1.00 39.25           C  
ANISOU  849  CD  GLN B  90     5033   4965   4914   -458    226    -34       C  
ATOM    850  OE1 GLN B  90       4.271 -13.515 -14.818  1.00 42.28           O  
ANISOU  850  OE1 GLN B  90     5475   5271   5316   -513    268    -37       O  
ATOM    851  NE2 GLN B  90       3.773 -15.438 -13.758  1.00 39.06           N  
ANISOU  851  NE2 GLN B  90     4994   4969   4876   -427    176    -64       N  
ATOM    852  N   LYS B  91       1.656 -13.911 -19.196  1.00 34.38           N  
ANISOU  852  N   LYS B  91     4583   4214   4263   -219    359    150       N  
ATOM    853  CA  LYS B  91       1.232 -13.548 -20.545  1.00 35.09           C  
ANISOU  853  CA  LYS B  91     4709   4286   4337   -160    405    207       C  
ATOM    854  C   LYS B  91       2.392 -13.608 -21.533  1.00 35.35           C  
ANISOU  854  C   LYS B  91     4697   4362   4372   -188    436    240       C  
ATOM    855  O   LYS B  91       3.486 -13.118 -21.252  1.00 36.37           O  
ANISOU  855  O   LYS B  91     4806   4485   4527   -278    457    231       O  
ATOM    856  CB  LYS B  91       0.614 -12.146 -20.541  1.00 36.32           C  
ANISOU  856  CB  LYS B  91     4961   4337   4501   -162    459    229       C  
ATOM    857  CG  LYS B  91      -0.470 -11.947 -21.583  1.00 37.87           C  
ANISOU  857  CG  LYS B  91     5204   4519   4665    -60    486    281       C  
ATOM    858  CD  LYS B  91      -1.593 -11.082 -21.026  1.00 41.79           C  
ANISOU  858  CD  LYS B  91     5785   4933   5159    -28    503    279       C  
ATOM    859  CE  LYS B  91      -1.459  -9.626 -21.437  1.00 44.49           C  
ANISOU  859  CE  LYS B  91     6211   5176   5515    -48    583    322       C  
ATOM    860  NZ  LYS B  91      -1.811  -9.441 -22.876  1.00 46.15           N  
ANISOU  860  NZ  LYS B  91     6439   5400   5693     33    628    393       N  
ATOM    861  N   GLY B  92       2.152 -14.230 -22.683  1.00 34.54           N  
ANISOU  861  N   GLY B  92     4573   4311   4240   -113    439    274       N  
ATOM    862  CA  GLY B  92       3.166 -14.316 -23.727  1.00 34.36           C  
ANISOU  862  CA  GLY B  92     4508   4335   4212   -125    471    310       C  
ATOM    863  C   GLY B  92       4.037 -15.552 -23.660  1.00 33.58           C  
ANISOU  863  C   GLY B  92     4317   4331   4108   -133    429    286       C  
ATOM    864  O   GLY B  92       4.878 -15.765 -24.532  1.00 34.05           O  
ANISOU  864  O   GLY B  92     4335   4443   4159   -135    452    314       O  
ATOM    865  N   GLU B  93       3.856 -16.371 -22.627  1.00 32.45           N  
ANISOU  865  N   GLU B  93     4146   4213   3969   -134    371    237       N  
ATOM    866  CA  GLU B  93       4.632 -17.608 -22.516  1.00 31.67           C  
ANISOU  866  CA  GLU B  93     3965   4201   3864   -130    333    216       C  
ATOM    867  C   GLU B  93       3.811 -18.828 -22.924  1.00 29.49           C  
ANISOU  867  C   GLU B  93     3679   3964   3562    -38    297    208       C  
ATOM    868  O   GLU B  93       2.625 -18.932 -22.597  1.00 28.23           O  
ANISOU  868  O   GLU B  93     3559   3770   3397      2    276    194       O  
ATOM    869  CB  GLU B  93       5.201 -17.773 -21.105  1.00 32.48           C  
ANISOU  869  CB  GLU B  93     4034   4317   3987   -195    297    170       C  
ATOM    870  CG  GLU B  93       6.375 -16.835 -20.813  1.00 36.89           C  
ANISOU  870  CG  GLU B  93     4575   4872   4570   -298    328    170       C  
ATOM    871  CD  GLU B  93       7.084 -17.149 -19.503  1.00 42.16           C  
ANISOU  871  CD  GLU B  93     5189   5582   5247   -357    288    122       C  
ATOM    872  OE1 GLU B  93       8.119 -16.503 -19.225  1.00 45.05           O  
ANISOU  872  OE1 GLU B  93     5524   5963   5628   -446    307    113       O  
ATOM    873  OE2 GLU B  93       6.613 -18.039 -18.754  1.00 44.26           O  
ANISOU  873  OE2 GLU B  93     5440   5871   5503   -315    238     95       O  
ATOM    874  N   GLU B  94       4.439 -19.742 -23.660  1.00 27.62           N  
ANISOU  874  N   GLU B  94     3387   3798   3308     -5    293    215       N  
ATOM    875  CA  GLU B  94       3.748 -20.955 -24.081  1.00 25.92           C  
ANISOU  875  CA  GLU B  94     3161   3617   3070     74    262    200       C  
ATOM    876  C   GLU B  94       3.608 -21.916 -22.908  1.00 23.49           C  
ANISOU  876  C   GLU B  94     2830   3320   2775     73    212    157       C  
ATOM    877  O   GLU B  94       4.388 -21.873 -21.951  1.00 22.85           O  
ANISOU  877  O   GLU B  94     2719   3250   2712     19    199    143       O  
ATOM    878  CB  GLU B  94       4.424 -21.616 -25.288  1.00 26.71           C  
ANISOU  878  CB  GLU B  94     3218   3785   3145    114    277    219       C  
ATOM    879  CG  GLU B  94       4.269 -20.781 -26.565  1.00 30.35           C  
ANISOU  879  CG  GLU B  94     3708   4239   3583    138    326    265       C  
ATOM    880  CD  GLU B  94       4.846 -21.424 -27.810  1.00 35.29           C  
ANISOU  880  CD  GLU B  94     4294   4936   4177    186    342    283       C  
ATOM    881  OE1 GLU B  94       5.254 -22.598 -27.764  1.00 37.58           O  
ANISOU  881  OE1 GLU B  94     4539   5277   4461    211    314    256       O  
ATOM    882  OE2 GLU B  94       4.874 -20.748 -28.861  1.00 39.65           O  
ANISOU  882  OE2 GLU B  94     4863   5493   4707    206    386    326       O  
ATOM    883  N   VAL B  95       2.579 -22.751 -22.976  1.00 21.26           N  
ANISOU  883  N   VAL B  95     2561   3035   2482    132    185    138       N  
ATOM    884  CA  VAL B  95       2.321 -23.759 -21.945  1.00 19.06           C  
ANISOU  884  CA  VAL B  95     2265   2761   2213    140    143    103       C  
ATOM    885  C   VAL B  95       2.160 -25.126 -22.608  1.00 18.62           C  
ANISOU  885  C   VAL B  95     2187   2744   2143    202    129     88       C  
ATOM    886  O   VAL B  95       2.013 -25.224 -23.827  1.00 18.23           O  
ANISOU  886  O   VAL B  95     2140   2715   2070    241    146     99       O  
ATOM    887  CB  VAL B  95       1.030 -23.433 -21.123  1.00 18.31           C  
ANISOU  887  CB  VAL B  95     2218   2611   2126    142    124     86       C  
ATOM    888  CG1 VAL B  95       1.161 -22.093 -20.383  1.00 17.72           C  
ANISOU  888  CG1 VAL B  95     2174   2490   2067     82    139     93       C  
ATOM    889  CG2 VAL B  95      -0.235 -23.466 -22.027  1.00 17.59           C  
ANISOU  889  CG2 VAL B  95     2161   2508   2013    199    129     90       C  
ATOM    890  N   GLN B  96       2.194 -26.189 -21.808  1.00 18.09           N  
ANISOU  890  N   GLN B  96     2099   2686   2088    213    100     63       N  
ATOM    891  CA  GLN B  96       1.741 -27.480 -22.284  1.00 17.54           C  
ANISOU  891  CA  GLN B  96     2024   2630   2010    269     87     42       C  
ATOM    892  C   GLN B  96       0.555 -27.937 -21.460  1.00 17.30           C  
ANISOU  892  C   GLN B  96     2020   2560   1992    277     61     16       C  
ATOM    893  O   GLN B  96       0.469 -27.634 -20.264  1.00 17.88           O  
ANISOU  893  O   GLN B  96     2099   2610   2082    246     47     15       O  
ATOM    894  CB  GLN B  96       2.876 -28.506 -22.246  1.00 17.81           C  
ANISOU  894  CB  GLN B  96     2013   2709   2045    287     86     40       C  
ATOM    895  CG  GLN B  96       3.885 -28.283 -23.379  1.00 18.41           C  
ANISOU  895  CG  GLN B  96     2060   2834   2100    295    114     62       C  
ATOM    896  CD  GLN B  96       5.041 -29.262 -23.351  1.00 19.27           C  
ANISOU  896  CD  GLN B  96     2120   2994   2205    320    116     63       C  
ATOM    897  OE1 GLN B  96       5.075 -30.175 -22.530  1.00 20.61           O  
ANISOU  897  OE1 GLN B  96     2282   3160   2387    337     97     48       O  
ATOM    898  NE2 GLN B  96       5.978 -29.094 -24.276  1.00 20.54           N  
ANISOU  898  NE2 GLN B  96     2250   3206   2347    329    142     84       N  
ATOM    899  N   VAL B  97      -0.367 -28.648 -22.098  1.00 17.33           N  
ANISOU  899  N   VAL B  97     2038   2560   1986    317     55     -4       N  
ATOM    900  CA  VAL B  97      -1.402 -29.361 -21.355  1.00 16.78           C  
ANISOU  900  CA  VAL B  97     1984   2460   1931    325     32    -31       C  
ATOM    901  C   VAL B  97      -1.037 -30.841 -21.374  1.00 16.56           C  
ANISOU  901  C   VAL B  97     1937   2442   1913    353     28    -52       C  
ATOM    902  O   VAL B  97      -0.772 -31.409 -22.444  1.00 16.92           O  
ANISOU  902  O   VAL B  97     1973   2511   1943    384     39    -63       O  
ATOM    903  CB  VAL B  97      -2.803 -29.169 -21.985  1.00 16.64           C  
ANISOU  903  CB  VAL B  97     1992   2433   1897    344     29    -46       C  
ATOM    904  CG1 VAL B  97      -3.881 -29.905 -21.144  1.00 16.18           C  
ANISOU  904  CG1 VAL B  97     1945   2347   1857    344      8    -73       C  
ATOM    905  CG2 VAL B  97      -3.137 -27.682 -22.097  1.00 17.94           C  
ANISOU  905  CG2 VAL B  97     2181   2587   2048    330     41    -19       C  
ATOM    906  N   ILE B  98      -0.991 -31.458 -20.198  1.00 16.09           N  
ANISOU  906  N   ILE B  98     1874   2362   1876    346     15    -55       N  
ATOM    907  CA  ILE B  98      -0.838 -32.910 -20.105  1.00 16.76           C  
ANISOU  907  CA  ILE B  98     1952   2440   1973    377     16    -73       C  
ATOM    908  C   ILE B  98      -2.243 -33.514 -20.170  1.00 16.75           C  
ANISOU  908  C   ILE B  98     1978   2403   1982    383      8   -105       C  
ATOM    909  O   ILE B  98      -2.911 -33.718 -19.147  1.00 15.91           O  
ANISOU  909  O   ILE B  98     1884   2266   1895    369     -1   -107       O  
ATOM    910  CB  ILE B  98      -0.070 -33.349 -18.824  1.00 16.80           C  
ANISOU  910  CB  ILE B  98     1941   2446   1995    376     11    -55       C  
ATOM    911  CG1 ILE B  98       1.254 -32.587 -18.709  1.00 17.13           C  
ANISOU  911  CG1 ILE B  98     1948   2535   2025    359     16    -27       C  
ATOM    912  CG2 ILE B  98       0.187 -34.884 -18.823  1.00 17.25           C  
ANISOU  912  CG2 ILE B  98     1998   2492   2065    419     22    -66       C  
ATOM    913  CD1 ILE B  98       2.031 -32.842 -17.387  1.00 17.39           C  
ANISOU  913  CD1 ILE B  98     1954   2587   2063    356      7     -9       C  
ATOM    914  N   ALA B  99      -2.695 -33.761 -21.395  1.00 16.83           N  
ANISOU  914  N   ALA B  99     1994   2424   1975    401     14   -132       N  
ATOM    915  CA  ALA B  99      -4.058 -34.209 -21.630  1.00 17.78           C  
ANISOU  915  CA  ALA B  99     2131   2526   2098    399      6   -169       C  
ATOM    916  C   ALA B  99      -4.175 -35.682 -21.274  1.00 18.12           C  
ANISOU  916  C   ALA B  99     2182   2532   2169    409     11   -196       C  
ATOM    917  O   ALA B  99      -3.451 -36.506 -21.813  1.00 19.39           O  
ANISOU  917  O   ALA B  99     2340   2696   2330    436     25   -208       O  
ATOM    918  CB  ALA B  99      -4.445 -33.967 -23.084  1.00 18.03           C  
ANISOU  918  CB  ALA B  99     2160   2593   2094    417      9   -191       C  
ATOM    919  N   VAL B 100      -5.064 -35.998 -20.336  1.00 17.57           N  
ANISOU  919  N   VAL B 100     2125   2427   2124    389      3   -202       N  
ATOM    920  CA  VAL B 100      -5.296 -37.371 -19.929  1.00 17.49           C  
ANISOU  920  CA  VAL B 100     2128   2371   2144    393     14   -224       C  
ATOM    921  C   VAL B 100      -6.725 -37.767 -20.331  1.00 17.83           C  
ANISOU  921  C   VAL B 100     2181   2402   2192    371      9   -271       C  
ATOM    922  O   VAL B 100      -7.662 -37.701 -19.545  1.00 17.29           O  
ANISOU  922  O   VAL B 100     2116   2314   2137    346      2   -269       O  
ATOM    923  CB  VAL B 100      -5.006 -37.593 -18.412  1.00 17.79           C  
ANISOU  923  CB  VAL B 100     2170   2380   2209    389     16   -187       C  
ATOM    924  CG1 VAL B 100      -5.139 -39.079 -18.044  1.00 17.76           C  
ANISOU  924  CG1 VAL B 100     2186   2321   2238    401     38   -202       C  
ATOM    925  CG2 VAL B 100      -3.583 -37.097 -18.059  1.00 18.30           C  
ANISOU  925  CG2 VAL B 100     2215   2476   2261    407     17   -145       C  
ATOM    926  N   GLU B 101      -6.875 -38.163 -21.587  1.00 18.60           N  
ANISOU  926  N   GLU B 101     2277   2518   2272    381     13   -315       N  
ATOM    927  CA  GLU B 101      -8.172 -38.564 -22.109  1.00 19.97           C  
ANISOU  927  CA  GLU B 101     2450   2693   2442    357      6   -369       C  
ATOM    928  C   GLU B 101      -8.537 -39.976 -21.668  1.00 20.20           C  
ANISOU  928  C   GLU B 101     2500   2660   2515    339     24   -401       C  
ATOM    929  O   GLU B 101      -7.663 -40.852 -21.610  1.00 20.92           O  
ANISOU  929  O   GLU B 101     2609   2712   2626    362     46   -400       O  
ATOM    930  CB  GLU B 101      -8.174 -38.461 -23.642  1.00 20.59           C  
ANISOU  930  CB  GLU B 101     2518   2824   2480    376      3   -408       C  
ATOM    931  CG  GLU B 101      -7.943 -37.034 -24.146  1.00 22.48           C  
ANISOU  931  CG  GLU B 101     2741   3123   2675    395     -7   -372       C  
ATOM    932  CD  GLU B 101      -8.022 -36.905 -25.656  1.00 27.68           C  
ANISOU  932  CD  GLU B 101     3387   3841   3287    419     -9   -406       C  
ATOM    933  OE1 GLU B 101      -8.648 -35.926 -26.148  1.00 27.45           O  
ANISOU  933  OE1 GLU B 101     3346   3864   3220    426    -21   -397       O  
ATOM    934  OE2 GLU B 101      -7.450 -37.781 -26.351  1.00 29.36           O  
ANISOU  934  OE2 GLU B 101     3604   4052   3498    437      2   -440       O  
ATOM    935  N   PRO B 102      -9.834 -40.218 -21.391  1.00 20.77           N  
ANISOU  935  N   PRO B 102     2570   2721   2601    300     18   -430       N  
ATOM    936  CA  PRO B 102     -10.285 -41.576 -21.059  1.00 22.00           C  
ANISOU  936  CA  PRO B 102     2747   2811   2800    273     40   -466       C  
ATOM    937  C   PRO B 102      -9.837 -42.595 -22.105  1.00 23.81           C  
ANISOU  937  C   PRO B 102     2993   3021   3032    286     59   -522       C  
ATOM    938  O   PRO B 102      -9.900 -42.316 -23.301  1.00 24.15           O  
ANISOU  938  O   PRO B 102     3020   3118   3035    295     46   -561       O  
ATOM    939  CB  PRO B 102     -11.810 -41.444 -21.051  1.00 22.08           C  
ANISOU  939  CB  PRO B 102     2737   2843   2807    226     25   -501       C  
ATOM    940  CG  PRO B 102     -12.029 -39.994 -20.607  1.00 21.14           C  
ANISOU  940  CG  PRO B 102     2596   2776   2657    237      0   -450       C  
ATOM    941  CD  PRO B 102     -10.943 -39.243 -21.334  1.00 20.31           C  
ANISOU  941  CD  PRO B 102     2489   2709   2517    280     -5   -428       C  
ATOM    942  N   GLY B 103      -9.353 -43.743 -21.642  1.00 25.17           N  
ANISOU  942  N   GLY B 103     3199   3116   3245    293     92   -522       N  
ATOM    943  CA  GLY B 103      -8.918 -44.825 -22.541  1.00 27.43           C  
ANISOU  943  CA  GLY B 103     3512   3369   3539    308    117   -577       C  
ATOM    944  C   GLY B 103      -7.649 -44.581 -23.340  1.00 28.12           C  
ANISOU  944  C   GLY B 103     3596   3494   3592    367    118   -565       C  
ATOM    945  O   GLY B 103      -7.245 -45.438 -24.132  1.00 29.40           O  
ANISOU  945  O   GLY B 103     3781   3634   3755    387    139   -612       O  
ATOM    946  N   LYS B 104      -6.996 -43.437 -23.129  1.00 27.38           N  
ANISOU  946  N   LYS B 104     3476   3455   3469    394     98   -505       N  
ATOM    947  CA  LYS B 104      -5.819 -43.072 -23.924  1.00 27.62           C  
ANISOU  947  CA  LYS B 104     3495   3533   3464    444     99   -490       C  
ATOM    948  C   LYS B 104      -4.600 -42.812 -23.055  1.00 27.12           C  
ANISOU  948  C   LYS B 104     3428   3468   3408    480    108   -416       C  
ATOM    949  O   LYS B 104      -4.737 -42.450 -21.883  1.00 25.88           O  
ANISOU  949  O   LYS B 104     3267   3296   3270    464    102   -371       O  
ATOM    950  CB  LYS B 104      -6.103 -41.847 -24.807  1.00 27.96           C  
ANISOU  950  CB  LYS B 104     3505   3661   3455    441     71   -493       C  
ATOM    951  CG  LYS B 104      -7.345 -42.005 -25.685  1.00 30.63           C  
ANISOU  951  CG  LYS B 104     3837   4025   3775    410     57   -565       C  
ATOM    952  CD  LYS B 104      -7.299 -41.176 -26.955  1.00 36.10           C  
ANISOU  952  CD  LYS B 104     4503   4804   4408    433     40   -578       C  
ATOM    953  CE  LYS B 104      -6.831 -42.015 -28.147  1.00 39.00           C  
ANISOU  953  CE  LYS B 104     4880   5182   4754    463     55   -636       C  
ATOM    954  NZ  LYS B 104      -7.488 -41.584 -29.423  1.00 42.21           N  
ANISOU  954  NZ  LYS B 104     5262   5672   5103    466     36   -683       N  
ATOM    955  N   ASN B 105      -3.412 -42.990 -23.636  1.00 26.84           N  
ANISOU  955  N   ASN B 105     3389   3455   3353    529    123   -406       N  
ATOM    956  CA  ASN B 105      -2.181 -42.606 -22.968  1.00 27.21           C  
ANISOU  956  CA  ASN B 105     3417   3523   3395    564    127   -339       C  
ATOM    957  C   ASN B 105      -2.101 -41.080 -22.833  1.00 26.22           C  
ANISOU  957  C   ASN B 105     3255   3461   3243    542     99   -299       C  
ATOM    958  O   ASN B 105      -2.485 -40.350 -23.749  1.00 25.78           O  
ANISOU  958  O   ASN B 105     3187   3450   3157    529     85   -318       O  
ATOM    959  CB  ASN B 105      -0.952 -43.146 -23.714  1.00 28.30           C  
ANISOU  959  CB  ASN B 105     3556   3682   3516    623    151   -340       C  
ATOM    960  CG  ASN B 105      -0.790 -44.663 -23.568  1.00 30.50           C  
ANISOU  960  CG  ASN B 105     3877   3886   3825    657    188   -364       C  
ATOM    961  OD1 ASN B 105      -0.987 -45.220 -22.489  1.00 34.23           O  
ANISOU  961  OD1 ASN B 105     4371   4299   4334    653    201   -342       O  
ATOM    962  ND2 ASN B 105      -0.412 -45.326 -24.653  1.00 33.10           N  
ANISOU  962  ND2 ASN B 105     4222   4215   4139    693    207   -408       N  
ATOM    963  N   PRO B 106      -1.611 -40.594 -21.681  1.00 25.59           N  
ANISOU  963  N   PRO B 106     3161   3387   3172    538     93   -244       N  
ATOM    964  CA  PRO B 106      -1.395 -39.152 -21.557  1.00 24.76           C  
ANISOU  964  CA  PRO B 106     3027   3335   3044    516     72   -209       C  
ATOM    965  C   PRO B 106      -0.508 -38.619 -22.677  1.00 24.56           C  
ANISOU  965  C   PRO B 106     2978   3370   2983    538     77   -203       C  
ATOM    966  O   PRO B 106       0.430 -39.307 -23.127  1.00 24.42           O  
ANISOU  966  O   PRO B 106     2955   3364   2958    581     96   -204       O  
ATOM    967  CB  PRO B 106      -0.695 -39.008 -20.204  1.00 24.61           C  
ANISOU  967  CB  PRO B 106     2995   3317   3039    518     70   -158       C  
ATOM    968  CG  PRO B 106      -1.126 -40.221 -19.439  1.00 26.19           C  
ANISOU  968  CG  PRO B 106     3224   3454   3273    530     85   -166       C  
ATOM    969  CD  PRO B 106      -1.200 -41.321 -20.468  1.00 25.84           C  
ANISOU  969  CD  PRO B 106     3203   3379   3233    557    108   -212       C  
ATOM    970  N   LYS B 107      -0.818 -37.412 -23.137  1.00 23.44           N  
ANISOU  970  N   LYS B 107     2823   3263   2817    513     63   -195       N  
ATOM    971  CA  LYS B 107      -0.024 -36.767 -24.166  1.00 24.38           C  
ANISOU  971  CA  LYS B 107     2921   3440   2902    530     71   -182       C  
ATOM    972  C   LYS B 107       0.092 -35.269 -23.892  1.00 23.12           C  
ANISOU  972  C   LYS B 107     2745   3306   2730    496     62   -141       C  
ATOM    973  O   LYS B 107      -0.884 -34.633 -23.490  1.00 21.99           O  
ANISOU  973  O   LYS B 107     2617   3143   2593    465     47   -142       O  
ATOM    974  CB  LYS B 107      -0.654 -37.007 -25.545  1.00 25.04           C  
ANISOU  974  CB  LYS B 107     3014   3539   2958    547     74   -227       C  
ATOM    975  CG  LYS B 107       0.227 -36.570 -26.700  1.00 29.27           C  
ANISOU  975  CG  LYS B 107     3528   4137   3455    576     89   -214       C  
ATOM    976  CD  LYS B 107      -0.435 -36.861 -28.030  1.00 33.09           C  
ANISOU  976  CD  LYS B 107     4021   4644   3906    598     90   -262       C  
ATOM    977  CE  LYS B 107       0.459 -36.431 -29.178  1.00 36.49           C  
ANISOU  977  CE  LYS B 107     4429   5140   4294    633    108   -244       C  
ATOM    978  NZ  LYS B 107      -0.244 -36.652 -30.471  1.00 39.70           N  
ANISOU  978  NZ  LYS B 107     4843   5581   4661    657    107   -293       N  
ATOM    979  N   ASN B 108       1.287 -34.716 -24.103  1.00 22.41           N  
ANISOU  979  N   ASN B 108     2627   3261   2626    500     74   -106       N  
ATOM    980  CA  ASN B 108       1.512 -33.282 -23.938  1.00 21.36           C  
ANISOU  980  CA  ASN B 108     2483   3148   2485    462     73    -70       C  
ATOM    981  C   ASN B 108       1.270 -32.515 -25.217  1.00 21.47           C  
ANISOU  981  C   ASN B 108     2500   3190   2466    469     84    -67       C  
ATOM    982  O   ASN B 108       1.745 -32.922 -26.292  1.00 21.31           O  
ANISOU  982  O   ASN B 108     2467   3205   2421    505    100    -75       O  
ATOM    983  CB  ASN B 108       2.941 -32.988 -23.479  1.00 21.57           C  
ANISOU  983  CB  ASN B 108     2471   3211   2511    453     82    -34       C  
ATOM    984  CG  ASN B 108       3.174 -33.340 -22.025  1.00 22.59           C  
ANISOU  984  CG  ASN B 108     2593   3323   2666    439     68    -26       C  
ATOM    985  OD1 ASN B 108       2.728 -34.390 -21.552  1.00 22.71           O  
ANISOU  985  OD1 ASN B 108     2624   3305   2697    463     62    -45       O  
ATOM    986  ND2 ASN B 108       3.890 -32.467 -21.306  1.00 22.03           N  
ANISOU  986  ND2 ASN B 108     2496   3278   2597    400     64      1       N  
ATOM    987  N   PHE B 109       0.572 -31.389 -25.087  1.00 20.43           N  
ANISOU  987  N   PHE B 109     2385   3044   2331    439     80    -52       N  
ATOM    988  CA  PHE B 109       0.265 -30.516 -26.223  1.00 21.11           C  
ANISOU  988  CA  PHE B 109     2479   3155   2384    450     95    -39       C  
ATOM    989  C   PHE B 109       0.742 -29.124 -25.875  1.00 21.63           C  
ANISOU  989  C   PHE B 109     2546   3217   2454    410    109      5       C  
ATOM    990  O   PHE B 109       0.410 -28.600 -24.802  1.00 21.65           O  
ANISOU  990  O   PHE B 109     2563   3181   2479    373     97     11       O  
ATOM    991  CB  PHE B 109      -1.243 -30.484 -26.496  1.00 20.96           C  
ANISOU  991  CB  PHE B 109     2488   3122   2353    461     80    -67       C  
ATOM    992  CG  PHE B 109      -1.792 -31.766 -27.036  1.00 21.46           C  
ANISOU  992  CG  PHE B 109     2550   3192   2408    493     69   -119       C  
ATOM    993  CD1 PHE B 109      -2.020 -31.916 -28.407  1.00 23.75           C  
ANISOU  993  CD1 PHE B 109     2837   3529   2657    531     77   -139       C  
ATOM    994  CD2 PHE B 109      -2.066 -32.835 -26.184  1.00 22.27           C  
ANISOU  994  CD2 PHE B 109     2659   3257   2544    484     54   -150       C  
ATOM    995  CE1 PHE B 109      -2.529 -33.120 -28.924  1.00 24.41           C  
ANISOU  995  CE1 PHE B 109     2921   3619   2733    554     68   -198       C  
ATOM    996  CE2 PHE B 109      -2.574 -34.034 -26.681  1.00 23.01           C  
ANISOU  996  CE2 PHE B 109     2757   3347   2636    505     50   -203       C  
ATOM    997  CZ  PHE B 109      -2.808 -34.178 -28.057  1.00 24.94           C  
ANISOU  997  CZ  PHE B 109     2997   3638   2839    537     55   -232       C  
ATOM    998  N   GLN B 110       1.529 -28.525 -26.762  1.00 21.18           N  
ANISOU  998  N   GLN B 110     2474   3196   2375    415    137     36       N  
ATOM    999  CA  GLN B 110       2.048 -27.191 -26.522  1.00 22.14           C  
ANISOU  999  CA  GLN B 110     2600   3309   2504    370    158     79       C  
ATOM   1000  C   GLN B 110       1.207 -26.141 -27.256  1.00 23.14           C  
ANISOU 1000  C   GLN B 110     2762   3423   2607    382    176    101       C  
ATOM   1001  O   GLN B 110       0.778 -26.363 -28.392  1.00 23.44           O  
ANISOU 1001  O   GLN B 110     2802   3493   2608    431    184     97       O  
ATOM   1002  CB  GLN B 110       3.525 -27.107 -26.916  1.00 22.61           C  
ANISOU 1002  CB  GLN B 110     2617   3414   2558    360    183    106       C  
ATOM   1003  CG  GLN B 110       4.209 -25.815 -26.485  1.00 23.24           C  
ANISOU 1003  CG  GLN B 110     2695   3481   2654    296    205    143       C  
ATOM   1004  CD  GLN B 110       5.708 -25.878 -26.643  1.00 25.11           C  
ANISOU 1004  CD  GLN B 110     2878   3772   2889    277    225    164       C  
ATOM   1005  OE1 GLN B 110       6.318 -26.916 -26.412  1.00 24.07           O  
ANISOU 1005  OE1 GLN B 110     2709   3678   2759    298    210    148       O  
ATOM   1006  NE2 GLN B 110       6.315 -24.759 -27.043  1.00 26.71           N  
ANISOU 1006  NE2 GLN B 110     3076   3980   3090    237    262    203       N  
ATOM   1007  N   THR B 111       0.958 -25.015 -26.590  1.00 23.39           N  
ANISOU 1007  N   THR B 111     2823   3409   2655    341    184    123       N  
ATOM   1008  CA  THR B 111       0.118 -23.959 -27.151  1.00 24.12           C  
ANISOU 1008  CA  THR B 111     2956   3481   2726    358    206    149       C  
ATOM   1009  C   THR B 111       0.513 -22.584 -26.604  1.00 24.44           C  
ANISOU 1009  C   THR B 111     3023   3474   2789    303    234    185       C  
ATOM   1010  O   THR B 111       1.103 -22.483 -25.534  1.00 24.67           O  
ANISOU 1010  O   THR B 111     3042   3479   2850    247    224    175       O  
ATOM   1011  CB  THR B 111      -1.397 -24.256 -26.900  1.00 23.77           C  
ANISOU 1011  CB  THR B 111     2937   3420   2673    389    177    119       C  
ATOM   1012  OG1 THR B 111      -2.199 -23.321 -27.628  1.00 26.70           O  
ANISOU 1012  OG1 THR B 111     3342   3789   3012    423    200    148       O  
ATOM   1013  CG2 THR B 111      -1.757 -24.174 -25.412  1.00 23.49           C  
ANISOU 1013  CG2 THR B 111     2917   3333   2674    348    152    101       C  
ATOM   1014  N   MET B 112       0.199 -21.528 -27.351  1.00 25.14           N  
ANISOU 1014  N   MET B 112     3146   3547   2856    319    272    226       N  
ATOM   1015  CA  MET B 112       0.287 -20.173 -26.823  1.00 25.64           C  
ANISOU 1015  CA  MET B 112     3252   3546   2941    271    303    256       C  
ATOM   1016  C   MET B 112      -1.106 -19.738 -26.377  1.00 25.41           C  
ANISOU 1016  C   MET B 112     3273   3473   2906    298    292    249       C  
ATOM   1017  O   MET B 112      -2.014 -19.615 -27.208  1.00 25.23           O  
ANISOU 1017  O   MET B 112     3271   3469   2847    363    300    264       O  
ATOM   1018  CB  MET B 112       0.830 -19.186 -27.868  1.00 27.11           C  
ANISOU 1018  CB  MET B 112     3455   3732   3112    273    362    313       C  
ATOM   1019  CG  MET B 112       0.847 -17.735 -27.378  1.00 28.63           C  
ANISOU 1019  CG  MET B 112     3704   3844   3330    224    403    344       C  
ATOM   1020  SD  MET B 112       2.061 -17.470 -26.077  1.00 33.11           S  
ANISOU 1020  SD  MET B 112     4248   4380   3951    111    397    319       S  
ATOM   1021  CE  MET B 112       3.535 -17.154 -27.052  1.00 34.04           C  
ANISOU 1021  CE  MET B 112     4327   4537   4067     76    449    364       C  
ATOM   1022  N   PRO B 113      -1.293 -19.525 -25.064  1.00 24.73           N  
ANISOU 1022  N   PRO B 113     3204   3338   2852    253    272    225       N  
ATOM   1023  CA  PRO B 113      -2.618 -19.092 -24.617  1.00 24.80           C  
ANISOU 1023  CA  PRO B 113     3259   3308   2853    283    263    220       C  
ATOM   1024  C   PRO B 113      -2.962 -17.667 -25.050  1.00 26.26           C  
ANISOU 1024  C   PRO B 113     3505   3443   3026    297    315    268       C  
ATOM   1025  O   PRO B 113      -2.068 -16.820 -25.193  1.00 26.01           O  
ANISOU 1025  O   PRO B 113     3491   3378   3013    252    357    297       O  
ATOM   1026  CB  PRO B 113      -2.530 -19.160 -23.085  1.00 24.08           C  
ANISOU 1026  CB  PRO B 113     3170   3180   2799    227    234    185       C  
ATOM   1027  CG  PRO B 113      -1.300 -19.968 -22.782  1.00 23.91           C  
ANISOU 1027  CG  PRO B 113     3091   3194   2797    184    216    165       C  
ATOM   1028  CD  PRO B 113      -0.365 -19.719 -23.938  1.00 24.41           C  
ANISOU 1028  CD  PRO B 113     3137   3286   2849    182    254    200       C  
ATOM   1029  N   GLY B 114      -4.252 -17.435 -25.284  1.00 26.98           N  
ANISOU 1029  N   GLY B 114     3629   3533   3088    361    314    276       N  
ATOM   1030  CA  GLY B 114      -4.788 -16.081 -25.396  1.00 29.10           C  
ANISOU 1030  CA  GLY B 114     3965   3742   3346    384    360    319       C  
ATOM   1031  C   GLY B 114      -5.284 -15.652 -24.025  1.00 30.08           C  
ANISOU 1031  C   GLY B 114     4127   3804   3498    353    346    293       C  
ATOM   1032  O   GLY B 114      -4.836 -16.178 -23.005  1.00 28.96           O  
ANISOU 1032  O   GLY B 114     3958   3656   3388    296    311    251       O  
ATOM   1033  N   THR B 115      -6.217 -14.708 -23.981  1.00 32.05           N  
ANISOU 1033  N   THR B 115     4437   4009   3730    397    373    319       N  
ATOM   1034  CA  THR B 115      -6.760 -14.274 -22.698  1.00 34.51           C  
ANISOU 1034  CA  THR B 115     4787   4263   4062    377    362    294       C  
ATOM   1035  C   THR B 115      -8.268 -14.100 -22.748  1.00 36.27           C  
ANISOU 1035  C   THR B 115     5035   4498   4246    462    357    304       C  
ATOM   1036  O   THR B 115      -8.823 -13.709 -23.780  1.00 36.72           O  
ANISOU 1036  O   THR B 115     5110   4579   4262    536    386    348       O  
ATOM   1037  CB  THR B 115      -6.128 -12.946 -22.198  1.00 35.28           C  
ANISOU 1037  CB  THR B 115     4951   4260   4192    319    412    310       C  
ATOM   1038  OG1 THR B 115      -6.235 -11.955 -23.218  1.00 36.47           O  
ANISOU 1038  OG1 THR B 115     5154   4378   4322    364    476    372       O  
ATOM   1039  CG2 THR B 115      -4.658 -13.130 -21.833  1.00 35.53           C  
ANISOU 1039  CG2 THR B 115     4949   4286   4266    220    409    287       C  
ATOM   1040  N   PHE B 116      -8.916 -14.417 -21.628  1.00 37.64           N  
ANISOU 1040  N   PHE B 116     5205   4667   4429    455    320    265       N  
ATOM   1041  CA  PHE B 116     -10.298 -14.034 -21.376  1.00 39.99           C  
ANISOU 1041  CA  PHE B 116     5534   4963   4695    525    320    274       C  
ATOM   1042  C   PHE B 116     -10.285 -12.705 -20.641  1.00 42.60           C  
ANISOU 1042  C   PHE B 116     5947   5193   5043    509    362    287       C  
ATOM   1043  O   PHE B 116      -9.505 -12.520 -19.700  1.00 42.71           O  
ANISOU 1043  O   PHE B 116     5973   5154   5098    430    359    257       O  
ATOM   1044  CB  PHE B 116     -10.990 -15.057 -20.480  1.00 38.82           C  
ANISOU 1044  CB  PHE B 116     5341   4859   4549    521    262    225       C  
ATOM   1045  CG  PHE B 116     -11.427 -16.303 -21.186  1.00 37.55           C  
ANISOU 1045  CG  PHE B 116     5110   4792   4364    553    224    209       C  
ATOM   1046  CD1 PHE B 116     -12.587 -16.317 -21.954  1.00 37.07           C  
ANISOU 1046  CD1 PHE B 116     5041   4791   4253    634    225    227       C  
ATOM   1047  CD2 PHE B 116     -10.704 -17.483 -21.043  1.00 36.00           C  
ANISOU 1047  CD2 PHE B 116     4858   4627   4194    501    188    173       C  
ATOM   1048  CE1 PHE B 116     -13.007 -17.484 -22.590  1.00 37.35           C  
ANISOU 1048  CE1 PHE B 116     5009   4914   4265    655    189    202       C  
ATOM   1049  CE2 PHE B 116     -11.113 -18.651 -21.678  1.00 35.15           C  
ANISOU 1049  CE2 PHE B 116     4692   4596   4066    526    156    152       C  
ATOM   1050  CZ  PHE B 116     -12.267 -18.655 -22.451  1.00 35.69           C  
ANISOU 1050  CZ  PHE B 116     4751   4723   4087    598    156    162       C  
ATOM   1051  N   GLN B 117     -11.154 -11.794 -21.067  1.00 45.85           N  
ANISOU 1051  N   GLN B 117     6415   5583   5422    587    403    330       N  
ATOM   1052  CA  GLN B 117     -11.274 -10.476 -20.452  1.00 49.21           C  
ANISOU 1052  CA  GLN B 117     6931   5906   5860    587    452    346       C  
ATOM   1053  C   GLN B 117     -12.427 -10.448 -19.456  1.00 50.44           C  
ANISOU 1053  C   GLN B 117     7100   6062   5999    627    428    322       C  
ATOM   1054  O   GLN B 117     -13.487 -11.030 -19.703  1.00 50.68           O  
ANISOU 1054  O   GLN B 117     7092   6174   5991    697    399    325       O  
ATOM   1055  CB  GLN B 117     -11.499  -9.410 -21.525  1.00 50.23           C  
ANISOU 1055  CB  GLN B 117     7123   6001   5960    658    522    416       C  
ATOM   1056  CG  GLN B 117     -10.875  -8.061 -21.202  1.00 52.56           C  
ANISOU 1056  CG  GLN B 117     7512   6166   6290    615    589    436       C  
ATOM   1057  CD  GLN B 117      -9.354  -8.115 -21.168  1.00 54.86           C  
ANISOU 1057  CD  GLN B 117     7788   6423   6633    500    596    417       C  
ATOM   1058  OE1 GLN B 117      -8.725  -7.556 -20.267  1.00 56.57           O  
ANISOU 1058  OE1 GLN B 117     8044   6557   6893    417    610    384       O  
ATOM   1059  NE2 GLN B 117      -8.757  -8.798 -22.146  1.00 54.54           N  
ANISOU 1059  NE2 GLN B 117     7685   6452   6584    493    586    434       N  
ATOM   1060  N   THR B 118     -12.208  -9.784 -18.325  1.00 52.36           N  
ANISOU 1060  N   THR B 118     7398   6222   6273    580    440    295       N  
ATOM   1061  CA  THR B 118     -13.259  -9.571 -17.327  1.00 53.82           C  
ANISOU 1061  CA  THR B 118     7609   6396   6442    621    427    276       C  
ATOM   1062  C   THR B 118     -13.061  -8.201 -16.675  1.00 55.26           C  
ANISOU 1062  C   THR B 118     7893   6457   6644    603    482    276       C  
ATOM   1063  O   THR B 118     -11.987  -7.596 -16.798  1.00 55.90           O  
ANISOU 1063  O   THR B 118     8012   6464   6762    533    518    277       O  
ATOM   1064  CB  THR B 118     -13.264 -10.680 -16.230  1.00 53.20           C  
ANISOU 1064  CB  THR B 118     7463   6368   6379    570    359    216       C  
ATOM   1065  OG1 THR B 118     -12.835 -11.931 -16.788  1.00 53.42           O  
ANISOU 1065  OG1 THR B 118     7406   6478   6412    544    317    206       O  
ATOM   1066  CG2 THR B 118     -14.664 -10.852 -15.632  1.00 53.40           C  
ANISOU 1066  CG2 THR B 118     7483   6434   6370    642    338    210       C  
ATOM   1067  N   THR B 119     -14.106  -7.716 -16.000  1.00 56.26           N  
ANISOU 1067  N   THR B 119     8064   6563   6747    665    490    274       N  
ATOM   1068  CA  THR B 119     -14.027  -6.526 -15.142  1.00 57.44           C  
ANISOU 1068  CA  THR B 119     8311   6597   6915    647    534    259       C  
ATOM   1069  C   THR B 119     -13.162  -6.794 -13.904  1.00 57.26           C  
ANISOU 1069  C   THR B 119     8272   6548   6934    534    498    187       C  
ATOM   1070  O   THR B 119     -12.608  -5.861 -13.315  1.00 58.17           O  
ANISOU 1070  O   THR B 119     8460   6563   7078    479    534    162       O  
ATOM   1071  CB  THR B 119     -15.425  -6.059 -14.683  1.00 57.73           C  
ANISOU 1071  CB  THR B 119     8391   6634   6909    752    546    272       C  
ATOM   1072  OG1 THR B 119     -16.231  -7.203 -14.371  1.00 57.89           O  
ANISOU 1072  OG1 THR B 119     8323   6769   6901    783    481    253       O  
ATOM   1073  CG2 THR B 119     -16.109  -5.234 -15.773  1.00 58.68           C  
ANISOU 1073  CG2 THR B 119     8567   6736   6989    863    608    347       C  
ATOM   1074  N   THR B 120     -13.064  -8.070 -13.517  1.00 56.38           N  
ANISOU 1074  N   THR B 120     8066   6528   6824    502    429    153       N  
ATOM   1075  CA  THR B 120     -12.155  -8.520 -12.457  1.00 55.87           C  
ANISOU 1075  CA  THR B 120     7968   6464   6794    401    389     91       C  
ATOM   1076  C   THR B 120     -10.702  -8.308 -12.902  1.00 55.53           C  
ANISOU 1076  C   THR B 120     7922   6383   6790    307    409     86       C  
ATOM   1077  O   THR B 120     -10.019  -7.391 -12.430  1.00 56.34           O  
ANISOU 1077  O   THR B 120     8085   6401   6921    241    442     61       O  
ATOM   1078  CB  THR B 120     -12.358 -10.025 -12.120  1.00 55.12           C  
ANISOU 1078  CB  THR B 120     7772   6478   6691    398    318     70       C  
ATOM   1079  OG1 THR B 120     -13.688 -10.440 -12.470  1.00 55.31           O  
ANISOU 1079  OG1 THR B 120     7774   6564   6675    494    307     99       O  
ATOM   1080  CG2 THR B 120     -12.099 -10.289 -10.638  1.00 55.28           C  
ANISOU 1080  CG2 THR B 120     7779   6501   6724    343    281     11       C  
ATOM   1081  N   GLY B 121     -10.255  -9.165 -13.822  1.00 54.12           N  
ANISOU 1081  N   GLY B 121     7675   6273   6614    300    389    109       N  
ATOM   1082  CA  GLY B 121      -8.912  -9.110 -14.400  1.00 52.70           C  
ANISOU 1082  CA  GLY B 121     7476   6079   6465    221    406    112       C  
ATOM   1083  C   GLY B 121      -8.802 -10.096 -15.551  1.00 50.88           C  
ANISOU 1083  C   GLY B 121     7174   5934   6222    251    386    146       C  
ATOM   1084  O   GLY B 121      -9.812 -10.452 -16.167  1.00 50.81           O  
ANISOU 1084  O   GLY B 121     7152   5973   6178    339    380    176       O  
ATOM   1085  N   GLU B 122      -7.584 -10.550 -15.837  1.00 49.23           N  
ANISOU 1085  N   GLU B 122     6914   5750   6038    179    376    136       N  
ATOM   1086  CA  GLU B 122      -7.359 -11.456 -16.964  1.00 47.12           C  
ANISOU 1086  CA  GLU B 122     6584   5561   5759    205    362    164       C  
ATOM   1087  C   GLU B 122      -7.039 -12.887 -16.572  1.00 44.79           C  
ANISOU 1087  C   GLU B 122     6199   5350   5468    181    298    129       C  
ATOM   1088  O   GLU B 122      -6.311 -13.150 -15.609  1.00 44.93           O  
ANISOU 1088  O   GLU B 122     6191   5369   5509    113    271     87       O  
ATOM   1089  CB  GLU B 122      -6.262 -10.935 -17.884  1.00 47.97           C  
ANISOU 1089  CB  GLU B 122     6699   5641   5885    161    408    195       C  
ATOM   1090  CG  GLU B 122      -6.752 -10.001 -18.968  1.00 49.79           C  
ANISOU 1090  CG  GLU B 122     6994   5829   6095    226    472    258       C  
ATOM   1091  CD  GLU B 122      -5.626  -9.533 -19.866  1.00 51.91           C  
ANISOU 1091  CD  GLU B 122     7267   6073   6382    179    521    292       C  
ATOM   1092  OE1 GLU B 122      -4.500  -9.331 -19.357  1.00 53.58           O  
ANISOU 1092  OE1 GLU B 122     7469   6255   6631     78    525    263       O  
ATOM   1093  OE2 GLU B 122      -5.863  -9.370 -21.081  1.00 52.63           O  
ANISOU 1093  OE2 GLU B 122     7369   6182   6447    242    555    349       O  
ATOM   1094  N   ILE B 123      -7.580 -13.800 -17.367  1.00 41.81           N  
ANISOU 1094  N   ILE B 123     5776   5042   5065    241    276    146       N  
ATOM   1095  CA  ILE B 123      -7.355 -15.229 -17.220  1.00 38.96           C  
ANISOU 1095  CA  ILE B 123     5337   4757   4708    231    224    119       C  
ATOM   1096  C   ILE B 123      -6.878 -15.764 -18.571  1.00 36.42           C  
ANISOU 1096  C   ILE B 123     4975   4484   4376    248    231    145       C  
ATOM   1097  O   ILE B 123      -7.412 -15.377 -19.614  1.00 35.94           O  
ANISOU 1097  O   ILE B 123     4937   4429   4288    306    260    182       O  
ATOM   1098  CB  ILE B 123      -8.652 -15.939 -16.698  1.00 39.01           C  
ANISOU 1098  CB  ILE B 123     5326   4800   4694    285    186    103       C  
ATOM   1099  CG1 ILE B 123      -8.776 -17.374 -17.210  1.00 39.10           C  
ANISOU 1099  CG1 ILE B 123     5268   4889   4697    305    149     93       C  
ATOM   1100  CG2 ILE B 123      -9.918 -15.126 -17.044  1.00 40.51           C  
ANISOU 1100  CG2 ILE B 123     5568   4970   4851    359    213    132       C  
ATOM   1101  CD1 ILE B 123     -10.052 -18.055 -16.814  1.00 39.97           C  
ANISOU 1101  CD1 ILE B 123     5360   5036   4790    350    119     78       C  
ATOM   1102  N   GLY B 124      -5.859 -16.623 -18.548  1.00 33.14           N  
ANISOU 1102  N   GLY B 124     4502   4108   3978    203    208    126       N  
ATOM   1103  CA  GLY B 124      -5.366 -17.264 -19.764  1.00 30.47           C  
ANISOU 1103  CA  GLY B 124     4123   3824   3630    221    212    144       C  
ATOM   1104  C   GLY B 124      -6.445 -18.086 -20.450  1.00 28.16           C  
ANISOU 1104  C   GLY B 124     3809   3586   3305    295    191    145       C  
ATOM   1105  O   GLY B 124      -7.367 -18.570 -19.796  1.00 27.22           O  
ANISOU 1105  O   GLY B 124     3683   3477   3180    316    160    122       O  
ATOM   1106  N   ALA B 125      -6.319 -18.234 -21.767  1.00 26.65           N  
ANISOU 1106  N   ALA B 125     3602   3433   3089    331    208    170       N  
ATOM   1107  CA  ALA B 125      -7.301 -18.935 -22.588  1.00 25.37           C  
ANISOU 1107  CA  ALA B 125     3416   3331   2890    399    191    167       C  
ATOM   1108  C   ALA B 125      -6.608 -19.964 -23.478  1.00 24.39           C  
ANISOU 1108  C   ALA B 125     3240   3266   2760    401    180    156       C  
ATOM   1109  O   ALA B 125      -5.801 -19.603 -24.337  1.00 24.95           O  
ANISOU 1109  O   ALA B 125     3310   3345   2823    399    211    185       O  
ATOM   1110  CB  ALA B 125      -8.075 -17.933 -23.451  1.00 26.08           C  
ANISOU 1110  CB  ALA B 125     3549   3417   2940    463    229    210       C  
ATOM   1111  N   ILE B 126      -6.973 -21.230 -23.314  1.00 22.15           N  
ANISOU 1111  N   ILE B 126     2916   3023   2477    408    140    116       N  
ATOM   1112  CA  ILE B 126      -6.342 -22.336 -24.046  1.00 21.42           C  
ANISOU 1112  CA  ILE B 126     2776   2980   2380    412    128     98       C  
ATOM   1113  C   ILE B 126      -7.252 -22.814 -25.172  1.00 20.52           C  
ANISOU 1113  C   ILE B 126     2646   2927   2223    473    121     87       C  
ATOM   1114  O   ILE B 126      -8.297 -23.404 -24.913  1.00 19.30           O  
ANISOU 1114  O   ILE B 126     2480   2792   2060    489     93     56       O  
ATOM   1115  CB  ILE B 126      -6.064 -23.535 -23.095  1.00 20.92           C  
ANISOU 1115  CB  ILE B 126     2680   2915   2350    378     92     56       C  
ATOM   1116  CG1 ILE B 126      -5.272 -23.086 -21.850  1.00 22.67           C  
ANISOU 1116  CG1 ILE B 126     2913   3091   2609    321     92     61       C  
ATOM   1117  CG2 ILE B 126      -5.398 -24.725 -23.846  1.00 22.58           C  
ANISOU 1117  CG2 ILE B 126     2849   3171   2557    387     84     35       C  
ATOM   1118  CD1 ILE B 126      -3.876 -22.563 -22.150  1.00 24.99           C  
ANISOU 1118  CD1 ILE B 126     3199   3381   2912    286    119     85       C  
ATOM   1119  N   ALA B 127      -6.856 -22.565 -26.418  1.00 20.11           N  
ANISOU 1119  N   ALA B 127     2589   2911   2139    504    146    112       N  
ATOM   1120  CA  ALA B 127      -7.653 -23.019 -27.556  1.00 21.11           C  
ANISOU 1120  CA  ALA B 127     2696   3109   2216    564    138     98       C  
ATOM   1121  C   ALA B 127      -7.265 -24.444 -27.981  1.00 20.87           C  
ANISOU 1121  C   ALA B 127     2620   3121   2186    560    114     50       C  
ATOM   1122  O   ALA B 127      -6.672 -24.667 -29.035  1.00 21.49           O  
ANISOU 1122  O   ALA B 127     2682   3243   2240    583    127     55       O  
ATOM   1123  CB  ALA B 127      -7.568 -22.003 -28.746  1.00 21.46           C  
ANISOU 1123  CB  ALA B 127     2760   3179   2213    614    180    152       C  
ATOM   1124  N   LEU B 128      -7.612 -25.409 -27.132  1.00 20.42           N  
ANISOU 1124  N   LEU B 128     2548   3049   2160    532     80      4       N  
ATOM   1125  CA  LEU B 128      -7.402 -26.830 -27.386  1.00 21.11           C  
ANISOU 1125  CA  LEU B 128     2603   3162   2255    527     59    -45       C  
ATOM   1126  C   LEU B 128      -8.650 -27.590 -26.966  1.00 21.19           C  
ANISOU 1126  C   LEU B 128     2602   3180   2268    525     28    -93       C  
ATOM   1127  O   LEU B 128      -9.269 -27.271 -25.938  1.00 20.09           O  
ANISOU 1127  O   LEU B 128     2477   3005   2149    506     19    -87       O  
ATOM   1128  CB  LEU B 128      -6.192 -27.362 -26.611  1.00 20.81           C  
ANISOU 1128  CB  LEU B 128     2557   3083   2264    484     59    -47       C  
ATOM   1129  CG  LEU B 128      -4.804 -26.872 -27.018  1.00 22.82           C  
ANISOU 1129  CG  LEU B 128     2808   3340   2519    478     87     -9       C  
ATOM   1130  CD1 LEU B 128      -3.734 -27.382 -26.048  1.00 22.85           C  
ANISOU 1130  CD1 LEU B 128     2799   3314   2567    436     82    -13       C  
ATOM   1131  CD2 LEU B 128      -4.492 -27.335 -28.427  1.00 25.69           C  
ANISOU 1131  CD2 LEU B 128     3152   3764   2844    519     98    -19       C  
ATOM   1132  N   ASP B 129      -9.024 -28.582 -27.772  1.00 21.51           N  
ANISOU 1132  N   ASP B 129     2617   3268   2287    542     15   -141       N  
ATOM   1133  CA  ASP B 129     -10.298 -29.260 -27.613  1.00 21.86           C  
ANISOU 1133  CA  ASP B 129     2645   3333   2326    538    -10   -190       C  
ATOM   1134  C   ASP B 129     -10.085 -30.753 -27.364  1.00 21.55           C  
ANISOU 1134  C   ASP B 129     2592   3272   2322    508    -24   -246       C  
ATOM   1135  O   ASP B 129     -10.016 -31.548 -28.300  1.00 22.39           O  
ANISOU 1135  O   ASP B 129     2682   3417   2409    521    -26   -289       O  
ATOM   1136  CB  ASP B 129     -11.160 -29.034 -28.866  1.00 22.87           C  
ANISOU 1136  CB  ASP B 129     2754   3546   2388    587    -13   -205       C  
ATOM   1137  CG  ASP B 129     -12.559 -29.636 -28.744  1.00 25.23           C  
ANISOU 1137  CG  ASP B 129     3027   3881   2675    579    -41   -257       C  
ATOM   1138  OD1 ASP B 129     -13.088 -29.759 -27.620  1.00 27.08           O  
ANISOU 1138  OD1 ASP B 129     3267   4075   2947    546    -51   -260       O  
ATOM   1139  OD2 ASP B 129     -13.134 -29.992 -29.792  1.00 29.46           O  
ANISOU 1139  OD2 ASP B 129     3535   4495   3163    605    -51   -297       O  
ATOM   1140  N   PHE B 130      -9.973 -31.135 -26.099  1.00 19.94           N  
ANISOU 1140  N   PHE B 130     2398   3007   2170    469    -29   -244       N  
ATOM   1141  CA  PHE B 130      -9.756 -32.536 -25.762  1.00 20.13           C  
ANISOU 1141  CA  PHE B 130     2417   2999   2232    444    -35   -288       C  
ATOM   1142  C   PHE B 130     -11.072 -33.239 -25.477  1.00 20.86           C  
ANISOU 1142  C   PHE B 130     2498   3096   2332    421    -52   -336       C  
ATOM   1143  O   PHE B 130     -12.097 -32.580 -25.280  1.00 21.08           O  
ANISOU 1143  O   PHE B 130     2519   3149   2340    424    -62   -327       O  
ATOM   1144  CB  PHE B 130      -8.785 -32.636 -24.585  1.00 19.23           C  
ANISOU 1144  CB  PHE B 130     2318   2824   2165    420    -27   -256       C  
ATOM   1145  CG  PHE B 130      -7.444 -32.019 -24.876  1.00 19.32           C  
ANISOU 1145  CG  PHE B 130     2332   2839   2170    434    -10   -215       C  
ATOM   1146  CD1 PHE B 130      -6.642 -32.531 -25.890  1.00 19.08           C  
ANISOU 1146  CD1 PHE B 130     2291   2835   2123    457      0   -229       C  
ATOM   1147  CD2 PHE B 130      -6.977 -30.932 -24.136  1.00 18.12           C  
ANISOU 1147  CD2 PHE B 130     2192   2665   2027    420     -4   -165       C  
ATOM   1148  CE1 PHE B 130      -5.405 -31.959 -26.174  1.00 19.55           C  
ANISOU 1148  CE1 PHE B 130     2347   2905   2175    468     19   -189       C  
ATOM   1149  CE2 PHE B 130      -5.734 -30.358 -24.410  1.00 19.61           C  
ANISOU 1149  CE2 PHE B 130     2378   2860   2211    423     13   -130       C  
ATOM   1150  CZ  PHE B 130      -4.946 -30.880 -25.435  1.00 19.63           C  
ANISOU 1150  CZ  PHE B 130     2366   2895   2198    447     25   -139       C  
ATOM   1151  N   LYS B 131     -11.045 -34.575 -25.461  1.00 21.24           N  
ANISOU 1151  N   LYS B 131     2542   3118   2408    400    -52   -385       N  
ATOM   1152  CA  LYS B 131     -12.257 -35.366 -25.205  1.00 21.99           C  
ANISOU 1152  CA  LYS B 131     2626   3212   2517    368    -63   -436       C  
ATOM   1153  C   LYS B 131     -12.823 -35.119 -23.796  1.00 21.02           C  
ANISOU 1153  C   LYS B 131     2510   3050   2427    340    -67   -406       C  
ATOM   1154  O   LYS B 131     -12.073 -34.808 -22.872  1.00 20.56           O  
ANISOU 1154  O   LYS B 131     2470   2945   2396    339    -59   -359       O  
ATOM   1155  CB  LYS B 131     -11.976 -36.865 -25.391  1.00 22.85           C  
ANISOU 1155  CB  LYS B 131     2740   3282   2657    346    -54   -492       C  
ATOM   1156  CG  LYS B 131     -11.787 -37.307 -26.851  1.00 26.54           C  
ANISOU 1156  CG  LYS B 131     3198   3799   3087    368    -53   -545       C  
ATOM   1157  CD  LYS B 131     -13.133 -37.464 -27.544  1.00 32.79           C  
ANISOU 1157  CD  LYS B 131     3958   4656   3844    353    -72   -606       C  
ATOM   1158  CE  LYS B 131     -12.966 -37.799 -29.013  1.00 36.46           C  
ANISOU 1158  CE  LYS B 131     4409   5182   4260    379    -75   -660       C  
ATOM   1159  NZ  LYS B 131     -14.186 -38.474 -29.538  1.00 39.53           N  
ANISOU 1159  NZ  LYS B 131     4769   5619   4631    345    -91   -744       N  
ATOM   1160  N   PRO B 132     -14.154 -35.234 -23.638  1.00 20.77           N  
ANISOU 1160  N   PRO B 132     2457   3044   2388    320    -79   -433       N  
ATOM   1161  CA  PRO B 132     -14.770 -35.232 -22.306  1.00 20.07           C  
ANISOU 1161  CA  PRO B 132     2372   2919   2332    292    -80   -412       C  
ATOM   1162  C   PRO B 132     -14.073 -36.226 -21.387  1.00 19.36           C  
ANISOU 1162  C   PRO B 132     2304   2748   2300    266    -64   -407       C  
ATOM   1163  O   PRO B 132     -13.725 -37.340 -21.816  1.00 19.28           O  
ANISOU 1163  O   PRO B 132     2301   2712   2312    254    -54   -447       O  
ATOM   1164  CB  PRO B 132     -16.206 -35.679 -22.591  1.00 20.82           C  
ANISOU 1164  CB  PRO B 132     2433   3061   2414    266    -92   -463       C  
ATOM   1165  CG  PRO B 132     -16.462 -35.129 -23.979  1.00 21.44           C  
ANISOU 1165  CG  PRO B 132     2489   3226   2430    301   -104   -485       C  
ATOM   1166  CD  PRO B 132     -15.167 -35.387 -24.705  1.00 20.96           C  
ANISOU 1166  CD  PRO B 132     2448   3144   2369    322    -93   -487       C  
ATOM   1167  N   GLY B 133     -13.802 -35.778 -20.161  1.00 17.83           N  
ANISOU 1167  N   GLY B 133     2127   2518   2129    266    -61   -356       N  
ATOM   1168  CA  GLY B 133     -13.063 -36.569 -19.185  1.00 17.71           C  
ANISOU 1168  CA  GLY B 133     2132   2436   2161    254    -46   -338       C  
ATOM   1169  C   GLY B 133     -11.678 -36.019 -18.908  1.00 16.37           C  
ANISOU 1169  C   GLY B 133     1977   2251   1989    280    -41   -292       C  
ATOM   1170  O   GLY B 133     -10.980 -36.526 -18.028  1.00 16.23           O  
ANISOU 1170  O   GLY B 133     1972   2190   2002    279    -30   -269       O  
ATOM   1171  N   THR B 134     -11.304 -34.968 -19.644  1.00 15.70           N  
ANISOU 1171  N   THR B 134     1888   2206   1867    303    -48   -278       N  
ATOM   1172  CA ATHR B 134      -9.975 -34.343 -19.512  0.50 14.41           C  
ANISOU 1172  CA ATHR B 134     1734   2039   1701    320    -43   -239       C  
ATOM   1173  CA BTHR B 134      -9.976 -34.368 -19.537  0.50 15.25           C  
ANISOU 1173  CA BTHR B 134     1841   2145   1808    320    -43   -240       C  
ATOM   1174  C   THR B 134      -9.951 -33.217 -18.496  1.00 14.36           C  
ANISOU 1174  C   THR B 134     1736   2026   1691    315    -49   -196       C  
ATOM   1175  O   THR B 134      -8.880 -32.742 -18.118  1.00 13.87           O  
ANISOU 1175  O   THR B 134     1679   1956   1632    318    -45   -166       O  
ATOM   1176  CB ATHR B 134      -9.434 -33.746 -20.837  0.50 14.48           C  
ANISOU 1176  CB ATHR B 134     1738   2090   1674    344    -40   -240       C  
ATOM   1177  CB BTHR B 134      -9.490 -33.931 -20.954  0.50 15.59           C  
ANISOU 1177  CB BTHR B 134     1877   2231   1816    344    -40   -248       C  
ATOM   1178  OG1ATHR B 134     -10.479 -33.073 -21.559  0.50 12.10           O  
ANISOU 1178  OG1ATHR B 134     1428   1831   1335    354    -49   -252       O  
ATOM   1179  OG1BTHR B 134      -9.627 -35.038 -21.859  0.50 16.25           O  
ANISOU 1179  OG1BTHR B 134     1953   2321   1898    348    -36   -297       O  
ATOM   1180  CG2ATHR B 134      -8.786 -34.821 -21.687  0.50 13.70           C  
ANISOU 1180  CG2ATHR B 134     1634   1990   1580    356    -30   -272       C  
ATOM   1181  CG2BTHR B 134      -8.037 -33.492 -20.965  0.50 16.34           C  
ANISOU 1181  CG2BTHR B 134     1974   2324   1909    357    -30   -212       C  
ATOM   1182  N   SER B 135     -11.124 -32.778 -18.042  1.00 13.80           N  
ANISOU 1182  N   SER B 135     1666   1961   1613    308    -58   -195       N  
ATOM   1183  CA  SER B 135     -11.176 -31.758 -16.995  1.00 13.42           C  
ANISOU 1183  CA  SER B 135     1632   1904   1563    305    -62   -160       C  
ATOM   1184  C   SER B 135     -10.280 -32.098 -15.810  1.00 13.08           C  
ANISOU 1184  C   SER B 135     1593   1827   1547    294    -59   -139       C  
ATOM   1185  O   SER B 135     -10.345 -33.218 -15.285  1.00 13.39           O  
ANISOU 1185  O   SER B 135     1628   1844   1612    287    -55   -146       O  
ATOM   1186  CB  SER B 135     -12.607 -31.561 -16.479  1.00 13.28           C  
ANISOU 1186  CB  SER B 135     1612   1895   1538    301    -69   -165       C  
ATOM   1187  OG  SER B 135     -13.295 -30.645 -17.294  1.00 13.52           O  
ANISOU 1187  OG  SER B 135     1641   1965   1531    322    -72   -166       O  
ATOM   1188  N   GLY B 136      -9.472 -31.123 -15.382  1.00 12.41           N  
ANISOU 1188  N   GLY B 136     1519   1742   1455    292    -60   -112       N  
ATOM   1189  CA  GLY B 136      -8.503 -31.331 -14.299  1.00 12.80           C  
ANISOU 1189  CA  GLY B 136     1565   1776   1520    284    -60    -92       C  
ATOM   1190  C   GLY B 136      -7.089 -31.616 -14.810  1.00 13.07           C  
ANISOU 1190  C   GLY B 136     1586   1821   1557    288    -53    -87       C  
ATOM   1191  O   GLY B 136      -6.133 -31.618 -14.032  1.00 13.76           O  
ANISOU 1191  O   GLY B 136     1664   1912   1649    284    -55    -70       O  
ATOM   1192  N   SER B 137      -6.950 -31.837 -16.120  1.00 13.42           N  
ANISOU 1192  N   SER B 137     1626   1879   1593    300    -46   -102       N  
ATOM   1193  CA  SER B 137      -5.610 -32.034 -16.733  1.00 13.76           C  
ANISOU 1193  CA  SER B 137     1654   1940   1634    309    -36    -95       C  
ATOM   1194  C   SER B 137      -4.765 -30.774 -16.510  1.00 13.82           C  
ANISOU 1194  C   SER B 137     1658   1961   1628    291    -36    -70       C  
ATOM   1195  O   SER B 137      -5.251 -29.666 -16.733  1.00 14.65           O  
ANISOU 1195  O   SER B 137     1780   2064   1719    281    -35    -65       O  
ATOM   1196  CB  SER B 137      -5.726 -32.348 -18.234  1.00 14.00           C  
ANISOU 1196  CB  SER B 137     1680   1987   1649    328    -28   -118       C  
ATOM   1197  OG  SER B 137      -6.309 -33.635 -18.438  1.00 16.20           O  
ANISOU 1197  OG  SER B 137     1961   2251   1944    337    -26   -149       O  
ATOM   1198  N   PRO B 138      -3.503 -30.936 -16.063  1.00 14.01           N  
ANISOU 1198  N   PRO B 138     1661   2002   1657    286    -34    -56       N  
ATOM   1199  CA  PRO B 138      -2.704 -29.756 -15.734  1.00 14.55           C  
ANISOU 1199  CA  PRO B 138     1725   2086   1717    257    -34    -38       C  
ATOM   1200  C   PRO B 138      -2.151 -29.005 -16.935  1.00 14.64           C  
ANISOU 1200  C   PRO B 138     1733   2115   1714    251    -17    -30       C  
ATOM   1201  O   PRO B 138      -1.772 -29.598 -17.954  1.00 15.12           O  
ANISOU 1201  O   PRO B 138     1780   2195   1769    275     -7    -33       O  
ATOM   1202  CB  PRO B 138      -1.551 -30.323 -14.904  1.00 14.72           C  
ANISOU 1202  CB  PRO B 138     1715   2133   1744    257    -38    -28       C  
ATOM   1203  CG  PRO B 138      -1.348 -31.719 -15.469  1.00 14.67           C  
ANISOU 1203  CG  PRO B 138     1696   2130   1745    297    -30    -33       C  
ATOM   1204  CD  PRO B 138      -2.789 -32.189 -15.747  1.00 14.37           C  
ANISOU 1204  CD  PRO B 138     1688   2054   1716    308    -31    -54       C  
ATOM   1205  N   ILE B 139      -2.128 -27.691 -16.779  1.00 14.81           N  
ANISOU 1205  N   ILE B 139     1771   2125   1728    220    -12    -20       N  
ATOM   1206  CA  ILE B 139      -1.510 -26.776 -17.707  1.00 14.96           C  
ANISOU 1206  CA  ILE B 139     1791   2155   1737    205      9     -4       C  
ATOM   1207  C   ILE B 139      -0.209 -26.392 -17.038  1.00 15.57           C  
ANISOU 1207  C   ILE B 139     1840   2254   1820    164      9      3       C  
ATOM   1208  O   ILE B 139      -0.215 -25.979 -15.881  1.00 15.11           O  
ANISOU 1208  O   ILE B 139     1787   2185   1768    135     -2     -2       O  
ATOM   1209  CB  ILE B 139      -2.388 -25.544 -17.909  1.00 15.29           C  
ANISOU 1209  CB  ILE B 139     1876   2162   1769    197     20      3       C  
ATOM   1210  CG1 ILE B 139      -3.792 -25.965 -18.384  1.00 14.99           C  
ANISOU 1210  CG1 ILE B 139     1856   2116   1720    239     13     -8       C  
ATOM   1211  CG2 ILE B 139      -1.733 -24.553 -18.902  1.00 15.86           C  
ANISOU 1211  CG2 ILE B 139     1955   2239   1832    183     51     26       C  
ATOM   1212  CD1 ILE B 139      -4.886 -24.884 -18.121  1.00 14.47           C  
ANISOU 1212  CD1 ILE B 139     1834   2018   1645    241     18     -1       C  
ATOM   1213  N   ILE B 140       0.907 -26.542 -17.756  1.00 16.08           N  
ANISOU 1213  N   ILE B 140     1871   2358   1879    162     24     15       N  
ATOM   1214  CA  ILE B 140       2.227 -26.404 -17.132  1.00 17.08           C  
ANISOU 1214  CA  ILE B 140     1955   2524   2008    126     22     20       C  
ATOM   1215  C   ILE B 140       3.163 -25.436 -17.850  1.00 18.84           C  
ANISOU 1215  C   ILE B 140     2164   2765   2226     86     49     37       C  
ATOM   1216  O   ILE B 140       3.021 -25.206 -19.053  1.00 18.29           O  
ANISOU 1216  O   ILE B 140     2108   2691   2148    104     72     52       O  
ATOM   1217  CB  ILE B 140       2.935 -27.773 -16.990  1.00 17.89           C  
ANISOU 1217  CB  ILE B 140     2014   2674   2109    164     12     19       C  
ATOM   1218  CG1 ILE B 140       3.179 -28.392 -18.370  1.00 17.91           C  
ANISOU 1218  CG1 ILE B 140     2006   2695   2101    206     31     27       C  
ATOM   1219  CG2 ILE B 140       2.103 -28.724 -16.118  1.00 17.23           C  
ANISOU 1219  CG2 ILE B 140     1945   2566   2033    196     -8      6       C  
ATOM   1220  CD1 ILE B 140       4.252 -29.485 -18.355  1.00 21.49           C  
ANISOU 1220  CD1 ILE B 140     2411   3202   2549    239     31     32       C  
ATOM   1221  N   ASN B 141       4.102 -24.861 -17.101  1.00 19.67           N  
ANISOU 1221  N   ASN B 141     2240   2895   2335     31     47     35       N  
ATOM   1222  CA  ASN B 141       5.142 -24.034 -17.710  1.00 21.54           C  
ANISOU 1222  CA  ASN B 141     2455   3158   2572    -15     75     51       C  
ATOM   1223  C   ASN B 141       6.404 -24.856 -17.964  1.00 22.59           C  
ANISOU 1223  C   ASN B 141     2517   3371   2693     -1     75     61       C  
ATOM   1224  O   ASN B 141       6.449 -26.051 -17.646  1.00 21.69           O  
ANISOU 1224  O   ASN B 141     2380   3288   2574     49     55     55       O  
ATOM   1225  CB  ASN B 141       5.436 -22.775 -16.877  1.00 22.29           C  
ANISOU 1225  CB  ASN B 141     2559   3230   2677    -96     80     38       C  
ATOM   1226  CG  ASN B 141       6.006 -23.083 -15.490  1.00 22.51           C  
ANISOU 1226  CG  ASN B 141     2546   3303   2703   -123     47     13       C  
ATOM   1227  OD1 ASN B 141       6.598 -24.137 -15.253  1.00 21.33           O  
ANISOU 1227  OD1 ASN B 141     2344   3218   2542    -89     29     15       O  
ATOM   1228  ND2 ASN B 141       5.836 -22.135 -14.565  1.00 23.33           N  
ANISOU 1228  ND2 ASN B 141     2674   3375   2814   -181     42    -10       N  
ATOM   1229  N   ARG B 142       7.429 -24.213 -18.519  1.00 24.31           N  
ANISOU 1229  N   ARG B 142     2702   3624   2908    -44    102     77       N  
ATOM   1230  CA  ARG B 142       8.639 -24.914 -18.944  1.00 26.74           C  
ANISOU 1230  CA  ARG B 142     2940   4016   3201    -26    108     91       C  
ATOM   1231  C   ARG B 142       9.481 -25.454 -17.779  1.00 27.45           C  
ANISOU 1231  C   ARG B 142     2969   4175   3284    -36     80     77       C  
ATOM   1232  O   ARG B 142      10.377 -26.290 -17.987  1.00 27.51           O  
ANISOU 1232  O   ARG B 142     2918   4257   3274      1     80     89       O  
ATOM   1233  CB  ARG B 142       9.477 -24.018 -19.874  1.00 27.68           C  
ANISOU 1233  CB  ARG B 142     3039   4158   3319    -73    148    116       C  
ATOM   1234  CG  ARG B 142      10.474 -24.781 -20.728  1.00 30.97           C  
ANISOU 1234  CG  ARG B 142     3395   4655   3715    -32    163    138       C  
ATOM   1235  CD  ARG B 142      11.137 -23.872 -21.768  1.00 37.46           C  
ANISOU 1235  CD  ARG B 142     4204   5493   4535    -74    209    168       C  
ATOM   1236  NE  ARG B 142      11.979 -24.641 -22.684  1.00 42.32           N  
ANISOU 1236  NE  ARG B 142     4766   6186   5127    -23    225    191       N  
ATOM   1237  CZ  ARG B 142      11.611 -25.034 -23.901  1.00 45.24           C  
ANISOU 1237  CZ  ARG B 142     5159   6549   5481     41    244    208       C  
ATOM   1238  NH1 ARG B 142      12.452 -25.736 -24.649  1.00 47.78           N  
ANISOU 1238  NH1 ARG B 142     5429   6946   5778     88    259    225       N  
ATOM   1239  NH2 ARG B 142      10.412 -24.717 -24.385  1.00 46.52           N  
ANISOU 1239  NH2 ARG B 142     5392   6635   5645     63    250    207       N  
ATOM   1240  N   GLU B 143       9.181 -24.990 -16.566  1.00 27.72           N  
ANISOU 1240  N   GLU B 143     3016   4188   3325    -78     57     53       N  
ATOM   1241  CA  GLU B 143       9.802 -25.518 -15.343  1.00 28.80           C  
ANISOU 1241  CA  GLU B 143     3100   4393   3450    -78     26     39       C  
ATOM   1242  C   GLU B 143       9.124 -26.786 -14.834  1.00 27.57           C  
ANISOU 1242  C   GLU B 143     2960   4227   3289      2      2     39       C  
ATOM   1243  O   GLU B 143       9.573 -27.382 -13.852  1.00 27.93           O  
ANISOU 1243  O   GLU B 143     2964   4327   3318     21    -20     35       O  
ATOM   1244  CB  GLU B 143       9.761 -24.484 -14.222  1.00 29.62           C  
ANISOU 1244  CB  GLU B 143     3211   4484   3559   -158     11      9       C  
ATOM   1245  CG  GLU B 143      10.721 -23.325 -14.371  1.00 35.20           C  
ANISOU 1245  CG  GLU B 143     3884   5220   4269   -253     31      1       C  
ATOM   1246  CD  GLU B 143      10.497 -22.276 -13.294  1.00 40.89           C  
ANISOU 1246  CD  GLU B 143     4628   5908   4997   -332     19    -37       C  
ATOM   1247  OE1 GLU B 143      10.725 -22.571 -12.094  1.00 43.52           O  
ANISOU 1247  OE1 GLU B 143     4926   6294   5313   -336    -15    -62       O  
ATOM   1248  OE2 GLU B 143      10.084 -21.151 -13.651  1.00 44.92           O  
ANISOU 1248  OE2 GLU B 143     5196   6340   5531   -387     46    -43       O  
ATOM   1249  N   GLY B 144       8.029 -27.184 -15.474  1.00 25.97           N  
ANISOU 1249  N   GLY B 144     2815   3953   3097     49      9     43       N  
ATOM   1250  CA  GLY B 144       7.266 -28.341 -15.018  1.00 24.54           C  
ANISOU 1250  CA  GLY B 144     2656   3747   2917    117     -7     40       C  
ATOM   1251  C   GLY B 144       6.346 -28.023 -13.846  1.00 23.36           C  
ANISOU 1251  C   GLY B 144     2544   3555   2776     98    -29     22       C  
ATOM   1252  O   GLY B 144       5.971 -28.920 -13.080  1.00 23.78           O  
ANISOU 1252  O   GLY B 144     2601   3606   2828    141    -45     23       O  
ATOM   1253  N   LYS B 145       5.987 -26.751 -13.696  1.00 22.00           N  
ANISOU 1253  N   LYS B 145     2402   3344   2612     35    -27      8       N  
ATOM   1254  CA  LYS B 145       5.079 -26.326 -12.634  1.00 20.97           C  
ANISOU 1254  CA  LYS B 145     2310   3170   2485     18    -45    -10       C  
ATOM   1255  C   LYS B 145       3.678 -26.087 -13.194  1.00 19.38           C  
ANISOU 1255  C   LYS B 145     2177   2886   2298     36    -36    -10       C  
ATOM   1256  O   LYS B 145       3.524 -25.617 -14.323  1.00 17.52           O  
ANISOU 1256  O   LYS B 145     1963   2626   2068     32    -12     -1       O  
ATOM   1257  CB  LYS B 145       5.589 -25.069 -11.934  1.00 22.20           C  
ANISOU 1257  CB  LYS B 145     2457   3338   2639    -61    -49    -31       C  
ATOM   1258  CG  LYS B 145       7.031 -25.203 -11.400  1.00 25.77           C  
ANISOU 1258  CG  LYS B 145     2830   3888   3072    -88    -60    -35       C  
ATOM   1259  CD  LYS B 145       7.301 -24.147 -10.355  1.00 32.59           C  
ANISOU 1259  CD  LYS B 145     3688   4764   3929   -165    -74    -70       C  
ATOM   1260  CE  LYS B 145       8.742 -24.161  -9.891  1.00 36.50           C  
ANISOU 1260  CE  LYS B 145     4097   5367   4401   -202    -85    -79       C  
ATOM   1261  NZ  LYS B 145       9.005 -22.977  -9.013  1.00 39.57           N  
ANISOU 1261  NZ  LYS B 145     4485   5763   4787   -292    -95   -123       N  
ATOM   1262  N   VAL B 146       2.675 -26.404 -12.390  1.00 17.92           N  
ANISOU 1262  N   VAL B 146     2022   2670   2116     59    -53    -19       N  
ATOM   1263  CA  VAL B 146       1.282 -26.352 -12.844  1.00 17.25           C  
ANISOU 1263  CA  VAL B 146     1992   2521   2039     84    -47    -20       C  
ATOM   1264  C   VAL B 146       0.764 -24.919 -12.666  1.00 17.39           C  
ANISOU 1264  C   VAL B 146     2054   2494   2059     40    -39    -30       C  
ATOM   1265  O   VAL B 146       0.693 -24.422 -11.541  1.00 18.00           O  
ANISOU 1265  O   VAL B 146     2138   2566   2132     12    -53    -47       O  
ATOM   1266  CB  VAL B 146       0.410 -27.360 -12.059  1.00 16.81           C  
ANISOU 1266  CB  VAL B 146     1946   2453   1987    127    -64    -23       C  
ATOM   1267  CG1 VAL B 146      -1.071 -27.283 -12.505  1.00 16.51           C  
ANISOU 1267  CG1 VAL B 146     1957   2360   1956    148    -59    -27       C  
ATOM   1268  CG2 VAL B 146       0.970 -28.805 -12.205  1.00 17.05           C  
ANISOU 1268  CG2 VAL B 146     1941   2518   2018    174    -65    -11       C  
ATOM   1269  N   VAL B 147       0.437 -24.254 -13.776  1.00 16.77           N  
ANISOU 1269  N   VAL B 147     2006   2382   1983     38    -15    -20       N  
ATOM   1270  CA  VAL B 147      -0.094 -22.896 -13.737  1.00 16.37           C  
ANISOU 1270  CA  VAL B 147     2006   2279   1933      7      0    -24       C  
ATOM   1271  C   VAL B 147      -1.621 -22.871 -13.692  1.00 15.73           C  
ANISOU 1271  C   VAL B 147     1972   2154   1849     48     -2    -24       C  
ATOM   1272  O   VAL B 147      -2.226 -21.833 -13.478  1.00 15.84           O  
ANISOU 1272  O   VAL B 147     2032   2122   1860     35      9    -27       O  
ATOM   1273  CB  VAL B 147       0.418 -22.014 -14.911  1.00 16.67           C  
ANISOU 1273  CB  VAL B 147     2055   2303   1973    -16     36     -5       C  
ATOM   1274  CG1 VAL B 147       1.937 -21.845 -14.835  1.00 17.89           C  
ANISOU 1274  CG1 VAL B 147     2160   2503   2131    -70     42     -6       C  
ATOM   1275  CG2 VAL B 147       0.006 -22.581 -16.272  1.00 15.57           C  
ANISOU 1275  CG2 VAL B 147     1918   2171   1826     37     49     15       C  
ATOM   1276  N   GLY B 148      -2.245 -24.022 -13.886  1.00 15.09           N  
ANISOU 1276  N   GLY B 148     1878   2087   1766     96    -16    -23       N  
ATOM   1277  CA  GLY B 148      -3.707 -24.069 -13.820  1.00 14.44           C  
ANISOU 1277  CA  GLY B 148     1830   1975   1679    131    -20    -26       C  
ATOM   1278  C   GLY B 148      -4.218 -25.395 -14.296  1.00 13.33           C  
ANISOU 1278  C   GLY B 148     1669   1854   1540    174    -30    -28       C  
ATOM   1279  O   GLY B 148      -3.428 -26.265 -14.696  1.00 13.53           O  
ANISOU 1279  O   GLY B 148     1660   1908   1570    181    -31    -26       O  
ATOM   1280  N   LEU B 149      -5.540 -25.548 -14.229  1.00 12.13           N  
ANISOU 1280  N   LEU B 149     1538   1687   1383    201    -35    -33       N  
ATOM   1281  CA  LEU B 149      -6.200 -26.749 -14.700  1.00 12.02           C  
ANISOU 1281  CA  LEU B 149     1508   1686   1373    233    -42    -42       C  
ATOM   1282  C   LEU B 149      -7.126 -26.445 -15.868  1.00 12.20           C  
ANISOU 1282  C   LEU B 149     1545   1710   1377    260    -32    -42       C  
ATOM   1283  O   LEU B 149      -7.773 -25.397 -15.901  1.00 12.79           O  
ANISOU 1283  O   LEU B 149     1650   1770   1436    266    -24    -33       O  
ATOM   1284  CB  LEU B 149      -6.986 -27.412 -13.566  1.00 11.12           C  
ANISOU 1284  CB  LEU B 149     1393   1564   1268    240    -58    -50       C  
ATOM   1285  CG  LEU B 149      -6.193 -27.755 -12.299  1.00 11.07           C  
ANISOU 1285  CG  LEU B 149     1370   1563   1271    223    -69    -46       C  
ATOM   1286  CD1 LEU B 149      -7.146 -28.441 -11.321  1.00 12.08           C  
ANISOU 1286  CD1 LEU B 149     1500   1683   1405    237    -78    -49       C  
ATOM   1287  CD2 LEU B 149      -4.973 -28.641 -12.593  1.00 10.70           C  
ANISOU 1287  CD2 LEU B 149     1290   1540   1234    226    -67    -42       C  
ATOM   1288  N   TYR B 150      -7.189 -27.408 -16.786  1.00 12.08           N  
ANISOU 1288  N   TYR B 150     1510   1718   1361    280    -32    -54       N  
ATOM   1289  CA  TYR B 150      -7.947 -27.333 -18.033  1.00 12.53           C  
ANISOU 1289  CA  TYR B 150     1570   1794   1394    309    -25    -60       C  
ATOM   1290  C   TYR B 150      -9.327 -27.900 -17.830  1.00 12.59           C  
ANISOU 1290  C   TYR B 150     1575   1809   1400    323    -39    -80       C  
ATOM   1291  O   TYR B 150      -9.485 -28.921 -17.159  1.00 13.26           O  
ANISOU 1291  O   TYR B 150     1646   1885   1507    313    -49    -96       O  
ATOM   1292  CB  TYR B 150      -7.239 -28.222 -19.080  1.00 12.90           C  
ANISOU 1292  CB  TYR B 150     1592   1867   1440    321    -21    -72       C  
ATOM   1293  CG  TYR B 150      -8.009 -28.437 -20.382  1.00 12.63           C  
ANISOU 1293  CG  TYR B 150     1553   1867   1379    352    -18    -89       C  
ATOM   1294  CD1 TYR B 150      -7.875 -27.534 -21.445  1.00 14.69           C  
ANISOU 1294  CD1 TYR B 150     1822   2149   1608    373     -1    -69       C  
ATOM   1295  CD2 TYR B 150      -8.841 -29.544 -20.557  1.00 13.21           C  
ANISOU 1295  CD2 TYR B 150     1611   1952   1455    360    -31   -125       C  
ATOM   1296  CE1 TYR B 150      -8.550 -27.728 -22.674  1.00 14.68           C  
ANISOU 1296  CE1 TYR B 150     1811   2192   1572    408      0    -84       C  
ATOM   1297  CE2 TYR B 150      -9.554 -29.736 -21.777  1.00 13.86           C  
ANISOU 1297  CE2 TYR B 150     1682   2077   1506    386    -32   -148       C  
ATOM   1298  CZ  TYR B 150      -9.388 -28.819 -22.825  1.00 16.00           C  
ANISOU 1298  CZ  TYR B 150     1959   2380   1740    413    -18   -127       C  
ATOM   1299  OH  TYR B 150     -10.057 -28.987 -24.026  1.00 15.94           O  
ANISOU 1299  OH  TYR B 150     1937   2426   1693    445    -20   -150       O  
ATOM   1300  N   GLY B 151     -10.331 -27.268 -18.435  1.00 12.57           N  
ANISOU 1300  N   GLY B 151     1581   1825   1368    348    -35    -78       N  
ATOM   1301  CA  GLY B 151     -11.623 -27.916 -18.551  1.00 12.27           C  
ANISOU 1301  CA  GLY B 151     1527   1812   1321    361    -48   -103       C  
ATOM   1302  C   GLY B 151     -12.847 -27.076 -18.236  1.00 12.80           C  
ANISOU 1302  C   GLY B 151     1607   1889   1364    382    -48    -93       C  
ATOM   1303  O   GLY B 151     -13.973 -27.548 -18.429  1.00 13.75           O  
ANISOU 1303  O   GLY B 151     1707   2043   1472    393    -58   -114       O  
ATOM   1304  N   ASN B 152     -12.648 -25.845 -17.767  1.00 12.64           N  
ANISOU 1304  N   ASN B 152     1621   1841   1337    387    -37    -63       N  
ATOM   1305  CA  ASN B 152     -13.777 -24.904 -17.646  1.00 13.31           C  
ANISOU 1305  CA  ASN B 152     1725   1938   1393    420    -31    -48       C  
ATOM   1306  C   ASN B 152     -13.623 -23.843 -18.723  1.00 14.14           C  
ANISOU 1306  C   ASN B 152     1853   2051   1465    456     -8    -21       C  
ATOM   1307  O   ASN B 152     -12.708 -23.018 -18.676  1.00 13.92           O  
ANISOU 1307  O   ASN B 152     1858   1984   1446    444     10      1       O  
ATOM   1308  CB  ASN B 152     -13.855 -24.254 -16.260  1.00 12.91           C  
ANISOU 1308  CB  ASN B 152     1704   1844   1355    408    -30    -35       C  
ATOM   1309  CG  ASN B 152     -15.150 -23.439 -16.083  1.00 15.67           C  
ANISOU 1309  CG  ASN B 152     2070   2209   1672    451    -23    -22       C  
ATOM   1310  OD1 ASN B 152     -15.411 -22.497 -16.833  1.00 15.85           O  
ANISOU 1310  OD1 ASN B 152     2117   2241   1664    490     -4     -1       O  
ATOM   1311  ND2 ASN B 152     -15.974 -23.830 -15.115  1.00 15.69           N  
ANISOU 1311  ND2 ASN B 152     2061   2221   1680    448    -36    -33       N  
ATOM   1312  N   GLY B 153     -14.515 -23.890 -19.705  1.00 15.56           N  
ANISOU 1312  N   GLY B 153     2015   2288   1607    498     -9    -25       N  
ATOM   1313  CA  GLY B 153     -14.300 -23.136 -20.940  1.00 16.58           C  
ANISOU 1313  CA  GLY B 153     2158   2439   1701    538     13      1       C  
ATOM   1314  C   GLY B 153     -15.564 -22.560 -21.534  1.00 17.50           C  
ANISOU 1314  C   GLY B 153     2273   2611   1764    602     19     15       C  
ATOM   1315  O   GLY B 153     -16.563 -22.370 -20.842  1.00 17.05           O  
ANISOU 1315  O   GLY B 153     2216   2562   1698    617     11     14       O  
ATOM   1316  N   VAL B 154     -15.501 -22.268 -22.835  1.00 18.49           N  
ANISOU 1316  N   VAL B 154     2393   2780   1849    644     33     31       N  
ATOM   1317  CA  VAL B 154     -16.647 -21.778 -23.579  1.00 19.74           C  
ANISOU 1317  CA  VAL B 154     2542   3010   1947    715     38     46       C  
ATOM   1318  C   VAL B 154     -16.586 -22.438 -24.943  1.00 20.19           C  
ANISOU 1318  C   VAL B 154     2557   3145   1969    735     29     25       C  
ATOM   1319  O   VAL B 154     -15.494 -22.763 -25.429  1.00 19.55           O  
ANISOU 1319  O   VAL B 154     2476   3044   1905    710     36     22       O  
ATOM   1320  CB  VAL B 154     -16.610 -20.216 -23.783  1.00 21.36           C  
ANISOU 1320  CB  VAL B 154     2807   3180   2125    770     82    110       C  
ATOM   1321  CG1 VAL B 154     -16.738 -19.502 -22.494  1.00 21.96           C  
ANISOU 1321  CG1 VAL B 154     2930   3183   2229    756     93    125       C  
ATOM   1322  CG2 VAL B 154     -15.334 -19.772 -24.481  1.00 20.93           C  
ANISOU 1322  CG2 VAL B 154     2782   3088   2081    760    112    139       C  
ATOM   1323  N   VAL B 155     -17.750 -22.656 -25.547  1.00 20.84           N  
ANISOU 1323  N   VAL B 155     2598   3320   1998    780     14      8       N  
ATOM   1324  CA  VAL B 155     -17.797 -23.058 -26.947  1.00 22.36           C  
ANISOU 1324  CA  VAL B 155     2753   3600   2142    813      9     -8       C  
ATOM   1325  C   VAL B 155     -17.994 -21.774 -27.761  1.00 22.78           C  
ANISOU 1325  C   VAL B 155     2835   3684   2135    899     44     55       C  
ATOM   1326  O   VAL B 155     -18.924 -21.011 -27.506  1.00 22.96           O  
ANISOU 1326  O   VAL B 155     2869   3727   2125    951     53     85       O  
ATOM   1327  CB  VAL B 155     -18.918 -24.082 -27.219  1.00 22.85           C  
ANISOU 1327  CB  VAL B 155     2747   3757   2177    809    -28    -70       C  
ATOM   1328  CG1 VAL B 155     -18.970 -24.468 -28.717  1.00 23.45           C  
ANISOU 1328  CG1 VAL B 155     2782   3932   2193    845    -35    -95       C  
ATOM   1329  CG2 VAL B 155     -18.737 -25.323 -26.335  1.00 24.35           C  
ANISOU 1329  CG2 VAL B 155     2918   3900   2431    724    -54   -126       C  
ATOM   1330  N   THR B 156     -17.103 -21.523 -28.715  1.00 23.47           N  
ANISOU 1330  N   THR B 156     2937   3772   2207    918     67     80       N  
ATOM   1331  CA  THR B 156     -17.168 -20.296 -29.505  1.00 24.82           C  
ANISOU 1331  CA  THR B 156     3142   3963   2323   1000    109    149       C  
ATOM   1332  C   THR B 156     -18.248 -20.407 -30.586  1.00 25.55           C  
ANISOU 1332  C   THR B 156     3185   4193   2329   1079     96    141       C  
ATOM   1333  O   THR B 156     -18.797 -21.502 -30.822  1.00 24.73           O  
ANISOU 1333  O   THR B 156     3016   4168   2210   1058     53     73       O  
ATOM   1334  CB  THR B 156     -15.793 -19.900 -30.114  1.00 25.27           C  
ANISOU 1334  CB  THR B 156     3234   3970   2395    991    146    188       C  
ATOM   1335  OG1 THR B 156     -15.399 -20.861 -31.101  1.00 25.86           O  
ANISOU 1335  OG1 THR B 156     3260   4114   2448    986    126    148       O  
ATOM   1336  CG2 THR B 156     -14.731 -19.819 -29.021  1.00 25.18           C  
ANISOU 1336  CG2 THR B 156     3262   3837   2466    909    155    190       C  
ATOM   1337  N   LYS B 157     -18.579 -19.279 -31.211  1.00 26.49           N  
ANISOU 1337  N   LYS B 157     3333   4342   2390   1170    134    209       N  
ATOM   1338  CA  LYS B 157     -19.651 -19.270 -32.216  1.00 28.16           C  
ANISOU 1338  CA  LYS B 157     3493   4698   2507   1258    123    208       C  
ATOM   1339  C   LYS B 157     -19.410 -20.291 -33.344  1.00 27.96           C  
ANISOU 1339  C   LYS B 157     3406   4769   2446   1251     94    154       C  
ATOM   1340  O   LYS B 157     -20.362 -20.883 -33.854  1.00 29.18           O  
ANISOU 1340  O   LYS B 157     3494   5048   2544   1277     59    106       O  
ATOM   1341  CB  LYS B 157     -19.951 -17.858 -32.760  1.00 29.64           C  
ANISOU 1341  CB  LYS B 157     3728   4899   2633   1369    176    301       C  
ATOM   1342  CG  LYS B 157     -18.758 -16.900 -32.956  1.00 32.15           C  
ANISOU 1342  CG  LYS B 157     4125   5109   2980   1374    237    374       C  
ATOM   1343  CD  LYS B 157     -18.172 -17.030 -34.361  1.00 38.50           C  
ANISOU 1343  CD  LYS B 157     4910   5984   3734   1413    252    391       C  
ATOM   1344  CE  LYS B 157     -17.598 -15.732 -34.922  1.00 40.19           C  
ANISOU 1344  CE  LYS B 157     5196   6146   3928   1478    326    492       C  
ATOM   1345  NZ  LYS B 157     -16.738 -14.948 -33.983  1.00 44.37           N  
ANISOU 1345  NZ  LYS B 157     5807   6509   4539   1418    369    531       N  
ATOM   1346  N   ASN B 158     -18.149 -20.531 -33.691  1.00 26.77           N  
ANISOU 1346  N   ASN B 158     3276   4564   2330   1212    109    155       N  
ATOM   1347  CA  ASN B 158     -17.825 -21.467 -34.784  1.00 26.55           C  
ANISOU 1347  CA  ASN B 158     3197   4623   2268   1209     87    104       C  
ATOM   1348  C   ASN B 158     -17.570 -22.909 -34.338  1.00 25.91           C  
ANISOU 1348  C   ASN B 158     3079   4522   2243   1113     42     11       C  
ATOM   1349  O   ASN B 158     -16.995 -23.703 -35.078  1.00 25.15           O  
ANISOU 1349  O   ASN B 158     2958   4460   2139   1096     31    -31       O  
ATOM   1350  CB  ASN B 158     -16.677 -20.926 -35.650  1.00 26.75           C  
ANISOU 1350  CB  ASN B 158     3257   4626   2279   1240    131    162       C  
ATOM   1351  CG  ASN B 158     -15.313 -21.039 -34.990  1.00 26.63           C  
ANISOU 1351  CG  ASN B 158     3283   4481   2352   1157    148    169       C  
ATOM   1352  OD1 ASN B 158     -14.285 -21.051 -35.683  1.00 28.42           O  
ANISOU 1352  OD1 ASN B 158     3517   4702   2576   1157    172    188       O  
ATOM   1353  ND2 ASN B 158     -15.284 -21.130 -33.659  1.00 24.76           N  
ANISOU 1353  ND2 ASN B 158     3068   4148   2189   1088    136    153       N  
ATOM   1354  N   GLY B 159     -17.994 -23.229 -33.113  1.00 25.06           N  
ANISOU 1354  N   GLY B 159     2972   4356   2192   1054     21    -16       N  
ATOM   1355  CA  GLY B 159     -17.889 -24.576 -32.588  1.00 25.32           C  
ANISOU 1355  CA  GLY B 159     2975   4365   2280    967    -15    -98       C  
ATOM   1356  C   GLY B 159     -16.538 -24.918 -31.971  1.00 24.91           C  
ANISOU 1356  C   GLY B 159     2960   4194   2308    898     -4    -96       C  
ATOM   1357  O   GLY B 159     -16.312 -26.064 -31.600  1.00 26.13           O  
ANISOU 1357  O   GLY B 159     3096   4323   2508    834    -28   -158       O  
ATOM   1358  N   GLY B 160     -15.638 -23.942 -31.868  1.00 23.66           N  
ANISOU 1358  N   GLY B 160     2855   3967   2167    912     35    -25       N  
ATOM   1359  CA  GLY B 160     -14.323 -24.176 -31.255  1.00 22.12           C  
ANISOU 1359  CA  GLY B 160     2689   3670   2043    848     46    -20       C  
ATOM   1360  C   GLY B 160     -14.429 -24.126 -29.738  1.00 20.94           C  
ANISOU 1360  C   GLY B 160     2564   3433   1959    793     38    -20       C  
ATOM   1361  O   GLY B 160     -15.281 -23.428 -29.190  1.00 21.27           O  
ANISOU 1361  O   GLY B 160     2620   3469   1990    816     41      3       O  
ATOM   1362  N   TYR B 161     -13.570 -24.877 -29.069  1.00 19.40           N  
ANISOU 1362  N   TYR B 161     2371   3174   1826    727     29    -47       N  
ATOM   1363  CA  TYR B 161     -13.559 -24.882 -27.620  1.00 18.52           C  
ANISOU 1363  CA  TYR B 161     2280   2983   1774    676     21    -47       C  
ATOM   1364  C   TYR B 161     -12.377 -24.056 -27.119  1.00 18.31           C  
ANISOU 1364  C   TYR B 161     2297   2875   1783    653     51      2       C  
ATOM   1365  O   TYR B 161     -11.270 -24.161 -27.645  1.00 18.71           O  
ANISOU 1365  O   TYR B 161     2348   2918   1841    643     66     12       O  
ATOM   1366  CB  TYR B 161     -13.448 -26.312 -27.116  1.00 17.84           C  
ANISOU 1366  CB  TYR B 161     2164   2882   1730    621     -7   -109       C  
ATOM   1367  CG  TYR B 161     -13.543 -26.386 -25.610  1.00 17.91           C  
ANISOU 1367  CG  TYR B 161     2189   2822   1792    575    -16   -108       C  
ATOM   1368  CD1 TYR B 161     -14.771 -26.227 -24.975  1.00 18.00           C  
ANISOU 1368  CD1 TYR B 161     2195   2847   1796    581    -29   -114       C  
ATOM   1369  CD2 TYR B 161     -12.402 -26.577 -24.824  1.00 17.19           C  
ANISOU 1369  CD2 TYR B 161     2116   2660   1753    530    -10    -99       C  
ATOM   1370  CE1 TYR B 161     -14.872 -26.265 -23.582  1.00 17.30           C  
ANISOU 1370  CE1 TYR B 161     2121   2699   1751    544    -35   -110       C  
ATOM   1371  CE2 TYR B 161     -12.499 -26.622 -23.420  1.00 15.72           C  
ANISOU 1371  CE2 TYR B 161     1943   2419   1609    493    -18    -97       C  
ATOM   1372  CZ  TYR B 161     -13.744 -26.473 -22.824  1.00 17.58           C  
ANISOU 1372  CZ  TYR B 161     2175   2666   1836    501    -30   -103       C  
ATOM   1373  OH  TYR B 161     -13.879 -26.513 -21.448  1.00 17.72           O  
ANISOU 1373  OH  TYR B 161     2205   2636   1890    470    -37   -100       O  
ATOM   1374  N   VAL B 162     -12.607 -23.259 -26.083  1.00 18.11           N  
ANISOU 1374  N   VAL B 162     2307   2793   1780    641     60     29       N  
ATOM   1375  CA  VAL B 162     -11.526 -22.535 -25.441  1.00 17.76           C  
ANISOU 1375  CA  VAL B 162     2302   2670   1775    604     84     64       C  
ATOM   1376  C   VAL B 162     -11.646 -22.677 -23.918  1.00 17.20           C  
ANISOU 1376  C   VAL B 162     2241   2542   1750    557     67     47       C  
ATOM   1377  O   VAL B 162     -12.650 -22.272 -23.343  1.00 17.53           O  
ANISOU 1377  O   VAL B 162     2297   2580   1782    575     62     51       O  
ATOM   1378  CB  VAL B 162     -11.544 -21.040 -25.821  1.00 18.47           C  
ANISOU 1378  CB  VAL B 162     2440   2737   1839    644    127    125       C  
ATOM   1379  CG1 VAL B 162     -10.383 -20.315 -25.164  1.00 18.39           C  
ANISOU 1379  CG1 VAL B 162     2468   2644   1873    592    154    152       C  
ATOM   1380  CG2 VAL B 162     -11.480 -20.849 -27.352  1.00 18.65           C  
ANISOU 1380  CG2 VAL B 162     2453   2824   1808    701    149    149       C  
ATOM   1381  N   SER B 163     -10.614 -23.231 -23.283  1.00 16.65           N  
ANISOU 1381  N   SER B 163     2165   2435   1726    502     59     32       N  
ATOM   1382  CA  SER B 163     -10.618 -23.424 -21.824  1.00 16.04           C  
ANISOU 1382  CA  SER B 163     2094   2311   1688    460     42     18       C  
ATOM   1383  C   SER B 163      -9.985 -22.240 -21.106  1.00 16.48           C  
ANISOU 1383  C   SER B 163     2193   2305   1763    434     65     48       C  
ATOM   1384  O   SER B 163      -8.999 -21.682 -21.580  1.00 16.89           O  
ANISOU 1384  O   SER B 163     2258   2340   1818    420     90     72       O  
ATOM   1385  CB  SER B 163      -9.826 -24.691 -21.454  1.00 15.75           C  
ANISOU 1385  CB  SER B 163     2024   2272   1686    420     22    -13       C  
ATOM   1386  OG  SER B 163      -9.786 -24.867 -20.034  1.00 15.45           O  
ANISOU 1386  OG  SER B 163     1991   2195   1681    385      8    -21       O  
ATOM   1387  N   GLY B 164     -10.518 -21.880 -19.936  1.00 16.20           N  
ANISOU 1387  N   GLY B 164     2180   2236   1740    423     58     45       N  
ATOM   1388  CA  GLY B 164      -9.792 -20.969 -19.068  1.00 16.83           C  
ANISOU 1388  CA  GLY B 164     2296   2255   1843    383     74     58       C  
ATOM   1389  C   GLY B 164      -8.607 -21.688 -18.442  1.00 17.09           C  
ANISOU 1389  C   GLY B 164     2300   2282   1911    328     57     38       C  
ATOM   1390  O   GLY B 164      -8.580 -22.930 -18.378  1.00 17.07           O  
ANISOU 1390  O   GLY B 164     2257   2310   1918    325     32     15       O  
ATOM   1391  N   ILE B 165      -7.596 -20.930 -18.025  1.00 16.69           N  
ANISOU 1391  N   ILE B 165     2269   2194   1879    284     74     48       N  
ATOM   1392  CA  ILE B 165      -6.561 -21.502 -17.156  1.00 16.78           C  
ANISOU 1392  CA  ILE B 165     2251   2206   1918    234     56     29       C  
ATOM   1393  C   ILE B 165      -7.073 -21.275 -15.743  1.00 16.43           C  
ANISOU 1393  C   ILE B 165     2225   2136   1882    220     40     12       C  
ATOM   1394  O   ILE B 165      -7.028 -20.143 -15.237  1.00 17.04           O  
ANISOU 1394  O   ILE B 165     2343   2169   1959    200     57     16       O  
ATOM   1395  CB  ILE B 165      -5.184 -20.840 -17.337  1.00 16.52           C  
ANISOU 1395  CB  ILE B 165     2218   2159   1898    186     78     41       C  
ATOM   1396  CG1 ILE B 165      -4.721 -20.954 -18.791  1.00 18.05           C  
ANISOU 1396  CG1 ILE B 165     2397   2381   2079    206    100     63       C  
ATOM   1397  CG2 ILE B 165      -4.140 -21.459 -16.376  1.00 18.75           C  
ANISOU 1397  CG2 ILE B 165     2461   2459   2202    140     56     20       C  
ATOM   1398  CD1 ILE B 165      -3.333 -20.351 -19.040  1.00 18.06           C  
ANISOU 1398  CD1 ILE B 165     2392   2376   2094    156    126     79       C  
ATOM   1399  N   ALA B 166      -7.583 -22.340 -15.129  1.00 14.87           N  
ANISOU 1399  N   ALA B 166     2000   1961   1688    232     11     -5       N  
ATOM   1400  CA  ALA B 166      -8.229 -22.232 -13.809  1.00 15.47           C  
ANISOU 1400  CA  ALA B 166     2090   2021   1765    229     -3    -18       C  
ATOM   1401  C   ALA B 166      -7.175 -22.354 -12.730  1.00 15.44           C  
ANISOU 1401  C   ALA B 166     2071   2017   1779    183    -16    -31       C  
ATOM   1402  O   ALA B 166      -6.506 -23.380 -12.624  1.00 15.18           O  
ANISOU 1402  O   ALA B 166     1996   2014   1757    175    -31    -36       O  
ATOM   1403  CB  ALA B 166      -9.298 -23.293 -13.638  1.00 14.37           C  
ANISOU 1403  CB  ALA B 166     1927   1907   1622    261    -23    -27       C  
ATOM   1404  N   GLN B 167      -7.036 -21.306 -11.923  1.00 16.17           N  
ANISOU 1404  N   GLN B 167     2196   2077   1870    157     -9    -38       N  
ATOM   1405  CA  GLN B 167      -5.984 -21.270 -10.911  1.00 16.57           C  
ANISOU 1405  CA  GLN B 167     2229   2136   1929    109    -22    -56       C  
ATOM   1406  C   GLN B 167      -6.459 -20.431  -9.727  1.00 17.77           C  
ANISOU 1406  C   GLN B 167     2419   2260   2072     98    -24    -74       C  
ATOM   1407  O   GLN B 167      -7.348 -19.595  -9.863  1.00 17.70           O  
ANISOU 1407  O   GLN B 167     2459   2212   2054    121     -7    -69       O  
ATOM   1408  CB  GLN B 167      -4.656 -20.725 -11.507  1.00 16.57           C  
ANISOU 1408  CB  GLN B 167     2220   2136   1939     62     -4    -54       C  
ATOM   1409  CG  GLN B 167      -3.431 -20.653 -10.541  1.00 18.63           C  
ANISOU 1409  CG  GLN B 167     2450   2422   2205      5    -19    -76       C  
ATOM   1410  CD  GLN B 167      -3.001 -22.022  -9.984  1.00 19.69           C  
ANISOU 1410  CD  GLN B 167     2526   2616   2338     20    -49    -78       C  
ATOM   1411  OE1 GLN B 167      -3.789 -22.720  -9.333  1.00 18.64           O  
ANISOU 1411  OE1 GLN B 167     2391   2489   2200     56    -66    -79       O  
ATOM   1412  NE2 GLN B 167      -1.747 -22.401 -10.231  1.00 18.70           N  
ANISOU 1412  NE2 GLN B 167     2354   2534   2217     -3    -51    -76       N  
ATOM   1413  N   THR B 168      -5.888 -20.698  -8.561  1.00 18.66           N  
ANISOU 1413  N   THR B 168     2508   2397   2184     72    -46    -95       N  
ATOM   1414  CA  THR B 168      -6.093 -19.833  -7.399  1.00 20.24           C  
ANISOU 1414  CA  THR B 168     2742   2575   2372     53    -49   -120       C  
ATOM   1415  C   THR B 168      -4.771 -19.722  -6.628  1.00 21.75           C  
ANISOU 1415  C   THR B 168     2902   2796   2563     -4    -63   -147       C  
ATOM   1416  O   THR B 168      -3.854 -20.517  -6.844  1.00 21.04           O  
ANISOU 1416  O   THR B 168     2759   2755   2480    -16    -75   -140       O  
ATOM   1417  CB  THR B 168      -7.252 -20.363  -6.515  1.00 19.91           C  
ANISOU 1417  CB  THR B 168     2703   2545   2316     99    -66   -120       C  
ATOM   1418  OG1 THR B 168      -7.631 -19.366  -5.555  1.00 21.52           O  
ANISOU 1418  OG1 THR B 168     2951   2720   2503     91    -62   -143       O  
ATOM   1419  CG2 THR B 168      -6.885 -21.681  -5.814  1.00 18.05           C  
ANISOU 1419  CG2 THR B 168     2411   2367   2080    106    -93   -117       C  
ATOM   1420  N   ASN B 169      -4.666 -18.747  -5.730  1.00 24.29           N  
ANISOU 1420  N   ASN B 169     3255   3097   2875    -39    -62   -180       N  
ATOM   1421  CA  ASN B 169      -3.450 -18.629  -4.915  1.00 26.38           C  
ANISOU 1421  CA  ASN B 169     3484   3405   3134    -97    -80   -214       C  
ATOM   1422  C   ASN B 169      -3.246 -19.823  -3.991  1.00 26.92           C  
ANISOU 1422  C   ASN B 169     3494   3549   3185    -72   -115   -212       C  
ATOM   1423  O   ASN B 169      -4.208 -20.351  -3.415  1.00 25.93           O  
ANISOU 1423  O   ASN B 169     3376   3428   3048    -21   -126   -201       O  
ATOM   1424  CB  ASN B 169      -3.472 -17.340  -4.089  1.00 27.68           C  
ANISOU 1424  CB  ASN B 169     3698   3528   3288   -141    -72   -259       C  
ATOM   1425  CG  ASN B 169      -3.352 -16.094  -4.945  1.00 30.38           C  
ANISOU 1425  CG  ASN B 169     4098   3793   3650   -179    -30   -262       C  
ATOM   1426  OD1 ASN B 169      -3.004 -16.154  -6.129  1.00 33.64           O  
ANISOU 1426  OD1 ASN B 169     4504   4195   4083   -184     -9   -231       O  
ATOM   1427  ND2 ASN B 169      -3.640 -14.952  -4.344  1.00 33.94           N  
ANISOU 1427  ND2 ASN B 169     4611   4187   4095   -204    -14   -297       N  
ATOM   1428  N   ALA B 170      -1.989 -20.252  -3.861  1.00 28.06           N  
ANISOU 1428  N   ALA B 170     3579   3756   3327   -104   -130   -219       N  
ATOM   1429  CA  ALA B 170      -1.626 -21.307  -2.923  1.00 30.01           C  
ANISOU 1429  CA  ALA B 170     3769   4079   3551    -78   -160   -215       C  
ATOM   1430  C   ALA B 170      -1.814 -20.784  -1.492  1.00 31.88           C  
ANISOU 1430  C   ALA B 170     4018   4335   3758    -90   -179   -253       C  
ATOM   1431  O   ALA B 170      -1.622 -19.594  -1.236  1.00 32.49           O  
ANISOU 1431  O   ALA B 170     4127   4384   3831   -144   -172   -295       O  
ATOM   1432  CB  ALA B 170      -0.188 -21.755  -3.157  1.00 29.86           C  
ANISOU 1432  CB  ALA B 170     3683   4130   3531   -106   -169   -213       C  
ATOM   1433  N   GLU B 171      -2.193 -21.675  -0.577  1.00 33.67           N  
ANISOU 1433  N   GLU B 171     4221   4608   3962    -39   -198   -238       N  
ATOM   1434  CA  GLU B 171      -2.581 -21.299   0.795  1.00 36.25           C  
ANISOU 1434  CA  GLU B 171     4561   4956   4254    -34   -215   -268       C  
ATOM   1435  C   GLU B 171      -1.482 -20.573   1.576  1.00 37.45           C  
ANISOU 1435  C   GLU B 171     4687   5162   4379    -96   -234   -323       C  
ATOM   1436  O   GLU B 171      -1.721 -19.510   2.171  1.00 38.97           O  
ANISOU 1436  O   GLU B 171     4922   5328   4557   -130   -233   -370       O  
ATOM   1437  CB  GLU B 171      -3.050 -22.536   1.575  1.00 36.26           C  
ANISOU 1437  CB  GLU B 171     4534   5006   4236     34   -229   -233       C  
ATOM   1438  CG  GLU B 171      -2.000 -23.637   1.623  1.00 39.81           C  
ANISOU 1438  CG  GLU B 171     4913   5534   4679     50   -242   -207       C  
ATOM   1439  CD  GLU B 171      -2.313 -24.738   2.621  1.00 43.99           C  
ANISOU 1439  CD  GLU B 171     5416   6116   5182    116   -253   -174       C  
ATOM   1440  OE1 GLU B 171      -3.393 -24.720   3.257  1.00 45.67           O  
ANISOU 1440  OE1 GLU B 171     5661   6306   5384    148   -250   -168       O  
ATOM   1441  OE2 GLU B 171      -1.451 -25.626   2.773  1.00 45.96           O  
ANISOU 1441  OE2 GLU B 171     5611   6431   5419    139   -261   -150       O  
TER    1442      GLU B 171                                                      
ATOM   1443  N   ARG E   1     -44.218 -31.183 -24.373  1.00 60.24           N  
ANISOU 1443  N   ARG E   1     5211   7808   9868   1109  -1945   -610       N  
ATOM   1444  CA  ARG E   1     -44.255 -32.617 -23.962  1.00 58.58           C  
ANISOU 1444  CA  ARG E   1     5090   7874   9292    959  -1741   -607       C  
ATOM   1445  C   ARG E   1     -44.088 -32.880 -22.451  1.00 57.98           C  
ANISOU 1445  C   ARG E   1     4894   8044   9092    958  -1412   -869       C  
ATOM   1446  O   ARG E   1     -44.807 -33.730 -21.908  1.00 58.84           O  
ANISOU 1446  O   ARG E   1     4862   8387   9104    855  -1296   -914       O  
ATOM   1447  CB  ARG E   1     -43.235 -33.446 -24.763  1.00 56.30           C  
ANISOU 1447  CB  ARG E   1     5184   7582   8622    809  -1779   -389       C  
ATOM   1448  CG  ARG E   1     -43.137 -34.907 -24.326  1.00 54.97           C  
ANISOU 1448  CG  ARG E   1     5111   7622   8150    665  -1618   -385       C  
ATOM   1449  CD  ARG E   1     -42.212 -35.727 -25.212  1.00 53.78           C  
ANISOU 1449  CD  ARG E   1     5286   7435   7709    542  -1678   -236       C  
ATOM   1450  NE  ARG E   1     -42.572 -37.144 -25.158  1.00 53.86           N  
ANISOU 1450  NE  ARG E   1     5331   7563   7570    402  -1659   -195       N  
ATOM   1451  CZ  ARG E   1     -43.313 -37.768 -26.070  1.00 55.47           C  
ANISOU 1451  CZ  ARG E   1     5550   7758   7768    305  -1834    -79       C  
ATOM   1452  NH1 ARG E   1     -43.769 -37.112 -27.134  1.00 56.45           N  
ANISOU 1452  NH1 ARG E   1     5665   7783   7999    311  -2046     29       N  
ATOM   1453  NH2 ARG E   1     -43.590 -39.058 -25.925  1.00 56.24           N  
ANISOU 1453  NH2 ARG E   1     5673   7935   7759    177  -1828    -53       N  
ATOM   1454  N   PRO E   2     -43.197 -32.138 -21.746  1.00 57.04           N  
ANISOU 1454  N   PRO E   2     4811   7894   8968   1040  -1276  -1032       N  
ATOM   1455  CA  PRO E   2     -42.492 -30.848 -21.937  1.00 56.87           C  
ANISOU 1455  CA  PRO E   2     4837   7619   9150   1184  -1371  -1077       C  
ATOM   1456  C   PRO E   2     -41.627 -30.708 -23.188  1.00 54.96           C  
ANISOU 1456  C   PRO E   2     4909   7167   8804   1137  -1593   -779       C  
ATOM   1457  O   PRO E   2     -40.982 -31.668 -23.614  1.00 52.65           O  
ANISOU 1457  O   PRO E   2     4877   6962   8163    997  -1559   -616       O  
ATOM   1458  CB  PRO E   2     -41.604 -30.740 -20.692  1.00 55.87           C  
ANISOU 1458  CB  PRO E   2     4748   7642   8837   1179  -1096  -1291       C  
ATOM   1459  CG  PRO E   2     -42.153 -31.711 -19.720  1.00 56.54           C  
ANISOU 1459  CG  PRO E   2     4695   8073   8715   1047   -868  -1408       C  
ATOM   1460  CD  PRO E   2     -42.713 -32.823 -20.535  1.00 55.84           C  
ANISOU 1460  CD  PRO E   2     4688   8017   8511    927   -994  -1154       C  
ATOM   1461  N   ASP E   3     -41.618 -29.499 -23.748  1.00 55.92           N  
ANISOU 1461  N   ASP E   3     4980   7020   9247   1239  -1828   -725       N  
ATOM   1462  CA  ASP E   3     -40.877 -29.179 -24.970  1.00 55.03           C  
ANISOU 1462  CA  ASP E   3     5123   6740   9043   1149  -2071   -423       C  
ATOM   1463  C   ASP E   3     -39.368 -29.411 -24.863  1.00 51.91           C  
ANISOU 1463  C   ASP E   3     5026   6416   8281   1072  -1916   -384       C  
ATOM   1464  O   ASP E   3     -38.711 -29.682 -25.873  1.00 50.88           O  
ANISOU 1464  O   ASP E   3     5132   6291   7906    929  -2023   -156       O  
ATOM   1465  CB  ASP E   3     -41.148 -27.731 -25.394  1.00 58.11           C  
ANISOU 1465  CB  ASP E   3     5366   6811   9903   1255  -2383   -360       C  
ATOM   1466  CG  ASP E   3     -42.489 -27.565 -26.097  1.00 61.85           C  
ANISOU 1466  CG  ASP E   3     5616   7158  10723   1266  -2675   -239       C  
ATOM   1467  OD1 ASP E   3     -42.723 -28.255 -27.113  1.00 62.52           O  
ANISOU 1467  OD1 ASP E   3     5845   7320  10590   1091  -2819     27       O  
ATOM   1468  OD2 ASP E   3     -43.303 -26.730 -25.645  1.00 65.91           O  
ANISOU 1468  OD2 ASP E   3     5798   7494  11749   1447  -2772   -429       O  
ATOM   1469  N   PHE E   4     -38.821 -29.300 -23.653  1.00 50.35           N  
ANISOU 1469  N   PHE E   4     4797   6294   8039   1148  -1665   -617       N  
ATOM   1470  CA  PHE E   4     -37.382 -29.535 -23.453  1.00 47.55           C  
ANISOU 1470  CA  PHE E   4     4696   6001   7369   1081  -1521   -585       C  
ATOM   1471  C   PHE E   4     -36.977 -30.989 -23.706  1.00 45.40           C  
ANISOU 1471  C   PHE E   4     4612   5917   6719    935  -1403   -495       C  
ATOM   1472  O   PHE E   4     -35.798 -31.275 -23.927  1.00 43.57           O  
ANISOU 1472  O   PHE E   4     4592   5710   6251    865  -1344   -428       O  
ATOM   1473  CB  PHE E   4     -36.895 -29.035 -22.082  1.00 47.23           C  
ANISOU 1473  CB  PHE E   4     4574   5996   7372   1172  -1309   -844       C  
ATOM   1474  CG  PHE E   4     -37.391 -29.840 -20.906  1.00 46.56           C  
ANISOU 1474  CG  PHE E   4     4351   6168   7170   1145  -1057  -1049       C  
ATOM   1475  CD1 PHE E   4     -36.921 -31.132 -20.667  1.00 44.33           C  
ANISOU 1475  CD1 PHE E   4     4221   6076   6544   1001   -919   -966       C  
ATOM   1476  CD2 PHE E   4     -38.292 -29.281 -20.004  1.00 48.50           C  
ANISOU 1476  CD2 PHE E   4     4292   6472   7663   1242   -969  -1336       C  
ATOM   1477  CE1 PHE E   4     -37.367 -31.870 -19.569  1.00 44.36           C  
ANISOU 1477  CE1 PHE E   4     4098   6329   6427    919   -731  -1094       C  
ATOM   1478  CE2 PHE E   4     -38.743 -30.006 -18.901  1.00 48.83           C  
ANISOU 1478  CE2 PHE E   4     4193   6821   7539   1155   -731  -1512       C  
ATOM   1479  CZ  PHE E   4     -38.279 -31.302 -18.681  1.00 46.57           C  
ANISOU 1479  CZ  PHE E   4     4082   6729   6882    975   -627  -1357       C  
ATOM   1480  N   CYS E   5     -37.963 -31.891 -23.682  1.00 45.54           N  
ANISOU 1480  N   CYS E   5     4531   6051   6720    892  -1385   -506       N  
ATOM   1481  CA  CYS E   5     -37.752 -33.311 -23.976  1.00 44.18           C  
ANISOU 1481  CA  CYS E   5     4505   6008   6272    758  -1329   -430       C  
ATOM   1482  C   CYS E   5     -37.397 -33.523 -25.445  1.00 43.72           C  
ANISOU 1482  C   CYS E   5     4636   5898   6076    656  -1499   -253       C  
ATOM   1483  O   CYS E   5     -36.828 -34.554 -25.815  1.00 42.39           O  
ANISOU 1483  O   CYS E   5     4621   5803   5681    556  -1449   -238       O  
ATOM   1484  CB  CYS E   5     -39.000 -34.130 -23.625  1.00 45.16           C  
ANISOU 1484  CB  CYS E   5     4457   6255   6446    719  -1309   -465       C  
ATOM   1485  SG  CYS E   5     -39.480 -34.098 -21.874  1.00 47.05           S  
ANISOU 1485  SG  CYS E   5     4448   6683   6744    747  -1075   -689       S  
ATOM   1486  N   LEU E   6     -37.726 -32.533 -26.270  1.00 44.85           N  
ANISOU 1486  N   LEU E   6     4750   5921   6370    664  -1713   -129       N  
ATOM   1487  CA  LEU E   6     -37.513 -32.605 -27.714  1.00 45.48           C  
ANISOU 1487  CA  LEU E   6     4984   6007   6286    507  -1901     61       C  
ATOM   1488  C   LEU E   6     -36.193 -31.967 -28.156  1.00 44.89           C  
ANISOU 1488  C   LEU E   6     5080   5919   6056    444  -1909    134       C  
ATOM   1489  O   LEU E   6     -35.830 -32.039 -29.332  1.00 45.87           O  
ANISOU 1489  O   LEU E   6     5338   6121   5967    265  -2028    274       O  
ATOM   1490  CB  LEU E   6     -38.703 -31.974 -28.459  1.00 48.00           C  
ANISOU 1490  CB  LEU E   6     5168   6224   6844    483  -2193    225       C  
ATOM   1491  CG  LEU E   6     -40.062 -32.663 -28.261  1.00 49.33           C  
ANISOU 1491  CG  LEU E   6     5162   6433   7147    508  -2215    181       C  
ATOM   1492  CD1 LEU E   6     -41.199 -31.645 -28.212  1.00 53.09           C  
ANISOU 1492  CD1 LEU E   6     5374   6740   8055    617  -2427    227       C  
ATOM   1493  CD2 LEU E   6     -40.328 -33.707 -29.342  1.00 50.38           C  
ANISOU 1493  CD2 LEU E   6     5425   6685   7030    315  -2311    291       C  
ATOM   1494  N   GLU E   7     -35.469 -31.360 -27.214  1.00 43.46           N  
ANISOU 1494  N   GLU E   7     4885   5671   5954    562  -1778     35       N  
ATOM   1495  CA  GLU E   7     -34.208 -30.691 -27.536  1.00 42.58           C  
ANISOU 1495  CA  GLU E   7     4915   5544   5718    501  -1787    112       C  
ATOM   1496  C   GLU E   7     -33.041 -31.693 -27.464  1.00 39.47           C  
ANISOU 1496  C   GLU E   7     4674   5307   5016    440  -1562      7       C  
ATOM   1497  O   GLU E   7     -33.035 -32.578 -26.599  1.00 38.29           O  
ANISOU 1497  O   GLU E   7     4496   5198   4853    510  -1383   -146       O  
ATOM   1498  CB  GLU E   7     -33.997 -29.447 -26.645  1.00 43.38           C  
ANISOU 1498  CB  GLU E   7     4921   5468   6092    649  -1798     60       C  
ATOM   1499  CG  GLU E   7     -33.072 -29.636 -25.457  1.00 43.58           C  
ANISOU 1499  CG  GLU E   7     4982   5538   6039    734  -1536   -124       C  
ATOM   1500  CD  GLU E   7     -33.473 -28.848 -24.209  1.00 46.84           C  
ANISOU 1500  CD  GLU E   7     5218   5838   6741    904  -1479   -307       C  
ATOM   1501  OE1 GLU E   7     -33.911 -27.675 -24.329  1.00 49.75           O  
ANISOU 1501  OE1 GLU E   7     5471   6011   7421    978  -1673   -281       O  
ATOM   1502  OE2 GLU E   7     -33.332 -29.414 -23.099  1.00 44.67           O  
ANISOU 1502  OE2 GLU E   7     4907   5675   6387    946  -1252   -486       O  
ATOM   1503  N   PRO E   8     -32.071 -31.578 -28.393  1.00 38.44           N  
ANISOU 1503  N   PRO E   8     4681   5271   4650    287  -1590     93       N  
ATOM   1504  CA  PRO E   8     -30.933 -32.497 -28.424  1.00 36.33           C  
ANISOU 1504  CA  PRO E   8     4515   5142   4143    238  -1388    -45       C  
ATOM   1505  C   PRO E   8     -30.122 -32.415 -27.125  1.00 33.43           C  
ANISOU 1505  C   PRO E   8     4135   4702   3862    379  -1208   -160       C  
ATOM   1506  O   PRO E   8     -30.135 -31.372 -26.465  1.00 33.46           O  
ANISOU 1506  O   PRO E   8     4092   4585   4033    468  -1244   -118       O  
ATOM   1507  CB  PRO E   8     -30.102 -31.988 -29.610  1.00 37.75           C  
ANISOU 1507  CB  PRO E   8     4797   5461   4083     34  -1464     74       C  
ATOM   1508  CG  PRO E   8     -30.537 -30.569 -29.807  1.00 39.82           C  
ANISOU 1508  CG  PRO E   8     5025   5591   4512      7  -1709    316       C  
ATOM   1509  CD  PRO E   8     -31.982 -30.561 -29.459  1.00 40.28           C  
ANISOU 1509  CD  PRO E   8     4958   5501   4843    128  -1827    329       C  
ATOM   1510  N   PRO E   9     -29.428 -33.508 -26.752  1.00 31.46           N  
ANISOU 1510  N   PRO E   9     3916   4511   3524    392  -1040   -309       N  
ATOM   1511  CA  PRO E   9     -28.680 -33.464 -25.492  1.00 29.05           C  
ANISOU 1511  CA  PRO E   9     3597   4145   3296    491   -904   -379       C  
ATOM   1512  C   PRO E   9     -27.551 -32.436 -25.566  1.00 28.01           C  
ANISOU 1512  C   PRO E   9     3524   4005   3112    471   -891   -320       C  
ATOM   1513  O   PRO E   9     -27.039 -32.174 -26.651  1.00 29.51           O  
ANISOU 1513  O   PRO E   9     3775   4290   3144    348   -939   -257       O  
ATOM   1514  CB  PRO E   9     -28.114 -34.886 -25.371  1.00 28.43           C  
ANISOU 1514  CB  PRO E   9     3531   4104   3165    474   -800   -510       C  
ATOM   1515  CG  PRO E   9     -28.034 -35.391 -26.766  1.00 30.37           C  
ANISOU 1515  CG  PRO E   9     3822   4459   3257    361   -837   -560       C  
ATOM   1516  CD  PRO E   9     -29.165 -34.746 -27.513  1.00 31.54           C  
ANISOU 1516  CD  PRO E   9     3967   4633   3382    302   -993   -424       C  
ATOM   1517  N   TYR E  10     -27.161 -31.869 -24.427  1.00 25.95           N  
ANISOU 1517  N   TYR E  10     3241   3661   2958    559   -829   -339       N  
ATOM   1518  CA  TYR E  10     -26.217 -30.756 -24.421  1.00 24.93           C  
ANISOU 1518  CA  TYR E  10     3159   3493   2818    541   -850   -265       C  
ATOM   1519  C   TYR E  10     -25.051 -31.079 -23.499  1.00 22.95           C  
ANISOU 1519  C   TYR E  10     2929   3249   2541    569   -702   -343       C  
ATOM   1520  O   TYR E  10     -25.232 -31.174 -22.289  1.00 21.76           O  
ANISOU 1520  O   TYR E  10     2732   3052   2481    638   -639   -409       O  
ATOM   1521  CB  TYR E  10     -26.932 -29.477 -23.969  1.00 26.09           C  
ANISOU 1521  CB  TYR E  10     3243   3490   3178    619   -973   -219       C  
ATOM   1522  CG  TYR E  10     -26.078 -28.224 -23.896  1.00 27.20           C  
ANISOU 1522  CG  TYR E  10     3425   3538   3370    602  -1045   -133       C  
ATOM   1523  CD1 TYR E  10     -25.609 -27.605 -25.054  1.00 29.22           C  
ANISOU 1523  CD1 TYR E  10     3749   3819   3532    459  -1192     57       C  
ATOM   1524  CD2 TYR E  10     -25.758 -27.648 -22.666  1.00 26.55           C  
ANISOU 1524  CD2 TYR E  10     3310   3362   3415    696   -979   -235       C  
ATOM   1525  CE1 TYR E  10     -24.823 -26.450 -24.986  1.00 30.98           C  
ANISOU 1525  CE1 TYR E  10     4007   3947   3815    417  -1289    170       C  
ATOM   1526  CE2 TYR E  10     -24.985 -26.482 -22.589  1.00 27.99           C  
ANISOU 1526  CE2 TYR E  10     3530   3433   3670    677  -1068   -159       C  
ATOM   1527  CZ  TYR E  10     -24.524 -25.895 -23.756  1.00 29.69           C  
ANISOU 1527  CZ  TYR E  10     3813   3646   3819    542  -1232     56       C  
ATOM   1528  OH  TYR E  10     -23.755 -24.760 -23.682  1.00 31.62           O  
ANISOU 1528  OH  TYR E  10     4094   3775   4145    499  -1346    162       O  
ATOM   1529  N   THR E  11     -23.871 -31.269 -24.083  1.00 22.25           N  
ANISOU 1529  N   THR E  11     2893   3243   2318    491   -649   -338       N  
ATOM   1530  CA  THR E  11     -22.666 -31.577 -23.296  1.00 20.63           C  
ANISOU 1530  CA  THR E  11     2689   3030   2119    512   -534   -394       C  
ATOM   1531  C   THR E  11     -22.216 -30.378 -22.453  1.00 19.85           C  
ANISOU 1531  C   THR E  11     2611   2843   2088    541   -553   -329       C  
ATOM   1532  O   THR E  11     -21.827 -30.531 -21.285  1.00 18.94           O  
ANISOU 1532  O   THR E  11     2479   2685   2029    579   -488   -373       O  
ATOM   1533  CB  THR E  11     -21.512 -32.101 -24.190  1.00 21.64           C  
ANISOU 1533  CB  THR E  11     2820   3284   2117    427   -461   -453       C  
ATOM   1534  OG1 THR E  11     -21.933 -33.302 -24.841  1.00 22.07           O  
ANISOU 1534  OG1 THR E  11     2838   3400   2144    413   -438   -579       O  
ATOM   1535  CG2 THR E  11     -20.262 -32.419 -23.347  1.00 20.64           C  
ANISOU 1535  CG2 THR E  11     2664   3119   2057    460   -369   -503       C  
ATOM   1536  N   GLY E  12     -22.284 -29.188 -23.044  1.00 20.28           N  
ANISOU 1536  N   GLY E  12     2697   2864   2144    499   -670   -215       N  
ATOM   1537  CA  GLY E  12     -21.916 -27.963 -22.354  1.00 20.68           C  
ANISOU 1537  CA  GLY E  12     2761   2792   2302    526   -727   -167       C  
ATOM   1538  C   GLY E  12     -20.435 -27.644 -22.445  1.00 20.02           C  
ANISOU 1538  C   GLY E  12     2726   2756   2123    443   -689   -100       C  
ATOM   1539  O   GLY E  12     -19.676 -28.379 -23.101  1.00 20.88           O  
ANISOU 1539  O   GLY E  12     2835   3013   2083    366   -602   -112       O  
ATOM   1540  N   PRO E  13     -20.020 -26.549 -21.798  1.00 19.92           N  
ANISOU 1540  N   PRO E  13     2733   2622   2211    455   -752    -56       N  
ATOM   1541  CA  PRO E  13     -18.675 -25.995 -21.950  1.00 19.40           C  
ANISOU 1541  CA  PRO E  13     2710   2587   2073    356   -759     48       C  
ATOM   1542  C   PRO E  13     -17.614 -26.521 -20.968  1.00 17.89           C  
ANISOU 1542  C   PRO E  13     2512   2426   1859    376   -616    -29       C  
ATOM   1543  O   PRO E  13     -16.513 -25.972 -20.931  1.00 17.47           O  
ANISOU 1543  O   PRO E  13     2481   2381   1775    302   -628     53       O  
ATOM   1544  CB  PRO E  13     -18.908 -24.498 -21.729  1.00 21.14           C  
ANISOU 1544  CB  PRO E  13     2949   2609   2471    360   -951    137       C  
ATOM   1545  CG  PRO E  13     -19.996 -24.460 -20.687  1.00 21.05           C  
ANISOU 1545  CG  PRO E  13     2880   2470   2644    517   -935    -48       C  
ATOM   1546  CD  PRO E  13     -20.883 -25.659 -20.984  1.00 20.15           C  
ANISOU 1546  CD  PRO E  13     2727   2473   2455    557   -843   -123       C  
ATOM   1547  N   CYS E  14     -17.932 -27.552 -20.178  1.00 16.31           N  
ANISOU 1547  N   CYS E  14     2274   2239   1681    450   -512   -155       N  
ATOM   1548  CA  CYS E  14     -16.924 -28.147 -19.290  1.00 15.91           C  
ANISOU 1548  CA  CYS E  14     2205   2207   1629    438   -426   -182       C  
ATOM   1549  C   CYS E  14     -16.528 -29.524 -19.785  1.00 15.35           C  
ANISOU 1549  C   CYS E  14     2073   2224   1535    433   -347   -235       C  
ATOM   1550  O   CYS E  14     -17.270 -30.151 -20.565  1.00 16.42           O  
ANISOU 1550  O   CYS E  14     2186   2408   1642    451   -338   -290       O  
ATOM   1551  CB  CYS E  14     -17.385 -28.185 -17.825  1.00 15.66           C  
ANISOU 1551  CB  CYS E  14     2167   2125   1655    467   -412   -252       C  
ATOM   1552  SG  CYS E  14     -17.532 -26.550 -17.089  1.00 18.51           S  
ANISOU 1552  SG  CYS E  14     2567   2376   2088    476   -488   -284       S  
ATOM   1553  N   LYS E  15     -15.359 -29.987 -19.350  1.00 15.07           N  
ANISOU 1553  N   LYS E  15     1993   2192   1541    409   -306   -232       N  
ATOM   1554  CA  LYS E  15     -14.735 -31.170 -19.945  1.00 15.66           C  
ANISOU 1554  CA  LYS E  15     1965   2319   1663    414   -246   -322       C  
ATOM   1555  C   LYS E  15     -14.695 -32.399 -19.033  1.00 15.53           C  
ANISOU 1555  C   LYS E  15     1880   2205   1814    447   -274   -352       C  
ATOM   1556  O   LYS E  15     -13.796 -33.234 -19.155  1.00 15.14           O  
ANISOU 1556  O   LYS E  15     1719   2128   1905    458   -265   -414       O  
ATOM   1557  CB  LYS E  15     -13.326 -30.824 -20.475  1.00 16.11           C  
ANISOU 1557  CB  LYS E  15     1965   2465   1689    353   -194   -314       C  
ATOM   1558  CG  LYS E  15     -13.342 -29.956 -21.733  1.00 17.48           C  
ANISOU 1558  CG  LYS E  15     2173   2795   1673    260   -180   -276       C  
ATOM   1559  CD  LYS E  15     -13.797 -30.784 -22.935  1.00 19.43           C  
ANISOU 1559  CD  LYS E  15     2359   3185   1838    244   -115   -427       C  
ATOM   1560  CE  LYS E  15     -13.760 -29.991 -24.229  1.00 20.17           C  
ANISOU 1560  CE  LYS E  15     2477   3494   1691     82   -116   -360       C  
ATOM   1561  NZ  LYS E  15     -14.173 -30.880 -25.363  1.00 20.94           N  
ANISOU 1561  NZ  LYS E  15     2508   3770   1677     38    -41   -543       N  
ATOM   1562  N   ALA E  16     -15.651 -32.516 -18.115  1.00 15.03           N  
ANISOU 1562  N   ALA E  16     1861   2093   1755    444   -326   -306       N  
ATOM   1563  CA  ALA E  16     -15.794 -33.778 -17.386  1.00 15.47           C  
ANISOU 1563  CA  ALA E  16     1850   2074   1953    425   -395   -288       C  
ATOM   1564  C   ALA E  16     -16.525 -34.792 -18.272  1.00 16.11           C  
ANISOU 1564  C   ALA E  16     1880   2143   2097    479   -398   -399       C  
ATOM   1565  O   ALA E  16     -17.042 -34.445 -19.329  1.00 17.76           O  
ANISOU 1565  O   ALA E  16     2120   2429   2198    515   -339   -481       O  
ATOM   1566  CB  ALA E  16     -16.534 -33.578 -16.050  1.00 15.67           C  
ANISOU 1566  CB  ALA E  16     1922   2121   1909    342   -442   -196       C  
ATOM   1567  N   ARG E  17     -16.558 -36.043 -17.849  1.00 17.20           N  
ANISOU 1567  N   ARG E  17     1937   2175   2422    462   -496   -386       N  
ATOM   1568  CA  ARG E  17     -17.265 -37.062 -18.605  1.00 18.13           C  
ANISOU 1568  CA  ARG E  17     2004   2252   2632    506   -524   -502       C  
ATOM   1569  C   ARG E  17     -18.274 -37.699 -17.672  1.00 18.87           C  
ANISOU 1569  C   ARG E  17     2104   2305   2758    426   -641   -372       C  
ATOM   1570  O   ARG E  17     -17.947 -38.582 -16.885  1.00 20.14           O  
ANISOU 1570  O   ARG E  17     2196   2345   3109    352   -789   -262       O  
ATOM   1571  CB  ARG E  17     -16.298 -38.107 -19.180  1.00 19.63           C  
ANISOU 1571  CB  ARG E  17     2047   2322   3089    563   -559   -655       C  
ATOM   1572  CG  ARG E  17     -16.971 -39.049 -20.209  1.00 22.11           C  
ANISOU 1572  CG  ARG E  17     2306   2609   3484    616   -566   -853       C  
ATOM   1573  CD  ARG E  17     -16.018 -40.154 -20.669  1.00 26.30           C  
ANISOU 1573  CD  ARG E  17     2649   2991   4353    685   -613  -1072       C  
ATOM   1574  NE  ARG E  17     -16.664 -41.037 -21.651  1.00 32.83           N  
ANISOU 1574  NE  ARG E  17     3421   3794   5256    727   -618  -1308       N  
ATOM   1575  CZ  ARG E  17     -17.339 -42.139 -21.335  1.00 35.81           C  
ANISOU 1575  CZ  ARG E  17     3758   3976   5870    722   -800  -1281       C  
ATOM   1576  NH1 ARG E  17     -17.464 -42.505 -20.063  1.00 37.78           N  
ANISOU 1576  NH1 ARG E  17     4012   4062   6279    649   -995  -1003       N  
ATOM   1577  NH2 ARG E  17     -17.886 -42.885 -22.284  1.00 38.42           N  
ANISOU 1577  NH2 ARG E  17     4043   4289   6266    758   -803  -1521       N  
ATOM   1578  N   ILE E  18     -19.503 -37.231 -17.759  1.00 18.86           N  
ANISOU 1578  N   ILE E  18     2169   2413   2582    420   -593   -370       N  
ATOM   1579  CA  ILE E  18     -20.563 -37.699 -16.883  1.00 20.41           C  
ANISOU 1579  CA  ILE E  18     2354   2643   2754    316   -671   -259       C  
ATOM   1580  C   ILE E  18     -21.664 -38.266 -17.759  1.00 20.71           C  
ANISOU 1580  C   ILE E  18     2380   2682   2807    361   -683   -344       C  
ATOM   1581  O   ILE E  18     -22.316 -37.530 -18.498  1.00 20.96           O  
ANISOU 1581  O   ILE E  18     2456   2800   2706    428   -594   -425       O  
ATOM   1582  CB  ILE E  18     -21.109 -36.553 -16.004  1.00 19.73           C  
ANISOU 1582  CB  ILE E  18     2319   2719   2458    256   -590   -214       C  
ATOM   1583  CG1 ILE E  18     -19.961 -35.904 -15.213  1.00 20.45           C  
ANISOU 1583  CG1 ILE E  18     2437   2814   2518    204   -578   -150       C  
ATOM   1584  CG2 ILE E  18     -22.227 -37.082 -15.077  1.00 21.50           C  
ANISOU 1584  CG2 ILE E  18     2496   3052   2618    107   -644   -125       C  
ATOM   1585  CD1 ILE E  18     -20.253 -34.517 -14.710  1.00 22.26           C  
ANISOU 1585  CD1 ILE E  18     2718   3167   2572    200   -474   -203       C  
ATOM   1586  N   ILE E  19     -21.875 -39.570 -17.671  1.00 22.14           N  
ANISOU 1586  N   ILE E  19     2493   2747   3170    310   -825   -306       N  
ATOM   1587  CA  ILE E  19     -22.910 -40.204 -18.497  1.00 22.86           C  
ANISOU 1587  CA  ILE E  19     2570   2826   3290    338   -858   -389       C  
ATOM   1588  C   ILE E  19     -24.269 -39.873 -17.902  1.00 22.84           C  
ANISOU 1588  C   ILE E  19     2578   2979   3121    252   -842   -289       C  
ATOM   1589  O   ILE E  19     -24.481 -40.016 -16.694  1.00 23.62           O  
ANISOU 1589  O   ILE E  19     2644   3147   3181    104   -897   -131       O  
ATOM   1590  CB  ILE E  19     -22.714 -41.733 -18.604  1.00 24.44           C  
ANISOU 1590  CB  ILE E  19     2680   2813   3790    311  -1048   -396       C  
ATOM   1591  CG1 ILE E  19     -21.252 -42.062 -18.953  1.00 26.54           C  
ANISOU 1591  CG1 ILE E  19     2880   2918   4286    397  -1067   -524       C  
ATOM   1592  CG2 ILE E  19     -23.670 -42.334 -19.638  1.00 24.44           C  
ANISOU 1592  CG2 ILE E  19     2674   2795   3816    351  -1072   -530       C  
ATOM   1593  CD1 ILE E  19     -20.799 -41.535 -20.312  1.00 29.16           C  
ANISOU 1593  CD1 ILE E  19     3225   3334   4519    527   -888   -792       C  
ATOM   1594  N   ARG E  20     -25.160 -39.384 -18.756  1.00 22.41           N  
ANISOU 1594  N   ARG E  20     2550   3004   2960    327   -768   -385       N  
ATOM   1595  CA  ARG E  20     -26.503 -39.005 -18.353  1.00 23.22           C  
ANISOU 1595  CA  ARG E  20     2622   3252   2946    277   -740   -342       C  
ATOM   1596  C   ARG E  20     -27.471 -39.594 -19.367  1.00 23.83           C  
ANISOU 1596  C   ARG E  20     2686   3305   3064    305   -798   -397       C  
ATOM   1597  O   ARG E  20     -27.055 -40.042 -20.435  1.00 22.92           O  
ANISOU 1597  O   ARG E  20     2602   3090   3016    368   -827   -501       O  
ATOM   1598  CB  ARG E  20     -26.630 -37.479 -18.309  1.00 22.01           C  
ANISOU 1598  CB  ARG E  20     2497   3203   2663    353   -611   -403       C  
ATOM   1599  CG  ARG E  20     -25.862 -36.822 -17.163  1.00 23.00           C  
ANISOU 1599  CG  ARG E  20     2630   3382   2727    302   -552   -366       C  
ATOM   1600  CD  ARG E  20     -26.567 -37.108 -15.844  1.00 24.38           C  
ANISOU 1600  CD  ARG E  20     2719   3719   2822    133   -554   -295       C  
ATOM   1601  NE  ARG E  20     -25.846 -36.621 -14.685  1.00 25.66           N  
ANISOU 1601  NE  ARG E  20     2888   3970   2892     30   -511   -261       N  
ATOM   1602  CZ  ARG E  20     -25.884 -35.370 -14.238  1.00 26.63           C  
ANISOU 1602  CZ  ARG E  20     3003   4191   2921     67   -392   -384       C  
ATOM   1603  NH1 ARG E  20     -26.605 -34.440 -14.863  1.00 25.35           N  
ANISOU 1603  NH1 ARG E  20     2816   4019   2794    218   -327   -534       N  
ATOM   1604  NH2 ARG E  20     -25.184 -35.051 -13.165  1.00 27.46           N  
ANISOU 1604  NH2 ARG E  20     3119   4386   2926    -56   -366   -355       N  
ATOM   1605  N   TYR E  21     -28.756 -39.585 -19.031  1.00 25.21           N  
ANISOU 1605  N   TYR E  21     2797   3593   3186    245   -807   -349       N  
ATOM   1606  CA  TYR E  21     -29.785 -39.938 -19.989  1.00 26.93           C  
ANISOU 1606  CA  TYR E  21     3000   3807   3425    269   -862   -390       C  
ATOM   1607  C   TYR E  21     -30.446 -38.695 -20.567  1.00 26.68           C  
ANISOU 1607  C   TYR E  21     2967   3856   3313    365   -788   -451       C  
ATOM   1608  O   TYR E  21     -30.633 -37.697 -19.869  1.00 26.35           O  
ANISOU 1608  O   TYR E  21     2880   3902   3229    388   -704   -462       O  
ATOM   1609  CB  TYR E  21     -30.864 -40.816 -19.335  1.00 28.51           C  
ANISOU 1609  CB  TYR E  21     3102   4073   3655    125   -952   -279       C  
ATOM   1610  CG  TYR E  21     -30.496 -42.277 -19.217  1.00 31.57           C  
ANISOU 1610  CG  TYR E  21     3485   4306   4203     23  -1124   -196       C  
ATOM   1611  CD1 TYR E  21     -29.987 -42.787 -18.029  1.00 33.74           C  
ANISOU 1611  CD1 TYR E  21     3723   4573   4521   -127  -1203    -37       C  
ATOM   1612  CD2 TYR E  21     -30.670 -43.149 -20.292  1.00 35.46           C  
ANISOU 1612  CD2 TYR E  21     3999   4649   4824     58  -1237   -278       C  
ATOM   1613  CE1 TYR E  21     -29.656 -44.135 -17.904  1.00 37.66           C  
ANISOU 1613  CE1 TYR E  21     4194   4871   5240   -230  -1425     68       C  
ATOM   1614  CE2 TYR E  21     -30.339 -44.511 -20.180  1.00 38.27           C  
ANISOU 1614  CE2 TYR E  21     4326   4806   5408    -21  -1433   -231       C  
ATOM   1615  CZ  TYR E  21     -29.832 -44.987 -18.978  1.00 39.10           C  
ANISOU 1615  CZ  TYR E  21     4386   4863   5607   -160  -1542    -42       C  
ATOM   1616  OH  TYR E  21     -29.499 -46.318 -18.848  1.00 44.29           O  
ANISOU 1616  OH  TYR E  21     4996   5272   6558   -247  -1794     34       O  
ATOM   1617  N   PHE E  22     -30.823 -38.778 -21.842  1.00 27.38           N  
ANISOU 1617  N   PHE E  22     3094   3909   3400    404   -844   -497       N  
ATOM   1618  CA  PHE E  22     -31.744 -37.812 -22.444  1.00 27.64           C  
ANISOU 1618  CA  PHE E  22     3098   3993   3410    455   -857   -497       C  
ATOM   1619  C   PHE E  22     -32.884 -38.559 -23.114  1.00 28.93           C  
ANISOU 1619  C   PHE E  22     3220   4168   3601    404   -965   -478       C  
ATOM   1620  O   PHE E  22     -32.744 -39.735 -23.462  1.00 28.91           O  
ANISOU 1620  O   PHE E  22     3251   4114   3620    345  -1029   -500       O  
ATOM   1621  CB  PHE E  22     -31.035 -36.916 -23.468  1.00 27.03           C  
ANISOU 1621  CB  PHE E  22     3117   3888   3263    504   -857   -518       C  
ATOM   1622  CG  PHE E  22     -30.643 -37.625 -24.738  1.00 27.98           C  
ANISOU 1622  CG  PHE E  22     3319   4006   3306    450   -905   -575       C  
ATOM   1623  CD1 PHE E  22     -29.540 -38.469 -24.776  1.00 26.60           C  
ANISOU 1623  CD1 PHE E  22     3182   3790   3134    437   -860   -676       C  
ATOM   1624  CD2 PHE E  22     -31.383 -37.443 -25.900  1.00 28.95           C  
ANISOU 1624  CD2 PHE E  22     3458   4176   3363    401  -1004   -549       C  
ATOM   1625  CE1 PHE E  22     -29.185 -39.126 -25.942  1.00 29.21           C  
ANISOU 1625  CE1 PHE E  22     3550   4145   3400    386   -879   -809       C  
ATOM   1626  CE2 PHE E  22     -31.032 -38.095 -27.078  1.00 30.95           C  
ANISOU 1626  CE2 PHE E  22     3777   4482   3498    315  -1031   -644       C  
ATOM   1627  CZ  PHE E  22     -29.931 -38.937 -27.099  1.00 30.81           C  
ANISOU 1627  CZ  PHE E  22     3783   4443   3481    314   -952   -805       C  
ATOM   1628  N   TYR E  23     -34.003 -37.866 -23.307  1.00 29.85           N  
ANISOU 1628  N   TYR E  23     3251   4333   3757    432  -1004   -448       N  
ATOM   1629  CA  TYR E  23     -35.110 -38.429 -24.061  1.00 31.24           C  
ANISOU 1629  CA  TYR E  23     3387   4522   3959    380  -1125   -413       C  
ATOM   1630  C   TYR E  23     -34.909 -38.176 -25.548  1.00 31.73           C  
ANISOU 1630  C   TYR E  23     3559   4557   3939    363  -1217   -410       C  
ATOM   1631  O   TYR E  23     -34.768 -37.027 -25.982  1.00 31.92           O  
ANISOU 1631  O   TYR E  23     3601   4573   3952    400  -1244   -367       O  
ATOM   1632  CB  TYR E  23     -36.449 -37.859 -23.585  1.00 32.13           C  
ANISOU 1632  CB  TYR E  23     3318   4707   4184    407  -1140   -386       C  
ATOM   1633  CG  TYR E  23     -37.640 -38.524 -24.249  1.00 34.11           C  
ANISOU 1633  CG  TYR E  23     3506   4976   4474    338  -1273   -330       C  
ATOM   1634  CD1 TYR E  23     -38.027 -39.823 -23.903  1.00 34.78           C  
ANISOU 1634  CD1 TYR E  23     3563   5096   4553    227  -1304   -299       C  
ATOM   1635  CD2 TYR E  23     -38.370 -37.861 -25.231  1.00 35.57           C  
ANISOU 1635  CD2 TYR E  23     3660   5132   4720    362  -1405   -278       C  
ATOM   1636  CE1 TYR E  23     -39.124 -40.442 -24.523  1.00 36.23           C  
ANISOU 1636  CE1 TYR E  23     3693   5293   4778    153  -1441   -243       C  
ATOM   1637  CE2 TYR E  23     -39.470 -38.472 -25.855  1.00 37.36           C  
ANISOU 1637  CE2 TYR E  23     3830   5380   4982    285  -1544   -214       C  
ATOM   1638  CZ  TYR E  23     -39.834 -39.760 -25.497  1.00 37.45           C  
ANISOU 1638  CZ  TYR E  23     3819   5434   4974    186  -1549   -209       C  
ATOM   1639  OH  TYR E  23     -40.921 -40.354 -26.116  1.00 39.04           O  
ANISOU 1639  OH  TYR E  23     3965   5652   5215    101  -1697   -142       O  
ATOM   1640  N   ASN E  24     -34.881 -39.264 -26.313  1.00 32.51           N  
ANISOU 1640  N   ASN E  24     3723   4649   3980    279  -1281   -457       N  
ATOM   1641  CA  ASN E  24     -34.822 -39.211 -27.769  1.00 33.73           C  
ANISOU 1641  CA  ASN E  24     3968   4847   3998    199  -1368   -480       C  
ATOM   1642  C   ASN E  24     -36.214 -39.465 -28.338  1.00 35.23           C  
ANISOU 1642  C   ASN E  24     4099   5064   4222    129  -1524   -399       C  
ATOM   1643  O   ASN E  24     -36.633 -40.619 -28.491  1.00 35.59           O  
ANISOU 1643  O   ASN E  24     4139   5093   4289     64  -1579   -453       O  
ATOM   1644  CB  ASN E  24     -33.823 -40.244 -28.309  1.00 33.96           C  
ANISOU 1644  CB  ASN E  24     4085   4872   3944    145  -1324   -662       C  
ATOM   1645  CG  ASN E  24     -33.682 -40.198 -29.832  1.00 36.12           C  
ANISOU 1645  CG  ASN E  24     4443   5273   4008     15  -1379   -736       C  
ATOM   1646  OD1 ASN E  24     -34.539 -39.662 -30.539  1.00 38.97           O  
ANISOU 1646  OD1 ASN E  24     4806   5706   4294    -68  -1505   -605       O  
ATOM   1647  ND2 ASN E  24     -32.601 -40.775 -30.342  1.00 37.62           N  
ANISOU 1647  ND2 ASN E  24     4681   5506   4106    -22  -1292   -956       N  
ATOM   1648  N   ALA E  25     -36.910 -38.373 -28.653  1.00 36.47           N  
ANISOU 1648  N   ALA E  25     4201   5236   4419    138  -1621   -264       N  
ATOM   1649  CA  ALA E  25     -38.307 -38.409 -29.089  1.00 38.68           C  
ANISOU 1649  CA  ALA E  25     4385   5526   4783     87  -1790   -156       C  
ATOM   1650  C   ALA E  25     -38.523 -39.181 -30.391  1.00 40.54           C  
ANISOU 1650  C   ALA E  25     4720   5830   4850    -83  -1918   -170       C  
ATOM   1651  O   ALA E  25     -39.612 -39.727 -30.624  1.00 41.64           O  
ANISOU 1651  O   ALA E  25     4794   5975   5053   -144  -2042   -119       O  
ATOM   1652  CB  ALA E  25     -38.855 -36.991 -29.212  1.00 39.53           C  
ANISOU 1652  CB  ALA E  25     4396   5590   5033    140  -1906    -11       C  
ATOM   1653  N   LYS E  26     -37.493 -39.217 -31.236  1.00 41.40           N  
ANISOU 1653  N   LYS E  26     4975   6020   4736   -177  -1883   -258       N  
ATOM   1654  CA  LYS E  26     -37.543 -39.969 -32.494  1.00 43.83           C  
ANISOU 1654  CA  LYS E  26     5375   6445   4833   -368  -1969   -348       C  
ATOM   1655  C   LYS E  26     -37.542 -41.472 -32.244  1.00 43.60           C  
ANISOU 1655  C   LYS E  26     5345   6354   4867   -359  -1921   -554       C  
ATOM   1656  O   LYS E  26     -38.312 -42.215 -32.854  1.00 45.18           O  
ANISOU 1656  O   LYS E  26     5547   6577   5042   -473  -2049   -582       O  
ATOM   1657  CB  LYS E  26     -36.383 -39.572 -33.420  1.00 44.75           C  
ANISOU 1657  CB  LYS E  26     5611   6725   4665   -499  -1910   -430       C  
ATOM   1658  CG  LYS E  26     -36.702 -38.395 -34.337  1.00 48.69           C  
ANISOU 1658  CG  LYS E  26     6139   7340   5021   -666  -2093   -178       C  
ATOM   1659  CD  LYS E  26     -36.872 -37.101 -33.554  1.00 50.68           C  
ANISOU 1659  CD  LYS E  26     6309   7440   5507   -514  -2143     44       C  
ATOM   1660  CE  LYS E  26     -38.027 -36.275 -34.106  1.00 54.74           C  
ANISOU 1660  CE  LYS E  26     6752   7917   6128   -606  -2436    334       C  
ATOM   1661  NZ  LYS E  26     -38.488 -35.295 -33.072  1.00 56.34           N  
ANISOU 1661  NZ  LYS E  26     6802   7901   6700   -383  -2473    448       N  
ATOM   1662  N   ALA E  27     -36.670 -41.909 -31.342  1.00 42.35           N  
ANISOU 1662  N   ALA E  27     5179   6098   4813   -237  -1769   -683       N  
ATOM   1663  CA  ALA E  27     -36.603 -43.303 -30.933  1.00 42.47           C  
ANISOU 1663  CA  ALA E  27     5172   5990   4975   -221  -1771   -839       C  
ATOM   1664  C   ALA E  27     -37.729 -43.652 -29.955  1.00 41.96           C  
ANISOU 1664  C   ALA E  27     4992   5834   5114   -189  -1853   -666       C  
ATOM   1665  O   ALA E  27     -38.065 -44.825 -29.792  1.00 43.16           O  
ANISOU 1665  O   ALA E  27     5118   5889   5392   -237  -1941   -719       O  
ATOM   1666  CB  ALA E  27     -35.236 -43.604 -30.309  1.00 41.38           C  
ANISOU 1666  CB  ALA E  27     5047   5764   4912   -123  -1625   -998       C  
ATOM   1667  N   GLY E  28     -38.304 -42.633 -29.315  1.00 40.85           N  
ANISOU 1667  N   GLY E  28     4766   5735   5020   -122  -1830   -476       N  
ATOM   1668  CA  GLY E  28     -39.347 -42.819 -28.306  1.00 40.83           C  
ANISOU 1668  CA  GLY E  28     4612   5720   5179   -108  -1862   -341       C  
ATOM   1669  C   GLY E  28     -38.858 -43.414 -26.994  1.00 40.42           C  
ANISOU 1669  C   GLY E  28     4515   5610   5231    -82  -1774   -345       C  
ATOM   1670  O   GLY E  28     -39.618 -44.065 -26.277  1.00 41.10           O  
ANISOU 1670  O   GLY E  28     4493   5705   5417   -152  -1831   -250       O  
ATOM   1671  N   LEU E  29     -37.585 -43.191 -26.675  1.00 39.07           N  
ANISOU 1671  N   LEU E  29     4419   5396   5030    -12  -1655   -429       N  
ATOM   1672  CA  LEU E  29     -37.004 -43.706 -25.437  1.00 38.81           C  
ANISOU 1672  CA  LEU E  29     4348   5304   5090    -13  -1603   -402       C  
ATOM   1673  C   LEU E  29     -35.788 -42.901 -25.009  1.00 37.35           C  
ANISOU 1673  C   LEU E  29     4217   5120   4853     83  -1451   -450       C  
ATOM   1674  O   LEU E  29     -35.302 -42.034 -25.745  1.00 36.33           O  
ANISOU 1674  O   LEU E  29     4161   5023   4617    149  -1390   -516       O  
ATOM   1675  CB  LEU E  29     -36.644 -45.196 -25.562  1.00 39.69           C  
ANISOU 1675  CB  LEU E  29     4492   5249   5335    -89  -1734   -470       C  
ATOM   1676  CG  LEU E  29     -36.008 -45.730 -26.852  1.00 41.34           C  
ANISOU 1676  CG  LEU E  29     4804   5365   5536    -77  -1778   -705       C  
ATOM   1677  CD1 LEU E  29     -34.532 -45.366 -26.942  1.00 39.85           C  
ANISOU 1677  CD1 LEU E  29     4678   5146   5315     15  -1643   -861       C  
ATOM   1678  CD2 LEU E  29     -36.197 -47.249 -26.964  1.00 43.04           C  
ANISOU 1678  CD2 LEU E  29     4996   5393   5961   -163  -1968   -772       C  
ATOM   1679  N   CYS E  30     -35.304 -43.206 -23.813  1.00 37.42           N  
ANISOU 1679  N   CYS E  30     4185   5104   4927     60  -1414   -390       N  
ATOM   1680  CA  CYS E  30     -34.162 -42.515 -23.254  1.00 36.74           C  
ANISOU 1680  CA  CYS E  30     4140   5016   4802    133  -1285   -418       C  
ATOM   1681  C   CYS E  30     -32.869 -43.219 -23.639  1.00 36.11           C  
ANISOU 1681  C   CYS E  30     4141   4780   4800    158  -1309   -540       C  
ATOM   1682  O   CYS E  30     -32.777 -44.456 -23.613  1.00 37.09           O  
ANISOU 1682  O   CYS E  30     4246   4760   5085     96  -1443   -558       O  
ATOM   1683  CB  CYS E  30     -34.301 -42.402 -21.735  1.00 37.10           C  
ANISOU 1683  CB  CYS E  30     4090   5156   4850     62  -1234   -291       C  
ATOM   1684  SG  CYS E  30     -35.746 -41.422 -21.258  1.00 42.47           S  
ANISOU 1684  SG  CYS E  30     4613   6057   5463     58  -1153   -252       S  
ATOM   1685  N   GLN E  31     -31.878 -42.419 -24.009  1.00 34.23           N  
ANISOU 1685  N   GLN E  31     3971   4558   4475    246  -1193   -634       N  
ATOM   1686  CA  GLN E  31     -30.578 -42.930 -24.407  1.00 33.83           C  
ANISOU 1686  CA  GLN E  31     3959   4395   4498    283  -1179   -795       C  
ATOM   1687  C   GLN E  31     -29.516 -42.188 -23.611  1.00 31.87           C  
ANISOU 1687  C   GLN E  31     3723   4156   4229    335  -1068   -751       C  
ATOM   1688  O   GLN E  31     -29.821 -41.207 -22.944  1.00 31.38           O  
ANISOU 1688  O   GLN E  31     3657   4195   4070    345   -997   -632       O  
ATOM   1689  CB  GLN E  31     -30.373 -42.728 -25.906  1.00 34.37           C  
ANISOU 1689  CB  GLN E  31     4088   4536   4432    293  -1141   -984       C  
ATOM   1690  CG  GLN E  31     -31.335 -43.544 -26.766  1.00 37.19           C  
ANISOU 1690  CG  GLN E  31     4442   4887   4801    221  -1262  -1057       C  
ATOM   1691  CD  GLN E  31     -31.200 -43.242 -28.241  1.00 38.75           C  
ANISOU 1691  CD  GLN E  31     4701   5229   4792    173  -1223  -1228       C  
ATOM   1692  OE1 GLN E  31     -30.849 -42.130 -28.629  1.00 37.81           O  
ANISOU 1692  OE1 GLN E  31     4631   5254   4479    168  -1134  -1185       O  
ATOM   1693  NE2 GLN E  31     -31.483 -44.236 -29.076  1.00 42.45           N  
ANISOU 1693  NE2 GLN E  31     5164   5672   5293    107  -1306  -1418       N  
ATOM   1694  N   THR E  32     -28.273 -42.646 -23.677  1.00 31.09           N  
ANISOU 1694  N   THR E  32     3621   3947   4244    370  -1058   -872       N  
ATOM   1695  CA  THR E  32     -27.210 -41.988 -22.923  1.00 29.12           C  
ANISOU 1695  CA  THR E  32     3379   3699   3985    408   -970   -819       C  
ATOM   1696  C   THR E  32     -26.469 -40.939 -23.755  1.00 27.95           C  
ANISOU 1696  C   THR E  32     3290   3665   3662    466   -828   -926       C  
ATOM   1697  O   THR E  32     -26.452 -40.997 -24.986  1.00 28.60           O  
ANISOU 1697  O   THR E  32     3393   3818   3653    458   -802  -1083       O  
ATOM   1698  CB  THR E  32     -26.199 -43.006 -22.356  1.00 30.09           C  
ANISOU 1698  CB  THR E  32     3435   3623   4375    404  -1066   -845       C  
ATOM   1699  OG1 THR E  32     -25.735 -43.854 -23.409  1.00 32.21           O  
ANISOU 1699  OG1 THR E  32     3660   3783   4793    451  -1100  -1107       O  
ATOM   1700  CG2 THR E  32     -26.835 -43.860 -21.267  1.00 31.09           C  
ANISOU 1700  CG2 THR E  32     3505   3653   4652    287  -1244   -636       C  
ATOM   1701  N   PHE E  33     -25.876 -39.967 -23.068  1.00 25.70           N  
ANISOU 1701  N   PHE E  33     3030   3422   3312    490   -747   -830       N  
ATOM   1702  CA  PHE E  33     -24.962 -39.016 -23.699  1.00 25.02           C  
ANISOU 1702  CA  PHE E  33     2990   3425   3091    517   -638   -893       C  
ATOM   1703  C   PHE E  33     -23.931 -38.583 -22.670  1.00 23.69           C  
ANISOU 1703  C   PHE E  33     2815   3209   2975    540   -593   -818       C  
ATOM   1704  O   PHE E  33     -24.055 -38.907 -21.491  1.00 23.34           O  
ANISOU 1704  O   PHE E  33     2741   3094   3030    516   -646   -705       O  
ATOM   1705  CB  PHE E  33     -25.704 -37.796 -24.272  1.00 24.43           C  
ANISOU 1705  CB  PHE E  33     2977   3476   2828    502   -624   -810       C  
ATOM   1706  CG  PHE E  33     -26.142 -36.787 -23.234  1.00 23.39           C  
ANISOU 1706  CG  PHE E  33     2847   3338   2700    533   -617   -663       C  
ATOM   1707  CD1 PHE E  33     -27.247 -37.033 -22.413  1.00 23.31           C  
ANISOU 1707  CD1 PHE E  33     2780   3318   2756    528   -658   -601       C  
ATOM   1708  CD2 PHE E  33     -25.463 -35.569 -23.096  1.00 23.56           C  
ANISOU 1708  CD2 PHE E  33     2909   3381   2661    553   -570   -614       C  
ATOM   1709  CE1 PHE E  33     -27.678 -36.087 -21.463  1.00 22.49           C  
ANISOU 1709  CE1 PHE E  33     2642   3248   2655    551   -625   -544       C  
ATOM   1710  CE2 PHE E  33     -25.875 -34.616 -22.146  1.00 21.11           C  
ANISOU 1710  CE2 PHE E  33     2582   3053   2385    589   -565   -543       C  
ATOM   1711  CZ  PHE E  33     -26.981 -34.874 -21.328  1.00 22.82           C  
ANISOU 1711  CZ  PHE E  33     2724   3281   2665    592   -579   -536       C  
ATOM   1712  N   VAL E  34     -22.920 -37.850 -23.124  1.00 23.43           N  
ANISOU 1712  N   VAL E  34     2807   3242   2853    553   -505   -865       N  
ATOM   1713  CA  VAL E  34     -21.875 -37.362 -22.225  1.00 22.48           C  
ANISOU 1713  CA  VAL E  34     2683   3081   2774    566   -468   -793       C  
ATOM   1714  C   VAL E  34     -22.175 -35.922 -21.850  1.00 21.16           C  
ANISOU 1714  C   VAL E  34     2589   2981   2470    563   -439   -664       C  
ATOM   1715  O   VAL E  34     -22.218 -35.046 -22.708  1.00 21.96           O  
ANISOU 1715  O   VAL E  34     2736   3166   2440    550   -419   -657       O  
ATOM   1716  CB  VAL E  34     -20.474 -37.450 -22.866  1.00 23.26           C  
ANISOU 1716  CB  VAL E  34     2734   3207   2893    575   -393   -933       C  
ATOM   1717  CG1 VAL E  34     -19.423 -36.811 -21.941  1.00 23.36           C  
ANISOU 1717  CG1 VAL E  34     2749   3184   2940    579   -368   -827       C  
ATOM   1718  CG2 VAL E  34     -20.106 -38.904 -23.178  1.00 25.52           C  
ANISOU 1718  CG2 VAL E  34     2905   3385   3406    605   -433  -1129       C  
ATOM   1719  N   TYR E  35     -22.398 -35.696 -20.559  1.00 20.07           N  
ANISOU 1719  N   TYR E  35     2446   2807   2370    554   -455   -566       N  
ATOM   1720  CA  TYR E  35     -22.542 -34.354 -20.006  1.00 18.80           C  
ANISOU 1720  CA  TYR E  35     2325   2681   2137    563   -426   -505       C  
ATOM   1721  C   TYR E  35     -21.187 -33.902 -19.460  1.00 18.58           C  
ANISOU 1721  C   TYR E  35     2317   2627   2113    548   -392   -471       C  
ATOM   1722  O   TYR E  35     -20.486 -34.689 -18.805  1.00 18.14           O  
ANISOU 1722  O   TYR E  35     2224   2524   2141    512   -410   -447       O  
ATOM   1723  CB  TYR E  35     -23.613 -34.368 -18.905  1.00 18.69           C  
ANISOU 1723  CB  TYR E  35     2266   2701   2133    536   -437   -481       C  
ATOM   1724  CG  TYR E  35     -23.745 -33.082 -18.108  1.00 18.29           C  
ANISOU 1724  CG  TYR E  35     2216   2682   2050    548   -397   -496       C  
ATOM   1725  CD1 TYR E  35     -23.902 -31.848 -18.744  1.00 17.53           C  
ANISOU 1725  CD1 TYR E  35     2147   2545   1967    618   -415   -518       C  
ATOM   1726  CD2 TYR E  35     -23.709 -33.105 -16.716  1.00 17.05           C  
ANISOU 1726  CD2 TYR E  35     2022   2596   1858    465   -363   -493       C  
ATOM   1727  CE1 TYR E  35     -24.001 -30.680 -18.015  1.00 18.00           C  
ANISOU 1727  CE1 TYR E  35     2187   2587   2062    644   -402   -574       C  
ATOM   1728  CE2 TYR E  35     -23.841 -31.932 -15.976  1.00 18.80           C  
ANISOU 1728  CE2 TYR E  35     2226   2859   2054    472   -314   -577       C  
ATOM   1729  CZ  TYR E  35     -23.967 -30.730 -16.636  1.00 16.80           C  
ANISOU 1729  CZ  TYR E  35     1992   2517   1872    582   -335   -635       C  
ATOM   1730  OH  TYR E  35     -24.090 -29.578 -15.911  1.00 17.77           O  
ANISOU 1730  OH  TYR E  35     2079   2636   2034    605   -309   -757       O  
ATOM   1731  N   GLY E  36     -20.829 -32.647 -19.747  1.00 17.29           N  
ANISOU 1731  N   GLY E  36     2205   2477   1886    561   -376   -447       N  
ATOM   1732  CA  GLY E  36     -19.511 -32.100 -19.382  1.00 16.89           C  
ANISOU 1732  CA  GLY E  36     2178   2409   1830    537   -351   -406       C  
ATOM   1733  C   GLY E  36     -19.363 -31.599 -17.953  1.00 16.08           C  
ANISOU 1733  C   GLY E  36     2084   2284   1739    507   -351   -371       C  
ATOM   1734  O   GLY E  36     -18.261 -31.269 -17.528  1.00 15.29           O  
ANISOU 1734  O   GLY E  36     2001   2165   1643    473   -345   -326       O  
ATOM   1735  N   GLY E  37     -20.470 -31.475 -17.217  1.00 16.26           N  
ANISOU 1735  N   GLY E  37     2084   2337   1754    504   -351   -410       N  
ATOM   1736  CA  GLY E  37     -20.367 -31.068 -15.821  1.00 17.54           C  
ANISOU 1736  CA  GLY E  37     2238   2543   1880    434   -331   -422       C  
ATOM   1737  C   GLY E  37     -20.821 -29.671 -15.446  1.00 18.35           C  
ANISOU 1737  C   GLY E  37     2343   2639   1989    472   -316   -528       C  
ATOM   1738  O   GLY E  37     -20.961 -29.372 -14.252  1.00 18.89           O  
ANISOU 1738  O   GLY E  37     2380   2790   2004    400   -276   -608       O  
ATOM   1739  N   CYS E  38     -21.048 -28.812 -16.445  1.00 18.58           N  
ANISOU 1739  N   CYS E  38     2393   2572   2092    565   -367   -537       N  
ATOM   1740  CA ACYS E  38     -21.542 -27.445 -16.217  0.50 20.01           C  
ANISOU 1740  CA ACYS E  38     2549   2672   2379    626   -409   -647       C  
ATOM   1741  CA BCYS E  38     -21.582 -27.482 -16.182  0.50 19.35           C  
ANISOU 1741  CA BCYS E  38     2462   2594   2294    625   -405   -652       C  
ATOM   1742  C   CYS E  38     -22.616 -27.064 -17.229  1.00 20.52           C  
ANISOU 1742  C   CYS E  38     2571   2656   2569    716   -498   -656       C  
ATOM   1743  O   CYS E  38     -22.584 -27.530 -18.374  1.00 19.20           O  
ANISOU 1743  O   CYS E  38     2442   2490   2361    707   -544   -530       O  
ATOM   1744  CB ACYS E  38     -20.426 -26.401 -16.325  0.50 20.41           C  
ANISOU 1744  CB ACYS E  38     2675   2612   2467    613   -474   -582       C  
ATOM   1745  CB BCYS E  38     -20.459 -26.439 -16.028  0.50 19.71           C  
ANISOU 1745  CB BCYS E  38     2577   2542   2370    605   -455   -612       C  
ATOM   1746  SG ACYS E  38     -18.840 -26.756 -15.538  0.50 22.05           S  
ANISOU 1746  SG ACYS E  38     2946   2878   2553    499   -420   -496       S  
ATOM   1747  SG BCYS E  38     -19.504 -26.049 -17.527  0.50 17.73           S  
ANISOU 1747  SG BCYS E  38     2411   2207   2118    587   -560   -399       S  
ATOM   1748  N   ARG E  39     -23.539 -26.201 -16.800  1.00 22.44           N  
ANISOU 1748  N   ARG E  39     2715   2833   2975    791   -530   -821       N  
ATOM   1749  CA  ARG E  39     -24.553 -25.581 -17.682  1.00 25.70           C  
ANISOU 1749  CA  ARG E  39     3060   3111   3594    884   -673   -821       C  
ATOM   1750  C   ARG E  39     -25.543 -26.559 -18.299  1.00 25.39           C  
ANISOU 1750  C   ARG E  39     2973   3160   3512    890   -662   -782       C  
ATOM   1751  O   ARG E  39     -25.938 -26.401 -19.465  1.00 26.38           O  
ANISOU 1751  O   ARG E  39     3111   3205   3707    902   -804   -651       O  
ATOM   1752  CB  ARG E  39     -23.885 -24.746 -18.796  1.00 25.99           C  
ANISOU 1752  CB  ARG E  39     3188   2984   3701    861   -860   -613       C  
ATOM   1753  CG  ARG E  39     -22.955 -23.653 -18.281  1.00 29.18           C  
ANISOU 1753  CG  ARG E  39     3634   3261   4191    849   -917   -628       C  
ATOM   1754  CD  ARG E  39     -23.729 -22.514 -17.619  1.00 35.60           C  
ANISOU 1754  CD  ARG E  39     4313   3889   5321    964  -1006   -860       C  
ATOM   1755  NE  ARG E  39     -22.901 -21.877 -16.599  1.00 40.49           N  
ANISOU 1755  NE  ARG E  39     4958   4474   5950    945   -961   -992       N  
ATOM   1756  CZ  ARG E  39     -22.399 -20.650 -16.689  1.00 43.34           C  
ANISOU 1756  CZ  ARG E  39     5341   4601   6525    954  -1145   -963       C  
ATOM   1757  NH1 ARG E  39     -21.660 -20.178 -15.699  1.00 43.50           N  
ANISOU 1757  NH1 ARG E  39     5387   4614   6527    924  -1088  -1104       N  
ATOM   1758  NH2 ARG E  39     -22.644 -19.889 -17.753  1.00 45.92           N  
ANISOU 1758  NH2 ARG E  39     5659   4699   7087    968  -1413   -776       N  
ATOM   1759  N   ALA E  40     -25.949 -27.560 -17.523  1.00 25.35           N  
ANISOU 1759  N   ALA E  40     2914   3328   3387    852   -517   -874       N  
ATOM   1760  CA  ALA E  40     -26.880 -28.580 -18.008  1.00 25.60           C  
ANISOU 1760  CA  ALA E  40     2899   3446   3379    842   -512   -836       C  
ATOM   1761  C   ALA E  40     -28.180 -27.948 -18.491  1.00 27.75           C  
ANISOU 1761  C   ALA E  40     3041   3628   3874    941   -619   -906       C  
ATOM   1762  O   ALA E  40     -28.659 -26.965 -17.912  1.00 28.53           O  
ANISOU 1762  O   ALA E  40     3012   3656   4173   1023   -633  -1089       O  
ATOM   1763  CB  ALA E  40     -27.180 -29.594 -16.910  1.00 25.75           C  
ANISOU 1763  CB  ALA E  40     2856   3663   3263    753   -373   -911       C  
ATOM   1764  N   LYS E  41     -28.721 -28.508 -19.571  1.00 28.40           N  
ANISOU 1764  N   LYS E  41     3142   3704   3945    929   -708   -775       N  
ATOM   1765  CA  LYS E  41     -30.078 -28.211 -20.008  1.00 30.81           C  
ANISOU 1765  CA  LYS E  41     3302   3948   4453   1000   -819   -813       C  
ATOM   1766  C   LYS E  41     -31.012 -29.241 -19.381  1.00 31.23           C  
ANISOU 1766  C   LYS E  41     3240   4186   4439    972   -692   -918       C  
ATOM   1767  O   LYS E  41     -30.557 -30.194 -18.751  1.00 29.60           O  
ANISOU 1767  O   LYS E  41     3087   4130   4029    878   -560   -911       O  
ATOM   1768  CB  LYS E  41     -30.169 -28.223 -21.536  1.00 31.43           C  
ANISOU 1768  CB  LYS E  41     3467   3945   4527    957  -1009   -590       C  
ATOM   1769  CG  LYS E  41     -29.430 -27.066 -22.186  1.00 33.20           C  
ANISOU 1769  CG  LYS E  41     3772   4006   4835    940  -1181   -449       C  
ATOM   1770  CD  LYS E  41     -29.684 -27.016 -23.682  1.00 37.86           C  
ANISOU 1770  CD  LYS E  41     4422   4569   5394    837  -1394   -211       C  
ATOM   1771  CE  LYS E  41     -28.896 -25.883 -24.324  1.00 41.05           C  
ANISOU 1771  CE  LYS E  41     4905   4844   5845    756  -1590    -16       C  
ATOM   1772  NZ  LYS E  41     -29.109 -24.587 -23.607  1.00 45.16           N  
ANISOU 1772  NZ  LYS E  41     5308   5114   6736    886  -1712   -108       N  
ATOM   1773  N   ARG E  42     -32.320 -29.042 -19.538  1.00 33.12           N  
ANISOU 1773  N   ARG E  42     3302   4408   4871   1037   -756   -995       N  
ATOM   1774  CA  ARG E  42     -33.300 -29.856 -18.819  1.00 34.42           C  
ANISOU 1774  CA  ARG E  42     3312   4778   4987    994   -631  -1114       C  
ATOM   1775  C   ARG E  42     -33.419 -31.310 -19.301  1.00 32.93           C  
ANISOU 1775  C   ARG E  42     3217   4694   4599    877   -633   -943       C  
ATOM   1776  O   ARG E  42     -33.784 -32.191 -18.519  1.00 33.35           O  
ANISOU 1776  O   ARG E  42     3201   4938   4531    777   -522   -981       O  
ATOM   1777  CB  ARG E  42     -34.672 -29.167 -18.820  1.00 37.08           C  
ANISOU 1777  CB  ARG E  42     3387   5068   5631   1108   -695  -1280       C  
ATOM   1778  CG  ARG E  42     -34.658 -27.725 -18.333  1.00 41.88           C  
ANISOU 1778  CG  ARG E  42     3855   5526   6531   1245   -720  -1509       C  
ATOM   1779  CD  ARG E  42     -36.035 -27.316 -17.800  1.00 48.27           C  
ANISOU 1779  CD  ARG E  42     4323   6392   7626   1342   -680  -1807       C  
ATOM   1780  NE  ARG E  42     -36.026 -27.165 -16.341  1.00 54.46           N  
ANISOU 1780  NE  ARG E  42     4953   7417   8322   1306   -426  -2149       N  
ATOM   1781  CZ  ARG E  42     -35.969 -28.167 -15.460  1.00 56.08           C  
ANISOU 1781  CZ  ARG E  42     5168   7971   8167   1120   -209  -2172       C  
ATOM   1782  NH1 ARG E  42     -35.963 -27.897 -14.161  1.00 58.47           N  
ANISOU 1782  NH1 ARG E  42     5320   8525   8370   1048      4  -2487       N  
ATOM   1783  NH2 ARG E  42     -35.917 -29.436 -15.861  1.00 55.27           N  
ANISOU 1783  NH2 ARG E  42     5217   7973   7808    982   -224  -1885       N  
ATOM   1784  N   ASN E  43     -33.123 -31.562 -20.575  1.00 32.10           N  
ANISOU 1784  N   ASN E  43     3259   4479   4458    865   -769   -763       N  
ATOM   1785  CA  ASN E  43     -33.125 -32.932 -21.101  1.00 30.92           C  
ANISOU 1785  CA  ASN E  43     3201   4399   4148    763   -781   -651       C  
ATOM   1786  C   ASN E  43     -31.836 -33.663 -20.705  1.00 29.40           C  
ANISOU 1786  C   ASN E  43     3149   4239   3781    690   -690   -619       C  
ATOM   1787  O   ASN E  43     -30.958 -33.906 -21.529  1.00 28.75           O  
ANISOU 1787  O   ASN E  43     3207   4098   3619    669   -727   -551       O  
ATOM   1788  CB  ASN E  43     -33.339 -32.954 -22.623  1.00 31.11           C  
ANISOU 1788  CB  ASN E  43     3305   4338   4175    748   -951   -520       C  
ATOM   1789  CG  ASN E  43     -33.771 -34.331 -23.143  1.00 30.39           C  
ANISOU 1789  CG  ASN E  43     3247   4317   3981    655   -980   -471       C  
ATOM   1790  OD1 ASN E  43     -33.992 -35.268 -22.373  1.00 30.89           O  
ANISOU 1790  OD1 ASN E  43     3263   4464   4009    605   -902   -506       O  
ATOM   1791  ND2 ASN E  43     -33.891 -34.449 -24.454  1.00 30.31           N  
ANISOU 1791  ND2 ASN E  43     3316   4280   3919    603  -1112   -384       N  
ATOM   1792  N   ASN E  44     -31.761 -34.029 -19.431  1.00 29.55           N  
ANISOU 1792  N   ASN E  44     3106   4373   3748    629   -577   -675       N  
ATOM   1793  CA  ASN E  44     -30.531 -34.499 -18.816  1.00 29.06           C  
ANISOU 1793  CA  ASN E  44     3142   4321   3576    558   -519   -635       C  
ATOM   1794  C   ASN E  44     -30.898 -35.145 -17.484  1.00 30.21           C  
ANISOU 1794  C   ASN E  44     3186   4643   3647    418   -450   -639       C  
ATOM   1795  O   ASN E  44     -31.257 -34.452 -16.537  1.00 30.88           O  
ANISOU 1795  O   ASN E  44     3159   4863   3711    398   -353   -758       O  
ATOM   1796  CB  ASN E  44     -29.598 -33.294 -18.635  1.00 28.40           C  
ANISOU 1796  CB  ASN E  44     3116   4167   3504    629   -479   -682       C  
ATOM   1797  CG  ASN E  44     -28.278 -33.649 -17.984  1.00 27.46           C  
ANISOU 1797  CG  ASN E  44     3087   4054   3293    558   -430   -634       C  
ATOM   1798  OD1 ASN E  44     -28.191 -34.583 -17.181  1.00 27.26           O  
ANISOU 1798  OD1 ASN E  44     3037   4113   3205    437   -414   -584       O  
ATOM   1799  ND2 ASN E  44     -27.242 -32.874 -18.303  1.00 24.08           N  
ANISOU 1799  ND2 ASN E  44     2750   3531   2867    612   -431   -625       N  
ATOM   1800  N   PHE E  45     -30.820 -36.475 -17.420  1.00 31.23           N  
ANISOU 1800  N   PHE E  45     3341   4782   3742    297   -515   -517       N  
ATOM   1801  CA  PHE E  45     -31.323 -37.222 -16.260  1.00 33.47           C  
ANISOU 1801  CA  PHE E  45     3519   5254   3941     99   -504   -452       C  
ATOM   1802  C   PHE E  45     -30.307 -38.194 -15.702  1.00 34.14           C  
ANISOU 1802  C   PHE E  45     3677   5291   4001    -46   -588   -291       C  
ATOM   1803  O   PHE E  45     -29.525 -38.777 -16.442  1.00 33.61           O  
ANISOU 1803  O   PHE E  45     3711   5018   4041     15   -683   -241       O  
ATOM   1804  CB  PHE E  45     -32.605 -37.986 -16.624  1.00 34.23           C  
ANISOU 1804  CB  PHE E  45     3520   5409   4077     43   -574   -410       C  
ATOM   1805  CG  PHE E  45     -33.704 -37.109 -17.161  1.00 34.80           C  
ANISOU 1805  CG  PHE E  45     3484   5516   4223    177   -528   -548       C  
ATOM   1806  CD1 PHE E  45     -33.782 -36.825 -18.519  1.00 33.22           C  
ANISOU 1806  CD1 PHE E  45     3360   5131   4128    330   -612   -556       C  
ATOM   1807  CD2 PHE E  45     -34.657 -36.561 -16.307  1.00 37.23           C  
ANISOU 1807  CD2 PHE E  45     3588   6052   4504    131   -414   -680       C  
ATOM   1808  CE1 PHE E  45     -34.790 -36.011 -19.024  1.00 34.94           C  
ANISOU 1808  CE1 PHE E  45     3466   5346   4460    438   -627   -640       C  
ATOM   1809  CE2 PHE E  45     -35.673 -35.745 -16.804  1.00 38.12           C  
ANISOU 1809  CE2 PHE E  45     3562   6154   4767    275   -402   -822       C  
ATOM   1810  CZ  PHE E  45     -35.738 -35.468 -18.167  1.00 36.58           C  
ANISOU 1810  CZ  PHE E  45     3457   5728   4715    431   -531   -777       C  
ATOM   1811  N   LYS E  46     -30.341 -38.397 -14.391  1.00 36.90           N  
ANISOU 1811  N   LYS E  46     3955   5844   4221   -262   -566   -215       N  
ATOM   1812  CA  LYS E  46     -29.373 -39.283 -13.756  1.00 38.67           C  
ANISOU 1812  CA  LYS E  46     4231   6009   4450   -435   -697    -13       C  
ATOM   1813  C   LYS E  46     -29.741 -40.758 -13.935  1.00 40.32           C  
ANISOU 1813  C   LYS E  46     4416   6125   4779   -571   -904    179       C  
ATOM   1814  O   LYS E  46     -28.896 -41.643 -13.772  1.00 40.62           O  
ANISOU 1814  O   LYS E  46     4494   5987   4951   -658  -1085    345       O  
ATOM   1815  CB  LYS E  46     -29.189 -38.907 -12.283  1.00 40.25           C  
ANISOU 1815  CB  LYS E  46     4374   6483   4435   -668   -627     26       C  
ATOM   1816  CG  LYS E  46     -28.505 -37.549 -12.102  1.00 41.09           C  
ANISOU 1816  CG  LYS E  46     4529   6602   4479   -532   -469   -159       C  
ATOM   1817  CD  LYS E  46     -28.650 -37.028 -10.686  1.00 45.90           C  
ANISOU 1817  CD  LYS E  46     5049   7552   4838   -764   -354   -218       C  
ATOM   1818  CE  LYS E  46     -28.207 -35.576 -10.604  1.00 46.94           C  
ANISOU 1818  CE  LYS E  46     5207   7675   4952   -597   -197   -468       C  
ATOM   1819  NZ  LYS E  46     -28.345 -35.022  -9.226  1.00 50.21           N  
ANISOU 1819  NZ  LYS E  46     5521   8443   5111   -827    -65   -599       N  
ATOM   1820  N   SER E  47     -30.997 -41.012 -14.300  1.00 42.04           N  
ANISOU 1820  N   SER E  47     4551   6430   4990   -582   -902    152       N  
ATOM   1821  CA  SER E  47     -31.494 -42.378 -14.461  1.00 44.46           C  
ANISOU 1821  CA  SER E  47     4824   6652   5416   -727  -1114    332       C  
ATOM   1822  C   SER E  47     -32.550 -42.481 -15.554  1.00 44.66           C  
ANISOU 1822  C   SER E  47     4824   6629   5515   -592  -1110    226       C  
ATOM   1823  O   SER E  47     -33.287 -41.524 -15.806  1.00 44.47           O  
ANISOU 1823  O   SER E  47     4745   6745   5406   -476   -947     64       O  
ATOM   1824  CB  SER E  47     -32.081 -42.888 -13.141  1.00 46.81           C  
ANISOU 1824  CB  SER E  47     4998   7241   5543  -1088  -1175    545       C  
ATOM   1825  OG  SER E  47     -33.256 -42.166 -12.808  1.00 48.59           O  
ANISOU 1825  OG  SER E  47     5085   7804   5570  -1129   -977    406       O  
ATOM   1826  N   ALA E  48     -32.620 -43.656 -16.180  1.00 45.87           N  
ANISOU 1826  N   ALA E  48     5004   6566   5856   -616  -1315    314       N  
ATOM   1827  CA  ALA E  48     -33.621 -43.962 -17.200  1.00 46.89           C  
ANISOU 1827  CA  ALA E  48     5114   6646   6055   -538  -1357    244       C  
ATOM   1828  C   ALA E  48     -35.048 -43.840 -16.656  1.00 48.65           C  
ANISOU 1828  C   ALA E  48     5181   7163   6138   -691  -1304    303       C  
ATOM   1829  O   ALA E  48     -35.936 -43.316 -17.335  1.00 48.34           O  
ANISOU 1829  O   ALA E  48     5095   7184   6086   -569  -1223    178       O  
ATOM   1830  CB  ALA E  48     -33.383 -45.362 -17.771  1.00 47.86           C  
ANISOU 1830  CB  ALA E  48     5276   6482   6424   -579  -1611    318       C  
ATOM   1831  N   GLU E  49     -35.243 -44.326 -15.429  1.00 50.89           N  
ANISOU 1831  N   GLU E  49     5368   7647   6318   -982  -1361    502       N  
ATOM   1832  CA  GLU E  49     -36.522 -44.251 -14.716  1.00 53.31           C  
ANISOU 1832  CA  GLU E  49     5486   8317   6451  -1190  -1286    552       C  
ATOM   1833  C   GLU E  49     -37.048 -42.814 -14.705  1.00 52.69           C  
ANISOU 1833  C   GLU E  49     5310   8456   6254  -1016  -1004    277       C  
ATOM   1834  O   GLU E  49     -38.157 -42.547 -15.181  1.00 53.20           O  
ANISOU 1834  O   GLU E  49     5256   8606   6351   -942   -951    175       O  
ATOM   1835  CB  GLU E  49     -36.346 -44.788 -13.283  1.00 55.76           C  
ANISOU 1835  CB  GLU E  49     5719   8873   6593  -1574  -1362    802       C  
ATOM   1836  CG  GLU E  49     -37.458 -44.434 -12.283  1.00 59.65           C  
ANISOU 1836  CG  GLU E  49     5985   9877   6802  -1835  -1196    790       C  
ATOM   1837  CD  GLU E  49     -38.517 -45.518 -12.135  1.00 64.37           C  
ANISOU 1837  CD  GLU E  49     6455  10610   7390  -2128  -1374   1030       C  
ATOM   1838  OE1 GLU E  49     -39.486 -45.297 -11.375  1.00 67.67           O  
ANISOU 1838  OE1 GLU E  49     6656  11486   7570  -2364  -1230   1009       O  
ATOM   1839  OE2 GLU E  49     -38.390 -46.591 -12.770  1.00 65.50           O  
ANISOU 1839  OE2 GLU E  49     6696  10417   7773  -2134  -1657   1221       O  
ATOM   1840  N   ASP E  50     -36.227 -41.902 -14.183  1.00 51.79           N  
ANISOU 1840  N   ASP E  50     5236   8396   6047   -948   -854    158       N  
ATOM   1841  CA  ASP E  50     -36.566 -40.486 -14.076  1.00 51.52           C  
ANISOU 1841  CA  ASP E  50     5101   8514   5959   -778   -616   -125       C  
ATOM   1842  C   ASP E  50     -36.742 -39.820 -15.443  1.00 49.55           C  
ANISOU 1842  C   ASP E  50     4914   8004   5905   -450   -618   -275       C  
ATOM   1843  O   ASP E  50     -37.546 -38.904 -15.592  1.00 50.24           O  
ANISOU 1843  O   ASP E  50     4859   8182   6049   -323   -508   -467       O  
ATOM   1844  CB  ASP E  50     -35.496 -39.751 -13.263  1.00 51.48           C  
ANISOU 1844  CB  ASP E  50     5156   8570   5834   -789   -500   -200       C  
ATOM   1845  CG  ASP E  50     -35.898 -38.325 -12.908  1.00 53.09           C  
ANISOU 1845  CG  ASP E  50     5217   8955   6001   -659   -267   -521       C  
ATOM   1846  OD1 ASP E  50     -37.113 -38.033 -12.842  1.00 56.34           O  
ANISOU 1846  OD1 ASP E  50     5413   9565   6429   -658   -173   -675       O  
ATOM   1847  OD2 ASP E  50     -34.993 -37.493 -12.683  1.00 52.92           O  
ANISOU 1847  OD2 ASP E  50     5279   8863   5964   -557   -189   -634       O  
ATOM   1848  N   CYS E  51     -35.985 -40.281 -16.434  1.00 47.47           N  
ANISOU 1848  N   CYS E  51     4847   7431   5758   -334   -757   -194       N  
ATOM   1849  CA  CYS E  51     -36.076 -39.739 -17.784  1.00 45.65           C  
ANISOU 1849  CA  CYS E  51     4692   6996   5656    -96   -785   -294       C  
ATOM   1850  C   CYS E  51     -37.417 -40.100 -18.423  1.00 46.99           C  
ANISOU 1850  C   CYS E  51     4754   7198   5901   -106   -866   -275       C  
ATOM   1851  O   CYS E  51     -38.071 -39.248 -19.022  1.00 46.88           O  
ANISOU 1851  O   CYS E  51     4669   7170   5973     37   -843   -381       O  
ATOM   1852  CB  CYS E  51     -34.905 -40.234 -18.634  1.00 44.05           C  
ANISOU 1852  CB  CYS E  51     4697   6528   5510    -21   -888   -249       C  
ATOM   1853  SG  CYS E  51     -34.964 -39.762 -20.378  1.00 40.42           S  
ANISOU 1853  SG  CYS E  51     4341   5889   5125    171   -946   -336       S  
ATOM   1854  N   MET E  52     -37.817 -41.363 -18.278  1.00 48.19           N  
ANISOU 1854  N   MET E  52     4885   7375   6048   -289   -991   -120       N  
ATOM   1855  CA  MET E  52     -39.087 -41.856 -18.825  1.00 49.66           C  
ANISOU 1855  CA  MET E  52     4967   7598   6300   -336  -1089    -74       C  
ATOM   1856  C   MET E  52     -40.303 -41.282 -18.097  1.00 51.46           C  
ANISOU 1856  C   MET E  52     4930   8127   6493   -396   -961   -149       C  
ATOM   1857  O   MET E  52     -41.358 -41.075 -18.707  1.00 52.01           O  
ANISOU 1857  O   MET E  52     4882   8213   6665   -332   -997   -189       O  
ATOM   1858  CB  MET E  52     -39.135 -43.388 -18.808  1.00 50.58           C  
ANISOU 1858  CB  MET E  52     5129   7637   6451   -535  -1287    118       C  
ATOM   1859  CG  MET E  52     -38.325 -44.068 -19.916  1.00 50.38           C  
ANISOU 1859  CG  MET E  52     5306   7290   6545   -441  -1440    107       C  
ATOM   1860  SD  MET E  52     -38.724 -43.521 -21.600  1.00 52.05           S  
ANISOU 1860  SD  MET E  52     5594   7379   6802   -241  -1465    -37       S  
ATOM   1861  CE  MET E  52     -40.400 -44.130 -21.806  1.00 52.68           C  
ANISOU 1861  CE  MET E  52     5517   7565   6932   -373  -1591     64       C  
ATOM   1862  N   ARG E  53     -40.152 -41.025 -16.798  1.00 52.38           N  
ANISOU 1862  N   ARG E  53     4935   8500   6467   -533   -814   -184       N  
ATOM   1863  CA  ARG E  53     -41.233 -40.455 -15.994  1.00 54.75           C  
ANISOU 1863  CA  ARG E  53     4941   9148   6713   -609   -646   -332       C  
ATOM   1864  C   ARG E  53     -41.591 -39.030 -16.417  1.00 54.49           C  
ANISOU 1864  C   ARG E  53     4793   9056   6851   -328   -534   -606       C  
ATOM   1865  O   ARG E  53     -42.765 -38.672 -16.433  1.00 56.26           O  
ANISOU 1865  O   ARG E  53     4765   9424   7187   -297   -487   -733       O  
ATOM   1866  CB  ARG E  53     -40.893 -40.488 -14.499  1.00 56.54           C  
ANISOU 1866  CB  ARG E  53     5077   9710   6696   -863   -503   -338       C  
ATOM   1867  CG  ARG E  53     -41.027 -41.860 -13.857  1.00 59.01           C  
ANISOU 1867  CG  ARG E  53     5381  10188   6851  -1232   -639    -37       C  
ATOM   1868  CD  ARG E  53     -41.109 -41.763 -12.337  1.00 63.28           C  
ANISOU 1868  CD  ARG E  53     5744  11201   7097  -1558   -478    -56       C  
ATOM   1869  NE  ARG E  53     -41.252 -43.078 -11.706  1.00 66.91           N  
ANISOU 1869  NE  ARG E  53     6189  11829   7402  -1970   -659    298       N  
ATOM   1870  CZ  ARG E  53     -42.364 -43.818 -11.724  1.00 70.16           C  
ANISOU 1870  CZ  ARG E  53     6438  12418   7798  -2176   -744    439       C  
ATOM   1871  NH1 ARG E  53     -43.455 -43.390 -12.351  1.00 70.83           N  
ANISOU 1871  NH1 ARG E  53     6354  12541   8017  -1995   -653    242       N  
ATOM   1872  NH2 ARG E  53     -42.386 -44.999 -11.116  1.00 72.63           N  
ANISOU 1872  NH2 ARG E  53     6752  12858   7985  -2582   -953    804       N  
ATOM   1873  N   THR E  54     -40.588 -38.221 -16.761  1.00 52.34           N  
ANISOU 1873  N   THR E  54     4687   8561   6635   -132   -517   -687       N  
ATOM   1874  CA  THR E  54     -40.845 -36.820 -17.118  1.00 52.46           C  
ANISOU 1874  CA  THR E  54     4596   8475   6860    117   -464   -916       C  
ATOM   1875  C   THR E  54     -41.029 -36.590 -18.629  1.00 51.33           C  
ANISOU 1875  C   THR E  54     4560   8022   6918    298   -661   -828       C  
ATOM   1876  O   THR E  54     -41.719 -35.651 -19.036  1.00 52.69           O  
ANISOU 1876  O   THR E  54     4573   8116   7330    457   -699   -952       O  
ATOM   1877  CB  THR E  54     -39.785 -35.824 -16.536  1.00 51.70           C  
ANISOU 1877  CB  THR E  54     4567   8341   6733    209   -340  -1075       C  
ATOM   1878  OG1 THR E  54     -38.796 -35.524 -17.522  1.00 50.26           O  
ANISOU 1878  OG1 THR E  54     4644   7835   6614    359   -463   -972       O  
ATOM   1879  CG2 THR E  54     -39.115 -36.369 -15.277  1.00 51.53           C  
ANISOU 1879  CG2 THR E  54     4582   8566   6430    -26   -218  -1038       C  
ATOM   1880  N   CYS E  55     -40.429 -37.450 -19.449  1.00 49.02           N  
ANISOU 1880  N   CYS E  55     4518   7564   6543    253   -801   -626       N  
ATOM   1881  CA  CYS E  55     -40.441 -37.259 -20.904  1.00 47.86           C  
ANISOU 1881  CA  CYS E  55     4501   7179   6504    365   -980   -543       C  
ATOM   1882  C   CYS E  55     -41.121 -38.383 -21.689  1.00 47.93           C  
ANISOU 1882  C   CYS E  55     4545   7167   6498    258  -1136   -396       C  
ATOM   1883  O   CYS E  55     -41.390 -38.231 -22.883  1.00 47.88           O  
ANISOU 1883  O   CYS E  55     4604   7025   6562    308  -1292   -334       O  
ATOM   1884  CB  CYS E  55     -39.011 -37.062 -21.425  1.00 45.87           C  
ANISOU 1884  CB  CYS E  55     4512   6751   6164    421   -998   -505       C  
ATOM   1885  SG  CYS E  55     -38.239 -35.468 -21.019  1.00 45.63           S  
ANISOU 1885  SG  CYS E  55     4475   6647   6214    581   -903   -645       S  
ATOM   1886  N   GLY E  56     -41.388 -39.505 -21.025  1.00 48.07           N  
ANISOU 1886  N   GLY E  56     4520   7324   6419     82  -1120   -324       N  
ATOM   1887  CA  GLY E  56     -41.940 -40.684 -21.692  1.00 48.52           C  
ANISOU 1887  CA  GLY E  56     4622   7336   6476    -37  -1287   -187       C  
ATOM   1888  C   GLY E  56     -43.433 -40.586 -21.950  1.00 50.46           C  
ANISOU 1888  C   GLY E  56     4646   7680   6846    -54  -1354   -173       C  
ATOM   1889  O   GLY E  56     -43.912 -40.999 -23.006  1.00 50.91           O  
ANISOU 1889  O   GLY E  56     4762   7629   6952    -70  -1528    -90       O  
TER    1890      GLY E  56                                                      
HETATM 1891  O   HOH A   8      -2.647 -45.465  -9.009  1.00 34.66           O  
ANISOU 1891  O   HOH A   8     3942   3286   5941    426    -72   1020       O  
HETATM 1892  O   HOH A  39     -17.250 -46.384  -2.108  1.00 58.35           O  
ANISOU 1892  O   HOH A  39     7066   6660   8443  -1012    246   1268       O  
HETATM 1893  O   HOH A  96      -3.843 -44.644 -15.503  1.00 36.61           O  
ANISOU 1893  O   HOH A  96     4620   3383   5905    322    276   -469       O  
HETATM 1894  O   HOH A  97     -21.699 -43.053  -5.441  1.00 58.51           O  
ANISOU 1894  O   HOH A  97     6157   7831   8240   -870    399   1324       O  
HETATM 1895  O   HOH A  98     -19.480 -44.591  -5.552  1.00 77.76           O  
ANISOU 1895  O   HOH A  98     9014   9733  10796  -1038    174    968       O  
HETATM 1896  O   HOH A  99      -1.111 -28.773 -29.715  1.00 39.93           O  
ANISOU 1896  O   HOH A  99     4431   7019   3718    712    337    114       O  
HETATM 1897  O   HOH A 100       0.135 -30.237 -35.796  1.00 67.40           O  
ANISOU 1897  O   HOH A 100     7894  11797   5918    438    588   -318       O  
HETATM 1898  O   HOH A 101       7.070 -31.661 -12.236  1.00 39.38           O  
ANISOU 1898  O   HOH A 101     4053   6425   4483  -1298   -893   1185       O  
HETATM 1899  O   HOH A 102       5.362 -42.738 -10.871  1.00 59.79           O  
ANISOU 1899  O   HOH A 102     5840   7815   9060    938   -222   2186       O  
HETATM 1900  O   HOH A 103       4.593 -39.525 -17.155  1.00 40.96           O  
ANISOU 1900  O   HOH A 103     4092   5272   6196    935    171    597       O  
HETATM 1901  O   HOH A 131      -1.545 -30.254 -33.865  1.00 61.73           O  
ANISOU 1901  O   HOH A 131     7111  10807   5536    441    327   -202       O  
HETATM 1902  O   HOH A 134       2.332 -42.587 -14.398  1.00 51.93           O  
ANISOU 1902  O   HOH A 134     5712   6034   7983    951    175    722       O  
HETATM 1903  O   HOH A 140      11.743 -33.241 -22.986  1.00 55.95           O  
ANISOU 1903  O   HOH A 140     4927   8799   7529    786    527   1293       O  
HETATM 1904  O   HOH A 169       4.752 -35.451 -10.911  1.00 23.58           O  
ANISOU 1904  O   HOH A 169     1998   3987   2971   -580   -849   1240       O  
HETATM 1905  O   HOH A 171      -3.138 -35.701 -31.650  1.00 54.02           O  
ANISOU 1905  O   HOH A 171     6609   9014   4899   -119    243  -1388       O  
HETATM 1906  O   HOH A 180     -11.211 -48.842  -7.824  1.00 46.65           O  
ANISOU 1906  O   HOH A 180     5974   4103   7648   -650    140    390       O  
HETATM 1907  O   HOH A 195     -10.466 -46.944  -9.672  1.00 48.82           O  
ANISOU 1907  O   HOH A 195     6192   4740   7617   -524      8     59       O  
HETATM 1908  O   HOH A 199     -18.272 -43.461  -7.589  1.00 45.02           O  
ANISOU 1908  O   HOH A 199     4907   5670   6526   -880     27    669       O  
HETATM 1909  O   HOH A 203       2.857 -24.957 -30.718  1.00 52.47           O  
ANISOU 1909  O   HOH A 203     6048   8480   5406    753    793    717       O  
HETATM 1910  O   HOH A 210     -20.439 -44.594  -3.114  1.00 56.04           O  
ANISOU 1910  O   HOH A 210     6291   6993   8006   -989    439   1336       O  
HETATM 1911  O   HOH A 211       9.427 -35.260 -25.371  1.00 54.97           O  
ANISOU 1911  O   HOH A 211     5442   8084   7359   1300   1011    426       O  
HETATM 1912  O   HOH A 217     -21.613 -42.376  -1.285  1.00 55.56           O  
ANISOU 1912  O   HOH A 217     6287   7171   7651   -615    950   1640       O  
HETATM 1913  O   HOH A 241      -5.138 -46.250  -7.282  1.00 44.63           O  
ANISOU 1913  O   HOH A 241     5387   4399   7170    136   -106   1035       O  
HETATM 1914  O   HOH A 249      -1.374 -20.564 -29.822  1.00 51.05           O  
ANISOU 1914  O   HOH A 249     6192   7765   5438   1242   1287   1783       O  
HETATM 1915  O   HOH A 251       0.739 -36.999 -34.213  1.00 75.53           O  
ANISOU 1915  O   HOH A 251     9758  11481   7456    122   1126  -1949       O  
HETATM 1916  O   HOH A 255       1.368 -21.988 -30.634  1.00 66.36           O  
ANISOU 1916  O   HOH A 255     8008   9984   7220    903   1059   1322       O  
HETATM 1917  O   HOH B 183       3.477 -27.507  -9.475  1.00 15.44           O  
ANISOU 1917  O   HOH B 183     1637   2456   1771     79   -104    -28       O  
HETATM 1918  O   HOH B 184       5.637 -38.734  -4.879  1.00 38.33           O  
ANISOU 1918  O   HOH B 184     4423   5543   4596    720    -24    255       O  
HETATM 1919  O   HOH B 185      -9.809 -43.969 -18.490  1.00 32.88           O  
ANISOU 1919  O   HOH B 185     4196   3999   4296    268    115   -409       O  
HETATM 1920  O   HOH B 186      -7.297 -29.355 -29.848  1.00 26.24           O  
ANISOU 1920  O   HOH B 186     3188   3936   2843    586     40   -154       O  
HETATM 1921  O   HOH B 187      -3.164 -17.361 -11.749  1.00 47.89           O  
ANISOU 1921  O   HOH B 187     6281   5991   5924    -66     71    -65       O  
HETATM 1922  O   HOH B 188     -18.132 -28.966 -33.620  1.00 65.19           O  
ANISOU 1922  O   HOH B 188     7888   9524   7356    809   -115   -388       O  
HETATM 1923  O   HOH B 189     -18.086 -20.382  -4.251  1.00 17.19           O  
ANISOU 1923  O   HOH B 189     2432   2277   1822    479    -38    -38       O  
HETATM 1924  O   HOH B 190       0.223 -43.551  -4.907  1.00 35.90           O  
ANISOU 1924  O   HOH B 190     4430   4707   4500    801    151    307       O  
HETATM 1925  O   HOH B 191     -20.239 -21.943 -24.150  1.00 26.29           O  
ANISOU 1925  O   HOH B 191     3276   4062   2651    837      2     20       O  
HETATM 1926  O   HOH B 192     -10.292 -24.499 -16.764  1.00 14.99           O  
ANISOU 1926  O   HOH B 192     1964   2062   1668    333    -15    -27       O  
HETATM 1927  O   HOH B 193     -12.425 -44.728 -18.403  1.00 39.34           O  
ANISOU 1927  O   HOH B 193     5005   4788   5153    155    121   -490       O  
HETATM 1928  O   HOH B 194      -4.140 -21.765 -27.020  1.00 24.57           O  
ANISOU 1928  O   HOH B 194     3149   3454   2730    445    207    173       O  
HETATM 1929  O   HOH B 195      -6.902 -27.735   5.558  1.00 26.90           O  
ANISOU 1929  O   HOH B 195     3304   3932   2984    355   -212    -22       O  
HETATM 1930  O   HOH B 196      -4.693 -17.703 -28.668  1.00 60.05           O  
ANISOU 1930  O   HOH B 196     7788   7864   7162    521    359    347       O  
HETATM 1931  O   HOH B 197      -4.642 -11.690  -5.194  1.00 63.09           O  
ANISOU 1931  O   HOH B 197     8520   7636   7814   -229    101   -310       O  
HETATM 1932  O   HOH B 198     -16.898 -41.008 -17.661  1.00 47.90           O  
ANISOU 1932  O   HOH B 198     5936   6134   6129     66     10   -476       O  
HETATM 1933  O   HOH B 199       2.087 -24.796  -9.106  1.00 22.52           O  
ANISOU 1933  O   HOH B 199     2634   3242   2679    -21    -97    -73       O  
HETATM 1934  O   HOH B 200      -4.522 -38.607 -23.413  1.00 22.00           O  
ANISOU 1934  O   HOH B 200     2696   2996   2664    456     41   -318       O  
HETATM 1935  O   HOH B 201       1.040 -21.609   0.470  1.00 61.33           O  
ANISOU 1935  O   HOH B 201     7581   8305   7416   -140   -244   -297       O  
HETATM 1936  O   HOH B 202     -17.933 -36.132   4.939  1.00 47.57           O  
ANISOU 1936  O   HOH B 202     5942   6252   5879    441     85    306       O  
HETATM 1937  O   HOH B 203      -2.156 -19.155 -13.804  1.00 22.92           O  
ANISOU 1937  O   HOH B 203     3021   2924   2763    -28     67    -20       O  
HETATM 1938  O   HOH B 204     -10.405 -20.400 -10.839  1.00 18.37           O  
ANISOU 1938  O   HOH B 204     2552   2321   2106    252     -7    -36       O  
HETATM 1939  O   HOH B 205     -15.522 -30.191   2.349  1.00 21.80           O  
ANISOU 1939  O   HOH B 205     2743   3025   2512    405    -73     96       O  
HETATM 1940  O   HOH B 206     -19.390 -38.200  -1.233  1.00 41.36           O  
ANISOU 1940  O   HOH B 206     5136   5299   5279    235    106    137       O  
HETATM 1941  O   HOH B 207      -8.532 -44.726  -5.459  1.00 24.18           O  
ANISOU 1941  O   HOH B 207     2974   2126   4085   -307   -226    883       O  
HETATM 1942  O   HOH B 208      -6.114 -25.834  20.523  1.00 62.67           O  
ANISOU 1942  O   HOH B 208     7642   9441   6728    739   -391   -159       O  
HETATM 1943  O   HOH B 209      -0.012 -43.878  -7.266  1.00 47.56           O  
ANISOU 1943  O   HOH B 209     5144   5699   7227    335   -448   1744       O  
HETATM 1944  O   HOH B 210      -3.443 -44.091 -26.400  1.00 36.57           O  
ANISOU 1944  O   HOH B 210     4640   4716   4537    566    141   -538       O  
HETATM 1945  O   HOH B 211       2.898 -23.297 -28.957  1.00 49.28           O  
ANISOU 1945  O   HOH B 211     6080   6755   5889    340    289    230       O  
HETATM 1946  O   HOH B 212     -17.352 -16.816 -30.013  1.00 47.11           O  
ANISOU 1946  O   HOH B 212     6115   6706   5077   1170    238    344       O  
HETATM 1947  O   HOH B 213      -1.910 -15.625 -15.256  1.00 43.14           O  
ANISOU 1947  O   HOH B 213     5727   5324   5341    -94    192     25       O  
HETATM 1948  O   HOH B 214      -4.162 -27.167   4.915  1.00 42.17           O  
ANISOU 1948  O   HOH B 214     5175   5942   4906    285   -246    -72       O  
HETATM 1949  O   HOH B 215       7.536 -36.717  -5.241  1.00 47.88           O  
ANISOU 1949  O   HOH B 215     5512   6929   5748    626    -78    210       O  
HETATM 1950  O   HOH B 216       3.437 -36.425 -25.048  1.00 33.41           O  
ANISOU 1950  O   HOH B 216     3982   4711   3998    593    113   -106       O  
HETATM 1951  O   HOH B 217     -16.993 -29.440   0.010  0.50 19.70           O  
ANISOU 1951  O   HOH B 217     2487   2725   2273    378    -69     57       O  
HETATM 1952  O   HOH B 218     -17.110 -16.309 -27.158  1.00 57.68           O  
ANISOU 1952  O   HOH B 218     7534   7837   6543   1052    237    323       O  
HETATM 1953  O   HOH B 219      -7.292  -7.021 -12.134  1.00 56.26           O  
ANISOU 1953  O   HOH B 219     8050   6339   6986     19    453      0       O  
HETATM 1954  O   HOH B 220     -19.880 -36.192  -7.842  1.00 27.35           O  
ANISOU 1954  O   HOH B 220     3318   3606   3467    165      2    -92       O  
HETATM 1955  O   HOH B 221      -6.884 -23.528  -0.131  1.00 24.21           O  
ANISOU 1955  O   HOH B 221     3107   3319   2772    158   -175   -141       O  
HETATM 1956  O   HOH B 222      -7.398 -23.812   2.892  1.00 23.83           O  
ANISOU 1956  O   HOH B 222     3042   3362   2648    208   -203   -150       O  
HETATM 1957  O   HOH B 223      -9.017 -21.543   3.607  1.00 21.79           O  
ANISOU 1957  O   HOH B 223     2890   3033   2356    209   -189   -208       O  
HETATM 1958  O   HOH B 224      -7.048 -19.955  -2.664  1.00 37.93           O  
ANISOU 1958  O   HOH B 224     4983   4882   4545     72   -114   -190       O  
HETATM 1959  O   HOH B 225      -6.168 -20.669  -0.388  1.00 47.20           O  
ANISOU 1959  O   HOH B 225     6096   6160   5677     61   -161   -221       O  
HETATM 1960  O   HOH B 226       7.563 -21.457 -12.325  1.00 40.21           O  
ANISOU 1960  O   HOH B 226     4721   5616   4937   -306      4    -69       O  
HETATM 1961  O   HOH B 227     -15.816 -18.228 -33.160  1.00 47.72           O  
ANISOU 1961  O   HOH B 227     6098   6959   5072   1196    232    320       O  
HETATM 1962  O   HOH B 228     -11.682 -21.309 -34.482  1.00 36.03           O  
ANISOU 1962  O   HOH B 228     4535   5461   3694   1005    200    198       O  
HETATM 1963  O   HOH B 229     -16.425 -29.000 -27.357  1.00 51.82           O  
ANISOU 1963  O   HOH B 229     6352   7331   6006    583    -85   -279       O  
HETATM 1964  O   HOH B 230      -6.521 -27.310   8.353  1.00 36.59           O  
ANISOU 1964  O   HOH B 230     4500   5304   4097    400   -246    -42       O  
HETATM 1965  O   HOH B 231       2.628 -37.464 -21.072  1.00 52.30           O  
ANISOU 1965  O   HOH B 231     6405   6987   6479    555     80    -81       O  
HETATM 1966  O   HOH B 232      -6.689 -13.573 -26.813  1.00 43.14           O  
ANISOU 1966  O   HOH B 232     5886   5459   5046    544    470    443       O  
HETATM 1967  O   HOH B 233     -10.340 -12.728 -26.196  1.00 69.22           O  
ANISOU 1967  O   HOH B 233     9266   8773   8262    737    456    459       O  
HETATM 1968  O   HOH B 234       5.788 -42.767  -7.293  1.00 64.75           O  
ANISOU 1968  O   HOH B 234     7890   8685   8026    921    114    307       O  
HETATM 1969  O   HOH B 235      -9.339 -14.885  -4.527  1.00 53.08           O  
ANISOU 1969  O   HOH B 235     7190   6512   6464     99     21   -201       O  
HETATM 1970  O   HOH B 236       6.901 -21.598 -19.634  1.00 41.11           O  
ANISOU 1970  O   HOH B 236     4922   5642   5056   -132    172    106       O  
HETATM 1971  O   HOH B 237       1.933 -41.731 -22.369  1.00 50.71           O  
ANISOU 1971  O   HOH B 237     6306   6641   6318    680    147   -189       O  
HETATM 1972  O   HOH B 238     -12.084 -31.133 -31.990  1.00 49.67           O  
ANISOU 1972  O   HOH B 238     6066   7138   5666    644    -45   -362       O  
HETATM 1973  O   HOH B 239      -4.881 -39.862   7.333  1.00 48.01           O  
ANISOU 1973  O   HOH B 239     5890   6605   5744    843     51    512       O  
HETATM 1974  O   HOH B 240      -4.787 -38.034 -26.415  1.00 51.31           O  
ANISOU 1974  O   HOH B 240     6387   6821   6285    493     36   -381       O  
HETATM 1975  O   HOH B 241      -6.940 -31.850   7.413  1.00 27.28           O  
ANISOU 1975  O   HOH B 241     3282   4064   3016    532   -158    161       O  
HETATM 1976  O   HOH B 242       4.199 -18.936 -17.703  1.00 28.08           O  
ANISOU 1976  O   HOH B 242     3466   3762   3441   -203    175     62       O  
HETATM 1977  O   HOH B 243      -0.816 -21.520   4.623  1.00 56.72           O  
ANISOU 1977  O   HOH B 243     7031   7809   6709    -46   -300   -352       O  
HETATM 1978  O   HOH B 244      -7.335 -19.424   9.114  1.00 48.81           O  
ANISOU 1978  O   HOH B 244     6301   6675   5570    169   -273   -404       O  
HETATM 1979  O   HOH B 245       2.155 -36.465  -2.432  1.00 31.68           O  
ANISOU 1979  O   HOH B 245     3666   4605   3765    570    -84    199       O  
HETATM 1980  O   HOH B 246       1.472 -21.817   3.679  1.00 61.55           O  
ANISOU 1980  O   HOH B 246     7539   8514   7331   -115   -310   -356       O  
HETATM 1981  O   HOH B 247      -1.955 -44.295 -18.525  1.00 59.41           O  
ANISOU 1981  O   HOH B 247     7569   6328   8673    546    595   -816       O  
HETATM 1982  O   HOH B 248     -16.145 -39.887   5.367  1.00 60.64           O  
ANISOU 1982  O   HOH B 248     7625   7790   7625    483    189    425       O  
HETATM 1983  O   HOH B 249     -14.284 -39.110 -23.549  1.00 42.69           O  
ANISOU 1983  O   HOH B 249     5250   5698   5271    223    -49   -576       O  
HETATM 1984  O   HOH B 250       1.067 -12.014 -16.922  1.00 54.54           O  
ANISOU 1984  O   HOH B 250     7255   6614   6853   -317    372     77       O  
HETATM 1985  O   HOH B 251      -8.762 -35.608   2.499  1.00 30.99           O  
ANISOU 1985  O   HOH B 251     3822   4212   3739    492    -36    226       O  
HETATM 1986  O   HOH B 252       6.918 -28.117   0.422  1.00 58.90           O  
ANISOU 1986  O   HOH B 252     6836   8546   6996    120   -289    -92       O  
HETATM 1987  O   HOH B 253       3.222 -26.864   1.011  1.00 48.20           O  
ANISOU 1987  O   HOH B 253     5687   6929   5695     98   -275   -127       O  
HETATM 1988  O   HOH B 254     -14.272 -43.721 -19.331  1.00 46.58           O  
ANISOU 1988  O   HOH B 254     5859   5816   6021     96     72   -556       O  
HETATM 1989  O   HOH B 255     -19.139 -36.085 -10.677  1.00 30.20           O  
ANISOU 1989  O   HOH B 255     3675   3985   3814    158    -23   -172       O  
HETATM 1990  O   HOH B 256     -11.252 -37.341   5.162  1.00 27.82           O  
ANISOU 1990  O   HOH B 256     3438   3793   3335    561     42    345       O  
HETATM 1991  O   HOH B 257      -9.667 -47.546  -1.086  1.00 38.04           O  
ANISOU 1991  O   HOH B 257     4960   4442   5050    579    392    395       O  
HETATM 1992  O   HOH B 258      -6.890 -29.407   9.691  1.00 42.44           O  
ANISOU 1992  O   HOH B 258     5201   6113   4809    514   -219     66       O  
HETATM 1993  O   HOH B 259       4.714 -18.265 -11.041  1.00 37.29           O  
ANISOU 1993  O   HOH B 259     4590   4974   4603   -391     34   -133       O  
HETATM 1994  O   HOH B 260     -11.173 -40.358 -24.778  1.00 33.19           O  
ANISOU 1994  O   HOH B 260     4102   4425   4081    296     -7   -583       O  
HETATM 1995  O   HOH B 261     -18.283 -31.861   0.042  0.50 28.72           O  
ANISOU 1995  O   HOH B 261     3581   3860   3470    360    -28     98       O  
HETATM 1996  O   HOH B 262     -15.215 -28.485 -30.653  1.00 45.97           O  
ANISOU 1996  O   HOH B 262     5596   6729   5140    695    -59   -267       O  
HETATM 1997  O   HOH B 263      -8.770 -35.334 -28.657  1.00 47.59           O  
ANISOU 1997  O   HOH B 263     5870   6542   5670    486    -23   -430       O  
HETATM 1998  O   HOH B 264     -13.045 -47.413 -16.732  1.00 41.45           O  
ANISOU 1998  O   HOH B 264     5351   4849   5546    100    221   -481       O  
HETATM 1999  O   HOH B 265     -12.028 -34.002 -28.641  1.00 50.73           O  
ANISOU 1999  O   HOH B 265     6229   7040   6003    475    -66   -448       O  
HETATM 2000  O   HOH B 266      -7.615 -22.158  11.657  1.00 35.18           O  
ANISOU 2000  O   HOH B 266     4452   5170   3744    326   -302   -297       O  
HETATM 2001  O   HOH B 267     -20.164 -44.406 -15.312  1.00 43.94           O  
ANISOU 2001  O   HOH B 267     5423   5481   5788   -145    111   -526       O  
HETATM 2002  O   HOH B 268       2.716 -33.178  -9.185  1.00 40.59           O  
ANISOU 2002  O   HOH B 268     4947   5932   4543  -1202   -819    782       O  
HETATM 2003  O   HOH B 269      -3.059 -13.062 -16.393  1.00 48.72           O  
ANISOU 2003  O   HOH B 269     6598   5869   6044    -56    302     86       O  
HETATM 2004  O   HOH B 270      -6.431 -17.215 -11.973  1.00 43.23           O  
ANISOU 2004  O   HOH B 270     5776   5351   5297     83     77    -35       O  
HETATM 2005  O   HOH B 271      -0.266 -14.821 -24.510  1.00 44.09           O  
ANISOU 2005  O   HOH B 271     5829   5554   5367    103    437    330       O  
HETATM 2006  O   HOH B 272      -8.182 -18.809 -13.056  1.00 28.00           O  
ANISOU 2006  O   HOH B 272     3806   3488   3342    194     54     -6       O  
HETATM 2007  O   HOH B 273      -5.282 -41.619   0.958  1.00 42.61           O  
ANISOU 2007  O   HOH B 273     5313   5557   5318    685    117    382       O  
HETATM 2008  O   HOH B 274       2.904 -24.910  -2.848  1.00 37.78           O  
ANISOU 2008  O   HOH B 274     4467   5392   4494    -37   -210   -152       O  
HETATM 2009  O   HOH B 275      -0.042 -18.817  -5.386  1.00 36.42           O  
ANISOU 2009  O   HOH B 275     4628   4792   4418   -228    -90   -237       O  
HETATM 2010  O   HOH B 276     -11.323 -43.038   6.360  1.00 46.50           O  
ANISOU 2010  O   HOH B 276     5871   5972   5822    697    263    587       O  
HETATM 2011  O   HOH B 277      -8.971 -17.805  -8.891  1.00 40.04           O  
ANISOU 2011  O   HOH B 277     5391   4965   4856    157     18    -80       O  
HETATM 2012  O   HOH B 278      -1.293 -19.982  -7.893  1.00 36.06           O  
ANISOU 2012  O   HOH B 278     4603   4695   4401   -118    -57   -147       O  
HETATM 2013  O   HOH B 279     -13.526 -44.626   6.378  1.00 73.19           O  
ANISOU 2013  O   HOH B 279     9296   9213   9301    635    365    630       O  
HETATM 2014  O   HOH B 280      -4.908 -17.297  -9.462  1.00 49.35           O  
ANISOU 2014  O   HOH B 280     6510   6155   6084    -24     31   -108       O  
HETATM 2015  O   HOH B 281      -7.067 -33.027 -29.393  1.00 51.30           O  
ANISOU 2015  O   HOH B 281     6340   7062   6088    543      7   -304       O  
HETATM 2016  O   HOH B 282     -22.440 -48.358 -11.444  1.00 42.29           O  
ANISOU 2016  O   HOH B 282     5274   4981   5811   -347    314   -443       O  
HETATM 2017  O   HOH B 283      -5.098 -46.270 -26.926  1.00 63.59           O  
ANISOU 2017  O   HOH B 283     8129   8021   8009    509    169   -688       O  
HETATM 2018  O   HOH B 284      -2.698 -30.896   4.890  1.00 55.81           O  
ANISOU 2018  O   HOH B 284     6805   7756   6644    425   -215     71       O  
HETATM 2019  O   HOH B 285       2.588 -45.571  -2.966  1.00 43.80           O  
ANISOU 2019  O   HOH B 285     5398   5814   5428   1039    218    464       O  
HETATM 2020  O   HOH B 286     -20.057 -30.622  -2.533  1.00 33.34           O  
ANISOU 2020  O   HOH B 286     4154   4469   4043    345    -42     38       O  
HETATM 2021  O   HOH B 287      -3.802 -17.299 -16.217  1.00 44.35           O  
ANISOU 2021  O   HOH B 287     5855   5540   5454     54    155     52       O  
HETATM 2022  O   HOH B 288     -20.985 -34.055  -2.618  1.00 49.01           O  
ANISOU 2022  O   HOH B 288     6078   6419   6122    268     11     56       O  
HETATM 2023  O   HOH B 289     -17.700 -34.683   0.614  1.00 59.22           O  
ANISOU 2023  O   HOH B 289     7426   7672   7401    345     20    154       O  
HETATM 2024  O   HOH B 290       6.732 -26.134  -1.373  1.00 60.38           O  
ANISOU 2024  O   HOH B 290     7088   8599   7254    -29   -264   -151       O  
HETATM 2025  O   HOH B 291     -21.018 -39.321  -4.114  1.00 47.51           O  
ANISOU 2025  O   HOH B 291     5197   6339   6514   -122    997   1425       O  
HETATM 2026  O   HOH B 292     -22.322 -35.443  -6.959  1.00 51.78           O  
ANISOU 2026  O   HOH B 292     6360   6792   6522    162      3    -79       O  
HETATM 2027  O   HOH B 293     -22.943 -35.577  -3.627  1.00 62.93           O  
ANISOU 2027  O   HOH B 293     7779   8199   7931    193     41     23       O  
HETATM 2028  O   HOH B 294      -2.728 -34.813   2.928  1.00 43.68           O  
ANISOU 2028  O   HOH B 294     5285   6092   5220    545   -119    208       O  
HETATM 2029  O   HOH B 295     -21.725 -35.379 -11.305  1.00 41.38           O  
ANISOU 2029  O   HOH B 295     5020   5523   5179    142    -39   -209       O  
HETATM 2030  O   HOH B 296       5.232 -32.693  -9.743  1.00 50.31           O  
ANISOU 2030  O   HOH B 296     5755   7636   5720  -1431  -1003   1127       O  
HETATM 2031  O   HOH B 297       7.073 -19.161 -24.413  1.00 43.89           O  
ANISOU 2031  O   HOH B 297     5357   5940   5379   -103    354    258       O  
HETATM 2032  O   HOH B 298     -12.444 -12.641 -24.491  1.00 56.08           O  
ANISOU 2032  O   HOH B 298     7624   7099   6582    790    410    416       O  
HETATM 2033  O   HOH B 299     -21.583 -23.694 -33.067  1.00 59.10           O  
ANISOU 2033  O   HOH B 299     7148   8923   6383   1118    -52    -99       O  
HETATM 2034  O   HOH B 300       6.727 -13.337 -21.118  1.00 60.18           O  
ANISOU 2034  O   HOH B 300     7661   7625   7576   -463    468    209       O  
HETATM 2035  O   HOH B 301       4.761 -19.465 -15.132  1.00 24.83           O  
ANISOU 2035  O   HOH B 301     2997   3404   3031   -261    104     -8       O  
HETATM 2036  O   HOH B 302     -12.601 -33.644  12.537  1.00 25.25           O  
ANISOU 2036  O   HOH B 302     3070   3859   2665    732    -33    371       O  
HETATM 2037  O   HOH B 303      -7.966 -46.411 -17.534  1.00 59.76           O  
ANISOU 2037  O   HOH B 303     7935   6234   8534   -563    299  -1303       O  
HETATM 2038  O   HOH B 304      -6.444 -16.259  -5.588  1.00 55.31           O  
ANISOU 2038  O   HOH B 304     7341   6879   6791    -17     -7   -198       O  
HETATM 2039  O   HOH B 305     -25.607 -48.626 -15.213  1.00 52.83           O  
ANISOU 2039  O   HOH B 305     6433   6548   7091   -584    237   -771       O  
HETATM 2040  O   HOH B 306       9.120 -27.482 -26.352  1.00 43.63           O  
ANISOU 2040  O   HOH B 306     4351   7146   5080    223    591    735       O  
HETATM 2041  O   HOH E  59     -20.513 -28.898 -19.426  1.00 15.55           O  
ANISOU 2041  O   HOH E  59     2087   2143   1676    585   -471   -350       O  
HETATM 2042  O   HOH E  60     -23.512 -30.656 -26.863  1.00 34.95           O  
ANISOU 2042  O   HOH E  60     4578   5125   3575    181   -795   -166       O  
HETATM 2043  O   HOH E  61     -20.567 -31.198 -12.318  1.00 15.60           O  
ANISOU 2043  O   HOH E  61     1817   2319   1788    288    -82   -156       O  
HETATM 2044  O   HOH E  62     -20.721 -41.346 -15.314  1.00 31.59           O  
ANISOU 2044  O   HOH E  62     3791   4109   4101    -58     27   -465       O  
HETATM 2045  O   HOH E  63     -20.637 -20.781 -21.015  1.00 40.52           O  
ANISOU 2045  O   HOH E  63     5301   4309   5784    529  -1582    146       O  
HETATM 2046  O   HOH E  64     -27.177 -24.072 -20.495  1.00 41.19           O  
ANISOU 2046  O   HOH E  64     4832   4647   6172   1032  -1252   -597       O  
HETATM 2047  O   HOH E  65     -29.086 -32.077 -22.321  1.00 24.95           O  
ANISOU 2047  O   HOH E  65     2897   3480   3101    713   -769   -480       O  
HETATM 2048  O   HOH E  66     -27.320 -30.920 -20.680  1.00 21.34           O  
ANISOU 2048  O   HOH E  66     2487   2974   2647    749   -628   -548       O  
HETATM 2049  O   HOH E  67     -30.897 -30.593 -23.832  1.00 37.33           O  
ANISOU 2049  O   HOH E  67     4355   4906   4922    749  -1099   -339       O  
HETATM 2050  O   HOH E  68     -23.321 -41.750 -14.918  1.00 28.37           O  
ANISOU 2050  O   HOH E  68     3299   3781   3698   -156     33   -509       O  
HETATM 2051  O   HOH E  69     -22.445 -37.558 -26.001  1.00 34.25           O  
ANISOU 2051  O   HOH E  69     4196   4923   3892    441   -396  -1143       O  
HETATM 2052  O   HOH E  70     -17.288 -29.509 -23.231  1.00 29.47           O  
ANISOU 2052  O   HOH E  70     3859   4298   3039    286   -376   -224       O  
HETATM 2053  O   HOH E  71     -17.138 -32.596 -21.878  1.00 29.02           O  
ANISOU 2053  O   HOH E  71     3474   4171   3378    340   -105   -351       O  
HETATM 2054  O   HOH E  76     -32.988 -33.530 -14.665  1.00 55.90           O  
ANISOU 2054  O   HOH E  76     5940   8457   6841    300   -126  -1111       O  
HETATM 2055  O   HOH E  78     -27.903 -21.389 -23.243  1.00 64.02           O  
ANISOU 2055  O   HOH E  78     7670   6913   9740    922  -2179     16       O  
HETATM 2056  O   HOH E  90     -24.168 -34.152 -26.563  1.00 49.90           O  
ANISOU 2056  O   HOH E  90     6369   7039   5550    319   -581   -616       O  
HETATM 2057  O   HOH E  94     -35.921 -35.515 -28.164  1.00 39.49           O  
ANISOU 2057  O   HOH E  94     4564   5528   4912    298  -1593   -130       O  
HETATM 2058  O   HOH E  98     -29.468 -22.593 -25.255  1.00 57.68           O  
ANISOU 2058  O   HOH E  98     6856   6302   8757    747  -2377    352       O  
HETATM 2059  O   HOH E 101     -32.423 -37.292 -12.913  1.00 46.90           O  
ANISOU 2059  O   HOH E 101     4884   7695   5241   -432   -294   -485       O  
HETATM 2060  O   HOH E 104     -33.568 -35.847 -28.033  1.00 52.11           O  
ANISOU 2060  O   HOH E 104     6359   7181   6258    280  -1355   -284       O  
HETATM 2061  O   HOH E 145     -29.165 -28.900 -26.993  1.00 48.67           O  
ANISOU 2061  O   HOH E 145     6073   6353   6065    389  -1499    158       O  
HETATM 2062  O   HOH E 147     -22.731 -32.944 -12.795  1.00 32.54           O  
ANISOU 2062  O   HOH E 147     3873   4542   3947    223    -78   -217       O  
HETATM 2063  O   HOH E 149     -19.555 -44.767 -19.827  1.00 42.47           O  
ANISOU 2063  O   HOH E 149     5212   5407   5516   -147     57   -752       O  
HETATM 2064  O   HOH E 151     -14.504 -33.415 -27.652  1.00 51.09           O  
ANISOU 2064  O   HOH E 151     6245   7127   6037    447    -95   -456       O  
HETATM 2065  O   HOH E 155     -26.928 -22.792 -25.595  1.00 56.18           O  
ANISOU 2065  O   HOH E 155     6979   6398   7967    476  -2179    550       O  
HETATM 2066  O   HOH E 161     -19.725 -37.157 -26.554  1.00 62.31           O  
ANISOU 2066  O   HOH E 161     7638   8661   7374    395   -179  -1362       O  
HETATM 2067  O   HOH E 162     -18.516 -47.003 -20.582  1.00 43.56           O  
ANISOU 2067  O   HOH E 162     5433   5388   5728   -180    118   -839       O  
HETATM 2068  O   HOH E 163     -16.812 -31.755 -24.769  1.00 30.00           O  
ANISOU 2068  O   HOH E 163     3576   4427   3394    424   -109   -370       O  
HETATM 2069  O   HOH E 164     -46.263 -28.432 -25.083  1.00 68.44           O  
ANISOU 2069  O   HOH E 164     5532   8220  12252   1472  -2583   -693       O  
HETATM 2070  O   HOH E 165     -34.926 -32.012 -15.965  1.00 61.43           O  
ANISOU 2070  O   HOH E 165     6362   8961   8015    643   -209  -1379       O  
HETATM 2071  O   HOH E 168     -18.030 -33.205 -26.639  1.00 36.17           O  
ANISOU 2071  O   HOH E 168     4283   5340   4119    409   -135   -498       O  
HETATM 2072  O   HOH E 177     -22.315 -28.497 -25.799  1.00 33.94           O  
ANISOU 2072  O   HOH E 177     4490   4799   3605    208   -884     39       O  
HETATM 2073  O   HOH E 186     -43.477 -27.119 -22.905  1.00 57.24           O  
ANISOU 2073  O   HOH E 186     4359   6807  10581   1651  -2045  -1225       O  
HETATM 2074  O   HOH E 189     -22.651 -42.401 -23.926  1.00 53.83           O  
ANISOU 2074  O   HOH E 189     6370   6651   7432    592   -776  -1377       O  
HETATM 2075  O   HOH E 191     -22.397 -40.801 -26.126  1.00 55.53           O  
ANISOU 2075  O   HOH E 191     6681   7329   7086    527   -498  -1596       O  
HETATM 2076  O   HOH E 193     -33.516 -26.564 -21.208  1.00 46.87           O  
ANISOU 2076  O   HOH E 193     4846   5625   7335   1248  -1283   -903       O  
HETATM 2077  O   HOH E 200     -23.567 -20.805 -20.284  1.00 59.61           O  
ANISOU 2077  O   HOH E 200     7435   6517   8695    861  -1618   -289       O  
HETATM 2078  O   HOH E 214     -24.453 -35.254  -9.236  1.00 56.05           O  
ANISOU 2078  O   HOH E 214     6813   7461   7021    125    -19   -167       O  
HETATM 2079  O   HOH E 233     -24.773 -38.728 -13.410  1.00 43.42           O  
ANISOU 2079  O   HOH E 233     5108   6139   5250   -308   -798    110       O  
HETATM 2080  O   HOH E 245     -25.629 -33.004  -8.966  1.00 60.99           O  
ANISOU 2080  O   HOH E 245     7421   8198   7552    213    -43   -134       O  
HETATM 2081  O   HOH E 256     -40.964 -46.352 -28.876  1.00 67.51           O  
ANISOU 2081  O   HOH E 256     7959   8910   8779   -419  -2269   -383       O  
HETATM 2082  O   HOH E 257     -29.335 -47.475 -22.157  1.00 57.93           O  
ANISOU 2082  O   HOH E 257     6765   6647   8597     68  -1838   -639       O  
HETATM 2083  O   HOH E 259     -44.992 -41.675 -27.299  1.00 65.02           O  
ANISOU 2083  O   HOH E 259     6875   9065   8765   -157  -2159    127       O  
CONECT 1485 1885                                                                
CONECT 1552 1746 1747                                                           
CONECT 1684 1853                                                                
CONECT 1746 1552                                                                
CONECT 1747 1552                                                                
CONECT 1853 1684                                                                
CONECT 1885 1485                                                                
MASTER      403    0    0    3   19    0    0    6 2049    3    7   24          
END

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Related entries of code: 3u1j

Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code	Check Database	Protein Sequence Similarity
3u1i	RCSB PDB PDBbind	51aa, >3U1I_1\|Chains... *
Complexes with the same small molecule ligand
PDB Code	Check Database	Ligand Name
2ijo	RCSB PDB PDBbind	pancreatic trypsin inhibitor

Entry Information

PDB ID	3u1j
Complex Type	Protein-Protein
PDBbind Subset	general set
Protein Name	dengue virus serotype 3 (DENV-3) protease (covalently bound)
Ligand Name	Pancreatic trypsin inhibitor
EC.Number	E.C.3.4.21.91
Resolution	1.8(Å)
Affinity (Kd/Ki/IC50)	Ki=0.026uM
Release Year	2011
Protein/NA Sequence	Check fasta file
Primary Reference	(2012) Journal of Virology Vol. 86, PP:438-446

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): Q5UB51 P00974
Entrez Gene ID	No matched NCBI Entrez Gene ID found!
ASD	Information of known allosteric effects of PDB entries

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